data_8VIT
# 
_entry.id   8VIT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8VIT         pdb_00008vit 10.2210/pdb8vit/pdb 
WWPDB D_1000280333 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-13 
3 'Structure model' 1 2 2024-12-04 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 3 'Structure model' citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.page_first'              
2 2 'Structure model' '_citation.page_last'               
3 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
4 2 'Structure model' '_citation.title'                   
5 3 'Structure model' '_citation.journal_volume'          
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8VIT 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu Scott   Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 jbose@kumc.edu  Jeffrey Bose   ? 'principal investigator/group leader' 0000-0003-3394-9557 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lovell, S.'       1 0000-0002-3215-4472 
'Kashipathy, M.M.' 2 0000-0003-0435-989X 
'Battaile, K.P.'   3 0000-0003-0833-3259 
'Bose, J.L.'       4 0000-0003-0514-281X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_id_ASTM           JBCHA3 
_citation.journal_id_CSD            0071 
_citation.journal_id_ISSN           1083-351X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            300 
_citation.language                  ? 
_citation.page_first                107920 
_citation.page_last                 107920 
_citation.title                     
'Molecular insights into the structure and function of the Staphylococcus aureus fatty acid kinase.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.jbc.2024.107920 
_citation.pdbx_database_id_PubMed   39454961 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Myers, M.J.'       1  ? 
primary 'Xu, Z.'            2  ? 
primary 'Ryan, B.J.'        3  ? 
primary 'DeMars, Z.R.'      4  ? 
primary 'Ridder, M.J.'      5  ? 
primary 'Johnson, D.K.'     6  ? 
primary 'Krute, C.N.'       7  ? 
primary 'Flynn, T.S.'       8  ? 
primary 'Kashipathy, M.M.'  9  ? 
primary 'Battaile, K.P.'    10 ? 
primary 'Schnicker, N.'     11 ? 
primary 'Lovell, S.'        12 ? 
primary 'Freudenthal, B.D.' 13 ? 
primary 'Bose, J.L.'        14 ? 
# 
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 'FATTY ACID KINASE A'      24816.246 1   ? ? 'N-terminal domain (M1-A212)' ? 
2 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE" 427.201   1   ? ? ?                             ? 
3 non-polymer syn 'MAGNESIUM ION'            24.305    2   ? ? ?                             ? 
4 non-polymer syn 'TETRAETHYLENE GLYCOL'     194.226   1   ? ? ?                             ? 
5 water       nat water                      18.015    186 ? ? ?                             ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNL
SKNIGELGKTFSKGLLMGARGNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAA
QAAIEKANNTEDCIELMEYIIVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNL
SKNIGELGKTFSKGLLMGARGNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAA
QAAIEKANNTEDCIELMEYIIVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "ADENOSINE-5'-DIPHOSPHATE" ADP 
3 'MAGNESIUM ION'            MG  
4 'TETRAETHYLENE GLYCOL'     PG4 
5 water                      HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ILE n 
1 23  SER n 
1 24  LYS n 
1 25  ILE n 
1 26  ASN n 
1 27  GLY n 
1 28  LYS n 
1 29  LEU n 
1 30  PHE n 
1 31  ALA n 
1 32  ASP n 
1 33  MET n 
1 34  ILE n 
1 35  ILE n 
1 36  GLN n 
1 37  GLY n 
1 38  ALA n 
1 39  GLN n 
1 40  ASN n 
1 41  LEU n 
1 42  SER n 
1 43  ASN n 
1 44  ASN n 
1 45  ALA n 
1 46  ASP n 
1 47  LEU n 
1 48  VAL n 
1 49  ASP n 
1 50  SER n 
1 51  LEU n 
1 52  ASN n 
1 53  VAL n 
1 54  TYR n 
1 55  PRO n 
1 56  VAL n 
1 57  PRO n 
1 58  ASP n 
1 59  GLY n 
1 60  ASP n 
1 61  THR n 
1 62  GLY n 
1 63  THR n 
1 64  ASN n 
1 65  MET n 
1 66  ASN n 
1 67  LEU n 
1 68  THR n 
1 69  MET n 
1 70  THR n 
1 71  SER n 
1 72  GLY n 
1 73  ARG n 
1 74  GLU n 
1 75  GLU n 
1 76  VAL n 
1 77  GLU n 
1 78  ASN n 
1 79  ASN n 
1 80  LEU n 
1 81  SER n 
1 82  LYS n 
1 83  ASN n 
1 84  ILE n 
1 85  GLY n 
1 86  GLU n 
1 87  LEU n 
1 88  GLY n 
1 89  LYS n 
1 90  THR n 
1 91  PHE n 
1 92  SER n 
1 93  LYS n 
1 94  GLY n 
1 95  LEU n 
1 96  LEU n 
1 97  MET n 
1 98  GLY n 
1 99  ALA n 
1 100 ARG n 
1 101 GLY n 
1 102 ASN n 
1 103 SER n 
1 104 GLY n 
1 105 VAL n 
1 106 ILE n 
1 107 LEU n 
1 108 SER n 
1 109 GLN n 
1 110 LEU n 
1 111 PHE n 
1 112 ARG n 
1 113 GLY n 
1 114 PHE n 
1 115 CYS n 
1 116 LYS n 
1 117 ASN n 
1 118 ILE n 
1 119 GLU n 
1 120 SER n 
1 121 GLU n 
1 122 SER n 
1 123 GLU n 
1 124 ILE n 
1 125 ASN n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 LEU n 
1 130 ALA n 
1 131 GLU n 
1 132 SER n 
1 133 PHE n 
1 134 GLN n 
1 135 ALA n 
1 136 GLY n 
1 137 VAL n 
1 138 GLU n 
1 139 THR n 
1 140 ALA n 
1 141 TYR n 
1 142 LYS n 
1 143 ALA n 
1 144 VAL n 
1 145 MET n 
1 146 LYS n 
1 147 PRO n 
1 148 VAL n 
1 149 GLU n 
1 150 GLY n 
1 151 THR n 
1 152 ILE n 
1 153 LEU n 
1 154 THR n 
1 155 VAL n 
1 156 ALA n 
1 157 LYS n 
1 158 ASP n 
1 159 ALA n 
1 160 ALA n 
1 161 GLN n 
1 162 ALA n 
1 163 ALA n 
1 164 ILE n 
1 165 GLU n 
1 166 LYS n 
1 167 ALA n 
1 168 ASN n 
1 169 ASN n 
1 170 THR n 
1 171 GLU n 
1 172 ASP n 
1 173 CYS n 
1 174 ILE n 
1 175 GLU n 
1 176 LEU n 
1 177 MET n 
1 178 GLU n 
1 179 TYR n 
1 180 ILE n 
1 181 ILE n 
1 182 VAL n 
1 183 LYS n 
1 184 ALA n 
1 185 ASN n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 GLU n 
1 190 ASN n 
1 191 THR n 
1 192 PRO n 
1 193 ASN n 
1 194 LEU n 
1 195 LEU n 
1 196 ALA n 
1 197 VAL n 
1 198 LEU n 
1 199 LYS n 
1 200 GLU n 
1 201 VAL n 
1 202 GLY n 
1 203 VAL n 
1 204 VAL n 
1 205 ASP n 
1 206 SER n 
1 207 GLY n 
1 208 GLY n 
1 209 LYS n 
1 210 GLY n 
1 211 LEU n 
1 212 LEU n 
1 213 CYS n 
1 214 VAL n 
1 215 TYR n 
1 216 GLU n 
1 217 GLY n 
1 218 PHE n 
1 219 LEU n 
1 220 LYS n 
1 221 ALA n 
1 222 LEU n 
1 223 LYS n 
1 224 GLY n 
1 225 GLU n 
1 226 LYS n 
1 227 VAL n 
1 228 GLU n 
1 229 ALA n 
1 230 LYS n 
1 231 VAL n 
1 232 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   232 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SAOUHSC_01193 
_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      'Staphylococcus aureus subsp. aureus NCTC 8325' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     93061 
_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(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21(DE3)' 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET28a 
_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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
ALA 'L-peptide linking' y ALANINE                    ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                   ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                 ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'            ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                   ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                      ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'            ? 'Mg 2'              24.305  
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'     ? 'C8 H18 O5'         194.226 
PHE 'L-peptide linking' y PHENYLALANINE              ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                    ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                     ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                  ? 'C4 H9 N O3'        119.119 
TYR 'L-peptide linking' y TYROSINE                   ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                     ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  ?   ?   ?   A . n 
A 1 19  SER 19  -1  -1  SER SER A . n 
A 1 20  HIS 20  0   0   HIS HIS A . n 
A 1 21  MET 21  1   1   MET MET A . n 
A 1 22  ILE 22  2   2   ILE ILE A . n 
A 1 23  SER 23  3   3   SER SER A . n 
A 1 24  LYS 24  4   4   LYS LYS A . n 
A 1 25  ILE 25  5   5   ILE ILE A . n 
A 1 26  ASN 26  6   6   ASN ASN A . n 
A 1 27  GLY 27  7   7   GLY GLY A . n 
A 1 28  LYS 28  8   8   LYS LYS A . n 
A 1 29  LEU 29  9   9   LEU LEU A . n 
A 1 30  PHE 30  10  10  PHE PHE A . n 
A 1 31  ALA 31  11  11  ALA ALA A . n 
A 1 32  ASP 32  12  12  ASP ASP A . n 
A 1 33  MET 33  13  13  MET MET A . n 
A 1 34  ILE 34  14  14  ILE ILE A . n 
A 1 35  ILE 35  15  15  ILE ILE A . n 
A 1 36  GLN 36  16  16  GLN GLN A . n 
A 1 37  GLY 37  17  17  GLY GLY A . n 
A 1 38  ALA 38  18  18  ALA ALA A . n 
A 1 39  GLN 39  19  19  GLN GLN A . n 
A 1 40  ASN 40  20  20  ASN ASN A . n 
A 1 41  LEU 41  21  21  LEU LEU A . n 
A 1 42  SER 42  22  22  SER SER A . n 
A 1 43  ASN 43  23  23  ASN ASN A . n 
A 1 44  ASN 44  24  24  ASN ASN A . n 
A 1 45  ALA 45  25  25  ALA ALA A . n 
A 1 46  ASP 46  26  26  ASP ASP A . n 
A 1 47  LEU 47  27  27  LEU LEU A . n 
A 1 48  VAL 48  28  28  VAL VAL A . n 
A 1 49  ASP 49  29  29  ASP ASP A . n 
A 1 50  SER 50  30  30  SER SER A . n 
A 1 51  LEU 51  31  31  LEU LEU A . n 
A 1 52  ASN 52  32  32  ASN ASN A . n 
A 1 53  VAL 53  33  33  VAL VAL A . n 
A 1 54  TYR 54  34  34  TYR TYR A . n 
A 1 55  PRO 55  35  35  PRO PRO A . n 
A 1 56  VAL 56  36  36  VAL VAL A . n 
A 1 57  PRO 57  37  37  PRO PRO A . n 
A 1 58  ASP 58  38  38  ASP ASP A . n 
A 1 59  GLY 59  39  39  GLY GLY A . n 
A 1 60  ASP 60  40  40  ASP ASP A . n 
A 1 61  THR 61  41  41  THR THR A . n 
A 1 62  GLY 62  42  42  GLY GLY A . n 
A 1 63  THR 63  43  43  THR THR A . n 
A 1 64  ASN 64  44  44  ASN ASN A . n 
A 1 65  MET 65  45  45  MET MET A . n 
A 1 66  ASN 66  46  46  ASN ASN A . n 
A 1 67  LEU 67  47  47  LEU LEU A . n 
A 1 68  THR 68  48  48  THR THR A . n 
A 1 69  MET 69  49  49  MET MET A . n 
A 1 70  THR 70  50  50  THR THR A . n 
A 1 71  SER 71  51  51  SER SER A . n 
A 1 72  GLY 72  52  52  GLY GLY A . n 
A 1 73  ARG 73  53  53  ARG ARG A . n 
A 1 74  GLU 74  54  54  GLU GLU A . n 
A 1 75  GLU 75  55  55  GLU GLU A . n 
A 1 76  VAL 76  56  56  VAL VAL A . n 
A 1 77  GLU 77  57  57  GLU GLU A . n 
A 1 78  ASN 78  58  58  ASN ASN A . n 
A 1 79  ASN 79  59  59  ASN ASN A . n 
A 1 80  LEU 80  60  60  LEU LEU A . n 
A 1 81  SER 81  61  61  SER SER A . n 
A 1 82  LYS 82  62  62  LYS LYS A . n 
A 1 83  ASN 83  63  63  ASN ASN A . n 
A 1 84  ILE 84  64  64  ILE ILE A . n 
A 1 85  GLY 85  65  65  GLY GLY A . n 
A 1 86  GLU 86  66  66  GLU GLU A . n 
A 1 87  LEU 87  67  67  LEU LEU A . n 
A 1 88  GLY 88  68  68  GLY GLY A . n 
A 1 89  LYS 89  69  69  LYS LYS A . n 
A 1 90  THR 90  70  70  THR THR A . n 
A 1 91  PHE 91  71  71  PHE PHE A . n 
A 1 92  SER 92  72  72  SER SER A . n 
A 1 93  LYS 93  73  73  LYS LYS A . n 
A 1 94  GLY 94  74  74  GLY GLY A . n 
A 1 95  LEU 95  75  75  LEU LEU A . n 
A 1 96  LEU 96  76  76  LEU LEU A . n 
A 1 97  MET 97  77  77  MET MET A . n 
A 1 98  GLY 98  78  78  GLY GLY A . n 
A 1 99  ALA 99  79  79  ALA ALA A . n 
A 1 100 ARG 100 80  80  ARG ARG A . n 
A 1 101 GLY 101 81  81  GLY GLY A . n 
A 1 102 ASN 102 82  82  ASN ASN A . n 
A 1 103 SER 103 83  83  SER SER A . n 
A 1 104 GLY 104 84  84  GLY GLY A . n 
A 1 105 VAL 105 85  85  VAL VAL A . n 
A 1 106 ILE 106 86  86  ILE ILE A . n 
A 1 107 LEU 107 87  87  LEU LEU A . n 
A 1 108 SER 108 88  88  SER SER A . n 
A 1 109 GLN 109 89  89  GLN GLN A . n 
A 1 110 LEU 110 90  90  LEU LEU A . n 
A 1 111 PHE 111 91  91  PHE PHE A . n 
A 1 112 ARG 112 92  92  ARG ARG A . n 
A 1 113 GLY 113 93  93  GLY GLY A . n 
A 1 114 PHE 114 94  94  PHE PHE A . n 
A 1 115 CYS 115 95  95  CYS CYS A . n 
A 1 116 LYS 116 96  96  LYS LYS A . n 
A 1 117 ASN 117 97  97  ASN ASN A . n 
A 1 118 ILE 118 98  98  ILE ILE A . n 
A 1 119 GLU 119 99  99  GLU GLU A . n 
A 1 120 SER 120 100 100 SER SER A . n 
A 1 121 GLU 121 101 101 GLU GLU A . n 
A 1 122 SER 122 102 102 SER SER A . n 
A 1 123 GLU 123 103 103 GLU GLU A . n 
A 1 124 ILE 124 104 104 ILE ILE A . n 
A 1 125 ASN 125 105 105 ASN ASN A . n 
A 1 126 SER 126 106 106 SER SER A . n 
A 1 127 LYS 127 107 107 LYS LYS A . n 
A 1 128 LEU 128 108 108 LEU LEU A . n 
A 1 129 LEU 129 109 109 LEU LEU A . n 
A 1 130 ALA 130 110 110 ALA ALA A . n 
A 1 131 GLU 131 111 111 GLU GLU A . n 
A 1 132 SER 132 112 112 SER SER A . n 
A 1 133 PHE 133 113 113 PHE PHE A . n 
A 1 134 GLN 134 114 114 GLN GLN A . n 
A 1 135 ALA 135 115 115 ALA ALA A . n 
A 1 136 GLY 136 116 116 GLY GLY A . n 
A 1 137 VAL 137 117 117 VAL VAL A . n 
A 1 138 GLU 138 118 118 GLU GLU A . n 
A 1 139 THR 139 119 119 THR THR A . n 
A 1 140 ALA 140 120 120 ALA ALA A . n 
A 1 141 TYR 141 121 121 TYR TYR A . n 
A 1 142 LYS 142 122 122 LYS LYS A . n 
A 1 143 ALA 143 123 123 ALA ALA A . n 
A 1 144 VAL 144 124 124 VAL VAL A . n 
A 1 145 MET 145 125 125 MET MET A . n 
A 1 146 LYS 146 126 126 LYS LYS A . n 
A 1 147 PRO 147 127 127 PRO PRO A . n 
A 1 148 VAL 148 128 128 VAL VAL A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 GLY 150 130 130 GLY GLY A . n 
A 1 151 THR 151 131 131 THR THR A . n 
A 1 152 ILE 152 132 132 ILE ILE A . n 
A 1 153 LEU 153 133 133 LEU LEU A . n 
A 1 154 THR 154 134 134 THR THR A . n 
A 1 155 VAL 155 135 135 VAL VAL A . n 
A 1 156 ALA 156 136 136 ALA ALA A . n 
A 1 157 LYS 157 137 137 LYS LYS A . n 
A 1 158 ASP 158 138 138 ASP ASP A . n 
A 1 159 ALA 159 139 139 ALA ALA A . n 
A 1 160 ALA 160 140 140 ALA ALA A . n 
A 1 161 GLN 161 141 141 GLN GLN A . n 
A 1 162 ALA 162 142 142 ALA ALA A . n 
A 1 163 ALA 163 143 143 ALA ALA A . n 
A 1 164 ILE 164 144 144 ILE ILE A . n 
A 1 165 GLU 165 145 145 GLU GLU A . n 
A 1 166 LYS 166 146 146 LYS LYS A . n 
A 1 167 ALA 167 147 147 ALA ALA A . n 
A 1 168 ASN 168 148 148 ASN ASN A . n 
A 1 169 ASN 169 149 149 ASN ASN A . n 
A 1 170 THR 170 150 150 THR THR A . n 
A 1 171 GLU 171 151 151 GLU GLU A . n 
A 1 172 ASP 172 152 152 ASP ASP A . n 
A 1 173 CYS 173 153 153 CYS CYS A . n 
A 1 174 ILE 174 154 154 ILE ILE A . n 
A 1 175 GLU 175 155 155 GLU GLU A . n 
A 1 176 LEU 176 156 156 LEU LEU A . n 
A 1 177 MET 177 157 157 MET MET A . n 
A 1 178 GLU 178 158 158 GLU GLU A . n 
A 1 179 TYR 179 159 159 TYR TYR A . n 
A 1 180 ILE 180 160 160 ILE ILE A . n 
A 1 181 ILE 181 161 161 ILE ILE A . n 
A 1 182 VAL 182 162 162 VAL VAL A . n 
A 1 183 LYS 183 163 163 LYS LYS A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 ASN 185 165 165 ASN ASN A . n 
A 1 186 GLU 186 166 166 GLU GLU A . n 
A 1 187 SER 187 167 167 SER SER A . n 
A 1 188 LEU 188 168 168 LEU LEU A . n 
A 1 189 GLU 189 169 169 GLU GLU A . n 
A 1 190 ASN 190 170 170 ASN ASN A . n 
A 1 191 THR 191 171 171 THR THR A . n 
A 1 192 PRO 192 172 172 PRO PRO A . n 
A 1 193 ASN 193 173 173 ASN ASN A . n 
A 1 194 LEU 194 174 174 LEU LEU A . n 
A 1 195 LEU 195 175 175 LEU LEU A . n 
A 1 196 ALA 196 176 176 ALA ALA A . n 
A 1 197 VAL 197 177 177 VAL VAL A . n 
A 1 198 LEU 198 178 178 LEU LEU A . n 
A 1 199 LYS 199 179 179 LYS LYS A . n 
A 1 200 GLU 200 180 180 GLU GLU A . n 
A 1 201 VAL 201 181 181 VAL VAL A . n 
A 1 202 GLY 202 182 182 GLY GLY A . n 
A 1 203 VAL 203 183 183 VAL VAL A . n 
A 1 204 VAL 204 184 184 VAL VAL A . n 
A 1 205 ASP 205 185 185 ASP ASP A . n 
A 1 206 SER 206 186 186 SER SER A . n 
A 1 207 GLY 207 187 187 GLY GLY A . n 
A 1 208 GLY 208 188 188 GLY GLY A . n 
A 1 209 LYS 209 189 189 LYS LYS A . n 
A 1 210 GLY 210 190 190 GLY GLY A . n 
A 1 211 LEU 211 191 191 LEU LEU A . n 
A 1 212 LEU 212 192 192 LEU LEU A . n 
A 1 213 CYS 213 193 193 CYS CYS A . n 
A 1 214 VAL 214 194 194 VAL VAL A . n 
A 1 215 TYR 215 195 195 TYR TYR A . n 
A 1 216 GLU 216 196 196 GLU GLU A . n 
A 1 217 GLY 217 197 197 GLY GLY A . n 
A 1 218 PHE 218 198 198 PHE PHE A . n 
A 1 219 LEU 219 199 199 LEU LEU A . n 
A 1 220 LYS 220 200 200 LYS LYS A . n 
A 1 221 ALA 221 201 201 ALA ALA A . n 
A 1 222 LEU 222 202 202 LEU LEU A . n 
A 1 223 LYS 223 203 203 LYS LYS A . n 
A 1 224 GLY 224 204 204 GLY GLY A . n 
A 1 225 GLU 225 205 205 GLU GLU A . n 
A 1 226 LYS 226 206 206 LYS LYS A . n 
A 1 227 VAL 227 207 207 VAL VAL A . n 
A 1 228 GLU 228 208 208 GLU GLU A . n 
A 1 229 ALA 229 209 209 ALA ALA A . n 
A 1 230 LYS 230 210 210 LYS LYS A . n 
A 1 231 VAL 231 211 ?   ?   ?   A . n 
A 1 232 ALA 232 212 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ADP 1   301 1   ADP ADP A . 
C 3 MG  1   302 1   MG  MG  A . 
D 3 MG  1   303 2   MG  MG  A . 
E 4 PG4 1   304 1   PG4 PG4 A . 
F 5 HOH 1   401 117 HOH HOH A . 
F 5 HOH 2   402 130 HOH HOH A . 
F 5 HOH 3   403 143 HOH HOH A . 
F 5 HOH 4   404 50  HOH HOH A . 
F 5 HOH 5   405 171 HOH HOH A . 
F 5 HOH 6   406 100 HOH HOH A . 
F 5 HOH 7   407 39  HOH HOH A . 
F 5 HOH 8   408 62  HOH HOH A . 
F 5 HOH 9   409 8   HOH HOH A . 
F 5 HOH 10  410 55  HOH HOH A . 
F 5 HOH 11  411 126 HOH HOH A . 
F 5 HOH 12  412 91  HOH HOH A . 
F 5 HOH 13  413 134 HOH HOH A . 
F 5 HOH 14  414 89  HOH HOH A . 
F 5 HOH 15  415 72  HOH HOH A . 
F 5 HOH 16  416 52  HOH HOH A . 
F 5 HOH 17  417 177 HOH HOH A . 
F 5 HOH 18  418 101 HOH HOH A . 
F 5 HOH 19  419 118 HOH HOH A . 
F 5 HOH 20  420 54  HOH HOH A . 
F 5 HOH 21  421 46  HOH HOH A . 
F 5 HOH 22  422 121 HOH HOH A . 
F 5 HOH 23  423 154 HOH HOH A . 
F 5 HOH 24  424 78  HOH HOH A . 
F 5 HOH 25  425 75  HOH HOH A . 
F 5 HOH 26  426 112 HOH HOH A . 
F 5 HOH 27  427 6   HOH HOH A . 
F 5 HOH 28  428 14  HOH HOH A . 
F 5 HOH 29  429 92  HOH HOH A . 
F 5 HOH 30  430 11  HOH HOH A . 
F 5 HOH 31  431 43  HOH HOH A . 
F 5 HOH 32  432 2   HOH HOH A . 
F 5 HOH 33  433 127 HOH HOH A . 
F 5 HOH 34  434 105 HOH HOH A . 
F 5 HOH 35  435 114 HOH HOH A . 
F 5 HOH 36  436 56  HOH HOH A . 
F 5 HOH 37  437 152 HOH HOH A . 
F 5 HOH 38  438 20  HOH HOH A . 
F 5 HOH 39  439 64  HOH HOH A . 
F 5 HOH 40  440 68  HOH HOH A . 
F 5 HOH 41  441 16  HOH HOH A . 
F 5 HOH 42  442 33  HOH HOH A . 
F 5 HOH 43  443 27  HOH HOH A . 
F 5 HOH 44  444 106 HOH HOH A . 
F 5 HOH 45  445 45  HOH HOH A . 
F 5 HOH 46  446 88  HOH HOH A . 
F 5 HOH 47  447 140 HOH HOH A . 
F 5 HOH 48  448 17  HOH HOH A . 
F 5 HOH 49  449 40  HOH HOH A . 
F 5 HOH 50  450 168 HOH HOH A . 
F 5 HOH 51  451 158 HOH HOH A . 
F 5 HOH 52  452 113 HOH HOH A . 
F 5 HOH 53  453 18  HOH HOH A . 
F 5 HOH 54  454 146 HOH HOH A . 
F 5 HOH 55  455 48  HOH HOH A . 
F 5 HOH 56  456 66  HOH HOH A . 
F 5 HOH 57  457 120 HOH HOH A . 
F 5 HOH 58  458 4   HOH HOH A . 
F 5 HOH 59  459 181 HOH HOH A . 
F 5 HOH 60  460 3   HOH HOH A . 
F 5 HOH 61  461 22  HOH HOH A . 
F 5 HOH 62  462 80  HOH HOH A . 
F 5 HOH 63  463 164 HOH HOH A . 
F 5 HOH 64  464 5   HOH HOH A . 
F 5 HOH 65  465 1   HOH HOH A . 
F 5 HOH 66  466 82  HOH HOH A . 
F 5 HOH 67  467 139 HOH HOH A . 
F 5 HOH 68  468 41  HOH HOH A . 
F 5 HOH 69  469 15  HOH HOH A . 
F 5 HOH 70  470 102 HOH HOH A . 
F 5 HOH 71  471 10  HOH HOH A . 
F 5 HOH 72  472 44  HOH HOH A . 
F 5 HOH 73  473 136 HOH HOH A . 
F 5 HOH 74  474 124 HOH HOH A . 
F 5 HOH 75  475 19  HOH HOH A . 
F 5 HOH 76  476 132 HOH HOH A . 
F 5 HOH 77  477 7   HOH HOH A . 
F 5 HOH 78  478 13  HOH HOH A . 
F 5 HOH 79  479 21  HOH HOH A . 
F 5 HOH 80  480 162 HOH HOH A . 
F 5 HOH 81  481 86  HOH HOH A . 
F 5 HOH 82  482 85  HOH HOH A . 
F 5 HOH 83  483 30  HOH HOH A . 
F 5 HOH 84  484 99  HOH HOH A . 
F 5 HOH 85  485 53  HOH HOH A . 
F 5 HOH 86  486 24  HOH HOH A . 
F 5 HOH 87  487 103 HOH HOH A . 
F 5 HOH 88  488 9   HOH HOH A . 
F 5 HOH 89  489 141 HOH HOH A . 
F 5 HOH 90  490 25  HOH HOH A . 
F 5 HOH 91  491 47  HOH HOH A . 
F 5 HOH 92  492 119 HOH HOH A . 
F 5 HOH 93  493 34  HOH HOH A . 
F 5 HOH 94  494 36  HOH HOH A . 
F 5 HOH 95  495 182 HOH HOH A . 
F 5 HOH 96  496 153 HOH HOH A . 
F 5 HOH 97  497 122 HOH HOH A . 
F 5 HOH 98  498 147 HOH HOH A . 
F 5 HOH 99  499 173 HOH HOH A . 
F 5 HOH 100 500 38  HOH HOH A . 
F 5 HOH 101 501 57  HOH HOH A . 
F 5 HOH 102 502 32  HOH HOH A . 
F 5 HOH 103 503 28  HOH HOH A . 
F 5 HOH 104 504 87  HOH HOH A . 
F 5 HOH 105 505 49  HOH HOH A . 
F 5 HOH 106 506 42  HOH HOH A . 
F 5 HOH 107 507 104 HOH HOH A . 
F 5 HOH 108 508 35  HOH HOH A . 
F 5 HOH 109 509 31  HOH HOH A . 
F 5 HOH 110 510 174 HOH HOH A . 
F 5 HOH 111 511 96  HOH HOH A . 
F 5 HOH 112 512 29  HOH HOH A . 
F 5 HOH 113 513 83  HOH HOH A . 
F 5 HOH 114 514 179 HOH HOH A . 
F 5 HOH 115 515 116 HOH HOH A . 
F 5 HOH 116 516 133 HOH HOH A . 
F 5 HOH 117 517 23  HOH HOH A . 
F 5 HOH 118 518 84  HOH HOH A . 
F 5 HOH 119 519 144 HOH HOH A . 
F 5 HOH 120 520 178 HOH HOH A . 
F 5 HOH 121 521 148 HOH HOH A . 
F 5 HOH 122 522 76  HOH HOH A . 
F 5 HOH 123 523 108 HOH HOH A . 
F 5 HOH 124 524 79  HOH HOH A . 
F 5 HOH 125 525 97  HOH HOH A . 
F 5 HOH 126 526 172 HOH HOH A . 
F 5 HOH 127 527 51  HOH HOH A . 
F 5 HOH 128 528 67  HOH HOH A . 
F 5 HOH 129 529 73  HOH HOH A . 
F 5 HOH 130 530 115 HOH HOH A . 
F 5 HOH 131 531 137 HOH HOH A . 
F 5 HOH 132 532 98  HOH HOH A . 
F 5 HOH 133 533 155 HOH HOH A . 
F 5 HOH 134 534 135 HOH HOH A . 
F 5 HOH 135 535 26  HOH HOH A . 
F 5 HOH 136 536 167 HOH HOH A . 
F 5 HOH 137 537 65  HOH HOH A . 
F 5 HOH 138 538 176 HOH HOH A . 
F 5 HOH 139 539 37  HOH HOH A . 
F 5 HOH 140 540 93  HOH HOH A . 
F 5 HOH 141 541 12  HOH HOH A . 
F 5 HOH 142 542 129 HOH HOH A . 
F 5 HOH 143 543 180 HOH HOH A . 
F 5 HOH 144 544 131 HOH HOH A . 
F 5 HOH 145 545 110 HOH HOH A . 
F 5 HOH 146 546 109 HOH HOH A . 
F 5 HOH 147 547 60  HOH HOH A . 
F 5 HOH 148 548 74  HOH HOH A . 
F 5 HOH 149 549 70  HOH HOH A . 
F 5 HOH 150 550 123 HOH HOH A . 
F 5 HOH 151 551 150 HOH HOH A . 
F 5 HOH 152 552 183 HOH HOH A . 
F 5 HOH 153 553 94  HOH HOH A . 
F 5 HOH 154 554 77  HOH HOH A . 
F 5 HOH 155 555 169 HOH HOH A . 
F 5 HOH 156 556 95  HOH HOH A . 
F 5 HOH 157 557 138 HOH HOH A . 
F 5 HOH 158 558 58  HOH HOH A . 
F 5 HOH 159 559 170 HOH HOH A . 
F 5 HOH 160 560 59  HOH HOH A . 
F 5 HOH 161 561 111 HOH HOH A . 
F 5 HOH 162 562 142 HOH HOH A . 
F 5 HOH 163 563 186 HOH HOH A . 
F 5 HOH 164 564 184 HOH HOH A . 
F 5 HOH 165 565 160 HOH HOH A . 
F 5 HOH 166 566 149 HOH HOH A . 
F 5 HOH 167 567 161 HOH HOH A . 
F 5 HOH 168 568 81  HOH HOH A . 
F 5 HOH 169 569 90  HOH HOH A . 
F 5 HOH 170 570 145 HOH HOH A . 
F 5 HOH 171 571 166 HOH HOH A . 
F 5 HOH 172 572 151 HOH HOH A . 
F 5 HOH 173 573 165 HOH HOH A . 
F 5 HOH 174 574 125 HOH HOH A . 
F 5 HOH 175 575 175 HOH HOH A . 
F 5 HOH 176 576 156 HOH HOH A . 
F 5 HOH 177 577 185 HOH HOH A . 
F 5 HOH 178 578 61  HOH HOH A . 
F 5 HOH 179 579 63  HOH HOH A . 
F 5 HOH 180 580 157 HOH HOH A . 
F 5 HOH 181 581 69  HOH HOH A . 
F 5 HOH 182 582 71  HOH HOH A . 
F 5 HOH 183 583 163 HOH HOH A . 
F 5 HOH 184 584 107 HOH HOH A . 
F 5 HOH 185 585 159 HOH HOH A . 
F 5 HOH 186 586 128 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A HIS 0   ? CG  ? A HIS 20  CG  
2  1 Y 1 A HIS 0   ? ND1 ? A HIS 20  ND1 
3  1 Y 1 A HIS 0   ? CD2 ? A HIS 20  CD2 
4  1 Y 1 A HIS 0   ? CE1 ? A HIS 20  CE1 
5  1 Y 1 A HIS 0   ? NE2 ? A HIS 20  NE2 
6  1 Y 1 A LYS 4   ? CD  ? A LYS 24  CD  
7  1 Y 1 A LYS 4   ? CE  ? A LYS 24  CE  
8  1 Y 1 A LYS 4   ? NZ  ? A LYS 24  NZ  
9  1 Y 1 A LYS 73  ? CD  ? A LYS 93  CD  
10 1 Y 1 A LYS 73  ? CE  ? A LYS 93  CE  
11 1 Y 1 A LYS 73  ? NZ  ? A LYS 93  NZ  
12 1 Y 1 A ARG 80  ? CD  ? A ARG 100 CD  
13 1 Y 1 A ARG 80  ? NE  ? A ARG 100 NE  
14 1 Y 1 A ARG 80  ? CZ  ? A ARG 100 CZ  
15 1 Y 1 A ARG 80  ? NH1 ? A ARG 100 NH1 
16 1 Y 1 A ARG 80  ? NH2 ? A ARG 100 NH2 
17 1 Y 1 A LYS 107 ? CD  ? A LYS 127 CD  
18 1 Y 1 A LYS 107 ? CE  ? A LYS 127 CE  
19 1 Y 1 A LYS 107 ? NZ  ? A LYS 127 NZ  
20 1 Y 1 A LYS 122 ? CE  ? A LYS 142 CE  
21 1 Y 1 A LYS 122 ? NZ  ? A LYS 142 NZ  
22 1 Y 1 A GLU 151 ? CD  ? A GLU 171 CD  
23 1 Y 1 A GLU 151 ? OE1 ? A GLU 171 OE1 
24 1 Y 1 A GLU 151 ? OE2 ? A GLU 171 OE2 
25 1 Y 1 A LYS 179 ? CE  ? A LYS 199 CE  
26 1 Y 1 A LYS 179 ? NZ  ? A LYS 199 NZ  
27 1 Y 1 A LYS 206 ? CD  ? A LYS 226 CD  
28 1 Y 1 A LYS 206 ? CE  ? A LYS 226 CE  
29 1 Y 1 A LYS 206 ? NZ  ? A LYS 226 NZ  
30 1 Y 1 A GLU 208 ? CG  ? A GLU 228 CG  
31 1 Y 1 A GLU 208 ? CD  ? A GLU 228 CD  
32 1 Y 1 A GLU 208 ? OE1 ? A GLU 228 OE1 
33 1 Y 1 A GLU 208 ? OE2 ? A GLU 228 OE2 
34 1 Y 1 A LYS 210 ? CG  ? A LYS 230 CG  
35 1 Y 1 A LYS 210 ? CD  ? A LYS 230 CD  
36 1 Y 1 A LYS 210 ? CE  ? A LYS 230 CE  
37 1 Y 1 A LYS 210 ? NZ  ? A LYS 230 NZ  
38 1 N 1 A PG4 304 ? O1  ? E PG4 1   O1  
39 1 N 1 A PG4 304 ? C1  ? E PG4 1   C1  
# 
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  ? ? ? '(1.17rc1_3605: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                     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                     8VIT 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.936 
_cell.length_a_esd                 ? 
_cell.length_b                     57.094 
_cell.length_b_esd                 ? 
_cell.length_c                     81.029 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VIT 
_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                   8VIT 
_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             2.00 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.53 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              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    
;Proplex C3: 20% (w/v) PEG 4000, 100 mM sodium acetate pH 5.0, 200 mM ammonium acetate, Cryo: 80% well solution and 20% (v/v) PEG 200, 2.5 mM MgCl2 and 2.5 mM ADP added to the protein prior to crystallization.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-06-15 
_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                    'Double Crystal Si 111' 
_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   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 17-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   17-ID 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8VIT 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.25 
_reflns.d_resolution_low                               46.67 
_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                                     55921 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.95 
_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                                0.058 
_reflns.pdbx_Rpim_I_all                                0.023 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       353128 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.25 
_reflns_shell.d_res_low                                     1.27 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           16710 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2765 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.0 
_reflns_shell.pdbx_chi_squared                              0.94 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.5 
_reflns_shell.pdbx_Rrim_I_all                               1.263 
_reflns_shell.pdbx_Rpim_I_all                               0.511 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.754 
_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                                  1.152 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8VIT 
_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                             34.32 
_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                     55824 
_refine.ls_number_reflns_R_free                  2753 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.91 
_refine.ls_percent_reflns_R_free                 4.93 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1390 
_refine.ls_R_factor_R_free                       0.1607 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1379 
_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                          1.04 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 16.44 
_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                            0.11 
_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                        34.32 
_refine_hist.number_atoms_solvent             186 
_refine_hist.number_atoms_total               1773 
_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        1547 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         40 
_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' ? 0.006  ? 1645 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.980  ? 2237 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.315 ? 617  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.066  ? 268  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005  ? 289  ? 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 1.27  . . 138 2646 100.00 . . . . 0.2399 . . . . . . . . . . . 0.3023 
'X-RAY DIFFRACTION' 1.27 1.29  . . 136 2586 100.00 . . . . 0.2249 . . . . . . . . . . . 0.2633 
'X-RAY DIFFRACTION' 1.29 1.32  . . 132 2617 100.00 . . . . 0.2121 . . . . . . . . . . . 0.1962 
'X-RAY DIFFRACTION' 1.32 1.35  . . 140 2620 100.00 . . . . 0.1868 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 1.35 1.38  . . 139 2615 100.00 . . . . 0.1823 . . . . . . . . . . . 0.2183 
'X-RAY DIFFRACTION' 1.38 1.41  . . 146 2611 100.00 . . . . 0.1683 . . . . . . . . . . . 0.1920 
'X-RAY DIFFRACTION' 1.41 1.44  . . 147 2604 100.00 . . . . 0.1530 . . . . . . . . . . . 0.2177 
'X-RAY DIFFRACTION' 1.44 1.48  . . 133 2653 100.00 . . . . 0.1273 . . . . . . . . . . . 0.1693 
'X-RAY DIFFRACTION' 1.48 1.53  . . 124 2643 100.00 . . . . 0.1218 . . . . . . . . . . . 0.1382 
'X-RAY DIFFRACTION' 1.53 1.57  . . 127 2619 100.00 . . . . 0.1129 . . . . . . . . . . . 0.1530 
'X-RAY DIFFRACTION' 1.57 1.63  . . 151 2620 100.00 . . . . 0.1111 . . . . . . . . . . . 0.1436 
'X-RAY DIFFRACTION' 1.63 1.70  . . 129 2653 100.00 . . . . 0.1073 . . . . . . . . . . . 0.1432 
'X-RAY DIFFRACTION' 1.70 1.77  . . 135 2652 100.00 . . . . 0.1164 . . . . . . . . . . . 0.1479 
'X-RAY DIFFRACTION' 1.77 1.87  . . 137 2663 100.00 . . . . 0.1252 . . . . . . . . . . . 0.1519 
'X-RAY DIFFRACTION' 1.87 1.98  . . 128 2678 100.00 . . . . 0.1250 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 1.98 2.14  . . 138 2646 100.00 . . . . 0.1217 . . . . . . . . . . . 0.1442 
'X-RAY DIFFRACTION' 2.14 2.35  . . 132 2688 100.00 . . . . 0.1241 . . . . . . . . . . . 0.1436 
'X-RAY DIFFRACTION' 2.35 2.69  . . 129 2714 100.00 . . . . 0.1298 . . . . . . . . . . . 0.1642 
'X-RAY DIFFRACTION' 2.69 3.39  . . 156 2708 100.00 . . . . 0.1455 . . . . . . . . . . . 0.1521 
'X-RAY DIFFRACTION' 3.39 34.32 . . 156 2835 100.00 . . . . 0.1456 . . . . . . . . . . . 0.1574 
# 
_struct.entry_id                     8VIT 
_struct.title                        
'Crystal structure of the N-terminal domain of fatty acid kinase A (FakA) from Staphylococcus aureus (Mg and ADP)' 
_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        8VIT 
_struct_keywords.text            
'Fatty Acid Kinase A, Staphylococcus aureus, MRSA, proline isomerization, fatty acid metabolism, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Y1193_STAA8 
_struct_ref.pdbx_db_accession          Q2FZ58 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MISKINGKLFADMIIQGAQNLSNNADLVDSLNVYPVPDGDTGTNMNLTMTSGREEVENNLSKNIGELGKTFSKGLLMGAR
GNSGVILSQLFRGFCKNIESESEINSKLLAESFQAGVETAYKAVMKPVEGTILTVAKDAAQAAIEKANNTEDCIELMEYI
IVKANESLENTPNLLAVLKEVGVVDSGGKGLLCVYEGFLKALKGEKVEAKVA
;
_struct_ref.pdbx_align_begin           0 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VIT 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 232 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q2FZ58 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  212 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       212 
# 
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 8VIT MET A 1  ? UNP Q2FZ58 ? ? 'expression tag' -19 1  
1 8VIT GLY A 2  ? UNP Q2FZ58 ? ? 'expression tag' -18 2  
1 8VIT SER A 3  ? UNP Q2FZ58 ? ? 'expression tag' -17 3  
1 8VIT SER A 4  ? UNP Q2FZ58 ? ? 'expression tag' -16 4  
1 8VIT HIS A 5  ? UNP Q2FZ58 ? ? 'expression tag' -15 5  
1 8VIT HIS A 6  ? UNP Q2FZ58 ? ? 'expression tag' -14 6  
1 8VIT HIS A 7  ? UNP Q2FZ58 ? ? 'expression tag' -13 7  
1 8VIT HIS A 8  ? UNP Q2FZ58 ? ? 'expression tag' -12 8  
1 8VIT HIS A 9  ? UNP Q2FZ58 ? ? 'expression tag' -11 9  
1 8VIT HIS A 10 ? UNP Q2FZ58 ? ? 'expression tag' -10 10 
1 8VIT SER A 11 ? UNP Q2FZ58 ? ? 'expression tag' -9  11 
1 8VIT SER A 12 ? UNP Q2FZ58 ? ? 'expression tag' -8  12 
1 8VIT GLY A 13 ? UNP Q2FZ58 ? ? 'expression tag' -7  13 
1 8VIT LEU A 14 ? UNP Q2FZ58 ? ? 'expression tag' -6  14 
1 8VIT VAL A 15 ? UNP Q2FZ58 ? ? 'expression tag' -5  15 
1 8VIT PRO A 16 ? UNP Q2FZ58 ? ? 'expression tag' -4  16 
1 8VIT ARG A 17 ? UNP Q2FZ58 ? ? 'expression tag' -3  17 
1 8VIT GLY A 18 ? UNP Q2FZ58 ? ? 'expression tag' -2  18 
1 8VIT SER A 19 ? UNP Q2FZ58 ? ? 'expression tag' -1  19 
1 8VIT HIS A 20 ? UNP Q2FZ58 ? ? 'expression tag' 0   20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 26  ? ASN A 44  ? ASN A 6   ASN A 24  1 ? 19 
HELX_P HELX_P2  AA2 ASN A 44  ? ASN A 52  ? ASN A 24  ASN A 32  1 ? 9  
HELX_P HELX_P3  AA3 ASP A 60  ? ASN A 79  ? ASP A 40  ASN A 59  1 ? 20 
HELX_P HELX_P4  AA4 ASN A 83  ? MET A 97  ? ASN A 63  MET A 77  1 ? 15 
HELX_P HELX_P5  AA5 ARG A 100 ? ILE A 118 ? ARG A 80  ILE A 98  1 ? 19 
HELX_P HELX_P6  AA6 ASN A 125 ? VAL A 144 ? ASN A 105 VAL A 124 1 ? 20 
HELX_P HELX_P7  AA7 THR A 151 ? ASN A 168 ? THR A 131 ASN A 148 1 ? 18 
HELX_P HELX_P8  AA8 ASP A 172 ? THR A 191 ? ASP A 152 THR A 171 1 ? 20 
HELX_P HELX_P9  AA9 PRO A 192 ? LEU A 194 ? PRO A 172 LEU A 174 5 ? 3  
HELX_P HELX_P10 AB1 LEU A 195 ? GLY A 202 ? LEU A 175 GLY A 182 1 ? 8  
HELX_P HELX_P11 AB2 ASP A 205 ? LYS A 223 ? ASP A 185 LYS A 203 1 ? 19 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASN 52 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASN 32  A MG  302 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc2  metalc ? ? A ASP 58 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASP 38  A MG  302 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc3  metalc ? ? A ASP 58 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 38  A MG  303 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc4  metalc ? ? A ASP 60 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASP 40  A MG  302 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc5  metalc ? ? A ASP 60 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 40  A MG  303 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc6  metalc ? ? B ADP .  O3B ? ? ? 1_555 C MG  . MG ? ? A ADP 301 A MG  302 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc7  metalc ? ? B ADP .  O2A ? ? ? 1_555 C MG  . MG ? ? A ADP 301 A MG  302 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc8  metalc ? ? B ADP .  O3B ? ? ? 1_555 D MG  . MG ? ? A ADP 301 A MG  303 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc9  metalc ? ? C MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  302 A HOH 460 1_555 ? ? ? ? ? ? ? 2.122 ? ? 
metalc10 metalc ? ? D MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  303 A HOH 409 2_455 ? ? ? ? ? ? ? 2.138 ? ? 
metalc11 metalc ? ? D MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  303 A HOH 443 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc12 metalc ? ? D MG  .  MG  ? ? ? 1_555 F HOH . O  ? ? A MG  303 A HOH 502 1_555 ? ? ? ? ? ? ? 2.104 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 OD1 ? A ASP 58 ? A ASP 38  ? 1_555 85.3  ? 
2  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 91.1  ? 
3  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 88.4  ? 
4  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O3B ? B ADP .  ? A ADP 301 ? 1_555 174.2 ? 
5  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O3B ? B ADP .  ? A ADP 301 ? 1_555 99.6  ? 
6  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O3B ? B ADP .  ? A ADP 301 ? 1_555 92.1  ? 
7  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2A ? B ADP .  ? A ADP 301 ? 1_555 86.2  ? 
8  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2A ? B ADP .  ? A ADP 301 ? 1_555 171.4 ? 
9  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2A ? B ADP .  ? A ADP 301 ? 1_555 90.6  ? 
10 O3B ? B ADP .  ? A ADP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2A ? B ADP .  ? A ADP 301 ? 1_555 88.9  ? 
11 OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? F HOH .  ? A HOH 460 ? 1_555 90.0  ? 
12 OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? F HOH .  ? A HOH 460 ? 1_555 88.4  ? 
13 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? F HOH .  ? A HOH 460 ? 1_555 176.6 ? 
14 O3B ? B ADP .  ? A ADP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? F HOH .  ? A HOH 460 ? 1_555 87.2  ? 
15 O2A ? B ADP .  ? A ADP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? F HOH .  ? A HOH 460 ? 1_555 92.7  ? 
16 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 93.3  ? 
17 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O3B ? B ADP .  ? A ADP 301 ? 1_555 95.5  ? 
18 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O3B ? B ADP .  ? A ADP 301 ? 1_555 93.2  ? 
19 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 409 ? 2_455 89.0  ? 
20 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 409 ? 2_455 83.6  ? 
21 O3B ? B ADP .  ? A ADP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 409 ? 2_455 174.7 ? 
22 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 443 ? 1_555 175.3 ? 
23 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 443 ? 1_555 91.3  ? 
24 O3B ? B ADP .  ? A ADP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 443 ? 1_555 85.1  ? 
25 O   ? F HOH .  ? A HOH 409 ? 2_455 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 443 ? 1_555 90.7  ? 
26 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 502 ? 1_555 87.3  ? 
27 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 502 ? 1_555 173.3 ? 
28 O3B ? B ADP .  ? A ADP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 502 ? 1_555 93.4  ? 
29 O   ? F HOH .  ? A HOH 409 ? 2_455 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 502 ? 1_555 89.7  ? 
30 O   ? F HOH .  ? A HOH 443 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? F HOH .  ? A HOH 502 ? 1_555 88.0  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           54 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            34 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    55 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     35 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.66 
# 
_pdbx_entry_details.entry_id                   8VIT 
_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_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     59 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -150.36 
_pdbx_validate_torsion.psi             70.17 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A GLY -2  ? A GLY 18  
19 1 Y 1 A VAL 211 ? A VAL 231 
20 1 Y 1 A ALA 212 ? A ALA 232 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CYS N      N  N N 116 
CYS CA     C  N R 117 
CYS C      C  N N 118 
CYS O      O  N N 119 
CYS CB     C  N N 120 
CYS SG     S  N N 121 
CYS OXT    O  N N 122 
CYS H      H  N N 123 
CYS H2     H  N N 124 
CYS HA     H  N N 125 
CYS HB2    H  N N 126 
CYS HB3    H  N N 127 
CYS HG     H  N N 128 
CYS HXT    H  N N 129 
GLN N      N  N N 130 
GLN CA     C  N S 131 
GLN C      C  N N 132 
GLN O      O  N N 133 
GLN CB     C  N N 134 
GLN CG     C  N N 135 
GLN CD     C  N N 136 
GLN OE1    O  N N 137 
GLN NE2    N  N N 138 
GLN OXT    O  N N 139 
GLN H      H  N N 140 
GLN H2     H  N N 141 
GLN HA     H  N N 142 
GLN HB2    H  N N 143 
GLN HB3    H  N N 144 
GLN HG2    H  N N 145 
GLN HG3    H  N N 146 
GLN HE21   H  N N 147 
GLN HE22   H  N N 148 
GLN HXT    H  N N 149 
GLU N      N  N N 150 
GLU CA     C  N S 151 
GLU C      C  N N 152 
GLU O      O  N N 153 
GLU CB     C  N N 154 
GLU CG     C  N N 155 
GLU CD     C  N N 156 
GLU OE1    O  N N 157 
GLU OE2    O  N N 158 
GLU OXT    O  N N 159 
GLU H      H  N N 160 
GLU H2     H  N N 161 
GLU HA     H  N N 162 
GLU HB2    H  N N 163 
GLU HB3    H  N N 164 
GLU HG2    H  N N 165 
GLU HG3    H  N N 166 
GLU HE2    H  N N 167 
GLU HXT    H  N N 168 
GLY N      N  N N 169 
GLY CA     C  N N 170 
GLY C      C  N N 171 
GLY O      O  N N 172 
GLY OXT    O  N N 173 
GLY H      H  N N 174 
GLY H2     H  N N 175 
GLY HA2    H  N N 176 
GLY HA3    H  N N 177 
GLY HXT    H  N N 178 
HIS N      N  N N 179 
HIS CA     C  N S 180 
HIS C      C  N N 181 
HIS O      O  N N 182 
HIS CB     C  N N 183 
HIS CG     C  Y N 184 
HIS ND1    N  Y N 185 
HIS CD2    C  Y N 186 
HIS CE1    C  Y N 187 
HIS NE2    N  Y N 188 
HIS OXT    O  N N 189 
HIS H      H  N N 190 
HIS H2     H  N N 191 
HIS HA     H  N N 192 
HIS HB2    H  N N 193 
HIS HB3    H  N N 194 
HIS HD1    H  N N 195 
HIS HD2    H  N N 196 
HIS HE1    H  N N 197 
HIS HE2    H  N N 198 
HIS HXT    H  N N 199 
HOH O      O  N N 200 
HOH H1     H  N N 201 
HOH H2     H  N N 202 
ILE N      N  N N 203 
ILE CA     C  N S 204 
ILE C      C  N N 205 
ILE O      O  N N 206 
ILE CB     C  N S 207 
ILE CG1    C  N N 208 
ILE CG2    C  N N 209 
ILE CD1    C  N N 210 
ILE OXT    O  N N 211 
ILE H      H  N N 212 
ILE H2     H  N N 213 
ILE HA     H  N N 214 
ILE HB     H  N N 215 
ILE HG12   H  N N 216 
ILE HG13   H  N N 217 
ILE HG21   H  N N 218 
ILE HG22   H  N N 219 
ILE HG23   H  N N 220 
ILE HD11   H  N N 221 
ILE HD12   H  N N 222 
ILE HD13   H  N N 223 
ILE HXT    H  N N 224 
LEU N      N  N N 225 
LEU CA     C  N S 226 
LEU C      C  N N 227 
LEU O      O  N N 228 
LEU CB     C  N N 229 
LEU CG     C  N N 230 
LEU CD1    C  N N 231 
LEU CD2    C  N N 232 
LEU OXT    O  N N 233 
LEU H      H  N N 234 
LEU H2     H  N N 235 
LEU HA     H  N N 236 
LEU HB2    H  N N 237 
LEU HB3    H  N N 238 
LEU HG     H  N N 239 
LEU HD11   H  N N 240 
LEU HD12   H  N N 241 
LEU HD13   H  N N 242 
LEU HD21   H  N N 243 
LEU HD22   H  N N 244 
LEU HD23   H  N N 245 
LEU HXT    H  N N 246 
LYS N      N  N N 247 
LYS CA     C  N S 248 
LYS C      C  N N 249 
LYS O      O  N N 250 
LYS CB     C  N N 251 
LYS CG     C  N N 252 
LYS CD     C  N N 253 
LYS CE     C  N N 254 
LYS NZ     N  N N 255 
LYS OXT    O  N N 256 
LYS H      H  N N 257 
LYS H2     H  N N 258 
LYS HA     H  N N 259 
LYS HB2    H  N N 260 
LYS HB3    H  N N 261 
LYS HG2    H  N N 262 
LYS HG3    H  N N 263 
LYS HD2    H  N N 264 
LYS HD3    H  N N 265 
LYS HE2    H  N N 266 
LYS HE3    H  N N 267 
LYS HZ1    H  N N 268 
LYS HZ2    H  N N 269 
LYS HZ3    H  N N 270 
LYS HXT    H  N N 271 
MET N      N  N N 272 
MET CA     C  N S 273 
MET C      C  N N 274 
MET O      O  N N 275 
MET CB     C  N N 276 
MET CG     C  N N 277 
MET SD     S  N N 278 
MET CE     C  N N 279 
MET OXT    O  N N 280 
MET H      H  N N 281 
MET H2     H  N N 282 
MET HA     H  N N 283 
MET HB2    H  N N 284 
MET HB3    H  N N 285 
MET HG2    H  N N 286 
MET HG3    H  N N 287 
MET HE1    H  N N 288 
MET HE2    H  N N 289 
MET HE3    H  N N 290 
MET HXT    H  N N 291 
MG  MG     MG N N 292 
PG4 O1     O  N N 293 
PG4 C1     C  N N 294 
PG4 C2     C  N N 295 
PG4 O2     O  N N 296 
PG4 C3     C  N N 297 
PG4 C4     C  N N 298 
PG4 O3     O  N N 299 
PG4 C5     C  N N 300 
PG4 C6     C  N N 301 
PG4 O4     O  N N 302 
PG4 C7     C  N N 303 
PG4 C8     C  N N 304 
PG4 O5     O  N N 305 
PG4 HO1    H  N N 306 
PG4 H11    H  N N 307 
PG4 H12    H  N N 308 
PG4 H21    H  N N 309 
PG4 H22    H  N N 310 
PG4 H31    H  N N 311 
PG4 H32    H  N N 312 
PG4 H41    H  N N 313 
PG4 H42    H  N N 314 
PG4 H51    H  N N 315 
PG4 H52    H  N N 316 
PG4 H61    H  N N 317 
PG4 H62    H  N N 318 
PG4 H71    H  N N 319 
PG4 H72    H  N N 320 
PG4 H81    H  N N 321 
PG4 H82    H  N N 322 
PG4 HO5    H  N N 323 
PHE N      N  N N 324 
PHE CA     C  N S 325 
PHE C      C  N N 326 
PHE O      O  N N 327 
PHE CB     C  N N 328 
PHE CG     C  Y N 329 
PHE CD1    C  Y N 330 
PHE CD2    C  Y N 331 
PHE CE1    C  Y N 332 
PHE CE2    C  Y N 333 
PHE CZ     C  Y N 334 
PHE OXT    O  N N 335 
PHE H      H  N N 336 
PHE H2     H  N N 337 
PHE HA     H  N N 338 
PHE HB2    H  N N 339 
PHE HB3    H  N N 340 
PHE HD1    H  N N 341 
PHE HD2    H  N N 342 
PHE HE1    H  N N 343 
PHE HE2    H  N N 344 
PHE HZ     H  N N 345 
PHE HXT    H  N N 346 
PRO N      N  N N 347 
PRO CA     C  N S 348 
PRO C      C  N N 349 
PRO O      O  N N 350 
PRO CB     C  N N 351 
PRO CG     C  N N 352 
PRO CD     C  N N 353 
PRO OXT    O  N N 354 
PRO H      H  N N 355 
PRO HA     H  N N 356 
PRO HB2    H  N N 357 
PRO HB3    H  N N 358 
PRO HG2    H  N N 359 
PRO HG3    H  N N 360 
PRO HD2    H  N N 361 
PRO HD3    H  N N 362 
PRO HXT    H  N N 363 
SER N      N  N N 364 
SER CA     C  N S 365 
SER C      C  N N 366 
SER O      O  N N 367 
SER CB     C  N N 368 
SER OG     O  N N 369 
SER OXT    O  N N 370 
SER H      H  N N 371 
SER H2     H  N N 372 
SER HA     H  N N 373 
SER HB2    H  N N 374 
SER HB3    H  N N 375 
SER HG     H  N N 376 
SER HXT    H  N N 377 
THR N      N  N N 378 
THR CA     C  N S 379 
THR C      C  N N 380 
THR O      O  N N 381 
THR CB     C  N R 382 
THR OG1    O  N N 383 
THR CG2    C  N N 384 
THR OXT    O  N N 385 
THR H      H  N N 386 
THR H2     H  N N 387 
THR HA     H  N N 388 
THR HB     H  N N 389 
THR HG1    H  N N 390 
THR HG21   H  N N 391 
THR HG22   H  N N 392 
THR HG23   H  N N 393 
THR HXT    H  N N 394 
TYR N      N  N N 395 
TYR CA     C  N S 396 
TYR C      C  N N 397 
TYR O      O  N N 398 
TYR CB     C  N N 399 
TYR CG     C  Y N 400 
TYR CD1    C  Y N 401 
TYR CD2    C  Y N 402 
TYR CE1    C  Y N 403 
TYR CE2    C  Y N 404 
TYR CZ     C  Y N 405 
TYR OH     O  N N 406 
TYR OXT    O  N N 407 
TYR H      H  N N 408 
TYR H2     H  N N 409 
TYR HA     H  N N 410 
TYR HB2    H  N N 411 
TYR HB3    H  N N 412 
TYR HD1    H  N N 413 
TYR HD2    H  N N 414 
TYR HE1    H  N N 415 
TYR HE2    H  N N 416 
TYR HH     H  N N 417 
TYR HXT    H  N N 418 
VAL N      N  N N 419 
VAL CA     C  N S 420 
VAL C      C  N N 421 
VAL O      O  N N 422 
VAL CB     C  N N 423 
VAL CG1    C  N N 424 
VAL CG2    C  N N 425 
VAL OXT    O  N N 426 
VAL H      H  N N 427 
VAL H2     H  N N 428 
VAL HA     H  N N 429 
VAL HB     H  N N 430 
VAL HG11   H  N N 431 
VAL HG12   H  N N 432 
VAL HG13   H  N N 433 
VAL HG21   H  N N 434 
VAL HG22   H  N N 435 
VAL HG23   H  N N 436 
VAL HXT    H  N N 437 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GLN N     CA     sing N N 127 
GLN N     H      sing N N 128 
GLN N     H2     sing N N 129 
GLN CA    C      sing N N 130 
GLN CA    CB     sing N N 131 
GLN CA    HA     sing N N 132 
GLN C     O      doub N N 133 
GLN C     OXT    sing N N 134 
GLN CB    CG     sing N N 135 
GLN CB    HB2    sing N N 136 
GLN CB    HB3    sing N N 137 
GLN CG    CD     sing N N 138 
GLN CG    HG2    sing N N 139 
GLN CG    HG3    sing N N 140 
GLN CD    OE1    doub N N 141 
GLN CD    NE2    sing N N 142 
GLN NE2   HE21   sing N N 143 
GLN NE2   HE22   sing N N 144 
GLN OXT   HXT    sing N N 145 
GLU N     CA     sing N N 146 
GLU N     H      sing N N 147 
GLU N     H2     sing N N 148 
GLU CA    C      sing N N 149 
GLU CA    CB     sing N N 150 
GLU CA    HA     sing N N 151 
GLU C     O      doub N N 152 
GLU C     OXT    sing N N 153 
GLU CB    CG     sing N N 154 
GLU CB    HB2    sing N N 155 
GLU CB    HB3    sing N N 156 
GLU CG    CD     sing N N 157 
GLU CG    HG2    sing N N 158 
GLU CG    HG3    sing N N 159 
GLU CD    OE1    doub N N 160 
GLU CD    OE2    sing N N 161 
GLU OE2   HE2    sing N N 162 
GLU OXT   HXT    sing N N 163 
GLY N     CA     sing N N 164 
GLY N     H      sing N N 165 
GLY N     H2     sing N N 166 
GLY CA    C      sing N N 167 
GLY CA    HA2    sing N N 168 
GLY CA    HA3    sing N N 169 
GLY C     O      doub N N 170 
GLY C     OXT    sing N N 171 
GLY OXT   HXT    sing N N 172 
HIS N     CA     sing N N 173 
HIS N     H      sing N N 174 
HIS N     H2     sing N N 175 
HIS CA    C      sing N N 176 
HIS CA    CB     sing N N 177 
HIS CA    HA     sing N N 178 
HIS C     O      doub N N 179 
HIS C     OXT    sing N N 180 
HIS CB    CG     sing N N 181 
HIS CB    HB2    sing N N 182 
HIS CB    HB3    sing N N 183 
HIS CG    ND1    sing Y N 184 
HIS CG    CD2    doub Y N 185 
HIS ND1   CE1    doub Y N 186 
HIS ND1   HD1    sing N N 187 
HIS CD2   NE2    sing Y N 188 
HIS CD2   HD2    sing N N 189 
HIS CE1   NE2    sing Y N 190 
HIS CE1   HE1    sing N N 191 
HIS NE2   HE2    sing N N 192 
HIS OXT   HXT    sing N N 193 
HOH O     H1     sing N N 194 
HOH O     H2     sing N N 195 
ILE N     CA     sing N N 196 
ILE N     H      sing N N 197 
ILE N     H2     sing N N 198 
ILE CA    C      sing N N 199 
ILE CA    CB     sing N N 200 
ILE CA    HA     sing N N 201 
ILE C     O      doub N N 202 
ILE C     OXT    sing N N 203 
ILE CB    CG1    sing N N 204 
ILE CB    CG2    sing N N 205 
ILE CB    HB     sing N N 206 
ILE CG1   CD1    sing N N 207 
ILE CG1   HG12   sing N N 208 
ILE CG1   HG13   sing N N 209 
ILE CG2   HG21   sing N N 210 
ILE CG2   HG22   sing N N 211 
ILE CG2   HG23   sing N N 212 
ILE CD1   HD11   sing N N 213 
ILE CD1   HD12   sing N N 214 
ILE CD1   HD13   sing N N 215 
ILE OXT   HXT    sing N N 216 
LEU N     CA     sing N N 217 
LEU N     H      sing N N 218 
LEU N     H2     sing N N 219 
LEU CA    C      sing N N 220 
LEU CA    CB     sing N N 221 
LEU CA    HA     sing N N 222 
LEU C     O      doub N N 223 
LEU C     OXT    sing N N 224 
LEU CB    CG     sing N N 225 
LEU CB    HB2    sing N N 226 
LEU CB    HB3    sing N N 227 
LEU CG    CD1    sing N N 228 
LEU CG    CD2    sing N N 229 
LEU CG    HG     sing N N 230 
LEU CD1   HD11   sing N N 231 
LEU CD1   HD12   sing N N 232 
LEU CD1   HD13   sing N N 233 
LEU CD2   HD21   sing N N 234 
LEU CD2   HD22   sing N N 235 
LEU CD2   HD23   sing N N 236 
LEU OXT   HXT    sing N N 237 
LYS N     CA     sing N N 238 
LYS N     H      sing N N 239 
LYS N     H2     sing N N 240 
LYS CA    C      sing N N 241 
LYS CA    CB     sing N N 242 
LYS CA    HA     sing N N 243 
LYS C     O      doub N N 244 
LYS C     OXT    sing N N 245 
LYS CB    CG     sing N N 246 
LYS CB    HB2    sing N N 247 
LYS CB    HB3    sing N N 248 
LYS CG    CD     sing N N 249 
LYS CG    HG2    sing N N 250 
LYS CG    HG3    sing N N 251 
LYS CD    CE     sing N N 252 
LYS CD    HD2    sing N N 253 
LYS CD    HD3    sing N N 254 
LYS CE    NZ     sing N N 255 
LYS CE    HE2    sing N N 256 
LYS CE    HE3    sing N N 257 
LYS NZ    HZ1    sing N N 258 
LYS NZ    HZ2    sing N N 259 
LYS NZ    HZ3    sing N N 260 
LYS OXT   HXT    sing N N 261 
MET N     CA     sing N N 262 
MET N     H      sing N N 263 
MET N     H2     sing N N 264 
MET CA    C      sing N N 265 
MET CA    CB     sing N N 266 
MET CA    HA     sing N N 267 
MET C     O      doub N N 268 
MET C     OXT    sing N N 269 
MET CB    CG     sing N N 270 
MET CB    HB2    sing N N 271 
MET CB    HB3    sing N N 272 
MET CG    SD     sing N N 273 
MET CG    HG2    sing N N 274 
MET CG    HG3    sing N N 275 
MET SD    CE     sing N N 276 
MET CE    HE1    sing N N 277 
MET CE    HE2    sing N N 278 
MET CE    HE3    sing N N 279 
MET OXT   HXT    sing N N 280 
PG4 O1    C1     sing N N 281 
PG4 O1    HO1    sing N N 282 
PG4 C1    C2     sing N N 283 
PG4 C1    H11    sing N N 284 
PG4 C1    H12    sing N N 285 
PG4 C2    O2     sing N N 286 
PG4 C2    H21    sing N N 287 
PG4 C2    H22    sing N N 288 
PG4 O2    C3     sing N N 289 
PG4 C3    C4     sing N N 290 
PG4 C3    H31    sing N N 291 
PG4 C3    H32    sing N N 292 
PG4 C4    O3     sing N N 293 
PG4 C4    H41    sing N N 294 
PG4 C4    H42    sing N N 295 
PG4 O3    C5     sing N N 296 
PG4 C5    C6     sing N N 297 
PG4 C5    H51    sing N N 298 
PG4 C5    H52    sing N N 299 
PG4 C6    O4     sing N N 300 
PG4 C6    H61    sing N N 301 
PG4 C6    H62    sing N N 302 
PG4 O4    C7     sing N N 303 
PG4 C7    C8     sing N N 304 
PG4 C7    H71    sing N N 305 
PG4 C7    H72    sing N N 306 
PG4 C8    O5     sing N N 307 
PG4 C8    H81    sing N N 308 
PG4 C8    H82    sing N N 309 
PG4 O5    HO5    sing N N 310 
PHE N     CA     sing N N 311 
PHE N     H      sing N N 312 
PHE N     H2     sing N N 313 
PHE CA    C      sing N N 314 
PHE CA    CB     sing N N 315 
PHE CA    HA     sing N N 316 
PHE C     O      doub N N 317 
PHE C     OXT    sing N N 318 
PHE CB    CG     sing N N 319 
PHE CB    HB2    sing N N 320 
PHE CB    HB3    sing N N 321 
PHE CG    CD1    doub Y N 322 
PHE CG    CD2    sing Y N 323 
PHE CD1   CE1    sing Y N 324 
PHE CD1   HD1    sing N N 325 
PHE CD2   CE2    doub Y N 326 
PHE CD2   HD2    sing N N 327 
PHE CE1   CZ     doub Y N 328 
PHE CE1   HE1    sing N N 329 
PHE CE2   CZ     sing Y N 330 
PHE CE2   HE2    sing N N 331 
PHE CZ    HZ     sing N N 332 
PHE OXT   HXT    sing N N 333 
PRO N     CA     sing N N 334 
PRO N     CD     sing N N 335 
PRO N     H      sing N N 336 
PRO CA    C      sing N N 337 
PRO CA    CB     sing N N 338 
PRO CA    HA     sing N N 339 
PRO C     O      doub N N 340 
PRO C     OXT    sing N N 341 
PRO CB    CG     sing N N 342 
PRO CB    HB2    sing N N 343 
PRO CB    HB3    sing N N 344 
PRO CG    CD     sing N N 345 
PRO CG    HG2    sing N N 346 
PRO CG    HG3    sing N N 347 
PRO CD    HD2    sing N N 348 
PRO CD    HD3    sing N N 349 
PRO OXT   HXT    sing N N 350 
SER N     CA     sing N N 351 
SER N     H      sing N N 352 
SER N     H2     sing N N 353 
SER CA    C      sing N N 354 
SER CA    CB     sing N N 355 
SER CA    HA     sing N N 356 
SER C     O      doub N N 357 
SER C     OXT    sing N N 358 
SER CB    OG     sing N N 359 
SER CB    HB2    sing N N 360 
SER CB    HB3    sing N N 361 
SER OG    HG     sing N N 362 
SER OXT   HXT    sing N N 363 
THR N     CA     sing N N 364 
THR N     H      sing N N 365 
THR N     H2     sing N N 366 
THR CA    C      sing N N 367 
THR CA    CB     sing N N 368 
THR CA    HA     sing N N 369 
THR C     O      doub N N 370 
THR C     OXT    sing N N 371 
THR CB    OG1    sing N N 372 
THR CB    CG2    sing N N 373 
THR CB    HB     sing N N 374 
THR OG1   HG1    sing N N 375 
THR CG2   HG21   sing N N 376 
THR CG2   HG22   sing N N 377 
THR CG2   HG23   sing N N 378 
THR OXT   HXT    sing N N 379 
TYR N     CA     sing N N 380 
TYR N     H      sing N N 381 
TYR N     H2     sing N N 382 
TYR CA    C      sing N N 383 
TYR CA    CB     sing N N 384 
TYR CA    HA     sing N N 385 
TYR C     O      doub N N 386 
TYR C     OXT    sing N N 387 
TYR CB    CG     sing N N 388 
TYR CB    HB2    sing N N 389 
TYR CB    HB3    sing N N 390 
TYR CG    CD1    doub Y N 391 
TYR CG    CD2    sing Y N 392 
TYR CD1   CE1    sing Y N 393 
TYR CD1   HD1    sing N N 394 
TYR CD2   CE2    doub Y N 395 
TYR CD2   HD2    sing N N 396 
TYR CE1   CZ     doub Y N 397 
TYR CE1   HE1    sing N N 398 
TYR CE2   CZ     sing Y N 399 
TYR CE2   HE2    sing N N 400 
TYR CZ    OH     sing N N 401 
TYR OH    HH     sing N N 402 
TYR OXT   HXT    sing N N 403 
VAL N     CA     sing N N 404 
VAL N     H      sing N N 405 
VAL N     H2     sing N N 406 
VAL CA    C      sing N N 407 
VAL CA    CB     sing N N 408 
VAL CA    HA     sing N N 409 
VAL C     O      doub N N 410 
VAL C     OXT    sing N N 411 
VAL CB    CG1    sing N N 412 
VAL CB    CG2    sing N N 413 
VAL CB    HB     sing N N 414 
VAL CG1   HG11   sing N N 415 
VAL CG1   HG12   sing N N 416 
VAL CG1   HG13   sing N N 417 
VAL CG2   HG21   sing N N 418 
VAL CG2   HG22   sing N N 419 
VAL CG2   HG23   sing N N 420 
VAL OXT   HXT    sing N N 421 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           'P30 GM110761' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8VIP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8VIT 
_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]   0.023290 
_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]   0.017515 
_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]   0.012341 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . SER A 1 19  ? -23.276 5.353   -33.034 1.00 51.28 ? -1  SER A N     1 
ATOM   2    C  CA    . SER A 1 19  ? -22.068 6.223   -33.135 1.00 50.80 ? -1  SER A CA    1 
ATOM   3    C  C     . SER A 1 19  ? -21.051 5.872   -32.062 1.00 48.96 ? -1  SER A C     1 
ATOM   4    O  O     . SER A 1 19  ? -19.846 5.975   -32.289 1.00 49.18 ? -1  SER A O     1 
ATOM   5    C  CB    . SER A 1 19  ? -22.449 7.699   -33.012 1.00 51.81 ? -1  SER A CB    1 
ATOM   6    O  OG    . SER A 1 19  ? -23.004 8.187   -34.219 1.00 52.24 ? -1  SER A OG    1 
ATOM   7    N  N     . HIS A 1 20  ? -21.548 5.468   -30.884 1.00 46.60 ? 0   HIS A N     1 
ATOM   8    C  CA    . HIS A 1 20  ? -20.710 5.065   -29.758 1.00 45.28 ? 0   HIS A CA    1 
ATOM   9    C  C     . HIS A 1 20  ? -21.281 3.769   -29.182 1.00 43.84 ? 0   HIS A C     1 
ATOM   10   O  O     . HIS A 1 20  ? -21.916 3.766   -28.127 1.00 45.65 ? 0   HIS A O     1 
ATOM   11   C  CB    . HIS A 1 20  ? -20.636 6.160   -28.691 1.00 45.19 ? 0   HIS A CB    1 
ATOM   12   N  N     . MET A 1 21  ? -21.071 2.673   -29.902 1.00 40.99 ? 1   MET A N     1 
ATOM   13   C  CA    . MET A 1 21  ? -21.341 1.334   -29.405 1.00 38.94 ? 1   MET A CA    1 
ATOM   14   C  C     . MET A 1 21  ? -20.032 0.566   -29.393 1.00 32.22 ? 1   MET A C     1 
ATOM   15   O  O     . MET A 1 21  ? -19.190 0.733   -30.278 1.00 33.29 ? 1   MET A O     1 
ATOM   16   C  CB    . MET A 1 21  ? -22.313 0.554   -30.303 1.00 43.79 ? 1   MET A CB    1 
ATOM   17   C  CG    . MET A 1 21  ? -22.300 -0.949  -29.979 1.00 47.93 ? 1   MET A CG    1 
ATOM   18   S  SD    . MET A 1 21  ? -23.575 -1.986  -30.713 1.00 51.69 ? 1   MET A SD    1 
ATOM   19   C  CE    . MET A 1 21  ? -22.889 -2.253  -32.347 1.00 52.26 ? 1   MET A CE    1 
ATOM   20   N  N     . ILE A 1 22  ? -19.875 -0.304  -28.413 1.00 25.28 ? 2   ILE A N     1 
ATOM   21   C  CA    . ILE A 1 22  ? -18.705 -1.158  -28.324 1.00 21.74 ? 2   ILE A CA    1 
ATOM   22   C  C     . ILE A 1 22  ? -19.186 -2.580  -28.547 1.00 20.62 ? 2   ILE A C     1 
ATOM   23   O  O     . ILE A 1 22  ? -19.847 -3.165  -27.681 1.00 21.77 ? 2   ILE A O     1 
ATOM   24   C  CB    . ILE A 1 22  ? -18.026 -1.023  -26.958 1.00 20.59 ? 2   ILE A CB    1 
ATOM   25   C  CG1   . ILE A 1 22  ? -17.506 0.402   -26.741 1.00 21.30 ? 2   ILE A CG1   1 
ATOM   26   C  CG2   . ILE A 1 22  ? -16.908 -2.032  -26.818 1.00 20.48 ? 2   ILE A CG2   1 
ATOM   27   C  CD1   . ILE A 1 22  ? -16.418 0.842   -27.711 1.00 21.62 ? 2   ILE A CD1   1 
ATOM   28   N  N     . SER A 1 23  ? -18.857 -3.149  -29.698 1.00 20.28 ? 3   SER A N     1 
ATOM   29   C  CA    A SER A 1 23  ? -19.216 -4.537  -29.939 0.50 21.51 ? 3   SER A CA    1 
ATOM   30   C  CA    B SER A 1 23  ? -19.195 -4.533  -30.003 0.50 21.08 ? 3   SER A CA    1 
ATOM   31   C  C     . SER A 1 23  ? -18.079 -5.497  -29.634 1.00 20.76 ? 3   SER A C     1 
ATOM   32   O  O     . SER A 1 23  ? -18.346 -6.665  -29.330 1.00 22.87 ? 3   SER A O     1 
ATOM   33   C  CB    A SER A 1 23  ? -19.700 -4.737  -31.378 0.50 23.86 ? 3   SER A CB    1 
ATOM   34   C  CB    B SER A 1 23  ? -19.487 -4.682  -31.500 0.50 22.52 ? 3   SER A CB    1 
ATOM   35   O  OG    A SER A 1 23  ? -18.617 -4.784  -32.272 0.50 25.58 ? 3   SER A OG    1 
ATOM   36   O  OG    B SER A 1 23  ? -20.632 -3.936  -31.874 0.50 23.82 ? 3   SER A OG    1 
ATOM   37   N  N     . LYS A 1 24  ? -16.832 -5.037  -29.674 1.00 20.05 ? 4   LYS A N     1 
ATOM   38   C  CA    . LYS A 1 24  ? -15.696 -5.874  -29.324 1.00 20.66 ? 4   LYS A CA    1 
ATOM   39   C  C     . LYS A 1 24  ? -14.697 -5.056  -28.525 1.00 18.91 ? 4   LYS A C     1 
ATOM   40   O  O     . LYS A 1 24  ? -14.506 -3.861  -28.775 1.00 17.90 ? 4   LYS A O     1 
ATOM   41   C  CB    . LYS A 1 24  ? -15.004 -6.455  -30.559 1.00 23.95 ? 4   LYS A CB    1 
ATOM   42   C  CG    . LYS A 1 24  ? -15.886 -7.407  -31.367 1.00 25.42 ? 4   LYS A CG    1 
ATOM   43   N  N     . ILE A 1 25  ? -14.049 -5.727  -27.577 1.00 17.41 ? 5   ILE A N     1 
ATOM   44   C  CA    . ILE A 1 25  ? -13.044 -5.134  -26.705 1.00 15.95 ? 5   ILE A CA    1 
ATOM   45   C  C     . ILE A 1 25  ? -11.706 -5.785  -27.023 1.00 16.18 ? 5   ILE A C     1 
ATOM   46   O  O     . ILE A 1 25  ? -11.528 -6.982  -26.762 1.00 16.30 ? 5   ILE A O     1 
ATOM   47   C  CB    . ILE A 1 25  ? -13.396 -5.379  -25.229 1.00 15.49 ? 5   ILE A CB    1 
ATOM   48   C  CG1   . ILE A 1 25  ? -14.780 -4.813  -24.893 1.00 17.00 ? 5   ILE A CG1   1 
ATOM   49   C  CG2   . ILE A 1 25  ? -12.315 -4.809  -24.320 1.00 15.84 ? 5   ILE A CG2   1 
ATOM   50   C  CD1   . ILE A 1 25  ? -15.280 -5.168  -23.514 1.00 17.94 ? 5   ILE A CD1   1 
ATOM   51   N  N     . ASN A 1 26  ? -10.764 -5.014  -27.583 1.00 16.01 ? 6   ASN A N     1 
ATOM   52   C  CA    . ASN A 1 26  ? -9.425  -5.513  -27.856 1.00 15.61 ? 6   ASN A CA    1 
ATOM   53   C  C     . ASN A 1 26  ? -8.525  -5.252  -26.647 1.00 15.40 ? 6   ASN A C     1 
ATOM   54   O  O     . ASN A 1 26  ? -8.965  -4.778  -25.596 1.00 15.24 ? 6   ASN A O     1 
ATOM   55   C  CB    . ASN A 1 26  ? -8.874  -4.979  -29.193 1.00 16.60 ? 6   ASN A CB    1 
ATOM   56   C  CG    . ASN A 1 26  ? -8.429  -3.531  -29.142 1.00 16.45 ? 6   ASN A CG    1 
ATOM   57   O  OD1   . ASN A 1 26  ? -8.432  -2.881  -28.115 1.00 16.55 ? 6   ASN A OD1   1 
ATOM   58   N  ND2   . ASN A 1 26  ? -7.985  -3.030  -30.284 1.00 19.10 ? 6   ASN A ND2   1 
ATOM   59   N  N     . GLY A 1 27  ? -7.246  -5.604  -26.786 1.00 15.00 ? 7   GLY A N     1 
ATOM   60   C  CA    . GLY A 1 27  ? -6.336  -5.474  -25.664 1.00 15.36 ? 7   GLY A CA    1 
ATOM   61   C  C     . GLY A 1 27  ? -6.119  -4.043  -25.226 1.00 14.39 ? 7   GLY A C     1 
ATOM   62   O  O     . GLY A 1 27  ? -5.916  -3.792  -24.040 1.00 15.58 ? 7   GLY A O     1 
ATOM   63   N  N     . LYS A 1 28  ? -6.159  -3.084  -26.156 1.00 14.21 ? 8   LYS A N     1 
ATOM   64   C  CA    . LYS A 1 28  ? -5.965  -1.693  -25.746 1.00 13.82 ? 8   LYS A CA    1 
ATOM   65   C  C     . LYS A 1 28  ? -7.191  -1.141  -25.021 1.00 13.84 ? 8   LYS A C     1 
ATOM   66   O  O     . LYS A 1 28  ? -7.055  -0.374  -24.066 1.00 14.78 ? 8   LYS A O     1 
ATOM   67   C  CB    . LYS A 1 28  ? -5.545  -0.810  -26.929 1.00 14.98 ? 8   LYS A CB    1 
ATOM   68   C  CG    . LYS A 1 28  ? -5.265  0.646   -26.525 1.00 15.74 ? 8   LYS A CG    1 
ATOM   69   C  CD    . LYS A 1 28  ? -4.288  0.763   -25.350 1.00 17.08 ? 8   LYS A CD    1 
ATOM   70   C  CE    . LYS A 1 28  ? -3.658  2.147   -25.218 1.00 18.88 ? 8   LYS A CE    1 
ATOM   71   N  NZ    . LYS A 1 28  ? -4.627  3.252   -24.966 1.00 19.51 ? 8   LYS A NZ    1 
ATOM   72   N  N     . LEU A 1 29  ? -8.392  -1.513  -25.451 1.00 13.44 ? 9   LEU A N     1 
ATOM   73   C  CA    . LEU A 1 29  ? -9.579  -1.095  -24.720 1.00 13.53 ? 9   LEU A CA    1 
ATOM   74   C  C     . LEU A 1 29  ? -9.590  -1.710  -23.326 1.00 13.83 ? 9   LEU A C     1 
ATOM   75   O  O     . LEU A 1 29  ? -9.915  -1.027  -22.351 1.00 14.08 ? 9   LEU A O     1 
ATOM   76   C  CB    . LEU A 1 29  ? -10.857 -1.401  -25.510 1.00 14.17 ? 9   LEU A CB    1 
ATOM   77   C  CG    . LEU A 1 29  ? -12.166 -0.887  -24.871 1.00 15.39 ? 9   LEU A CG    1 
ATOM   78   C  CD1   . LEU A 1 29  ? -12.081 0.579   -24.483 1.00 15.81 ? 9   LEU A CD1   1 
ATOM   79   C  CD2   . LEU A 1 29  ? -13.349 -1.122  -25.808 1.00 16.28 ? 9   LEU A CD2   1 
ATOM   80   N  N     . PHE A 1 30  ? -9.222  -2.992  -23.201 1.00 13.96 ? 10  PHE A N     1 
ATOM   81   C  CA    . PHE A 1 30  ? -9.122  -3.585  -21.869 1.00 14.44 ? 10  PHE A CA    1 
ATOM   82   C  C     . PHE A 1 30  ? -8.079  -2.855  -21.033 1.00 14.60 ? 10  PHE A C     1 
ATOM   83   O  O     . PHE A 1 30  ? -8.303  -2.591  -19.843 1.00 14.08 ? 10  PHE A O     1 
ATOM   84   C  CB    . PHE A 1 30  ? -8.812  -5.078  -21.981 1.00 14.51 ? 10  PHE A CB    1 
ATOM   85   C  CG    . PHE A 1 30  ? -8.918  -5.850  -20.673 1.00 14.55 ? 10  PHE A CG    1 
ATOM   86   C  CD1   . PHE A 1 30  ? -9.862  -5.533  -19.716 1.00 15.75 ? 10  PHE A CD1   1 
ATOM   87   C  CD2   . PHE A 1 30  ? -8.069  -6.922  -20.428 1.00 15.41 ? 10  PHE A CD2   1 
ATOM   88   C  CE1   . PHE A 1 30  ? -9.957  -6.265  -18.539 1.00 16.30 ? 10  PHE A CE1   1 
ATOM   89   C  CE2   . PHE A 1 30  ? -8.161  -7.647  -19.249 1.00 16.04 ? 10  PHE A CE2   1 
ATOM   90   C  CZ    . PHE A 1 30  ? -9.116  -7.310  -18.306 1.00 16.27 ? 10  PHE A CZ    1 
ATOM   91   N  N     . ALA A 1 31  ? -6.928  -2.517  -21.628 1.00 14.36 ? 11  ALA A N     1 
ATOM   92   C  CA    . ALA A 1 31  ? -5.925  -1.757  -20.889 1.00 14.56 ? 11  ALA A CA    1 
ATOM   93   C  C     . ALA A 1 31  ? -6.502  -0.437  -20.400 1.00 14.54 ? 11  ALA A C     1 
ATOM   94   O  O     . ALA A 1 31  ? -6.280  -0.039  -19.251 1.00 14.99 ? 11  ALA A O     1 
ATOM   95   C  CB    . ALA A 1 31  ? -4.675  -1.519  -21.743 1.00 15.76 ? 11  ALA A CB    1 
ATOM   96   N  N     . ASP A 1 32  ? -7.254  0.252   -21.257 1.00 15.04 ? 12  ASP A N     1 
ATOM   97   C  CA    . ASP A 1 32  ? -7.881  1.504   -20.860 1.00 15.03 ? 12  ASP A CA    1 
ATOM   98   C  C     . ASP A 1 32  ? -8.844  1.289   -19.697 1.00 14.50 ? 12  ASP A C     1 
ATOM   99   O  O     . ASP A 1 32  ? -8.900  2.108   -18.779 1.00 14.75 ? 12  ASP A O     1 
ATOM   100  C  CB    . ASP A 1 32  ? -8.644  2.122   -22.042 1.00 15.64 ? 12  ASP A CB    1 
ATOM   101  C  CG    . ASP A 1 32  ? -7.748  2.718   -23.097 1.00 18.40 ? 12  ASP A CG    1 
ATOM   102  O  OD1   . ASP A 1 32  ? -6.519  2.805   -22.893 1.00 20.20 ? 12  ASP A OD1   1 
ATOM   103  O  OD2   . ASP A 1 32  ? -8.316  3.124   -24.127 1.00 19.10 ? 12  ASP A OD2   1 
ATOM   104  N  N     . MET A 1 33  ? -9.638  0.212   -19.746 1.00 14.44 ? 13  MET A N     1 
ATOM   105  C  CA    . MET A 1 33  ? -10.544 -0.115  -18.640 1.00 14.06 ? 13  MET A CA    1 
ATOM   106  C  C     . MET A 1 33  ? -9.769  -0.296  -17.341 1.00 14.16 ? 13  MET A C     1 
ATOM   107  O  O     . MET A 1 33  ? -10.155 0.238   -16.297 1.00 14.50 ? 13  MET A O     1 
ATOM   108  C  CB    . MET A 1 33  ? -11.342 -1.380  -18.981 1.00 14.42 ? 13  MET A CB    1 
ATOM   109  C  CG    . MET A 1 33  ? -12.336 -1.197  -20.132 1.00 14.69 ? 13  MET A CG    1 
ATOM   110  S  SD    . MET A 1 33  ? -12.904 -2.730  -20.867 1.00 15.83 ? 13  MET A SD    1 
ATOM   111  C  CE    . MET A 1 33  ? -14.002 -3.340  -19.602 1.00 17.37 ? 13  MET A CE    1 
ATOM   112  N  N     . ILE A 1 34  ? -8.656  -1.021  -17.408 1.00 14.31 ? 14  ILE A N     1 
ATOM   113  C  CA    . ILE A 1 34  ? -7.799  -1.232  -16.240 1.00 14.20 ? 14  ILE A CA    1 
ATOM   114  C  C     . ILE A 1 34  ? -7.253  0.094   -15.720 1.00 14.31 ? 14  ILE A C     1 
ATOM   115  O  O     . ILE A 1 34  ? -7.241  0.351   -14.508 1.00 15.25 ? 14  ILE A O     1 
ATOM   116  C  CB    . ILE A 1 34  ? -6.671  -2.219  -16.609 1.00 14.77 ? 14  ILE A CB    1 
ATOM   117  C  CG1   . ILE A 1 34  ? -7.255  -3.621  -16.797 1.00 14.76 ? 14  ILE A CG1   1 
ATOM   118  C  CG2   . ILE A 1 34  ? -5.505  -2.174  -15.603 1.00 15.76 ? 14  ILE A CG2   1 
ATOM   119  C  CD1   . ILE A 1 34  ? -6.369  -4.542  -17.610 1.00 15.59 ? 14  ILE A CD1   1 
ATOM   120  N  N     . ILE A 1 35  ? -6.771  0.943   -16.625 1.00 15.22 ? 15  ILE A N     1 
ATOM   121  C  CA    . ILE A 1 35  ? -6.120  2.183   -16.217 1.00 15.68 ? 15  ILE A CA    1 
ATOM   122  C  C     . ILE A 1 35  ? -7.125  3.147   -15.608 1.00 14.94 ? 15  ILE A C     1 
ATOM   123  O  O     . ILE A 1 35  ? -6.866  3.739   -14.550 1.00 16.16 ? 15  ILE A O     1 
ATOM   124  C  CB    . ILE A 1 35  ? -5.378  2.800   -17.418 1.00 17.59 ? 15  ILE A CB    1 
ATOM   125  C  CG1   . ILE A 1 35  ? -4.178  1.932   -17.811 1.00 18.36 ? 15  ILE A CG1   1 
ATOM   126  C  CG2   . ILE A 1 35  ? -4.911  4.195   -17.083 1.00 19.14 ? 15  ILE A CG2   1 
ATOM   127  C  CD1   . ILE A 1 35  ? -3.655  2.196   -19.204 1.00 20.64 ? 15  ILE A CD1   1 
ATOM   128  N  N     . GLN A 1 36  ? -8.295  3.290   -16.231 1.00 15.05 ? 16  GLN A N     1 
ATOM   129  C  CA    . GLN A 1 36  ? -9.304  4.201   -15.696 1.00 15.54 ? 16  GLN A CA    1 
ATOM   130  C  C     . GLN A 1 36  ? -9.941  3.648   -14.425 1.00 15.31 ? 16  GLN A C     1 
ATOM   131  O  O     . GLN A 1 36  ? -10.243 4.410   -13.507 1.00 15.29 ? 16  GLN A O     1 
ATOM   132  C  CB    . GLN A 1 36  ? -10.364 4.532   -16.756 1.00 16.55 ? 16  GLN A CB    1 
ATOM   133  C  CG    . GLN A 1 36  ? -9.817  5.128   -18.042 1.00 18.24 ? 16  GLN A CG    1 
ATOM   134  C  CD    . GLN A 1 36  ? -8.816  6.235   -17.826 1.00 21.23 ? 16  GLN A CD    1 
ATOM   135  O  OE1   . GLN A 1 36  ? -9.029  7.135   -17.022 1.00 22.16 ? 16  GLN A OE1   1 
ATOM   136  N  NE2   . GLN A 1 36  ? -7.714  6.181   -18.568 1.00 23.49 ? 16  GLN A NE2   1 
ATOM   137  N  N     . GLY A 1 37  ? -10.161 2.331   -14.361 1.00 14.80 ? 17  GLY A N     1 
ATOM   138  C  CA    . GLY A 1 37  ? -10.612 1.726   -13.122 1.00 14.70 ? 17  GLY A CA    1 
ATOM   139  C  C     . GLY A 1 37  ? -9.629  1.932   -11.987 1.00 14.67 ? 17  GLY A C     1 
ATOM   140  O  O     . GLY A 1 37  ? -10.023 2.257   -10.859 1.00 15.09 ? 17  GLY A O     1 
ATOM   141  N  N     . ALA A 1 38  ? -8.335  1.740   -12.262 1.00 15.04 ? 18  ALA A N     1 
ATOM   142  C  CA    . ALA A 1 38  ? -7.309  1.975   -11.254 1.00 15.13 ? 18  ALA A CA    1 
ATOM   143  C  C     . ALA A 1 38  ? -7.307  3.426   -10.810 1.00 14.88 ? 18  ALA A C     1 
ATOM   144  O  O     . ALA A 1 38  ? -7.196  3.714   -9.614  1.00 15.84 ? 18  ALA A O     1 
ATOM   145  C  CB    . ALA A 1 38  ? -5.927  1.585   -11.783 1.00 15.07 ? 18  ALA A CB    1 
ATOM   146  N  N     . GLN A 1 39  ? -7.424  4.363   -11.754 1.00 15.89 ? 19  GLN A N     1 
ATOM   147  C  CA    . GLN A 1 39  ? -7.412  5.769   -11.371 1.00 15.77 ? 19  GLN A CA    1 
ATOM   148  C  C     . GLN A 1 39  ? -8.630  6.120   -10.526 1.00 16.56 ? 19  GLN A C     1 
ATOM   149  O  O     . GLN A 1 39  ? -8.528  6.896   -9.572  1.00 17.64 ? 19  GLN A O     1 
ATOM   150  C  CB    . GLN A 1 39  ? -7.366  6.667   -12.604 1.00 18.44 ? 19  GLN A CB    1 
ATOM   151  C  CG    . GLN A 1 39  ? -7.189  8.128   -12.256 1.00 21.36 ? 19  GLN A CG    1 
ATOM   152  C  CD    . GLN A 1 39  ? -5.876  8.380   -11.544 1.00 24.28 ? 19  GLN A CD    1 
ATOM   153  O  OE1   . GLN A 1 39  ? -4.805  8.074   -12.071 1.00 26.51 ? 19  GLN A OE1   1 
ATOM   154  N  NE2   . GLN A 1 39  ? -5.948  8.931   -10.337 1.00 25.38 ? 19  GLN A NE2   1 
ATOM   155  N  N     . ASN A 1 40  ? -9.798  5.592   -10.881 1.00 16.03 ? 20  ASN A N     1 
ATOM   156  C  CA    . ASN A 1 40  ? -10.999 5.905   -10.116 1.00 16.44 ? 20  ASN A CA    1 
ATOM   157  C  C     . ASN A 1 40  ? -10.903 5.342   -8.700  1.00 16.56 ? 20  ASN A C     1 
ATOM   158  O  O     . ASN A 1 40  ? -11.316 5.995   -7.736  1.00 17.14 ? 20  ASN A O     1 
ATOM   159  C  CB    . ASN A 1 40  ? -12.237 5.377   -10.835 1.00 17.58 ? 20  ASN A CB    1 
ATOM   160  C  CG    . ASN A 1 40  ? -13.491 6.082   -10.401 1.00 19.35 ? 20  ASN A CG    1 
ATOM   161  O  OD1   . ASN A 1 40  ? -13.525 7.312   -10.309 1.00 21.45 ? 20  ASN A OD1   1 
ATOM   162  N  ND2   . ASN A 1 40  ? -14.533 5.321   -10.152 1.00 19.59 ? 20  ASN A ND2   1 
ATOM   163  N  N     . LEU A 1 41  ? -10.337 4.145   -8.556  1.00 15.35 ? 21  LEU A N     1 
ATOM   164  C  CA    . LEU A 1 41  ? -10.107 3.593   -7.227  1.00 15.68 ? 21  LEU A CA    1 
ATOM   165  C  C     . LEU A 1 41  ? -9.105  4.443   -6.450  1.00 16.31 ? 21  LEU A C     1 
ATOM   166  O  O     . LEU A 1 41  ? -9.321  4.754   -5.271  1.00 16.68 ? 21  LEU A O     1 
ATOM   167  C  CB    . LEU A 1 41  ? -9.624  2.148   -7.362  1.00 15.24 ? 21  LEU A CB    1 
ATOM   168  C  CG    . LEU A 1 41  ? -9.211  1.453   -6.070  1.00 15.57 ? 21  LEU A CG    1 
ATOM   169  C  CD1   . LEU A 1 41  ? -10.380 1.379   -5.090  1.00 16.88 ? 21  LEU A CD1   1 
ATOM   170  C  CD2   . LEU A 1 41  ? -8.682  0.070   -6.377  1.00 16.30 ? 21  LEU A CD2   1 
ATOM   171  N  N     . SER A 1 42  ? -7.995  4.825   -7.083  1.00 16.65 ? 22  SER A N     1 
ATOM   172  C  CA    A SER A 1 42  ? -7.019  5.661   -6.392  0.50 17.46 ? 22  SER A CA    1 
ATOM   173  C  CA    B SER A 1 42  ? -7.010  5.678   -6.419  0.50 18.18 ? 22  SER A CA    1 
ATOM   174  C  C     . SER A 1 42  ? -7.660  6.946   -5.886  1.00 18.26 ? 22  SER A C     1 
ATOM   175  O  O     . SER A 1 42  ? -7.432  7.356   -4.743  1.00 19.27 ? 22  SER A O     1 
ATOM   176  C  CB    A SER A 1 42  ? -5.846  5.975   -7.321  0.50 17.43 ? 22  SER A CB    1 
ATOM   177  C  CB    B SER A 1 42  ? -5.898  6.061   -7.400  0.50 19.52 ? 22  SER A CB    1 
ATOM   178  O  OG    A SER A 1 42  ? -4.872  6.757   -6.647  0.50 17.84 ? 22  SER A OG    1 
ATOM   179  O  OG    B SER A 1 42  ? -5.167  4.938   -7.837  0.50 21.18 ? 22  SER A OG    1 
ATOM   180  N  N     . ASN A 1 43  ? -8.479  7.587   -6.709  1.00 18.43 ? 23  ASN A N     1 
ATOM   181  C  CA    . ASN A 1 43  ? -9.120  8.825   -6.300  1.00 19.74 ? 23  ASN A CA    1 
ATOM   182  C  C     . ASN A 1 43  ? -10.027 8.640   -5.093  1.00 20.05 ? 23  ASN A C     1 
ATOM   183  O  O     . ASN A 1 43  ? -10.272 9.605   -4.367  1.00 22.02 ? 23  ASN A O     1 
ATOM   184  C  CB    . ASN A 1 43  ? -9.961  9.377   -7.450  1.00 20.78 ? 23  ASN A CB    1 
ATOM   185  C  CG    . ASN A 1 43  ? -9.130  9.923   -8.597  1.00 22.57 ? 23  ASN A CG    1 
ATOM   186  O  OD1   . ASN A 1 43  ? -7.909  10.036  -8.518  1.00 23.64 ? 23  ASN A OD1   1 
ATOM   187  N  ND2   . ASN A 1 43  ? -9.805  10.273  -9.671  1.00 22.80 ? 23  ASN A ND2   1 
ATOM   188  N  N     . ASN A 1 44  ? -10.548 7.435   -4.878  1.00 18.47 ? 24  ASN A N     1 
ATOM   189  C  CA    . ASN A 1 44  ? -11.487 7.163   -3.799  1.00 18.58 ? 24  ASN A CA    1 
ATOM   190  C  C     . ASN A 1 44  ? -10.887 6.314   -2.687  1.00 19.07 ? 24  ASN A C     1 
ATOM   191  O  O     . ASN A 1 44  ? -11.621 5.864   -1.804  1.00 19.10 ? 24  ASN A O     1 
ATOM   192  C  CB    . ASN A 1 44  ? -12.746 6.508   -4.371  1.00 20.53 ? 24  ASN A CB    1 
ATOM   193  C  CG    . ASN A 1 44  ? -13.607 7.495   -5.134  1.00 23.02 ? 24  ASN A CG    1 
ATOM   194  O  OD1   . ASN A 1 44  ? -14.264 8.345   -4.535  1.00 25.04 ? 24  ASN A OD1   1 
ATOM   195  N  ND2   . ASN A 1 44  ? -13.595 7.407   -6.455  1.00 22.97 ? 24  ASN A ND2   1 
ATOM   196  N  N     . ALA A 1 45  ? -9.566  6.133   -2.675  1.00 18.84 ? 25  ALA A N     1 
ATOM   197  C  CA    . ALA A 1 45  ? -8.960  5.183   -1.747  1.00 18.93 ? 25  ALA A CA    1 
ATOM   198  C  C     . ALA A 1 45  ? -9.133  5.608   -0.292  1.00 18.98 ? 25  ALA A C     1 
ATOM   199  O  O     . ALA A 1 45  ? -9.346  4.757   0.573   1.00 18.56 ? 25  ALA A O     1 
ATOM   200  C  CB    . ALA A 1 45  ? -7.484  4.989   -2.088  1.00 19.68 ? 25  ALA A CB    1 
ATOM   201  N  N     . ASP A 1 46  ? -9.019  6.908   0.006   1.00 20.15 ? 26  ASP A N     1 
ATOM   202  C  CA    . ASP A 1 46  ? -9.152  7.358   1.393   1.00 21.96 ? 26  ASP A CA    1 
ATOM   203  C  C     . ASP A 1 46  ? -10.565 7.118   1.907   1.00 20.76 ? 26  ASP A C     1 
ATOM   204  O  O     . ASP A 1 46  ? -10.758 6.711   3.062   1.00 21.02 ? 26  ASP A O     1 
ATOM   205  C  CB    . ASP A 1 46  ? -8.790  8.841   1.511   1.00 26.29 ? 26  ASP A CB    1 
ATOM   206  C  CG    . ASP A 1 46  ? -7.302  9.097   1.329   1.00 30.76 ? 26  ASP A CG    1 
ATOM   207  O  OD1   . ASP A 1 46  ? -6.509  8.146   1.517   1.00 32.73 ? 26  ASP A OD1   1 
ATOM   208  O  OD2   . ASP A 1 46  ? -6.924  10.257  1.017   1.00 33.95 ? 26  ASP A OD2   1 
ATOM   209  N  N     . LEU A 1 47  ? -11.561 7.345   1.055   1.00 20.55 ? 27  LEU A N     1 
ATOM   210  C  CA    . LEU A 1 47  ? -12.943 7.058   1.420   1.00 21.36 ? 27  LEU A CA    1 
ATOM   211  C  C     . LEU A 1 47  ? -13.138 5.576   1.686   1.00 19.83 ? 27  LEU A C     1 
ATOM   212  O  O     . LEU A 1 47  ? -13.754 5.178   2.684   1.00 20.62 ? 27  LEU A O     1 
ATOM   213  C  CB    . LEU A 1 47  ? -13.862 7.507   0.288   1.00 23.50 ? 27  LEU A CB    1 
ATOM   214  C  CG    . LEU A 1 47  ? -15.318 7.052   0.433   1.00 26.42 ? 27  LEU A CG    1 
ATOM   215  C  CD1   . LEU A 1 47  ? -15.941 7.519   1.749   1.00 27.57 ? 27  LEU A CD1   1 
ATOM   216  C  CD2   . LEU A 1 47  ? -16.129 7.537   -0.750  1.00 28.19 ? 27  LEU A CD2   1 
ATOM   217  N  N     . VAL A 1 48  ? -12.645 4.737   0.782   1.00 18.35 ? 28  VAL A N     1 
ATOM   218  C  CA    . VAL A 1 48  ? -12.791 3.296   0.951   1.00 17.29 ? 28  VAL A CA    1 
ATOM   219  C  C     . VAL A 1 48  ? -12.089 2.827   2.228   1.00 18.81 ? 28  VAL A C     1 
ATOM   220  O  O     . VAL A 1 48  ? -12.607 1.969   2.953   1.00 19.36 ? 28  VAL A O     1 
ATOM   221  C  CB    . VAL A 1 48  ? -12.312 2.578   -0.325  1.00 16.18 ? 28  VAL A CB    1 
ATOM   222  C  CG1   . VAL A 1 48  ? -12.342 1.086   -0.152  1.00 16.22 ? 28  VAL A CG1   1 
ATOM   223  C  CG2   . VAL A 1 48  ? -13.200 2.966   -1.513  1.00 16.84 ? 28  VAL A CG2   1 
ATOM   224  N  N     . ASP A 1 49  ? -10.915 3.395   2.535   1.00 18.43 ? 29  ASP A N     1 
ATOM   225  C  CA    . ASP A 1 49  ? -10.234 3.100   3.799   1.00 19.65 ? 29  ASP A CA    1 
ATOM   226  C  C     . ASP A 1 49  ? -11.133 3.393   4.991   1.00 19.63 ? 29  ASP A C     1 
ATOM   227  O  O     . ASP A 1 49  ? -11.233 2.598   5.937   1.00 20.85 ? 29  ASP A O     1 
ATOM   228  C  CB    . ASP A 1 49  ? -8.991  3.989   3.958   1.00 20.90 ? 29  ASP A CB    1 
ATOM   229  C  CG    . ASP A 1 49  ? -7.767  3.441   3.268   1.00 22.17 ? 29  ASP A CG    1 
ATOM   230  O  OD1   . ASP A 1 49  ? -7.789  2.278   2.825   1.00 21.59 ? 29  ASP A OD1   1 
ATOM   231  O  OD2   . ASP A 1 49  ? -6.774  4.195   3.146   1.00 23.66 ? 29  ASP A OD2   1 
ATOM   232  N  N     . SER A 1 50  ? -11.742 4.571   4.991   1.00 20.03 ? 30  SER A N     1 
ATOM   233  C  CA    . SER A 1 50  ? -12.492 5.011   6.154   1.00 21.42 ? 30  SER A CA    1 
ATOM   234  C  C     . SER A 1 50  ? -13.746 4.173   6.382   1.00 19.32 ? 30  SER A C     1 
ATOM   235  O  O     . SER A 1 50  ? -14.218 4.096   7.527   1.00 20.68 ? 30  SER A O     1 
ATOM   236  C  CB    . SER A 1 50  ? -12.849 6.491   6.015   1.00 25.53 ? 30  SER A CB    1 
ATOM   237  O  OG    . SER A 1 50  ? -13.868 6.676   5.054   1.00 28.05 ? 30  SER A OG    1 
ATOM   238  N  N     . LEU A 1 51  ? -14.287 3.546   5.332   1.00 17.66 ? 31  LEU A N     1 
ATOM   239  C  CA    . LEU A 1 51  ? -15.453 2.688   5.467   1.00 16.39 ? 31  LEU A CA    1 
ATOM   240  C  C     . LEU A 1 51  ? -15.127 1.340   6.093   1.00 15.26 ? 31  LEU A C     1 
ATOM   241  O  O     . LEU A 1 51  ? -16.044 0.619   6.485   1.00 15.69 ? 31  LEU A O     1 
ATOM   242  C  CB    . LEU A 1 51  ? -16.067 2.434   4.088   1.00 18.15 ? 31  LEU A CB    1 
ATOM   243  C  CG    . LEU A 1 51  ? -16.687 3.636   3.387   1.00 19.09 ? 31  LEU A CG    1 
ATOM   244  C  CD1   . LEU A 1 51  ? -17.120 3.224   1.983   1.00 19.92 ? 31  LEU A CD1   1 
ATOM   245  C  CD2   . LEU A 1 51  ? -17.841 4.188   4.188   1.00 20.69 ? 31  LEU A CD2   1 
ATOM   246  N  N     . ASN A 1 52  ? -13.858 0.967   6.173   1.00 15.09 ? 32  ASN A N     1 
ATOM   247  C  CA    . ASN A 1 52  ? -13.483 -0.405  6.516   1.00 15.33 ? 32  ASN A CA    1 
ATOM   248  C  C     . ASN A 1 52  ? -13.859 -0.699  7.967   1.00 15.27 ? 32  ASN A C     1 
ATOM   249  O  O     . ASN A 1 52  ? -13.375 -0.037  8.885   1.00 17.32 ? 32  ASN A O     1 
ATOM   250  C  CB    . ASN A 1 52  ? -11.980 -0.544  6.261   1.00 15.93 ? 32  ASN A CB    1 
ATOM   251  C  CG    . ASN A 1 52  ? -11.407 -1.968  6.488   1.00 15.39 ? 32  ASN A CG    1 
ATOM   252  O  OD1   . ASN A 1 52  ? -10.195 -2.093  6.675   1.00 15.39 ? 32  ASN A OD1   1 
ATOM   253  N  ND2   . ASN A 1 52  ? -12.222 -3.010  6.410   1.00 15.03 ? 32  ASN A ND2   1 
ATOM   254  N  N     . VAL A 1 53  ? -14.728 -1.691  8.162   1.00 15.54 ? 33  VAL A N     1 
ATOM   255  C  CA    . VAL A 1 53  ? -15.063 -2.204  9.489   1.00 16.09 ? 33  VAL A CA    1 
ATOM   256  C  C     . VAL A 1 53  ? -14.909 -3.710  9.602   1.00 16.54 ? 33  VAL A C     1 
ATOM   257  O  O     . VAL A 1 53  ? -14.765 -4.225  10.731  1.00 18.12 ? 33  VAL A O     1 
ATOM   258  C  CB    . VAL A 1 53  ? -16.488 -1.777  9.931   1.00 16.74 ? 33  VAL A CB    1 
ATOM   259  C  CG1   . VAL A 1 53  ? -16.594 -0.269  10.001  1.00 17.93 ? 33  VAL A CG1   1 
ATOM   260  C  CG2   . VAL A 1 53  ? -17.577 -2.357  9.032   1.00 16.64 ? 33  VAL A CG2   1 
ATOM   261  N  N     . TYR A 1 54  ? -14.946 -4.467  8.500   1.00 16.35 ? 34  TYR A N     1 
ATOM   262  C  CA    . TYR A 1 54  ? -14.942 -5.909  8.532   1.00 17.00 ? 34  TYR A CA    1 
ATOM   263  C  C     . TYR A 1 54  ? -13.741 -6.446  7.764   1.00 16.77 ? 34  TYR A C     1 
ATOM   264  O  O     . TYR A 1 54  ? -13.488 -5.990  6.642   1.00 16.90 ? 34  TYR A O     1 
ATOM   265  C  CB    . TYR A 1 54  ? -16.226 -6.480  7.883   1.00 17.74 ? 34  TYR A CB    1 
ATOM   266  C  CG    . TYR A 1 54  ? -16.285 -7.986  7.979   1.00 19.64 ? 34  TYR A CG    1 
ATOM   267  C  CD1   . TYR A 1 54  ? -16.752 -8.596  9.130   1.00 21.67 ? 34  TYR A CD1   1 
ATOM   268  C  CD2   . TYR A 1 54  ? -15.816 -8.798  6.954   1.00 21.62 ? 34  TYR A CD2   1 
ATOM   269  C  CE1   . TYR A 1 54  ? -16.775 -9.966  9.263   1.00 23.75 ? 34  TYR A CE1   1 
ATOM   270  C  CE2   . TYR A 1 54  ? -15.838 -10.188 7.079   1.00 22.99 ? 34  TYR A CE2   1 
ATOM   271  C  CZ    . TYR A 1 54  ? -16.311 -10.755 8.245   1.00 24.27 ? 34  TYR A CZ    1 
ATOM   272  O  OH    . TYR A 1 54  ? -16.348 -12.125 8.417   1.00 27.62 ? 34  TYR A OH    1 
ATOM   273  N  N     . PRO A 1 55  ? -13.030 -7.462  8.285   1.00 16.66 ? 35  PRO A N     1 
ATOM   274  C  CA    . PRO A 1 55  ? -13.243 -8.117  9.586   1.00 17.19 ? 35  PRO A CA    1 
ATOM   275  C  C     . PRO A 1 55  ? -12.760 -7.305  10.785  1.00 17.42 ? 35  PRO A C     1 
ATOM   276  O  O     . PRO A 1 55  ? -13.170 -7.590  11.913  1.00 20.48 ? 35  PRO A O     1 
ATOM   277  C  CB    . PRO A 1 55  ? -12.419 -9.403  9.460   1.00 18.60 ? 35  PRO A CB    1 
ATOM   278  C  CG    . PRO A 1 55  ? -11.369 -9.097  8.494   1.00 20.00 ? 35  PRO A CG    1 
ATOM   279  C  CD    . PRO A 1 55  ? -12.008 -8.169  7.488   1.00 17.73 ? 35  PRO A CD    1 
ATOM   280  N  N     . VAL A 1 56  ? -11.900 -6.323  10.532  1.00 16.53 ? 36  VAL A N     1 
ATOM   281  C  CA    A VAL A 1 56  ? -11.344 -5.422  11.544  0.50 16.59 ? 36  VAL A CA    1 
ATOM   282  C  CA    B VAL A 1 56  ? -11.454 -5.395  11.572  0.50 17.15 ? 36  VAL A CA    1 
ATOM   283  C  C     . VAL A 1 56  ? -11.405 -4.003  10.989  1.00 16.08 ? 36  VAL A C     1 
ATOM   284  O  O     . VAL A 1 56  ? -11.137 -3.815  9.794   1.00 15.91 ? 36  VAL A O     1 
ATOM   285  C  CB    A VAL A 1 56  ? -9.888  -5.795  11.882  0.50 17.44 ? 36  VAL A CB    1 
ATOM   286  C  CB    B VAL A 1 56  ? -10.059 -5.766  12.122  0.50 19.15 ? 36  VAL A CB    1 
ATOM   287  C  CG1   A VAL A 1 56  ? -9.316  -4.880  12.979  0.50 17.79 ? 36  VAL A CG1   1 
ATOM   288  C  CG1   B VAL A 1 56  ? -10.129 -7.061  12.927  0.50 20.38 ? 36  VAL A CG1   1 
ATOM   289  C  CG2   A VAL A 1 56  ? -9.793  -7.257  12.295  0.50 17.85 ? 36  VAL A CG2   1 
ATOM   290  C  CG2   B VAL A 1 56  ? -9.041  -5.873  10.987  0.50 19.39 ? 36  VAL A CG2   1 
ATOM   291  N  N     . PRO A 1 57  ? -11.694 -2.992  11.808  1.00 15.24 ? 37  PRO A N     1 
ATOM   292  C  CA    . PRO A 1 57  ? -11.727 -1.608  11.287  1.00 15.78 ? 37  PRO A CA    1 
ATOM   293  C  C     . PRO A 1 57  ? -10.339 -0.985  11.254  1.00 16.22 ? 37  PRO A C     1 
ATOM   294  O  O     . PRO A 1 57  ? -10.037 -0.046  11.992  1.00 18.19 ? 37  PRO A O     1 
ATOM   295  C  CB    . PRO A 1 57  ? -12.655 -0.912  12.288  1.00 16.03 ? 37  PRO A CB    1 
ATOM   296  C  CG    . PRO A 1 57  ? -12.357 -1.612  13.581  1.00 16.63 ? 37  PRO A CG    1 
ATOM   297  C  CD    . PRO A 1 57  ? -12.184 -3.060  13.204  1.00 16.04 ? 37  PRO A CD    1 
ATOM   298  N  N     . ASP A 1 58  ? -9.458  -1.522  10.407  1.00 16.65 ? 38  ASP A N     1 
ATOM   299  C  CA    . ASP A 1 58  ? -8.055  -1.126  10.426  1.00 17.95 ? 38  ASP A CA    1 
ATOM   300  C  C     . ASP A 1 58  ? -7.700  -0.127  9.332   1.00 19.35 ? 38  ASP A C     1 
ATOM   301  O  O     . ASP A 1 58  ? -6.506  0.099   9.076   1.00 21.07 ? 38  ASP A O     1 
ATOM   302  C  CB    . ASP A 1 58  ? -7.121  -2.344  10.428  1.00 17.83 ? 38  ASP A CB    1 
ATOM   303  C  CG    . ASP A 1 58  ? -7.221  -3.181  9.161   1.00 17.54 ? 38  ASP A CG    1 
ATOM   304  O  OD1   . ASP A 1 58  ? -8.202  -3.024  8.406   1.00 16.44 ? 38  ASP A OD1   1 
ATOM   305  O  OD2   . ASP A 1 58  ? -6.317  -4.018  8.946   1.00 18.68 ? 38  ASP A OD2   1 
ATOM   306  N  N     . GLY A 1 59  ? -8.709  0.469   8.690   1.00 20.09 ? 39  GLY A N     1 
ATOM   307  C  CA    . GLY A 1 59  ? -8.533  1.664   7.880   1.00 20.85 ? 39  GLY A CA    1 
ATOM   308  C  C     . GLY A 1 59  ? -7.706  1.494   6.628   1.00 20.26 ? 39  GLY A C     1 
ATOM   309  O  O     . GLY A 1 59  ? -6.999  2.430   6.228   1.00 23.31 ? 39  GLY A O     1 
ATOM   310  N  N     . ASP A 1 60  ? -7.777  0.331   5.980   1.00 18.17 ? 40  ASP A N     1 
ATOM   311  C  CA    . ASP A 1 60  ? -6.849  0.064   4.897   1.00 16.84 ? 40  ASP A CA    1 
ATOM   312  C  C     . ASP A 1 60  ? -7.438  -0.529  3.624   1.00 15.82 ? 40  ASP A C     1 
ATOM   313  O  O     . ASP A 1 60  ? -6.662  -0.831  2.715   1.00 17.13 ? 40  ASP A O     1 
ATOM   314  C  CB    . ASP A 1 60  ? -5.710  -0.851  5.376   1.00 16.95 ? 40  ASP A CB    1 
ATOM   315  C  CG    . ASP A 1 60  ? -6.216  -2.197  5.848   1.00 16.17 ? 40  ASP A CG    1 
ATOM   316  O  OD1   . ASP A 1 60  ? -7.439  -2.397  5.773   1.00 15.61 ? 40  ASP A OD1   1 
ATOM   317  O  OD2   . ASP A 1 60  ? -5.409  -3.050  6.281   1.00 17.15 ? 40  ASP A OD2   1 
ATOM   318  N  N     . THR A 1 61  ? -8.758  -0.710  3.512   1.00 15.27 ? 41  THR A N     1 
ATOM   319  C  CA    . THR A 1 61  ? -9.284  -1.385  2.321   1.00 14.38 ? 41  THR A CA    1 
ATOM   320  C  C     . THR A 1 61  ? -8.905  -0.643  1.054   1.00 14.51 ? 41  THR A C     1 
ATOM   321  O  O     . THR A 1 61  ? -8.493  -1.258  0.060   1.00 15.09 ? 41  THR A O     1 
ATOM   322  C  CB    . THR A 1 61  ? -10.809 -1.498  2.385   1.00 14.25 ? 41  THR A CB    1 
ATOM   323  O  OG1   . THR A 1 61  ? -11.205 -2.083  3.635   1.00 14.33 ? 41  THR A OG1   1 
ATOM   324  C  CG2   . THR A 1 61  ? -11.329 -2.349  1.216   1.00 14.92 ? 41  THR A CG2   1 
ATOM   325  N  N     . GLY A 1 62  ? -9.084  0.675   1.061   1.00 14.89 ? 42  GLY A N     1 
ATOM   326  C  CA    . GLY A 1 62  ? -8.792  1.459   -0.121  1.00 15.34 ? 42  GLY A CA    1 
ATOM   327  C  C     . GLY A 1 62  ? -7.323  1.423   -0.486  1.00 16.89 ? 42  GLY A C     1 
ATOM   328  O  O     . GLY A 1 62  ? -6.957  1.273   -1.659  1.00 17.17 ? 42  GLY A O     1 
ATOM   329  N  N     . THR A 1 63  ? -6.462  1.589   0.512   1.00 17.89 ? 43  THR A N     1 
ATOM   330  C  CA    . THR A 1 63  ? -5.027  1.491   0.289   1.00 18.37 ? 43  THR A CA    1 
ATOM   331  C  C     . THR A 1 63  ? -4.647  0.112   -0.247  1.00 17.28 ? 43  THR A C     1 
ATOM   332  O  O     . THR A 1 63  ? -3.861  -0.007  -1.194  1.00 18.04 ? 43  THR A O     1 
ATOM   333  C  CB    . THR A 1 63  ? -4.308  1.790   1.604   1.00 21.89 ? 43  THR A CB    1 
ATOM   334  O  OG1   . THR A 1 63  ? -4.576  3.140   2.007   1.00 24.92 ? 43  THR A OG1   1 
ATOM   335  C  CG2   . THR A 1 63  ? -2.815  1.602   1.447   1.00 22.68 ? 43  THR A CG2   1 
ATOM   336  N  N     . ASN A 1 64  ? -5.182  -0.947  0.361   1.00 15.96 ? 44  ASN A N     1 
ATOM   337  C  CA    . ASN A 1 64  ? -4.862  -2.299  -0.068  1.00 16.16 ? 44  ASN A CA    1 
ATOM   338  C  C     . ASN A 1 64  ? -5.292  -2.534  -1.513  1.00 15.35 ? 44  ASN A C     1 
ATOM   339  O  O     . ASN A 1 64  ? -4.530  -3.080  -2.326  1.00 15.51 ? 44  ASN A O     1 
ATOM   340  C  CB    . ASN A 1 64  ? -5.552  -3.304  0.849   1.00 15.63 ? 44  ASN A CB    1 
ATOM   341  C  CG    . ASN A 1 64  ? -4.882  -3.421  2.199   1.00 16.69 ? 44  ASN A CG    1 
ATOM   342  O  OD1   . ASN A 1 64  ? -3.733  -3.009  2.376   1.00 18.59 ? 44  ASN A OD1   1 
ATOM   343  N  ND2   . ASN A 1 64  ? -5.584  -4.019  3.139   1.00 16.58 ? 44  ASN A ND2   1 
ATOM   344  N  N     . MET A 1 65  ? -6.538  -2.172  -1.843  1.00 14.70 ? 45  MET A N     1 
ATOM   345  C  CA    . MET A 1 65  ? -7.015  -2.383  -3.210  1.00 14.41 ? 45  MET A CA    1 
ATOM   346  C  C     . MET A 1 65  ? -6.272  -1.491  -4.190  1.00 14.76 ? 45  MET A C     1 
ATOM   347  O  O     . MET A 1 65  ? -5.935  -1.932  -5.292  1.00 14.56 ? 45  MET A O     1 
ATOM   348  C  CB    . MET A 1 65  ? -8.526  -2.163  -3.290  1.00 14.31 ? 45  MET A CB    1 
ATOM   349  C  CG    . MET A 1 65  ? -9.337  -3.185  -2.502  1.00 13.82 ? 45  MET A CG    1 
ATOM   350  S  SD    . MET A 1 65  ? -11.117 -2.972  -2.595  1.00 14.26 ? 45  MET A SD    1 
ATOM   351  C  CE    . MET A 1 65  ? -11.451 -3.574  -4.235  1.00 14.86 ? 45  MET A CE    1 
ATOM   352  N  N     . ASN A 1 66  ? -6.010  -0.242  -3.813  1.00 15.40 ? 46  ASN A N     1 
ATOM   353  C  CA    . ASN A 1 66  ? -5.266  0.669   -4.682  1.00 16.52 ? 46  ASN A CA    1 
ATOM   354  C  C     . ASN A 1 66  ? -3.872  0.127   -4.973  1.00 17.07 ? 46  ASN A C     1 
ATOM   355  O  O     . ASN A 1 66  ? -3.426  0.131   -6.118  1.00 17.66 ? 46  ASN A O     1 
ATOM   356  C  CB    . ASN A 1 66  ? -5.189  2.046   -4.005  1.00 17.96 ? 46  ASN A CB    1 
ATOM   357  C  CG    . ASN A 1 66  ? -4.569  3.120   -4.882  1.00 20.85 ? 46  ASN A CG    1 
ATOM   358  O  OD1   . ASN A 1 66  ? -4.641  3.071   -6.099  1.00 21.69 ? 46  ASN A OD1   1 
ATOM   359  N  ND2   . ASN A 1 66  ? -3.966  4.111   -4.248  1.00 24.40 ? 46  ASN A ND2   1 
ATOM   360  N  N     . LEU A 1 67  ? -3.166  -0.357  -3.952  1.00 16.58 ? 47  LEU A N     1 
ATOM   361  C  CA    . LEU A 1 67  ? -1.817  -0.863  -4.183  1.00 18.34 ? 47  LEU A CA    1 
ATOM   362  C  C     . LEU A 1 67  ? -1.841  -2.111  -5.054  1.00 17.76 ? 47  LEU A C     1 
ATOM   363  O  O     . LEU A 1 67  ? -0.971  -2.290  -5.919  1.00 18.78 ? 47  LEU A O     1 
ATOM   364  C  CB    . LEU A 1 67  ? -1.129  -1.152  -2.854  1.00 20.44 ? 47  LEU A CB    1 
ATOM   365  C  CG    . LEU A 1 67  ? -0.730  0.083   -2.045  1.00 22.76 ? 47  LEU A CG    1 
ATOM   366  C  CD1   . LEU A 1 67  ? -0.306  -0.321  -0.644  1.00 23.52 ? 47  LEU A CD1   1 
ATOM   367  C  CD2   . LEU A 1 67  ? 0.381   0.855   -2.729  1.00 25.28 ? 47  LEU A CD2   1 
ATOM   368  N  N     . THR A 1 68  ? -2.838  -2.977  -4.850  1.00 15.65 ? 48  THR A N     1 
ATOM   369  C  CA    . THR A 1 68  ? -2.967  -4.179  -5.669  1.00 15.23 ? 48  THR A CA    1 
ATOM   370  C  C     . THR A 1 68  ? -3.260  -3.807  -7.117  1.00 15.74 ? 48  THR A C     1 
ATOM   371  O  O     . THR A 1 68  ? -2.577  -4.261  -8.046  1.00 16.71 ? 48  THR A O     1 
ATOM   372  C  CB    . THR A 1 68  ? -4.095  -5.052  -5.100  1.00 15.34 ? 48  THR A CB    1 
ATOM   373  O  OG1   . THR A 1 68  ? -3.832  -5.407  -3.723  1.00 15.50 ? 48  THR A OG1   1 
ATOM   374  C  CG2   . THR A 1 68  ? -4.278  -6.304  -5.927  1.00 16.24 ? 48  THR A CG2   1 
ATOM   375  N  N     . MET A 1 69  ? -4.271  -2.965  -7.321  1.00 15.51 ? 49  MET A N     1 
ATOM   376  C  CA    . MET A 1 69  ? -4.633  -2.529  -8.665  1.00 16.24 ? 49  MET A CA    1 
ATOM   377  C  C     . MET A 1 69  ? -3.483  -1.800  -9.348  1.00 17.60 ? 49  MET A C     1 
ATOM   378  O  O     . MET A 1 69  ? -3.278  -1.958  -10.554 1.00 18.74 ? 49  MET A O     1 
ATOM   379  C  CB    . MET A 1 69  ? -5.878  -1.648  -8.573  1.00 19.01 ? 49  MET A CB    1 
ATOM   380  C  CG    . MET A 1 69  ? -6.595  -1.468  -9.853  1.00 20.90 ? 49  MET A CG    1 
ATOM   381  S  SD    . MET A 1 69  ? -7.457  -2.949  -10.402 1.00 19.98 ? 49  MET A SD    1 
ATOM   382  C  CE    . MET A 1 69  ? -8.101  -2.203  -11.911 1.00 20.76 ? 49  MET A CE    1 
ATOM   383  N  N     . THR A 1 70  ? -2.723  -0.996  -8.599  1.00 19.31 ? 50  THR A N     1 
ATOM   384  C  CA    . THR A 1 70  ? -1.586  -0.282  -9.178  1.00 21.11 ? 50  THR A CA    1 
ATOM   385  C  C     . THR A 1 70  ? -0.522  -1.250  -9.674  1.00 21.20 ? 50  THR A C     1 
ATOM   386  O  O     . THR A 1 70  ? 0.089   -1.023  -10.724 1.00 21.96 ? 50  THR A O     1 
ATOM   387  C  CB    . THR A 1 70  ? -0.996  0.696   -8.156  1.00 23.86 ? 50  THR A CB    1 
ATOM   388  O  OG1   . THR A 1 70  ? -1.956  1.723   -7.875  1.00 26.00 ? 50  THR A OG1   1 
ATOM   389  C  CG2   . THR A 1 70  ? 0.287   1.323   -8.685  1.00 24.57 ? 50  THR A CG2   1 
ATOM   390  N  N     . SER A 1 71  ? -0.286  -2.337  -8.939  1.00 20.92 ? 51  SER A N     1 
ATOM   391  C  CA    . SER A 1 71  ? 0.659   -3.354  -9.395  1.00 21.17 ? 51  SER A CA    1 
ATOM   392  C  C     . SER A 1 71  ? 0.235   -3.928  -10.743 1.00 21.29 ? 51  SER A C     1 
ATOM   393  O  O     . SER A 1 71  ? 1.063   -4.101  -11.649 1.00 22.21 ? 51  SER A O     1 
ATOM   394  C  CB    . SER A 1 71  ? 0.766   -4.448  -8.330  1.00 22.77 ? 51  SER A CB    1 
ATOM   395  O  OG    . SER A 1 71  ? 1.765   -5.404  -8.636  1.00 25.34 ? 51  SER A OG    1 
ATOM   396  N  N     . GLY A 1 72  ? -1.058  -4.201  -10.915 1.00 19.90 ? 52  GLY A N     1 
ATOM   397  C  CA    . GLY A 1 72  ? -1.531  -4.663  -12.210 1.00 18.65 ? 52  GLY A CA    1 
ATOM   398  C  C     . GLY A 1 72  ? -1.431  -3.586  -13.274 1.00 18.83 ? 52  GLY A C     1 
ATOM   399  O  O     . GLY A 1 72  ? -0.997  -3.849  -14.396 1.00 19.55 ? 52  GLY A O     1 
ATOM   400  N  N     . ARG A 1 73  ? -1.855  -2.364  -12.942 1.00 18.35 ? 53  ARG A N     1 
ATOM   401  C  CA    . ARG A 1 73  ? -1.845  -1.270  -13.913 1.00 19.47 ? 53  ARG A CA    1 
ATOM   402  C  C     . ARG A 1 73  ? -0.441  -1.009  -14.427 1.00 20.27 ? 53  ARG A C     1 
ATOM   403  O  O     . ARG A 1 73  ? -0.243  -0.751  -15.623 1.00 20.60 ? 53  ARG A O     1 
ATOM   404  C  CB    . ARG A 1 73  ? -2.406  -0.003  -13.256 1.00 20.94 ? 53  ARG A CB    1 
ATOM   405  C  CG    . ARG A 1 73  ? -2.339  1.285   -14.100 1.00 23.83 ? 53  ARG A CG    1 
ATOM   406  C  CD    . ARG A 1 73  ? -2.372  2.543   -13.211 1.00 26.80 ? 53  ARG A CD    1 
ATOM   407  N  NE    . ARG A 1 73  ? -2.190  3.795   -13.952 1.00 30.04 ? 53  ARG A NE    1 
ATOM   408  C  CZ    . ARG A 1 73  ? -3.007  4.849   -13.899 1.00 31.56 ? 53  ARG A CZ    1 
ATOM   409  N  NH1   . ARG A 1 73  ? -4.095  4.828   -13.135 1.00 31.84 ? 53  ARG A NH1   1 
ATOM   410  N  NH2   . ARG A 1 73  ? -2.732  5.933   -14.619 1.00 32.19 ? 53  ARG A NH2   1 
ATOM   411  N  N     . GLU A 1 74  ? 0.548   -1.049  -13.536 1.00 20.72 ? 54  GLU A N     1 
ATOM   412  C  CA    . GLU A 1 74  ? 1.915   -0.760  -13.948 1.00 24.05 ? 54  GLU A CA    1 
ATOM   413  C  C     . GLU A 1 74  ? 2.426   -1.809  -14.926 1.00 23.26 ? 54  GLU A C     1 
ATOM   414  O  O     . GLU A 1 74  ? 3.107   -1.473  -15.902 1.00 24.09 ? 54  GLU A O     1 
ATOM   415  C  CB    . GLU A 1 74  ? 2.814   -0.650  -12.715 1.00 27.25 ? 54  GLU A CB    1 
ATOM   416  C  CG    . GLU A 1 74  ? 2.597   0.644   -11.931 1.00 31.03 ? 54  GLU A CG    1 
ATOM   417  C  CD    . GLU A 1 74  ? 3.430   0.735   -10.652 1.00 34.75 ? 54  GLU A CD    1 
ATOM   418  O  OE1   . GLU A 1 74  ? 3.937   -0.305  -10.173 1.00 36.29 ? 54  GLU A OE1   1 
ATOM   419  O  OE2   . GLU A 1 74  ? 3.569   1.857   -10.115 1.00 36.12 ? 54  GLU A OE2   1 
ATOM   420  N  N     . GLU A 1 75  ? 2.102   -3.083  -14.699 1.00 22.90 ? 55  GLU A N     1 
ATOM   421  C  CA    . GLU A 1 75  ? 2.528   -4.101  -15.652 1.00 23.51 ? 55  GLU A CA    1 
ATOM   422  C  C     . GLU A 1 75  ? 1.878   -3.857  -17.005 1.00 21.54 ? 55  GLU A C     1 
ATOM   423  O  O     . GLU A 1 75  ? 2.530   -3.962  -18.049 1.00 21.60 ? 55  GLU A O     1 
ATOM   424  C  CB    . GLU A 1 75  ? 2.165   -5.496  -15.150 1.00 26.71 ? 55  GLU A CB    1 
ATOM   425  C  CG    . GLU A 1 75  ? 2.949   -5.971  -13.956 1.00 30.43 ? 55  GLU A CG    1 
ATOM   426  C  CD    . GLU A 1 75  ? 4.438   -6.078  -14.219 1.00 33.94 ? 55  GLU A CD    1 
ATOM   427  O  OE1   . GLU A 1 75  ? 5.216   -5.517  -13.421 1.00 36.00 ? 55  GLU A OE1   1 
ATOM   428  O  OE2   . GLU A 1 75  ? 4.833   -6.719  -15.217 1.00 35.14 ? 55  GLU A OE2   1 
ATOM   429  N  N     . VAL A 1 76  ? 0.587   -3.521  -16.999 1.00 20.55 ? 56  VAL A N     1 
ATOM   430  C  CA    . VAL A 1 76  ? -0.145  -3.260  -18.237 1.00 19.55 ? 56  VAL A CA    1 
ATOM   431  C  C     . VAL A 1 76  ? 0.466   -2.081  -18.993 1.00 21.62 ? 56  VAL A C     1 
ATOM   432  O  O     . VAL A 1 76  ? 0.700   -2.154  -20.206 1.00 21.34 ? 56  VAL A O     1 
ATOM   433  C  CB    . VAL A 1 76  ? -1.628  -3.026  -17.912 1.00 19.17 ? 56  VAL A CB    1 
ATOM   434  C  CG1   . VAL A 1 76  ? -2.354  -2.383  -19.095 1.00 20.17 ? 56  VAL A CG1   1 
ATOM   435  C  CG2   . VAL A 1 76  ? -2.277  -4.341  -17.529 1.00 18.73 ? 56  VAL A CG2   1 
ATOM   436  N  N     . GLU A 1 77  ? 0.729   -0.975  -18.291 1.00 22.74 ? 57  GLU A N     1 
ATOM   437  C  CA    . GLU A 1 77  ? 1.233   0.223   -18.958 1.00 25.73 ? 57  GLU A CA    1 
ATOM   438  C  C     . GLU A 1 77  ? 2.587   -0.020  -19.602 1.00 27.05 ? 57  GLU A C     1 
ATOM   439  O  O     . GLU A 1 77  ? 2.917   0.622   -20.607 1.00 28.83 ? 57  GLU A O     1 
ATOM   440  C  CB    . GLU A 1 77  ? 1.307   1.379   -17.963 1.00 27.90 ? 57  GLU A CB    1 
ATOM   441  C  CG    . GLU A 1 77  ? -0.057  1.994   -17.675 1.00 30.38 ? 57  GLU A CG    1 
ATOM   442  C  CD    . GLU A 1 77  ? -0.038  3.009   -16.548 1.00 33.33 ? 57  GLU A CD    1 
ATOM   443  O  OE1   . GLU A 1 77  ? 0.903   2.987   -15.726 1.00 34.50 ? 57  GLU A OE1   1 
ATOM   444  O  OE2   . GLU A 1 77  ? -0.982  3.828   -16.478 1.00 34.77 ? 57  GLU A OE2   1 
ATOM   445  N  N     . ASN A 1 78  ? 3.372   -0.949  -19.067 1.00 26.56 ? 58  ASN A N     1 
ATOM   446  C  CA    . ASN A 1 78  ? 4.695   -1.234  -19.600 1.00 28.84 ? 58  ASN A CA    1 
ATOM   447  C  C     . ASN A 1 78  ? 4.697   -2.322  -20.667 1.00 27.03 ? 58  ASN A C     1 
ATOM   448  O  O     . ASN A 1 78  ? 5.739   -2.552  -21.288 1.00 27.92 ? 58  ASN A O     1 
ATOM   449  C  CB    . ASN A 1 78  ? 5.630   -1.665  -18.466 1.00 33.13 ? 58  ASN A CB    1 
ATOM   450  C  CG    . ASN A 1 78  ? 6.038   -0.511  -17.575 1.00 37.59 ? 58  ASN A CG    1 
ATOM   451  O  OD1   . ASN A 1 78  ? 6.164   0.629   -18.029 1.00 40.29 ? 58  ASN A OD1   1 
ATOM   452  N  ND2   . ASN A 1 78  ? 6.259   -0.802  -16.302 1.00 38.54 ? 58  ASN A ND2   1 
ATOM   453  N  N     . ASN A 1 79  ? 3.567   -2.993  -20.897 1.00 24.55 ? 59  ASN A N     1 
ATOM   454  C  CA    A ASN A 1 79  ? 3.506   -4.111  -21.836 0.50 24.12 ? 59  ASN A CA    1 
ATOM   455  C  CA    B ASN A 1 79  ? 3.483   -4.140  -21.787 0.50 23.57 ? 59  ASN A CA    1 
ATOM   456  C  C     . ASN A 1 79  ? 2.095   -4.170  -22.427 1.00 22.27 ? 59  ASN A C     1 
ATOM   457  O  O     . ASN A 1 79  ? 1.294   -5.065  -22.175 1.00 23.92 ? 59  ASN A O     1 
ATOM   458  C  CB    A ASN A 1 79  ? 3.907   -5.437  -21.186 0.50 26.11 ? 59  ASN A CB    1 
ATOM   459  C  CB    B ASN A 1 79  ? 3.715   -5.446  -21.020 0.50 24.54 ? 59  ASN A CB    1 
ATOM   460  C  CG    A ASN A 1 79  ? 4.087   -6.552  -22.203 0.50 27.52 ? 59  ASN A CG    1 
ATOM   461  C  CG    B ASN A 1 79  ? 5.018   -5.459  -20.271 0.50 25.39 ? 59  ASN A CG    1 
ATOM   462  O  OD1   A ASN A 1 79  ? 4.067   -6.315  -23.408 0.50 28.10 ? 59  ASN A OD1   1 
ATOM   463  O  OD1   B ASN A 1 79  ? 6.061   -5.771  -20.838 0.50 25.56 ? 59  ASN A OD1   1 
ATOM   464  N  ND2   A ASN A 1 79  ? 4.265   -7.774  -21.720 0.50 28.40 ? 59  ASN A ND2   1 
ATOM   465  N  ND2   B ASN A 1 79  ? 4.970   -5.127  -18.987 0.50 26.05 ? 59  ASN A ND2   1 
ATOM   466  N  N     . LEU A 1 80  ? 1.786   -3.182  -23.261 1.00 19.97 ? 60  LEU A N     1 
ATOM   467  C  CA    . LEU A 1 80  ? 0.494   -3.158  -23.925 1.00 19.33 ? 60  LEU A CA    1 
ATOM   468  C  C     . LEU A 1 80  ? 0.479   -4.141  -25.096 1.00 19.26 ? 60  LEU A C     1 
ATOM   469  O  O     . LEU A 1 80  ? 1.517   -4.506  -25.650 1.00 21.09 ? 60  LEU A O     1 
ATOM   470  C  CB    . LEU A 1 80  ? 0.190   -1.746  -24.423 1.00 19.15 ? 60  LEU A CB    1 
ATOM   471  C  CG    . LEU A 1 80  ? 0.033   -0.677  -23.337 1.00 20.37 ? 60  LEU A CG    1 
ATOM   472  C  CD1   . LEU A 1 80  ? -0.009  0.691   -23.964 1.00 22.12 ? 60  LEU A CD1   1 
ATOM   473  C  CD2   . LEU A 1 80  ? -1.225  -0.895  -22.515 1.00 21.10 ? 60  LEU A CD2   1 
ATOM   474  N  N     . SER A 1 81  ? -0.725  -4.564  -25.473 1.00 20.38 ? 61  SER A N     1 
ATOM   475  C  CA    . SER A 1 81  ? -0.932  -5.489  -26.578 1.00 20.37 ? 61  SER A CA    1 
ATOM   476  C  C     . SER A 1 81  ? -2.316  -5.260  -27.166 1.00 19.79 ? 61  SER A C     1 
ATOM   477  O  O     . SER A 1 81  ? -3.255  -4.911  -26.451 1.00 19.88 ? 61  SER A O     1 
ATOM   478  C  CB    . SER A 1 81  ? -0.845  -6.943  -26.113 1.00 21.23 ? 61  SER A CB    1 
ATOM   479  O  OG    . SER A 1 81  ? -1.108  -7.829  -27.186 1.00 21.21 ? 61  SER A OG    1 
ATOM   480  N  N     . LYS A 1 82  ? -2.439  -5.477  -28.483 1.00 18.78 ? 62  LYS A N     1 
ATOM   481  C  CA    . LYS A 1 82  ? -3.756  -5.491  -29.114 1.00 20.23 ? 62  LYS A CA    1 
ATOM   482  C  C     . LYS A 1 82  ? -4.541  -6.736  -28.734 1.00 18.09 ? 62  LYS A C     1 
ATOM   483  O  O     . LYS A 1 82  ? -5.762  -6.763  -28.911 1.00 18.58 ? 62  LYS A O     1 
ATOM   484  C  CB    . LYS A 1 82  ? -3.632  -5.418  -30.643 1.00 23.76 ? 62  LYS A CB    1 
ATOM   485  C  CG    . LYS A 1 82  ? -3.130  -6.708  -31.262 1.00 27.07 ? 62  LYS A CG    1 
ATOM   486  C  CD    . LYS A 1 82  ? -2.722  -6.535  -32.701 1.00 30.73 ? 62  LYS A CD    1 
ATOM   487  C  CE    . LYS A 1 82  ? -1.738  -7.631  -33.094 1.00 34.47 ? 62  LYS A CE    1 
ATOM   488  N  NZ    . LYS A 1 82  ? -1.375  -7.550  -34.529 1.00 36.91 ? 62  LYS A NZ    1 
ATOM   489  N  N     . ASN A 1 83  ? -3.866  -7.764  -28.221 1.00 17.82 ? 63  ASN A N     1 
ATOM   490  C  CA    . ASN A 1 83  ? -4.481  -9.058  -27.958 1.00 17.61 ? 63  ASN A CA    1 
ATOM   491  C  C     . ASN A 1 83  ? -4.975  -9.061  -26.516 1.00 16.18 ? 63  ASN A C     1 
ATOM   492  O  O     . ASN A 1 83  ? -4.172  -8.995  -25.578 1.00 16.59 ? 63  ASN A O     1 
ATOM   493  C  CB    . ASN A 1 83  ? -3.454  -10.165 -28.184 1.00 18.54 ? 63  ASN A CB    1 
ATOM   494  C  CG    . ASN A 1 83  ? -4.046  -11.554 -28.043 1.00 20.20 ? 63  ASN A CG    1 
ATOM   495  O  OD1   . ASN A 1 83  ? -4.214  -12.051 -26.941 1.00 21.56 ? 63  ASN A OD1   1 
ATOM   496  N  ND2   . ASN A 1 83  ? -4.367  -12.182 -29.156 1.00 21.68 ? 63  ASN A ND2   1 
ATOM   497  N  N     . ILE A 1 84  ? -6.290  -9.152  -26.335 1.00 14.90 ? 64  ILE A N     1 
ATOM   498  C  CA    . ILE A 1 84  ? -6.839  -9.012  -24.984 1.00 14.52 ? 64  ILE A CA    1 
ATOM   499  C  C     . ILE A 1 84  ? -6.367  -10.144 -24.078 1.00 15.09 ? 64  ILE A C     1 
ATOM   500  O  O     . ILE A 1 84  ? -6.151  -9.939  -22.879 1.00 15.45 ? 64  ILE A O     1 
ATOM   501  C  CB    . ILE A 1 84  ? -8.373  -8.884  -25.027 1.00 15.02 ? 64  ILE A CB    1 
ATOM   502  C  CG1   . ILE A 1 84  ? -8.868  -8.335  -23.683 1.00 14.97 ? 64  ILE A CG1   1 
ATOM   503  C  CG2   . ILE A 1 84  ? -9.038  -10.215 -25.392 1.00 15.72 ? 64  ILE A CG2   1 
ATOM   504  C  CD1   . ILE A 1 84  ? -10.363 -8.153  -23.597 1.00 15.60 ? 64  ILE A CD1   1 
ATOM   505  N  N     . GLY A 1 85  ? -6.243  -11.361 -24.610 1.00 15.40 ? 65  GLY A N     1 
ATOM   506  C  CA    . GLY A 1 85  ? -5.792  -12.469 -23.782 1.00 15.58 ? 65  GLY A CA    1 
ATOM   507  C  C     . GLY A 1 85  ? -4.391  -12.260 -23.248 1.00 16.37 ? 65  GLY A C     1 
ATOM   508  O  O     . GLY A 1 85  ? -4.120  -12.517 -22.072 1.00 15.79 ? 65  GLY A O     1 
ATOM   509  N  N     . GLU A 1 86  ? -3.481  -11.794 -24.100 1.00 17.20 ? 66  GLU A N     1 
ATOM   510  C  CA    . GLU A 1 86  ? -2.128  -11.509 -23.647 1.00 17.77 ? 66  GLU A CA    1 
ATOM   511  C  C     . GLU A 1 86  ? -2.113  -10.365 -22.649 1.00 16.24 ? 66  GLU A C     1 
ATOM   512  O  O     . GLU A 1 86  ? -1.420  -10.435 -21.627 1.00 16.83 ? 66  GLU A O     1 
ATOM   513  C  CB    . GLU A 1 86  ? -1.233  -11.189 -24.846 1.00 22.05 ? 66  GLU A CB    1 
ATOM   514  C  CG    . GLU A 1 86  ? -0.944  -12.403 -25.721 1.00 28.60 ? 66  GLU A CG    1 
ATOM   515  C  CD    . GLU A 1 86  ? -0.364  -13.569 -24.934 1.00 34.28 ? 66  GLU A CD    1 
ATOM   516  O  OE1   . GLU A 1 86  ? 0.491   -13.335 -24.046 1.00 36.11 ? 66  GLU A OE1   1 
ATOM   517  O  OE2   . GLU A 1 86  ? -0.788  -14.720 -25.181 1.00 36.55 ? 66  GLU A OE2   1 
ATOM   518  N  N     . LEU A 1 87  ? -2.896  -9.321  -22.906 1.00 15.78 ? 67  LEU A N     1 
ATOM   519  C  CA    . LEU A 1 87  ? -2.960  -8.201  -21.971 1.00 15.43 ? 67  LEU A CA    1 
ATOM   520  C  C     . LEU A 1 87  ? -3.499  -8.662  -20.621 1.00 15.44 ? 67  LEU A C     1 
ATOM   521  O  O     . LEU A 1 87  ? -3.000  -8.247  -19.562 1.00 16.23 ? 67  LEU A O     1 
ATOM   522  C  CB    . LEU A 1 87  ? -3.817  -7.085  -22.575 1.00 17.03 ? 67  LEU A CB    1 
ATOM   523  C  CG    . LEU A 1 87  ? -3.712  -5.662  -22.027 1.00 17.71 ? 67  LEU A CG    1 
ATOM   524  C  CD1   . LEU A 1 87  ? -4.481  -5.492  -20.730 1.00 18.28 ? 67  LEU A CD1   1 
ATOM   525  C  CD2   . LEU A 1 87  ? -2.259  -5.244  -21.877 1.00 18.71 ? 67  LEU A CD2   1 
ATOM   526  N  N     . GLY A 1 88  ? -4.507  -9.537  -20.642 1.00 15.52 ? 68  GLY A N     1 
ATOM   527  C  CA    . GLY A 1 88  ? -5.028  -10.093 -19.407 1.00 15.37 ? 68  GLY A CA    1 
ATOM   528  C  C     . GLY A 1 88  ? -3.987  -10.879 -18.630 1.00 15.19 ? 68  GLY A C     1 
ATOM   529  O  O     . GLY A 1 88  ? -3.981  -10.851 -17.398 1.00 16.34 ? 68  GLY A O     1 
ATOM   530  N  N     . LYS A 1 89  ? -3.132  -11.634 -19.328 1.00 16.09 ? 69  LYS A N     1 
ATOM   531  C  CA    . LYS A 1 89  ? -2.068  -12.353 -18.630 1.00 16.82 ? 69  LYS A CA    1 
ATOM   532  C  C     . LYS A 1 89  ? -1.141  -11.379 -17.914 1.00 16.16 ? 69  LYS A C     1 
ATOM   533  O  O     . LYS A 1 89  ? -0.722  -11.617 -16.775 1.00 17.35 ? 69  LYS A O     1 
ATOM   534  C  CB    . LYS A 1 89  ? -1.260  -13.206 -19.607 1.00 19.18 ? 69  LYS A CB    1 
ATOM   535  C  CG    . LYS A 1 89  ? -1.990  -14.401 -20.158 1.00 22.59 ? 69  LYS A CG    1 
ATOM   536  C  CD    . LYS A 1 89  ? -1.100  -15.190 -21.087 1.00 25.94 ? 69  LYS A CD    1 
ATOM   537  C  CE    . LYS A 1 89  ? -1.929  -16.070 -22.000 1.00 28.85 ? 69  LYS A CE    1 
ATOM   538  N  NZ    . LYS A 1 89  ? -1.081  -16.874 -22.919 1.00 30.59 ? 69  LYS A NZ    1 
ATOM   539  N  N     . THR A 1 90  ? -0.825  -10.270 -18.571 1.00 15.96 ? 70  THR A N     1 
ATOM   540  C  CA    . THR A 1 90  ? 0.040   -9.256  -17.990 1.00 16.12 ? 70  THR A CA    1 
ATOM   541  C  C     . THR A 1 90  ? -0.607  -8.611  -16.767 1.00 16.13 ? 70  THR A C     1 
ATOM   542  O  O     . THR A 1 90  ? 0.034   -8.441  -15.717 1.00 17.27 ? 70  THR A O     1 
ATOM   543  C  CB    . THR A 1 90  ? 0.336   -8.226  -19.080 1.00 17.67 ? 70  THR A CB    1 
ATOM   544  O  OG1   . THR A 1 90  ? 1.085   -8.869  -20.117 1.00 19.30 ? 70  THR A OG1   1 
ATOM   545  C  CG2   . THR A 1 90  ? 1.102   -7.040  -18.537 1.00 18.81 ? 70  THR A CG2   1 
ATOM   546  N  N     . PHE A 1 91  ? -1.885  -8.247  -16.887 1.00 15.54 ? 71  PHE A N     1 
ATOM   547  C  CA    . PHE A 1 91  ? -2.608  -7.632  -15.778 1.00 15.33 ? 71  PHE A CA    1 
ATOM   548  C  C     . PHE A 1 91  ? -2.709  -8.589  -14.597 1.00 15.16 ? 71  PHE A C     1 
ATOM   549  O  O     . PHE A 1 91  ? -2.414  -8.220  -13.453 1.00 15.81 ? 71  PHE A O     1 
ATOM   550  C  CB    . PHE A 1 91  ? -4.000  -7.252  -16.278 1.00 15.53 ? 71  PHE A CB    1 
ATOM   551  C  CG    . PHE A 1 91  ? -4.887  -6.625  -15.239 1.00 16.71 ? 71  PHE A CG    1 
ATOM   552  C  CD1   . PHE A 1 91  ? -4.431  -5.583  -14.456 1.00 17.72 ? 71  PHE A CD1   1 
ATOM   553  C  CD2   . PHE A 1 91  ? -6.202  -7.034  -15.115 1.00 17.32 ? 71  PHE A CD2   1 
ATOM   554  C  CE1   . PHE A 1 91  ? -5.268  -4.992  -13.515 1.00 17.97 ? 71  PHE A CE1   1 
ATOM   555  C  CE2   . PHE A 1 91  ? -7.044  -6.448  -14.188 1.00 17.73 ? 71  PHE A CE2   1 
ATOM   556  C  CZ    . PHE A 1 91  ? -6.578  -5.421  -13.390 1.00 18.35 ? 71  PHE A CZ    1 
ATOM   557  N  N     . SER A 1 92  ? -3.121  -9.828  -14.876 1.00 15.87 ? 72  SER A N     1 
ATOM   558  C  CA    . SER A 1 92  ? -3.301  -10.844 -13.847 1.00 16.93 ? 72  SER A CA    1 
ATOM   559  C  C     . SER A 1 92  ? -2.008  -11.062 -13.064 1.00 16.84 ? 72  SER A C     1 
ATOM   560  O  O     . SER A 1 92  ? -2.011  -11.074 -11.825 1.00 16.92 ? 72  SER A O     1 
ATOM   561  C  CB    . SER A 1 92  ? -3.794  -12.138 -14.518 1.00 19.53 ? 72  SER A CB    1 
ATOM   562  O  OG    . SER A 1 92  ? -3.967  -13.183 -13.581 1.00 22.51 ? 72  SER A OG    1 
ATOM   563  N  N     . LYS A 1 93  ? -0.892  -11.213 -13.772 1.00 16.78 ? 73  LYS A N     1 
ATOM   564  C  CA    . LYS A 1 93  ? 0.390   -11.426 -13.117 1.00 18.51 ? 73  LYS A CA    1 
ATOM   565  C  C     . LYS A 1 93  ? 0.727   -10.255 -12.204 1.00 18.04 ? 73  LYS A C     1 
ATOM   566  O  O     . LYS A 1 93  ? 1.191   -10.451 -11.076 1.00 17.96 ? 73  LYS A O     1 
ATOM   567  C  CB    . LYS A 1 93  ? 1.471   -11.632 -14.180 1.00 21.29 ? 73  LYS A CB    1 
ATOM   568  C  CG    . LYS A 1 93  ? 2.842   -11.926 -13.608 1.00 23.56 ? 73  LYS A CG    1 
ATOM   569  N  N     . GLY A 1 94  ? 0.489   -9.028  -12.669 1.00 17.90 ? 74  GLY A N     1 
ATOM   570  C  CA    . GLY A 1 94  ? 0.787   -7.869  -11.847 1.00 18.41 ? 74  GLY A CA    1 
ATOM   571  C  C     . GLY A 1 94  ? -0.031  -7.849  -10.567 1.00 17.36 ? 74  GLY A C     1 
ATOM   572  O  O     . GLY A 1 94  ? 0.495   -7.586  -9.478  1.00 18.44 ? 74  GLY A O     1 
ATOM   573  N  N     . LEU A 1 95  ? -1.331  -8.135  -10.672 1.00 16.05 ? 75  LEU A N     1 
ATOM   574  C  CA    . LEU A 1 95  ? -2.181  -8.180  -9.484  1.00 15.37 ? 75  LEU A CA    1 
ATOM   575  C  C     . LEU A 1 95  ? -1.710  -9.249  -8.505  1.00 14.63 ? 75  LEU A C     1 
ATOM   576  O  O     . LEU A 1 95  ? -1.691  -9.029  -7.285  1.00 15.41 ? 75  LEU A O     1 
ATOM   577  C  CB    . LEU A 1 95  ? -3.628  -8.493  -9.869  1.00 15.64 ? 75  LEU A CB    1 
ATOM   578  C  CG    . LEU A 1 95  ? -4.375  -7.478  -10.723 1.00 15.37 ? 75  LEU A CG    1 
ATOM   579  C  CD1   . LEU A 1 95  ? -5.710  -8.047  -11.141 1.00 17.34 ? 75  LEU A CD1   1 
ATOM   580  C  CD2   . LEU A 1 95  ? -4.575  -6.181  -9.972  1.00 17.02 ? 75  LEU A CD2   1 
ATOM   581  N  N     . LEU A 1 96  ? -1.371  -10.432 -9.024  1.00 14.69 ? 76  LEU A N     1 
ATOM   582  C  CA    . LEU A 1 96  ? -1.075  -11.582 -8.188  1.00 15.01 ? 76  LEU A CA    1 
ATOM   583  C  C     . LEU A 1 96  ? 0.269   -11.470 -7.481  1.00 16.62 ? 76  LEU A C     1 
ATOM   584  O  O     . LEU A 1 96  ? 0.486   -12.174 -6.491  1.00 20.21 ? 76  LEU A O     1 
ATOM   585  C  CB    . LEU A 1 96  ? -1.163  -12.868 -9.008  1.00 14.88 ? 76  LEU A CB    1 
ATOM   586  C  CG    . LEU A 1 96  ? -2.591  -13.208 -9.452  1.00 14.60 ? 76  LEU A CG    1 
ATOM   587  C  CD1   . LEU A 1 96  ? -2.576  -14.197 -10.616 1.00 15.30 ? 76  LEU A CD1   1 
ATOM   588  C  CD2   . LEU A 1 96  ? -3.405  -13.757 -8.279  1.00 15.65 ? 76  LEU A CD2   1 
ATOM   589  N  N     . MET A 1 97  ? 1.172   -10.616 -7.956  1.00 16.70 ? 77  MET A N     1 
ATOM   590  C  CA    . MET A 1 97  ? 2.461   -10.390 -7.317  1.00 18.09 ? 77  MET A CA    1 
ATOM   591  C  C     . MET A 1 97  ? 2.446   -9.163  -6.418  1.00 18.86 ? 77  MET A C     1 
ATOM   592  O  O     . MET A 1 97  ? 3.490   -8.801  -5.859  1.00 20.41 ? 77  MET A O     1 
ATOM   593  C  CB    . MET A 1 97  ? 3.560   -10.255 -8.374  1.00 22.51 ? 77  MET A CB    1 
ATOM   594  C  CG    . MET A 1 97  ? 3.780   -11.509 -9.183  1.00 27.77 ? 77  MET A CG    1 
ATOM   595  S  SD    . MET A 1 97  ? 5.153   -11.334 -10.316 1.00 34.37 ? 77  MET A SD    1 
ATOM   596  C  CE    . MET A 1 97  ? 5.271   -9.553  -10.462 1.00 35.72 ? 77  MET A CE    1 
ATOM   597  N  N     . GLY A 1 98  ? 1.289   -8.526  -6.252  1.00 20.07 ? 78  GLY A N     1 
ATOM   598  C  CA    . GLY A 1 98  ? 1.192   -7.351  -5.407  1.00 21.24 ? 78  GLY A CA    1 
ATOM   599  C  C     . GLY A 1 98  ? -0.094  -7.283  -4.612  1.00 20.65 ? 78  GLY A C     1 
ATOM   600  O  O     . GLY A 1 98  ? -0.543  -6.190  -4.257  1.00 20.79 ? 78  GLY A O     1 
ATOM   601  N  N     . ALA A 1 99  ? -0.688  -8.435  -4.303  1.00 19.72 ? 79  ALA A N     1 
ATOM   602  C  CA    . ALA A 1 99  ? -1.996  -8.462  -3.667  1.00 18.88 ? 79  ALA A CA    1 
ATOM   603  C  C     . ALA A 1 99  ? -1.850  -8.199  -2.170  1.00 20.30 ? 79  ALA A C     1 
ATOM   604  O  O     . ALA A 1 99  ? -1.144  -8.933  -1.470  1.00 24.28 ? 79  ALA A O     1 
ATOM   605  C  CB    . ALA A 1 99  ? -2.669  -9.805  -3.923  1.00 18.06 ? 79  ALA A CB    1 
ATOM   606  N  N     . ARG A 1 100 ? -2.543  -7.174  -1.677  1.00 18.07 ? 80  ARG A N     1 
ATOM   607  C  CA    . ARG A 1 100 ? -2.425  -6.720  -0.297  1.00 18.58 ? 80  ARG A CA    1 
ATOM   608  C  C     . ARG A 1 100 ? -3.763  -6.858  0.414   1.00 17.24 ? 80  ARG A C     1 
ATOM   609  O  O     . ARG A 1 100 ? -4.784  -6.352  -0.060  1.00 17.55 ? 80  ARG A O     1 
ATOM   610  C  CB    . ARG A 1 100 ? -1.998  -5.250  -0.238  1.00 20.86 ? 80  ARG A CB    1 
ATOM   611  C  CG    . ARG A 1 100 ? -0.624  -4.962  -0.816  1.00 23.54 ? 80  ARG A CG    1 
ATOM   612  N  N     . GLY A 1 101 ? -3.737  -7.480  1.586   1.00 16.68 ? 81  GLY A N     1 
ATOM   613  C  CA    . GLY A 1 101 ? -4.911  -7.546  2.433   1.00 16.77 ? 81  GLY A CA    1 
ATOM   614  C  C     . GLY A 1 101 ? -5.990  -8.476  1.925   1.00 16.34 ? 81  GLY A C     1 
ATOM   615  O  O     . GLY A 1 101 ? -5.909  -9.014  0.815   1.00 16.78 ? 81  GLY A O     1 
ATOM   616  N  N     . ASN A 1 102 ? -7.034  -8.669  2.729   1.00 15.36 ? 82  ASN A N     1 
ATOM   617  C  CA    . ASN A 1 102 ? -8.132  -9.508  2.265   1.00 15.03 ? 82  ASN A CA    1 
ATOM   618  C  C     . ASN A 1 102 ? -8.715  -8.984  0.961   1.00 14.49 ? 82  ASN A C     1 
ATOM   619  O  O     . ASN A 1 102 ? -9.033  -9.768  0.062   1.00 14.61 ? 82  ASN A O     1 
ATOM   620  C  CB    . ASN A 1 102 ? -9.217  -9.598  3.337   1.00 16.15 ? 82  ASN A CB    1 
ATOM   621  C  CG    . ASN A 1 102 ? -8.830  -10.506 4.470   1.00 19.39 ? 82  ASN A CG    1 
ATOM   622  O  OD1   . ASN A 1 102 ? -8.324  -11.599 4.252   1.00 23.43 ? 82  ASN A OD1   1 
ATOM   623  N  ND2   . ASN A 1 102 ? -9.040  -10.047 5.690   1.00 19.91 ? 82  ASN A ND2   1 
ATOM   624  N  N     . SER A 1 103 ? -8.893  -7.665  0.850   1.00 13.95 ? 83  SER A N     1 
ATOM   625  C  CA    . SER A 1 103 ? -9.554  -7.122  -0.330  1.00 13.41 ? 83  SER A CA    1 
ATOM   626  C  C     . SER A 1 103 ? -8.670  -7.227  -1.561  1.00 13.41 ? 83  SER A C     1 
ATOM   627  O  O     . SER A 1 103 ? -9.166  -7.506  -2.656  1.00 13.77 ? 83  SER A O     1 
ATOM   628  C  CB    . SER A 1 103 ? -9.965  -5.671  -0.098  1.00 14.04 ? 83  SER A CB    1 
ATOM   629  O  OG    . SER A 1 103 ? -8.854  -4.834  0.135   1.00 14.29 ? 83  SER A OG    1 
ATOM   630  N  N     . GLY A 1 104 ? -7.374  -6.951  -1.417  1.00 14.04 ? 84  GLY A N     1 
ATOM   631  C  CA    . GLY A 1 104 ? -6.477  -7.054  -2.552  1.00 14.36 ? 84  GLY A CA    1 
ATOM   632  C  C     . GLY A 1 104 ? -6.324  -8.481  -3.033  1.00 12.98 ? 84  GLY A C     1 
ATOM   633  O  O     . GLY A 1 104 ? -6.283  -8.743  -4.239  1.00 13.78 ? 84  GLY A O     1 
ATOM   634  N  N     . VAL A 1 105 ? -6.229  -9.428  -2.110  1.00 13.22 ? 85  VAL A N     1 
ATOM   635  C  CA    . VAL A 1 105 ? -6.193  -10.826 -2.511  1.00 13.59 ? 85  VAL A CA    1 
ATOM   636  C  C     . VAL A 1 105 ? -7.471  -11.198 -3.260  1.00 12.87 ? 85  VAL A C     1 
ATOM   637  O  O     . VAL A 1 105 ? -7.422  -11.783 -4.344  1.00 12.48 ? 85  VAL A O     1 
ATOM   638  C  CB    . VAL A 1 105 ? -5.917  -11.747 -1.311  1.00 14.84 ? 85  VAL A CB    1 
ATOM   639  C  CG1   . VAL A 1 105 ? -6.052  -13.197 -1.743  1.00 16.71 ? 85  VAL A CG1   1 
ATOM   640  C  CG2   . VAL A 1 105 ? -4.517  -11.486 -0.768  1.00 15.78 ? 85  VAL A CG2   1 
ATOM   641  N  N     . ILE A 1 106 ? -8.637  -10.848 -2.720  1.00 12.91 ? 86  ILE A N     1 
ATOM   642  C  CA    . ILE A 1 106 ? -9.878  -11.196 -3.410  1.00 12.77 ? 86  ILE A CA    1 
ATOM   643  C  C     . ILE A 1 106 ? -9.950  -10.521 -4.779  1.00 12.66 ? 86  ILE A C     1 
ATOM   644  O  O     . ILE A 1 106 ? -10.309 -11.152 -5.776  1.00 13.06 ? 86  ILE A O     1 
ATOM   645  C  CB    . ILE A 1 106 ? -11.112 -10.915 -2.534  1.00 13.31 ? 86  ILE A CB    1 
ATOM   646  C  CG1   . ILE A 1 106 ? -11.118 -11.841 -1.312  1.00 14.05 ? 86  ILE A CG1   1 
ATOM   647  C  CG2   . ILE A 1 106 ? -12.399 -11.109 -3.347  1.00 14.66 ? 86  ILE A CG2   1 
ATOM   648  C  CD1   . ILE A 1 106 ? -12.091 -11.423 -0.236  1.00 15.14 ? 86  ILE A CD1   1 
ATOM   649  N  N     . LEU A 1 107 ? -9.574  -9.247  -4.860  1.00 12.83 ? 87  LEU A N     1 
ATOM   650  C  CA    . LEU A 1 107 ? -9.590  -8.550  -6.141  1.00 12.41 ? 87  LEU A CA    1 
ATOM   651  C  C     . LEU A 1 107 ? -8.687  -9.250  -7.151  1.00 12.44 ? 87  LEU A C     1 
ATOM   652  O  O     . LEU A 1 107 ? -9.045  -9.401  -8.332  1.00 12.69 ? 87  LEU A O     1 
ATOM   653  C  CB    . LEU A 1 107 ? -9.150  -7.108  -5.914  1.00 13.29 ? 87  LEU A CB    1 
ATOM   654  C  CG    . LEU A 1 107 ? -9.134  -6.202  -7.145  1.00 14.96 ? 87  LEU A CG    1 
ATOM   655  C  CD1   . LEU A 1 107 ? -10.521 -5.954  -7.658  1.00 15.77 ? 87  LEU A CD1   1 
ATOM   656  C  CD2   . LEU A 1 107 ? -8.447  -4.885  -6.815  1.00 16.36 ? 87  LEU A CD2   1 
ATOM   657  N  N     . SER A 1 108 ? -7.493  -9.650  -6.721  1.00 12.56 ? 88  SER A N     1 
ATOM   658  C  CA    . SER A 1 108 ? -6.584  -10.340 -7.627  1.00 12.55 ? 88  SER A CA    1 
ATOM   659  C  C     . SER A 1 108 ? -7.146  -11.671 -8.097  1.00 12.30 ? 88  SER A C     1 
ATOM   660  O  O     . SER A 1 108 ? -6.892  -12.074 -9.231  1.00 13.56 ? 88  SER A O     1 
ATOM   661  C  CB    . SER A 1 108 ? -5.213  -10.532 -6.990  1.00 12.97 ? 88  SER A CB    1 
ATOM   662  O  OG    . SER A 1 108 ? -5.218  -11.504 -5.947  1.00 13.14 ? 88  SER A OG    1 
ATOM   663  N  N     . GLN A 1 109 ? -7.924  -12.359 -7.260  1.00 12.35 ? 89  GLN A N     1 
ATOM   664  C  CA    . GLN A 1 109 ? -8.495  -13.647 -7.640  1.00 12.34 ? 89  GLN A CA    1 
ATOM   665  C  C     . GLN A 1 109 ? -9.694  -13.484 -8.570  1.00 12.33 ? 89  GLN A C     1 
ATOM   666  O  O     . GLN A 1 109 ? -9.855  -14.266 -9.517  1.00 13.45 ? 89  GLN A O     1 
ATOM   667  C  CB    . GLN A 1 109 ? -8.856  -14.448 -6.386  1.00 12.70 ? 89  GLN A CB    1 
ATOM   668  C  CG    . GLN A 1 109 ? -7.617  -14.824 -5.555  1.00 13.32 ? 89  GLN A CG    1 
ATOM   669  C  CD    . GLN A 1 109 ? -6.702  -15.807 -6.267  1.00 13.38 ? 89  GLN A CD    1 
ATOM   670  O  OE1   . GLN A 1 109 ? -7.165  -16.657 -7.040  1.00 14.23 ? 89  GLN A OE1   1 
ATOM   671  N  NE2   . GLN A 1 109 ? -5.403  -15.702 -6.014  1.00 14.01 ? 89  GLN A NE2   1 
ATOM   672  N  N     . LEU A 1 110 ? -10.526 -12.463 -8.331  1.00 12.18 ? 90  LEU A N     1 
ATOM   673  C  CA    . LEU A 1 110 ? -11.594 -12.114 -9.262  1.00 12.27 ? 90  LEU A CA    1 
ATOM   674  C  C     . LEU A 1 110 ? -11.016 -11.890 -10.646 1.00 12.99 ? 90  LEU A C     1 
ATOM   675  O  O     . LEU A 1 110 ? -11.504 -12.439 -11.638 1.00 13.67 ? 90  LEU A O     1 
ATOM   676  C  CB    . LEU A 1 110 ? -12.314 -10.844 -8.807  1.00 13.48 ? 90  LEU A CB    1 
ATOM   677  C  CG    . LEU A 1 110 ? -13.268 -10.946 -7.626  1.00 13.62 ? 90  LEU A CG    1 
ATOM   678  C  CD1   . LEU A 1 110 ? -13.631 -9.568  -7.118  1.00 14.77 ? 90  LEU A CD1   1 
ATOM   679  C  CD2   . LEU A 1 110 ? -14.519 -11.723 -7.990  1.00 14.15 ? 90  LEU A CD2   1 
ATOM   680  N  N     . PHE A 1 111 ? -9.950  -11.112 -10.729 1.00 12.85 ? 91  PHE A N     1 
ATOM   681  C  CA    . PHE A 1 111 ? -9.380  -10.823 -12.036 1.00 13.34 ? 91  PHE A CA    1 
ATOM   682  C  C     . PHE A 1 111 ? -8.552  -11.971 -12.577 1.00 12.98 ? 91  PHE A C     1 
ATOM   683  O  O     . PHE A 1 111 ? -8.483  -12.135 -13.801 1.00 14.02 ? 91  PHE A O     1 
ATOM   684  C  CB    . PHE A 1 111 ? -8.658  -9.477  -12.037 1.00 15.87 ? 91  PHE A CB    1 
ATOM   685  C  CG    . PHE A 1 111 ? -9.601  -8.327  -12.208 1.00 20.18 ? 91  PHE A CG    1 
ATOM   686  C  CD1   . PHE A 1 111 ? -10.385 -8.231  -13.358 1.00 22.60 ? 91  PHE A CD1   1 
ATOM   687  C  CD2   . PHE A 1 111 ? -9.744  -7.369  -11.225 1.00 23.44 ? 91  PHE A CD2   1 
ATOM   688  C  CE1   . PHE A 1 111 ? -11.277 -7.212  -13.520 1.00 25.67 ? 91  PHE A CE1   1 
ATOM   689  C  CE2   . PHE A 1 111 ? -10.637 -6.331  -11.394 1.00 25.71 ? 91  PHE A CE2   1 
ATOM   690  C  CZ    . PHE A 1 111 ? -11.409 -6.256  -12.535 1.00 27.00 ? 91  PHE A CZ    1 
ATOM   691  N  N     . ARG A 1 112 ? -7.977  -12.815 -11.725 1.00 13.05 ? 92  ARG A N     1 
ATOM   692  C  CA    . ARG A 1 112 ? -7.324  -14.015 -12.235 1.00 13.23 ? 92  ARG A CA    1 
ATOM   693  C  C     . ARG A 1 112 ? -8.319  -14.861 -13.014 1.00 13.36 ? 92  ARG A C     1 
ATOM   694  O  O     . ARG A 1 112 ? -8.034  -15.301 -14.132 1.00 13.85 ? 92  ARG A O     1 
ATOM   695  C  CB    . ARG A 1 112 ? -6.698  -14.830 -11.099 1.00 13.94 ? 92  ARG A CB    1 
ATOM   696  C  CG    . ARG A 1 112 ? -6.075  -16.124 -11.621 1.00 15.46 ? 92  ARG A CG    1 
ATOM   697  C  CD    . ARG A 1 112 ? -5.296  -16.871 -10.574 1.00 16.50 ? 92  ARG A CD    1 
ATOM   698  N  NE    . ARG A 1 112 ? -6.067  -17.482 -9.501  1.00 15.93 ? 92  ARG A NE    1 
ATOM   699  C  CZ    . ARG A 1 112 ? -6.416  -18.767 -9.437  1.00 16.16 ? 92  ARG A CZ    1 
ATOM   700  N  NH1   . ARG A 1 112 ? -6.174  -19.598 -10.434 1.00 16.69 ? 92  ARG A NH1   1 
ATOM   701  N  NH2   . ARG A 1 112 ? -6.990  -19.229 -8.340  1.00 17.19 ? 92  ARG A NH2   1 
ATOM   702  N  N     . GLY A 1 113 ? -9.503  -15.089 -12.448 1.00 13.58 ? 93  GLY A N     1 
ATOM   703  C  CA    . GLY A 1 113 ? -10.489 -15.910 -13.131 1.00 13.24 ? 93  GLY A CA    1 
ATOM   704  C  C     . GLY A 1 113 ? -11.042 -15.247 -14.375 1.00 13.58 ? 93  GLY A C     1 
ATOM   705  O  O     . GLY A 1 113 ? -11.251 -15.910 -15.395 1.00 14.65 ? 93  GLY A O     1 
ATOM   706  N  N     . PHE A 1 114 ? -11.265 -13.933 -14.308 1.00 12.76 ? 94  PHE A N     1 
ATOM   707  C  CA    . PHE A 1 114 ? -11.724 -13.171 -15.469 1.00 13.48 ? 94  PHE A CA    1 
ATOM   708  C  C     . PHE A 1 114 ? -10.726 -13.299 -16.608 1.00 13.65 ? 94  PHE A C     1 
ATOM   709  O  O     . PHE A 1 114 ? -11.083 -13.646 -17.745 1.00 14.23 ? 94  PHE A O     1 
ATOM   710  C  CB    . PHE A 1 114 ? -11.892 -11.711 -15.018 1.00 13.75 ? 94  PHE A CB    1 
ATOM   711  C  CG    . PHE A 1 114 ? -12.378 -10.759 -16.079 1.00 13.79 ? 94  PHE A CG    1 
ATOM   712  C  CD1   . PHE A 1 114 ? -11.535 -10.329 -17.087 1.00 14.93 ? 94  PHE A CD1   1 
ATOM   713  C  CD2   . PHE A 1 114 ? -13.657 -10.245 -16.027 1.00 14.15 ? 94  PHE A CD2   1 
ATOM   714  C  CE1   . PHE A 1 114 ? -11.973 -9.442  -18.054 1.00 16.16 ? 94  PHE A CE1   1 
ATOM   715  C  CE2   . PHE A 1 114 ? -14.101 -9.340  -16.994 1.00 15.73 ? 94  PHE A CE2   1 
ATOM   716  C  CZ    . PHE A 1 114 ? -13.253 -8.948  -18.003 1.00 16.16 ? 94  PHE A CZ    1 
ATOM   717  N  N     . CYS A 1 115 ? -9.453  -13.055 -16.314 1.00 13.46 ? 95  CYS A N     1 
ATOM   718  C  CA    . CYS A 1 115 ? -8.440  -13.064 -17.363 1.00 13.73 ? 95  CYS A CA    1 
ATOM   719  C  C     . CYS A 1 115 ? -8.173  -14.476 -17.882 1.00 14.13 ? 95  CYS A C     1 
ATOM   720  O  O     . CYS A 1 115 ? -7.956  -14.670 -19.083 1.00 14.97 ? 95  CYS A O     1 
ATOM   721  C  CB    . CYS A 1 115 ? -7.168  -12.400 -16.852 1.00 14.72 ? 95  CYS A CB    1 
ATOM   722  S  SG    . CYS A 1 115 ? -7.324  -10.619 -16.521 1.00 15.55 ? 95  CYS A SG    1 
ATOM   723  N  N     . LYS A 1 116 ? -8.199  -15.482 -17.017 1.00 14.44 ? 96  LYS A N     1 
ATOM   724  C  CA    . LYS A 1 116 ? -8.026  -16.848 -17.492 1.00 15.34 ? 96  LYS A CA    1 
ATOM   725  C  C     . LYS A 1 116 ? -9.089  -17.195 -18.523 1.00 15.28 ? 96  LYS A C     1 
ATOM   726  O  O     . LYS A 1 116 ? -8.799  -17.855 -19.532 1.00 16.51 ? 96  LYS A O     1 
ATOM   727  C  CB    . LYS A 1 116 ? -8.072  -17.826 -16.320 1.00 15.96 ? 96  LYS A CB    1 
ATOM   728  C  CG    . LYS A 1 116 ? -7.946  -19.285 -16.713 1.00 19.56 ? 96  LYS A CG    1 
ATOM   729  C  CD    . LYS A 1 116 ? -6.629  -19.558 -17.404 1.00 23.17 ? 96  LYS A CD    1 
ATOM   730  C  CE    . LYS A 1 116 ? -6.430  -21.040 -17.626 1.00 27.10 ? 96  LYS A CE    1 
ATOM   731  N  NZ    . LYS A 1 116 ? -5.082  -21.326 -18.179 1.00 29.24 ? 96  LYS A NZ    1 
ATOM   732  N  N     . ASN A 1 117 ? -10.315 -16.713 -18.315 1.00 15.29 ? 97  ASN A N     1 
ATOM   733  C  CA    . ASN A 1 117 ? -11.415 -17.041 -19.212 1.00 15.67 ? 97  ASN A CA    1 
ATOM   734  C  C     . ASN A 1 117 ? -11.207 -16.520 -20.630 1.00 16.50 ? 97  ASN A C     1 
ATOM   735  O  O     . ASN A 1 117 ? -11.832 -17.047 -21.565 1.00 18.94 ? 97  ASN A O     1 
ATOM   736  C  CB    . ASN A 1 117 ? -12.708 -16.473 -18.644 1.00 16.39 ? 97  ASN A CB    1 
ATOM   737  C  CG    . ASN A 1 117 ? -13.908 -17.089 -19.268 1.00 18.18 ? 97  ASN A CG    1 
ATOM   738  O  OD1   . ASN A 1 117 ? -14.090 -18.299 -19.190 1.00 20.73 ? 97  ASN A OD1   1 
ATOM   739  N  ND2   . ASN A 1 117 ? -14.738 -16.273 -19.888 1.00 18.47 ? 97  ASN A ND2   1 
ATOM   740  N  N     . ILE A 1 118 ? -10.381 -15.488 -20.813 1.00 15.89 ? 98  ILE A N     1 
ATOM   741  C  CA    . ILE A 1 118 ? -10.169 -14.872 -22.120 1.00 16.92 ? 98  ILE A CA    1 
ATOM   742  C  C     . ILE A 1 118 ? -8.746  -15.042 -22.630 1.00 17.09 ? 98  ILE A C     1 
ATOM   743  O  O     . ILE A 1 118 ? -8.368  -14.389 -23.608 1.00 17.27 ? 98  ILE A O     1 
ATOM   744  C  CB    . ILE A 1 118 ? -10.551 -13.378 -22.111 1.00 18.84 ? 98  ILE A CB    1 
ATOM   745  C  CG1   . ILE A 1 118 ? -9.641  -12.596 -21.147 1.00 19.19 ? 98  ILE A CG1   1 
ATOM   746  C  CG2   . ILE A 1 118 ? -12.010 -13.208 -21.742 1.00 21.61 ? 98  ILE A CG2   1 
ATOM   747  C  CD1   . ILE A 1 118 ? -9.904  -11.121 -21.123 1.00 20.85 ? 98  ILE A CD1   1 
ATOM   748  N  N     . GLU A 1 119 ? -7.965  -15.940 -22.026 1.00 18.69 ? 99  GLU A N     1 
ATOM   749  C  CA    A GLU A 1 119 ? -6.532  -15.977 -22.294 0.50 20.94 ? 99  GLU A CA    1 
ATOM   750  C  CA    B GLU A 1 119 ? -6.530  -15.983 -22.290 0.50 20.87 ? 99  GLU A CA    1 
ATOM   751  C  C     . GLU A 1 119 ? -6.217  -16.225 -23.758 1.00 21.63 ? 99  GLU A C     1 
ATOM   752  O  O     . GLU A 1 119 ? -5.169  -15.791 -24.240 1.00 22.92 ? 99  GLU A O     1 
ATOM   753  C  CB    A GLU A 1 119 ? -5.872  -17.070 -21.463 0.50 22.75 ? 99  GLU A CB    1 
ATOM   754  C  CB    B GLU A 1 119 ? -5.865  -17.070 -21.437 0.50 22.43 ? 99  GLU A CB    1 
ATOM   755  C  CG    A GLU A 1 119 ? -5.181  -16.582 -20.221 0.50 24.84 ? 99  GLU A CG    1 
ATOM   756  C  CG    B GLU A 1 119 ? -6.426  -18.478 -21.666 0.50 24.03 ? 99  GLU A CG    1 
ATOM   757  C  CD    A GLU A 1 119 ? -4.423  -17.693 -19.532 0.50 25.92 ? 99  GLU A CD    1 
ATOM   758  C  CD    B GLU A 1 119 ? -5.648  -19.571 -20.947 0.50 26.88 ? 99  GLU A CD    1 
ATOM   759  O  OE1   A GLU A 1 119 ? -3.715  -17.413 -18.548 0.50 26.22 ? 99  GLU A OE1   1 
ATOM   760  O  OE1   B GLU A 1 119 ? -4.589  -19.280 -20.351 0.50 27.26 ? 99  GLU A OE1   1 
ATOM   761  O  OE2   A GLU A 1 119 ? -4.525  -18.851 -19.989 0.50 26.73 ? 99  GLU A OE2   1 
ATOM   762  O  OE2   B GLU A 1 119 ? -6.099  -20.737 -20.987 0.50 28.43 ? 99  GLU A OE2   1 
ATOM   763  N  N     . SER A 1 120 ? -7.086  -16.927 -24.472 1.00 21.80 ? 100 SER A N     1 
ATOM   764  C  CA    A SER A 1 120 ? -6.828  -17.286 -25.861 0.50 23.51 ? 100 SER A CA    1 
ATOM   765  C  CA    B SER A 1 120 ? -6.822  -17.279 -25.863 0.50 23.14 ? 100 SER A CA    1 
ATOM   766  C  C     . SER A 1 120 ? -7.505  -16.361 -26.864 1.00 23.27 ? 100 SER A C     1 
ATOM   767  O  O     . SER A 1 120 ? -7.417  -16.618 -28.067 1.00 24.58 ? 100 SER A O     1 
ATOM   768  C  CB    A SER A 1 120 ? -7.273  -18.726 -26.121 0.50 25.96 ? 100 SER A CB    1 
ATOM   769  C  CB    B SER A 1 120 ? -7.241  -18.725 -26.141 0.50 24.91 ? 100 SER A CB    1 
ATOM   770  O  OG    A SER A 1 120 ? -8.667  -18.862 -25.931 0.50 27.78 ? 100 SER A OG    1 
ATOM   771  O  OG    B SER A 1 120 ? -6.470  -19.628 -25.375 0.50 26.00 ? 100 SER A OG    1 
ATOM   772  N  N     . GLU A 1 121 ? -8.172  -15.307 -26.411 1.00 21.00 ? 101 GLU A N     1 
ATOM   773  C  CA    . GLU A 1 121 ? -8.904  -14.419 -27.297 1.00 20.63 ? 101 GLU A CA    1 
ATOM   774  C  C     . GLU A 1 121 ? -8.045  -13.223 -27.674 1.00 19.40 ? 101 GLU A C     1 
ATOM   775  O  O     . GLU A 1 121 ? -7.184  -12.794 -26.901 1.00 19.95 ? 101 GLU A O     1 
ATOM   776  C  CB    . GLU A 1 121 ? -10.159 -13.884 -26.607 1.00 22.28 ? 101 GLU A CB    1 
ATOM   777  C  CG    . GLU A 1 121 ? -11.050 -14.931 -25.993 1.00 26.40 ? 101 GLU A CG    1 
ATOM   778  C  CD    . GLU A 1 121 ? -11.522 -15.965 -26.979 1.00 31.07 ? 101 GLU A CD    1 
ATOM   779  O  OE1   . GLU A 1 121 ? -11.790 -15.619 -28.155 1.00 32.25 ? 101 GLU A OE1   1 
ATOM   780  O  OE2   . GLU A 1 121 ? -11.618 -17.137 -26.560 1.00 34.25 ? 101 GLU A OE2   1 
ATOM   781  N  N     . SER A 1 122 ? -8.308  -12.666 -28.861 1.00 19.53 ? 102 SER A N     1 
ATOM   782  C  CA    . SER A 1 122 ? -7.715  -11.385 -29.229 1.00 20.05 ? 102 SER A CA    1 
ATOM   783  C  C     . SER A 1 122 ? -8.645  -10.221 -28.909 1.00 18.42 ? 102 SER A C     1 
ATOM   784  O  O     . SER A 1 122 ? -8.168  -9.136  -28.570 1.00 17.94 ? 102 SER A O     1 
ATOM   785  C  CB    . SER A 1 122 ? -7.329  -11.368 -30.715 1.00 23.51 ? 102 SER A CB    1 
ATOM   786  O  OG    . SER A 1 122 ? -8.440  -11.704 -31.504 1.00 26.12 ? 102 SER A OG    1 
ATOM   787  N  N     . GLU A 1 123 ? -9.961  -10.428 -29.009 1.00 18.82 ? 103 GLU A N     1 
ATOM   788  C  CA    . GLU A 1 123 ? -10.967 -9.461  -28.590 1.00 19.71 ? 103 GLU A CA    1 
ATOM   789  C  C     . GLU A 1 123 ? -12.140 -10.246 -28.023 1.00 18.92 ? 103 GLU A C     1 
ATOM   790  O  O     . GLU A 1 123 ? -12.305 -11.430 -28.316 1.00 20.67 ? 103 GLU A O     1 
ATOM   791  C  CB    . GLU A 1 123 ? -11.500 -8.599  -29.747 1.00 24.45 ? 103 GLU A CB    1 
ATOM   792  C  CG    . GLU A 1 123 ? -10.441 -7.997  -30.631 1.00 30.14 ? 103 GLU A CG    1 
ATOM   793  C  CD    . GLU A 1 123 ? -10.113 -8.872  -31.827 1.00 34.34 ? 103 GLU A CD    1 
ATOM   794  O  OE1   . GLU A 1 123 ? -11.054 -9.414  -32.459 1.00 36.83 ? 103 GLU A OE1   1 
ATOM   795  O  OE2   . GLU A 1 123 ? -8.912  -9.025  -32.135 1.00 34.67 ? 103 GLU A OE2   1 
ATOM   796  N  N     . ILE A 1 124 ? -12.965 -9.582  -27.216 1.00 17.26 ? 104 ILE A N     1 
ATOM   797  C  CA    . ILE A 1 124 ? -14.159 -10.221 -26.671 1.00 17.46 ? 104 ILE A CA    1 
ATOM   798  C  C     . ILE A 1 124 ? -15.407 -9.392  -26.950 1.00 17.68 ? 104 ILE A C     1 
ATOM   799  O  O     . ILE A 1 124 ? -15.350 -8.167  -27.083 1.00 19.10 ? 104 ILE A O     1 
ATOM   800  C  CB    . ILE A 1 124 ? -14.043 -10.531 -25.164 1.00 17.67 ? 104 ILE A CB    1 
ATOM   801  C  CG1   . ILE A 1 124 ? -13.971 -9.240  -24.329 1.00 17.31 ? 104 ILE A CG1   1 
ATOM   802  C  CG2   . ILE A 1 124 ? -12.835 -11.425 -24.912 1.00 19.04 ? 104 ILE A CG2   1 
ATOM   803  C  CD1   . ILE A 1 124 ? -13.981 -9.473  -22.808 1.00 18.08 ? 104 ILE A CD1   1 
ATOM   804  N  N     . ASN A 1 125 ? -16.545 -10.081 -27.023 1.00 18.15 ? 105 ASN A N     1 
ATOM   805  C  CA    . ASN A 1 125 ? -17.849 -9.459  -27.176 1.00 17.63 ? 105 ASN A CA    1 
ATOM   806  C  C     . ASN A 1 125 ? -18.534 -9.369  -25.806 1.00 16.20 ? 105 ASN A C     1 
ATOM   807  O  O     . ASN A 1 125 ? -17.984 -9.756  -24.767 1.00 16.54 ? 105 ASN A O     1 
ATOM   808  C  CB    . ASN A 1 125 ? -18.690 -10.199 -28.229 1.00 18.55 ? 105 ASN A CB    1 
ATOM   809  C  CG    . ASN A 1 125 ? -19.037 -11.623 -27.825 1.00 20.74 ? 105 ASN A CG    1 
ATOM   810  O  OD1   . ASN A 1 125 ? -18.838 -12.020 -26.689 1.00 21.22 ? 105 ASN A OD1   1 
ATOM   811  N  ND2   . ASN A 1 125 ? -19.558 -12.397 -28.754 1.00 23.36 ? 105 ASN A ND2   1 
ATOM   812  N  N     . SER A 1 126 ? -19.762 -8.859  -25.804 1.00 16.83 ? 106 SER A N     1 
ATOM   813  C  CA    . SER A 1 126 ? -20.463 -8.622  -24.545 1.00 17.13 ? 106 SER A CA    1 
ATOM   814  C  C     . SER A 1 126 ? -20.761 -9.927  -23.813 1.00 16.67 ? 106 SER A C     1 
ATOM   815  O  O     . SER A 1 126 ? -20.717 -9.974  -22.578 1.00 15.66 ? 106 SER A O     1 
ATOM   816  C  CB    . SER A 1 126 ? -21.752 -7.844  -24.820 1.00 19.12 ? 106 SER A CB    1 
ATOM   817  O  OG    . SER A 1 126 ? -22.629 -8.593  -25.640 1.00 20.36 ? 106 SER A OG    1 
ATOM   818  N  N     . LYS A 1 127 ? -21.072 -10.998 -24.543 1.00 16.98 ? 107 LYS A N     1 
ATOM   819  C  CA    . LYS A 1 127 ? -21.356 -12.270 -23.888 1.00 18.07 ? 107 LYS A CA    1 
ATOM   820  C  C     . LYS A 1 127 ? -20.112 -12.823 -23.215 1.00 16.87 ? 107 LYS A C     1 
ATOM   821  O  O     . LYS A 1 127 ? -20.176 -13.314 -22.079 1.00 16.75 ? 107 LYS A O     1 
ATOM   822  C  CB    . LYS A 1 127 ? -21.915 -13.261 -24.899 1.00 20.21 ? 107 LYS A CB    1 
ATOM   823  C  CG    . LYS A 1 127 ? -23.388 -13.019 -25.185 1.00 23.31 ? 107 LYS A CG    1 
ATOM   824  N  N     . LEU A 1 128 ? -18.958 -12.729 -23.871 1.00 16.15 ? 108 LEU A N     1 
ATOM   825  C  CA    A LEU A 1 128 ? -17.735 -13.212 -23.238 0.50 16.31 ? 108 LEU A CA    1 
ATOM   826  C  CA    B LEU A 1 128 ? -17.730 -13.205 -23.241 0.50 16.81 ? 108 LEU A CA    1 
ATOM   827  C  C     . LEU A 1 128 ? -17.303 -12.300 -22.092 1.00 16.16 ? 108 LEU A C     1 
ATOM   828  O  O     . LEU A 1 128 ? -16.736 -12.778 -21.100 1.00 16.72 ? 108 LEU A O     1 
ATOM   829  C  CB    A LEU A 1 128 ? -16.632 -13.387 -24.286 0.50 17.78 ? 108 LEU A CB    1 
ATOM   830  C  CB    B LEU A 1 128 ? -16.606 -13.335 -24.270 0.50 19.28 ? 108 LEU A CB    1 
ATOM   831  C  CG    A LEU A 1 128 ? -15.364 -14.113 -23.823 0.50 19.83 ? 108 LEU A CG    1 
ATOM   832  C  CG    B LEU A 1 128 ? -16.639 -14.524 -25.235 0.50 22.35 ? 108 LEU A CG    1 
ATOM   833  C  CD1   A LEU A 1 128 ? -15.692 -15.348 -22.992 0.50 19.98 ? 108 LEU A CD1   1 
ATOM   834  C  CD1   B LEU A 1 128 ? -15.213 -14.984 -25.523 0.50 23.74 ? 108 LEU A CD1   1 
ATOM   835  C  CD2   A LEU A 1 128 ? -14.515 -14.506 -25.015 0.50 21.33 ? 108 LEU A CD2   1 
ATOM   836  C  CD2   B LEU A 1 128 ? -17.477 -15.683 -24.730 0.50 23.55 ? 108 LEU A CD2   1 
ATOM   837  N  N     . LEU A 1 129 ? -17.582 -10.995 -22.188 1.00 15.52 ? 109 LEU A N     1 
ATOM   838  C  CA    . LEU A 1 129 ? -17.332 -10.107 -21.055 1.00 15.24 ? 109 LEU A CA    1 
ATOM   839  C  C     . LEU A 1 129 ? -18.126 -10.571 -19.840 1.00 14.44 ? 109 LEU A C     1 
ATOM   840  O  O     . LEU A 1 129 ? -17.575 -10.715 -18.738 1.00 14.83 ? 109 LEU A O     1 
ATOM   841  C  CB    . LEU A 1 129 ? -17.703 -8.669  -21.431 1.00 15.29 ? 109 LEU A CB    1 
ATOM   842  C  CG    . LEU A 1 129 ? -17.560 -7.616  -20.321 1.00 15.57 ? 109 LEU A CG    1 
ATOM   843  C  CD1   . LEU A 1 129 ? -16.149 -7.560  -19.783 1.00 16.13 ? 109 LEU A CD1   1 
ATOM   844  C  CD2   . LEU A 1 129 ? -17.961 -6.251  -20.797 1.00 17.21 ? 109 LEU A CD2   1 
ATOM   845  N  N     . ALA A 1 130 ? -19.423 -10.822 -20.024 1.00 14.74 ? 110 ALA A N     1 
ATOM   846  C  CA    . ALA A 1 130 ? -20.265 -11.279 -18.922 1.00 14.45 ? 110 ALA A CA    1 
ATOM   847  C  C     . ALA A 1 130 ? -19.772 -12.607 -18.368 1.00 14.71 ? 110 ALA A C     1 
ATOM   848  O  O     . ALA A 1 130 ? -19.706 -12.801 -17.147 1.00 14.65 ? 110 ALA A O     1 
ATOM   849  C  CB    . ALA A 1 130 ? -21.711 -11.396 -19.407 1.00 15.10 ? 110 ALA A CB    1 
ATOM   850  N  N     . GLU A 1 131 ? -19.432 -13.543 -19.247 1.00 15.19 ? 111 GLU A N     1 
ATOM   851  C  CA    . GLU A 1 131 ? -18.952 -14.843 -18.800 1.00 16.92 ? 111 GLU A CA    1 
ATOM   852  C  C     . GLU A 1 131 ? -17.657 -14.719 -18.019 1.00 15.18 ? 111 GLU A C     1 
ATOM   853  O  O     . GLU A 1 131 ? -17.391 -15.528 -17.127 1.00 15.21 ? 111 GLU A O     1 
ATOM   854  C  CB    . GLU A 1 131 ? -18.736 -15.708 -20.037 1.00 21.15 ? 111 GLU A CB    1 
ATOM   855  C  CG    . GLU A 1 131 ? -18.249 -17.117 -19.808 1.00 26.85 ? 111 GLU A CG    1 
ATOM   856  C  CD    . GLU A 1 131 ? -17.894 -17.778 -21.134 1.00 30.12 ? 111 GLU A CD    1 
ATOM   857  O  OE1   . GLU A 1 131 ? -16.692 -17.839 -21.467 1.00 28.95 ? 111 GLU A OE1   1 
ATOM   858  O  OE2   . GLU A 1 131 ? -18.820 -18.180 -21.878 1.00 33.39 ? 111 GLU A OE2   1 
ATOM   859  N  N     . SER A 1 132 ? -16.831 -13.732 -18.355 1.00 14.40 ? 112 SER A N     1 
ATOM   860  C  CA    . SER A 1 132 ? -15.557 -13.548 -17.673 1.00 14.68 ? 112 SER A CA    1 
ATOM   861  C  C     . SER A 1 132 ? -15.760 -12.989 -16.268 1.00 13.67 ? 112 SER A C     1 
ATOM   862  O  O     . SER A 1 132 ? -15.064 -13.396 -15.330 1.00 13.45 ? 112 SER A O     1 
ATOM   863  C  CB    . SER A 1 132 ? -14.639 -12.673 -18.529 1.00 15.79 ? 112 SER A CB    1 
ATOM   864  O  OG    . SER A 1 132 ? -14.385 -13.315 -19.781 1.00 16.97 ? 112 SER A OG    1 
ATOM   865  N  N     . PHE A 1 133 ? -16.722 -12.080 -16.099 1.00 13.19 ? 113 PHE A N     1 
ATOM   866  C  CA    . PHE A 1 133 ? -17.091 -11.672 -14.746 1.00 13.14 ? 113 PHE A CA    1 
ATOM   867  C  C     . PHE A 1 133 ? -17.539 -12.879 -13.930 1.00 13.59 ? 113 PHE A C     1 
ATOM   868  O  O     . PHE A 1 133 ? -17.128 -13.048 -12.776 1.00 13.42 ? 113 PHE A O     1 
ATOM   869  C  CB    . PHE A 1 133 ? -18.178 -10.594 -14.765 1.00 13.97 ? 113 PHE A CB    1 
ATOM   870  C  CG    . PHE A 1 133 ? -17.682 -9.210  -15.117 1.00 14.55 ? 113 PHE A CG    1 
ATOM   871  C  CD1   . PHE A 1 133 ? -16.736 -8.568  -14.325 1.00 15.94 ? 113 PHE A CD1   1 
ATOM   872  C  CD2   . PHE A 1 133 ? -18.196 -8.536  -16.211 1.00 14.28 ? 113 PHE A CD2   1 
ATOM   873  C  CE1   . PHE A 1 133 ? -16.313 -7.298  -14.632 1.00 16.12 ? 113 PHE A CE1   1 
ATOM   874  C  CE2   . PHE A 1 133 ? -17.779 -7.267  -16.509 1.00 15.16 ? 113 PHE A CE2   1 
ATOM   875  C  CZ    . PHE A 1 133 ? -16.831 -6.647  -15.733 1.00 15.42 ? 113 PHE A CZ    1 
ATOM   876  N  N     . GLN A 1 134 ? -18.387 -13.735 -14.509 1.00 14.22 ? 114 GLN A N     1 
ATOM   877  C  CA    . GLN A 1 134 ? -18.823 -14.923 -13.785 1.00 14.00 ? 114 GLN A CA    1 
ATOM   878  C  C     . GLN A 1 134 ? -17.643 -15.828 -13.440 1.00 12.99 ? 114 GLN A C     1 
ATOM   879  O  O     . GLN A 1 134 ? -17.562 -16.364 -12.325 1.00 13.95 ? 114 GLN A O     1 
ATOM   880  C  CB    . GLN A 1 134 ? -19.883 -15.673 -14.609 1.00 15.84 ? 114 GLN A CB    1 
ATOM   881  C  CG    . GLN A 1 134 ? -20.433 -16.911 -13.921 1.00 20.27 ? 114 GLN A CG    1 
ATOM   882  C  CD    . GLN A 1 134 ? -20.972 -16.620 -12.530 1.00 27.23 ? 114 GLN A CD    1 
ATOM   883  O  OE1   . GLN A 1 134 ? -21.603 -15.581 -12.299 1.00 29.90 ? 114 GLN A OE1   1 
ATOM   884  N  NE2   . GLN A 1 134 ? -20.711 -17.529 -11.588 1.00 30.39 ? 114 GLN A NE2   1 
ATOM   885  N  N     . ALA A 1 135 ? -16.724 -16.035 -14.386 1.00 13.62 ? 115 ALA A N     1 
ATOM   886  C  CA    . ALA A 1 135 ? -15.565 -16.882 -14.117 1.00 14.08 ? 115 ALA A CA    1 
ATOM   887  C  C     . ALA A 1 135 ? -14.742 -16.319 -12.964 1.00 13.44 ? 115 ALA A C     1 
ATOM   888  O  O     . ALA A 1 135 ? -14.216 -17.071 -12.141 1.00 14.69 ? 115 ALA A O     1 
ATOM   889  C  CB    . ALA A 1 135 ? -14.716 -17.022 -15.385 1.00 15.59 ? 115 ALA A CB    1 
ATOM   890  N  N     . GLY A 1 136 ? -14.615 -14.995 -12.899 1.00 13.21 ? 116 GLY A N     1 
ATOM   891  C  CA    . GLY A 1 136 ? -13.902 -14.383 -11.792 1.00 13.28 ? 116 GLY A CA    1 
ATOM   892  C  C     . GLY A 1 136 ? -14.560 -14.654 -10.451 1.00 12.61 ? 116 GLY A C     1 
ATOM   893  O  O     . GLY A 1 136 ? -13.882 -14.925 -9.456  1.00 12.93 ? 116 GLY A O     1 
ATOM   894  N  N     . VAL A 1 137 ? -15.891 -14.554 -10.401 1.00 12.52 ? 117 VAL A N     1 
ATOM   895  C  CA    . VAL A 1 137 ? -16.627 -14.856 -9.173  1.00 13.30 ? 117 VAL A CA    1 
ATOM   896  C  C     . VAL A 1 137 ? -16.345 -16.276 -8.719  1.00 13.34 ? 117 VAL A C     1 
ATOM   897  O  O     . VAL A 1 137 ? -16.091 -16.526 -7.535  1.00 14.26 ? 117 VAL A O     1 
ATOM   898  C  CB    . VAL A 1 137 ? -18.134 -14.625 -9.384  1.00 14.28 ? 117 VAL A CB    1 
ATOM   899  C  CG1   . VAL A 1 137 ? -18.948 -15.169 -8.201  1.00 15.08 ? 117 VAL A CG1   1 
ATOM   900  C  CG2   . VAL A 1 137 ? -18.421 -13.164 -9.604  1.00 15.34 ? 117 VAL A CG2   1 
ATOM   901  N  N     . GLU A 1 138 ? -16.398 -17.232 -9.642  1.00 13.57 ? 118 GLU A N     1 
ATOM   902  C  CA    . GLU A 1 138 ? -16.139 -18.619 -9.280  1.00 15.47 ? 118 GLU A CA    1 
ATOM   903  C  C     . GLU A 1 138 ? -14.744 -18.786 -8.691  1.00 14.59 ? 118 GLU A C     1 
ATOM   904  O  O     . GLU A 1 138 ? -14.560 -19.454 -7.664  1.00 15.29 ? 118 GLU A O     1 
ATOM   905  C  CB    . GLU A 1 138 ? -16.308 -19.507 -10.505 1.00 18.92 ? 118 GLU A CB    1 
ATOM   906  C  CG    . GLU A 1 138 ? -17.741 -19.641 -10.968 1.00 26.48 ? 118 GLU A CG    1 
ATOM   907  C  CD    . GLU A 1 138 ? -18.426 -20.856 -10.377 1.00 33.96 ? 118 GLU A CD    1 
ATOM   908  O  OE1   . GLU A 1 138 ? -17.919 -21.391 -9.370  1.00 37.39 ? 118 GLU A OE1   1 
ATOM   909  O  OE2   . GLU A 1 138 ? -19.469 -21.274 -10.926 1.00 37.05 ? 118 GLU A OE2   1 
ATOM   910  N  N     . THR A 1 139 ? -13.742 -18.174 -9.322  1.00 13.79 ? 119 THR A N     1 
ATOM   911  C  CA    . THR A 1 139 ? -12.376 -18.285 -8.823  1.00 13.81 ? 119 THR A CA    1 
ATOM   912  C  C     . THR A 1 139 ? -12.251 -17.668 -7.434  1.00 13.93 ? 119 THR A C     1 
ATOM   913  O  O     . THR A 1 139 ? -11.631 -18.247 -6.534  1.00 14.00 ? 119 THR A O     1 
ATOM   914  C  CB    . THR A 1 139 ? -11.425 -17.612 -9.819  1.00 14.03 ? 119 THR A CB    1 
ATOM   915  O  OG1   . THR A 1 139 ? -11.529 -18.273 -11.090 1.00 15.77 ? 119 THR A OG1   1 
ATOM   916  C  CG2   . THR A 1 139 ? -9.986  -17.679 -9.356  1.00 14.13 ? 119 THR A CG2   1 
ATOM   917  N  N     . ALA A 1 140 ? -12.857 -16.503 -7.226  1.00 13.11 ? 120 ALA A N     1 
ATOM   918  C  CA    . ALA A 1 140 ? -12.710 -15.824 -5.943  1.00 13.54 ? 120 ALA A CA    1 
ATOM   919  C  C     . ALA A 1 140 ? -13.394 -16.590 -4.817  1.00 13.86 ? 120 ALA A C     1 
ATOM   920  O  O     . ALA A 1 140 ? -12.838 -16.712 -3.716  1.00 14.20 ? 120 ALA A O     1 
ATOM   921  C  CB    . ALA A 1 140 ? -13.257 -14.405 -6.044  1.00 14.68 ? 120 ALA A CB    1 
ATOM   922  N  N     . TYR A 1 141 ? -14.606 -17.092 -5.050  1.00 14.02 ? 121 TYR A N     1 
ATOM   923  C  CA    . TYR A 1 141 ? -15.259 -17.877 -4.005  1.00 14.32 ? 121 TYR A CA    1 
ATOM   924  C  C     . TYR A 1 141 ? -14.454 -19.120 -3.663  1.00 14.67 ? 121 TYR A C     1 
ATOM   925  O  O     . TYR A 1 141 ? -14.346 -19.490 -2.487  1.00 16.59 ? 121 TYR A O     1 
ATOM   926  C  CB    . TYR A 1 141 ? -16.692 -18.260 -4.387  1.00 14.40 ? 121 TYR A CB    1 
ATOM   927  C  CG    . TYR A 1 141 ? -17.752 -17.286 -3.959  1.00 14.85 ? 121 TYR A CG    1 
ATOM   928  C  CD1   . TYR A 1 141 ? -18.103 -16.213 -4.756  1.00 15.15 ? 121 TYR A CD1   1 
ATOM   929  C  CD2   . TYR A 1 141 ? -18.403 -17.436 -2.742  1.00 16.29 ? 121 TYR A CD2   1 
ATOM   930  C  CE1   . TYR A 1 141 ? -19.080 -15.320 -4.361  1.00 15.89 ? 121 TYR A CE1   1 
ATOM   931  C  CE2   . TYR A 1 141 ? -19.386 -16.544 -2.334  1.00 16.48 ? 121 TYR A CE2   1 
ATOM   932  C  CZ    . TYR A 1 141 ? -19.725 -15.491 -3.162  1.00 15.55 ? 121 TYR A CZ    1 
ATOM   933  O  OH    . TYR A 1 141 ? -20.692 -14.574 -2.814  1.00 16.33 ? 121 TYR A OH    1 
ATOM   934  N  N     . LYS A 1 142 ? -13.882 -19.787 -4.672  1.00 15.05 ? 122 LYS A N     1 
ATOM   935  C  CA    . LYS A 1 142 ? -13.097 -20.987 -4.396  1.00 15.86 ? 122 LYS A CA    1 
ATOM   936  C  C     . LYS A 1 142 ? -11.818 -20.665 -3.630  1.00 15.36 ? 122 LYS A C     1 
ATOM   937  O  O     . LYS A 1 142 ? -11.307 -21.520 -2.905  1.00 17.16 ? 122 LYS A O     1 
ATOM   938  C  CB    . LYS A 1 142 ? -12.756 -21.712 -5.697  1.00 17.45 ? 122 LYS A CB    1 
ATOM   939  C  CG    . LYS A 1 142 ? -13.939 -22.407 -6.381  1.00 19.94 ? 122 LYS A CG    1 
ATOM   940  C  CD    . LYS A 1 142 ? -13.543 -22.971 -7.752  1.00 22.40 ? 122 LYS A CD    1 
ATOM   941  N  N     . ALA A 1 143 ? -11.293 -19.447 -3.772  1.00 14.73 ? 123 ALA A N     1 
ATOM   942  C  CA    . ALA A 1 143 ? -10.048 -19.043 -3.134  1.00 15.52 ? 123 ALA A CA    1 
ATOM   943  C  C     . ALA A 1 143 ? -10.219 -18.707 -1.656  1.00 15.72 ? 123 ALA A C     1 
ATOM   944  O  O     . ALA A 1 143 ? -9.245  -18.780 -0.892  1.00 16.49 ? 123 ALA A O     1 
ATOM   945  C  CB    . ALA A 1 143 ? -9.509  -17.802 -3.838  1.00 15.70 ? 123 ALA A CB    1 
ATOM   946  N  N     . VAL A 1 144 ? -11.419 -18.336 -1.243  1.00 15.88 ? 124 VAL A N     1 
ATOM   947  C  CA    . VAL A 1 144 ? -11.704 -17.875 0.111   1.00 15.55 ? 124 VAL A CA    1 
ATOM   948  C  C     . VAL A 1 144 ? -12.219 -19.064 0.906   1.00 16.53 ? 124 VAL A C     1 
ATOM   949  O  O     . VAL A 1 144 ? -13.271 -19.631 0.587   1.00 18.05 ? 124 VAL A O     1 
ATOM   950  C  CB    . VAL A 1 144 ? -12.727 -16.728 0.105   1.00 15.18 ? 124 VAL A CB    1 
ATOM   951  C  CG1   . VAL A 1 144 ? -13.078 -16.343 1.537   1.00 15.63 ? 124 VAL A CG1   1 
ATOM   952  C  CG2   . VAL A 1 144 ? -12.183 -15.514 -0.640  1.00 15.41 ? 124 VAL A CG2   1 
ATOM   953  N  N     . MET A 1 145 ? -11.506 -19.424 1.972   1.00 16.69 ? 125 MET A N     1 
ATOM   954  C  CA    . MET A 1 145 ? -11.865 -20.644 2.683   1.00 18.27 ? 125 MET A CA    1 
ATOM   955  C  C     . MET A 1 145 ? -13.202 -20.517 3.390   1.00 20.04 ? 125 MET A C     1 
ATOM   956  O  O     . MET A 1 145 ? -13.964 -21.489 3.463   1.00 21.96 ? 125 MET A O     1 
ATOM   957  C  CB    . MET A 1 145 ? -10.773 -20.998 3.683   1.00 18.59 ? 125 MET A CB    1 
ATOM   958  C  CG    . MET A 1 145 ? -9.572  -21.628 3.011   1.00 20.80 ? 125 MET A CG    1 
ATOM   959  S  SD    . MET A 1 145 ? -8.262  -22.112 4.132   1.00 23.65 ? 125 MET A SD    1 
ATOM   960  C  CE    . MET A 1 145 ? -7.707  -20.517 4.713   1.00 25.01 ? 125 MET A CE    1 
ATOM   961  N  N     . LYS A 1 146 ? -13.493 -19.347 3.948   1.00 18.68 ? 126 LYS A N     1 
ATOM   962  C  CA    . LYS A 1 146 ? -14.726 -19.109 4.696   1.00 20.24 ? 126 LYS A CA    1 
ATOM   963  C  C     . LYS A 1 146 ? -15.376 -17.846 4.152   1.00 19.94 ? 126 LYS A C     1 
ATOM   964  O  O     . LYS A 1 146 ? -15.308 -16.781 4.779   1.00 19.75 ? 126 LYS A O     1 
ATOM   965  C  CB    . LYS A 1 146 ? -14.433 -18.954 6.189   1.00 23.69 ? 126 LYS A CB    1 
ATOM   966  C  CG    . LYS A 1 146 ? -13.659 -20.102 6.855   1.00 28.46 ? 126 LYS A CG    1 
ATOM   967  C  CD    . LYS A 1 146 ? -14.567 -21.103 7.512   1.00 32.21 ? 126 LYS A CD    1 
ATOM   968  C  CE    . LYS A 1 146 ? -13.767 -22.057 8.376   1.00 35.30 ? 126 LYS A CE    1 
ATOM   969  N  NZ    . LYS A 1 146 ? -13.716 -21.630 9.819   1.00 37.91 ? 126 LYS A NZ    1 
ATOM   970  N  N     . PRO A 1 147 ? -16.027 -17.932 2.993   1.00 18.73 ? 127 PRO A N     1 
ATOM   971  C  CA    . PRO A 1 147 ? -16.659 -16.740 2.417   1.00 17.82 ? 127 PRO A CA    1 
ATOM   972  C  C     . PRO A 1 147 ? -17.770 -16.213 3.316   1.00 16.74 ? 127 PRO A C     1 
ATOM   973  O  O     . PRO A 1 147 ? -18.505 -16.978 3.942   1.00 19.28 ? 127 PRO A O     1 
ATOM   974  C  CB    . PRO A 1 147 ? -17.222 -17.245 1.083   1.00 19.85 ? 127 PRO A CB    1 
ATOM   975  C  CG    . PRO A 1 147 ? -16.499 -18.510 0.769   1.00 20.98 ? 127 PRO A CG    1 
ATOM   976  C  CD    . PRO A 1 147 ? -16.120 -19.106 2.103   1.00 20.84 ? 127 PRO A CD    1 
ATOM   977  N  N     . VAL A 1 148 ? -17.888 -14.891 3.362   1.00 14.95 ? 128 VAL A N     1 
ATOM   978  C  CA    . VAL A 1 148 ? -18.938 -14.192 4.095   1.00 15.26 ? 128 VAL A CA    1 
ATOM   979  C  C     . VAL A 1 148 ? -19.697 -13.294 3.124   1.00 13.97 ? 128 VAL A C     1 
ATOM   980  O  O     . VAL A 1 148 ? -19.088 -12.624 2.286   1.00 14.55 ? 128 VAL A O     1 
ATOM   981  C  CB    . VAL A 1 148 ? -18.304 -13.383 5.246   1.00 17.05 ? 128 VAL A CB    1 
ATOM   982  C  CG1   . VAL A 1 148 ? -19.325 -12.461 5.906   1.00 17.80 ? 128 VAL A CG1   1 
ATOM   983  C  CG2   . VAL A 1 148 ? -17.708 -14.338 6.265   1.00 18.34 ? 128 VAL A CG2   1 
ATOM   984  N  N     . GLU A 1 149 ? -21.028 -13.293 3.224   1.00 13.58 ? 129 GLU A N     1 
ATOM   985  C  CA    . GLU A 1 149 ? -21.884 -12.472 2.383   1.00 13.53 ? 129 GLU A CA    1 
ATOM   986  C  C     . GLU A 1 149 ? -22.018 -11.057 2.946   1.00 13.27 ? 129 GLU A C     1 
ATOM   987  O  O     . GLU A 1 149 ? -21.802 -10.800 4.138   1.00 14.40 ? 129 GLU A O     1 
ATOM   988  C  CB    . GLU A 1 149 ? -23.255 -13.114 2.215   1.00 14.98 ? 129 GLU A CB    1 
ATOM   989  C  CG    . GLU A 1 149 ? -23.200 -14.451 1.487   1.00 16.23 ? 129 GLU A CG    1 
ATOM   990  C  CD    . GLU A 1 149 ? -22.699 -14.344 0.050   1.00 18.55 ? 129 GLU A CD    1 
ATOM   991  O  OE1   . GLU A 1 149 ? -23.126 -13.418 -0.685  1.00 19.00 ? 129 GLU A OE1   1 
ATOM   992  O  OE2   . GLU A 1 149 ? -21.862 -15.181 -0.349  1.00 19.38 ? 129 GLU A OE2   1 
ATOM   993  N  N     . GLY A 1 150 ? -22.400 -10.134 2.066   1.00 12.94 ? 130 GLY A N     1 
ATOM   994  C  CA    . GLY A 1 150 ? -22.378 -8.723  2.378   1.00 12.90 ? 130 GLY A CA    1 
ATOM   995  C  C     . GLY A 1 150 ? -21.061 -8.061  2.079   1.00 13.16 ? 130 GLY A C     1 
ATOM   996  O  O     . GLY A 1 150 ? -20.754 -7.015  2.663   1.00 13.47 ? 130 GLY A O     1 
ATOM   997  N  N     . THR A 1 151 ? -20.280 -8.634  1.168   1.00 13.07 ? 131 THR A N     1 
ATOM   998  C  CA    . THR A 1 151 ? -18.892 -8.270  0.973   1.00 12.94 ? 131 THR A CA    1 
ATOM   999  C  C     . THR A 1 151 ? -18.602 -8.064  -0.514  1.00 12.50 ? 131 THR A C     1 
ATOM   1000 O  O     . THR A 1 151 ? -19.503 -8.107  -1.369  1.00 12.64 ? 131 THR A O     1 
ATOM   1001 C  CB    . THR A 1 151 ? -18.014 -9.419  1.464   1.00 13.66 ? 131 THR A CB    1 
ATOM   1002 O  OG1   . THR A 1 151 ? -18.363 -10.569 0.674   1.00 13.47 ? 131 THR A OG1   1 
ATOM   1003 C  CG2   . THR A 1 151 ? -18.204 -9.687  2.958   1.00 14.23 ? 131 THR A CG2   1 
ATOM   1004 N  N     . ILE A 1 152 ? -17.321 -7.891  -0.839  1.00 12.25 ? 132 ILE A N     1 
ATOM   1005 C  CA    . ILE A 1 152 ? -16.917 -7.781  -2.236  1.00 11.81 ? 132 ILE A CA    1 
ATOM   1006 C  C     . ILE A 1 152 ? -17.353 -9.014  -3.012  1.00 11.96 ? 132 ILE A C     1 
ATOM   1007 O  O     . ILE A 1 152 ? -17.636 -8.927  -4.214  1.00 12.46 ? 132 ILE A O     1 
ATOM   1008 C  CB    . ILE A 1 152 ? -15.392 -7.546  -2.291  1.00 12.48 ? 132 ILE A CB    1 
ATOM   1009 C  CG1   . ILE A 1 152 ? -14.935 -7.210  -3.711  1.00 13.53 ? 132 ILE A CG1   1 
ATOM   1010 C  CG2   . ILE A 1 152 ? -14.634 -8.731  -1.729  1.00 13.35 ? 132 ILE A CG2   1 
ATOM   1011 C  CD1   . ILE A 1 152 ? -13.466 -6.833  -3.805  1.00 14.35 ? 132 ILE A CD1   1 
ATOM   1012 N  N     . LEU A 1 153 ? -17.364 -10.187 -2.376  1.00 12.21 ? 133 LEU A N     1 
ATOM   1013 C  CA    . LEU A 1 153 ? -17.799 -11.392 -3.086  1.00 12.27 ? 133 LEU A CA    1 
ATOM   1014 C  C     . LEU A 1 153 ? -19.256 -11.287 -3.509  1.00 12.52 ? 133 LEU A C     1 
ATOM   1015 O  O     . LEU A 1 153 ? -19.610 -11.636 -4.645  1.00 12.84 ? 133 LEU A O     1 
ATOM   1016 C  CB    . LEU A 1 153 ? -17.604 -12.637 -2.224  1.00 13.36 ? 133 LEU A CB    1 
ATOM   1017 C  CG    . LEU A 1 153 ? -16.180 -13.107 -1.976  1.00 13.82 ? 133 LEU A CG    1 
ATOM   1018 C  CD1   . LEU A 1 153 ? -16.242 -14.361 -1.111  1.00 15.66 ? 133 LEU A CD1   1 
ATOM   1019 C  CD2   . LEU A 1 153 ? -15.413 -13.384 -3.239  1.00 14.99 ? 133 LEU A CD2   1 
ATOM   1020 N  N     . THR A 1 154 ? -20.114 -10.789 -2.619  1.00 11.98 ? 134 THR A N     1 
ATOM   1021 C  CA    . THR A 1 154 ? -21.527 -10.646 -2.932  1.00 12.77 ? 134 THR A CA    1 
ATOM   1022 C  C     . THR A 1 154 ? -21.729 -9.664  -4.070  1.00 12.22 ? 134 THR A C     1 
ATOM   1023 O  O     . THR A 1 154 ? -22.520 -9.907  -4.995  1.00 12.69 ? 134 THR A O     1 
ATOM   1024 C  CB    . THR A 1 154 ? -22.264 -10.126 -1.701  1.00 13.79 ? 134 THR A CB    1 
ATOM   1025 O  OG1   . THR A 1 154 ? -21.993 -10.967 -0.580  1.00 14.78 ? 134 THR A OG1   1 
ATOM   1026 C  CG2   . THR A 1 154 ? -23.741 -10.102 -1.939  1.00 16.23 ? 134 THR A CG2   1 
ATOM   1027 N  N     . VAL A 1 155 ? -21.064 -8.518  -3.994  1.00 12.54 ? 135 VAL A N     1 
ATOM   1028 C  CA    . VAL A 1 155 ? -21.216 -7.507  -5.034  1.00 12.83 ? 135 VAL A CA    1 
ATOM   1029 C  C     . VAL A 1 155 ? -20.750 -8.056  -6.377  1.00 12.79 ? 135 VAL A C     1 
ATOM   1030 O  O     . VAL A 1 155 ? -21.406 -7.869  -7.410  1.00 13.01 ? 135 VAL A O     1 
ATOM   1031 C  CB    . VAL A 1 155 ? -20.477 -6.218  -4.628  1.00 13.30 ? 135 VAL A CB    1 
ATOM   1032 C  CG1   . VAL A 1 155 ? -20.540 -5.185  -5.732  1.00 14.11 ? 135 VAL A CG1   1 
ATOM   1033 C  CG2   . VAL A 1 155 ? -21.062 -5.644  -3.315  1.00 13.55 ? 135 VAL A CG2   1 
ATOM   1034 N  N     . ALA A 1 156 ? -19.596 -8.727  -6.392  1.00 11.85 ? 136 ALA A N     1 
ATOM   1035 C  CA    . ALA A 1 156 ? -19.113 -9.303  -7.643  1.00 12.47 ? 136 ALA A CA    1 
ATOM   1036 C  C     . ALA A 1 156 ? -20.081 -10.343 -8.178  1.00 12.16 ? 136 ALA A C     1 
ATOM   1037 O  O     . ALA A 1 156 ? -20.336 -10.397 -9.386  1.00 12.59 ? 136 ALA A O     1 
ATOM   1038 C  CB    . ALA A 1 156 ? -17.735 -9.909  -7.422  1.00 12.66 ? 136 ALA A CB    1 
ATOM   1039 N  N     . LYS A 1 157 ? -20.621 -11.184 -7.300  1.00 12.76 ? 137 LYS A N     1 
ATOM   1040 C  CA    . LYS A 1 157 ? -21.553 -12.227 -7.715  1.00 12.85 ? 137 LYS A CA    1 
ATOM   1041 C  C     . LYS A 1 157 ? -22.805 -11.628 -8.341  1.00 13.62 ? 137 LYS A C     1 
ATOM   1042 O  O     . LYS A 1 157 ? -23.253 -12.073 -9.407  1.00 13.50 ? 137 LYS A O     1 
ATOM   1043 C  CB    . LYS A 1 157 ? -21.922 -13.071 -6.488  1.00 14.02 ? 137 LYS A CB    1 
ATOM   1044 C  CG    . LYS A 1 157 ? -22.961 -14.151 -6.751  1.00 17.66 ? 137 LYS A CG    1 
ATOM   1045 C  CD    . LYS A 1 157 ? -23.291 -14.965 -5.485  1.00 21.40 ? 137 LYS A CD    1 
ATOM   1046 C  CE    . LYS A 1 157 ? -23.772 -14.110 -4.294  1.00 24.72 ? 137 LYS A CE    1 
ATOM   1047 N  NZ    . LYS A 1 157 ? -25.096 -13.454 -4.502  1.00 27.72 ? 137 LYS A NZ    1 
ATOM   1048 N  N     . ASP A 1 158 ? -23.394 -10.624 -7.683  1.00 13.18 ? 138 ASP A N     1 
ATOM   1049 C  CA    . ASP A 1 158 ? -24.608 -10.000 -8.199  1.00 14.53 ? 138 ASP A CA    1 
ATOM   1050 C  C     . ASP A 1 158 ? -24.330 -9.238  -9.488  1.00 14.90 ? 138 ASP A C     1 
ATOM   1051 O  O     . ASP A 1 158 ? -25.154 -9.248  -10.406 1.00 14.98 ? 138 ASP A O     1 
ATOM   1052 C  CB    . ASP A 1 158 ? -25.222 -9.079  -7.139  1.00 16.49 ? 138 ASP A CB    1 
ATOM   1053 C  CG    . ASP A 1 158 ? -25.775 -9.837  -5.937  1.00 18.21 ? 138 ASP A CG    1 
ATOM   1054 O  OD1   . ASP A 1 158 ? -26.083 -11.040 -6.071  1.00 21.57 ? 138 ASP A OD1   1 
ATOM   1055 O  OD2   . ASP A 1 158 ? -25.909 -9.232  -4.847  1.00 17.46 ? 138 ASP A OD2   1 
ATOM   1056 N  N     . ALA A 1 159 ? -23.162 -8.600  -9.594  1.00 13.84 ? 139 ALA A N     1 
ATOM   1057 C  CA    . ALA A 1 159 ? -22.794 -7.922  -10.831 1.00 13.97 ? 139 ALA A CA    1 
ATOM   1058 C  C     . ALA A 1 159 ? -22.674 -8.907  -11.978 1.00 13.34 ? 139 ALA A C     1 
ATOM   1059 O  O     . ALA A 1 159 ? -23.114 -8.622  -13.100 1.00 14.36 ? 139 ALA A O     1 
ATOM   1060 C  CB    . ALA A 1 159 ? -21.468 -7.205  -10.644 1.00 14.61 ? 139 ALA A CB    1 
ATOM   1061 N  N     . ALA A 1 160 ? -22.063 -10.065 -11.723 1.00 13.69 ? 140 ALA A N     1 
ATOM   1062 C  CA    . ALA A 1 160 ? -21.864 -11.044 -12.792 1.00 13.32 ? 140 ALA A CA    1 
ATOM   1063 C  C     . ALA A 1 160 ? -23.185 -11.677 -13.216 1.00 14.17 ? 140 ALA A C     1 
ATOM   1064 O  O     . ALA A 1 160 ? -23.388 -11.951 -14.401 1.00 14.79 ? 140 ALA A O     1 
ATOM   1065 C  CB    . ALA A 1 160 ? -20.868 -12.113 -12.350 1.00 14.09 ? 140 ALA A CB    1 
ATOM   1066 N  N     . GLN A 1 161 ? -24.099 -11.912 -12.278 1.00 15.28 ? 141 GLN A N     1 
ATOM   1067 C  CA    . GLN A 1 161 ? -25.393 -12.461 -12.646 1.00 16.57 ? 141 GLN A CA    1 
ATOM   1068 C  C     . GLN A 1 161 ? -26.149 -11.472 -13.520 1.00 15.70 ? 141 GLN A C     1 
ATOM   1069 O  O     . GLN A 1 161 ? -26.765 -11.857 -14.520 1.00 16.81 ? 141 GLN A O     1 
ATOM   1070 C  CB    . GLN A 1 161 ? -26.185 -12.787 -11.381 1.00 19.15 ? 141 GLN A CB    1 
ATOM   1071 C  CG    . GLN A 1 161 ? -27.530 -13.417 -11.671 1.00 23.48 ? 141 GLN A CG    1 
ATOM   1072 C  CD    . GLN A 1 161 ? -27.392 -14.718 -12.444 1.00 28.34 ? 141 GLN A CD    1 
ATOM   1073 O  OE1   . GLN A 1 161 ? -26.520 -15.534 -12.142 1.00 30.62 ? 141 GLN A OE1   1 
ATOM   1074 N  NE2   . GLN A 1 161 ? -28.240 -14.912 -13.450 1.00 30.64 ? 141 GLN A NE2   1 
ATOM   1075 N  N     . ALA A 1 162 ? -26.097 -10.187 -13.162 1.00 15.78 ? 142 ALA A N     1 
ATOM   1076 C  CA    . ALA A 1 162 ? -26.692 -9.152  -13.995 1.00 16.10 ? 142 ALA A CA    1 
ATOM   1077 C  C     . ALA A 1 162 ? -26.049 -9.131  -15.373 1.00 15.77 ? 142 ALA A C     1 
ATOM   1078 O  O     . ALA A 1 162 ? -26.736 -8.980  -16.392 1.00 16.54 ? 142 ALA A O     1 
ATOM   1079 C  CB    . ALA A 1 162 ? -26.521 -7.797  -13.320 1.00 16.94 ? 142 ALA A CB    1 
ATOM   1080 N  N     . ALA A 1 163 ? -24.726 -9.279  -15.428 1.00 14.90 ? 143 ALA A N     1 
ATOM   1081 C  CA    . ALA A 1 163 ? -24.026 -9.249  -16.710 1.00 15.17 ? 143 ALA A CA    1 
ATOM   1082 C  C     . ALA A 1 163 ? -24.510 -10.367 -17.627 1.00 14.87 ? 143 ALA A C     1 
ATOM   1083 O  O     . ALA A 1 163 ? -24.760 -10.146 -18.822 1.00 15.64 ? 143 ALA A O     1 
ATOM   1084 C  CB    . ALA A 1 163 ? -22.522 -9.379  -16.474 1.00 14.82 ? 143 ALA A CB    1 
ATOM   1085 N  N     . ILE A 1 164 ? -24.615 -11.586 -17.099 1.00 15.67 ? 144 ILE A N     1 
ATOM   1086 C  CA    . ILE A 1 164 ? -25.045 -12.724 -17.909 1.00 17.92 ? 144 ILE A CA    1 
ATOM   1087 C  C     . ILE A 1 164 ? -26.455 -12.496 -18.441 1.00 18.96 ? 144 ILE A C     1 
ATOM   1088 O  O     . ILE A 1 164 ? -26.736 -12.723 -19.624 1.00 19.65 ? 144 ILE A O     1 
ATOM   1089 C  CB    . ILE A 1 164 ? -24.952 -14.035 -17.100 1.00 20.31 ? 144 ILE A CB    1 
ATOM   1090 C  CG1   . ILE A 1 164 ? -23.502 -14.396 -16.767 1.00 22.32 ? 144 ILE A CG1   1 
ATOM   1091 C  CG2   . ILE A 1 164 ? -25.637 -15.181 -17.833 1.00 21.59 ? 144 ILE A CG2   1 
ATOM   1092 C  CD1   . ILE A 1 164 ? -22.678 -14.815 -17.929 1.00 24.60 ? 144 ILE A CD1   1 
ATOM   1093 N  N     . GLU A 1 165 ? -27.365 -12.043 -17.576 1.00 18.96 ? 145 GLU A N     1 
ATOM   1094 C  CA    . GLU A 1 165 ? -28.748 -11.836 -17.999 1.00 20.16 ? 145 GLU A CA    1 
ATOM   1095 C  C     . GLU A 1 165 ? -28.831 -10.779 -19.092 1.00 20.53 ? 145 GLU A C     1 
ATOM   1096 O  O     . GLU A 1 165 ? -29.532 -10.961 -20.093 1.00 21.63 ? 145 GLU A O     1 
ATOM   1097 C  CB    . GLU A 1 165 ? -29.614 -11.435 -16.805 1.00 22.95 ? 145 GLU A CB    1 
ATOM   1098 C  CG    . GLU A 1 165 ? -29.829 -12.552 -15.809 1.00 26.96 ? 145 GLU A CG    1 
ATOM   1099 C  CD    . GLU A 1 165 ? -30.696 -12.139 -14.641 1.00 31.06 ? 145 GLU A CD    1 
ATOM   1100 O  OE1   . GLU A 1 165 ? -31.501 -11.192 -14.794 1.00 32.84 ? 145 GLU A OE1   1 
ATOM   1101 O  OE2   . GLU A 1 165 ? -30.573 -12.773 -13.575 1.00 31.85 ? 145 GLU A OE2   1 
ATOM   1102 N  N     . LYS A 1 166 ? -28.111 -9.674  -18.921 1.00 19.53 ? 146 LYS A N     1 
ATOM   1103 C  CA    . LYS A 1 166 ? -28.223 -8.553  -19.844 1.00 19.43 ? 146 LYS A CA    1 
ATOM   1104 C  C     . LYS A 1 166 ? -27.523 -8.843  -21.164 1.00 19.68 ? 146 LYS A C     1 
ATOM   1105 O  O     . LYS A 1 166 ? -28.020 -8.455  -22.223 1.00 20.43 ? 146 LYS A O     1 
ATOM   1106 C  CB    . LYS A 1 166 ? -27.634 -7.315  -19.180 1.00 20.31 ? 146 LYS A CB    1 
ATOM   1107 C  CG    . LYS A 1 166 ? -27.692 -6.043  -19.997 1.00 22.26 ? 146 LYS A CG    1 
ATOM   1108 C  CD    . LYS A 1 166 ? -29.101 -5.544  -20.218 1.00 25.85 ? 146 LYS A CD    1 
ATOM   1109 C  CE    . LYS A 1 166 ? -29.064 -4.186  -20.884 1.00 28.46 ? 146 LYS A CE    1 
ATOM   1110 N  NZ    . LYS A 1 166 ? -30.416 -3.606  -21.071 1.00 30.64 ? 146 LYS A NZ    1 
ATOM   1111 N  N     . ALA A 1 167 ? -26.353 -9.484  -21.123 1.00 19.34 ? 147 ALA A N     1 
ATOM   1112 C  CA    . ALA A 1 167 ? -25.607 -9.737  -22.348 1.00 19.98 ? 147 ALA A CA    1 
ATOM   1113 C  C     . ALA A 1 167 ? -26.368 -10.646 -23.287 1.00 22.30 ? 147 ALA A C     1 
ATOM   1114 O  O     . ALA A 1 167 ? -26.099 -10.633 -24.491 1.00 22.87 ? 147 ALA A O     1 
ATOM   1115 C  CB    . ALA A 1 167 ? -24.257 -10.373 -22.027 1.00 19.99 ? 147 ALA A CB    1 
ATOM   1116 N  N     . ASN A 1 168 ? -27.320 -11.422 -22.770 1.00 24.57 ? 148 ASN A N     1 
ATOM   1117 C  CA    . ASN A 1 168 ? -28.062 -12.355 -23.606 1.00 27.83 ? 148 ASN A CA    1 
ATOM   1118 C  C     . ASN A 1 168 ? -28.834 -11.638 -24.699 1.00 29.34 ? 148 ASN A C     1 
ATOM   1119 O  O     . ASN A 1 168 ? -29.137 -12.254 -25.722 1.00 31.25 ? 148 ASN A O     1 
ATOM   1120 C  CB    . ASN A 1 168 ? -28.999 -13.200 -22.742 1.00 30.69 ? 148 ASN A CB    1 
ATOM   1121 C  CG    . ASN A 1 168 ? -29.456 -14.454 -23.437 1.00 34.29 ? 148 ASN A CG    1 
ATOM   1122 O  OD1   . ASN A 1 168 ? -28.730 -15.028 -24.254 1.00 36.36 ? 148 ASN A OD1   1 
ATOM   1123 N  ND2   . ASN A 1 168 ? -30.674 -14.885 -23.134 1.00 35.29 ? 148 ASN A ND2   1 
ATOM   1124 N  N     . ASN A 1 169 ? -29.152 -10.349 -24.518 1.00 29.15 ? 149 ASN A N     1 
ATOM   1125 C  CA    . ASN A 1 169 ? -29.821 -9.605  -25.578 1.00 31.26 ? 149 ASN A CA    1 
ATOM   1126 C  C     . ASN A 1 169 ? -29.228 -8.213  -25.796 1.00 28.91 ? 149 ASN A C     1 
ATOM   1127 O  O     . ASN A 1 169 ? -29.891 -7.354  -26.390 1.00 29.98 ? 149 ASN A O     1 
ATOM   1128 C  CB    . ASN A 1 169 ? -31.326 -9.524  -25.310 1.00 34.65 ? 149 ASN A CB    1 
ATOM   1129 C  CG    . ASN A 1 169 ? -31.698 -8.372  -24.407 1.00 36.99 ? 149 ASN A CG    1 
ATOM   1130 O  OD1   . ASN A 1 169 ? -31.017 -8.079  -23.432 1.00 37.01 ? 149 ASN A OD1   1 
ATOM   1131 N  ND2   . ASN A 1 169 ? -32.790 -7.699  -24.742 1.00 38.68 ? 149 ASN A ND2   1 
ATOM   1132 N  N     . THR A 1 170 ? -27.981 -7.989  -25.391 1.00 25.83 ? 150 THR A N     1 
ATOM   1133 C  CA    . THR A 1 170 ? -27.323 -6.689  -25.495 1.00 24.94 ? 150 THR A CA    1 
ATOM   1134 C  C     . THR A 1 170 ? -25.944 -6.897  -26.113 1.00 23.87 ? 150 THR A C     1 
ATOM   1135 O  O     . THR A 1 170 ? -25.057 -7.457  -25.468 1.00 24.84 ? 150 THR A O     1 
ATOM   1136 C  CB    . THR A 1 170 ? -27.195 -6.068  -24.098 1.00 26.45 ? 150 THR A CB    1 
ATOM   1137 O  OG1   . THR A 1 170 ? -28.499 -5.979  -23.502 1.00 28.11 ? 150 THR A OG1   1 
ATOM   1138 C  CG2   . THR A 1 170 ? -26.586 -4.691  -24.168 1.00 26.59 ? 150 THR A CG2   1 
ATOM   1139 N  N     . GLU A 1 171 ? -25.756 -6.436  -27.354 1.00 22.47 ? 151 GLU A N     1 
ATOM   1140 C  CA    . GLU A 1 171 ? -24.441 -6.487  -27.978 1.00 22.38 ? 151 GLU A CA    1 
ATOM   1141 C  C     . GLU A 1 171 ? -23.528 -5.360  -27.510 1.00 20.44 ? 151 GLU A C     1 
ATOM   1142 O  O     . GLU A 1 171 ? -22.304 -5.519  -27.526 1.00 21.82 ? 151 GLU A O     1 
ATOM   1143 C  CB    . GLU A 1 171 ? -24.593 -6.400  -29.499 1.00 24.52 ? 151 GLU A CB    1 
ATOM   1144 C  CG    . GLU A 1 171 ? -23.317 -6.088  -30.252 1.00 26.43 ? 151 GLU A CG    1 
ATOM   1145 N  N     . ASP A 1 172 ? -24.087 -4.213  -27.133 1.00 19.99 ? 152 ASP A N     1 
ATOM   1146 C  CA    . ASP A 1 172 ? -23.291 -3.038  -26.787 1.00 18.86 ? 152 ASP A CA    1 
ATOM   1147 C  C     . ASP A 1 172 ? -22.688 -3.195  -25.393 1.00 17.78 ? 152 ASP A C     1 
ATOM   1148 O  O     . ASP A 1 172 ? -23.405 -3.272  -24.391 1.00 18.14 ? 152 ASP A O     1 
ATOM   1149 C  CB    . ASP A 1 172 ? -24.149 -1.775  -26.855 1.00 19.27 ? 152 ASP A CB    1 
ATOM   1150 C  CG    . ASP A 1 172 ? -23.399 -0.526  -26.394 1.00 21.36 ? 152 ASP A CG    1 
ATOM   1151 O  OD1   . ASP A 1 172 ? -24.083 0.426   -25.945 1.00 23.82 ? 152 ASP A OD1   1 
ATOM   1152 O  OD2   . ASP A 1 172 ? -22.138 -0.498  -26.459 1.00 20.91 ? 152 ASP A OD2   1 
ATOM   1153 N  N     . CYS A 1 173 ? -21.366 -3.212  -25.329 1.00 16.85 ? 153 CYS A N     1 
ATOM   1154 C  CA    . CYS A 1 173 ? -20.691 -3.335  -24.045 1.00 15.97 ? 153 CYS A CA    1 
ATOM   1155 C  C     . CYS A 1 173 ? -20.863 -2.111  -23.149 1.00 16.63 ? 153 CYS A C     1 
ATOM   1156 O  O     . CYS A 1 173 ? -20.744 -2.247  -21.924 1.00 16.77 ? 153 CYS A O     1 
ATOM   1157 C  CB    . CYS A 1 173 ? -19.213 -3.649  -24.246 1.00 17.09 ? 153 CYS A CB    1 
ATOM   1158 S  SG    . CYS A 1 173 ? -18.894 -5.277  -24.982 1.00 19.03 ? 153 CYS A SG    1 
ATOM   1159 N  N     . ILE A 1 174 ? -21.125 -0.927  -23.704 1.00 17.05 ? 154 ILE A N     1 
ATOM   1160 C  CA    . ILE A 1 174 ? -21.418 0.234   -22.867 1.00 17.21 ? 154 ILE A CA    1 
ATOM   1161 C  C     . ILE A 1 174 ? -22.733 0.018   -22.133 1.00 17.25 ? 154 ILE A C     1 
ATOM   1162 O  O     . ILE A 1 174 ? -22.806 0.137   -20.909 1.00 17.80 ? 154 ILE A O     1 
ATOM   1163 C  CB    . ILE A 1 174 ? -21.438 1.532   -23.701 1.00 19.04 ? 154 ILE A CB    1 
ATOM   1164 C  CG1   . ILE A 1 174 ? -20.040 1.843   -24.247 1.00 19.56 ? 154 ILE A CG1   1 
ATOM   1165 C  CG2   . ILE A 1 174 ? -21.970 2.705   -22.864 1.00 19.87 ? 154 ILE A CG2   1 
ATOM   1166 C  CD1   . ILE A 1 174 ? -20.015 2.957   -25.283 1.00 21.50 ? 154 ILE A CD1   1 
ATOM   1167 N  N     . GLU A 1 175 ? -23.787 -0.328  -22.877 1.00 18.29 ? 155 GLU A N     1 
ATOM   1168 C  CA    . GLU A 1 175 ? -25.083 -0.589  -22.260 1.00 19.49 ? 155 GLU A CA    1 
ATOM   1169 C  C     . GLU A 1 175 ? -24.976 -1.719  -21.249 1.00 17.67 ? 155 GLU A C     1 
ATOM   1170 O  O     . GLU A 1 175 ? -25.555 -1.651  -20.158 1.00 17.83 ? 155 GLU A O     1 
ATOM   1171 C  CB    . GLU A 1 175 ? -26.098 -0.935  -23.352 1.00 21.62 ? 155 GLU A CB    1 
ATOM   1172 C  CG    . GLU A 1 175 ? -27.514 -1.140  -22.830 1.00 25.30 ? 155 GLU A CG    1 
ATOM   1173 C  CD    . GLU A 1 175 ? -28.510 -1.514  -23.920 1.00 29.25 ? 155 GLU A CD    1 
ATOM   1174 O  OE1   . GLU A 1 175 ? -28.206 -1.311  -25.118 1.00 30.79 ? 155 GLU A OE1   1 
ATOM   1175 O  OE2   . GLU A 1 175 ? -29.603 -2.019  -23.563 1.00 31.08 ? 155 GLU A OE2   1 
ATOM   1176 N  N     . LEU A 1 176 ? -24.222 -2.762  -21.588 1.00 16.48 ? 156 LEU A N     1 
ATOM   1177 C  CA    . LEU A 1 176 ? -24.019 -3.863  -20.653 1.00 16.62 ? 156 LEU A CA    1 
ATOM   1178 C  C     . LEU A 1 176 ? -23.358 -3.374  -19.367 1.00 16.60 ? 156 LEU A C     1 
ATOM   1179 O  O     . LEU A 1 176 ? -23.840 -3.657  -18.261 1.00 16.23 ? 156 LEU A O     1 
ATOM   1180 C  CB    . LEU A 1 176 ? -23.184 -4.959  -21.316 1.00 17.02 ? 156 LEU A CB    1 
ATOM   1181 C  CG    . LEU A 1 176 ? -22.804 -6.109  -20.386 1.00 18.02 ? 156 LEU A CG    1 
ATOM   1182 C  CD1   . LEU A 1 176 ? -24.057 -6.756  -19.854 1.00 19.12 ? 156 LEU A CD1   1 
ATOM   1183 C  CD2   . LEU A 1 176 ? -21.927 -7.111  -21.098 1.00 19.13 ? 156 LEU A CD2   1 
ATOM   1184 N  N     . MET A 1 177 ? -22.257 -2.619  -19.491 1.00 15.96 ? 157 MET A N     1 
ATOM   1185 C  CA    . MET A 1 177 ? -21.527 -2.185  -18.298 1.00 15.16 ? 157 MET A CA    1 
ATOM   1186 C  C     . MET A 1 177 ? -22.364 -1.226  -17.456 1.00 15.72 ? 157 MET A C     1 
ATOM   1187 O  O     . MET A 1 177 ? -22.291 -1.253  -16.222 1.00 15.51 ? 157 MET A O     1 
ATOM   1188 C  CB    . MET A 1 177 ? -20.182 -1.576  -18.703 1.00 15.60 ? 157 MET A CB    1 
ATOM   1189 C  CG    . MET A 1 177 ? -19.217 -1.446  -17.547 1.00 16.75 ? 157 MET A CG    1 
ATOM   1190 S  SD    . MET A 1 177 ? -18.558 -3.063  -17.040 1.00 16.72 ? 157 MET A SD    1 
ATOM   1191 C  CE    . MET A 1 177 ? -18.425 -2.827  -15.281 1.00 16.65 ? 157 MET A CE    1 
ATOM   1192 N  N     . GLU A 1 178 ? -23.145 -0.357  -18.102 1.00 16.27 ? 158 GLU A N     1 
ATOM   1193 C  CA    . GLU A 1 178 ? -24.059 0.513   -17.367 1.00 16.53 ? 158 GLU A CA    1 
ATOM   1194 C  C     . GLU A 1 178 ? -25.002 -0.300  -16.497 1.00 16.95 ? 158 GLU A C     1 
ATOM   1195 O  O     . GLU A 1 178 ? -25.215 0.033   -15.327 1.00 16.62 ? 158 GLU A O     1 
ATOM   1196 C  CB    . GLU A 1 178 ? -24.835 1.402   -18.343 1.00 19.51 ? 158 GLU A CB    1 
ATOM   1197 C  CG    . GLU A 1 178 ? -23.977 2.525   -18.923 1.00 23.62 ? 158 GLU A CG    1 
ATOM   1198 C  CD    . GLU A 1 178 ? -24.640 3.309   -20.025 1.00 28.60 ? 158 GLU A CD    1 
ATOM   1199 O  OE1   . GLU A 1 178 ? -25.571 2.789   -20.675 1.00 30.19 ? 158 GLU A OE1   1 
ATOM   1200 O  OE2   . GLU A 1 178 ? -24.195 4.452   -20.256 1.00 31.43 ? 158 GLU A OE2   1 
ATOM   1201 N  N     . TYR A 1 179 ? -25.558 -1.381  -17.047 1.00 16.71 ? 159 TYR A N     1 
ATOM   1202 C  CA    . TYR A 1 179 ? -26.496 -2.211  -16.301 1.00 16.63 ? 159 TYR A CA    1 
ATOM   1203 C  C     . TYR A 1 179 ? -25.788 -2.951  -15.174 1.00 15.82 ? 159 TYR A C     1 
ATOM   1204 O  O     . TYR A 1 179 ? -26.316 -3.063  -14.056 1.00 15.98 ? 159 TYR A O     1 
ATOM   1205 C  CB    . TYR A 1 179 ? -27.145 -3.206  -17.258 1.00 16.90 ? 159 TYR A CB    1 
ATOM   1206 C  CG    . TYR A 1 179 ? -28.193 -4.074  -16.605 1.00 17.90 ? 159 TYR A CG    1 
ATOM   1207 C  CD1   . TYR A 1 179 ? -29.448 -3.561  -16.288 1.00 20.43 ? 159 TYR A CD1   1 
ATOM   1208 C  CD2   . TYR A 1 179 ? -27.935 -5.405  -16.305 1.00 17.89 ? 159 TYR A CD2   1 
ATOM   1209 C  CE1   . TYR A 1 179 ? -30.414 -4.355  -15.707 1.00 21.83 ? 159 TYR A CE1   1 
ATOM   1210 C  CE2   . TYR A 1 179 ? -28.907 -6.209  -15.738 1.00 18.71 ? 159 TYR A CE2   1 
ATOM   1211 C  CZ    . TYR A 1 179 ? -30.137 -5.676  -15.436 1.00 21.12 ? 159 TYR A CZ    1 
ATOM   1212 O  OH    . TYR A 1 179 ? -31.092 -6.479  -14.854 1.00 23.53 ? 159 TYR A OH    1 
ATOM   1213 N  N     . ILE A 1 180 ? -24.592 -3.470  -15.453 1.00 15.29 ? 160 ILE A N     1 
ATOM   1214 C  CA    . ILE A 1 180 ? -23.784 -4.109  -14.415 1.00 15.37 ? 160 ILE A CA    1 
ATOM   1215 C  C     . ILE A 1 180 ? -23.591 -3.160  -13.241 1.00 15.53 ? 160 ILE A C     1 
ATOM   1216 O  O     . ILE A 1 180 ? -23.739 -3.555  -12.083 1.00 15.69 ? 160 ILE A O     1 
ATOM   1217 C  CB    . ILE A 1 180 ? -22.441 -4.599  -14.993 1.00 15.66 ? 160 ILE A CB    1 
ATOM   1218 C  CG1   . ILE A 1 180 ? -22.678 -5.744  -15.979 1.00 15.94 ? 160 ILE A CG1   1 
ATOM   1219 C  CG2   . ILE A 1 180 ? -21.481 -5.047  -13.873 1.00 16.59 ? 160 ILE A CG2   1 
ATOM   1220 C  CD1   . ILE A 1 180 ? -21.428 -6.116  -16.785 1.00 17.00 ? 160 ILE A CD1   1 
ATOM   1221 N  N     . ILE A 1 181 ? -23.276 -1.897  -13.523 1.00 15.36 ? 161 ILE A N     1 
ATOM   1222 C  CA    . ILE A 1 181 ? -23.053 -0.924  -12.460 1.00 15.29 ? 161 ILE A CA    1 
ATOM   1223 C  C     . ILE A 1 181 ? -24.340 -0.646  -11.689 1.00 15.27 ? 161 ILE A C     1 
ATOM   1224 O  O     . ILE A 1 181 ? -24.323 -0.558  -10.459 1.00 15.47 ? 161 ILE A O     1 
ATOM   1225 C  CB    . ILE A 1 181 ? -22.399 0.345   -13.034 1.00 16.24 ? 161 ILE A CB    1 
ATOM   1226 C  CG1   . ILE A 1 181 ? -20.947 0.029   -13.408 1.00 17.12 ? 161 ILE A CG1   1 
ATOM   1227 C  CG2   . ILE A 1 181 ? -22.475 1.509   -12.061 1.00 17.30 ? 161 ILE A CG2   1 
ATOM   1228 C  CD1   . ILE A 1 181 ? -20.343 1.004   -14.385 1.00 17.94 ? 161 ILE A CD1   1 
ATOM   1229 N  N     . VAL A 1 182 ? -25.475 -0.509  -12.373 1.00 15.26 ? 162 VAL A N     1 
ATOM   1230 C  CA    . VAL A 1 182 ? -26.737 -0.325  -11.656 1.00 16.72 ? 162 VAL A CA    1 
ATOM   1231 C  C     . VAL A 1 182 ? -26.954 -1.466  -10.677 1.00 16.17 ? 162 VAL A C     1 
ATOM   1232 O  O     . VAL A 1 182 ? -27.277 -1.252  -9.501  1.00 16.05 ? 162 VAL A O     1 
ATOM   1233 C  CB    . VAL A 1 182 ? -27.913 -0.202  -12.641 1.00 19.33 ? 162 VAL A CB    1 
ATOM   1234 C  CG1   . VAL A 1 182 ? -29.248 -0.311  -11.887 1.00 21.40 ? 162 VAL A CG1   1 
ATOM   1235 C  CG2   . VAL A 1 182 ? -27.831 1.106   -13.394 1.00 21.26 ? 162 VAL A CG2   1 
ATOM   1236 N  N     . LYS A 1 183 ? -26.767 -2.692  -11.143 1.00 15.52 ? 163 LYS A N     1 
ATOM   1237 C  CA    . LYS A 1 183 ? -27.064 -3.849  -10.308 1.00 15.05 ? 163 LYS A CA    1 
ATOM   1238 C  C     . LYS A 1 183 ? -26.003 -4.064  -9.241  1.00 14.54 ? 163 LYS A C     1 
ATOM   1239 O  O     . LYS A 1 183 ? -26.324 -4.520  -8.134  1.00 15.17 ? 163 LYS A O     1 
ATOM   1240 C  CB    . LYS A 1 183 ? -27.255 -5.081  -11.190 1.00 16.40 ? 163 LYS A CB    1 
ATOM   1241 C  CG    . LYS A 1 183 ? -28.517 -4.987  -12.051 1.00 19.97 ? 163 LYS A CG    1 
ATOM   1242 C  CD    . LYS A 1 183 ? -29.746 -5.202  -11.178 1.00 24.45 ? 163 LYS A CD    1 
ATOM   1243 C  CE    . LYS A 1 183 ? -31.041 -4.883  -11.848 1.00 28.60 ? 163 LYS A CE    1 
ATOM   1244 N  NZ    . LYS A 1 183 ? -32.079 -5.038  -10.795 1.00 29.61 ? 163 LYS A NZ    1 
ATOM   1245 N  N     . ALA A 1 184 ? -24.749 -3.730  -9.541  1.00 14.46 ? 164 ALA A N     1 
ATOM   1246 C  CA    . ALA A 1 184 ? -23.689 -3.809  -8.545  1.00 14.41 ? 164 ALA A CA    1 
ATOM   1247 C  C     . ALA A 1 184 ? -23.918 -2.784  -7.445  1.00 14.34 ? 164 ALA A C     1 
ATOM   1248 O  O     . ALA A 1 184 ? -23.671 -3.062  -6.266  1.00 14.48 ? 164 ALA A O     1 
ATOM   1249 C  CB    . ALA A 1 184 ? -22.337 -3.575  -9.220  1.00 15.42 ? 164 ALA A CB    1 
ATOM   1250 N  N     . ASN A 1 185 ? -24.383 -1.591  -7.814  1.00 14.66 ? 165 ASN A N     1 
ATOM   1251 C  CA    . ASN A 1 185 ? -24.712 -0.578  -6.814  1.00 15.11 ? 165 ASN A CA    1 
ATOM   1252 C  C     . ASN A 1 185 ? -25.862 -1.036  -5.924  1.00 14.40 ? 165 ASN A C     1 
ATOM   1253 O  O     . ASN A 1 185 ? -25.832 -0.824  -4.709  1.00 15.02 ? 165 ASN A O     1 
ATOM   1254 C  CB    . ASN A 1 185 ? -25.063 0.741   -7.496  1.00 18.68 ? 165 ASN A CB    1 
ATOM   1255 C  CG    . ASN A 1 185 ? -23.848 1.610   -7.752  1.00 24.58 ? 165 ASN A CG    1 
ATOM   1256 O  OD1   . ASN A 1 185 ? -22.938 1.685   -6.922  1.00 28.06 ? 165 ASN A OD1   1 
ATOM   1257 N  ND2   . ASN A 1 185 ? -23.846 2.306   -8.884  1.00 27.58 ? 165 ASN A ND2   1 
ATOM   1258 N  N     . GLU A 1 186 ? -26.888 -1.657  -6.500  1.00 14.85 ? 166 GLU A N     1 
ATOM   1259 C  CA    . GLU A 1 186 ? -27.983 -2.180  -5.686  1.00 15.78 ? 166 GLU A CA    1 
ATOM   1260 C  C     . GLU A 1 186 ? -27.468 -3.220  -4.708  1.00 14.76 ? 166 GLU A C     1 
ATOM   1261 O  O     . GLU A 1 186 ? -27.840 -3.213  -3.532  1.00 14.64 ? 166 GLU A O     1 
ATOM   1262 C  CB    . GLU A 1 186 ? -29.065 -2.773  -6.587  1.00 18.24 ? 166 GLU A CB    1 
ATOM   1263 C  CG    . GLU A 1 186 ? -29.843 -1.719  -7.327  1.00 22.24 ? 166 GLU A CG    1 
ATOM   1264 C  CD    . GLU A 1 186 ? -30.875 -2.294  -8.276  1.00 26.32 ? 166 GLU A CD    1 
ATOM   1265 O  OE1   . GLU A 1 186 ? -31.042 -3.533  -8.309  1.00 27.00 ? 166 GLU A OE1   1 
ATOM   1266 O  OE2   . GLU A 1 186 ? -31.521 -1.497  -8.994  1.00 29.32 ? 166 GLU A OE2   1 
ATOM   1267 N  N     . SER A 1 187 ? -26.599 -4.114  -5.174  1.00 13.88 ? 167 SER A N     1 
ATOM   1268 C  CA    . SER A 1 187 ? -26.000 -5.117  -4.296  1.00 13.40 ? 167 SER A CA    1 
ATOM   1269 C  C     . SER A 1 187 ? -25.176 -4.456  -3.193  1.00 13.00 ? 167 SER A C     1 
ATOM   1270 O  O     . SER A 1 187 ? -25.285 -4.820  -2.011  1.00 13.79 ? 167 SER A O     1 
ATOM   1271 C  CB    . SER A 1 187 ? -25.135 -6.059  -5.136  1.00 14.39 ? 167 SER A CB    1 
ATOM   1272 O  OG    . SER A 1 187 ? -24.534 -7.061  -4.340  1.00 14.89 ? 167 SER A OG    1 
ATOM   1273 N  N     . LEU A 1 188 ? -24.373 -3.461  -3.550  1.00 13.67 ? 168 LEU A N     1 
ATOM   1274 C  CA    . LEU A 1 188 ? -23.564 -2.771  -2.553  1.00 12.98 ? 168 LEU A CA    1 
ATOM   1275 C  C     . LEU A 1 188 ? -24.444 -2.121  -1.493  1.00 13.32 ? 168 LEU A C     1 
ATOM   1276 O  O     . LEU A 1 188 ? -24.167 -2.220  -0.293  1.00 13.54 ? 168 LEU A O     1 
ATOM   1277 C  CB    . LEU A 1 188 ? -22.694 -1.716  -3.229  1.00 13.59 ? 168 LEU A CB    1 
ATOM   1278 C  CG    . LEU A 1 188 ? -21.785 -0.899  -2.304  1.00 15.23 ? 168 LEU A CG    1 
ATOM   1279 C  CD1   . LEU A 1 188 ? -20.830 -1.797  -1.490  1.00 15.28 ? 168 LEU A CD1   1 
ATOM   1280 C  CD2   . LEU A 1 188 ? -21.018 0.137   -3.111  1.00 17.21 ? 168 LEU A CD2   1 
ATOM   1281 N  N     . GLU A 1 189 ? -25.524 -1.466  -1.912  1.00 13.43 ? 169 GLU A N     1 
ATOM   1282 C  CA    . GLU A 1 189 ? -26.423 -0.827  -0.965  1.00 15.54 ? 169 GLU A CA    1 
ATOM   1283 C  C     . GLU A 1 189 ? -27.133 -1.847  -0.090  1.00 14.47 ? 169 GLU A C     1 
ATOM   1284 O  O     . GLU A 1 189 ? -27.571 -1.504  1.013   1.00 16.26 ? 169 GLU A O     1 
ATOM   1285 C  CB    . GLU A 1 189 ? -27.422 0.055   -1.713  1.00 18.45 ? 169 GLU A CB    1 
ATOM   1286 C  CG    . GLU A 1 189 ? -26.778 1.271   -2.396  1.00 24.18 ? 169 GLU A CG    1 
ATOM   1287 C  CD    . GLU A 1 189 ? -26.046 2.194   -1.422  1.00 33.09 ? 169 GLU A CD    1 
ATOM   1288 O  OE1   . GLU A 1 189 ? -26.571 2.446   -0.317  1.00 36.39 ? 169 GLU A OE1   1 
ATOM   1289 O  OE2   . GLU A 1 189 ? -24.933 2.661   -1.773  1.00 37.29 ? 169 GLU A OE2   1 
ATOM   1290 N  N     . ASN A 1 190 ? -27.220 -3.094  -0.535  1.00 14.81 ? 170 ASN A N     1 
ATOM   1291 C  CA    . ASN A 1 190 ? -27.828 -4.164  0.238   1.00 14.49 ? 170 ASN A CA    1 
ATOM   1292 C  C     . ASN A 1 190 ? -26.861 -4.857  1.191   1.00 13.43 ? 170 ASN A C     1 
ATOM   1293 O  O     . ASN A 1 190 ? -27.320 -5.620  2.050   1.00 14.17 ? 170 ASN A O     1 
ATOM   1294 C  CB    . ASN A 1 190 ? -28.436 -5.202  -0.709  1.00 15.45 ? 170 ASN A CB    1 
ATOM   1295 C  CG    . ASN A 1 190 ? -29.318 -6.189  0.010   1.00 16.85 ? 170 ASN A CG    1 
ATOM   1296 O  OD1   . ASN A 1 190 ? -30.283 -5.800  0.638   1.00 17.90 ? 170 ASN A OD1   1 
ATOM   1297 N  ND2   . ASN A 1 190 ? -29.002 -7.469  -0.097  1.00 17.25 ? 170 ASN A ND2   1 
ATOM   1298 N  N     . THR A 1 191 ? -25.556 -4.616  1.077   1.00 12.98 ? 171 THR A N     1 
ATOM   1299 C  CA    . THR A 1 191 ? -24.594 -5.306  1.941   1.00 12.36 ? 171 THR A CA    1 
ATOM   1300 C  C     . THR A 1 191 ? -24.910 -5.176  3.429   1.00 13.35 ? 171 THR A C     1 
ATOM   1301 O  O     . THR A 1 191 ? -24.742 -6.173  4.148   1.00 13.52 ? 171 THR A O     1 
ATOM   1302 C  CB    . THR A 1 191 ? -23.125 -4.956  1.626   1.00 13.20 ? 171 THR A CB    1 
ATOM   1303 O  OG1   . THR A 1 191 ? -22.891 -3.545  1.723   1.00 13.43 ? 171 THR A OG1   1 
ATOM   1304 C  CG2   . THR A 1 191 ? -22.719 -5.475  0.246   1.00 13.30 ? 171 THR A CG2   1 
ATOM   1305 N  N     . PRO A 1 192 ? -25.376 -4.034  3.952   1.00 13.22 ? 172 PRO A N     1 
ATOM   1306 C  CA    . PRO A 1 192 ? -25.678 -3.980  5.396   1.00 13.63 ? 172 PRO A CA    1 
ATOM   1307 C  C     . PRO A 1 192 ? -26.814 -4.886  5.815   1.00 13.87 ? 172 PRO A C     1 
ATOM   1308 O  O     . PRO A 1 192 ? -26.944 -5.161  7.018   1.00 15.25 ? 172 PRO A O     1 
ATOM   1309 C  CB    . PRO A 1 192 ? -26.016 -2.506  5.646   1.00 15.13 ? 172 PRO A CB    1 
ATOM   1310 C  CG    . PRO A 1 192 ? -25.425 -1.765  4.469   1.00 15.54 ? 172 PRO A CG    1 
ATOM   1311 C  CD    . PRO A 1 192 ? -25.541 -2.717  3.308   1.00 13.95 ? 172 PRO A CD    1 
ATOM   1312 N  N     . ASN A 1 193 ? -27.640 -5.350  4.876   1.00 13.47 ? 173 ASN A N     1 
ATOM   1313 C  CA    . ASN A 1 193 ? -28.707 -6.288  5.196   1.00 13.76 ? 173 ASN A CA    1 
ATOM   1314 C  C     . ASN A 1 193 ? -28.212 -7.722  5.279   1.00 13.73 ? 173 ASN A C     1 
ATOM   1315 O  O     . ASN A 1 193 ? -28.988 -8.608  5.648   1.00 15.21 ? 173 ASN A O     1 
ATOM   1316 C  CB    . ASN A 1 193 ? -29.849 -6.162  4.195   1.00 14.90 ? 173 ASN A CB    1 
ATOM   1317 C  CG    . ASN A 1 193 ? -30.426 -4.780  4.166   1.00 15.80 ? 173 ASN A CG    1 
ATOM   1318 O  OD1   . ASN A 1 193 ? -30.651 -4.175  5.216   1.00 17.86 ? 173 ASN A OD1   1 
ATOM   1319 N  ND2   . ASN A 1 193 ? -30.654 -4.252  2.968   1.00 17.92 ? 173 ASN A ND2   1 
ATOM   1320 N  N     . LEU A 1 194 ? -26.944 -7.966  4.965   1.00 13.03 ? 174 LEU A N     1 
ATOM   1321 C  CA    . LEU A 1 194 ? -26.352 -9.291  5.049   1.00 13.20 ? 174 LEU A CA    1 
ATOM   1322 C  C     . LEU A 1 194 ? -25.283 -9.402  6.114   1.00 13.62 ? 174 LEU A C     1 
ATOM   1323 O  O     . LEU A 1 194 ? -25.070 -10.490 6.642   1.00 13.91 ? 174 LEU A O     1 
ATOM   1324 C  CB    . LEU A 1 194 ? -25.729 -9.668  3.694   1.00 14.31 ? 174 LEU A CB    1 
ATOM   1325 C  CG    . LEU A 1 194 ? -26.730 -9.941  2.560   1.00 15.04 ? 174 LEU A CG    1 
ATOM   1326 C  CD1   . LEU A 1 194 ? -26.057 -9.811  1.203   1.00 16.15 ? 174 LEU A CD1   1 
ATOM   1327 C  CD2   . LEU A 1 194 ? -27.349 -11.321 2.709   1.00 16.43 ? 174 LEU A CD2   1 
ATOM   1328 N  N     . LEU A 1 195 ? -24.603 -8.308  6.418   1.00 14.55 ? 175 LEU A N     1 
ATOM   1329 C  CA    . LEU A 1 195 ? -23.453 -8.303  7.310   1.00 14.86 ? 175 LEU A CA    1 
ATOM   1330 C  C     . LEU A 1 195 ? -23.747 -7.302  8.426   1.00 14.72 ? 175 LEU A C     1 
ATOM   1331 O  O     . LEU A 1 195 ? -23.778 -6.088  8.195   1.00 15.15 ? 175 LEU A O     1 
ATOM   1332 C  CB    . LEU A 1 195 ? -22.183 -7.973  6.519   1.00 14.99 ? 175 LEU A CB    1 
ATOM   1333 C  CG    . LEU A 1 195 ? -20.845 -7.905  7.261   1.00 15.91 ? 175 LEU A CG    1 
ATOM   1334 C  CD1   . LEU A 1 195 ? -20.580 -9.190  8.037   1.00 16.88 ? 175 LEU A CD1   1 
ATOM   1335 C  CD2   . LEU A 1 195 ? -19.704 -7.609  6.299   1.00 15.59 ? 175 LEU A CD2   1 
ATOM   1336 N  N     . ALA A 1 196 ? -23.936 -7.816  9.647   1.00 15.27 ? 176 ALA A N     1 
ATOM   1337 C  CA    . ALA A 1 196 ? -24.496 -7.014  10.732  1.00 16.10 ? 176 ALA A CA    1 
ATOM   1338 C  C     . ALA A 1 196 ? -23.663 -5.779  11.050  1.00 15.85 ? 176 ALA A C     1 
ATOM   1339 O  O     . ALA A 1 196 ? -24.217 -4.702  11.290  1.00 16.53 ? 176 ALA A O     1 
ATOM   1340 C  CB    . ALA A 1 196 ? -24.635 -7.873  11.987  1.00 17.95 ? 176 ALA A CB    1 
ATOM   1341 N  N     . VAL A 1 197 ? -22.335 -5.909  11.079  1.00 14.91 ? 177 VAL A N     1 
ATOM   1342 C  CA    . VAL A 1 197 ? -21.514 -4.784  11.513  1.00 15.02 ? 177 VAL A CA    1 
ATOM   1343 C  C     . VAL A 1 197 ? -21.687 -3.594  10.582  1.00 15.20 ? 177 VAL A C     1 
ATOM   1344 O  O     . VAL A 1 197 ? -21.621 -2.442  11.014  1.00 15.71 ? 177 VAL A O     1 
ATOM   1345 C  CB    . VAL A 1 197 ? -20.046 -5.209  11.699  1.00 15.98 ? 177 VAL A CB    1 
ATOM   1346 C  CG1   . VAL A 1 197 ? -19.436 -5.670  10.382  1.00 16.41 ? 177 VAL A CG1   1 
ATOM   1347 C  CG2   . VAL A 1 197 ? -19.233 -4.077  12.326  1.00 17.51 ? 177 VAL A CG2   1 
ATOM   1348 N  N     . LEU A 1 198 ? -21.946 -3.845  9.298   1.00 14.15 ? 178 LEU A N     1 
ATOM   1349 C  CA    . LEU A 1 198 ? -22.170 -2.744  8.364   1.00 14.74 ? 178 LEU A CA    1 
ATOM   1350 C  C     . LEU A 1 198 ? -23.407 -1.942  8.756   1.00 14.80 ? 178 LEU A C     1 
ATOM   1351 O  O     . LEU A 1 198 ? -23.385 -0.703  8.776   1.00 15.81 ? 178 LEU A O     1 
ATOM   1352 C  CB    . LEU A 1 198 ? -22.336 -3.291  6.944   1.00 14.77 ? 178 LEU A CB    1 
ATOM   1353 C  CG    . LEU A 1 198 ? -21.204 -4.122  6.362   1.00 14.86 ? 178 LEU A CG    1 
ATOM   1354 C  CD1   . LEU A 1 198 ? -21.571 -4.533  4.936   1.00 15.26 ? 178 LEU A CD1   1 
ATOM   1355 C  CD2   . LEU A 1 198 ? -19.885 -3.369  6.348   1.00 15.43 ? 178 LEU A CD2   1 
ATOM   1356 N  N     . LYS A 1 199 ? -24.505 -2.633  9.065   1.00 16.38 ? 179 LYS A N     1 
ATOM   1357 C  CA    . LYS A 1 199 ? -25.723 -1.937  9.460   1.00 17.23 ? 179 LYS A CA    1 
ATOM   1358 C  C     . LYS A 1 199 ? -25.543 -1.225  10.794  1.00 17.38 ? 179 LYS A C     1 
ATOM   1359 O  O     . LYS A 1 199 ? -26.034 -0.107  10.979  1.00 18.37 ? 179 LYS A O     1 
ATOM   1360 C  CB    . LYS A 1 199 ? -26.871 -2.931  9.562   1.00 18.70 ? 179 LYS A CB    1 
ATOM   1361 C  CG    . LYS A 1 199 ? -28.233 -2.284  9.824   1.00 21.49 ? 179 LYS A CG    1 
ATOM   1362 C  CD    . LYS A 1 199 ? -29.376 -3.278  9.720   1.00 24.43 ? 179 LYS A CD    1 
ATOM   1363 N  N     . GLU A 1 200 ? -24.848 -1.867  11.735  1.00 16.60 ? 180 GLU A N     1 
ATOM   1364 C  CA    . GLU A 1 200 ? -24.650 -1.280  13.058  1.00 18.37 ? 180 GLU A CA    1 
ATOM   1365 C  C     . GLU A 1 200 ? -23.832 0.002   12.986  1.00 18.07 ? 180 GLU A C     1 
ATOM   1366 O  O     . GLU A 1 200 ? -24.121 0.970   13.697  1.00 19.04 ? 180 GLU A O     1 
ATOM   1367 C  CB    . GLU A 1 200 ? -24.003 -2.325  13.968  1.00 21.94 ? 180 GLU A CB    1 
ATOM   1368 C  CG    . GLU A 1 200 ? -24.920 -3.542  14.216  1.00 25.63 ? 180 GLU A CG    1 
ATOM   1369 C  CD    . GLU A 1 200 ? -24.206 -4.803  14.735  1.00 30.72 ? 180 GLU A CD    1 
ATOM   1370 O  OE1   . GLU A 1 200 ? -22.951 -4.891  14.684  1.00 32.94 ? 180 GLU A OE1   1 
ATOM   1371 O  OE2   . GLU A 1 200 ? -24.927 -5.728  15.177  1.00 32.06 ? 180 GLU A OE2   1 
ATOM   1372 N  N     . VAL A 1 201 ? -22.808 0.032   12.132  1.00 16.98 ? 181 VAL A N     1 
ATOM   1373 C  CA    . VAL A 1 201 ? -21.954 1.208   12.016  1.00 17.15 ? 181 VAL A CA    1 
ATOM   1374 C  C     . VAL A 1 201 ? -22.560 2.240   11.084  1.00 17.52 ? 181 VAL A C     1 
ATOM   1375 O  O     . VAL A 1 201 ? -22.348 3.443   11.271  1.00 20.36 ? 181 VAL A O     1 
ATOM   1376 C  CB    . VAL A 1 201 ? -20.525 0.815   11.597  1.00 16.89 ? 181 VAL A CB    1 
ATOM   1377 C  CG1   . VAL A 1 201 ? -19.663 2.038   11.382  1.00 18.73 ? 181 VAL A CG1   1 
ATOM   1378 C  CG2   . VAL A 1 201 ? -19.902 -0.120  12.640  1.00 16.74 ? 181 VAL A CG2   1 
ATOM   1379 N  N     . GLY A 1 202 ? -23.355 1.808   10.107  1.00 16.64 ? 182 GLY A N     1 
ATOM   1380 C  CA    . GLY A 1 202 ? -23.942 2.712   9.147   1.00 17.22 ? 182 GLY A CA    1 
ATOM   1381 C  C     . GLY A 1 202 ? -23.128 2.892   7.880   1.00 17.44 ? 182 GLY A C     1 
ATOM   1382 O  O     . GLY A 1 202 ? -23.093 3.995   7.324   1.00 20.90 ? 182 GLY A O     1 
ATOM   1383 N  N     . VAL A 1 203 ? -22.481 1.828   7.399   1.00 15.96 ? 183 VAL A N     1 
ATOM   1384 C  CA    . VAL A 1 203 ? -21.656 1.883   6.196   1.00 15.62 ? 183 VAL A CA    1 
ATOM   1385 C  C     . VAL A 1 203 ? -22.022 0.742   5.256   1.00 15.44 ? 183 VAL A C     1 
ATOM   1386 O  O     . VAL A 1 203 ? -22.599 -0.269  5.658   1.00 17.09 ? 183 VAL A O     1 
ATOM   1387 C  CB    . VAL A 1 203 ? -20.145 1.818   6.511   1.00 16.60 ? 183 VAL A CB    1 
ATOM   1388 C  CG1   . VAL A 1 203 ? -19.685 3.058   7.297   1.00 17.77 ? 183 VAL A CG1   1 
ATOM   1389 C  CG2   . VAL A 1 203 ? -19.812 0.549   7.282   1.00 16.85 ? 183 VAL A CG2   1 
ATOM   1390 N  N     . VAL A 1 204 ? -21.657 0.910   3.984   1.00 14.79 ? 184 VAL A N     1 
ATOM   1391 C  CA    . VAL A 1 204 ? -21.660 -0.213  3.054   1.00 13.48 ? 184 VAL A CA    1 
ATOM   1392 C  C     . VAL A 1 204 ? -20.309 -0.908  3.130   1.00 13.16 ? 184 VAL A C     1 
ATOM   1393 O  O     . VAL A 1 204 ? -19.361 -0.403  3.740   1.00 14.31 ? 184 VAL A O     1 
ATOM   1394 C  CB    . VAL A 1 204 ? -21.988 0.192   1.603   1.00 14.96 ? 184 VAL A CB    1 
ATOM   1395 C  CG1   . VAL A 1 204 ? -23.383 0.802   1.528   1.00 16.44 ? 184 VAL A CG1   1 
ATOM   1396 C  CG2   . VAL A 1 204 ? -20.913 1.112   1.028   1.00 16.74 ? 184 VAL A CG2   1 
ATOM   1397 N  N     . ASP A 1 205 ? -20.202 -2.064  2.490   1.00 13.15 ? 185 ASP A N     1 
ATOM   1398 C  CA    . ASP A 1 205 ? -18.955 -2.806  2.534   1.00 13.17 ? 185 ASP A CA    1 
ATOM   1399 C  C     . ASP A 1 205 ? -17.838 -2.081  1.795   1.00 13.08 ? 185 ASP A C     1 
ATOM   1400 O  O     . ASP A 1 205 ? -17.986 -1.719  0.629   1.00 13.24 ? 185 ASP A O     1 
ATOM   1401 C  CB    . ASP A 1 205 ? -19.125 -4.187  1.926   1.00 13.48 ? 185 ASP A CB    1 
ATOM   1402 C  CG    . ASP A 1 205 ? -17.878 -4.997  2.077   1.00 13.80 ? 185 ASP A CG    1 
ATOM   1403 O  OD1   . ASP A 1 205 ? -17.547 -5.342  3.236   1.00 15.45 ? 185 ASP A OD1   1 
ATOM   1404 O  OD2   . ASP A 1 205 ? -17.230 -5.260  1.061   1.00 14.28 ? 185 ASP A OD2   1 
ATOM   1405 N  N     . SER A 1 206 ? -16.680 -1.955  2.432   1.00 12.75 ? 186 SER A N     1 
ATOM   1406 C  CA    . SER A 1 206 ? -15.572 -1.216  1.829   1.00 12.91 ? 186 SER A CA    1 
ATOM   1407 C  C     . SER A 1 206 ? -15.001 -1.940  0.617   1.00 13.20 ? 186 SER A C     1 
ATOM   1408 O  O     . SER A 1 206 ? -14.708 -1.304  -0.396  1.00 13.74 ? 186 SER A O     1 
ATOM   1409 C  CB    . SER A 1 206 ? -14.485 -0.943  2.871   1.00 14.13 ? 186 SER A CB    1 
ATOM   1410 O  OG    . SER A 1 206 ? -14.036 -2.149  3.468   1.00 15.43 ? 186 SER A OG    1 
ATOM   1411 N  N     . GLY A 1 207 ? -14.816 -3.258  0.696   1.00 13.03 ? 187 GLY A N     1 
ATOM   1412 C  CA    . GLY A 1 207 ? -14.326 -3.979  -0.472  1.00 12.80 ? 187 GLY A CA    1 
ATOM   1413 C  C     . GLY A 1 207 ? -15.263 -3.841  -1.657  1.00 12.93 ? 187 GLY A C     1 
ATOM   1414 O  O     . GLY A 1 207 ? -14.827 -3.615  -2.793  1.00 13.18 ? 187 GLY A O     1 
ATOM   1415 N  N     . GLY A 1 208 ? -16.564 -3.985  -1.414  1.00 12.50 ? 188 GLY A N     1 
ATOM   1416 C  CA    . GLY A 1 208 ? -17.535 -3.779  -2.481  1.00 12.56 ? 188 GLY A CA    1 
ATOM   1417 C  C     . GLY A 1 208 ? -17.495 -2.377  -3.062  1.00 12.81 ? 188 GLY A C     1 
ATOM   1418 O  O     . GLY A 1 208 ? -17.629 -2.189  -4.277  1.00 13.12 ? 188 GLY A O     1 
ATOM   1419 N  N     . LYS A 1 209 ? -17.307 -1.372  -2.211  1.00 12.90 ? 189 LYS A N     1 
ATOM   1420 C  CA    . LYS A 1 209 ? -17.189 -0.007  -2.706  1.00 13.70 ? 189 LYS A CA    1 
ATOM   1421 C  C     . LYS A 1 209 ? -15.963 0.149   -3.589  1.00 13.27 ? 189 LYS A C     1 
ATOM   1422 O  O     . LYS A 1 209 ? -16.023 0.800   -4.641  1.00 14.03 ? 189 LYS A O     1 
ATOM   1423 C  CB    . LYS A 1 209 ? -17.138 0.965   -1.527  1.00 14.54 ? 189 LYS A CB    1 
ATOM   1424 C  CG    . LYS A 1 209 ? -17.101 2.432   -1.916  1.00 17.10 ? 189 LYS A CG    1 
ATOM   1425 C  CD    . LYS A 1 209 ? -18.379 2.888   -2.574  1.00 19.77 ? 189 LYS A CD    1 
ATOM   1426 C  CE    . LYS A 1 209 ? -18.450 4.408   -2.668  1.00 22.65 ? 189 LYS A CE    1 
ATOM   1427 N  NZ    . LYS A 1 209 ? -19.671 4.849   -3.397  1.00 24.17 ? 189 LYS A NZ    1 
ATOM   1428 N  N     . GLY A 1 210 ? -14.832 -0.431  -3.181  1.00 13.09 ? 190 GLY A N     1 
ATOM   1429 C  CA    . GLY A 1 210 ? -13.653 -0.377  -4.031  1.00 13.52 ? 190 GLY A CA    1 
ATOM   1430 C  C     . GLY A 1 210 ? -13.878 -1.037  -5.376  1.00 12.90 ? 190 GLY A C     1 
ATOM   1431 O  O     . GLY A 1 210 ? -13.426 -0.538  -6.408  1.00 13.11 ? 190 GLY A O     1 
ATOM   1432 N  N     . LEU A 1 211 ? -14.588 -2.163  -5.383  1.00 13.02 ? 191 LEU A N     1 
ATOM   1433 C  CA    . LEU A 1 211 ? -14.889 -2.832  -6.645  1.00 12.49 ? 191 LEU A CA    1 
ATOM   1434 C  C     . LEU A 1 211 ? -15.757 -1.955  -7.544  1.00 13.54 ? 191 LEU A C     1 
ATOM   1435 O  O     . LEU A 1 211 ? -15.534 -1.879  -8.763  1.00 13.50 ? 191 LEU A O     1 
ATOM   1436 C  CB    . LEU A 1 211 ? -15.564 -4.170  -6.360  1.00 12.99 ? 191 LEU A CB    1 
ATOM   1437 C  CG    . LEU A 1 211 ? -15.824 -5.049  -7.583  1.00 13.96 ? 191 LEU A CG    1 
ATOM   1438 C  CD1   . LEU A 1 211 ? -14.518 -5.472  -8.241  1.00 15.46 ? 191 LEU A CD1   1 
ATOM   1439 C  CD2   . LEU A 1 211 ? -16.655 -6.231  -7.212  1.00 15.45 ? 191 LEU A CD2   1 
ATOM   1440 N  N     . LEU A 1 212 ? -16.763 -1.296  -6.970  1.00 13.77 ? 192 LEU A N     1 
ATOM   1441 C  CA    . LEU A 1 212 ? -17.587 -0.387  -7.755  1.00 14.17 ? 192 LEU A CA    1 
ATOM   1442 C  C     . LEU A 1 212 ? -16.754 0.729   -8.362  1.00 14.00 ? 192 LEU A C     1 
ATOM   1443 O  O     . LEU A 1 212 ? -16.995 1.138   -9.506  1.00 14.84 ? 192 LEU A O     1 
ATOM   1444 C  CB    . LEU A 1 212 ? -18.703 0.207   -6.904  1.00 15.67 ? 192 LEU A CB    1 
ATOM   1445 C  CG    . LEU A 1 212 ? -20.104 -0.353  -7.126  1.00 17.27 ? 192 LEU A CG    1 
ATOM   1446 C  CD1   . LEU A 1 212 ? -20.557 -0.189  -8.567  1.00 18.17 ? 192 LEU A CD1   1 
ATOM   1447 C  CD2   . LEU A 1 212 ? -20.123 -1.810  -6.680  1.00 17.61 ? 192 LEU A CD2   1 
ATOM   1448 N  N     . CYS A 1 213 ? -15.757 1.228   -7.625  1.00 14.22 ? 193 CYS A N     1 
ATOM   1449 C  CA    . CYS A 1 213 ? -14.885 2.259   -8.181  1.00 15.15 ? 193 CYS A CA    1 
ATOM   1450 C  C     . CYS A 1 213 ? -14.191 1.756   -9.437  1.00 14.30 ? 193 CYS A C     1 
ATOM   1451 O  O     . CYS A 1 213 ? -14.115 2.465   -10.451 1.00 14.63 ? 193 CYS A O     1 
ATOM   1452 C  CB    . CYS A 1 213 ? -13.831 2.671   -7.153  1.00 16.54 ? 193 CYS A CB    1 
ATOM   1453 S  SG    . CYS A 1 213 ? -14.437 3.604   -5.751  1.00 19.84 ? 193 CYS A SG    1 
ATOM   1454 N  N     . VAL A 1 214 ? -13.705 0.518   -9.406  1.00 13.89 ? 194 VAL A N     1 
ATOM   1455 C  CA    . VAL A 1 214 ? -13.066 -0.058  -10.586 1.00 13.53 ? 194 VAL A CA    1 
ATOM   1456 C  C     . VAL A 1 214 ? -14.065 -0.169  -11.727 1.00 13.29 ? 194 VAL A C     1 
ATOM   1457 O  O     . VAL A 1 214 ? -13.771 0.200   -12.868 1.00 13.91 ? 194 VAL A O     1 
ATOM   1458 C  CB    . VAL A 1 214 ? -12.439 -1.419  -10.236 1.00 13.73 ? 194 VAL A CB    1 
ATOM   1459 C  CG1   . VAL A 1 214 ? -11.912 -2.095  -11.482 1.00 14.58 ? 194 VAL A CG1   1 
ATOM   1460 C  CG2   . VAL A 1 214 ? -11.314 -1.247  -9.210  1.00 14.89 ? 194 VAL A CG2   1 
ATOM   1461 N  N     . TYR A 1 215 ? -15.262 -0.679  -11.443 1.00 13.17 ? 195 TYR A N     1 
ATOM   1462 C  CA    . TYR A 1 215 ? -16.263 -0.866  -12.489 1.00 13.94 ? 195 TYR A CA    1 
ATOM   1463 C  C     . TYR A 1 215 ? -16.667 0.463   -13.116 1.00 13.73 ? 195 TYR A C     1 
ATOM   1464 O  O     . TYR A 1 215 ? -16.883 0.540   -14.332 1.00 14.33 ? 195 TYR A O     1 
ATOM   1465 C  CB    . TYR A 1 215 ? -17.496 -1.575  -11.932 1.00 13.78 ? 195 TYR A CB    1 
ATOM   1466 C  CG    . TYR A 1 215 ? -17.326 -3.051  -11.625 1.00 14.43 ? 195 TYR A CG    1 
ATOM   1467 C  CD1   . TYR A 1 215 ? -16.148 -3.729  -11.896 1.00 15.84 ? 195 TYR A CD1   1 
ATOM   1468 C  CD2   . TYR A 1 215 ? -18.355 -3.764  -11.026 1.00 16.46 ? 195 TYR A CD2   1 
ATOM   1469 C  CE1   . TYR A 1 215 ? -16.012 -5.082  -11.613 1.00 17.28 ? 195 TYR A CE1   1 
ATOM   1470 C  CE2   . TYR A 1 215 ? -18.227 -5.115  -10.725 1.00 17.32 ? 195 TYR A CE2   1 
ATOM   1471 C  CZ    . TYR A 1 215 ? -17.054 -5.767  -11.027 1.00 18.39 ? 195 TYR A CZ    1 
ATOM   1472 O  OH    . TYR A 1 215 ? -16.939 -7.108  -10.753 1.00 20.45 ? 195 TYR A OH    1 
ATOM   1473 N  N     A GLU A 1 216 ? -16.749 1.528   -12.319 0.50 14.84 ? 196 GLU A N     1 
ATOM   1474 N  N     B GLU A 1 216 ? -16.800 1.517   -12.308 0.50 13.86 ? 196 GLU A N     1 
ATOM   1475 C  CA    A GLU A 1 216 ? -17.132 2.823   -12.878 0.50 16.57 ? 196 GLU A CA    1 
ATOM   1476 C  CA    B GLU A 1 216 ? -17.125 2.821   -12.875 0.50 14.45 ? 196 GLU A CA    1 
ATOM   1477 C  C     A GLU A 1 216 ? -16.029 3.397   -13.760 0.50 16.03 ? 196 GLU A C     1 
ATOM   1478 C  C     B GLU A 1 216 ? -16.040 3.261   -13.847 0.50 14.53 ? 196 GLU A C     1 
ATOM   1479 O  O     A GLU A 1 216 ? -16.317 4.143   -14.704 0.50 16.67 ? 196 GLU A O     1 
ATOM   1480 O  O     B GLU A 1 216 ? -16.337 3.785   -14.927 0.50 14.12 ? 196 GLU A O     1 
ATOM   1481 C  CB    A GLU A 1 216 ? -17.566 3.767   -11.755 0.50 19.85 ? 196 GLU A CB    1 
ATOM   1482 C  CB    B GLU A 1 216 ? -17.328 3.859   -11.771 0.50 16.19 ? 196 GLU A CB    1 
ATOM   1483 C  CG    A GLU A 1 216 ? -18.836 3.249   -11.077 0.50 23.27 ? 196 GLU A CG    1 
ATOM   1484 C  CG    B GLU A 1 216 ? -18.589 3.636   -10.941 0.50 18.50 ? 196 GLU A CG    1 
ATOM   1485 C  CD    A GLU A 1 216 ? -19.443 4.199   -10.068 0.50 27.05 ? 196 GLU A CD    1 
ATOM   1486 C  CD    B GLU A 1 216 ? -19.852 4.206   -11.570 0.50 21.40 ? 196 GLU A CD    1 
ATOM   1487 O  OE1   A GLU A 1 216 ? -18.732 5.097   -9.567  0.50 28.53 ? 196 GLU A OE1   1 
ATOM   1488 O  OE1   B GLU A 1 216 ? -19.865 4.508   -12.781 0.50 23.06 ? 196 GLU A OE1   1 
ATOM   1489 O  OE2   A GLU A 1 216 ? -20.648 4.032   -9.770  0.50 28.85 ? 196 GLU A OE2   1 
ATOM   1490 O  OE2   B GLU A 1 216 ? -20.846 4.357   -10.833 0.50 22.04 ? 196 GLU A OE2   1 
ATOM   1491 N  N     . GLY A 1 217 ? -14.773 3.036   -13.495 1.00 14.75 ? 197 GLY A N     1 
ATOM   1492 C  CA    . GLY A 1 217 ? -13.698 3.364   -14.421 1.00 15.05 ? 197 GLY A CA    1 
ATOM   1493 C  C     . GLY A 1 217 ? -13.753 2.542   -15.697 1.00 14.61 ? 197 GLY A C     1 
ATOM   1494 O  O     . GLY A 1 217 ? -13.464 3.052   -16.781 1.00 15.09 ? 197 GLY A O     1 
ATOM   1495 N  N     . PHE A 1 218 ? -14.104 1.255   -15.587 1.00 15.09 ? 198 PHE A N     1 
ATOM   1496 C  CA    . PHE A 1 218 ? -14.304 0.439   -16.781 1.00 14.26 ? 198 PHE A CA    1 
ATOM   1497 C  C     . PHE A 1 218 ? -15.275 1.140   -17.720 1.00 14.41 ? 198 PHE A C     1 
ATOM   1498 O  O     . PHE A 1 218 ? -15.064 1.199   -18.936 1.00 14.76 ? 198 PHE A O     1 
ATOM   1499 C  CB    . PHE A 1 218 ? -14.894 -0.930  -16.426 1.00 14.08 ? 198 PHE A CB    1 
ATOM   1500 C  CG    . PHE A 1 218 ? -13.901 -1.958  -15.932 1.00 14.36 ? 198 PHE A CG    1 
ATOM   1501 C  CD1   . PHE A 1 218 ? -12.621 -1.622  -15.538 1.00 14.09 ? 198 PHE A CD1   1 
ATOM   1502 C  CD2   . PHE A 1 218 ? -14.265 -3.296  -15.915 1.00 16.94 ? 198 PHE A CD2   1 
ATOM   1503 C  CE1   . PHE A 1 218 ? -11.723 -2.605  -15.097 1.00 15.64 ? 198 PHE A CE1   1 
ATOM   1504 C  CE2   . PHE A 1 218 ? -13.379 -4.270  -15.472 1.00 18.19 ? 198 PHE A CE2   1 
ATOM   1505 C  CZ    . PHE A 1 218 ? -12.103 -3.913  -15.062 1.00 17.79 ? 198 PHE A CZ    1 
ATOM   1506 N  N     . LEU A 1 219 ? -16.375 1.652   -17.173 1.00 14.76 ? 199 LEU A N     1 
ATOM   1507 C  CA    . LEU A 1 219 ? -17.392 2.273   -18.015 1.00 15.48 ? 199 LEU A CA    1 
ATOM   1508 C  C     . LEU A 1 219 ? -16.854 3.529   -18.680 1.00 15.79 ? 199 LEU A C     1 
ATOM   1509 O  O     . LEU A 1 219 ? -17.088 3.755   -19.870 1.00 16.26 ? 199 LEU A O     1 
ATOM   1510 C  CB    . LEU A 1 219 ? -18.635 2.597   -17.187 1.00 16.37 ? 199 LEU A CB    1 
ATOM   1511 C  CG    . LEU A 1 219 ? -19.754 3.339   -17.924 1.00 17.97 ? 199 LEU A CG    1 
ATOM   1512 C  CD1   . LEU A 1 219 ? -20.291 2.511   -19.077 1.00 18.84 ? 199 LEU A CD1   1 
ATOM   1513 C  CD2   . LEU A 1 219 ? -20.863 3.689   -16.951 1.00 18.06 ? 199 LEU A CD2   1 
ATOM   1514 N  N     . LYS A 1 220 ? -16.142 4.368   -17.933 1.00 15.97 ? 200 LYS A N     1 
ATOM   1515 C  CA    . LYS A 1 220 ? -15.541 5.551   -18.536 1.00 17.71 ? 200 LYS A CA    1 
ATOM   1516 C  C     . LYS A 1 220 ? -14.679 5.161   -19.733 1.00 16.98 ? 200 LYS A C     1 
ATOM   1517 O  O     . LYS A 1 220 ? -14.756 5.780   -20.800 1.00 17.94 ? 200 LYS A O     1 
ATOM   1518 C  CB    . LYS A 1 220 ? -14.706 6.289   -17.491 1.00 21.07 ? 200 LYS A CB    1 
ATOM   1519 C  CG    . LYS A 1 220 ? -15.533 6.946   -16.403 1.00 25.74 ? 200 LYS A CG    1 
ATOM   1520 C  CD    . LYS A 1 220 ? -16.110 8.271   -16.845 1.00 30.59 ? 200 LYS A CD    1 
ATOM   1521 C  CE    . LYS A 1 220 ? -15.077 9.381   -16.755 1.00 33.84 ? 200 LYS A CE    1 
ATOM   1522 N  NZ    . LYS A 1 220 ? -15.698 10.719  -16.906 1.00 36.10 ? 200 LYS A NZ    1 
ATOM   1523 N  N     . ALA A 1 221 ? -13.845 4.132   -19.574 1.00 16.08 ? 201 ALA A N     1 
ATOM   1524 C  CA    . ALA A 1 221 ? -12.972 3.718   -20.675 1.00 15.75 ? 201 ALA A CA    1 
ATOM   1525 C  C     . ALA A 1 221 ? -13.772 3.216   -21.871 1.00 15.63 ? 201 ALA A C     1 
ATOM   1526 O  O     . ALA A 1 221 ? -13.421 3.498   -23.025 1.00 16.34 ? 201 ALA A O     1 
ATOM   1527 C  CB    . ALA A 1 221 ? -12.026 2.618   -20.190 1.00 15.70 ? 201 ALA A CB    1 
ATOM   1528 N  N     . LEU A 1 222 ? -14.847 2.473   -21.627 1.00 15.32 ? 202 LEU A N     1 
ATOM   1529 C  CA    . LEU A 1 222 ? -15.662 1.982   -22.729 1.00 15.32 ? 202 LEU A CA    1 
ATOM   1530 C  C     . LEU A 1 222 ? -16.271 3.130   -23.511 1.00 17.14 ? 202 LEU A C     1 
ATOM   1531 O  O     . LEU A 1 222 ? -16.472 3.008   -24.721 1.00 18.38 ? 202 LEU A O     1 
ATOM   1532 C  CB    . LEU A 1 222 ? -16.765 1.067   -22.204 1.00 15.70 ? 202 LEU A CB    1 
ATOM   1533 C  CG    . LEU A 1 222 ? -16.313 -0.311  -21.716 1.00 15.44 ? 202 LEU A CG    1 
ATOM   1534 C  CD1   . LEU A 1 222 ? -17.415 -0.994  -20.903 1.00 15.52 ? 202 LEU A CD1   1 
ATOM   1535 C  CD2   . LEU A 1 222 ? -15.894 -1.196  -22.882 1.00 16.93 ? 202 LEU A CD2   1 
ATOM   1536 N  N     . LYS A 1 223 ? -16.576 4.240   -22.840 1.00 17.31 ? 203 LYS A N     1 
ATOM   1537 C  CA    . LYS A 1 223 ? -17.092 5.439   -23.491 1.00 18.89 ? 203 LYS A CA    1 
ATOM   1538 C  C     . LYS A 1 223 ? -15.992 6.294   -24.110 1.00 19.44 ? 203 LYS A C     1 
ATOM   1539 O  O     . LYS A 1 223 ? -16.290 7.368   -24.649 1.00 21.73 ? 203 LYS A O     1 
ATOM   1540 C  CB    . LYS A 1 223 ? -17.848 6.289   -22.474 1.00 20.64 ? 203 LYS A CB    1 
ATOM   1541 C  CG    . LYS A 1 223 ? -19.087 5.626   -21.924 1.00 22.70 ? 203 LYS A CG    1 
ATOM   1542 C  CD    . LYS A 1 223 ? -19.739 6.531   -20.883 1.00 26.40 ? 203 LYS A CD    1 
ATOM   1543 C  CE    . LYS A 1 223 ? -20.976 5.927   -20.258 1.00 30.16 ? 203 LYS A CE    1 
ATOM   1544 N  NZ    . LYS A 1 223 ? -21.498 6.779   -19.146 1.00 32.43 ? 203 LYS A NZ    1 
ATOM   1545 N  N     . GLY A 1 224 ? -14.737 5.857   -24.045 1.00 18.50 ? 204 GLY A N     1 
ATOM   1546 C  CA    . GLY A 1 224 ? -13.645 6.657   -24.564 1.00 19.55 ? 204 GLY A CA    1 
ATOM   1547 C  C     . GLY A 1 224 ? -13.320 7.876   -23.735 1.00 21.24 ? 204 GLY A C     1 
ATOM   1548 O  O     . GLY A 1 224 ? -12.754 8.843   -24.258 1.00 23.87 ? 204 GLY A O     1 
ATOM   1549 N  N     . GLU A 1 225 ? -13.650 7.853   -22.449 1.00 21.04 ? 205 GLU A N     1 
ATOM   1550 C  CA    . GLU A 1 225 ? -13.446 8.974   -21.547 1.00 22.36 ? 205 GLU A CA    1 
ATOM   1551 C  C     . GLU A 1 225 ? -12.343 8.629   -20.553 1.00 22.80 ? 205 GLU A C     1 
ATOM   1552 O  O     . GLU A 1 225 ? -11.965 7.464   -20.384 1.00 21.61 ? 205 GLU A O     1 
ATOM   1553 C  CB    . GLU A 1 225 ? -14.756 9.302   -20.813 1.00 24.32 ? 205 GLU A CB    1 
ATOM   1554 C  CG    . GLU A 1 225 ? -15.876 9.723   -21.772 1.00 26.68 ? 205 GLU A CG    1 
ATOM   1555 C  CD    . GLU A 1 225 ? -17.215 10.005  -21.100 1.00 28.98 ? 205 GLU A CD    1 
ATOM   1556 O  OE1   . GLU A 1 225 ? -17.258 10.202  -19.865 1.00 31.13 ? 205 GLU A OE1   1 
ATOM   1557 O  OE2   . GLU A 1 225 ? -18.234 10.029  -21.828 1.00 28.77 ? 205 GLU A OE2   1 
ATOM   1558 N  N     . LYS A 1 226 ? -11.814 9.653   -19.893 1.00 24.94 ? 206 LYS A N     1 
ATOM   1559 C  CA    . LYS A 1 226 ? -10.766 9.453   -18.905 1.00 28.05 ? 206 LYS A CA    1 
ATOM   1560 C  C     . LYS A 1 226 ? -11.243 9.925   -17.538 1.00 29.06 ? 206 LYS A C     1 
ATOM   1561 O  O     . LYS A 1 226 ? -12.025 10.871  -17.425 1.00 30.53 ? 206 LYS A O     1 
ATOM   1562 C  CB    . LYS A 1 226 ? -9.473  10.181  -19.302 1.00 29.99 ? 206 LYS A CB    1 
ATOM   1563 C  CG    . LYS A 1 226 ? -8.856  9.642   -20.590 1.00 30.62 ? 206 LYS A CG    1 
ATOM   1564 N  N     . VAL A 1 227 ? -10.785 9.234   -16.503 1.00 28.39 ? 207 VAL A N     1 
ATOM   1565 C  CA    . VAL A 1 227 ? -11.035 9.648   -15.128 1.00 30.44 ? 207 VAL A CA    1 
ATOM   1566 C  C     . VAL A 1 227 ? -10.076 10.778  -14.781 1.00 35.12 ? 207 VAL A C     1 
ATOM   1567 O  O     . VAL A 1 227 ? -8.861  10.659  -14.973 1.00 35.70 ? 207 VAL A O     1 
ATOM   1568 C  CB    . VAL A 1 227 ? -10.853 8.455   -14.178 1.00 28.63 ? 207 VAL A CB    1 
ATOM   1569 C  CG1   . VAL A 1 227 ? -10.920 8.912   -12.744 1.00 27.78 ? 207 VAL A CG1   1 
ATOM   1570 C  CG2   . VAL A 1 227 ? -11.918 7.414   -14.435 1.00 28.72 ? 207 VAL A CG2   1 
ATOM   1571 N  N     . GLU A 1 228 ? -10.616 11.883  -14.276 1.00 38.84 ? 208 GLU A N     1 
ATOM   1572 C  CA    . GLU A 1 228 ? -9.767  12.985  -13.847 1.00 42.64 ? 208 GLU A CA    1 
ATOM   1573 C  C     . GLU A 1 228 ? -8.995  12.560  -12.605 1.00 44.96 ? 208 GLU A C     1 
ATOM   1574 O  O     . GLU A 1 228 ? -9.585  12.075  -11.640 1.00 45.16 ? 208 GLU A O     1 
ATOM   1575 C  CB    . GLU A 1 228 ? -10.620 14.213  -13.534 1.00 43.37 ? 208 GLU A CB    1 
ATOM   1576 N  N     . ALA A 1 229 ? -7.676  12.728  -12.630 1.00 47.38 ? 209 ALA A N     1 
ATOM   1577 C  CA    . ALA A 1 229 ? -6.846  12.320  -11.503 1.00 49.53 ? 209 ALA A CA    1 
ATOM   1578 C  C     . ALA A 1 229 ? -6.940  13.339  -10.369 1.00 50.72 ? 209 ALA A C     1 
ATOM   1579 O  O     . ALA A 1 229 ? -6.683  14.529  -10.570 1.00 51.12 ? 209 ALA A O     1 
ATOM   1580 C  CB    . ALA A 1 229 ? -5.395  12.174  -11.956 1.00 49.83 ? 209 ALA A CB    1 
ATOM   1581 N  N     . LYS A 1 230 ? -7.293  12.867  -9.175  1.00 51.30 ? 210 LYS A N     1 
ATOM   1582 C  CA    . LYS A 1 230 ? -7.453  13.743  -8.017  1.00 52.26 ? 210 LYS A CA    1 
ATOM   1583 C  C     . LYS A 1 230 ? -6.093  14.219  -7.526  1.00 53.16 ? 210 LYS A C     1 
ATOM   1584 O  O     . LYS A 1 230 ? -5.121  14.221  -8.281  1.00 53.71 ? 210 LYS A O     1 
ATOM   1585 C  CB    . LYS A 1 230 ? -8.188  13.017  -6.886  1.00 52.28 ? 210 LYS A CB    1 
HETATM 1586 P  PB    . ADP B 2 .   ? -7.948  -6.695  5.970   1.00 15.38 ? 301 ADP A PB    1 
HETATM 1587 O  O1B   . ADP B 2 .   ? -6.845  -7.543  5.370   1.00 15.71 ? 301 ADP A O1B   1 
HETATM 1588 O  O2B   . ADP B 2 .   ? -8.787  -7.374  7.032   1.00 16.65 ? 301 ADP A O2B   1 
HETATM 1589 O  O3B   . ADP B 2 .   ? -7.516  -5.299  6.311   1.00 15.06 ? 301 ADP A O3B   1 
HETATM 1590 P  PA    . ADP B 2 .   ? -9.286  -5.224  3.831   1.00 14.41 ? 301 ADP A PA    1 
HETATM 1591 O  O1A   . ADP B 2 .   ? -8.221  -5.149  2.771   1.00 15.10 ? 301 ADP A O1A   1 
HETATM 1592 O  O2A   . ADP B 2 .   ? -9.563  -4.008  4.680   1.00 13.96 ? 301 ADP A O2A   1 
HETATM 1593 O  O3A   . ADP B 2 .   ? -9.039  -6.516  4.760   1.00 14.58 ? 301 ADP A O3A   1 
HETATM 1594 O  "O5'" . ADP B 2 .   ? -10.638 -5.615  3.064   1.00 13.36 ? 301 ADP A "O5'" 1 
HETATM 1595 C  "C5'" . ADP B 2 .   ? -11.870 -5.737  3.778   1.00 13.70 ? 301 ADP A "C5'" 1 
HETATM 1596 C  "C4'" . ADP B 2 .   ? -12.869 -6.305  2.792   1.00 13.45 ? 301 ADP A "C4'" 1 
HETATM 1597 O  "O4'" . ADP B 2 .   ? -12.456 -7.619  2.401   1.00 13.77 ? 301 ADP A "O4'" 1 
HETATM 1598 C  "C3'" . ADP B 2 .   ? -14.265 -6.468  3.355   1.00 13.69 ? 301 ADP A "C3'" 1 
HETATM 1599 O  "O3'" . ADP B 2 .   ? -14.961 -5.221  3.364   1.00 15.21 ? 301 ADP A "O3'" 1 
HETATM 1600 C  "C2'" . ADP B 2 .   ? -14.824 -7.530  2.425   1.00 13.90 ? 301 ADP A "C2'" 1 
HETATM 1601 O  "O2'" . ADP B 2 .   ? -15.255 -6.966  1.190   1.00 13.11 ? 301 ADP A "O2'" 1 
HETATM 1602 C  "C1'" . ADP B 2 .   ? -13.605 -8.401  2.121   1.00 13.70 ? 301 ADP A "C1'" 1 
HETATM 1603 N  N9    . ADP B 2 .   ? -13.536 -9.615  2.947   1.00 13.60 ? 301 ADP A N9    1 
HETATM 1604 C  C8    . ADP B 2 .   ? -12.824 -9.811  4.087   1.00 15.41 ? 301 ADP A C8    1 
HETATM 1605 N  N7    . ADP B 2 .   ? -13.051 -11.059 4.553   1.00 15.82 ? 301 ADP A N7    1 
HETATM 1606 C  C5    . ADP B 2 .   ? -13.930 -11.650 3.712   1.00 14.63 ? 301 ADP A C5    1 
HETATM 1607 C  C6    . ADP B 2 .   ? -14.600 -12.934 3.628   1.00 14.55 ? 301 ADP A C6    1 
HETATM 1608 N  N6    . ADP B 2 .   ? -14.398 -13.909 4.524   1.00 16.24 ? 301 ADP A N6    1 
HETATM 1609 N  N1    . ADP B 2 .   ? -15.459 -13.135 2.624   1.00 14.39 ? 301 ADP A N1    1 
HETATM 1610 C  C2    . ADP B 2 .   ? -15.686 -12.192 1.682   1.00 14.29 ? 301 ADP A C2    1 
HETATM 1611 N  N3    . ADP B 2 .   ? -15.107 -10.985 1.684   1.00 13.74 ? 301 ADP A N3    1 
HETATM 1612 C  C4    . ADP B 2 .   ? -14.243 -10.682 2.682   1.00 13.85 ? 301 ADP A C4    1 
HETATM 1613 MG MG    . MG  C 3 .   ? -8.789  -3.638  6.552   1.00 15.36 ? 302 MG  A MG    1 
HETATM 1614 MG MG    . MG  D 3 .   ? -5.551  -4.845  7.215   1.00 17.14 ? 303 MG  A MG    1 
HETATM 1615 C  C2    . PG4 E 4 .   ? -20.659 3.890   -6.583  1.00 44.94 ? 304 PG4 A C2    1 
HETATM 1616 O  O2    . PG4 E 4 .   ? -19.465 3.680   -5.836  1.00 44.01 ? 304 PG4 A O2    1 
HETATM 1617 C  C3    . PG4 E 4 .   ? -18.275 3.893   -6.591  1.00 42.93 ? 304 PG4 A C3    1 
HETATM 1618 C  C4    . PG4 E 4 .   ? -17.999 5.359   -6.733  1.00 42.10 ? 304 PG4 A C4    1 
HETATM 1619 O  O3    . PG4 E 4 .   ? -17.812 5.943   -5.448  1.00 41.24 ? 304 PG4 A O3    1 
HETATM 1620 C  C5    . PG4 E 4 .   ? -17.497 7.329   -5.519  1.00 40.95 ? 304 PG4 A C5    1 
HETATM 1621 C  C6    . PG4 E 4 .   ? -17.607 7.956   -4.163  1.00 41.17 ? 304 PG4 A C6    1 
HETATM 1622 O  O4    . PG4 E 4 .   ? -18.902 7.711   -3.626  1.00 41.61 ? 304 PG4 A O4    1 
HETATM 1623 C  C7    . PG4 E 4 .   ? -19.208 8.542   -2.512  1.00 42.78 ? 304 PG4 A C7    1 
HETATM 1624 C  C8    . PG4 E 4 .   ? -20.463 8.066   -1.851  1.00 43.47 ? 304 PG4 A C8    1 
HETATM 1625 O  O5    . PG4 E 4 .   ? -20.314 6.778   -1.286  1.00 44.13 ? 304 PG4 A O5    1 
HETATM 1626 O  O     . HOH F 5 .   ? -17.072 6.763   -10.050 1.00 34.30 ? 401 HOH A O     1 
HETATM 1627 O  O     . HOH F 5 .   ? -30.925 -11.851 -11.368 1.00 34.08 ? 402 HOH A O     1 
HETATM 1628 O  O     . HOH F 5 .   ? 0.148   -5.729  -35.076 1.00 31.54 ? 403 HOH A O     1 
HETATM 1629 O  O     . HOH F 5 .   ? -17.533 1.556   -31.876 1.00 28.03 ? 404 HOH A O     1 
HETATM 1630 O  O     . HOH F 5 .   ? -4.504  2.674   6.432   1.00 43.94 ? 405 HOH A O     1 
HETATM 1631 O  O     . HOH F 5 .   ? -14.198 -13.352 7.948   1.00 40.78 ? 406 HOH A O     1 
HETATM 1632 O  O     . HOH F 5 .   ? -22.734 -14.765 -10.199 1.00 22.95 ? 407 HOH A O     1 
HETATM 1633 O  O     . HOH F 5 .   ? -11.166 1.183   9.268   1.00 21.51 ? 408 HOH A O     1 
HETATM 1634 O  O     . HOH F 5 .   ? -17.884 4.373   -32.608 1.00 20.68 ? 409 HOH A O     1 
HETATM 1635 O  O     . HOH F 5 .   ? -9.866  -17.991 -23.816 1.00 28.09 ? 410 HOH A O     1 
HETATM 1636 O  O     . HOH F 5 .   ? -1.552  -16.808 -17.255 1.00 43.36 ? 411 HOH A O     1 
HETATM 1637 O  O     . HOH F 5 .   ? -7.821  -8.654  9.099   1.00 34.51 ? 412 HOH A O     1 
HETATM 1638 O  O     . HOH F 5 .   ? -13.630 -13.858 -28.768 1.00 39.61 ? 413 HOH A O     1 
HETATM 1639 O  O     . HOH F 5 .   ? -31.165 1.092   -8.764  1.00 38.88 ? 414 HOH A O     1 
HETATM 1640 O  O     . HOH F 5 .   ? 1.051   -4.109  -4.126  1.00 33.36 ? 415 HOH A O     1 
HETATM 1641 O  O     . HOH F 5 .   ? -17.940 9.757   -24.440 1.00 31.30 ? 416 HOH A O     1 
HETATM 1642 O  O     . HOH F 5 .   ? 4.068   1.041   -22.955 1.00 39.02 ? 417 HOH A O     1 
HETATM 1643 O  O     . HOH F 5 .   ? 1.506   -1.324  -5.876  1.00 33.65 ? 418 HOH A O     1 
HETATM 1644 O  O     . HOH F 5 .   ? -2.943  5.140   -24.131 1.00 32.94 ? 419 HOH A O     1 
HETATM 1645 O  O     . HOH F 5 .   ? -6.010  5.623   0.820   1.00 36.55 ? 420 HOH A O     1 
HETATM 1646 O  O     . HOH F 5 .   ? -7.440  5.377   -25.249 1.00 27.12 ? 421 HOH A O     1 
HETATM 1647 O  O     . HOH F 5 .   ? -19.140 9.206   -18.254 1.00 47.29 ? 422 HOH A O     1 
HETATM 1648 O  O     . HOH F 5 .   ? -15.664 12.225  -19.142 1.00 38.66 ? 423 HOH A O     1 
HETATM 1649 O  O     . HOH F 5 .   ? -12.642 9.772   -9.724  1.00 30.29 ? 424 HOH A O     1 
HETATM 1650 O  O     . HOH F 5 .   ? -7.188  8.736   -15.909 1.00 35.07 ? 425 HOH A O     1 
HETATM 1651 O  O     . HOH F 5 .   ? -23.820 3.089   -26.124 1.00 46.48 ? 426 HOH A O     1 
HETATM 1652 O  O     . HOH F 5 .   ? -14.062 -21.835 -0.722  1.00 31.37 ? 427 HOH A O     1 
HETATM 1653 O  O     . HOH F 5 .   ? -5.761  1.774   -8.165  1.00 20.84 ? 428 HOH A O     1 
HETATM 1654 O  O     . HOH F 5 .   ? -21.322 5.735   10.319  1.00 27.28 ? 429 HOH A O     1 
HETATM 1655 O  O     . HOH F 5 .   ? -20.727 -7.573  -28.245 1.00 18.55 ? 430 HOH A O     1 
HETATM 1656 O  O     . HOH F 5 .   ? -15.706 -4.462  13.237  1.00 20.21 ? 431 HOH A O     1 
HETATM 1657 O  O     . HOH F 5 .   ? -17.266 -1.460  5.295   1.00 13.87 ? 432 HOH A O     1 
HETATM 1658 O  O     . HOH F 5 .   ? -25.709 -13.305 -1.429  1.00 32.96 ? 433 HOH A O     1 
HETATM 1659 O  O     . HOH F 5 .   ? -30.213 -8.952  -14.042 1.00 24.81 ? 434 HOH A O     1 
HETATM 1660 O  O     . HOH F 5 .   ? -23.516 4.717   -10.766 1.00 40.37 ? 435 HOH A O     1 
HETATM 1661 O  O     . HOH F 5 .   ? -21.187 -17.286 3.899   1.00 26.09 ? 436 HOH A O     1 
HETATM 1662 O  O     . HOH F 5 .   ? -5.894  4.617   7.363   1.00 36.02 ? 437 HOH A O     1 
HETATM 1663 O  O     . HOH F 5 .   ? -4.691  -15.017 -17.768 1.00 21.46 ? 438 HOH A O     1 
HETATM 1664 O  O     . HOH F 5 .   ? -21.081 -17.353 1.059   1.00 26.00 ? 439 HOH A O     1 
HETATM 1665 O  O     . HOH F 5 .   ? -4.196  -14.727 -26.546 1.00 28.68 ? 440 HOH A O     1 
HETATM 1666 O  O     . HOH F 5 .   ? -1.154  -13.947 -5.267  1.00 15.47 ? 441 HOH A O     1 
HETATM 1667 O  O     . HOH F 5 .   ? -18.501 5.834   -14.708 1.00 23.01 ? 442 HOH A O     1 
HETATM 1668 O  O     . HOH F 5 .   ? -4.765  -5.820  5.564   1.00 16.17 ? 443 HOH A O     1 
HETATM 1669 O  O     . HOH F 5 .   ? -25.296 -14.020 -21.523 1.00 31.73 ? 444 HOH A O     1 
HETATM 1670 O  O     . HOH F 5 .   ? -6.877  -7.363  -31.451 1.00 27.76 ? 445 HOH A O     1 
HETATM 1671 O  O     . HOH F 5 .   ? -5.456  -9.545  6.576   1.00 37.96 ? 446 HOH A O     1 
HETATM 1672 O  O     . HOH F 5 .   ? -9.554  -19.971 -21.067 1.00 48.20 ? 447 HOH A O     1 
HETATM 1673 O  O     . HOH F 5 .   ? -28.457 -6.393  8.918   1.00 18.55 ? 448 HOH A O     1 
HETATM 1674 O  O     . HOH F 5 .   ? 0.564   -7.666  -22.530 1.00 21.94 ? 449 HOH A O     1 
HETATM 1675 O  O     . HOH F 5 .   ? -8.075  -16.750 0.502   1.00 29.32 ? 450 HOH A O     1 
HETATM 1676 O  O     . HOH F 5 .   ? -21.998 10.723  -34.274 1.00 38.16 ? 451 HOH A O     1 
HETATM 1677 O  O     . HOH F 5 .   ? -26.725 0.466   -26.628 1.00 36.55 ? 452 HOH A O     1 
HETATM 1678 O  O     . HOH F 5 .   ? -14.561 -8.339  -11.284 1.00 24.23 ? 453 HOH A O     1 
HETATM 1679 O  O     . HOH F 5 .   ? -21.751 -17.444 -9.058  1.00 43.48 ? 454 HOH A O     1 
HETATM 1680 O  O     . HOH F 5 .   ? -30.592 -6.045  -7.314  1.00 28.20 ? 455 HOH A O     1 
HETATM 1681 O  O     . HOH F 5 .   ? -4.768  2.220   9.150   1.00 22.33 ? 456 HOH A O     1 
HETATM 1682 O  O     . HOH F 5 .   ? -5.724  9.443   -6.966  1.00 32.67 ? 457 HOH A O     1 
HETATM 1683 O  O     . HOH F 5 .   ? -31.359 -8.147  6.959   1.00 16.00 ? 458 HOH A O     1 
HETATM 1684 O  O     . HOH F 5 .   ? -25.258 -10.581 -27.108 1.00 37.15 ? 459 HOH A O     1 
HETATM 1685 O  O     . HOH F 5 .   ? -10.160 -4.958  7.490   1.00 14.16 ? 460 HOH A O     1 
HETATM 1686 O  O     . HOH F 5 .   ? -6.438  6.622   4.399   1.00 31.26 ? 461 HOH A O     1 
HETATM 1687 O  O     . HOH F 5 .   ? -25.261 1.432   16.166  1.00 24.53 ? 462 HOH A O     1 
HETATM 1688 O  O     . HOH F 5 .   ? -33.026 -5.938  0.364   1.00 25.41 ? 463 HOH A O     1 
HETATM 1689 O  O     . HOH F 5 .   ? -5.661  -13.335 -19.839 1.00 16.63 ? 464 HOH A O     1 
HETATM 1690 O  O     . HOH F 5 .   ? -22.726 -12.024 6.438   1.00 15.00 ? 465 HOH A O     1 
HETATM 1691 O  O     . HOH F 5 .   ? -22.247 -10.564 -27.543 1.00 30.52 ? 466 HOH A O     1 
HETATM 1692 O  O     . HOH F 5 .   ? -0.405  -14.265 -16.038 1.00 33.55 ? 467 HOH A O     1 
HETATM 1693 O  O     . HOH F 5 .   ? -24.999 2.728   -14.724 1.00 27.53 ? 468 HOH A O     1 
HETATM 1694 O  O     . HOH F 5 .   ? -27.836 -8.882  -9.785  1.00 20.81 ? 469 HOH A O     1 
HETATM 1695 O  O     . HOH F 5 .   ? -2.918  -2.711  5.094   1.00 33.06 ? 470 HOH A O     1 
HETATM 1696 O  O     . HOH F 5 .   ? -16.089 -10.912 -11.321 1.00 16.64 ? 471 HOH A O     1 
HETATM 1697 O  O     . HOH F 5 .   ? -30.377 -2.266  -2.879  1.00 25.65 ? 472 HOH A O     1 
HETATM 1698 O  O     . HOH F 5 .   ? 3.552   -1.842  -7.875  1.00 46.53 ? 473 HOH A O     1 
HETATM 1699 O  O     . HOH F 5 .   ? -13.547 10.021  -2.421  1.00 34.82 ? 474 HOH A O     1 
HETATM 1700 O  O     . HOH F 5 .   ? -18.398 -9.444  -11.224 1.00 15.95 ? 475 HOH A O     1 
HETATM 1701 O  O     . HOH F 5 .   ? -23.819 2.732   -4.337  1.00 44.03 ? 476 HOH A O     1 
HETATM 1702 O  O     . HOH F 5 .   ? -9.542  2.686   11.621  1.00 15.85 ? 477 HOH A O     1 
HETATM 1703 O  O     . HOH F 5 .   ? -3.881  -13.557 -4.586  1.00 14.44 ? 478 HOH A O     1 
HETATM 1704 O  O     . HOH F 5 .   ? -11.296 -18.694 -15.075 1.00 21.51 ? 479 HOH A O     1 
HETATM 1705 O  O     . HOH F 5 .   ? -10.885 4.282   -23.932 1.00 19.65 ? 480 HOH A O     1 
HETATM 1706 O  O     . HOH F 5 .   ? -16.995 4.650   -26.936 1.00 27.71 ? 481 HOH A O     1 
HETATM 1707 O  O     . HOH F 5 .   ? -19.549 6.996   -17.134 1.00 33.99 ? 482 HOH A O     1 
HETATM 1708 O  O     . HOH F 5 .   ? -27.402 -6.536  14.109  1.00 25.22 ? 483 HOH A O     1 
HETATM 1709 O  O     . HOH F 5 .   ? -12.198 -12.381 6.887   1.00 30.29 ? 484 HOH A O     1 
HETATM 1710 O  O     . HOH F 5 .   ? -28.312 1.241   -8.681  1.00 25.14 ? 485 HOH A O     1 
HETATM 1711 O  O     . HOH F 5 .   ? -9.037  7.440   5.176   1.00 26.26 ? 486 HOH A O     1 
HETATM 1712 O  O     . HOH F 5 .   ? -27.173 1.074   2.092   1.00 28.82 ? 487 HOH A O     1 
HETATM 1713 O  O     . HOH F 5 .   ? -28.036 -6.757  -7.897  1.00 19.36 ? 488 HOH A O     1 
HETATM 1714 O  O     . HOH F 5 .   ? 4.202   -5.426  -7.197  1.00 42.54 ? 489 HOH A O     1 
HETATM 1715 O  O     . HOH F 5 .   ? -27.040 -9.197  -2.251  1.00 26.60 ? 490 HOH A O     1 
HETATM 1716 O  O     . HOH F 5 .   ? -18.311 -18.198 -16.880 1.00 27.19 ? 491 HOH A O     1 
HETATM 1717 O  O     . HOH F 5 .   ? -6.086  4.694   -20.823 1.00 29.11 ? 492 HOH A O     1 
HETATM 1718 O  O     . HOH F 5 .   ? -28.035 -0.385  -19.616 1.00 25.29 ? 493 HOH A O     1 
HETATM 1719 O  O     . HOH F 5 .   ? -27.188 1.497   8.923   1.00 32.79 ? 494 HOH A O     1 
HETATM 1720 O  O     . HOH F 5 .   ? -17.140 -21.064 -6.639  1.00 55.72 ? 495 HOH A O     1 
HETATM 1721 O  O     . HOH F 5 .   ? -1.352  5.151   -18.989 1.00 37.39 ? 496 HOH A O     1 
HETATM 1722 O  O     . HOH F 5 .   ? -32.077 -7.868  -10.351 1.00 35.80 ? 497 HOH A O     1 
HETATM 1723 O  O     . HOH F 5 .   ? 3.882   -4.250  -11.141 1.00 34.01 ? 498 HOH A O     1 
HETATM 1724 O  O     . HOH F 5 .   ? -10.287 -20.858 -11.186 1.00 35.64 ? 499 HOH A O     1 
HETATM 1725 O  O     . HOH F 5 .   ? -5.343  -15.249 -15.141 1.00 18.30 ? 500 HOH A O     1 
HETATM 1726 O  O     . HOH F 5 .   ? -13.311 -19.611 -13.146 1.00 21.69 ? 501 HOH A O     1 
HETATM 1727 O  O     . HOH F 5 .   ? -5.464  -6.677  8.247   1.00 18.28 ? 502 HOH A O     1 
HETATM 1728 O  O     . HOH F 5 .   ? -6.354  -19.397 -13.300 1.00 18.87 ? 503 HOH A O     1 
HETATM 1729 O  O     . HOH F 5 .   ? -14.558 -15.912 7.419   1.00 32.22 ? 504 HOH A O     1 
HETATM 1730 O  O     . HOH F 5 .   ? -10.018 5.805   -21.710 1.00 27.50 ? 505 HOH A O     1 
HETATM 1731 O  O     . HOH F 5 .   ? -26.136 -7.442  -1.157  1.00 28.68 ? 506 HOH A O     1 
HETATM 1732 O  O     . HOH F 5 .   ? 2.879   -8.927  -15.711 1.00 34.57 ? 507 HOH A O     1 
HETATM 1733 O  O     . HOH F 5 .   ? -11.493 -17.435 4.771   1.00 24.04 ? 508 HOH A O     1 
HETATM 1734 O  O     . HOH F 5 .   ? -23.004 -10.414 10.514  1.00 18.94 ? 509 HOH A O     1 
HETATM 1735 O  O     . HOH F 5 .   ? -13.791 9.769   -26.799 1.00 37.75 ? 510 HOH A O     1 
HETATM 1736 O  O     . HOH F 5 .   ? -4.418  -4.546  11.070  1.00 32.75 ? 511 HOH A O     1 
HETATM 1737 O  O     . HOH F 5 .   ? -15.393 -3.471  5.815   1.00 14.97 ? 512 HOH A O     1 
HETATM 1738 O  O     . HOH F 5 .   ? -10.678 -13.633 -30.224 1.00 28.54 ? 513 HOH A O     1 
HETATM 1739 O  O     . HOH F 5 .   ? -4.807  7.535   -3.506  1.00 42.94 ? 514 HOH A O     1 
HETATM 1740 O  O     . HOH F 5 .   ? -15.224 8.888   -8.357  1.00 35.38 ? 515 HOH A O     1 
HETATM 1741 O  O     . HOH F 5 .   ? -28.236 -6.007  -28.827 1.00 36.64 ? 516 HOH A O     1 
HETATM 1742 O  O     . HOH F 5 .   ? -21.189 -8.555  11.580  1.00 18.35 ? 517 HOH A O     1 
HETATM 1743 O  O     . HOH F 5 .   ? 1.313   -11.497 -21.697 1.00 32.43 ? 518 HOH A O     1 
HETATM 1744 O  O     . HOH F 5 .   ? -21.633 -7.480  14.279  1.00 33.71 ? 519 HOH A O     1 
HETATM 1745 O  O     . HOH F 5 .   ? -4.778  8.370   -14.993 1.00 41.94 ? 520 HOH A O     1 
HETATM 1746 O  O     . HOH F 5 .   ? 4.659   -6.311  -4.815  1.00 43.68 ? 521 HOH A O     1 
HETATM 1747 O  O     . HOH F 5 .   ? -19.223 6.832   -35.036 1.00 29.89 ? 522 HOH A O     1 
HETATM 1748 O  O     . HOH F 5 .   ? -3.993  -10.759 -31.709 1.00 30.29 ? 523 HOH A O     1 
HETATM 1749 O  O     . HOH F 5 .   ? -8.049  8.879   -1.983  1.00 29.01 ? 524 HOH A O     1 
HETATM 1750 O  O     . HOH F 5 .   ? -5.583  -14.839 -29.730 1.00 31.19 ? 525 HOH A O     1 
HETATM 1751 O  O     . HOH F 5 .   ? -18.668 -8.753  -31.429 1.00 43.02 ? 526 HOH A O     1 
HETATM 1752 O  O     . HOH F 5 .   ? -5.317  7.962   -18.519 1.00 41.31 ? 527 HOH A O     1 
HETATM 1753 O  O     . HOH F 5 .   ? -9.361  -17.606 2.989   1.00 23.88 ? 528 HOH A O     1 
HETATM 1754 O  O     . HOH F 5 .   ? -1.405  -14.719 -13.839 1.00 30.02 ? 529 HOH A O     1 
HETATM 1755 O  O     . HOH F 5 .   ? -19.935 -11.257 -31.511 1.00 40.29 ? 530 HOH A O     1 
HETATM 1756 O  O     . HOH F 5 .   ? -26.994 -3.478  -27.433 1.00 33.70 ? 531 HOH A O     1 
HETATM 1757 O  O     . HOH F 5 .   ? -14.913 8.403   -12.756 1.00 37.22 ? 532 HOH A O     1 
HETATM 1758 O  O     . HOH F 5 .   ? -26.897 -15.761 -5.254  1.00 42.15 ? 533 HOH A O     1 
HETATM 1759 O  O     . HOH F 5 .   ? -22.733 -14.754 -21.349 1.00 37.92 ? 534 HOH A O     1 
HETATM 1760 O  O     . HOH F 5 .   ? -11.142 9.379   -1.154  1.00 25.68 ? 535 HOH A O     1 
HETATM 1761 O  O     . HOH F 5 .   ? -28.315 -12.298 -4.444  1.00 40.19 ? 536 HOH A O     1 
HETATM 1762 O  O     . HOH F 5 .   ? -4.094  4.763   -1.270  1.00 29.49 ? 537 HOH A O     1 
HETATM 1763 O  O     . HOH F 5 .   ? -30.901 -1.597  1.463   1.00 49.92 ? 538 HOH A O     1 
HETATM 1764 O  O     . HOH F 5 .   ? -12.243 -19.961 -17.391 1.00 28.65 ? 539 HOH A O     1 
HETATM 1765 O  O     . HOH F 5 .   ? -7.855  -11.550 8.108   1.00 33.32 ? 540 HOH A O     1 
HETATM 1766 O  O     . HOH F 5 .   ? -21.359 3.913   3.314   1.00 19.66 ? 541 HOH A O     1 
HETATM 1767 O  O     . HOH F 5 .   ? -12.792 -24.211 -3.327  1.00 34.41 ? 542 HOH A O     1 
HETATM 1768 O  O     . HOH F 5 .   ? -21.921 3.998   -1.437  1.00 37.58 ? 543 HOH A O     1 
HETATM 1769 O  O     . HOH F 5 .   ? -13.104 12.351  -20.723 1.00 34.33 ? 544 HOH A O     1 
HETATM 1770 O  O     . HOH F 5 .   ? -19.031 -12.564 9.952   1.00 43.47 ? 545 HOH A O     1 
HETATM 1771 O  O     . HOH F 5 .   ? -16.089 -13.012 -28.004 1.00 31.76 ? 546 HOH A O     1 
HETATM 1772 O  O     . HOH F 5 .   ? -25.385 0.826   6.634   1.00 24.93 ? 547 HOH A O     1 
HETATM 1773 O  O     . HOH F 5 .   ? -9.171  -19.213 -12.999 1.00 28.02 ? 548 HOH A O     1 
HETATM 1774 O  O     . HOH F 5 .   ? -3.505  3.576   -10.190 1.00 34.71 ? 549 HOH A O     1 
HETATM 1775 O  O     . HOH F 5 .   ? -31.562 -3.045  -0.395  1.00 34.49 ? 550 HOH A O     1 
HETATM 1776 O  O     . HOH F 5 .   ? 2.211   -8.732  -24.497 1.00 38.72 ? 551 HOH A O     1 
HETATM 1777 O  O     . HOH F 5 .   ? -6.877  -22.640 -11.581 1.00 42.20 ? 552 HOH A O     1 
HETATM 1778 O  O     . HOH F 5 .   ? -22.775 4.920   -14.454 1.00 48.47 ? 553 HOH A O     1 
HETATM 1779 O  O     . HOH F 5 .   ? -8.657  5.195   7.310   1.00 26.11 ? 554 HOH A O     1 
HETATM 1780 O  O     . HOH F 5 .   ? 1.624   -8.614  0.500   1.00 35.70 ? 555 HOH A O     1 
HETATM 1781 O  O     . HOH F 5 .   ? -11.119 -4.006  -31.360 1.00 23.64 ? 556 HOH A O     1 
HETATM 1782 O  O     . HOH F 5 .   ? -27.056 3.122   -9.899  1.00 39.83 ? 557 HOH A O     1 
HETATM 1783 O  O     . HOH F 5 .   ? -28.342 1.422   -5.855  1.00 32.78 ? 558 HOH A O     1 
HETATM 1784 O  O     . HOH F 5 .   ? -22.897 7.550   -37.690 1.00 51.50 ? 559 HOH A O     1 
HETATM 1785 O  O     . HOH F 5 .   ? -28.694 0.353   -16.920 1.00 30.65 ? 560 HOH A O     1 
HETATM 1786 O  O     . HOH F 5 .   ? -17.793 -19.507 -14.745 1.00 33.83 ? 561 HOH A O     1 
HETATM 1787 O  O     . HOH F 5 .   ? -5.367  -8.768  -33.002 1.00 49.25 ? 562 HOH A O     1 
HETATM 1788 O  O     . HOH F 5 .   ? -10.386 -14.605 3.918   1.00 35.35 ? 563 HOH A O     1 
HETATM 1789 O  O     . HOH F 5 .   ? -25.603 6.101   -35.928 1.00 35.41 ? 564 HOH A O     1 
HETATM 1790 O  O     . HOH F 5 .   ? -13.571 12.450  -23.386 1.00 38.73 ? 565 HOH A O     1 
HETATM 1791 O  O     . HOH F 5 .   ? -13.337 -23.651 0.391   1.00 46.05 ? 566 HOH A O     1 
HETATM 1792 O  O     . HOH F 5 .   ? -26.653 -14.767 -7.722  1.00 52.42 ? 567 HOH A O     1 
HETATM 1793 O  O     . HOH F 5 .   ? -16.893 -7.175  12.680  1.00 42.58 ? 568 HOH A O     1 
HETATM 1794 O  O     . HOH F 5 .   ? -7.301  6.628   -22.344 1.00 38.24 ? 569 HOH A O     1 
HETATM 1795 O  O     . HOH F 5 .   ? -24.341 4.131   3.706   1.00 51.05 ? 570 HOH A O     1 
HETATM 1796 O  O     . HOH F 5 .   ? -27.296 -11.769 -1.811  1.00 34.11 ? 571 HOH A O     1 
HETATM 1797 O  O     . HOH F 5 .   ? -17.386 7.622   -12.885 1.00 36.90 ? 572 HOH A O     1 
HETATM 1798 O  O     . HOH F 5 .   ? -9.703  -22.234 -8.702  1.00 32.44 ? 573 HOH A O     1 
HETATM 1799 O  O     . HOH F 5 .   ? -25.554 3.875   -12.264 1.00 41.00 ? 574 HOH A O     1 
HETATM 1800 O  O     . HOH F 5 .   ? -32.518 -3.613  -4.416  1.00 40.05 ? 575 HOH A O     1 
HETATM 1801 O  O     . HOH F 5 .   ? -4.498  -17.828 -14.425 1.00 22.41 ? 576 HOH A O     1 
HETATM 1802 O  O     . HOH F 5 .   ? -9.455  -14.729 1.620   1.00 31.13 ? 577 HOH A O     1 
HETATM 1803 O  O     . HOH F 5 .   ? -30.035 -9.153  -11.369 1.00 30.06 ? 578 HOH A O     1 
HETATM 1804 O  O     . HOH F 5 .   ? -25.820 2.315   4.367   1.00 34.03 ? 579 HOH A O     1 
HETATM 1805 O  O     . HOH F 5 .   ? -2.371  -17.169 -12.988 1.00 21.94 ? 580 HOH A O     1 
HETATM 1806 O  O     . HOH F 5 .   ? -30.426 0.313   -3.566  1.00 42.74 ? 581 HOH A O     1 
HETATM 1807 O  O     . HOH F 5 .   ? -15.477 -20.733 -14.340 1.00 33.60 ? 582 HOH A O     1 
HETATM 1808 O  O     . HOH F 5 .   ? -21.602 -12.281 9.034   1.00 20.21 ? 583 HOH A O     1 
HETATM 1809 O  O     . HOH F 5 .   ? -10.213 -18.642 7.135   1.00 32.55 ? 584 HOH A O     1 
HETATM 1810 O  O     . HOH F 5 .   ? -3.542  5.773   -20.667 1.00 40.39 ? 585 HOH A O     1 
HETATM 1811 O  O     . HOH F 5 .   ? -18.736 -9.329  11.908  1.00 35.91 ? 586 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . SER A 19  ? 0.7257 0.6642 0.5585 0.1481  0.0587  0.1509  -1  SER A N     
2    C  CA    . SER A 19  ? 0.7216 0.6552 0.5533 0.1395  0.0626  0.1522  -1  SER A CA    
3    C  C     . SER A 19  ? 0.6995 0.6332 0.5276 0.1271  0.0706  0.1514  -1  SER A C     
4    O  O     . SER A 19  ? 0.7057 0.6351 0.5281 0.1277  0.0865  0.1445  -1  SER A O     
5    C  CB    . SER A 19  ? 0.7333 0.6675 0.5679 0.1443  0.0591  0.1524  -1  SER A CB    
6    O  OG    . SER A 19  ? 0.7372 0.6725 0.5753 0.1560  0.0510  0.1563  -1  SER A OG    
7    N  N     . HIS A 20  ? 0.6715 0.6055 0.4936 0.1071  0.0663  0.1644  0   HIS A N     
8    C  CA    . HIS A 20  ? 0.6632 0.5879 0.4694 0.0770  0.0624  0.1633  0   HIS A CA    
9    C  C     . HIS A 20  ? 0.6481 0.5797 0.4380 0.0473  0.0568  0.1626  0   HIS A C     
10   O  O     . HIS A 20  ? 0.6837 0.5934 0.4573 0.0260  0.0544  0.1487  0   HIS A O     
11   C  CB    . HIS A 20  ? 0.6635 0.5861 0.4675 0.0832  0.0609  0.1630  0   HIS A CB    
12   N  N     . MET A 21  ? 0.5955 0.5624 0.3994 0.0526  0.0446  0.1640  1   MET A N     
13   C  CA    . MET A 21  ? 0.5497 0.5634 0.3664 0.0522  0.0299  0.1375  1   MET A CA    
14   C  C     . MET A 21  ? 0.4326 0.4937 0.2979 0.0551  0.0347  0.1445  1   MET A C     
15   O  O     . MET A 21  ? 0.4525 0.4972 0.3154 0.0564  0.0583  0.1807  1   MET A O     
16   C  CB    . MET A 21  ? 0.6216 0.6351 0.4069 0.0475  0.0191  0.1067  1   MET A CB    
17   C  CG    . MET A 21  ? 0.6906 0.7007 0.4297 0.0373  0.0249  0.0827  1   MET A CG    
18   S  SD    . MET A 21  ? 0.7587 0.7541 0.4511 0.0309  0.0293  0.0564  1   MET A SD    
19   C  CE    . MET A 21  ? 0.7680 0.7667 0.4510 0.0314  0.0246  0.0535  1   MET A CE    
20   N  N     . ILE A 22  ? 0.3184 0.4196 0.2226 0.0339  0.0144  0.1126  2   ILE A N     
21   C  CA    . ILE A 22  ? 0.2568 0.3820 0.1872 0.0023  0.0156  0.0772  2   ILE A CA    
22   C  C     . ILE A 22  ? 0.2460 0.3657 0.1719 -0.0178 -0.0005 0.0597  2   ILE A C     
23   O  O     . ILE A 22  ? 0.2976 0.3683 0.1615 -0.0322 0.0252  0.0561  2   ILE A O     
24   C  CB    . ILE A 22  ? 0.2355 0.3660 0.1808 -0.0046 0.0075  0.0641  2   ILE A CB    
25   C  CG1   . ILE A 22  ? 0.2509 0.3752 0.1832 -0.0179 0.0344  0.0581  2   ILE A CG1   
26   C  CG2   . ILE A 22  ? 0.2278 0.3583 0.1920 0.0034  0.0005  0.0651  2   ILE A CG2   
27   C  CD1   . ILE A 22  ? 0.2522 0.3817 0.1876 -0.0313 0.0426  0.0614  2   ILE A CD1   
28   N  N     . SER A 23  ? 0.2521 0.3512 0.1673 -0.0145 -0.0184 0.0449  3   SER A N     
29   C  CA    A SER A 23  ? 0.2812 0.3594 0.1766 -0.0209 -0.0250 0.0233  3   SER A CA    
30   C  CA    B SER A 23  ? 0.2697 0.3513 0.1801 -0.0137 -0.0254 0.0241  3   SER A CA    
31   C  C     . SER A 23  ? 0.2745 0.3456 0.1686 -0.0168 -0.0231 0.0272  3   SER A C     
32   O  O     . SER A 23  ? 0.3022 0.3625 0.2041 -0.0109 -0.0139 0.0375  3   SER A O     
33   C  CB    A SER A 23  ? 0.3228 0.3861 0.1976 -0.0194 -0.0508 0.0097  3   SER A CB    
34   C  CB    B SER A 23  ? 0.2869 0.3604 0.2084 0.0024  -0.0527 0.0110  3   SER A CB    
35   O  OG    A SER A 23  ? 0.3561 0.4068 0.2090 -0.0281 -0.0435 0.0089  3   SER A OG    
36   O  OG    B SER A 23  ? 0.3141 0.3628 0.2282 0.0161  -0.0609 0.0113  3   SER A OG    
37   N  N     . LYS A 24  ? 0.2785 0.3264 0.1568 0.0053  -0.0459 0.0098  4   LYS A N     
38   C  CA    . LYS A 24  ? 0.2769 0.3256 0.1824 0.0083  -0.0423 -0.0137 4   LYS A CA    
39   C  C     . LYS A 24  ? 0.2697 0.2793 0.1693 0.0080  -0.0365 -0.0050 4   LYS A C     
40   O  O     . LYS A 24  ? 0.2487 0.2663 0.1652 0.0001  -0.0385 0.0081  4   LYS A O     
41   C  CB    . LYS A 24  ? 0.3240 0.3695 0.2164 0.0126  -0.0430 -0.0389 4   LYS A CB    
42   C  CG    . LYS A 24  ? 0.3427 0.3882 0.2349 0.0173  -0.0306 -0.0586 4   LYS A CG    
43   N  N     . ILE A 25  ? 0.2401 0.2649 0.1563 0.0163  -0.0275 0.0032  5   ILE A N     
44   C  CA    . ILE A 25  ? 0.2222 0.2489 0.1347 -0.0012 -0.0264 0.0191  5   ILE A CA    
45   C  C     . ILE A 25  ? 0.2383 0.2365 0.1398 -0.0120 -0.0077 0.0257  5   ILE A C     
46   O  O     . ILE A 25  ? 0.2406 0.2263 0.1525 -0.0127 -0.0037 0.0202  5   ILE A O     
47   C  CB    . ILE A 25  ? 0.2092 0.2452 0.1342 -0.0106 -0.0160 0.0252  5   ILE A CB    
48   C  CG1   . ILE A 25  ? 0.2391 0.2534 0.1533 -0.0015 -0.0175 0.0119  5   ILE A CG1   
49   C  CG2   . ILE A 25  ? 0.2145 0.2416 0.1458 -0.0112 -0.0177 0.0186  5   ILE A CG2   
50   C  CD1   . ILE A 25  ? 0.2404 0.2756 0.1655 0.0111  -0.0135 -0.0043 5   ILE A CD1   
51   N  N     . ASN A 26  ? 0.2360 0.2359 0.1362 -0.0005 -0.0063 0.0158  6   ASN A N     
52   C  CA    . ASN A 26  ? 0.2451 0.2337 0.1144 0.0216  -0.0061 0.0275  6   ASN A CA    
53   C  C     . ASN A 26  ? 0.2357 0.2359 0.1136 0.0179  0.0076  0.0232  6   ASN A C     
54   O  O     . ASN A 26  ? 0.2181 0.2489 0.1120 0.0059  0.0135  0.0162  6   ASN A O     
55   C  CB    . ASN A 26  ? 0.2611 0.2542 0.1156 0.0169  -0.0033 0.0232  6   ASN A CB    
56   C  CG    . ASN A 26  ? 0.2620 0.2490 0.1139 -0.0010 -0.0031 0.0237  6   ASN A CG    
57   O  OD1   . ASN A 26  ? 0.2662 0.2433 0.1193 0.0116  0.0004  0.0216  6   ASN A OD1   
58   N  ND2   . ASN A 26  ? 0.3281 0.2690 0.1285 -0.0173 0.0154  0.0137  6   ASN A ND2   
59   N  N     . GLY A 27  ? 0.2271 0.2285 0.1141 0.0313  0.0127  0.0151  7   GLY A N     
60   C  CA    . GLY A 27  ? 0.2329 0.2238 0.1268 0.0194  0.0115  0.0218  7   GLY A CA    
61   C  C     . GLY A 27  ? 0.2084 0.2205 0.1178 0.0217  0.0213  0.0127  7   GLY A C     
62   O  O     . GLY A 27  ? 0.2374 0.2369 0.1178 0.0211  0.0189  0.0011  7   GLY A O     
63   N  N     . LYS A 28  ? 0.2043 0.2143 0.1212 0.0112  0.0129  0.0110  8   LYS A N     
64   C  CA    . LYS A 28  ? 0.1871 0.2113 0.1268 -0.0062 0.0136  0.0222  8   LYS A CA    
65   C  C     . LYS A 28  ? 0.1971 0.2112 0.1176 -0.0093 0.0072  0.0263  8   LYS A C     
66   O  O     . LYS A 28  ? 0.2218 0.2183 0.1215 -0.0058 0.0134  0.0106  8   LYS A O     
67   C  CB    . LYS A 28  ? 0.1945 0.2278 0.1469 0.0026  0.0207  0.0245  8   LYS A CB    
68   C  CG    . LYS A 28  ? 0.2130 0.2299 0.1551 -0.0143 0.0203  0.0380  8   LYS A CG    
69   C  CD    . LYS A 28  ? 0.2352 0.2400 0.1739 -0.0148 0.0198  0.0228  8   LYS A CD    
70   C  CE    . LYS A 28  ? 0.2641 0.2606 0.1926 -0.0190 0.0144  0.0256  8   LYS A CE    
71   N  NZ    . LYS A 28  ? 0.2832 0.2557 0.2022 -0.0107 0.0188  0.0423  8   LYS A NZ    
72   N  N     . LEU A 29  ? 0.1786 0.2145 0.1174 -0.0047 0.0177  0.0144  9   LEU A N     
73   C  CA    . LEU A 29  ? 0.1779 0.2209 0.1153 0.0044  0.0024  0.0265  9   LEU A CA    
74   C  C     . LEU A 29  ? 0.2053 0.2095 0.1108 -0.0044 0.0024  0.0218  9   LEU A C     
75   O  O     . LEU A 29  ? 0.2109 0.2138 0.1103 0.0031  0.0058  0.0047  9   LEU A O     
76   C  CB    . LEU A 29  ? 0.2082 0.2128 0.1174 0.0098  0.0283  0.0334  9   LEU A CB    
77   C  CG    . LEU A 29  ? 0.2203 0.2177 0.1467 0.0204  0.0224  0.0214  9   LEU A CG    
78   C  CD1   . LEU A 29  ? 0.2067 0.2270 0.1668 0.0442  0.0218  0.0085  9   LEU A CD1   
79   C  CD2   . LEU A 29  ? 0.2331 0.2388 0.1468 -0.0044 0.0082  0.0293  9   LEU A CD2   
80   N  N     . PHE A 30  ? 0.2358 0.2032 0.0914 0.0133  0.0063  0.0183  10  PHE A N     
81   C  CA    . PHE A 30  ? 0.2318 0.2060 0.1108 0.0103  0.0059  0.0315  10  PHE A CA    
82   C  C     . PHE A 30  ? 0.2163 0.2221 0.1164 0.0047  0.0123  0.0152  10  PHE A C     
83   O  O     . PHE A 30  ? 0.2138 0.2105 0.1105 0.0230  0.0191  0.0069  10  PHE A O     
84   C  CB    . PHE A 30  ? 0.2317 0.1984 0.1212 0.0159  -0.0022 0.0351  10  PHE A CB    
85   C  CG    . PHE A 30  ? 0.2170 0.2067 0.1291 0.0151  0.0066  0.0233  10  PHE A CG    
86   C  CD1   . PHE A 30  ? 0.2325 0.2229 0.1430 0.0076  0.0092  0.0306  10  PHE A CD1   
87   C  CD2   . PHE A 30  ? 0.2326 0.2220 0.1309 0.0018  -0.0149 0.0181  10  PHE A CD2   
88   C  CE1   . PHE A 30  ? 0.2405 0.2324 0.1465 0.0027  0.0011  0.0245  10  PHE A CE1   
89   C  CE2   . PHE A 30  ? 0.2410 0.2230 0.1454 0.0076  -0.0174 0.0280  10  PHE A CE2   
90   C  CZ    . PHE A 30  ? 0.2560 0.2223 0.1398 -0.0215 -0.0104 0.0292  10  PHE A CZ    
91   N  N     . ALA A 31  ? 0.1993 0.2264 0.1198 -0.0006 0.0106  0.0184  11  ALA A N     
92   C  CA    . ALA A 31  ? 0.2112 0.2216 0.1206 -0.0035 0.0228  0.0230  11  ALA A CA    
93   C  C     . ALA A 31  ? 0.2163 0.2116 0.1247 -0.0019 0.0305  0.0257  11  ALA A C     
94   O  O     . ALA A 31  ? 0.2150 0.2214 0.1331 -0.0048 0.0118  0.0070  11  ALA A O     
95   C  CB    . ALA A 31  ? 0.2334 0.2344 0.1311 0.0014  0.0257  0.0253  11  ALA A CB    
96   N  N     . ASP A 32  ? 0.2292 0.2155 0.1267 0.0172  0.0253  0.0229  12  ASP A N     
97   C  CA    . ASP A 32  ? 0.2389 0.2119 0.1201 0.0117  0.0254  0.0217  12  ASP A CA    
98   C  C     . ASP A 32  ? 0.2178 0.2071 0.1260 -0.0009 0.0245  0.0189  12  ASP A C     
99   O  O     . ASP A 32  ? 0.2195 0.2041 0.1369 0.0115  0.0227  0.0067  12  ASP A O     
100  C  CB    . ASP A 32  ? 0.2503 0.2208 0.1231 0.0244  0.0265  0.0252  12  ASP A CB    
101  C  CG    . ASP A 32  ? 0.2876 0.2445 0.1668 0.0080  0.0242  0.0384  12  ASP A CG    
102  O  OD1   . ASP A 32  ? 0.3134 0.2559 0.1984 -0.0058 0.0475  0.0489  12  ASP A OD1   
103  O  OD2   . ASP A 32  ? 0.2929 0.2716 0.1613 0.0150  0.0161  0.0417  12  ASP A OD2   
104  N  N     . MET A 33  ? 0.2210 0.2016 0.1261 -0.0173 0.0363  0.0190  13  MET A N     
105  C  CA    . MET A 33  ? 0.2094 0.2016 0.1233 -0.0118 0.0186  0.0212  13  MET A CA    
106  C  C     . MET A 33  ? 0.2090 0.2082 0.1210 -0.0118 0.0194  0.0156  13  MET A C     
107  O  O     . MET A 33  ? 0.1994 0.2094 0.1422 -0.0152 0.0347  -0.0039 13  MET A O     
108  C  CB    . MET A 33  ? 0.2087 0.2040 0.1351 0.0012  0.0132  0.0296  13  MET A CB    
109  C  CG    . MET A 33  ? 0.1949 0.2173 0.1459 -0.0071 0.0057  0.0291  13  MET A CG    
110  S  SD    . MET A 33  ? 0.2218 0.2354 0.1443 -0.0010 0.0011  -0.0062 13  MET A SD    
111  C  CE    . MET A 33  ? 0.2497 0.2468 0.1635 -0.0200 0.0054  -0.0004 13  MET A CE    
112  N  N     . ILE A 34  ? 0.2164 0.2093 0.1180 0.0069  0.0089  0.0101  14  ILE A N     
113  C  CA    . ILE A 34  ? 0.2045 0.2032 0.1317 -0.0008 0.0123  0.0170  14  ILE A CA    
114  C  C     . ILE A 34  ? 0.1977 0.2134 0.1325 -0.0211 0.0057  0.0061  14  ILE A C     
115  O  O     . ILE A 34  ? 0.2079 0.2356 0.1358 -0.0109 0.0039  -0.0036 14  ILE A O     
116  C  CB    . ILE A 34  ? 0.2146 0.2070 0.1395 0.0061  0.0030  0.0219  14  ILE A CB    
117  C  CG1   . ILE A 34  ? 0.2272 0.1957 0.1378 0.0098  -0.0033 0.0273  14  ILE A CG1   
118  C  CG2   . ILE A 34  ? 0.2295 0.2280 0.1411 0.0029  -0.0046 0.0057  14  ILE A CG2   
119  C  CD1   . ILE A 34  ? 0.2333 0.2062 0.1529 -0.0055 0.0110  0.0265  14  ILE A CD1   
120  N  N     . ILE A 35  ? 0.2113 0.2223 0.1446 -0.0324 0.0208  -0.0072 15  ILE A N     
121  C  CA    . ILE A 35  ? 0.2086 0.2322 0.1549 -0.0309 0.0281  -0.0050 15  ILE A CA    
122  C  C     . ILE A 35  ? 0.2083 0.2106 0.1486 -0.0223 0.0204  0.0062  15  ILE A C     
123  O  O     . ILE A 35  ? 0.2370 0.2184 0.1584 -0.0316 0.0261  -0.0234 15  ILE A O     
124  C  CB    . ILE A 35  ? 0.2477 0.2511 0.1697 -0.0387 0.0290  0.0068  15  ILE A CB    
125  C  CG1   . ILE A 35  ? 0.2348 0.2778 0.1852 -0.0396 0.0267  0.0053  15  ILE A CG1   
126  C  CG2   . ILE A 35  ? 0.2764 0.2652 0.1856 -0.0583 0.0256  0.0162  15  ILE A CG2   
127  C  CD1   . ILE A 35  ? 0.2881 0.2910 0.2050 -0.0331 0.0508  0.0079  15  ILE A CD1   
128  N  N     . GLN A 36  ? 0.2190 0.1926 0.1604 -0.0143 0.0143  0.0146  16  GLN A N     
129  C  CA    . GLN A 36  ? 0.2431 0.1908 0.1565 0.0033  0.0105  0.0184  16  GLN A CA    
130  C  C     . GLN A 36  ? 0.2370 0.1959 0.1490 -0.0208 0.0093  -0.0002 16  GLN A C     
131  O  O     . GLN A 36  ? 0.2460 0.1987 0.1361 -0.0178 0.0103  -0.0057 16  GLN A O     
132  C  CB    . GLN A 36  ? 0.2614 0.2000 0.1674 0.0004  0.0184  0.0226  16  GLN A CB    
133  C  CG    . GLN A 36  ? 0.2929 0.2113 0.1887 -0.0075 0.0231  0.0194  16  GLN A CG    
134  C  CD    . GLN A 36  ? 0.3373 0.2548 0.2145 -0.0271 0.0270  0.0161  16  GLN A CD    
135  O  OE1   . GLN A 36  ? 0.3620 0.2425 0.2373 -0.0156 0.0199  0.0213  16  GLN A OE1   
136  N  NE2   . GLN A 36  ? 0.3567 0.2938 0.2421 -0.0623 0.0292  0.0021  16  GLN A NE2   
137  N  N     . GLY A 37  ? 0.2377 0.1876 0.1369 -0.0211 0.0263  0.0077  17  GLY A N     
138  C  CA    . GLY A 37  ? 0.2380 0.1879 0.1326 -0.0092 0.0257  0.0106  17  GLY A CA    
139  C  C     . GLY A 37  ? 0.2264 0.2000 0.1311 -0.0071 0.0093  0.0039  17  GLY A C     
140  O  O     . GLY A 37  ? 0.2271 0.2106 0.1356 -0.0089 0.0228  -0.0087 17  GLY A O     
141  N  N     . ALA A 38  ? 0.2294 0.2108 0.1312 -0.0134 0.0123  -0.0025 18  ALA A N     
142  C  CA    . ALA A 38  ? 0.2113 0.2136 0.1499 -0.0278 0.0111  0.0032  18  ALA A CA    
143  C  C     . ALA A 38  ? 0.2143 0.2024 0.1488 -0.0273 0.0141  0.0036  18  ALA A C     
144  O  O     . ALA A 38  ? 0.2340 0.2213 0.1464 -0.0264 0.0153  -0.0033 18  ALA A O     
145  C  CB    . ALA A 38  ? 0.2249 0.2018 0.1459 -0.0323 0.0039  0.0042  18  ALA A CB    
146  N  N     . GLN A 39  ? 0.2391 0.2056 0.1591 -0.0241 0.0248  -0.0045 19  GLN A N     
147  C  CA    . GLN A 39  ? 0.2299 0.1987 0.1706 -0.0501 0.0218  -0.0026 19  GLN A CA    
148  C  C     . GLN A 39  ? 0.2590 0.2085 0.1617 -0.0570 0.0069  0.0006  19  GLN A C     
149  O  O     . GLN A 39  ? 0.2638 0.2266 0.1799 -0.0569 0.0122  -0.0190 19  GLN A O     
150  C  CB    . GLN A 39  ? 0.2610 0.2316 0.2081 -0.0571 0.0359  0.0017  19  GLN A CB    
151  C  CG    . GLN A 39  ? 0.3047 0.2647 0.2422 -0.0500 0.0454  -0.0042 19  GLN A CG    
152  C  CD    . GLN A 39  ? 0.3471 0.2966 0.2787 -0.0794 0.0536  -0.0337 19  GLN A CD    
153  O  OE1   . GLN A 39  ? 0.3796 0.3224 0.3053 -0.1066 0.0497  -0.0462 19  GLN A OE1   
154  N  NE2   . GLN A 39  ? 0.3694 0.3043 0.2906 -0.0746 0.0408  -0.0489 19  GLN A NE2   
155  N  N     . ASN A 40  ? 0.2458 0.1923 0.1712 -0.0467 0.0145  -0.0082 20  ASN A N     
156  C  CA    . ASN A 40  ? 0.2424 0.1981 0.1842 -0.0271 0.0147  -0.0136 20  ASN A CA    
157  C  C     . ASN A 40  ? 0.2567 0.1987 0.1739 -0.0248 0.0255  -0.0125 20  ASN A C     
158  O  O     . ASN A 40  ? 0.2754 0.1989 0.1771 0.0100  0.0345  -0.0228 20  ASN A O     
159  C  CB    . ASN A 40  ? 0.2478 0.2066 0.2136 -0.0167 0.0029  -0.0067 20  ASN A CB    
160  C  CG    . ASN A 40  ? 0.2762 0.2048 0.2543 -0.0162 0.0020  -0.0141 20  ASN A CG    
161  O  OD1   . ASN A 40  ? 0.2877 0.2154 0.3118 -0.0304 -0.0041 -0.0152 20  ASN A OD1   
162  N  ND2   . ASN A 40  ? 0.2879 0.2054 0.2509 -0.0091 0.0258  -0.0032 20  ASN A ND2   
163  N  N     . LEU A 41  ? 0.2366 0.1987 0.1481 -0.0221 0.0211  -0.0075 21  LEU A N     
164  C  CA    . LEU A 41  ? 0.2381 0.2071 0.1504 -0.0264 0.0136  -0.0088 21  LEU A CA    
165  C  C     . LEU A 41  ? 0.2418 0.2184 0.1594 -0.0444 0.0183  -0.0149 21  LEU A C     
166  O  O     . LEU A 41  ? 0.2638 0.2158 0.1541 -0.0359 0.0314  -0.0279 21  LEU A O     
167  C  CB    . LEU A 41  ? 0.2091 0.2226 0.1475 -0.0259 0.0162  -0.0094 21  LEU A CB    
168  C  CG    . LEU A 41  ? 0.2201 0.2333 0.1382 -0.0218 0.0132  -0.0063 21  LEU A CG    
169  C  CD1   . LEU A 41  ? 0.2338 0.2555 0.1523 -0.0257 0.0085  0.0151  21  LEU A CD1   
170  C  CD2   . LEU A 41  ? 0.2288 0.2458 0.1446 -0.0130 -0.0002 0.0005  21  LEU A CD2   
171  N  N     . SER A 42  ? 0.2344 0.2218 0.1763 -0.0576 0.0209  -0.0254 22  SER A N     
172  C  CA    A SER A 42  ? 0.2534 0.2242 0.1858 -0.0654 0.0261  -0.0158 22  SER A CA    
173  C  CA    B SER A 42  ? 0.2701 0.2282 0.1926 -0.0589 0.0196  -0.0187 22  SER A CA    
174  C  C     . SER A 42  ? 0.2891 0.2209 0.1838 -0.0594 0.0261  -0.0223 22  SER A C     
175  O  O     . SER A 42  ? 0.3146 0.2409 0.1766 -0.0623 0.0099  -0.0404 22  SER A O     
176  C  CB    A SER A 42  ? 0.2347 0.2315 0.1961 -0.0617 0.0251  -0.0152 22  SER A CB    
177  C  CB    B SER A 42  ? 0.2847 0.2413 0.2156 -0.0464 0.0094  -0.0247 22  SER A CB    
178  O  OG    A SER A 42  ? 0.2364 0.2382 0.2035 -0.0769 0.0100  -0.0131 22  SER A OG    
179  O  OG    B SER A 42  ? 0.3164 0.2523 0.2359 -0.0535 -0.0113 -0.0307 22  SER A OG    
180  N  N     . ASN A 43  ? 0.3002 0.2101 0.1899 -0.0582 0.0253  -0.0200 23  ASN A N     
181  C  CA    . ASN A 43  ? 0.3326 0.2196 0.1979 -0.0516 0.0208  -0.0371 23  ASN A CA    
182  C  C     . ASN A 43  ? 0.3285 0.2263 0.2070 -0.0454 0.0331  -0.0448 23  ASN A C     
183  O  O     . ASN A 43  ? 0.3672 0.2366 0.2328 -0.0517 0.0469  -0.0566 23  ASN A O     
184  C  CB    . ASN A 43  ? 0.3664 0.2141 0.2090 -0.0500 0.0087  -0.0183 23  ASN A CB    
185  C  CG    . ASN A 43  ? 0.4009 0.2234 0.2334 -0.0509 0.0031  -0.0108 23  ASN A CG    
186  O  OD1   . ASN A 43  ? 0.4211 0.2281 0.2489 -0.0692 0.0283  -0.0028 23  ASN A OD1   
187  N  ND2   . ASN A 43  ? 0.4152 0.2189 0.2320 -0.0336 -0.0153 -0.0046 23  ASN A ND2   
188  N  N     . ASN A 44  ? 0.2848 0.2256 0.1913 -0.0407 0.0300  -0.0374 24  ASN A N     
189  C  CA    . ASN A 44  ? 0.2795 0.2313 0.1952 -0.0212 0.0207  -0.0369 24  ASN A CA    
190  C  C     . ASN A 44  ? 0.2913 0.2403 0.1932 -0.0342 0.0188  -0.0406 24  ASN A C     
191  O  O     . ASN A 44  ? 0.2848 0.2442 0.1967 -0.0571 0.0188  -0.0370 24  ASN A O     
192  C  CB    . ASN A 44  ? 0.2875 0.2700 0.2225 0.0113  0.0217  -0.0345 24  ASN A CB    
193  C  CG    . ASN A 44  ? 0.3202 0.3048 0.2498 0.0427  0.0113  -0.0452 24  ASN A CG    
194  O  OD1   . ASN A 44  ? 0.3318 0.3434 0.2762 0.0755  0.0202  -0.0500 24  ASN A OD1   
195  N  ND2   . ASN A 44  ? 0.3320 0.2940 0.2466 0.0493  0.0068  -0.0456 24  ASN A ND2   
196  N  N     . ALA A 45  ? 0.2893 0.2408 0.1857 -0.0504 0.0297  -0.0383 25  ALA A N     
197  C  CA    . ALA A 45  ? 0.2969 0.2458 0.1766 -0.0435 0.0297  -0.0297 25  ALA A CA    
198  C  C     . ALA A 45  ? 0.3010 0.2414 0.1788 -0.0524 0.0125  -0.0360 25  ALA A C     
199  O  O     . ALA A 45  ? 0.2930 0.2385 0.1737 -0.0512 0.0124  -0.0264 25  ALA A O     
200  C  CB    . ALA A 45  ? 0.3122 0.2540 0.1814 -0.0187 0.0281  -0.0193 25  ALA A CB    
201  N  N     . ASP A 46  ? 0.3227 0.2493 0.1937 -0.0834 0.0158  -0.0362 26  ASP A N     
202  C  CA    . ASP A 46  ? 0.3625 0.2452 0.2268 -0.0858 0.0181  -0.0561 26  ASP A CA    
203  C  C     . ASP A 46  ? 0.3517 0.2382 0.1988 -0.0714 0.0196  -0.0595 26  ASP A C     
204  O  O     . ASP A 46  ? 0.3645 0.2519 0.1825 -0.0742 0.0410  -0.0455 26  ASP A O     
205  C  CB    . ASP A 46  ? 0.4259 0.2746 0.2985 -0.1115 0.0251  -0.0531 26  ASP A CB    
206  C  CG    . ASP A 46  ? 0.4894 0.3124 0.3667 -0.1333 0.0251  -0.0362 26  ASP A CG    
207  O  OD1   . ASP A 46  ? 0.5138 0.3451 0.3845 -0.1475 0.0242  -0.0485 26  ASP A OD1   
208  O  OD2   . ASP A 46  ? 0.5354 0.3529 0.4015 -0.1147 0.0165  -0.0192 26  ASP A OD2   
209  N  N     . LEU A 47  ? 0.3347 0.2371 0.2089 -0.0376 0.0111  -0.0609 27  LEU A N     
210  C  CA    . LEU A 47  ? 0.3311 0.2608 0.2196 -0.0245 0.0224  -0.0527 27  LEU A CA    
211  C  C     . LEU A 47  ? 0.3090 0.2509 0.1937 -0.0311 0.0325  -0.0454 27  LEU A C     
212  O  O     . LEU A 47  ? 0.3170 0.2724 0.1941 -0.0335 0.0524  -0.0390 27  LEU A O     
213  C  CB    . LEU A 47  ? 0.3459 0.2904 0.2564 -0.0022 0.0324  -0.0402 27  LEU A CB    
214  C  CG    . LEU A 47  ? 0.3692 0.3398 0.2947 0.0192  0.0467  -0.0227 27  LEU A CG    
215  C  CD1   . LEU A 47  ? 0.3867 0.3466 0.3145 0.0275  0.0503  -0.0188 27  LEU A CD1   
216  C  CD2   . LEU A 47  ? 0.3952 0.3714 0.3044 0.0102  0.0477  -0.0233 27  LEU A CD2   
217  N  N     . VAL A 48  ? 0.2740 0.2306 0.1926 -0.0303 0.0421  -0.0467 28  VAL A N     
218  C  CA    . VAL A 48  ? 0.2587 0.2296 0.1687 -0.0413 0.0298  -0.0375 28  VAL A CA    
219  C  C     . VAL A 48  ? 0.2939 0.2552 0.1657 -0.0606 0.0286  -0.0361 28  VAL A C     
220  O  O     . VAL A 48  ? 0.2946 0.2737 0.1674 -0.0719 0.0245  -0.0248 28  VAL A O     
221  C  CB    . VAL A 48  ? 0.2371 0.2185 0.1593 -0.0113 0.0077  -0.0265 28  VAL A CB    
222  C  CG1   . VAL A 48  ? 0.2436 0.2154 0.1571 -0.0178 0.0064  -0.0190 28  VAL A CG1   
223  C  CG2   . VAL A 48  ? 0.2486 0.2089 0.1822 -0.0095 -0.0020 -0.0047 28  VAL A CG2   
224  N  N     . ASP A 49  ? 0.2801 0.2576 0.1627 -0.0773 0.0290  -0.0301 29  ASP A N     
225  C  CA    . ASP A 49  ? 0.3036 0.2864 0.1568 -0.0815 0.0051  -0.0329 29  ASP A CA    
226  C  C     . ASP A 49  ? 0.3021 0.2941 0.1497 -0.0750 -0.0017 -0.0330 29  ASP A C     
227  O  O     . ASP A 49  ? 0.3074 0.3183 0.1666 -0.0794 0.0008  -0.0139 29  ASP A O     
228  C  CB    . ASP A 49  ? 0.3125 0.2998 0.1818 -0.0750 -0.0180 -0.0261 29  ASP A CB    
229  C  CG    . ASP A 49  ? 0.3300 0.3000 0.2125 -0.0652 -0.0115 -0.0283 29  ASP A CG    
230  O  OD1   . ASP A 49  ? 0.3153 0.2940 0.2111 -0.0548 0.0047  -0.0428 29  ASP A OD1   
231  O  OD2   . ASP A 49  ? 0.3628 0.2991 0.2370 -0.0641 -0.0266 -0.0459 29  ASP A OD2   
232  N  N     . SER A 50  ? 0.3173 0.2843 0.1596 -0.0663 0.0145  -0.0555 30  SER A N     
233  C  CA    . SER A 50  ? 0.3646 0.2800 0.1695 -0.0492 0.0320  -0.0532 30  SER A CA    
234  C  C     . SER A 50  ? 0.3152 0.2732 0.1457 -0.0318 0.0187  -0.0461 30  SER A C     
235  O  O     . SER A 50  ? 0.3363 0.2936 0.1560 -0.0251 0.0198  -0.0362 30  SER A O     
236  C  CB    . SER A 50  ? 0.4454 0.3095 0.2149 -0.0349 0.0678  -0.0527 30  SER A CB    
237  O  OG    . SER A 50  ? 0.4957 0.3284 0.2416 -0.0192 0.0993  -0.0545 30  SER A OG    
238  N  N     . LEU A 51  ? 0.2932 0.2392 0.1385 -0.0183 0.0022  -0.0384 31  LEU A N     
239  C  CA    . LEU A 51  ? 0.2465 0.2397 0.1364 -0.0055 -0.0159 -0.0215 31  LEU A CA    
240  C  C     . LEU A 51  ? 0.2066 0.2382 0.1348 0.0011  -0.0194 -0.0324 31  LEU A C     
241  O  O     . LEU A 51  ? 0.2105 0.2441 0.1415 -0.0040 -0.0089 -0.0303 31  LEU A O     
242  C  CB    . LEU A 51  ? 0.2733 0.2567 0.1595 0.0056  -0.0313 0.0104  31  LEU A CB    
243  C  CG    . LEU A 51  ? 0.2740 0.2766 0.1747 0.0235  -0.0263 0.0070  31  LEU A CG    
244  C  CD1   . LEU A 51  ? 0.3030 0.2800 0.1737 0.0150  -0.0462 0.0270  31  LEU A CD1   
245  C  CD2   . LEU A 51  ? 0.2839 0.3019 0.2001 0.0438  -0.0067 -0.0044 31  LEU A CD2   
246  N  N     . ASN A 52  ? 0.1922 0.2521 0.1288 -0.0052 -0.0011 -0.0254 32  ASN A N     
247  C  CA    . ASN A 52  ? 0.2016 0.2516 0.1293 0.0043  -0.0060 -0.0308 32  ASN A CA    
248  C  C     . ASN A 52  ? 0.2044 0.2519 0.1240 0.0134  -0.0239 -0.0282 32  ASN A C     
249  O  O     . ASN A 52  ? 0.2822 0.2412 0.1347 -0.0052 -0.0335 -0.0199 32  ASN A O     
250  C  CB    . ASN A 52  ? 0.2019 0.2515 0.1518 -0.0062 -0.0044 -0.0480 32  ASN A CB    
251  C  CG    . ASN A 52  ? 0.1997 0.2465 0.1386 -0.0028 -0.0204 -0.0444 32  ASN A CG    
252  O  OD1   . ASN A 52  ? 0.2085 0.2343 0.1419 0.0013  -0.0290 -0.0426 32  ASN A OD1   
253  N  ND2   . ASN A 52  ? 0.1970 0.2483 0.1259 -0.0007 -0.0034 -0.0240 32  ASN A ND2   
254  N  N     . VAL A 53  ? 0.1942 0.2698 0.1267 -0.0115 0.0000  -0.0116 33  VAL A N     
255  C  CA    . VAL A 53  ? 0.2014 0.2768 0.1330 -0.0070 -0.0017 -0.0004 33  VAL A CA    
256  C  C     . VAL A 53  ? 0.2186 0.2824 0.1274 -0.0005 -0.0071 0.0041  33  VAL A C     
257  O  O     . VAL A 53  ? 0.2678 0.2876 0.1331 -0.0136 -0.0119 0.0090  33  VAL A O     
258  C  CB    . VAL A 53  ? 0.2157 0.2869 0.1333 0.0039  0.0064  -0.0031 33  VAL A CB    
259  C  CG1   . VAL A 53  ? 0.2330 0.3028 0.1456 0.0253  0.0116  -0.0263 33  VAL A CG1   
260  C  CG2   . VAL A 53  ? 0.1955 0.2960 0.1408 -0.0190 -0.0066 0.0143  33  VAL A CG2   
261  N  N     . TYR A 54  ? 0.1956 0.2952 0.1302 0.0027  -0.0126 0.0035  34  TYR A N     
262  C  CA    . TYR A 54  ? 0.2035 0.3044 0.1380 -0.0096 -0.0097 -0.0032 34  TYR A CA    
263  C  C     . TYR A 54  ? 0.1982 0.2969 0.1420 -0.0162 -0.0078 0.0009  34  TYR A C     
264  O  O     . TYR A 54  ? 0.1958 0.3139 0.1326 -0.0200 -0.0177 0.0083  34  TYR A O     
265  C  CB    . TYR A 54  ? 0.1926 0.3292 0.1524 -0.0096 -0.0002 -0.0153 34  TYR A CB    
266  C  CG    . TYR A 54  ? 0.1971 0.3503 0.1987 -0.0159 0.0021  -0.0373 34  TYR A CG    
267  C  CD1   . TYR A 54  ? 0.2373 0.3563 0.2297 -0.0196 -0.0038 -0.0280 34  TYR A CD1   
268  C  CD2   . TYR A 54  ? 0.2239 0.3561 0.2413 -0.0442 0.0195  -0.0519 34  TYR A CD2   
269  C  CE1   . TYR A 54  ? 0.2798 0.3687 0.2538 -0.0234 -0.0055 -0.0452 34  TYR A CE1   
270  C  CE2   . TYR A 54  ? 0.2454 0.3621 0.2659 -0.0322 0.0086  -0.0397 34  TYR A CE2   
271  C  CZ    . TYR A 54  ? 0.2820 0.3615 0.2786 -0.0359 -0.0031 -0.0500 34  TYR A CZ    
272  O  OH    . TYR A 54  ? 0.3583 0.3739 0.3171 -0.0268 0.0010  -0.0468 34  TYR A OH    
273  N  N     . PRO A 55  ? 0.2204 0.2739 0.1388 -0.0111 0.0077  -0.0161 35  PRO A N     
274  C  CA    . PRO A 55  ? 0.2428 0.2630 0.1474 -0.0030 -0.0059 -0.0125 35  PRO A CA    
275  C  C     . PRO A 55  ? 0.2603 0.2639 0.1378 -0.0073 -0.0252 -0.0140 35  PRO A C     
276  O  O     . PRO A 55  ? 0.3171 0.3064 0.1546 -0.0151 -0.0208 0.0114  35  PRO A O     
277  C  CB    . PRO A 55  ? 0.2692 0.2628 0.1748 -0.0039 0.0038  -0.0194 35  PRO A CB    
278  C  CG    . PRO A 55  ? 0.2780 0.2849 0.1971 -0.0127 0.0202  -0.0197 35  PRO A CG    
279  C  CD    . PRO A 55  ? 0.2264 0.2786 0.1688 -0.0142 0.0104  -0.0320 35  PRO A CD    
280  N  N     . VAL A 56  ? 0.2591 0.2382 0.1306 0.0083  -0.0174 -0.0259 36  VAL A N     
281  C  CA    A VAL A 56  ? 0.2593 0.2390 0.1322 0.0093  -0.0219 -0.0255 36  VAL A CA    
282  C  CA    B VAL A 56  ? 0.2627 0.2450 0.1438 0.0022  -0.0297 -0.0288 36  VAL A CA    
283  C  C     . VAL A 56  ? 0.2309 0.2438 0.1361 0.0157  -0.0110 -0.0286 36  VAL A C     
284  O  O     . VAL A 56  ? 0.2234 0.2546 0.1266 0.0162  -0.0040 -0.0366 36  VAL A O     
285  C  CB    A VAL A 56  ? 0.2968 0.2373 0.1283 0.0134  -0.0237 -0.0335 36  VAL A CB    
286  C  CB    B VAL A 56  ? 0.3092 0.2550 0.1634 -0.0071 -0.0508 -0.0394 36  VAL A CB    
287  C  CG1   A VAL A 56  ? 0.3146 0.2276 0.1336 0.0226  -0.0312 -0.0372 36  VAL A CG1   
288  C  CG1   B VAL A 56  ? 0.3377 0.2646 0.1722 -0.0036 -0.0515 -0.0437 36  VAL A CG1   
289  C  CG2   A VAL A 56  ? 0.3121 0.2426 0.1235 0.0225  -0.0127 -0.0361 36  VAL A CG2   
290  C  CG2   B VAL A 56  ? 0.3096 0.2546 0.1725 -0.0101 -0.0480 -0.0391 36  VAL A CG2   
291  N  N     . PRO A 57  ? 0.2106 0.2412 0.1274 0.0205  -0.0085 -0.0376 37  PRO A N     
292  C  CA    . PRO A 57  ? 0.2063 0.2565 0.1369 0.0232  -0.0238 -0.0461 37  PRO A CA    
293  C  C     . PRO A 57  ? 0.2284 0.2468 0.1409 0.0235  -0.0261 -0.0484 37  PRO A C     
294  O  O     . PRO A 57  ? 0.2905 0.2522 0.1484 -0.0066 -0.0048 -0.0568 37  PRO A O     
295  C  CB    . PRO A 57  ? 0.2083 0.2578 0.1429 0.0253  -0.0230 -0.0524 37  PRO A CB    
296  C  CG    . PRO A 57  ? 0.2223 0.2650 0.1444 0.0021  -0.0013 -0.0629 37  PRO A CG    
297  C  CD    . PRO A 57  ? 0.2264 0.2561 0.1271 0.0170  0.0058  -0.0642 37  PRO A CD    
298  N  N     . ASP A 58  ? 0.2345 0.2551 0.1431 -0.0153 -0.0169 -0.0378 38  ASP A N     
299  C  CA    . ASP A 58  ? 0.2504 0.2725 0.1593 -0.0317 -0.0183 -0.0426 38  ASP A CA    
300  C  C     . ASP A 58  ? 0.2834 0.2945 0.1573 -0.0548 -0.0165 -0.0297 38  ASP A C     
301  O  O     . ASP A 58  ? 0.2895 0.3316 0.1795 -0.0705 -0.0381 -0.0183 38  ASP A O     
302  C  CB    . ASP A 58  ? 0.2308 0.2923 0.1544 -0.0041 -0.0209 -0.0636 38  ASP A CB    
303  C  CG    . ASP A 58  ? 0.2258 0.2967 0.1441 0.0257  -0.0262 -0.0606 38  ASP A CG    
304  O  OD1   . ASP A 58  ? 0.2013 0.2790 0.1442 0.0037  -0.0226 -0.0300 38  ASP A OD1   
305  O  OD2   . ASP A 58  ? 0.2427 0.3108 0.1562 0.0360  -0.0453 -0.0499 38  ASP A OD2   
306  N  N     . GLY A 59  ? 0.3570 0.2628 0.1436 -0.0477 -0.0175 -0.0304 39  GLY A N     
307  C  CA    . GLY A 59  ? 0.3885 0.2492 0.1545 -0.0464 -0.0124 -0.0299 39  GLY A CA    
308  C  C     . GLY A 59  ? 0.3716 0.2413 0.1569 -0.0773 -0.0243 -0.0237 39  GLY A C     
309  O  O     . GLY A 59  ? 0.4458 0.2584 0.1813 -0.0926 -0.0449 -0.0199 39  GLY A O     
310  N  N     . ASP A 60  ? 0.2908 0.2418 0.1578 -0.0660 -0.0206 -0.0392 40  ASP A N     
311  C  CA    . ASP A 60  ? 0.2368 0.2504 0.1527 -0.0583 -0.0148 -0.0196 40  ASP A CA    
312  C  C     . ASP A 60  ? 0.2030 0.2518 0.1463 -0.0411 -0.0217 -0.0179 40  ASP A C     
313  O  O     . ASP A 60  ? 0.2063 0.2906 0.1539 -0.0385 -0.0037 -0.0010 40  ASP A O     
314  C  CB    . ASP A 60  ? 0.2151 0.2569 0.1721 -0.0579 -0.0125 -0.0087 40  ASP A CB    
315  C  CG    . ASP A 60  ? 0.1995 0.2571 0.1576 -0.0332 -0.0109 -0.0118 40  ASP A CG    
316  O  OD1   . ASP A 60  ? 0.1927 0.2475 0.1529 -0.0298 -0.0061 -0.0286 40  ASP A OD1   
317  O  OD2   . ASP A 60  ? 0.1941 0.2782 0.1792 -0.0044 -0.0338 -0.0317 40  ASP A OD2   
318  N  N     . THR A 61  ? 0.1982 0.2427 0.1394 -0.0279 -0.0069 -0.0324 41  THR A N     
319  C  CA    . THR A 61  ? 0.1897 0.2331 0.1238 -0.0219 -0.0055 -0.0341 41  THR A CA    
320  C  C     . THR A 61  ? 0.1994 0.2193 0.1328 -0.0168 -0.0006 -0.0266 41  THR A C     
321  O  O     . THR A 61  ? 0.2095 0.2323 0.1316 -0.0234 0.0008  -0.0240 41  THR A O     
322  C  CB    . THR A 61  ? 0.1813 0.2347 0.1253 -0.0239 -0.0115 -0.0261 41  THR A CB    
323  O  OG1   . THR A 61  ? 0.1849 0.2387 0.1207 -0.0139 -0.0018 -0.0155 41  THR A OG1   
324  C  CG2   . THR A 61  ? 0.1961 0.2359 0.1350 -0.0167 -0.0291 -0.0254 41  THR A CG2   
325  N  N     . GLY A 62  ? 0.2009 0.2300 0.1350 -0.0239 0.0280  -0.0297 42  GLY A N     
326  C  CA    . GLY A 62  ? 0.1995 0.2410 0.1425 -0.0173 0.0079  -0.0212 42  GLY A CA    
327  C  C     . GLY A 62  ? 0.2118 0.2640 0.1658 -0.0278 0.0111  -0.0221 42  GLY A C     
328  O  O     . GLY A 62  ? 0.2092 0.2775 0.1655 -0.0254 0.0234  -0.0174 42  GLY A O     
329  N  N     . THR A 63  ? 0.2192 0.2769 0.1836 -0.0513 0.0104  -0.0267 43  THR A N     
330  C  CA    . THR A 63  ? 0.2010 0.2850 0.2121 -0.0509 0.0188  -0.0365 43  THR A CA    
331  C  C     . THR A 63  ? 0.1862 0.2870 0.1835 -0.0491 0.0050  -0.0162 43  THR A C     
332  O  O     . THR A 63  ? 0.1946 0.3079 0.1829 -0.0457 0.0142  -0.0117 43  THR A O     
333  C  CB    . THR A 63  ? 0.2362 0.3118 0.2839 -0.0495 -0.0067 -0.0726 43  THR A CB    
334  O  OG1   . THR A 63  ? 0.2823 0.3454 0.3191 -0.0538 -0.0108 -0.0745 43  THR A OG1   
335  C  CG2   . THR A 63  ? 0.2321 0.3299 0.2998 -0.0530 -0.0183 -0.0808 43  THR A CG2   
336  N  N     . ASN A 64  ? 0.1702 0.2853 0.1509 -0.0438 0.0077  -0.0179 44  ASN A N     
337  C  CA    . ASN A 64  ? 0.1876 0.2785 0.1478 -0.0200 0.0027  -0.0103 44  ASN A CA    
338  C  C     . ASN A 64  ? 0.1806 0.2572 0.1454 -0.0195 0.0050  -0.0109 44  ASN A C     
339  O  O     . ASN A 64  ? 0.1839 0.2594 0.1458 -0.0155 -0.0035 -0.0116 44  ASN A O     
340  C  CB    . ASN A 64  ? 0.1707 0.2893 0.1338 -0.0119 -0.0099 -0.0121 44  ASN A CB    
341  C  CG    . ASN A 64  ? 0.1705 0.3202 0.1434 -0.0197 -0.0073 -0.0118 44  ASN A CG    
342  O  OD1   . ASN A 64  ? 0.2018 0.3518 0.1528 -0.0335 -0.0222 -0.0079 44  ASN A OD1   
343  N  ND2   . ASN A 64  ? 0.1748 0.3123 0.1429 -0.0099 -0.0192 -0.0331 44  ASN A ND2   
344  N  N     . MET A 65  ? 0.1690 0.2453 0.1440 -0.0208 -0.0090 -0.0062 45  MET A N     
345  C  CA    . MET A 65  ? 0.1569 0.2474 0.1430 -0.0219 -0.0032 -0.0037 45  MET A CA    
346  C  C     . MET A 65  ? 0.1659 0.2423 0.1524 -0.0406 -0.0109 -0.0002 45  MET A C     
347  O  O     . MET A 65  ? 0.1623 0.2477 0.1434 -0.0354 -0.0106 -0.0031 45  MET A O     
348  C  CB    . MET A 65  ? 0.1704 0.2369 0.1363 -0.0312 0.0035  -0.0060 45  MET A CB    
349  C  CG    . MET A 65  ? 0.1710 0.2184 0.1355 -0.0233 0.0004  -0.0068 45  MET A CG    
350  S  SD    . MET A 65  ? 0.1732 0.2293 0.1393 -0.0079 0.0063  -0.0116 45  MET A SD    
351  C  CE    . MET A 65  ? 0.1852 0.2357 0.1436 -0.0056 0.0087  -0.0008 45  MET A CE    
352  N  N     . ASN A 66  ? 0.1848 0.2370 0.1632 -0.0459 0.0030  -0.0006 46  ASN A N     
353  C  CA    . ASN A 66  ? 0.2117 0.2424 0.1735 -0.0458 0.0148  -0.0158 46  ASN A CA    
354  C  C     . ASN A 66  ? 0.2125 0.2603 0.1758 -0.0500 0.0057  -0.0026 46  ASN A C     
355  O  O     . ASN A 66  ? 0.2327 0.2685 0.1699 -0.0439 0.0113  -0.0035 46  ASN A O     
356  C  CB    . ASN A 66  ? 0.2422 0.2407 0.1995 -0.0551 0.0136  -0.0178 46  ASN A CB    
357  C  CG    . ASN A 66  ? 0.3029 0.2752 0.2140 -0.0705 -0.0077 -0.0123 46  ASN A CG    
358  O  OD1   . ASN A 66  ? 0.3325 0.2886 0.2029 -0.0530 0.0001  0.0017  46  ASN A OD1   
359  N  ND2   . ASN A 66  ? 0.3734 0.3111 0.2425 -0.1046 -0.0209 -0.0115 46  ASN A ND2   
360  N  N     . LEU A 67  ? 0.1815 0.2790 0.1694 -0.0418 0.0143  -0.0039 47  LEU A N     
361  C  CA    . LEU A 67  ? 0.1975 0.3143 0.1849 -0.0500 0.0017  -0.0192 47  LEU A CA    
362  C  C     . LEU A 67  ? 0.1905 0.3117 0.1726 -0.0391 0.0034  -0.0198 47  LEU A C     
363  O  O     . LEU A 67  ? 0.2033 0.3231 0.1872 -0.0455 0.0182  -0.0146 47  LEU A O     
364  C  CB    . LEU A 67  ? 0.2169 0.3470 0.2127 -0.0395 -0.0053 -0.0347 47  LEU A CB    
365  C  CG    . LEU A 67  ? 0.2525 0.3740 0.2383 -0.0543 -0.0039 -0.0490 47  LEU A CG    
366  C  CD1   . LEU A 67  ? 0.2630 0.3959 0.2349 -0.0341 -0.0283 -0.0676 47  LEU A CD1   
367  C  CD2   . LEU A 67  ? 0.2968 0.3907 0.2731 -0.0791 0.0020  -0.0449 47  LEU A CD2   
368  N  N     . THR A 68  ? 0.1598 0.2831 0.1518 -0.0294 0.0122  -0.0150 48  THR A N     
369  C  CA    . THR A 68  ? 0.1661 0.2594 0.1530 -0.0225 0.0119  -0.0073 48  THR A CA    
370  C  C     . THR A 68  ? 0.1766 0.2581 0.1635 -0.0173 0.0233  -0.0071 48  THR A C     
371  O  O     . THR A 68  ? 0.1866 0.2731 0.1750 -0.0100 0.0212  -0.0106 48  THR A O     
372  C  CB    . THR A 68  ? 0.1812 0.2535 0.1482 -0.0213 0.0121  -0.0062 48  THR A CB    
373  O  OG1   . THR A 68  ? 0.1917 0.2565 0.1406 -0.0192 -0.0009 -0.0005 48  THR A OG1   
374  C  CG2   . THR A 68  ? 0.1961 0.2578 0.1633 -0.0309 0.0005  -0.0045 48  THR A CG2   
375  N  N     . MET A 69  ? 0.1837 0.2515 0.1544 -0.0127 0.0166  -0.0014 49  MET A N     
376  C  CA    . MET A 69  ? 0.2073 0.2533 0.1565 -0.0159 0.0127  -0.0146 49  MET A CA    
377  C  C     . MET A 69  ? 0.2319 0.2673 0.1694 -0.0231 0.0323  -0.0166 49  MET A C     
378  O  O     . MET A 69  ? 0.2668 0.2699 0.1753 -0.0317 0.0427  -0.0033 49  MET A O     
379  C  CB    . MET A 69  ? 0.2789 0.2638 0.1795 0.0216  0.0134  -0.0093 49  MET A CB    
380  C  CG    . MET A 69  ? 0.2916 0.2810 0.2214 0.0128  0.0160  -0.0196 49  MET A CG    
381  S  SD    . MET A 69  ? 0.2274 0.2762 0.2555 -0.0067 -0.0054 -0.0620 49  MET A SD    
382  C  CE    . MET A 69  ? 0.2393 0.2860 0.2635 0.0059  0.0023  -0.0357 49  MET A CE    
383  N  N     . THR A 70  ? 0.2622 0.2854 0.1860 -0.0671 0.0421  -0.0246 50  THR A N     
384  C  CA    . THR A 70  ? 0.2910 0.3026 0.2087 -0.0858 0.0628  -0.0383 50  THR A CA    
385  C  C     . THR A 70  ? 0.2591 0.3195 0.2268 -0.0816 0.0653  -0.0413 50  THR A C     
386  O  O     . THR A 70  ? 0.2798 0.3287 0.2258 -0.0844 0.0781  -0.0362 50  THR A O     
387  C  CB    . THR A 70  ? 0.3479 0.3151 0.2433 -0.1061 0.0786  -0.0345 50  THR A CB    
388  O  OG1   . THR A 70  ? 0.4098 0.3174 0.2607 -0.0971 0.1079  -0.0354 50  THR A OG1   
389  C  CG2   . THR A 70  ? 0.3573 0.3282 0.2480 -0.1173 0.0763  -0.0448 50  THR A CG2   
390  N  N     . SER A 71  ? 0.2336 0.3341 0.2270 -0.0631 0.0612  -0.0522 51  SER A N     
391  C  CA    . SER A 71  ? 0.2145 0.3495 0.2403 -0.0533 0.0663  -0.0511 51  SER A CA    
392  C  C     . SER A 71  ? 0.2399 0.3452 0.2240 -0.0467 0.0581  -0.0441 51  SER A C     
393  O  O     . SER A 71  ? 0.2453 0.3763 0.2224 -0.0548 0.0638  -0.0487 51  SER A O     
394  C  CB    . SER A 71  ? 0.2303 0.3665 0.2683 -0.0313 0.0496  -0.0644 51  SER A CB    
395  O  OG    . SER A 71  ? 0.2701 0.3894 0.3032 -0.0365 0.0346  -0.0653 51  SER A OG    
396  N  N     . GLY A 72  ? 0.2422 0.3141 0.1999 -0.0464 0.0302  -0.0359 52  GLY A N     
397  C  CA    . GLY A 72  ? 0.2379 0.2880 0.1828 -0.0356 0.0298  -0.0273 52  GLY A CA    
398  C  C     . GLY A 72  ? 0.2384 0.2863 0.1907 -0.0318 0.0461  -0.0082 52  GLY A C     
399  O  O     . GLY A 72  ? 0.2433 0.3028 0.1968 -0.0300 0.0436  -0.0069 52  GLY A O     
400  N  N     . ARG A 73  ? 0.2429 0.2684 0.1859 -0.0345 0.0504  -0.0090 53  ARG A N     
401  C  CA    . ARG A 73  ? 0.2590 0.2773 0.2036 -0.0376 0.0470  0.0043  53  ARG A CA    
402  C  C     . ARG A 73  ? 0.2596 0.3037 0.2067 -0.0548 0.0508  0.0118  53  ARG A C     
403  O  O     . ARG A 73  ? 0.2818 0.3038 0.1970 -0.0398 0.0603  0.0165  53  ARG A O     
404  C  CB    . ARG A 73  ? 0.3056 0.2725 0.2174 -0.0181 0.0379  0.0053  53  ARG A CB    
405  C  CG    . ARG A 73  ? 0.3679 0.2872 0.2505 0.0040  0.0364  0.0161  53  ARG A CG    
406  C  CD    . ARG A 73  ? 0.4182 0.2962 0.3039 -0.0149 0.0562  0.0394  53  ARG A CD    
407  N  NE    . ARG A 73  ? 0.4576 0.3321 0.3515 -0.0327 0.0646  0.0491  53  ARG A NE    
408  C  CZ    . ARG A 73  ? 0.4773 0.3466 0.3751 -0.0361 0.0749  0.0605  53  ARG A CZ    
409  N  NH1   . ARG A 73  ? 0.4688 0.3597 0.3814 -0.0115 0.1079  0.0600  53  ARG A NH1   
410  N  NH2   . ARG A 73  ? 0.4870 0.3475 0.3886 -0.0521 0.0536  0.0583  53  ARG A NH2   
411  N  N     . GLU A 74  ? 0.2307 0.3351 0.2215 -0.0932 0.0447  -0.0020 54  GLU A N     
412  C  CA    . GLU A 74  ? 0.2617 0.3941 0.2580 -0.0893 0.0484  -0.0173 54  GLU A CA    
413  C  C     . GLU A 74  ? 0.2388 0.4010 0.2441 -0.0705 0.0567  -0.0055 54  GLU A C     
414  O  O     . GLU A 74  ? 0.2598 0.4073 0.2483 -0.0555 0.0802  -0.0035 54  GLU A O     
415  C  CB    . GLU A 74  ? 0.2949 0.4448 0.2959 -0.1079 0.0465  -0.0312 54  GLU A CB    
416  C  CG    . GLU A 74  ? 0.3544 0.4862 0.3384 -0.1267 0.0405  -0.0394 54  GLU A CG    
417  C  CD    . GLU A 74  ? 0.4162 0.5278 0.3763 -0.1237 0.0382  -0.0506 54  GLU A CD    
418  O  OE1   . GLU A 74  ? 0.4340 0.5526 0.3921 -0.0984 0.0145  -0.0508 54  GLU A OE1   
419  O  OE2   . GLU A 74  ? 0.4381 0.5440 0.3903 -0.1364 0.0576  -0.0604 54  GLU A OE2   
420  N  N     . GLU A 75  ? 0.2243 0.4071 0.2387 -0.0592 0.0401  0.0003  55  GLU A N     
421  C  CA    . GLU A 75  ? 0.2202 0.4283 0.2446 -0.0409 0.0273  0.0045  55  GLU A CA    
422  C  C     . GLU A 75  ? 0.2176 0.3979 0.2030 -0.0417 0.0384  0.0085  55  GLU A C     
423  O  O     . GLU A 75  ? 0.2218 0.4010 0.1977 -0.0192 0.0657  0.0072  55  GLU A O     
424  C  CB    . GLU A 75  ? 0.2526 0.4779 0.2845 -0.0382 0.0101  0.0079  55  GLU A CB    
425  C  CG    . GLU A 75  ? 0.3019 0.5332 0.3210 -0.0305 0.0090  0.0041  55  GLU A CG    
426  C  CD    . GLU A 75  ? 0.3414 0.5921 0.3561 -0.0167 0.0140  -0.0177 55  GLU A CD    
427  O  OE1   . GLU A 75  ? 0.3736 0.6183 0.3761 -0.0175 0.0116  -0.0195 55  GLU A OE1   
428  O  OE2   . GLU A 75  ? 0.3485 0.6133 0.3736 0.0039  0.0233  -0.0251 55  GLU A OE2   
429  N  N     . VAL A 76  ? 0.2302 0.3641 0.1867 -0.0469 0.0310  0.0135  56  VAL A N     
430  C  CA    . VAL A 76  ? 0.2251 0.3415 0.1762 -0.0543 0.0303  0.0227  56  VAL A CA    
431  C  C     . VAL A 76  ? 0.2665 0.3605 0.1944 -0.0596 0.0438  0.0266  56  VAL A C     
432  O  O     . VAL A 76  ? 0.2679 0.3673 0.1758 -0.0496 0.0444  0.0286  56  VAL A O     
433  C  CB    . VAL A 76  ? 0.2322 0.3196 0.1766 -0.0389 0.0160  0.0184  56  VAL A CB    
434  C  CG1   . VAL A 76  ? 0.2611 0.3219 0.1833 -0.0327 0.0150  0.0194  56  VAL A CG1   
435  C  CG2   . VAL A 76  ? 0.2334 0.3009 0.1773 -0.0386 -0.0030 0.0072  56  VAL A CG2   
436  N  N     . GLU A 77  ? 0.2830 0.3544 0.2267 -0.0935 0.0499  0.0288  57  GLU A N     
437  C  CA    . GLU A 77  ? 0.3128 0.3937 0.2711 -0.1152 0.0634  0.0135  57  GLU A CA    
438  C  C     . GLU A 77  ? 0.3334 0.4276 0.2668 -0.1194 0.0881  0.0062  57  GLU A C     
439  O  O     . GLU A 77  ? 0.3857 0.4399 0.2697 -0.1152 0.0934  0.0201  57  GLU A O     
440  C  CB    . GLU A 77  ? 0.3447 0.4016 0.3136 -0.1169 0.0792  0.0025  57  GLU A CB    
441  C  CG    . GLU A 77  ? 0.3801 0.4227 0.3517 -0.1252 0.0817  -0.0097 57  GLU A CG    
442  C  CD    . GLU A 77  ? 0.4395 0.4366 0.3901 -0.1154 0.0684  -0.0263 57  GLU A CD    
443  O  OE1   . GLU A 77  ? 0.4594 0.4465 0.4049 -0.1132 0.0603  -0.0392 57  GLU A OE1   
444  O  OE2   . GLU A 77  ? 0.4730 0.4406 0.4073 -0.1057 0.0645  -0.0255 57  GLU A OE2   
445  N  N     . ASN A 78  ? 0.2811 0.4584 0.2696 -0.1131 0.0909  -0.0083 58  ASN A N     
446  C  CA    . ASN A 78  ? 0.3076 0.4903 0.2979 -0.0946 0.0770  -0.0102 58  ASN A CA    
447  C  C     . ASN A 78  ? 0.2731 0.4631 0.2909 -0.0409 0.0724  -0.0006 58  ASN A C     
448  O  O     . ASN A 78  ? 0.2616 0.4831 0.3160 -0.0338 0.0558  -0.0012 58  ASN A O     
449  C  CB    . ASN A 78  ? 0.3774 0.5428 0.3386 -0.0926 0.0629  -0.0195 58  ASN A CB    
450  C  CG    . ASN A 78  ? 0.4621 0.5872 0.3791 -0.0879 0.0622  -0.0252 58  ASN A CG    
451  O  OD1   . ASN A 78  ? 0.5148 0.6137 0.4023 -0.0729 0.0520  -0.0315 58  ASN A OD1   
452  N  ND2   . ASN A 78  ? 0.4713 0.6015 0.3915 -0.0909 0.0529  -0.0331 58  ASN A ND2   
453  N  N     . ASN A 79  ? 0.2546 0.4094 0.2687 -0.0160 0.0547  0.0163  59  ASN A N     
454  C  CA    A ASN A 79  ? 0.2658 0.3797 0.2708 0.0042  0.0549  0.0215  59  ASN A CA    
455  C  CA    B ASN A 79  ? 0.2348 0.3903 0.2703 0.0010  0.0553  0.0198  59  ASN A CA    
456  C  C     . ASN A 79  ? 0.2382 0.3549 0.2532 0.0049  0.0553  0.0344  59  ASN A C     
457  O  O     . ASN A 79  ? 0.2799 0.3511 0.2778 -0.0051 0.0377  0.0520  59  ASN A O     
458  C  CB    A ASN A 79  ? 0.3115 0.3837 0.2968 0.0229  0.0423  0.0155  59  ASN A CB    
459  C  CB    B ASN A 79  ? 0.2241 0.4144 0.2939 0.0129  0.0440  0.0119  59  ASN A CB    
460  C  CG    A ASN A 79  ? 0.3461 0.3845 0.3149 0.0486  0.0384  0.0087  59  ASN A CG    
461  C  CG    B ASN A 79  ? 0.2150 0.4343 0.3153 0.0315  0.0376  0.0058  59  ASN A CG    
462  O  OD1   A ASN A 79  ? 0.3599 0.3842 0.3236 0.0587  0.0341  0.0081  59  ASN A OD1   
463  O  OD1   B ASN A 79  ? 0.2156 0.4424 0.3131 0.0328  0.0439  0.0049  59  ASN A OD1   
464  N  ND2   A ASN A 79  ? 0.3672 0.3897 0.3222 0.0534  0.0293  0.0117  59  ASN A ND2   
465  N  ND2   B ASN A 79  ? 0.2166 0.4433 0.3301 0.0420  0.0357  0.0051  59  ASN A ND2   
466  N  N     . LEU A 80  ? 0.2277 0.3241 0.2068 0.0104  0.0386  0.0329  60  LEU A N     
467  C  CA    . LEU A 80  ? 0.2195 0.3030 0.2118 -0.0031 0.0530  0.0229  60  LEU A CA    
468  C  C     . LEU A 80  ? 0.2241 0.2920 0.2158 -0.0056 0.0666  0.0070  60  LEU A C     
469  O  O     . LEU A 80  ? 0.2431 0.3110 0.2471 -0.0111 0.0636  -0.0041 60  LEU A O     
470  C  CB    . LEU A 80  ? 0.2326 0.2964 0.1986 -0.0340 0.0423  0.0379  60  LEU A CB    
471  C  CG    . LEU A 80  ? 0.2668 0.3062 0.2009 -0.0195 0.0461  0.0403  60  LEU A CG    
472  C  CD1   . LEU A 80  ? 0.2992 0.3105 0.2307 -0.0384 0.0554  0.0396  60  LEU A CD1   
473  C  CD2   . LEU A 80  ? 0.2890 0.3117 0.2010 -0.0178 0.0376  0.0481  60  LEU A CD2   
474  N  N     . SER A 81  ? 0.2745 0.2840 0.2159 -0.0117 0.0525  -0.0045 61  SER A N     
475  C  CA    . SER A 81  ? 0.2825 0.2765 0.2149 -0.0125 0.0477  -0.0107 61  SER A CA    
476  C  C     . SER A 81  ? 0.2919 0.2596 0.2005 -0.0129 0.0431  -0.0040 61  SER A C     
477  O  O     . SER A 81  ? 0.2864 0.2731 0.1956 -0.0072 0.0359  0.0095  61  SER A O     
478  C  CB    . SER A 81  ? 0.2875 0.2802 0.2389 -0.0085 0.0393  -0.0093 61  SER A CB    
479  O  OG    . SER A 81  ? 0.2776 0.2706 0.2575 -0.0076 0.0284  -0.0174 61  SER A OG    
480  N  N     . LYS A 82  ? 0.2980 0.2364 0.1792 -0.0150 0.0476  -0.0013 62  LYS A N     
481  C  CA    . LYS A 82  ? 0.3526 0.2456 0.1706 -0.0031 0.0526  0.0068  62  LYS A CA    
482  C  C     . LYS A 82  ? 0.2932 0.2532 0.1411 0.0074  0.0660  0.0084  62  LYS A C     
483  O  O     . LYS A 82  ? 0.3001 0.2558 0.1501 0.0235  0.0468  0.0158  62  LYS A O     
484  C  CB    . LYS A 82  ? 0.4463 0.2666 0.1898 -0.0185 0.0781  0.0265  62  LYS A CB    
485  C  CG    . LYS A 82  ? 0.5136 0.3153 0.1997 -0.0329 0.1359  0.0261  62  LYS A CG    
486  C  CD    . LYS A 82  ? 0.5858 0.3497 0.2322 -0.0149 0.1665  0.0198  62  LYS A CD    
487  C  CE    . LYS A 82  ? 0.6580 0.3936 0.2582 -0.0054 0.1655  0.0233  62  LYS A CE    
488  N  NZ    . LYS A 82  ? 0.7008 0.4168 0.2849 -0.0049 0.1561  0.0348  62  LYS A NZ    
489  N  N     . ASN A 83  ? 0.2846 0.2570 0.1355 -0.0106 0.0531  0.0103  63  ASN A N     
490  C  CA    . ASN A 83  ? 0.2793 0.2514 0.1383 -0.0062 0.0427  0.0114  63  ASN A CA    
491  C  C     . ASN A 83  ? 0.2530 0.2332 0.1287 0.0001  0.0470  0.0147  63  ASN A C     
492  O  O     . ASN A 83  ? 0.2500 0.2435 0.1368 0.0045  0.0334  0.0212  63  ASN A O     
493  C  CB    . ASN A 83  ? 0.2888 0.2654 0.1501 -0.0080 0.0502  0.0156  63  ASN A CB    
494  C  CG    . ASN A 83  ? 0.3121 0.2838 0.1715 -0.0123 0.0447  0.0024  63  ASN A CG    
495  O  OD1   . ASN A 83  ? 0.3445 0.3059 0.1687 -0.0128 0.0607  0.0081  63  ASN A OD1   
496  N  ND2   . ASN A 83  ? 0.3483 0.2920 0.1833 0.0129  0.0298  -0.0058 63  ASN A ND2   
497  N  N     . ILE A 84  ? 0.2280 0.2155 0.1225 0.0046  0.0332  0.0014  64  ILE A N     
498  C  CA    . ILE A 84  ? 0.2286 0.1974 0.1257 0.0133  0.0267  0.0168  64  ILE A CA    
499  C  C     . ILE A 84  ? 0.2364 0.2078 0.1291 0.0233  0.0166  0.0161  64  ILE A C     
500  O  O     . ILE A 84  ? 0.2275 0.2378 0.1219 0.0013  0.0068  0.0088  64  ILE A O     
501  C  CB    . ILE A 84  ? 0.2283 0.2019 0.1404 0.0049  0.0298  0.0077  64  ILE A CB    
502  C  CG1   . ILE A 84  ? 0.2220 0.2042 0.1426 0.0072  0.0152  0.0005  64  ILE A CG1   
503  C  CG2   . ILE A 84  ? 0.2451 0.2106 0.1417 0.0159  0.0050  0.0035  64  ILE A CG2   
504  C  CD1   . ILE A 84  ? 0.2241 0.2106 0.1578 0.0186  0.0016  0.0028  64  ILE A CD1   
505  N  N     . GLY A 85  ? 0.2499 0.2045 0.1306 0.0240  0.0170  0.0242  65  GLY A N     
506  C  CA    . GLY A 85  ? 0.2306 0.2130 0.1484 0.0128  0.0305  0.0176  65  GLY A CA    
507  C  C     . GLY A 85  ? 0.2333 0.2380 0.1507 0.0317  0.0250  0.0174  65  GLY A C     
508  O  O     . GLY A 85  ? 0.2248 0.2350 0.1400 0.0215  0.0122  0.0215  65  GLY A O     
509  N  N     . GLU A 86  ? 0.2344 0.2606 0.1587 0.0458  0.0400  0.0168  66  GLU A N     
510  C  CA    . GLU A 86  ? 0.2282 0.2855 0.1613 0.0386  0.0581  0.0137  66  GLU A CA    
511  C  C     . GLU A 86  ? 0.2053 0.2574 0.1544 0.0315  0.0416  0.0214  66  GLU A C     
512  O  O     . GLU A 86  ? 0.2318 0.2632 0.1444 0.0284  0.0202  0.0196  66  GLU A O     
513  C  CB    . GLU A 86  ? 0.3112 0.3391 0.1875 0.0493  0.0785  0.0007  66  GLU A CB    
514  C  CG    . GLU A 86  ? 0.4307 0.4081 0.2478 0.0474  0.0579  0.0078  66  GLU A CG    
515  C  CD    . GLU A 86  ? 0.5326 0.4668 0.3030 0.0565  0.0418  0.0031  66  GLU A CD    
516  O  OE1   . GLU A 86  ? 0.5556 0.4994 0.3172 0.0544  0.0352  0.0083  66  GLU A OE1   
517  O  OE2   . GLU A 86  ? 0.5769 0.4760 0.3359 0.0614  0.0398  0.0035  66  GLU A OE2   
518  N  N     . LEU A 87  ? 0.2032 0.2442 0.1523 0.0200  0.0292  0.0137  67  LEU A N     
519  C  CA    . LEU A 87  ? 0.2116 0.2293 0.1455 0.0151  0.0274  0.0174  67  LEU A CA    
520  C  C     . LEU A 87  ? 0.2079 0.2406 0.1381 0.0083  0.0228  0.0197  67  LEU A C     
521  O  O     . LEU A 87  ? 0.2236 0.2535 0.1397 0.0118  0.0228  0.0302  67  LEU A O     
522  C  CB    . LEU A 87  ? 0.2414 0.2436 0.1621 0.0066  0.0215  0.0172  67  LEU A CB    
523  C  CG    . LEU A 87  ? 0.2405 0.2522 0.1801 0.0111  0.0442  0.0127  67  LEU A CG    
524  C  CD1   . LEU A 87  ? 0.2482 0.2603 0.1859 0.0180  0.0500  0.0100  67  LEU A CD1   
525  C  CD2   . LEU A 87  ? 0.2635 0.2507 0.1967 0.0048  0.0484  0.0099  67  LEU A CD2   
526  N  N     . GLY A 88  ? 0.2142 0.2433 0.1321 -0.0087 0.0234  0.0174  68  GLY A N     
527  C  CA    . GLY A 88  ? 0.2245 0.2348 0.1246 -0.0014 0.0241  0.0233  68  GLY A CA    
528  C  C     . GLY A 88  ? 0.2008 0.2473 0.1290 0.0054  0.0241  0.0185  68  GLY A C     
529  O  O     . GLY A 88  ? 0.2184 0.2749 0.1277 -0.0150 0.0203  0.0247  68  GLY A O     
530  N  N     . LYS A 89  ? 0.2100 0.2515 0.1499 0.0091  0.0081  0.0111  69  LYS A N     
531  C  CA    . LYS A 89  ? 0.2257 0.2559 0.1575 0.0164  0.0104  0.0218  69  LYS A CA    
532  C  C     . LYS A 89  ? 0.2099 0.2563 0.1477 0.0071  0.0019  0.0270  69  LYS A C     
533  O  O     . LYS A 89  ? 0.2166 0.2820 0.1607 0.0029  -0.0042 0.0260  69  LYS A O     
534  C  CB    . LYS A 89  ? 0.2632 0.2839 0.1817 0.0424  0.0080  0.0144  69  LYS A CB    
535  C  CG    . LYS A 89  ? 0.3366 0.3198 0.2019 0.0630  0.0231  0.0021  69  LYS A CG    
536  C  CD    . LYS A 89  ? 0.4050 0.3537 0.2268 0.0787  0.0260  -0.0156 69  LYS A CD    
537  C  CE    . LYS A 89  ? 0.4572 0.3902 0.2486 0.0865  0.0276  -0.0241 69  LYS A CE    
538  N  NZ    . LYS A 89  ? 0.4876 0.4125 0.2621 0.0891  0.0232  -0.0302 69  LYS A NZ    
539  N  N     . THR A 90  ? 0.1968 0.2546 0.1551 0.0181  0.0103  0.0200  70  THR A N     
540  C  CA    . THR A 90  ? 0.1934 0.2670 0.1522 -0.0026 0.0197  0.0234  70  THR A CA    
541  C  C     . THR A 90  ? 0.2092 0.2611 0.1426 0.0033  0.0220  0.0157  70  THR A C     
542  O  O     . THR A 90  ? 0.2326 0.2706 0.1529 0.0066  0.0102  0.0252  70  THR A O     
543  C  CB    . THR A 90  ? 0.2129 0.2906 0.1677 -0.0133 0.0515  0.0237  70  THR A CB    
544  O  OG1   . THR A 90  ? 0.2545 0.3074 0.1714 -0.0060 0.0600  0.0141  70  THR A OG1   
545  C  CG2   . THR A 90  ? 0.2241 0.3061 0.1844 -0.0279 0.0510  0.0160  70  THR A CG2   
546  N  N     . PHE A 91  ? 0.2009 0.2476 0.1420 0.0139  0.0252  0.0137  71  PHE A N     
547  C  CA    . PHE A 91  ? 0.2154 0.2378 0.1291 0.0179  0.0142  0.0158  71  PHE A CA    
548  C  C     . PHE A 91  ? 0.2149 0.2373 0.1236 0.0030  0.0063  0.0205  71  PHE A C     
549  O  O     . PHE A 91  ? 0.2281 0.2451 0.1276 0.0127  0.0072  0.0208  71  PHE A O     
550  C  CB    . PHE A 91  ? 0.2346 0.2296 0.1259 0.0222  0.0221  0.0216  71  PHE A CB    
551  C  CG    . PHE A 91  ? 0.2509 0.2391 0.1449 0.0446  0.0264  0.0267  71  PHE A CG    
552  C  CD1   . PHE A 91  ? 0.2810 0.2583 0.1342 0.0651  0.0258  0.0249  71  PHE A CD1   
553  C  CD2   . PHE A 91  ? 0.2639 0.2502 0.1441 0.0433  0.0259  0.0380  71  PHE A CD2   
554  C  CE1   . PHE A 91  ? 0.2751 0.2622 0.1456 0.0615  0.0199  0.0281  71  PHE A CE1   
555  C  CE2   . PHE A 91  ? 0.2679 0.2657 0.1400 0.0400  0.0331  0.0420  71  PHE A CE2   
556  C  CZ    . PHE A 91  ? 0.2804 0.2676 0.1492 0.0578  0.0311  0.0351  71  PHE A CZ    
557  N  N     . SER A 92  ? 0.2266 0.2413 0.1351 -0.0016 0.0017  0.0392  72  SER A N     
558  C  CA    . SER A 92  ? 0.2440 0.2527 0.1464 -0.0137 -0.0111 0.0467  72  SER A CA    
559  C  C     . SER A 92  ? 0.2390 0.2625 0.1384 -0.0074 -0.0052 0.0332  72  SER A C     
560  O  O     . SER A 92  ? 0.2361 0.2660 0.1409 -0.0191 -0.0073 0.0404  72  SER A O     
561  C  CB    . SER A 92  ? 0.2931 0.2721 0.1768 -0.0507 -0.0269 0.0769  72  SER A CB    
562  O  OG    . SER A 92  ? 0.3423 0.3068 0.2061 -0.0655 -0.0325 0.0655  72  SER A OG    
563  N  N     . LYS A 93  ? 0.2293 0.2665 0.1418 0.0005  -0.0065 0.0150  73  LYS A N     
564  C  CA    . LYS A 93  ? 0.2389 0.3040 0.1605 0.0249  -0.0084 0.0055  73  LYS A CA    
565  C  C     . LYS A 93  ? 0.2220 0.3067 0.1566 0.0083  -0.0009 0.0243  73  LYS A C     
566  O  O     . LYS A 93  ? 0.2089 0.3228 0.1508 -0.0160 -0.0152 0.0256  73  LYS A O     
567  C  CB    . LYS A 93  ? 0.2698 0.3419 0.1970 0.0436  -0.0352 -0.0119 73  LYS A CB    
568  C  CG    . LYS A 93  ? 0.2946 0.3675 0.2330 0.0453  -0.0471 -0.0167 73  LYS A CG    
569  N  N     . GLY A 94  ? 0.2190 0.3065 0.1546 0.0162  0.0221  0.0304  74  GLY A N     
570  C  CA    . GLY A 94  ? 0.2295 0.2983 0.1716 -0.0145 0.0286  0.0294  74  GLY A CA    
571  C  C     . GLY A 94  ? 0.2064 0.2897 0.1637 -0.0472 0.0185  0.0291  74  GLY A C     
572  O  O     . GLY A 94  ? 0.2250 0.3120 0.1634 -0.0576 0.0121  -0.0056 74  GLY A O     
573  N  N     . LEU A 95  ? 0.1814 0.2650 0.1633 -0.0331 0.0101  0.0298  75  LEU A N     
574  C  CA    . LEU A 95  ? 0.1805 0.2513 0.1523 -0.0372 0.0130  0.0242  75  LEU A CA    
575  C  C     . LEU A 95  ? 0.1802 0.2430 0.1327 -0.0085 0.0042  0.0103  75  LEU A C     
576  O  O     . LEU A 95  ? 0.2055 0.2403 0.1396 -0.0060 0.0043  0.0082  75  LEU A O     
577  C  CB    . LEU A 95  ? 0.1884 0.2462 0.1598 -0.0339 0.0135  0.0259  75  LEU A CB    
578  C  CG    . LEU A 95  ? 0.1872 0.2347 0.1622 -0.0258 0.0100  0.0265  75  LEU A CG    
579  C  CD1   . LEU A 95  ? 0.2177 0.2510 0.1902 -0.0222 0.0010  0.0414  75  LEU A CD1   
580  C  CD2   . LEU A 95  ? 0.2358 0.2559 0.1549 0.0015  -0.0110 0.0146  75  LEU A CD2   
581  N  N     . LEU A 96  ? 0.1835 0.2400 0.1348 -0.0021 0.0088  0.0137  76  LEU A N     
582  C  CA    . LEU A 96  ? 0.1761 0.2413 0.1529 -0.0193 -0.0060 0.0158  76  LEU A CA    
583  C  C     . LEU A 96  ? 0.1778 0.2849 0.1689 -0.0365 -0.0100 0.0271  76  LEU A C     
584  O  O     . LEU A 96  ? 0.2312 0.3441 0.1928 -0.0497 -0.0347 0.0589  76  LEU A O     
585  C  CB    . LEU A 96  ? 0.1750 0.2435 0.1470 -0.0121 0.0043  0.0128  76  LEU A CB    
586  C  CG    . LEU A 96  ? 0.1739 0.2360 0.1448 0.0003  0.0086  0.0132  76  LEU A CG    
587  C  CD1   . LEU A 96  ? 0.1898 0.2426 0.1488 -0.0088 0.0031  -0.0056 76  LEU A CD1   
588  C  CD2   . LEU A 96  ? 0.2080 0.2448 0.1417 -0.0012 0.0070  0.0161  76  LEU A CD2   
589  N  N     . MET A 97  ? 0.1583 0.2863 0.1899 -0.0140 0.0164  0.0284  77  MET A N     
590  C  CA    . MET A 97  ? 0.1376 0.3305 0.2194 0.0058  0.0175  0.0225  77  MET A CA    
591  C  C     . MET A 97  ? 0.1608 0.3219 0.2339 -0.0180 -0.0082 0.0037  77  MET A C     
592  O  O     . MET A 97  ? 0.2062 0.3367 0.2327 -0.0296 -0.0075 -0.0001 77  MET A O     
593  C  CB    . MET A 97  ? 0.1802 0.4151 0.2599 0.0368  0.0308  0.0170  77  MET A CB    
594  C  CG    . MET A 97  ? 0.2495 0.5084 0.2973 0.0410  0.0766  0.0413  77  MET A CG    
595  S  SD    . MET A 97  ? 0.3653 0.5920 0.3484 0.0501  0.0925  0.0594  77  MET A SD    
596  C  CE    . MET A 97  ? 0.3809 0.6032 0.3730 0.0237  0.0918  0.0427  77  MET A CE    
597  N  N     . GLY A 98  ? 0.1953 0.3176 0.2496 -0.0580 0.0031  -0.0281 78  GLY A N     
598  C  CA    . GLY A 98  ? 0.2384 0.3146 0.2542 -0.0456 0.0084  -0.0417 78  GLY A CA    
599  C  C     . GLY A 98  ? 0.2385 0.3080 0.2381 -0.0251 0.0011  -0.0418 78  GLY A C     
600  O  O     . GLY A 98  ? 0.2621 0.2980 0.2298 -0.0050 -0.0065 -0.0410 78  GLY A O     
601  N  N     . ALA A 99  ? 0.2087 0.3135 0.2272 -0.0035 0.0040  -0.0494 79  ALA A N     
602  C  CA    . ALA A 99  ? 0.1978 0.3102 0.2095 0.0152  -0.0053 -0.0354 79  ALA A CA    
603  C  C     . ALA A 99  ? 0.2334 0.3267 0.2112 0.0377  -0.0381 -0.0166 79  ALA A C     
604  O  O     . ALA A 99  ? 0.3189 0.3511 0.2525 0.0736  -0.0601 -0.0297 79  ALA A O     
605  C  CB    . ALA A 99  ? 0.1637 0.3126 0.2098 -0.0041 0.0060  -0.0164 79  ALA A CB    
606  N  N     . ARG A 100 ? 0.1828 0.3171 0.1865 0.0382  -0.0111 -0.0158 80  ARG A N     
607  C  CA    . ARG A 100 ? 0.1930 0.3237 0.1893 0.0231  -0.0193 -0.0255 80  ARG A CA    
608  C  C     . ARG A 100 ? 0.1760 0.3102 0.1690 -0.0054 -0.0258 -0.0246 80  ARG A C     
609  O  O     . ARG A 100 ? 0.1888 0.3022 0.1758 0.0059  -0.0253 -0.0365 80  ARG A O     
610  C  CB    . ARG A 100 ? 0.2253 0.3503 0.2172 -0.0010 0.0041  -0.0356 80  ARG A CB    
611  C  CG    . ARG A 100 ? 0.2751 0.3749 0.2446 -0.0066 0.0186  -0.0320 80  ARG A CG    
612  N  N     . GLY A 101 ? 0.1794 0.3075 0.1471 -0.0009 -0.0089 -0.0261 81  GLY A N     
613  C  CA    . GLY A 101 ? 0.1899 0.2942 0.1531 0.0242  -0.0019 -0.0316 81  GLY A CA    
614  C  C     . GLY A 101 ? 0.2026 0.2735 0.1448 0.0319  -0.0066 -0.0318 81  GLY A C     
615  O  O     . GLY A 101 ? 0.2064 0.2892 0.1419 0.0179  -0.0031 -0.0322 81  GLY A O     
616  N  N     . ASN A 102 ? 0.1985 0.2518 0.1334 0.0163  -0.0062 -0.0144 82  ASN A N     
617  C  CA    . ASN A 102 ? 0.2114 0.2335 0.1262 0.0076  -0.0031 -0.0086 82  ASN A CA    
618  C  C     . ASN A 102 ? 0.1972 0.2282 0.1250 0.0164  -0.0026 -0.0107 82  ASN A C     
619  O  O     . ASN A 102 ? 0.1938 0.2397 0.1216 0.0175  -0.0057 -0.0207 82  ASN A O     
620  C  CB    . ASN A 102 ? 0.2447 0.2407 0.1283 -0.0032 0.0044  0.0071  82  ASN A CB    
621  C  CG    . ASN A 102 ? 0.3350 0.2584 0.1433 -0.0150 0.0085  0.0014  82  ASN A CG    
622  O  OD1   . ASN A 102 ? 0.4413 0.2850 0.1638 -0.0055 -0.0054 0.0009  82  ASN A OD1   
623  N  ND2   . ASN A 102 ? 0.3329 0.2835 0.1403 -0.0423 0.0191  -0.0004 82  ASN A ND2   
624  N  N     . SER A 103 ? 0.1943 0.2148 0.1211 0.0125  -0.0094 -0.0088 83  SER A N     
625  C  CA    . SER A 103 ? 0.1855 0.2108 0.1130 0.0017  -0.0023 -0.0142 83  SER A CA    
626  C  C     . SER A 103 ? 0.1794 0.2124 0.1178 0.0042  -0.0012 -0.0128 83  SER A C     
627  O  O     . SER A 103 ? 0.1830 0.2279 0.1123 0.0110  -0.0143 -0.0127 83  SER A O     
628  C  CB    . SER A 103 ? 0.1887 0.2144 0.1303 -0.0008 -0.0082 0.0016  83  SER A CB    
629  O  OG    . SER A 103 ? 0.1966 0.2114 0.1351 0.0020  -0.0119 -0.0181 83  SER A OG    
630  N  N     . GLY A 104 ? 0.1825 0.2269 0.1239 -0.0149 -0.0016 -0.0219 84  GLY A N     
631  C  CA    . GLY A 104 ? 0.1833 0.2325 0.1298 -0.0151 0.0105  -0.0155 84  GLY A CA    
632  C  C     . GLY A 104 ? 0.1466 0.2233 0.1234 -0.0044 0.0130  -0.0034 84  GLY A C     
633  O  O     . GLY A 104 ? 0.1722 0.2305 0.1209 -0.0030 0.0106  -0.0035 84  GLY A O     
634  N  N     . VAL A 105 ? 0.1717 0.2213 0.1094 0.0076  0.0066  -0.0041 85  VAL A N     
635  C  CA    . VAL A 105 ? 0.1822 0.2169 0.1172 0.0160  -0.0084 -0.0009 85  VAL A CA    
636  C  C     . VAL A 105 ? 0.1726 0.1974 0.1189 0.0055  0.0084  -0.0011 85  VAL A C     
637  O  O     . VAL A 105 ? 0.1737 0.1926 0.1078 0.0107  0.0025  -0.0116 85  VAL A O     
638  C  CB    . VAL A 105 ? 0.1878 0.2362 0.1397 0.0239  -0.0159 -0.0035 85  VAL A CB    
639  C  CG1   . VAL A 105 ? 0.2421 0.2429 0.1498 0.0152  -0.0145 0.0022  85  VAL A CG1   
640  C  CG2   . VAL A 105 ? 0.1931 0.2547 0.1518 0.0290  -0.0160 -0.0106 85  VAL A CG2   
641  N  N     . ILE A 106 ? 0.1773 0.1960 0.1173 0.0014  0.0027  -0.0063 86  ILE A N     
642  C  CA    . ILE A 106 ? 0.1631 0.1993 0.1229 0.0023  0.0131  -0.0014 86  ILE A CA    
643  C  C     . ILE A 106 ? 0.1502 0.2020 0.1287 -0.0035 0.0077  -0.0044 86  ILE A C     
644  O  O     . ILE A 106 ? 0.1656 0.2072 0.1232 0.0006  -0.0025 -0.0161 86  ILE A O     
645  C  CB    . ILE A 106 ? 0.1698 0.2023 0.1338 0.0021  0.0062  0.0076  86  ILE A CB    
646  C  CG1   . ILE A 106 ? 0.1821 0.2104 0.1414 -0.0119 0.0212  -0.0001 86  ILE A CG1   
647  C  CG2   . ILE A 106 ? 0.1933 0.2095 0.1543 -0.0145 0.0058  -0.0119 86  ILE A CG2   
648  C  CD1   . ILE A 106 ? 0.1780 0.2403 0.1570 0.0028  0.0179  -0.0126 86  ILE A CD1   
649  N  N     . LEU A 107 ? 0.1652 0.1969 0.1254 0.0023  -0.0100 -0.0032 87  LEU A N     
650  C  CA    . LEU A 107 ? 0.1677 0.1859 0.1180 -0.0023 -0.0033 0.0011  87  LEU A CA    
651  C  C     . LEU A 107 ? 0.1762 0.1880 0.1084 -0.0038 0.0033  0.0046  87  LEU A C     
652  O  O     . LEU A 107 ? 0.1842 0.1949 0.1030 0.0098  -0.0104 0.0107  87  LEU A O     
653  C  CB    . LEU A 107 ? 0.1860 0.1939 0.1249 0.0080  -0.0031 0.0068  87  LEU A CB    
654  C  CG    . LEU A 107 ? 0.2215 0.2053 0.1418 0.0008  -0.0039 0.0183  87  LEU A CG    
655  C  CD1   . LEU A 107 ? 0.2383 0.2041 0.1566 -0.0166 -0.0142 0.0124  87  LEU A CD1   
656  C  CD2   . LEU A 107 ? 0.2414 0.2166 0.1635 -0.0007 0.0050  0.0201  87  LEU A CD2   
657  N  N     . SER A 108 ? 0.1768 0.1813 0.1190 0.0082  -0.0076 -0.0050 88  SER A N     
658  C  CA    . SER A 108 ? 0.1686 0.1913 0.1171 0.0114  0.0008  -0.0029 88  SER A CA    
659  C  C     . SER A 108 ? 0.1591 0.1860 0.1222 0.0140  0.0057  -0.0058 88  SER A C     
660  O  O     . SER A 108 ? 0.1906 0.2081 0.1164 -0.0072 0.0063  -0.0121 88  SER A O     
661  C  CB    . SER A 108 ? 0.1686 0.2085 0.1156 -0.0012 0.0144  0.0088  88  SER A CB    
662  O  OG    . SER A 108 ? 0.1638 0.2168 0.1187 0.0025  0.0085  0.0064  88  SER A OG    
663  N  N     . GLN A 109 ? 0.1582 0.1899 0.1213 -0.0021 0.0139  -0.0011 89  GLN A N     
664  C  CA    . GLN A 109 ? 0.1623 0.1905 0.1162 -0.0053 0.0092  -0.0023 89  GLN A CA    
665  C  C     . GLN A 109 ? 0.1702 0.1889 0.1095 -0.0006 0.0116  -0.0068 89  GLN A C     
666  O  O     . GLN A 109 ? 0.1948 0.2017 0.1145 0.0074  0.0082  0.0034  89  GLN A O     
667  C  CB    . GLN A 109 ? 0.1614 0.2052 0.1159 0.0003  0.0000  -0.0002 89  GLN A CB    
668  C  CG    . GLN A 109 ? 0.1667 0.2144 0.1251 -0.0010 0.0054  0.0044  89  GLN A CG    
669  C  CD    . GLN A 109 ? 0.1673 0.2077 0.1335 0.0145  -0.0052 0.0072  89  GLN A CD    
670  O  OE1   . GLN A 109 ? 0.1897 0.2078 0.1430 0.0029  -0.0093 -0.0137 89  GLN A OE1   
671  N  NE2   . GLN A 109 ? 0.1803 0.2180 0.1340 0.0070  0.0140  0.0213  89  GLN A NE2   
672  N  N     . LEU A 110 ? 0.1720 0.1800 0.1109 0.0103  -0.0040 -0.0034 90  LEU A N     
673  C  CA    . LEU A 110 ? 0.1628 0.1809 0.1225 0.0122  -0.0088 0.0140  90  LEU A CA    
674  C  C     . LEU A 110 ? 0.1737 0.1986 0.1211 -0.0080 -0.0064 0.0113  90  LEU A C     
675  O  O     . LEU A 110 ? 0.1895 0.2144 0.1156 -0.0113 -0.0070 0.0049  90  LEU A O     
676  C  CB    . LEU A 110 ? 0.1743 0.2007 0.1372 0.0255  -0.0106 0.0210  90  LEU A CB    
677  C  CG    . LEU A 110 ? 0.1662 0.2087 0.1426 0.0137  0.0028  0.0075  90  LEU A CG    
678  C  CD1   . LEU A 110 ? 0.1681 0.2288 0.1644 0.0361  0.0037  -0.0023 90  LEU A CD1   
679  C  CD2   . LEU A 110 ? 0.1751 0.2187 0.1439 0.0114  -0.0021 0.0140  90  LEU A CD2   
680  N  N     . PHE A 111 ? 0.1703 0.1967 0.1212 -0.0061 0.0083  0.0015  91  PHE A N     
681  C  CA    . PHE A 111 ? 0.1958 0.1951 0.1161 -0.0023 0.0002  0.0159  91  PHE A CA    
682  C  C     . PHE A 111 ? 0.1712 0.2039 0.1180 -0.0024 0.0037  0.0129  91  PHE A C     
683  O  O     . PHE A 111 ? 0.1906 0.2275 0.1148 0.0013  -0.0074 -0.0030 91  PHE A O     
684  C  CB    . PHE A 111 ? 0.2584 0.2188 0.1259 0.0021  0.0190  0.0122  91  PHE A CB    
685  C  CG    . PHE A 111 ? 0.3908 0.2297 0.1463 0.0398  0.0163  0.0307  91  PHE A CG    
686  C  CD1   . PHE A 111 ? 0.4456 0.2426 0.1705 0.0751  -0.0012 0.0419  91  PHE A CD1   
687  C  CD2   . PHE A 111 ? 0.4830 0.2419 0.1659 0.0920  0.0075  0.0272  91  PHE A CD2   
688  C  CE1   . PHE A 111 ? 0.5112 0.2739 0.1903 0.0911  -0.0193 0.0346  91  PHE A CE1   
689  C  CE2   . PHE A 111 ? 0.5404 0.2608 0.1758 0.1281  -0.0168 0.0255  91  PHE A CE2   
690  C  CZ    . PHE A 111 ? 0.5508 0.2842 0.1908 0.1276  -0.0254 0.0264  91  PHE A CZ    
691  N  N     . ARG A 112 ? 0.1837 0.1976 0.1146 0.0134  0.0102  -0.0019 92  ARG A N     
692  C  CA    . ARG A 112 ? 0.1784 0.2086 0.1156 0.0173  -0.0058 -0.0054 92  ARG A CA    
693  C  C     . ARG A 112 ? 0.1814 0.2042 0.1219 0.0097  0.0044  0.0061  92  ARG A C     
694  O  O     . ARG A 112 ? 0.1952 0.2082 0.1230 0.0165  0.0091  -0.0095 92  ARG A O     
695  C  CB    . ARG A 112 ? 0.1871 0.2223 0.1201 0.0154  0.0040  -0.0069 92  ARG A CB    
696  C  CG    . ARG A 112 ? 0.2069 0.2391 0.1414 0.0163  0.0041  0.0103  92  ARG A CG    
697  C  CD    . ARG A 112 ? 0.2109 0.2590 0.1571 0.0117  0.0083  0.0013  92  ARG A CD    
698  N  NE    . ARG A 112 ? 0.1914 0.2550 0.1590 0.0162  0.0104  -0.0126 92  ARG A NE    
699  C  CZ    . ARG A 112 ? 0.1977 0.2573 0.1592 0.0176  -0.0004 -0.0200 92  ARG A CZ    
700  N  NH1   . ARG A 112 ? 0.2128 0.2614 0.1601 0.0165  0.0186  -0.0241 92  ARG A NH1   
701  N  NH2   . ARG A 112 ? 0.2278 0.2567 0.1684 0.0232  0.0099  -0.0019 92  ARG A NH2   
702  N  N     . GLY A 113 ? 0.1944 0.1949 0.1264 0.0068  0.0027  -0.0033 93  GLY A N     
703  C  CA    . GLY A 113 ? 0.1882 0.1849 0.1301 -0.0140 0.0023  0.0095  93  GLY A CA    
704  C  C     . GLY A 113 ? 0.1944 0.1963 0.1252 -0.0100 0.0018  0.0013  93  GLY A C     
705  O  O     . GLY A 113 ? 0.2234 0.2104 0.1228 0.0012  -0.0047 -0.0087 93  GLY A O     
706  N  N     . PHE A 114 ? 0.1846 0.1905 0.1097 -0.0122 -0.0069 -0.0024 94  PHE A N     
707  C  CA    . PHE A 114 ? 0.1956 0.1976 0.1190 -0.0096 0.0040  0.0116  94  PHE A CA    
708  C  C     . PHE A 114 ? 0.2049 0.2001 0.1137 0.0034  -0.0008 0.0000  94  PHE A C     
709  O  O     . PHE A 114 ? 0.2121 0.2138 0.1147 -0.0016 0.0029  -0.0084 94  PHE A O     
710  C  CB    . PHE A 114 ? 0.1825 0.2039 0.1361 -0.0024 -0.0053 0.0051  94  PHE A CB    
711  C  CG    . PHE A 114 ? 0.1735 0.2039 0.1466 -0.0131 -0.0049 0.0171  94  PHE A CG    
712  C  CD1   . PHE A 114 ? 0.1934 0.2167 0.1573 0.0033  -0.0110 0.0174  94  PHE A CD1   
713  C  CD2   . PHE A 114 ? 0.1800 0.2150 0.1428 -0.0207 -0.0069 0.0182  94  PHE A CD2   
714  C  CE1   . PHE A 114 ? 0.2054 0.2285 0.1799 -0.0022 0.0032  0.0265  94  PHE A CE1   
715  C  CE2   . PHE A 114 ? 0.1932 0.2324 0.1722 -0.0200 -0.0030 0.0275  94  PHE A CE2   
716  C  CZ    . PHE A 114 ? 0.1919 0.2421 0.1799 -0.0107 -0.0035 0.0272  94  PHE A CZ    
717  N  N     . CYS A 115 ? 0.1851 0.2093 0.1170 -0.0013 -0.0059 -0.0022 95  CYS A N     
718  C  CA    . CYS A 115 ? 0.1907 0.2034 0.1274 0.0049  0.0118  -0.0035 95  CYS A CA    
719  C  C     . CYS A 115 ? 0.2031 0.2013 0.1325 -0.0051 0.0236  0.0058  95  CYS A C     
720  O  O     . CYS A 115 ? 0.2411 0.2001 0.1275 -0.0035 0.0297  -0.0017 95  CYS A O     
721  C  CB    . CYS A 115 ? 0.2129 0.2054 0.1411 0.0057  0.0227  0.0045  95  CYS A CB    
722  S  SG    . CYS A 115 ? 0.2242 0.2207 0.1459 -0.0095 0.0184  0.0107  95  CYS A SG    
723  N  N     . LYS A 116 ? 0.2166 0.2039 0.1282 0.0036  0.0111  0.0023  96  LYS A N     
724  C  CA    . LYS A 116 ? 0.2303 0.2055 0.1472 0.0091  0.0052  0.0090  96  LYS A CA    
725  C  C     . LYS A 116 ? 0.2267 0.2179 0.1358 -0.0035 0.0167  -0.0066 96  LYS A C     
726  O  O     . LYS A 116 ? 0.2543 0.2222 0.1507 0.0079  0.0174  -0.0148 96  LYS A O     
727  C  CB    . LYS A 116 ? 0.2428 0.2061 0.1574 0.0231  0.0176  0.0077  96  LYS A CB    
728  C  CG    . LYS A 116 ? 0.3083 0.2397 0.1953 0.0553  0.0239  0.0090  96  LYS A CG    
729  C  CD    . LYS A 116 ? 0.3733 0.2750 0.2320 0.0992  0.0279  0.0016  96  LYS A CD    
730  C  CE    . LYS A 116 ? 0.4323 0.3288 0.2684 0.1081  0.0222  -0.0026 96  LYS A CE    
731  N  NZ    . LYS A 116 ? 0.4628 0.3645 0.2836 0.1211  0.0348  0.0058  96  LYS A NZ    
732  N  N     . ASN A 117 ? 0.2323 0.2204 0.1281 -0.0096 0.0024  -0.0047 97  ASN A N     
733  C  CA    . ASN A 117 ? 0.2285 0.2215 0.1454 -0.0228 0.0147  0.0008  97  ASN A CA    
734  C  C     . ASN A 117 ? 0.2444 0.2486 0.1340 -0.0241 0.0011  -0.0029 97  ASN A C     
735  O  O     . ASN A 117 ? 0.2864 0.2859 0.1474 -0.0319 -0.0014 -0.0162 97  ASN A O     
736  C  CB    . ASN A 117 ? 0.2338 0.2279 0.1609 -0.0396 0.0189  -0.0049 97  ASN A CB    
737  C  CG    . ASN A 117 ? 0.2657 0.2434 0.1817 -0.0389 0.0104  -0.0291 97  ASN A CG    
738  O  OD1   . ASN A 117 ? 0.3022 0.2593 0.2263 -0.0418 0.0056  -0.0273 97  ASN A OD1   
739  N  ND2   . ASN A 117 ? 0.2489 0.2721 0.1807 -0.0238 0.0008  -0.0492 97  ASN A ND2   
740  N  N     . ILE A 118 ? 0.2302 0.2506 0.1230 -0.0264 0.0072  0.0119  98  ILE A N     
741  C  CA    . ILE A 118 ? 0.2474 0.2611 0.1346 -0.0008 0.0126  0.0248  98  ILE A CA    
742  C  C     . ILE A 118 ? 0.2677 0.2439 0.1379 0.0073  0.0302  0.0004  98  ILE A C     
743  O  O     . ILE A 118 ? 0.2845 0.2356 0.1359 0.0062  0.0395  0.0015  98  ILE A O     
744  C  CB    . ILE A 118 ? 0.2897 0.2703 0.1559 0.0224  0.0271  0.0399  98  ILE A CB    
745  C  CG1   . ILE A 118 ? 0.3404 0.2420 0.1467 0.0333  0.0308  0.0176  98  ILE A CG1   
746  C  CG2   . ILE A 118 ? 0.3249 0.3026 0.1935 0.0211  0.0513  0.0796  98  ILE A CG2   
747  C  CD1   . ILE A 118 ? 0.3788 0.2556 0.1577 0.0182  0.0510  0.0316  98  ILE A CD1   
748  N  N     . GLU A 119 ? 0.2806 0.2558 0.1737 0.0231  0.0395  0.0175  99  GLU A N     
749  C  CA    A GLU A 119 ? 0.3208 0.2740 0.2008 0.0404  0.0485  0.0252  99  GLU A CA    
750  C  CA    B GLU A 119 ? 0.3298 0.2699 0.1932 0.0535  0.0493  0.0228  99  GLU A CA    
751  C  C     . GLU A 119 ? 0.3422 0.2744 0.2051 0.0711  0.0446  0.0230  99  GLU A C     
752  O  O     . GLU A 119 ? 0.3533 0.2904 0.2271 0.0653  0.0522  0.0283  99  GLU A O     
753  C  CB    A GLU A 119 ? 0.3500 0.2959 0.2185 0.0328  0.0469  0.0362  99  GLU A CB    
754  C  CB    B GLU A 119 ? 0.3741 0.2826 0.1953 0.0703  0.0504  0.0292  99  GLU A CB    
755  C  CG    A GLU A 119 ? 0.3938 0.3086 0.2415 0.0230  0.0448  0.0285  99  GLU A CG    
756  C  CG    B GLU A 119 ? 0.4268 0.2826 0.2038 0.0881  0.0553  0.0128  99  GLU A CG    
757  C  CD    A GLU A 119 ? 0.4254 0.3083 0.2512 0.0135  0.0387  0.0327  99  GLU A CD    
758  C  CD    B GLU A 119 ? 0.4894 0.3026 0.2294 0.0758  0.0521  0.0078  99  GLU A CD    
759  O  OE1   A GLU A 119 ? 0.4345 0.3059 0.2559 0.0089  0.0388  0.0309  99  GLU A OE1   
760  O  OE1   B GLU A 119 ? 0.4989 0.3092 0.2277 0.0894  0.0462  0.0064  99  GLU A OE1   
761  O  OE2   A GLU A 119 ? 0.4452 0.3169 0.2535 0.0031  0.0245  0.0275  99  GLU A OE2   
762  O  OE2   B GLU A 119 ? 0.5230 0.3082 0.2489 0.0650  0.0549  0.0124  99  GLU A OE2   
763  N  N     . SER A 120 ? 0.3589 0.2740 0.1954 0.0718  0.0436  -0.0036 100 SER A N     
764  C  CA    A SER A 120 ? 0.3982 0.2929 0.2023 0.0712  0.0421  -0.0183 100 SER A CA    
765  C  CA    B SER A 120 ? 0.3946 0.2866 0.1981 0.0783  0.0388  -0.0176 100 SER A CA    
766  C  C     . SER A 120 ? 0.4011 0.2938 0.1892 0.0750  0.0408  -0.0258 100 SER A C     
767  O  O     . SER A 120 ? 0.4149 0.3300 0.1891 0.0866  0.0479  -0.0378 100 SER A O     
768  C  CB    A SER A 120 ? 0.4328 0.3224 0.2312 0.0551  0.0316  -0.0201 100 SER A CB    
769  C  CB    B SER A 120 ? 0.4229 0.3042 0.2193 0.0774  0.0206  -0.0174 100 SER A CB    
770  O  OG    A SER A 120 ? 0.4578 0.3427 0.2552 0.0465  0.0211  -0.0196 100 SER A OG    
771  O  OG    B SER A 120 ? 0.4419 0.3108 0.2353 0.0910  0.0025  -0.0136 100 SER A OG    
772  N  N     . GLU A 121 ? 0.3652 0.2617 0.1711 0.0576  0.0317  -0.0243 101 GLU A N     
773  C  CA    . GLU A 121 ? 0.3401 0.2722 0.1717 0.0363  0.0253  -0.0054 101 GLU A CA    
774  C  C     . GLU A 121 ? 0.3114 0.2770 0.1485 0.0368  0.0165  -0.0083 101 GLU A C     
775  O  O     . GLU A 121 ? 0.3174 0.2831 0.1577 0.0292  0.0072  -0.0215 101 GLU A O     
776  C  CB    . GLU A 121 ? 0.3582 0.2936 0.1947 0.0018  0.0371  0.0116  101 GLU A CB    
777  C  CG    . GLU A 121 ? 0.4117 0.3509 0.2405 -0.0330 0.0377  0.0158  101 GLU A CG    
778  C  CD    . GLU A 121 ? 0.4885 0.4065 0.2854 -0.0561 0.0323  0.0225  101 GLU A CD    
779  O  OE1   . GLU A 121 ? 0.5012 0.4330 0.2910 -0.0562 0.0155  0.0088  101 GLU A OE1   
780  O  OE2   . GLU A 121 ? 0.5456 0.4332 0.3227 -0.0840 0.0273  0.0183  101 GLU A OE2   
781  N  N     . SER A 122 ? 0.3086 0.2926 0.1409 0.0214  0.0261  0.0050  102 SER A N     
782  C  CA    . SER A 122 ? 0.3123 0.3056 0.1439 0.0235  0.0264  0.0242  102 SER A CA    
783  C  C     . SER A 122 ? 0.2804 0.2844 0.1349 0.0156  0.0132  0.0239  102 SER A C     
784  O  O     . SER A 122 ? 0.2793 0.2817 0.1206 0.0059  0.0063  0.0381  102 SER A O     
785  C  CB    . SER A 122 ? 0.3739 0.3546 0.1647 0.0400  0.0383  0.0128  102 SER A CB    
786  O  OG    . SER A 122 ? 0.4363 0.3832 0.1729 0.0297  0.0373  0.0118  102 SER A OG    
787  N  N     . GLU A 123 ? 0.2884 0.2730 0.1537 0.0035  0.0143  0.0081  103 GLU A N     
788  C  CA    . GLU A 123 ? 0.2986 0.2824 0.1677 0.0011  0.0155  0.0150  103 GLU A CA    
789  C  C     . GLU A 123 ? 0.2777 0.2643 0.1768 -0.0137 0.0010  0.0093  103 GLU A C     
790  O  O     . GLU A 123 ? 0.3092 0.2739 0.2022 0.0031  0.0242  -0.0173 103 GLU A O     
791  C  CB    . GLU A 123 ? 0.3843 0.3427 0.2019 -0.0101 0.0248  0.0139  103 GLU A CB    
792  C  CG    . GLU A 123 ? 0.4868 0.4171 0.2413 -0.0237 0.0314  -0.0063 103 GLU A CG    
793  C  CD    . GLU A 123 ? 0.5532 0.4843 0.2674 -0.0407 0.0240  -0.0342 103 GLU A CD    
794  O  OE1   . GLU A 123 ? 0.5876 0.5166 0.2951 -0.0527 0.0397  -0.0593 103 GLU A OE1   
795  O  OE2   . GLU A 123 ? 0.5531 0.4972 0.2669 -0.0437 0.0277  -0.0245 103 GLU A OE2   
796  N  N     . ILE A 124 ? 0.2481 0.2424 0.1655 -0.0103 -0.0125 0.0145  104 ILE A N     
797  C  CA    . ILE A 124 ? 0.2566 0.2469 0.1597 -0.0066 -0.0001 0.0226  104 ILE A CA    
798  C  C     . ILE A 124 ? 0.2608 0.2507 0.1601 -0.0035 -0.0025 0.0165  104 ILE A C     
799  O  O     . ILE A 124 ? 0.2768 0.2503 0.1987 -0.0090 -0.0292 0.0093  104 ILE A O     
800  C  CB    . ILE A 124 ? 0.2557 0.2557 0.1601 0.0031  0.0043  0.0252  104 ILE A CB    
801  C  CG1   . ILE A 124 ? 0.2442 0.2596 0.1539 0.0284  0.0027  0.0307  104 ILE A CG1   
802  C  CG2   . ILE A 124 ? 0.2932 0.2572 0.1730 -0.0013 -0.0073 0.0338  104 ILE A CG2   
803  C  CD1   . ILE A 124 ? 0.2509 0.2802 0.1557 0.0152  -0.0130 0.0526  104 ILE A CD1   
804  N  N     . ASN A 125 ? 0.2588 0.2738 0.1570 0.0065  -0.0088 0.0161  105 ASN A N     
805  C  CA    . ASN A 125 ? 0.2346 0.2869 0.1485 -0.0125 -0.0233 0.0046  105 ASN A CA    
806  C  C     . ASN A 125 ? 0.2146 0.2682 0.1327 -0.0079 -0.0317 0.0105  105 ASN A C     
807  O  O     . ASN A 125 ? 0.2232 0.2671 0.1381 -0.0185 -0.0330 0.0234  105 ASN A O     
808  C  CB    . ASN A 125 ? 0.2639 0.3031 0.1379 -0.0147 -0.0188 -0.0045 105 ASN A CB    
809  C  CG    . ASN A 125 ? 0.3292 0.3045 0.1544 -0.0121 -0.0275 -0.0277 105 ASN A CG    
810  O  OD1   . ASN A 125 ? 0.3590 0.3021 0.1453 -0.0065 -0.0359 -0.0135 105 ASN A OD1   
811  N  ND2   . ASN A 125 ? 0.3861 0.3230 0.1784 -0.0338 -0.0405 -0.0365 105 ASN A ND2   
812  N  N     . SER A 126 ? 0.2282 0.2734 0.1380 -0.0117 -0.0294 0.0039  106 SER A N     
813  C  CA    . SER A 126 ? 0.2271 0.2725 0.1512 -0.0045 -0.0154 0.0079  106 SER A CA    
814  C  C     . SER A 126 ? 0.2242 0.2579 0.1515 -0.0178 -0.0132 0.0072  106 SER A C     
815  O  O     . SER A 126 ? 0.2023 0.2471 0.1455 -0.0110 -0.0190 0.0104  106 SER A O     
816  C  CB    . SER A 126 ? 0.2577 0.2965 0.1721 0.0074  -0.0224 0.0018  106 SER A CB    
817  O  OG    . SER A 126 ? 0.2818 0.3100 0.1817 0.0069  -0.0436 0.0230  106 SER A OG    
818  N  N     . LYS A 127 ? 0.2440 0.2622 0.1388 -0.0284 -0.0314 0.0112  107 LYS A N     
819  C  CA    . LYS A 127 ? 0.2636 0.2583 0.1648 -0.0264 -0.0392 -0.0058 107 LYS A CA    
820  C  C     . LYS A 127 ? 0.2559 0.2432 0.1419 -0.0212 -0.0237 -0.0094 107 LYS A C     
821  O  O     . LYS A 127 ? 0.2659 0.2428 0.1276 -0.0238 -0.0180 -0.0024 107 LYS A O     
822  C  CB    . LYS A 127 ? 0.2909 0.2698 0.2073 -0.0229 -0.0693 -0.0082 107 LYS A CB    
823  C  CG    . LYS A 127 ? 0.3521 0.2959 0.2378 -0.0133 -0.0778 -0.0086 107 LYS A CG    
824  N  N     . LEU A 128 ? 0.2383 0.2409 0.1344 -0.0038 -0.0059 -0.0128 108 LEU A N     
825  C  CA    A LEU A 128 ? 0.2379 0.2390 0.1428 -0.0006 0.0054  -0.0091 108 LEU A CA    
826  C  CA    B LEU A 128 ? 0.2413 0.2442 0.1533 -0.0042 0.0037  -0.0170 108 LEU A CA    
827  C  C     . LEU A 128 ? 0.2390 0.2381 0.1371 -0.0171 -0.0097 -0.0019 108 LEU A C     
828  O  O     . LEU A 128 ? 0.2582 0.2506 0.1267 0.0040  -0.0294 0.0089  108 LEU A O     
829  C  CB    A LEU A 128 ? 0.2615 0.2528 0.1614 0.0109  0.0240  0.0022  108 LEU A CB    
830  C  CB    B LEU A 128 ? 0.2726 0.2673 0.1925 0.0014  0.0203  -0.0224 108 LEU A CB    
831  C  CG    A LEU A 128 ? 0.2944 0.2700 0.1892 0.0139  0.0221  0.0116  108 LEU A CG    
832  C  CG    B LEU A 128 ? 0.3165 0.2945 0.2381 -0.0041 0.0216  -0.0282 108 LEU A CG    
833  C  CD1   A LEU A 128 ? 0.3022 0.2602 0.1969 0.0209  0.0060  0.0076  108 LEU A CD1   
834  C  CD1   B LEU A 128 ? 0.3377 0.3127 0.2516 -0.0070 0.0092  -0.0392 108 LEU A CD1   
835  C  CD2   A LEU A 128 ? 0.3151 0.2888 0.2065 0.0036  0.0167  0.0045  108 LEU A CD2   
836  C  CD2   B LEU A 128 ? 0.3358 0.3029 0.2561 -0.0102 0.0132  -0.0228 108 LEU A CD2   
837  N  N     . LEU A 129 ? 0.2406 0.2233 0.1260 -0.0220 -0.0159 0.0062  109 LEU A N     
838  C  CA    . LEU A 129 ? 0.2229 0.2259 0.1302 -0.0234 -0.0052 0.0063  109 LEU A CA    
839  C  C     . LEU A 129 ? 0.1826 0.2390 0.1271 -0.0328 -0.0136 0.0072  109 LEU A C     
840  O  O     . LEU A 129 ? 0.2066 0.2386 0.1183 -0.0171 -0.0208 0.0135  109 LEU A O     
841  C  CB    . LEU A 129 ? 0.2196 0.2190 0.1425 -0.0235 -0.0076 0.0081  109 LEU A CB    
842  C  CG    . LEU A 129 ? 0.2101 0.2315 0.1500 -0.0085 -0.0210 0.0134  109 LEU A CG    
843  C  CD1   . LEU A 129 ? 0.1982 0.2414 0.1731 -0.0265 -0.0060 0.0084  109 LEU A CD1   
844  C  CD2   . LEU A 129 ? 0.2473 0.2420 0.1647 0.0000  -0.0151 0.0137  109 LEU A CD2   
845  N  N     . ALA A 130 ? 0.1883 0.2404 0.1314 -0.0238 -0.0115 0.0031  110 ALA A N     
846  C  CA    . ALA A 130 ? 0.1801 0.2372 0.1317 -0.0169 -0.0078 -0.0116 110 ALA A CA    
847  C  C     . ALA A 130 ? 0.1965 0.2294 0.1328 -0.0111 -0.0101 -0.0008 110 ALA A C     
848  O  O     . ALA A 130 ? 0.2100 0.2325 0.1142 -0.0117 -0.0033 0.0135  110 ALA A O     
849  C  CB    . ALA A 130 ? 0.1781 0.2602 0.1355 -0.0237 -0.0079 -0.0137 110 ALA A CB    
850  N  N     . GLU A 131 ? 0.2143 0.2176 0.1451 -0.0249 -0.0185 0.0006  111 GLU A N     
851  C  CA    . GLU A 131 ? 0.2369 0.2437 0.1624 -0.0182 -0.0162 -0.0172 111 GLU A CA    
852  C  C     . GLU A 131 ? 0.2267 0.2191 0.1309 -0.0057 -0.0044 -0.0020 111 GLU A C     
853  O  O     . GLU A 131 ? 0.2437 0.2070 0.1274 -0.0105 -0.0171 0.0054  111 GLU A O     
854  C  CB    . GLU A 131 ? 0.2776 0.3129 0.2131 -0.0182 -0.0250 -0.0466 111 GLU A CB    
855  C  CG    . GLU A 131 ? 0.3449 0.4092 0.2660 -0.0510 -0.0436 -0.0714 111 GLU A CG    
856  C  CD    . GLU A 131 ? 0.3803 0.4727 0.2916 -0.0689 -0.0484 -0.1010 111 GLU A CD    
857  O  OE1   . GLU A 131 ? 0.3343 0.4777 0.2879 -0.0628 -0.0377 -0.1083 111 GLU A OE1   
858  O  OE2   . GLU A 131 ? 0.4317 0.5152 0.3219 -0.0975 -0.0365 -0.1279 111 GLU A OE2   
859  N  N     . SER A 132 ? 0.2183 0.2100 0.1187 -0.0084 -0.0122 0.0093  112 SER A N     
860  C  CA    . SER A 132 ? 0.2156 0.2285 0.1137 -0.0054 0.0054  0.0065  112 SER A CA    
861  C  C     . SER A 132 ? 0.1814 0.2221 0.1158 -0.0023 0.0001  0.0038  112 SER A C     
862  O  O     . SER A 132 ? 0.1830 0.2066 0.1216 -0.0024 -0.0081 0.0050  112 SER A O     
863  C  CB    . SER A 132 ? 0.2293 0.2529 0.1175 -0.0223 0.0047  0.0064  112 SER A CB    
864  O  OG    . SER A 132 ? 0.2444 0.2721 0.1285 -0.0015 0.0036  0.0011  112 SER A OG    
865  N  N     . PHE A 133 ? 0.1918 0.2019 0.1075 0.0009  -0.0084 0.0001  113 PHE A N     
866  C  CA    . PHE A 133 ? 0.1923 0.1835 0.1235 -0.0086 0.0078  0.0014  113 PHE A CA    
867  C  C     . PHE A 133 ? 0.1886 0.1952 0.1324 -0.0211 0.0000  0.0006  113 PHE A C     
868  O  O     . PHE A 133 ? 0.1909 0.1970 0.1222 -0.0163 -0.0132 0.0069  113 PHE A O     
869  C  CB    . PHE A 133 ? 0.2100 0.1879 0.1330 -0.0125 0.0063  0.0032  113 PHE A CB    
870  C  CG    . PHE A 133 ? 0.2158 0.2004 0.1367 -0.0214 -0.0090 0.0028  113 PHE A CG    
871  C  CD1   . PHE A 133 ? 0.2533 0.1936 0.1590 -0.0320 -0.0111 -0.0079 113 PHE A CD1   
872  C  CD2   . PHE A 133 ? 0.2021 0.2024 0.1380 -0.0237 -0.0134 -0.0048 113 PHE A CD2   
873  C  CE1   . PHE A 133 ? 0.2647 0.1883 0.1595 -0.0289 -0.0099 -0.0111 113 PHE A CE1   
874  C  CE2   . PHE A 133 ? 0.2181 0.2012 0.1568 -0.0149 -0.0059 0.0030  113 PHE A CE2   
875  C  CZ    . PHE A 133 ? 0.2459 0.1853 0.1547 -0.0267 0.0016  0.0091  113 PHE A CZ    
876  N  N     . GLN A 134 ? 0.1930 0.2025 0.1448 -0.0295 -0.0036 -0.0028 114 GLN A N     
877  C  CA    . GLN A 134 ? 0.1974 0.1889 0.1455 -0.0450 -0.0077 -0.0073 114 GLN A CA    
878  C  C     . GLN A 134 ? 0.1936 0.1827 0.1172 -0.0246 -0.0010 0.0038  114 GLN A C     
879  O  O     . GLN A 134 ? 0.2026 0.2017 0.1258 -0.0105 -0.0124 0.0107  114 GLN A O     
880  C  CB    . GLN A 134 ? 0.2265 0.1947 0.1808 -0.0312 -0.0122 -0.0031 114 GLN A CB    
881  C  CG    . GLN A 134 ? 0.3134 0.2299 0.2269 -0.0504 -0.0099 -0.0040 114 GLN A CG    
882  C  CD    . GLN A 134 ? 0.4474 0.2891 0.2980 -0.0291 0.0420  -0.0002 114 GLN A CD    
883  O  OE1   . GLN A 134 ? 0.4959 0.3119 0.3282 -0.0315 0.0467  0.0006  114 GLN A OE1   
884  N  NE2   . GLN A 134 ? 0.5048 0.3272 0.3228 -0.0219 0.0591  0.0029  114 GLN A NE2   
885  N  N     . ALA A 135 ? 0.2091 0.1859 0.1225 0.0005  -0.0007 -0.0039 115 ALA A N     
886  C  CA    . ALA A 135 ? 0.2270 0.1917 0.1164 -0.0160 -0.0066 -0.0032 115 ALA A CA    
887  C  C     . ALA A 135 ? 0.1935 0.1945 0.1229 -0.0150 -0.0001 0.0072  115 ALA A C     
888  O  O     . ALA A 135 ? 0.2290 0.2014 0.1279 0.0018  -0.0026 0.0091  115 ALA A O     
889  C  CB    . ALA A 135 ? 0.2541 0.2219 0.1164 -0.0102 -0.0111 -0.0111 115 ALA A CB    
890  N  N     . GLY A 136 ? 0.1849 0.1951 0.1219 -0.0109 0.0028  -0.0042 116 GLY A N     
891  C  CA    . GLY A 136 ? 0.1826 0.2065 0.1155 -0.0064 -0.0026 -0.0019 116 GLY A CA    
892  C  C     . GLY A 136 ? 0.1697 0.1940 0.1156 -0.0123 -0.0056 0.0025  116 GLY A C     
893  O  O     . GLY A 136 ? 0.1863 0.1904 0.1146 -0.0127 -0.0093 -0.0012 116 GLY A O     
894  N  N     . VAL A 137 ? 0.1610 0.1958 0.1190 -0.0027 0.0042  0.0142  117 VAL A N     
895  C  CA    . VAL A 137 ? 0.1620 0.2116 0.1318 -0.0075 0.0046  -0.0024 117 VAL A CA    
896  C  C     . VAL A 137 ? 0.1609 0.2149 0.1312 -0.0019 0.0006  -0.0011 117 VAL A C     
897  O  O     . VAL A 137 ? 0.1827 0.2364 0.1227 0.0094  0.0050  0.0137  117 VAL A O     
898  C  CB    . VAL A 137 ? 0.1592 0.2303 0.1530 0.0063  0.0051  0.0009  117 VAL A CB    
899  C  CG1   . VAL A 137 ? 0.1569 0.2484 0.1675 0.0030  0.0065  0.0202  117 VAL A CG1   
900  C  CG2   . VAL A 137 ? 0.1856 0.2332 0.1642 0.0255  0.0064  -0.0009 117 VAL A CG2   
901  N  N     . GLU A 138 ? 0.1722 0.2020 0.1413 -0.0041 -0.0049 0.0137  118 GLU A N     
902  C  CA    . GLU A 138 ? 0.1999 0.2159 0.1721 -0.0132 -0.0049 0.0162  118 GLU A CA    
903  C  C     . GLU A 138 ? 0.1854 0.2037 0.1654 0.0051  -0.0003 0.0160  118 GLU A C     
904  O  O     . GLU A 138 ? 0.2074 0.2105 0.1628 -0.0025 -0.0050 0.0184  118 GLU A O     
905  C  CB    . GLU A 138 ? 0.2301 0.2723 0.2166 -0.0403 -0.0099 0.0101  118 GLU A CB    
906  C  CG    . GLU A 138 ? 0.3649 0.3658 0.2756 -0.0649 -0.0278 0.0199  118 GLU A CG    
907  C  CD    . GLU A 138 ? 0.4973 0.4624 0.3304 -0.0872 -0.0307 0.0209  118 GLU A CD    
908  O  OE1   . GLU A 138 ? 0.5574 0.4997 0.3635 -0.0897 -0.0256 0.0360  118 GLU A OE1   
909  O  OE2   . GLU A 138 ? 0.5500 0.4986 0.3590 -0.0998 -0.0233 0.0094  118 GLU A OE2   
910  N  N     . THR A 139 ? 0.1749 0.1929 0.1562 0.0028  -0.0042 0.0127  119 THR A N     
911  C  CA    . THR A 139 ? 0.1738 0.2059 0.1449 -0.0018 0.0023  0.0114  119 THR A CA    
912  C  C     . THR A 139 ? 0.1779 0.2102 0.1412 0.0016  -0.0047 0.0077  119 THR A C     
913  O  O     . THR A 139 ? 0.1869 0.2109 0.1343 0.0160  -0.0062 0.0157  119 THR A O     
914  C  CB    . THR A 139 ? 0.1831 0.2161 0.1338 0.0007  0.0075  0.0015  119 THR A CB    
915  O  OG1   . THR A 139 ? 0.2164 0.2387 0.1442 -0.0026 -0.0001 0.0129  119 THR A OG1   
916  C  CG2   . THR A 139 ? 0.1844 0.2079 0.1445 0.0113  0.0198  -0.0036 119 THR A CG2   
917  N  N     . ALA A 140 ? 0.1800 0.1912 0.1269 0.0144  -0.0085 0.0070  120 ALA A N     
918  C  CA    . ALA A 140 ? 0.1736 0.2132 0.1276 0.0263  -0.0034 -0.0003 120 ALA A CA    
919  C  C     . ALA A 140 ? 0.1730 0.2237 0.1299 0.0232  0.0013  0.0166  120 ALA A C     
920  O  O     . ALA A 140 ? 0.1743 0.2362 0.1289 0.0190  -0.0065 0.0120  120 ALA A O     
921  C  CB    . ALA A 140 ? 0.1964 0.2153 0.1462 0.0085  -0.0121 -0.0033 120 ALA A CB    
922  N  N     . TYR A 141 ? 0.1796 0.2210 0.1323 0.0124  0.0052  0.0140  121 TYR A N     
923  C  CA    . TYR A 141 ? 0.1783 0.2183 0.1476 0.0256  0.0124  0.0116  121 TYR A CA    
924  C  C     . TYR A 141 ? 0.1775 0.2252 0.1546 0.0313  0.0131  0.0144  121 TYR A C     
925  O  O     . TYR A 141 ? 0.2214 0.2556 0.1534 0.0288  0.0151  0.0289  121 TYR A O     
926  C  CB    . TYR A 141 ? 0.1771 0.2164 0.1538 0.0116  0.0038  0.0177  121 TYR A CB    
927  C  CG    . TYR A 141 ? 0.1807 0.2255 0.1579 0.0012  -0.0053 0.0096  121 TYR A CG    
928  C  CD1   . TYR A 141 ? 0.1924 0.2298 0.1534 0.0039  -0.0011 0.0044  121 TYR A CD1   
929  C  CD2   . TYR A 141 ? 0.1934 0.2437 0.1818 0.0079  0.0247  0.0097  121 TYR A CD2   
930  C  CE1   . TYR A 141 ? 0.2187 0.2326 0.1524 0.0076  0.0025  0.0041  121 TYR A CE1   
931  C  CE2   . TYR A 141 ? 0.1914 0.2450 0.1900 0.0058  0.0234  0.0092  121 TYR A CE2   
932  C  CZ    . TYR A 141 ? 0.1725 0.2431 0.1752 -0.0017 0.0068  0.0072  121 TYR A CZ    
933  O  OH    . TYR A 141 ? 0.1791 0.2586 0.1829 -0.0037 0.0129  -0.0010 121 TYR A OH    
934  N  N     . LYS A 142 ? 0.1903 0.2174 0.1643 0.0247  0.0082  0.0153  122 LYS A N     
935  C  CA    . LYS A 142 ? 0.1986 0.2165 0.1875 0.0167  0.0124  0.0142  122 LYS A CA    
936  C  C     . LYS A 142 ? 0.1923 0.2193 0.1720 0.0321  0.0097  0.0226  122 LYS A C     
937  O  O     . LYS A 142 ? 0.2065 0.2518 0.1938 0.0384  0.0055  0.0272  122 LYS A O     
938  C  CB    . LYS A 142 ? 0.2223 0.2301 0.2105 0.0142  -0.0054 0.0109  122 LYS A CB    
939  C  CG    . LYS A 142 ? 0.2664 0.2527 0.2385 0.0080  0.0103  -0.0015 122 LYS A CG    
940  C  CD    . LYS A 142 ? 0.3020 0.2848 0.2644 0.0320  0.0142  -0.0204 122 LYS A CD    
941  N  N     . ALA A 143 ? 0.1838 0.2251 0.1508 0.0263  0.0001  -0.0010 123 ALA A N     
942  C  CA    . ALA A 143 ? 0.1832 0.2477 0.1588 0.0208  -0.0005 0.0063  123 ALA A CA    
943  C  C     . ALA A 143 ? 0.1850 0.2577 0.1547 0.0344  -0.0090 0.0095  123 ALA A C     
944  O  O     . ALA A 143 ? 0.1973 0.2641 0.1651 0.0296  -0.0207 0.0060  123 ALA A O     
945  C  CB    . ALA A 143 ? 0.1913 0.2444 0.1608 0.0010  -0.0019 -0.0019 123 ALA A CB    
946  N  N     . VAL A 144 ? 0.1811 0.2671 0.1551 0.0326  -0.0127 0.0041  124 VAL A N     
947  C  CA    . VAL A 144 ? 0.1910 0.2486 0.1511 0.0219  -0.0033 0.0139  124 VAL A CA    
948  C  C     . VAL A 144 ? 0.2022 0.2520 0.1736 0.0245  -0.0175 0.0206  124 VAL A C     
949  O  O     . VAL A 144 ? 0.2407 0.2500 0.1953 0.0150  -0.0413 0.0284  124 VAL A O     
950  C  CB    . VAL A 144 ? 0.1840 0.2421 0.1507 0.0067  0.0146  0.0155  124 VAL A CB    
951  C  CG1   . VAL A 144 ? 0.1945 0.2521 0.1472 0.0129  0.0371  0.0125  124 VAL A CG1   
952  C  CG2   . VAL A 144 ? 0.1937 0.2327 0.1589 0.0229  0.0144  0.0114  124 VAL A CG2   
953  N  N     . MET A 145 ? 0.2009 0.2682 0.1652 0.0233  -0.0163 0.0283  125 MET A N     
954  C  CA    . MET A 145 ? 0.2012 0.2933 0.1996 0.0465  -0.0111 0.0467  125 MET A CA    
955  C  C     . MET A 145 ? 0.2216 0.2846 0.2551 0.0395  -0.0106 0.0706  125 MET A C     
956  O  O     . MET A 145 ? 0.2514 0.2816 0.3014 0.0303  -0.0296 0.0725  125 MET A O     
957  C  CB    . MET A 145 ? 0.1816 0.3416 0.1832 0.0791  -0.0018 0.0520  125 MET A CB    
958  C  CG    . MET A 145 ? 0.2171 0.3918 0.1813 0.1004  0.0291  0.0490  125 MET A CG    
959  S  SD    . MET A 145 ? 0.2632 0.4374 0.1979 0.1241  0.0278  0.0380  125 MET A SD    
960  C  CE    . MET A 145 ? 0.2777 0.4455 0.2270 0.0751  0.0109  0.0553  125 MET A CE    
961  N  N     . LYS A 146 ? 0.2087 0.2574 0.2434 0.0385  0.0282  0.0958  126 LYS A N     
962  C  CA    . LYS A 146 ? 0.2112 0.2839 0.2741 0.0525  0.0578  0.0985  126 LYS A CA    
963  C  C     . LYS A 146 ? 0.2167 0.2680 0.2728 0.0385  0.0511  0.0722  126 LYS A C     
964  O  O     . LYS A 146 ? 0.2183 0.2838 0.2484 0.0371  0.0565  0.0796  126 LYS A O     
965  C  CB    . LYS A 146 ? 0.2820 0.3248 0.2932 0.1012  0.0868  0.1209  126 LYS A CB    
966  C  CG    . LYS A 146 ? 0.3819 0.3838 0.3158 0.1030  0.0800  0.1277  126 LYS A CG    
967  C  CD    . LYS A 146 ? 0.4547 0.4216 0.3474 0.0946  0.0656  0.1165  126 LYS A CD    
968  C  CE    . LYS A 146 ? 0.5247 0.4525 0.3641 0.0742  0.0595  0.1185  126 LYS A CE    
969  N  NZ    . LYS A 146 ? 0.5771 0.4801 0.3833 0.0490  0.0639  0.1131  126 LYS A NZ    
970  N  N     . PRO A 147 ? 0.2048 0.2309 0.2759 0.0406  0.0209  0.0572  127 PRO A N     
971  C  CA    . PRO A 147 ? 0.1868 0.2212 0.2692 0.0284  0.0395  0.0603  127 PRO A CA    
972  C  C     . PRO A 147 ? 0.1802 0.2171 0.2387 0.0212  0.0344  0.0594  127 PRO A C     
973  O  O     . PRO A 147 ? 0.2381 0.2247 0.2696 0.0071  0.0438  0.0699  127 PRO A O     
974  C  CB    . PRO A 147 ? 0.2274 0.2339 0.2930 0.0319  0.0342  0.0377  127 PRO A CB    
975  C  CG    . PRO A 147 ? 0.2436 0.2439 0.3096 0.0118  0.0131  0.0253  127 PRO A CG    
976  C  CD    . PRO A 147 ? 0.2382 0.2480 0.3054 0.0264  -0.0040 0.0385  127 PRO A CD    
977  N  N     . VAL A 148 ? 0.1647 0.2139 0.1894 0.0181  0.0118  0.0464  128 VAL A N     
978  C  CA    . VAL A 148 ? 0.1895 0.2247 0.1654 0.0036  0.0109  0.0342  128 VAL A CA    
979  C  C     . VAL A 148 ? 0.1736 0.2100 0.1473 0.0072  0.0056  0.0307  128 VAL A C     
980  O  O     . VAL A 148 ? 0.1791 0.2147 0.1590 -0.0059 0.0132  0.0385  128 VAL A O     
981  C  CB    . VAL A 148 ? 0.2269 0.2493 0.1716 0.0163  0.0048  0.0254  128 VAL A CB    
982  C  CG1   . VAL A 148 ? 0.2467 0.2445 0.1853 0.0126  -0.0028 0.0155  128 VAL A CG1   
983  C  CG2   . VAL A 148 ? 0.2472 0.2772 0.1726 0.0294  -0.0126 0.0246  128 VAL A CG2   
984  N  N     . GLU A 149 ? 0.1759 0.1951 0.1452 -0.0052 0.0129  0.0336  129 GLU A N     
985  C  CA    . GLU A 149 ? 0.1664 0.2062 0.1416 0.0005  0.0111  0.0134  129 GLU A CA    
986  C  C     . GLU A 149 ? 0.1681 0.2096 0.1265 -0.0035 0.0065  0.0079  129 GLU A C     
987  O  O     . GLU A 149 ? 0.1979 0.2209 0.1284 -0.0170 0.0059  0.0020  129 GLU A O     
988  C  CB    . GLU A 149 ? 0.2064 0.1999 0.1630 0.0005  0.0060  0.0270  129 GLU A CB    
989  C  CG    . GLU A 149 ? 0.2161 0.2110 0.1894 -0.0148 0.0024  0.0207  129 GLU A CG    
990  C  CD    . GLU A 149 ? 0.2647 0.2370 0.2032 -0.0065 0.0044  0.0085  129 GLU A CD    
991  O  OE1   . GLU A 149 ? 0.2719 0.2527 0.1971 -0.0128 -0.0062 0.0039  129 GLU A OE1   
992  O  OE2   . GLU A 149 ? 0.2724 0.2577 0.2062 0.0011  0.0170  0.0178  129 GLU A OE2   
993  N  N     . GLY A 150 ? 0.1629 0.2118 0.1170 -0.0011 0.0169  0.0116  130 GLY A N     
994  C  CA    . GLY A 150 ? 0.1528 0.2178 0.1194 0.0179  0.0096  -0.0121 130 GLY A CA    
995  C  C     . GLY A 150 ? 0.1665 0.2123 0.1213 0.0170  -0.0040 -0.0176 130 GLY A C     
996  O  O     . GLY A 150 ? 0.1767 0.2103 0.1249 0.0108  0.0110  -0.0180 130 GLY A O     
997  N  N     . THR A 151 ? 0.1675 0.2133 0.1158 0.0046  0.0079  -0.0068 131 THR A N     
998  C  CA    . THR A 151 ? 0.1634 0.2029 0.1254 0.0079  0.0092  -0.0015 131 THR A CA    
999  C  C     . THR A 151 ? 0.1574 0.1948 0.1226 -0.0192 -0.0004 -0.0043 131 THR A C     
1000 O  O     . THR A 151 ? 0.1542 0.2017 0.1243 -0.0132 -0.0008 -0.0075 131 THR A O     
1001 C  CB    . THR A 151 ? 0.1962 0.2024 0.1202 -0.0109 0.0088  -0.0009 131 THR A CB    
1002 O  OG1   . THR A 151 ? 0.1940 0.1892 0.1286 0.0006  0.0017  0.0012  131 THR A OG1   
1003 C  CG2   . THR A 151 ? 0.1854 0.2251 0.1304 0.0015  0.0243  0.0061  131 THR A CG2   
1004 N  N     . ILE A 152 ? 0.1640 0.1961 0.1055 -0.0129 0.0043  -0.0029 132 ILE A N     
1005 C  CA    . ILE A 152 ? 0.1600 0.1953 0.0934 -0.0019 -0.0035 -0.0015 132 ILE A CA    
1006 C  C     . ILE A 152 ? 0.1587 0.1861 0.1096 -0.0075 -0.0104 0.0027  132 ILE A C     
1007 O  O     . ILE A 152 ? 0.1772 0.1936 0.1025 -0.0052 -0.0116 0.0089  132 ILE A O     
1008 C  CB    . ILE A 152 ? 0.1597 0.2077 0.1066 -0.0085 -0.0005 0.0011  132 ILE A CB    
1009 C  CG1   . ILE A 152 ? 0.1827 0.2146 0.1168 -0.0090 0.0005  0.0123  132 ILE A CG1   
1010 C  CG2   . ILE A 152 ? 0.1691 0.2148 0.1234 -0.0179 0.0125  0.0024  132 ILE A CG2   
1011 C  CD1   . ILE A 152 ? 0.1930 0.2204 0.1320 -0.0151 0.0160  0.0010  132 ILE A CD1   
1012 N  N     . LEU A 153 ? 0.1544 0.1899 0.1195 -0.0052 -0.0076 0.0021  133 LEU A N     
1013 C  CA    . LEU A 153 ? 0.1581 0.1909 0.1172 -0.0184 0.0004  -0.0028 133 LEU A CA    
1014 C  C     . LEU A 153 ? 0.1707 0.1899 0.1150 -0.0231 0.0012  -0.0037 133 LEU A C     
1015 O  O     . LEU A 153 ? 0.1844 0.1957 0.1078 -0.0026 -0.0149 -0.0037 133 LEU A O     
1016 C  CB    . LEU A 153 ? 0.1804 0.1956 0.1315 0.0024  0.0103  -0.0044 133 LEU A CB    
1017 C  CG    . LEU A 153 ? 0.1688 0.2007 0.1555 0.0018  0.0050  -0.0052 133 LEU A CG    
1018 C  CD1   . LEU A 153 ? 0.2032 0.2087 0.1829 -0.0003 -0.0116 0.0216  133 LEU A CD1   
1019 C  CD2   . LEU A 153 ? 0.1874 0.2113 0.1707 0.0072  -0.0013 0.0004  133 LEU A CD2   
1020 N  N     . THR A 154 ? 0.1548 0.1884 0.1122 -0.0025 0.0091  -0.0021 134 THR A N     
1021 C  CA    . THR A 154 ? 0.1540 0.2078 0.1235 -0.0079 0.0144  0.0135  134 THR A CA    
1022 C  C     . THR A 154 ? 0.1545 0.2048 0.1050 -0.0122 0.0012  0.0072  134 THR A C     
1023 O  O     . THR A 154 ? 0.1606 0.2237 0.0979 -0.0142 -0.0062 0.0052  134 THR A O     
1024 C  CB    . THR A 154 ? 0.1621 0.2336 0.1283 -0.0108 0.0267  0.0263  134 THR A CB    
1025 O  OG1   . THR A 154 ? 0.2084 0.2323 0.1211 -0.0082 0.0029  0.0285  134 THR A OG1   
1026 C  CG2   . THR A 154 ? 0.1824 0.2806 0.1536 0.0087  0.0189  0.0225  134 THR A CG2   
1027 N  N     . VAL A 155 ? 0.1677 0.1949 0.1140 -0.0091 -0.0034 0.0013  135 VAL A N     
1028 C  CA    . VAL A 155 ? 0.1668 0.1973 0.1232 -0.0009 0.0040  0.0024  135 VAL A CA    
1029 C  C     . VAL A 155 ? 0.1730 0.1971 0.1158 0.0018  -0.0074 0.0022  135 VAL A C     
1030 O  O     . VAL A 155 ? 0.1636 0.2109 0.1200 0.0155  -0.0134 0.0066  135 VAL A O     
1031 C  CB    . VAL A 155 ? 0.1829 0.1831 0.1393 -0.0005 0.0037  0.0019  135 VAL A CB    
1032 C  CG1   . VAL A 155 ? 0.1841 0.1908 0.1612 -0.0039 0.0020  0.0083  135 VAL A CG1   
1033 C  CG2   . VAL A 155 ? 0.1866 0.1826 0.1458 0.0066  -0.0101 -0.0113 135 VAL A CG2   
1034 N  N     . ALA A 156 ? 0.1450 0.1965 0.1088 -0.0016 -0.0108 -0.0029 136 ALA A N     
1035 C  CA    . ALA A 156 ? 0.1502 0.2022 0.1214 -0.0165 0.0058  -0.0107 136 ALA A CA    
1036 C  C     . ALA A 156 ? 0.1607 0.1976 0.1037 -0.0047 -0.0025 -0.0008 136 ALA A C     
1037 O  O     . ALA A 156 ? 0.1708 0.2037 0.1039 -0.0095 -0.0050 -0.0010 136 ALA A O     
1038 C  CB    . ALA A 156 ? 0.1520 0.1917 0.1373 -0.0095 0.0051  -0.0089 136 ALA A CB    
1039 N  N     . LYS A 157 ? 0.1595 0.2048 0.1205 -0.0162 0.0019  -0.0043 137 LYS A N     
1040 C  CA    . LYS A 157 ? 0.1596 0.2027 0.1259 -0.0170 -0.0158 0.0052  137 LYS A CA    
1041 C  C     . LYS A 157 ? 0.1809 0.2038 0.1328 -0.0092 -0.0161 -0.0057 137 LYS A C     
1042 O  O     . LYS A 157 ? 0.1765 0.2149 0.1215 -0.0154 -0.0243 -0.0072 137 LYS A O     
1043 C  CB    . LYS A 157 ? 0.1713 0.2112 0.1501 -0.0197 0.0026  0.0280  137 LYS A CB    
1044 C  CG    . LYS A 157 ? 0.2406 0.2341 0.1963 -0.0209 0.0049  0.0231  137 LYS A CG    
1045 C  CD    . LYS A 157 ? 0.3005 0.2713 0.2414 -0.0322 0.0119  0.0385  137 LYS A CD    
1046 C  CE    . LYS A 157 ? 0.3556 0.3117 0.2718 -0.0199 0.0152  0.0496  137 LYS A CE    
1047 N  NZ    . LYS A 157 ? 0.4160 0.3541 0.2831 -0.0146 0.0105  0.0510  137 LYS A NZ    
1048 N  N     . ASP A 158 ? 0.1605 0.2085 0.1318 0.0060  -0.0107 -0.0067 138 ASP A N     
1049 C  CA    . ASP A 158 ? 0.1660 0.2342 0.1521 0.0089  -0.0280 -0.0147 138 ASP A CA    
1050 C  C     . ASP A 158 ? 0.1718 0.2444 0.1501 0.0122  -0.0248 -0.0103 138 ASP A C     
1051 O  O     . ASP A 158 ? 0.1704 0.2563 0.1423 0.0155  -0.0318 -0.0024 138 ASP A O     
1052 C  CB    . ASP A 158 ? 0.2019 0.2484 0.1764 0.0107  -0.0191 -0.0178 138 ASP A CB    
1053 C  CG    . ASP A 158 ? 0.2413 0.2623 0.1883 -0.0257 -0.0147 -0.0283 138 ASP A CG    
1054 O  OD1   . ASP A 158 ? 0.3249 0.2906 0.2041 -0.0522 0.0195  -0.0160 138 ASP A OD1   
1055 O  OD2   . ASP A 158 ? 0.2025 0.2715 0.1893 -0.0162 -0.0170 -0.0191 138 ASP A OD2   
1056 N  N     . ALA A 159 ? 0.1711 0.2232 0.1317 0.0092  -0.0291 0.0148  139 ALA A N     
1057 C  CA    . ALA A 159 ? 0.1904 0.2148 0.1257 0.0055  -0.0245 0.0083  139 ALA A CA    
1058 C  C     . ALA A 159 ? 0.1724 0.2090 0.1257 0.0037  -0.0124 0.0098  139 ALA A C     
1059 O  O     . ALA A 159 ? 0.1921 0.2147 0.1390 0.0022  -0.0359 0.0086  139 ALA A O     
1060 C  CB    . ALA A 159 ? 0.2198 0.2041 0.1313 -0.0123 -0.0302 -0.0015 139 ALA A CB    
1061 N  N     . ALA A 160 ? 0.1950 0.2056 0.1195 0.0124  -0.0199 0.0020  140 ALA A N     
1062 C  CA    . ALA A 160 ? 0.1771 0.2072 0.1218 0.0071  -0.0064 -0.0034 140 ALA A CA    
1063 C  C     . ALA A 160 ? 0.1769 0.2269 0.1345 -0.0003 -0.0202 0.0120  140 ALA A C     
1064 O  O     . ALA A 160 ? 0.1955 0.2433 0.1233 -0.0039 -0.0289 0.0047  140 ALA A O     
1065 C  CB    . ALA A 160 ? 0.2018 0.1996 0.1339 0.0212  -0.0080 -0.0207 140 ALA A CB    
1066 N  N     . GLN A 161 ? 0.1840 0.2509 0.1456 -0.0148 -0.0316 0.0111  141 GLN A N     
1067 C  CA    . GLN A 161 ? 0.2032 0.2685 0.1580 -0.0296 -0.0225 0.0005  141 GLN A CA    
1068 C  C     . GLN A 161 ? 0.1743 0.2658 0.1566 -0.0205 -0.0224 -0.0030 141 GLN A C     
1069 O  O     . GLN A 161 ? 0.1942 0.2876 0.1568 -0.0220 -0.0309 -0.0062 141 GLN A O     
1070 C  CB    . GLN A 161 ? 0.2206 0.2921 0.2148 -0.0463 -0.0352 0.0131  141 GLN A CB    
1071 C  CG    . GLN A 161 ? 0.2944 0.3225 0.2753 -0.0422 -0.0411 0.0145  141 GLN A CG    
1072 C  CD    . GLN A 161 ? 0.3980 0.3484 0.3304 -0.0373 -0.0501 0.0127  141 GLN A CD    
1073 O  OE1   . GLN A 161 ? 0.4452 0.3581 0.3601 -0.0365 -0.0470 0.0072  141 GLN A OE1   
1074 N  NE2   . GLN A 161 ? 0.4435 0.3713 0.3494 -0.0311 -0.0468 0.0049  141 GLN A NE2   
1075 N  N     . ALA A 162 ? 0.1839 0.2638 0.1517 -0.0276 -0.0311 -0.0044 142 ALA A N     
1076 C  CA    . ALA A 162 ? 0.1999 0.2600 0.1519 -0.0102 -0.0282 0.0082  142 ALA A CA    
1077 C  C     . ALA A 162 ? 0.2082 0.2489 0.1422 -0.0026 -0.0356 0.0035  142 ALA A C     
1078 O  O     . ALA A 162 ? 0.2235 0.2640 0.1410 -0.0062 -0.0426 -0.0014 142 ALA A O     
1079 C  CB    . ALA A 162 ? 0.2123 0.2749 0.1566 0.0009  -0.0159 0.0190  142 ALA A CB    
1080 N  N     . ALA A 163 ? 0.1984 0.2300 0.1378 -0.0115 -0.0280 0.0011  143 ALA A N     
1081 C  CA    . ALA A 163 ? 0.2168 0.2207 0.1389 -0.0234 -0.0204 0.0097  143 ALA A CA    
1082 C  C     . ALA A 163 ? 0.2002 0.2311 0.1337 -0.0367 -0.0254 -0.0074 143 ALA A C     
1083 O  O     . ALA A 163 ? 0.2080 0.2539 0.1325 -0.0315 -0.0319 -0.0046 143 ALA A O     
1084 C  CB    . ALA A 163 ? 0.1996 0.2163 0.1470 -0.0225 -0.0204 0.0103  143 ALA A CB    
1085 N  N     . ILE A 164 ? 0.2012 0.2443 0.1497 -0.0401 -0.0248 -0.0124 144 ILE A N     
1086 C  CA    . ILE A 164 ? 0.2431 0.2639 0.1737 -0.0484 -0.0282 -0.0235 144 ILE A CA    
1087 C  C     . ILE A 164 ? 0.2415 0.2972 0.1817 -0.0520 -0.0340 -0.0042 144 ILE A C     
1088 O  O     . ILE A 164 ? 0.2515 0.3170 0.1781 -0.0437 -0.0405 -0.0198 144 ILE A O     
1089 C  CB    . ILE A 164 ? 0.2772 0.2784 0.2163 -0.0525 -0.0333 -0.0417 144 ILE A CB    
1090 C  CG1   . ILE A 164 ? 0.3144 0.2972 0.2366 -0.0615 -0.0256 -0.0568 144 ILE A CG1   
1091 C  CG2   . ILE A 164 ? 0.2911 0.2797 0.2495 -0.0449 -0.0182 -0.0440 144 ILE A CG2   
1092 C  CD1   . ILE A 164 ? 0.3468 0.3305 0.2573 -0.0421 -0.0242 -0.0466 144 ILE A CD1   
1093 N  N     . GLU A 165 ? 0.2205 0.3196 0.1804 -0.0435 -0.0437 0.0135  145 GLU A N     
1094 C  CA    . GLU A 165 ? 0.2210 0.3488 0.1964 -0.0387 -0.0343 0.0216  145 GLU A CA    
1095 C  C     . GLU A 165 ? 0.2296 0.3573 0.1929 -0.0333 -0.0551 0.0151  145 GLU A C     
1096 O  O     . GLU A 165 ? 0.2483 0.3745 0.1989 -0.0340 -0.0768 0.0037  145 GLU A O     
1097 C  CB    . GLU A 165 ? 0.2587 0.3888 0.2245 -0.0189 -0.0179 0.0384  145 GLU A CB    
1098 C  CG    . GLU A 165 ? 0.3255 0.4344 0.2646 -0.0264 0.0008  0.0339  145 GLU A CG    
1099 C  CD    . GLU A 165 ? 0.4047 0.4676 0.3079 -0.0271 0.0088  0.0332  145 GLU A CD    
1100 O  OE1   . GLU A 165 ? 0.4396 0.4724 0.3356 -0.0347 0.0164  0.0264  145 GLU A OE1   
1101 O  OE2   . GLU A 165 ? 0.4090 0.4861 0.3152 -0.0354 0.0013  0.0376  145 GLU A OE2   
1102 N  N     . LYS A 166 ? 0.2207 0.3484 0.1729 -0.0248 -0.0554 0.0163  146 LYS A N     
1103 C  CA    . LYS A 166 ? 0.2234 0.3448 0.1699 -0.0085 -0.0487 0.0106  146 LYS A CA    
1104 C  C     . LYS A 166 ? 0.2471 0.3395 0.1611 -0.0214 -0.0567 0.0103  146 LYS A C     
1105 O  O     . LYS A 166 ? 0.2624 0.3548 0.1590 -0.0122 -0.0685 0.0243  146 LYS A O     
1106 C  CB    . LYS A 166 ? 0.2264 0.3612 0.1841 -0.0032 -0.0449 0.0099  146 LYS A CB    
1107 C  CG    . LYS A 166 ? 0.2400 0.3912 0.2145 0.0039  -0.0515 0.0250  146 LYS A CG    
1108 C  CD    . LYS A 166 ? 0.3008 0.4263 0.2550 0.0097  -0.0698 0.0303  146 LYS A CD    
1109 C  CE    . LYS A 166 ? 0.3349 0.4628 0.2835 0.0244  -0.0795 0.0362  146 LYS A CE    
1110 N  NZ    . LYS A 166 ? 0.3616 0.4918 0.3110 0.0301  -0.0779 0.0236  146 LYS A NZ    
1111 N  N     . ALA A 167 ? 0.2459 0.3334 0.1555 -0.0229 -0.0342 0.0086  147 ALA A N     
1112 C  CA    . ALA A 167 ? 0.2610 0.3320 0.1662 -0.0384 -0.0421 0.0016  147 ALA A CA    
1113 C  C     . ALA A 167 ? 0.3036 0.3666 0.1770 -0.0721 -0.0463 -0.0064 147 ALA A C     
1114 O  O     . ALA A 167 ? 0.3204 0.3804 0.1682 -0.0604 -0.0453 -0.0072 147 ALA A O     
1115 C  CB    . ALA A 167 ? 0.2559 0.3280 0.1757 -0.0034 -0.0258 -0.0036 147 ALA A CB    
1116 N  N     . ASN A 168 ? 0.3373 0.3946 0.2015 -0.1008 -0.0565 -0.0180 148 ASN A N     
1117 C  CA    . ASN A 168 ? 0.3834 0.4397 0.2342 -0.0959 -0.0474 -0.0160 148 ASN A CA    
1118 C  C     . ASN A 168 ? 0.3856 0.4724 0.2569 -0.0826 -0.0845 -0.0145 148 ASN A C     
1119 O  O     . ASN A 168 ? 0.4321 0.4916 0.2639 -0.0769 -0.1099 -0.0224 148 ASN A O     
1120 C  CB    . ASN A 168 ? 0.4444 0.4565 0.2654 -0.0865 -0.0045 -0.0172 148 ASN A CB    
1121 C  CG    . ASN A 168 ? 0.5154 0.4860 0.3015 -0.0595 0.0435  -0.0183 148 ASN A CG    
1122 O  OD1   . ASN A 168 ? 0.5547 0.5040 0.3228 -0.0461 0.0480  -0.0280 148 ASN A OD1   
1123 N  ND2   . ASN A 168 ? 0.5355 0.4916 0.3138 -0.0563 0.0560  -0.0155 148 ASN A ND2   
1124 N  N     . ASN A 169 ? 0.3462 0.4880 0.2733 -0.0790 -0.0860 0.0013  149 ASN A N     
1125 C  CA    . ASN A 169 ? 0.3507 0.5229 0.3140 -0.0411 -0.0809 0.0188  149 ASN A CA    
1126 C  C     . ASN A 169 ? 0.3112 0.4947 0.2925 -0.0336 -0.0846 0.0390  149 ASN A C     
1127 O  O     . ASN A 169 ? 0.3210 0.5057 0.3123 -0.0256 -0.0888 0.0524  149 ASN A O     
1128 C  CB    . ASN A 169 ? 0.3887 0.5728 0.3549 -0.0136 -0.0757 0.0138  149 ASN A CB    
1129 C  CG    . ASN A 169 ? 0.4155 0.6112 0.3789 0.0014  -0.0869 0.0062  149 ASN A CG    
1130 O  OD1   . ASN A 169 ? 0.4021 0.6214 0.3828 -0.0019 -0.1000 0.0128  149 ASN A OD1   
1131 N  ND2   . ASN A 169 ? 0.4443 0.6321 0.3931 0.0100  -0.0853 -0.0021 149 ASN A ND2   
1132 N  N     . THR A 170 ? 0.2755 0.4589 0.2472 -0.0350 -0.0812 0.0329  150 THR A N     
1133 C  CA    . THR A 170 ? 0.2703 0.4398 0.2376 -0.0238 -0.0586 0.0419  150 THR A CA    
1134 C  C     . THR A 170 ? 0.2676 0.4140 0.2252 -0.0265 -0.0451 0.0633  150 THR A C     
1135 O  O     . THR A 170 ? 0.2862 0.4216 0.2359 -0.0088 -0.0380 0.0781  150 THR A O     
1136 C  CB    . THR A 170 ? 0.3101 0.4462 0.2486 -0.0269 -0.0305 0.0215  150 THR A CB    
1137 O  OG1   . THR A 170 ? 0.3441 0.4580 0.2658 -0.0191 -0.0247 0.0181  150 THR A OG1   
1138 C  CG2   . THR A 170 ? 0.3159 0.4492 0.2452 -0.0421 -0.0262 0.0136  150 THR A CG2   
1139 N  N     . GLU A 171 ? 0.2611 0.3849 0.2079 -0.0279 -0.0584 0.0538  151 GLU A N     
1140 C  CA    . GLU A 171 ? 0.2883 0.3765 0.1855 -0.0133 -0.0550 0.0422  151 GLU A CA    
1141 C  C     . GLU A 171 ? 0.2572 0.3440 0.1755 -0.0184 -0.0504 0.0442  151 GLU A C     
1142 O  O     . GLU A 171 ? 0.2915 0.3317 0.2058 -0.0170 -0.0501 0.0298  151 GLU A O     
1143 C  CB    . GLU A 171 ? 0.3171 0.4066 0.2077 -0.0067 -0.0534 0.0292  151 GLU A CB    
1144 C  CG    . GLU A 171 ? 0.3455 0.4305 0.2281 0.0112  -0.0491 0.0140  151 GLU A CG    
1145 N  N     . ASP A 172 ? 0.2625 0.3373 0.1596 -0.0115 -0.0254 0.0281  152 ASP A N     
1146 C  CA    . ASP A 172 ? 0.2445 0.3148 0.1573 0.0045  -0.0220 0.0370  152 ASP A CA    
1147 C  C     . ASP A 172 ? 0.2419 0.2873 0.1463 -0.0015 -0.0137 0.0390  152 ASP A C     
1148 O  O     . ASP A 172 ? 0.2391 0.3008 0.1495 -0.0047 -0.0146 0.0281  152 ASP A O     
1149 C  CB    . ASP A 172 ? 0.2454 0.3169 0.1700 0.0260  -0.0223 0.0253  152 ASP A CB    
1150 C  CG    . ASP A 172 ? 0.2960 0.3191 0.1964 0.0368  -0.0023 0.0238  152 ASP A CG    
1151 O  OD1   . ASP A 172 ? 0.3315 0.3450 0.2285 0.0359  -0.0060 0.0196  152 ASP A OD1   
1152 O  OD2   . ASP A 172 ? 0.3183 0.3063 0.1698 0.0373  -0.0210 0.0409  152 ASP A OD2   
1153 N  N     . CYS A 173 ? 0.2242 0.2777 0.1383 -0.0152 0.0029  0.0327  153 CYS A N     
1154 C  CA    . CYS A 173 ? 0.2076 0.2669 0.1322 -0.0090 0.0100  0.0460  153 CYS A CA    
1155 C  C     . CYS A 173 ? 0.2129 0.2720 0.1469 -0.0006 -0.0087 0.0419  153 CYS A C     
1156 O  O     . CYS A 173 ? 0.2066 0.2866 0.1438 0.0000  -0.0041 0.0490  153 CYS A O     
1157 C  CB    . CYS A 173 ? 0.2360 0.2554 0.1581 -0.0083 0.0071  0.0302  153 CYS A CB    
1158 S  SG    . CYS A 173 ? 0.2778 0.2658 0.1793 0.0049  0.0006  0.0186  153 CYS A SG    
1159 N  N     . ILE A 174 ? 0.2182 0.2797 0.1499 -0.0055 0.0031  0.0435  154 ILE A N     
1160 C  CA    . ILE A 174 ? 0.2111 0.2797 0.1631 0.0143  0.0008  0.0503  154 ILE A CA    
1161 C  C     . ILE A 174 ? 0.2137 0.2788 0.1629 0.0086  0.0047  0.0496  154 ILE A C     
1162 O  O     . ILE A 174 ? 0.2434 0.2800 0.1531 0.0130  0.0158  0.0466  154 ILE A O     
1163 C  CB    . ILE A 174 ? 0.2442 0.2821 0.1971 0.0020  -0.0034 0.0581  154 ILE A CB    
1164 C  CG1   . ILE A 174 ? 0.2538 0.2786 0.2107 0.0021  0.0123  0.0682  154 ILE A CG1   
1165 C  CG2   . ILE A 174 ? 0.2506 0.2848 0.2194 0.0022  -0.0089 0.0647  154 ILE A CG2   
1166 C  CD1   . ILE A 174 ? 0.2921 0.2930 0.2316 -0.0032 0.0385  0.0717  154 ILE A CD1   
1167 N  N     . GLU A 175 ? 0.1988 0.3048 0.1913 0.0091  0.0031  0.0413  155 GLU A N     
1168 C  CA    . GLU A 175 ? 0.2220 0.3186 0.2001 0.0133  -0.0024 0.0515  155 GLU A CA    
1169 C  C     . GLU A 175 ? 0.2076 0.2922 0.1715 0.0060  0.0012  0.0498  155 GLU A C     
1170 O  O     . GLU A 175 ? 0.2187 0.2898 0.1690 0.0021  0.0130  0.0324  155 GLU A O     
1171 C  CB    . GLU A 175 ? 0.2343 0.3633 0.2237 0.0094  -0.0192 0.0613  155 GLU A CB    
1172 C  CG    . GLU A 175 ? 0.2835 0.4229 0.2549 -0.0134 -0.0323 0.0649  155 GLU A CG    
1173 C  CD    . GLU A 175 ? 0.3395 0.4845 0.2873 -0.0208 -0.0450 0.0737  155 GLU A CD    
1174 O  OE1   . GLU A 175 ? 0.3701 0.5090 0.2908 -0.0114 -0.0658 0.0733  155 GLU A OE1   
1175 O  OE2   . GLU A 175 ? 0.3568 0.5092 0.3148 -0.0088 -0.0567 0.0786  155 GLU A OE2   
1176 N  N     . LEU A 176 ? 0.1962 0.2732 0.1569 0.0040  0.0077  0.0459  156 LEU A N     
1177 C  CA    . LEU A 176 ? 0.2197 0.2566 0.1550 -0.0003 -0.0038 0.0314  156 LEU A CA    
1178 C  C     . LEU A 176 ? 0.2291 0.2463 0.1552 -0.0007 0.0080  0.0306  156 LEU A C     
1179 O  O     . LEU A 176 ? 0.2146 0.2525 0.1494 -0.0045 0.0127  0.0288  156 LEU A O     
1180 C  CB    . LEU A 176 ? 0.2306 0.2607 0.1553 -0.0267 -0.0033 0.0234  156 LEU A CB    
1181 C  CG    . LEU A 176 ? 0.2390 0.2673 0.1785 -0.0203 -0.0194 0.0185  156 LEU A CG    
1182 C  CD1   . LEU A 176 ? 0.2600 0.2783 0.1881 -0.0276 -0.0217 0.0180  156 LEU A CD1   
1183 C  CD2   . LEU A 176 ? 0.2657 0.2556 0.2054 -0.0033 -0.0035 0.0222  156 LEU A CD2   
1184 N  N     . MET A 177 ? 0.2240 0.2362 0.1462 -0.0063 -0.0032 0.0321  157 MET A N     
1185 C  CA    . MET A 177 ? 0.2020 0.2259 0.1480 -0.0038 -0.0008 0.0303  157 MET A CA    
1186 C  C     . MET A 177 ? 0.2139 0.2342 0.1491 -0.0058 0.0091  0.0362  157 MET A C     
1187 O  O     . MET A 177 ? 0.2181 0.2357 0.1353 -0.0061 0.0043  0.0329  157 MET A O     
1188 C  CB    . MET A 177 ? 0.2247 0.2200 0.1480 0.0166  0.0070  0.0198  157 MET A CB    
1189 C  CG    . MET A 177 ? 0.2430 0.2334 0.1600 -0.0121 -0.0045 0.0240  157 MET A CG    
1190 S  SD    . MET A 177 ? 0.2423 0.2389 0.1540 0.0048  -0.0055 0.0160  157 MET A SD    
1191 C  CE    . MET A 177 ? 0.2404 0.2430 0.1490 0.0197  -0.0066 0.0156  157 MET A CE    
1192 N  N     . GLU A 178 ? 0.2126 0.2518 0.1538 0.0206  0.0035  0.0401  158 GLU A N     
1193 C  CA    . GLU A 178 ? 0.1934 0.2625 0.1721 0.0219  0.0020  0.0426  158 GLU A CA    
1194 C  C     . GLU A 178 ? 0.2129 0.2645 0.1668 0.0196  -0.0068 0.0377  158 GLU A C     
1195 O  O     . GLU A 178 ? 0.2240 0.2452 0.1621 0.0169  0.0009  0.0296  158 GLU A O     
1196 C  CB    . GLU A 178 ? 0.2464 0.2894 0.2055 0.0295  0.0193  0.0635  158 GLU A CB    
1197 C  CG    . GLU A 178 ? 0.3023 0.3313 0.2639 0.0319  0.0049  0.0703  158 GLU A CG    
1198 C  CD    . GLU A 178 ? 0.3960 0.3671 0.3235 0.0274  0.0009  0.0694  158 GLU A CD    
1199 O  OE1   . GLU A 178 ? 0.4161 0.3905 0.3404 0.0263  -0.0226 0.0700  158 GLU A OE1   
1200 O  OE2   . GLU A 178 ? 0.4684 0.3709 0.3547 0.0288  0.0135  0.0741  158 GLU A OE2   
1201 N  N     . TYR A 179 ? 0.1938 0.2737 0.1673 0.0167  0.0022  0.0244  159 TYR A N     
1202 C  CA    . TYR A 179 ? 0.2036 0.2703 0.1579 -0.0005 -0.0118 0.0174  159 TYR A CA    
1203 C  C     . TYR A 179 ? 0.2023 0.2546 0.1443 0.0040  -0.0011 0.0250  159 TYR A C     
1204 O  O     . TYR A 179 ? 0.2004 0.2573 0.1493 -0.0016 -0.0013 0.0031  159 TYR A O     
1205 C  CB    . TYR A 179 ? 0.2037 0.2716 0.1669 0.0059  -0.0053 0.0177  159 TYR A CB    
1206 C  CG    . TYR A 179 ? 0.1928 0.2898 0.1975 -0.0028 0.0043  0.0154  159 TYR A CG    
1207 C  CD1   . TYR A 179 ? 0.2294 0.3106 0.2363 0.0056  0.0233  0.0305  159 TYR A CD1   
1208 C  CD2   . TYR A 179 ? 0.2039 0.2968 0.1792 -0.0174 -0.0213 0.0040  159 TYR A CD2   
1209 C  CE1   . TYR A 179 ? 0.2499 0.3295 0.2501 0.0026  0.0293  0.0328  159 TYR A CE1   
1210 C  CE2   . TYR A 179 ? 0.2064 0.3110 0.1934 -0.0093 -0.0323 0.0226  159 TYR A CE2   
1211 C  CZ    . TYR A 179 ? 0.2335 0.3310 0.2378 -0.0139 0.0095  0.0459  159 TYR A CZ    
1212 O  OH    . TYR A 179 ? 0.2496 0.3686 0.2757 -0.0178 0.0270  0.0472  159 TYR A OH    
1213 N  N     . ILE A 180 ? 0.1938 0.2428 0.1443 0.0033  0.0007  0.0287  160 ILE A N     
1214 C  CA    . ILE A 180 ? 0.2197 0.2325 0.1316 0.0029  0.0002  0.0194  160 ILE A CA    
1215 C  C     . ILE A 180 ? 0.2369 0.2238 0.1294 -0.0009 0.0068  0.0132  160 ILE A C     
1216 O  O     . ILE A 180 ? 0.2341 0.2343 0.1277 0.0024  0.0150  0.0224  160 ILE A O     
1217 C  CB    . ILE A 180 ? 0.2252 0.2298 0.1399 -0.0016 -0.0036 0.0208  160 ILE A CB    
1218 C  CG1   . ILE A 180 ? 0.2152 0.2411 0.1495 -0.0051 0.0139  0.0199  160 ILE A CG1   
1219 C  CG2   . ILE A 180 ? 0.2463 0.2382 0.1458 0.0196  -0.0140 0.0252  160 ILE A CG2   
1220 C  CD1   . ILE A 180 ? 0.2306 0.2485 0.1667 0.0006  0.0274  0.0240  160 ILE A CD1   
1221 N  N     . ILE A 181 ? 0.2232 0.2243 0.1362 -0.0001 0.0110  0.0145  161 ILE A N     
1222 C  CA    . ILE A 181 ? 0.2147 0.2195 0.1468 0.0026  0.0100  0.0254  161 ILE A CA    
1223 C  C     . ILE A 181 ? 0.1990 0.2351 0.1459 0.0100  0.0125  0.0243  161 ILE A C     
1224 O  O     . ILE A 181 ? 0.2037 0.2475 0.1365 0.0094  0.0176  0.0127  161 ILE A O     
1225 C  CB    . ILE A 181 ? 0.2246 0.2298 0.1625 -0.0068 0.0190  0.0133  161 ILE A CB    
1226 C  CG1   . ILE A 181 ? 0.2388 0.2399 0.1716 -0.0197 0.0185  0.0158  161 ILE A CG1   
1227 C  CG2   . ILE A 181 ? 0.2484 0.2312 0.1779 -0.0092 0.0023  -0.0020 161 ILE A CG2   
1228 C  CD1   . ILE A 181 ? 0.2584 0.2420 0.1811 -0.0173 0.0188  0.0156  161 ILE A CD1   
1229 N  N     . VAL A 182 ? 0.1804 0.2521 0.1474 0.0167  0.0278  0.0206  162 VAL A N     
1230 C  CA    . VAL A 182 ? 0.2030 0.2613 0.1709 0.0313  0.0007  0.0263  162 VAL A CA    
1231 C  C     . VAL A 182 ? 0.2030 0.2559 0.1555 0.0149  0.0030  0.0006  162 VAL A C     
1232 O  O     . VAL A 182 ? 0.2059 0.2585 0.1453 0.0142  0.0077  -0.0094 162 VAL A O     
1233 C  CB    . VAL A 182 ? 0.2275 0.3059 0.2012 0.0647  -0.0054 0.0428  162 VAL A CB    
1234 C  CG1   . VAL A 182 ? 0.2385 0.3415 0.2332 0.0566  -0.0145 0.0292  162 VAL A CG1   
1235 C  CG2   . VAL A 182 ? 0.2678 0.3232 0.2166 0.0761  -0.0029 0.0611  162 VAL A CG2   
1236 N  N     . LYS A 183 ? 0.1932 0.2470 0.1493 -0.0082 0.0067  0.0008  163 LYS A N     
1237 C  CA    . LYS A 183 ? 0.1906 0.2497 0.1314 -0.0099 0.0017  0.0054  163 LYS A CA    
1238 C  C     . LYS A 183 ? 0.1827 0.2376 0.1320 -0.0206 0.0127  0.0083  163 LYS A C     
1239 O  O     . LYS A 183 ? 0.1994 0.2447 0.1324 -0.0165 0.0147  0.0146  163 LYS A O     
1240 C  CB    . LYS A 183 ? 0.1998 0.2673 0.1562 -0.0094 -0.0240 0.0006  163 LYS A CB    
1241 C  CG    . LYS A 183 ? 0.2484 0.3100 0.2006 -0.0021 -0.0218 -0.0238 163 LYS A CG    
1242 C  CD    . LYS A 183 ? 0.3076 0.3720 0.2494 0.0120  -0.0184 -0.0485 163 LYS A CD    
1243 C  CE    . LYS A 183 ? 0.3797 0.4055 0.3014 0.0080  0.0119  -0.0477 163 LYS A CE    
1244 N  NZ    . LYS A 183 ? 0.3865 0.4147 0.3240 -0.0050 0.0259  -0.0592 163 LYS A NZ    
1245 N  N     . ALA A 184 ? 0.1870 0.2277 0.1346 -0.0167 -0.0009 0.0164  164 ALA A N     
1246 C  CA    . ALA A 184 ? 0.1896 0.2217 0.1361 -0.0013 -0.0024 0.0157  164 ALA A CA    
1247 C  C     . ALA A 184 ? 0.1854 0.2209 0.1386 -0.0031 -0.0067 -0.0056 164 ALA A C     
1248 O  O     . ALA A 184 ? 0.1883 0.2337 0.1283 0.0085  -0.0062 0.0034  164 ALA A O     
1249 C  CB    . ALA A 184 ? 0.1863 0.2478 0.1518 0.0078  -0.0084 0.0016  164 ALA A CB    
1250 N  N     . ASN A 185 ? 0.1904 0.2154 0.1513 0.0080  0.0013  -0.0052 165 ASN A N     
1251 C  CA    . ASN A 185 ? 0.1997 0.2079 0.1665 0.0144  -0.0001 -0.0032 165 ASN A CA    
1252 C  C     . ASN A 185 ? 0.1730 0.2196 0.1544 0.0210  -0.0057 0.0035  165 ASN A C     
1253 O  O     . ASN A 185 ? 0.2071 0.2188 0.1447 0.0228  -0.0021 -0.0139 165 ASN A O     
1254 C  CB    . ASN A 185 ? 0.2694 0.2263 0.2142 0.0122  0.0119  -0.0109 165 ASN A CB    
1255 C  CG    . ASN A 185 ? 0.3757 0.2930 0.2654 -0.0025 -0.0032 0.0003  165 ASN A CG    
1256 O  OD1   . ASN A 185 ? 0.4083 0.3348 0.3231 -0.0232 0.0065  0.0068  165 ASN A OD1   
1257 N  ND2   . ASN A 185 ? 0.4398 0.3345 0.2735 -0.0173 0.0097  -0.0054 165 ASN A ND2   
1258 N  N     . GLU A 186 ? 0.1726 0.2427 0.1490 0.0164  -0.0057 0.0183  166 GLU A N     
1259 C  CA    . GLU A 186 ? 0.1816 0.2652 0.1528 0.0211  -0.0038 -0.0049 166 GLU A CA    
1260 C  C     . GLU A 186 ? 0.1760 0.2383 0.1465 0.0180  0.0114  -0.0058 166 GLU A C     
1261 O  O     . GLU A 186 ? 0.1799 0.2373 0.1390 0.0167  0.0145  -0.0154 166 GLU A O     
1262 C  CB    . GLU A 186 ? 0.1875 0.3165 0.1888 0.0440  -0.0258 0.0105  166 GLU A CB    
1263 C  CG    . GLU A 186 ? 0.2321 0.3766 0.2362 0.0549  -0.0194 0.0257  166 GLU A CG    
1264 C  CD    . GLU A 186 ? 0.2851 0.4351 0.2799 0.0621  -0.0460 0.0214  166 GLU A CD    
1265 O  OE1   . GLU A 186 ? 0.2734 0.4565 0.2962 0.0584  -0.0584 -0.0017 166 GLU A OE1   
1266 O  OE2   . GLU A 186 ? 0.3391 0.4720 0.3030 0.0651  -0.0584 0.0323  166 GLU A OE2   
1267 N  N     . SER A 187 ? 0.1734 0.2182 0.1358 0.0082  0.0064  0.0040  167 SER A N     
1268 C  CA    . SER A 187 ? 0.1814 0.2031 0.1244 0.0015  -0.0019 -0.0010 167 SER A CA    
1269 C  C     . SER A 187 ? 0.1658 0.2068 0.1213 -0.0044 -0.0072 -0.0077 167 SER A C     
1270 O  O     . SER A 187 ? 0.1821 0.2168 0.1249 -0.0123 -0.0027 -0.0005 167 SER A O     
1271 C  CB    . SER A 187 ? 0.2036 0.2023 0.1408 -0.0011 -0.0017 -0.0027 167 SER A CB    
1272 O  OG    . SER A 187 ? 0.2120 0.2131 0.1404 0.0043  -0.0100 -0.0063 167 SER A OG    
1273 N  N     . LEU A 188 ? 0.1722 0.2149 0.1322 -0.0186 -0.0048 0.0011  168 LEU A N     
1274 C  CA    . LEU A 188 ? 0.1634 0.1986 0.1313 -0.0086 -0.0036 -0.0030 168 LEU A CA    
1275 C  C     . LEU A 188 ? 0.1630 0.2102 0.1330 -0.0056 -0.0113 -0.0116 168 LEU A C     
1276 O  O     . LEU A 188 ? 0.1702 0.2138 0.1303 0.0032  -0.0092 -0.0085 168 LEU A O     
1277 C  CB    . LEU A 188 ? 0.1619 0.2092 0.1454 -0.0095 0.0066  -0.0066 168 LEU A CB    
1278 C  CG    . LEU A 188 ? 0.2068 0.2089 0.1631 -0.0146 0.0054  -0.0091 168 LEU A CG    
1279 C  CD1   . LEU A 188 ? 0.1917 0.2248 0.1641 -0.0080 -0.0004 -0.0241 168 LEU A CD1   
1280 C  CD2   . LEU A 188 ? 0.2433 0.2290 0.1816 -0.0280 0.0269  -0.0028 168 LEU A CD2   
1281 N  N     . GLU A 189 ? 0.1533 0.2169 0.1403 0.0095  0.0037  -0.0013 169 GLU A N     
1282 C  CA    . GLU A 189 ? 0.1953 0.2346 0.1604 0.0246  0.0137  -0.0102 169 GLU A CA    
1283 C  C     . GLU A 189 ? 0.1715 0.2335 0.1448 0.0147  0.0069  0.0021  169 GLU A C     
1284 O  O     . GLU A 189 ? 0.1995 0.2559 0.1622 0.0198  0.0144  -0.0059 169 GLU A O     
1285 C  CB    . GLU A 189 ? 0.2525 0.2593 0.1893 0.0377  0.0225  -0.0065 169 GLU A CB    
1286 C  CG    . GLU A 189 ? 0.3761 0.3034 0.2393 0.0196  0.0234  0.0008  169 GLU A CG    
1287 C  CD    . GLU A 189 ? 0.5590 0.3882 0.3100 -0.0122 0.0435  0.0184  169 GLU A CD    
1288 O  OE1   . GLU A 189 ? 0.6279 0.4121 0.3427 -0.0004 0.0407  0.0182  169 GLU A OE1   
1289 O  OE2   . GLU A 189 ? 0.6403 0.4276 0.3491 -0.0275 0.0344  0.0199  169 GLU A OE2   
1290 N  N     . ASN A 190 ? 0.1880 0.2361 0.1386 0.0013  -0.0032 0.0116  170 ASN A N     
1291 C  CA    . ASN A 190 ? 0.1804 0.2336 0.1367 -0.0024 -0.0082 0.0011  170 ASN A CA    
1292 C  C     . ASN A 190 ? 0.1697 0.2167 0.1240 -0.0068 -0.0073 0.0025  170 ASN A C     
1293 O  O     . ASN A 190 ? 0.1705 0.2363 0.1315 -0.0317 -0.0072 0.0177  170 ASN A O     
1294 C  CB    . ASN A 190 ? 0.1895 0.2559 0.1415 -0.0204 -0.0260 0.0034  170 ASN A CB    
1295 C  CG    . ASN A 190 ? 0.1975 0.2805 0.1621 -0.0275 -0.0097 0.0002  170 ASN A CG    
1296 O  OD1   . ASN A 190 ? 0.1973 0.3101 0.1728 -0.0330 0.0012  -0.0055 170 ASN A OD1   
1297 N  ND2   . ASN A 190 ? 0.1996 0.2925 0.1635 -0.0293 0.0018  0.0060  170 ASN A ND2   
1298 N  N     . THR A 191 ? 0.1558 0.2075 0.1300 -0.0063 -0.0066 -0.0045 171 THR A N     
1299 C  CA    . THR A 191 ? 0.1484 0.1931 0.1282 -0.0047 -0.0060 -0.0060 171 THR A CA    
1300 C  C     . THR A 191 ? 0.1710 0.2003 0.1358 -0.0088 -0.0132 -0.0017 171 THR A C     
1301 O  O     . THR A 191 ? 0.1558 0.2170 0.1408 -0.0056 -0.0046 0.0105  171 THR A O     
1302 C  CB    . THR A 191 ? 0.1716 0.1949 0.1349 0.0023  0.0085  -0.0072 171 THR A CB    
1303 O  OG1   . THR A 191 ? 0.1687 0.2005 0.1412 0.0039  -0.0045 -0.0027 171 THR A OG1   
1304 C  CG2   . THR A 191 ? 0.1720 0.2008 0.1326 0.0097  0.0145  -0.0080 171 THR A CG2   
1305 N  N     . PRO A 192 ? 0.1712 0.1986 0.1324 -0.0086 0.0169  0.0044  172 PRO A N     
1306 C  CA    . PRO A 192 ? 0.1679 0.2155 0.1344 -0.0112 0.0134  -0.0072 172 PRO A CA    
1307 C  C     . PRO A 192 ? 0.1761 0.2202 0.1306 -0.0030 0.0004  0.0012  172 PRO A C     
1308 O  O     . PRO A 192 ? 0.1986 0.2454 0.1356 -0.0159 0.0068  0.0026  172 PRO A O     
1309 C  CB    . PRO A 192 ? 0.2112 0.2142 0.1495 -0.0089 0.0075  0.0012  172 PRO A CB    
1310 C  CG    . PRO A 192 ? 0.2309 0.2138 0.1458 -0.0008 0.0109  -0.0117 172 PRO A CG    
1311 C  CD    . PRO A 192 ? 0.1795 0.2027 0.1480 0.0029  0.0087  -0.0139 172 PRO A CD    
1312 N  N     . ASN A 193 ? 0.1561 0.2192 0.1365 0.0059  0.0128  -0.0044 173 ASN A N     
1313 C  CA    . ASN A 193 ? 0.1490 0.2238 0.1500 -0.0179 0.0034  -0.0127 173 ASN A CA    
1314 C  C     . ASN A 193 ? 0.1476 0.2269 0.1472 -0.0043 -0.0032 -0.0028 173 ASN A C     
1315 O  O     . ASN A 193 ? 0.1588 0.2380 0.1812 -0.0089 0.0180  0.0060  173 ASN A O     
1316 C  CB    . ASN A 193 ? 0.1658 0.2382 0.1621 -0.0124 0.0099  -0.0233 173 ASN A CB    
1317 C  CG    . ASN A 193 ? 0.1811 0.2451 0.1740 0.0003  0.0059  -0.0274 173 ASN A CG    
1318 O  OD1   . ASN A 193 ? 0.2283 0.2587 0.1914 0.0264  -0.0016 -0.0413 173 ASN A OD1   
1319 N  ND2   . ASN A 193 ? 0.2423 0.2488 0.1898 0.0148  -0.0170 -0.0043 173 ASN A ND2   
1320 N  N     . LEU A 194 ? 0.1387 0.2087 0.1478 -0.0086 -0.0015 0.0005  174 LEU A N     
1321 C  CA    . LEU A 194 ? 0.1492 0.2113 0.1409 -0.0045 -0.0014 0.0060  174 LEU A CA    
1322 C  C     . LEU A 194 ? 0.1610 0.2130 0.1436 -0.0238 0.0043  0.0153  174 LEU A C     
1323 O  O     . LEU A 194 ? 0.1718 0.2148 0.1418 -0.0053 -0.0018 0.0117  174 LEU A O     
1324 C  CB    . LEU A 194 ? 0.1734 0.2295 0.1407 -0.0167 0.0042  -0.0046 174 LEU A CB    
1325 C  CG    . LEU A 194 ? 0.1819 0.2500 0.1395 -0.0202 0.0052  0.0059  174 LEU A CG    
1326 C  CD1   . LEU A 194 ? 0.2022 0.2674 0.1440 -0.0105 0.0114  0.0153  174 LEU A CD1   
1327 C  CD2   . LEU A 194 ? 0.2131 0.2651 0.1460 -0.0337 -0.0091 0.0064  174 LEU A CD2   
1328 N  N     . LEU A 195 ? 0.1947 0.2155 0.1424 -0.0169 -0.0299 0.0072  175 LEU A N     
1329 C  CA    . LEU A 195 ? 0.1793 0.2272 0.1581 -0.0146 -0.0280 -0.0004 175 LEU A CA    
1330 C  C     . LEU A 195 ? 0.1958 0.2208 0.1426 -0.0279 -0.0152 -0.0047 175 LEU A C     
1331 O  O     . LEU A 195 ? 0.2215 0.2184 0.1359 -0.0186 -0.0160 -0.0094 175 LEU A O     
1332 C  CB    . LEU A 195 ? 0.1877 0.2258 0.1560 -0.0108 -0.0146 -0.0086 175 LEU A CB    
1333 C  CG    . LEU A 195 ? 0.1866 0.2465 0.1714 0.0017  -0.0012 0.0022  175 LEU A CG    
1334 C  CD1   . LEU A 195 ? 0.2038 0.2591 0.1786 0.0064  0.0004  0.0160  175 LEU A CD1   
1335 C  CD2   . LEU A 195 ? 0.1614 0.2534 0.1776 0.0068  -0.0029 -0.0012 175 LEU A CD2   
1336 N  N     . ALA A 196 ? 0.1982 0.2292 0.1530 -0.0364 0.0026  -0.0071 176 ALA A N     
1337 C  CA    . ALA A 196 ? 0.2005 0.2528 0.1583 -0.0295 0.0153  -0.0100 176 ALA A CA    
1338 C  C     . ALA A 196 ? 0.1971 0.2510 0.1542 0.0010  0.0155  -0.0211 176 ALA A C     
1339 O  O     . ALA A 196 ? 0.2002 0.2638 0.1641 -0.0084 0.0133  -0.0238 176 ALA A O     
1340 C  CB    . ALA A 196 ? 0.2343 0.2740 0.1737 -0.0610 0.0112  -0.0046 176 ALA A CB    
1341 N  N     . VAL A 197 ? 0.1884 0.2391 0.1390 -0.0112 0.0121  -0.0226 177 VAL A N     
1342 C  CA    . VAL A 197 ? 0.1971 0.2416 0.1322 -0.0072 0.0039  -0.0197 177 VAL A CA    
1343 C  C     . VAL A 197 ? 0.2095 0.2354 0.1326 -0.0124 0.0046  -0.0132 177 VAL A C     
1344 O  O     . VAL A 197 ? 0.2146 0.2439 0.1383 0.0017  0.0123  -0.0137 177 VAL A O     
1345 C  CB    . VAL A 197 ? 0.2012 0.2562 0.1497 -0.0106 -0.0192 -0.0260 177 VAL A CB    
1346 C  CG1   . VAL A 197 ? 0.1907 0.2750 0.1580 -0.0038 -0.0061 -0.0085 177 VAL A CG1   
1347 C  CG2   . VAL A 197 ? 0.2419 0.2568 0.1666 -0.0046 -0.0183 -0.0174 177 VAL A CG2   
1348 N  N     . LEU A 198 ? 0.1841 0.2345 0.1191 -0.0079 0.0074  -0.0170 178 LEU A N     
1349 C  CA    . LEU A 198 ? 0.1936 0.2407 0.1257 0.0015  -0.0111 -0.0087 178 LEU A CA    
1350 C  C     . LEU A 198 ? 0.1900 0.2396 0.1327 -0.0002 -0.0074 -0.0253 178 LEU A C     
1351 O  O     . LEU A 198 ? 0.2242 0.2317 0.1448 0.0067  0.0013  -0.0282 178 LEU A O     
1352 C  CB    . LEU A 198 ? 0.2052 0.2347 0.1212 0.0007  -0.0021 0.0009  178 LEU A CB    
1353 C  CG    . LEU A 198 ? 0.1990 0.2305 0.1352 -0.0102 0.0079  -0.0100 178 LEU A CG    
1354 C  CD1   . LEU A 198 ? 0.2197 0.2280 0.1322 -0.0071 -0.0008 -0.0159 178 LEU A CD1   
1355 C  CD2   . LEU A 198 ? 0.2057 0.2295 0.1511 -0.0146 0.0023  -0.0168 178 LEU A CD2   
1356 N  N     . LYS A 199 ? 0.1915 0.2791 0.1517 0.0060  -0.0136 -0.0370 179 LYS A N     
1357 C  CA    . LYS A 199 ? 0.2006 0.2890 0.1652 0.0093  0.0048  -0.0405 179 LYS A CA    
1358 C  C     . LYS A 199 ? 0.2025 0.2889 0.1691 -0.0006 0.0042  -0.0523 179 LYS A C     
1359 O  O     . LYS A 199 ? 0.2190 0.3047 0.1742 0.0050  0.0184  -0.0511 179 LYS A O     
1360 C  CB    . LYS A 199 ? 0.2035 0.3143 0.1926 -0.0031 0.0126  -0.0653 179 LYS A CB    
1361 C  CG    . LYS A 199 ? 0.2356 0.3408 0.2402 -0.0003 0.0020  -0.0671 179 LYS A CG    
1362 C  CD    . LYS A 199 ? 0.2925 0.3649 0.2710 0.0039  0.0016  -0.0432 179 LYS A CD    
1363 N  N     . GLU A 200 ? 0.1951 0.2890 0.1465 -0.0114 0.0130  -0.0518 180 GLU A N     
1364 C  CA    . GLU A 200 ? 0.2285 0.3101 0.1596 0.0036  0.0105  -0.0491 180 GLU A CA    
1365 C  C     . GLU A 200 ? 0.2241 0.2994 0.1631 0.0206  0.0037  -0.0693 180 GLU A C     
1366 O  O     . GLU A 200 ? 0.2309 0.3184 0.1743 0.0044  0.0069  -0.0826 180 GLU A O     
1367 C  CB    . GLU A 200 ? 0.3048 0.3492 0.1796 -0.0075 0.0043  -0.0233 180 GLU A CB    
1368 C  CG    . GLU A 200 ? 0.3572 0.4058 0.2107 -0.0068 0.0195  0.0073  180 GLU A CG    
1369 C  CD    . GLU A 200 ? 0.4417 0.4654 0.2601 -0.0096 0.0225  0.0276  180 GLU A CD    
1370 O  OE1   . GLU A 200 ? 0.4800 0.4853 0.2861 0.0015  0.0324  0.0269  180 GLU A OE1   
1371 O  OE2   . GLU A 200 ? 0.4656 0.4826 0.2698 -0.0110 0.0116  0.0432  180 GLU A OE2   
1372 N  N     . VAL A 201 ? 0.2261 0.2780 0.1409 0.0031  -0.0013 -0.0659 181 VAL A N     
1373 C  CA    . VAL A 201 ? 0.2286 0.2674 0.1556 -0.0027 -0.0065 -0.0531 181 VAL A CA    
1374 C  C     . VAL A 201 ? 0.2369 0.2588 0.1698 -0.0021 -0.0086 -0.0347 181 VAL A C     
1375 O  O     . VAL A 201 ? 0.2912 0.2724 0.2100 0.0026  -0.0409 -0.0219 181 VAL A O     
1376 C  CB    . VAL A 201 ? 0.2185 0.2564 0.1668 -0.0129 -0.0186 -0.0472 181 VAL A CB    
1377 C  CG1   . VAL A 201 ? 0.2500 0.2684 0.1934 -0.0017 -0.0296 -0.0419 181 VAL A CG1   
1378 C  CG2   . VAL A 201 ? 0.2284 0.2390 0.1685 -0.0087 -0.0208 -0.0488 181 VAL A CG2   
1379 N  N     . GLY A 202 ? 0.2424 0.2441 0.1458 0.0117  0.0097  -0.0216 182 GLY A N     
1380 C  CA    . GLY A 202 ? 0.2517 0.2483 0.1541 0.0279  -0.0004 -0.0298 182 GLY A CA    
1381 C  C     . GLY A 202 ? 0.2659 0.2419 0.1547 0.0124  0.0076  -0.0300 182 GLY A C     
1382 O  O     . GLY A 202 ? 0.3330 0.2659 0.1952 0.0216  0.0360  -0.0275 182 GLY A O     
1383 N  N     . VAL A 203 ? 0.2335 0.2291 0.1440 -0.0027 0.0136  -0.0326 183 VAL A N     
1384 C  CA    . VAL A 203 ? 0.2362 0.2193 0.1381 -0.0297 0.0061  -0.0326 183 VAL A CA    
1385 C  C     . VAL A 203 ? 0.2357 0.2109 0.1401 -0.0216 0.0094  -0.0324 183 VAL A C     
1386 O  O     . VAL A 203 ? 0.2679 0.2330 0.1485 -0.0429 0.0241  -0.0357 183 VAL A O     
1387 C  CB    . VAL A 203 ? 0.2290 0.2499 0.1517 -0.0349 -0.0032 -0.0287 183 VAL A CB    
1388 C  CG1   . VAL A 203 ? 0.2404 0.2748 0.1600 -0.0511 -0.0134 -0.0399 183 VAL A CG1   
1389 C  CG2   . VAL A 203 ? 0.2147 0.2573 0.1683 -0.0160 0.0040  -0.0147 183 VAL A CG2   
1390 N  N     . VAL A 204 ? 0.2343 0.1895 0.1383 -0.0120 0.0100  -0.0192 184 VAL A N     
1391 C  CA    . VAL A 204 ? 0.1903 0.1937 0.1282 -0.0102 -0.0009 -0.0165 184 VAL A CA    
1392 C  C     . VAL A 204 ? 0.1726 0.2063 0.1212 -0.0104 -0.0102 -0.0100 184 VAL A C     
1393 O  O     . VAL A 204 ? 0.1973 0.2117 0.1348 -0.0089 -0.0133 -0.0123 184 VAL A O     
1394 C  CB    . VAL A 204 ? 0.2125 0.2104 0.1455 0.0017  -0.0128 -0.0141 184 VAL A CB    
1395 C  CG1   . VAL A 204 ? 0.2239 0.2309 0.1698 0.0282  -0.0279 -0.0151 184 VAL A CG1   
1396 C  CG2   . VAL A 204 ? 0.2434 0.2322 0.1604 -0.0023 -0.0100 -0.0012 184 VAL A CG2   
1397 N  N     . ASP A 205 ? 0.1734 0.2097 0.1167 -0.0016 -0.0035 -0.0223 185 ASP A N     
1398 C  CA    . ASP A 205 ? 0.1747 0.2075 0.1182 -0.0108 0.0027  -0.0135 185 ASP A CA    
1399 C  C     . ASP A 205 ? 0.1584 0.2133 0.1252 -0.0098 -0.0003 -0.0041 185 ASP A C     
1400 O  O     . ASP A 205 ? 0.1570 0.2260 0.1202 -0.0136 -0.0050 -0.0064 185 ASP A O     
1401 C  CB    . ASP A 205 ? 0.1793 0.2009 0.1319 -0.0173 0.0207  0.0026  185 ASP A CB    
1402 C  CG    . ASP A 205 ? 0.1893 0.2110 0.1239 -0.0043 0.0201  -0.0034 185 ASP A CG    
1403 O  OD1   . ASP A 205 ? 0.2339 0.2191 0.1340 -0.0059 0.0077  0.0011  185 ASP A OD1   
1404 O  OD2   . ASP A 205 ? 0.2068 0.2080 0.1278 0.0027  0.0047  -0.0080 185 ASP A OD2   
1405 N  N     . SER A 206 ? 0.1618 0.2079 0.1147 -0.0139 -0.0164 0.0107  186 SER A N     
1406 C  CA    . SER A 206 ? 0.1676 0.1963 0.1267 -0.0318 -0.0138 -0.0068 186 SER A CA    
1407 C  C     . SER A 206 ? 0.1671 0.1997 0.1346 -0.0119 -0.0076 -0.0066 186 SER A C     
1408 O  O     . SER A 206 ? 0.1901 0.1998 0.1321 -0.0148 -0.0025 -0.0036 186 SER A O     
1409 C  CB    . SER A 206 ? 0.1771 0.2178 0.1418 -0.0291 -0.0106 -0.0025 186 SER A CB    
1410 O  OG    . SER A 206 ? 0.2101 0.2382 0.1379 -0.0174 -0.0121 -0.0186 186 SER A OG    
1411 N  N     . GLY A 207 ? 0.1722 0.1963 0.1267 -0.0105 0.0001  -0.0113 187 GLY A N     
1412 C  CA    . GLY A 207 ? 0.1727 0.1980 0.1155 -0.0157 0.0002  -0.0126 187 GLY A CA    
1413 C  C     . GLY A 207 ? 0.1870 0.1898 0.1143 -0.0136 0.0080  0.0000  187 GLY A C     
1414 O  O     . GLY A 207 ? 0.1861 0.1924 0.1222 -0.0139 -0.0048 -0.0013 187 GLY A O     
1415 N  N     . GLY A 208 ? 0.1703 0.1905 0.1144 0.0009  0.0011  -0.0073 188 GLY A N     
1416 C  CA    . GLY A 208 ? 0.1700 0.1792 0.1279 -0.0103 0.0012  -0.0075 188 GLY A CA    
1417 C  C     . GLY A 208 ? 0.1576 0.2009 0.1281 -0.0012 0.0101  -0.0072 188 GLY A C     
1418 O  O     . GLY A 208 ? 0.1791 0.2065 0.1130 -0.0181 0.0046  -0.0021 188 GLY A O     
1419 N  N     . LYS A 209 ? 0.1699 0.1880 0.1323 -0.0034 -0.0053 -0.0110 189 LYS A N     
1420 C  CA    . LYS A 209 ? 0.1869 0.1876 0.1459 -0.0060 0.0114  -0.0065 189 LYS A CA    
1421 C  C     . LYS A 209 ? 0.1908 0.1748 0.1388 -0.0183 0.0102  0.0054  189 LYS A C     
1422 O  O     . LYS A 209 ? 0.2177 0.1910 0.1244 -0.0072 0.0020  0.0085  189 LYS A O     
1423 C  CB    . LYS A 209 ? 0.1983 0.1985 0.1556 0.0054  0.0181  -0.0011 189 LYS A CB    
1424 C  CG    . LYS A 209 ? 0.2501 0.2004 0.1993 0.0127  0.0094  0.0056  189 LYS A CG    
1425 C  CD    . LYS A 209 ? 0.3198 0.1871 0.2443 0.0188  -0.0069 0.0242  189 LYS A CD    
1426 C  CE    . LYS A 209 ? 0.3646 0.2143 0.2817 0.0340  -0.0116 0.0389  189 LYS A CE    
1427 N  NZ    . LYS A 209 ? 0.3761 0.2357 0.3064 0.0418  -0.0214 0.0323  189 LYS A NZ    
1428 N  N     . GLY A 210 ? 0.1873 0.1815 0.1285 -0.0142 0.0096  -0.0002 190 GLY A N     
1429 C  CA    . GLY A 210 ? 0.1911 0.1817 0.1409 -0.0147 0.0134  -0.0040 190 GLY A CA    
1430 C  C     . GLY A 210 ? 0.1791 0.1760 0.1352 -0.0294 0.0064  0.0072  190 GLY A C     
1431 O  O     . GLY A 210 ? 0.1968 0.1755 0.1259 -0.0325 0.0087  0.0030  190 GLY A O     
1432 N  N     . LEU A 211 ? 0.1869 0.1810 0.1269 -0.0305 0.0042  0.0029  191 LEU A N     
1433 C  CA    . LEU A 211 ? 0.1862 0.1708 0.1175 -0.0237 -0.0071 -0.0023 191 LEU A CA    
1434 C  C     . LEU A 211 ? 0.2087 0.1829 0.1228 -0.0184 -0.0018 0.0008  191 LEU A C     
1435 O  O     . LEU A 211 ? 0.2194 0.1798 0.1138 -0.0173 -0.0020 0.0051  191 LEU A O     
1436 C  CB    . LEU A 211 ? 0.1892 0.1732 0.1310 -0.0241 -0.0122 0.0013  191 LEU A CB    
1437 C  CG    . LEU A 211 ? 0.2094 0.1839 0.1373 -0.0181 -0.0185 -0.0061 191 LEU A CG    
1438 C  CD1   . LEU A 211 ? 0.2287 0.2003 0.1583 -0.0123 -0.0242 -0.0092 191 LEU A CD1   
1439 C  CD2   . LEU A 211 ? 0.2450 0.2092 0.1327 -0.0445 -0.0214 -0.0119 191 LEU A CD2   
1440 N  N     . LEU A 212 ? 0.1983 0.1967 0.1281 -0.0072 0.0014  -0.0018 192 LEU A N     
1441 C  CA    . LEU A 212 ? 0.1961 0.2073 0.1351 -0.0002 -0.0054 -0.0003 192 LEU A CA    
1442 C  C     . LEU A 212 ? 0.2042 0.1938 0.1339 0.0061  0.0039  0.0026  192 LEU A C     
1443 O  O     . LEU A 212 ? 0.2053 0.2271 0.1313 0.0054  0.0105  0.0192  192 LEU A O     
1444 C  CB    . LEU A 212 ? 0.2108 0.2345 0.1503 0.0019  -0.0006 0.0096  192 LEU A CB    
1445 C  CG    . LEU A 212 ? 0.2346 0.2472 0.1745 0.0125  -0.0059 -0.0041 192 LEU A CG    
1446 C  CD1   . LEU A 212 ? 0.2451 0.2566 0.1887 0.0036  -0.0158 -0.0022 192 LEU A CD1   
1447 C  CD2   . LEU A 212 ? 0.2451 0.2433 0.1808 0.0090  -0.0220 -0.0150 192 LEU A CD2   
1448 N  N     . CYS A 213 ? 0.2137 0.1870 0.1396 -0.0084 0.0074  0.0057  193 CYS A N     
1449 C  CA    . CYS A 213 ? 0.2314 0.1972 0.1472 -0.0195 0.0010  0.0107  193 CYS A CA    
1450 C  C     . CYS A 213 ? 0.2032 0.2012 0.1389 -0.0212 0.0066  0.0194  193 CYS A C     
1451 O  O     . CYS A 213 ? 0.2122 0.1991 0.1445 -0.0094 0.0042  0.0237  193 CYS A O     
1452 C  CB    . CYS A 213 ? 0.2640 0.2086 0.1556 -0.0294 0.0110  -0.0051 193 CYS A CB    
1453 S  SG    . CYS A 213 ? 0.3484 0.2292 0.1761 -0.0416 0.0184  -0.0202 193 CYS A SG    
1454 N  N     . VAL A 214 ? 0.1972 0.2026 0.1281 -0.0104 0.0150  0.0138  194 VAL A N     
1455 C  CA    . VAL A 214 ? 0.1819 0.1987 0.1336 -0.0203 0.0195  0.0075  194 VAL A CA    
1456 C  C     . VAL A 214 ? 0.1827 0.1942 0.1281 -0.0098 0.0108  0.0117  194 VAL A C     
1457 O  O     . VAL A 214 ? 0.1886 0.2059 0.1342 -0.0001 0.0154  0.0240  194 VAL A O     
1458 C  CB    . VAL A 214 ? 0.1889 0.1956 0.1372 -0.0093 0.0055  0.0032  194 VAL A CB    
1459 C  CG1   . VAL A 214 ? 0.2014 0.2081 0.1443 0.0000  0.0153  0.0058  194 VAL A CG1   
1460 C  CG2   . VAL A 214 ? 0.1964 0.2173 0.1519 -0.0022 0.0036  -0.0095 194 VAL A CG2   
1461 N  N     . TYR A 215 ? 0.1866 0.1998 0.1141 -0.0101 0.0087  0.0151  195 TYR A N     
1462 C  CA    . TYR A 215 ? 0.2043 0.1977 0.1277 -0.0193 0.0055  0.0116  195 TYR A CA    
1463 C  C     . TYR A 215 ? 0.1931 0.2015 0.1272 0.0004  0.0061  0.0164  195 TYR A C     
1464 O  O     . TYR A 215 ? 0.2180 0.2135 0.1131 0.0055  0.0063  0.0307  195 TYR A O     
1465 C  CB    . TYR A 215 ? 0.2033 0.1924 0.1280 -0.0252 0.0089  0.0014  195 TYR A CB    
1466 C  CG    . TYR A 215 ? 0.2102 0.1989 0.1390 -0.0406 -0.0133 0.0146  195 TYR A CG    
1467 C  CD1   . TYR A 215 ? 0.2641 0.1976 0.1403 -0.0266 -0.0034 0.0166  195 TYR A CD1   
1468 C  CD2   . TYR A 215 ? 0.2137 0.2303 0.1814 -0.0471 -0.0229 0.0311  195 TYR A CD2   
1469 C  CE1   . TYR A 215 ? 0.2937 0.2129 0.1500 -0.0325 -0.0227 0.0220  195 TYR A CE1   
1470 C  CE2   . TYR A 215 ? 0.2483 0.2320 0.1778 -0.0524 -0.0297 0.0377  195 TYR A CE2   
1471 C  CZ    . TYR A 215 ? 0.3116 0.2198 0.1674 -0.0542 -0.0476 0.0266  195 TYR A CZ    
1472 O  OH    . TYR A 215 ? 0.3845 0.2248 0.1677 -0.0965 -0.0625 0.0263  195 TYR A OH    
1473 N  N     A GLU A 216 ? 0.2225 0.2033 0.1381 0.0090  0.0098  0.0191  196 GLU A N     
1474 N  N     B GLU A 216 ? 0.2045 0.1938 0.1282 0.0039  0.0181  0.0148  196 GLU A N     
1475 C  CA    A GLU A 216 ? 0.2562 0.2153 0.1581 0.0194  0.0053  0.0154  196 GLU A CA    
1476 C  CA    B GLU A 216 ? 0.2166 0.1958 0.1368 0.0149  0.0269  0.0106  196 GLU A CA    
1477 C  C     A GLU A 216 ? 0.2509 0.2055 0.1526 0.0104  0.0009  0.0280  196 GLU A C     
1478 C  C     B GLU A 216 ? 0.2242 0.1850 0.1429 0.0114  0.0240  0.0168  196 GLU A C     
1479 O  O     A GLU A 216 ? 0.2709 0.2141 0.1484 0.0078  -0.0153 0.0333  196 GLU A O     
1480 O  O     B GLU A 216 ? 0.2277 0.1686 0.1403 0.0235  0.0254  0.0031  196 GLU A O     
1481 C  CB    A GLU A 216 ? 0.3187 0.2389 0.1965 0.0249  0.0099  0.0092  196 GLU A CB    
1482 C  CB    B GLU A 216 ? 0.2492 0.2092 0.1565 0.0156  0.0365  0.0121  196 GLU A CB    
1483 C  CG    A GLU A 216 ? 0.3800 0.2757 0.2283 0.0263  0.0190  -0.0086 196 GLU A CG    
1484 C  CG    B GLU A 216 ? 0.2935 0.2387 0.1708 0.0144  0.0537  0.0009  196 GLU A CG    
1485 C  CD    A GLU A 216 ? 0.4514 0.3109 0.2655 0.0156  0.0198  -0.0229 196 GLU A CD    
1486 C  CD    B GLU A 216 ? 0.3419 0.2752 0.1959 0.0029  0.0640  -0.0088 196 GLU A CD    
1487 O  OE1   A GLU A 216 ? 0.4907 0.3155 0.2778 0.0071  0.0100  -0.0405 196 GLU A OE1   
1488 O  OE1   B GLU A 216 ? 0.3702 0.2861 0.2200 -0.0063 0.0699  -0.0075 196 GLU A OE1   
1489 O  OE2   A GLU A 216 ? 0.4801 0.3353 0.2808 0.0166  0.0262  -0.0125 196 GLU A OE2   
1490 O  OE2   B GLU A 216 ? 0.3522 0.2956 0.1894 0.0086  0.0647  -0.0089 196 GLU A OE2   
1491 N  N     . GLY A 217 ? 0.2261 0.1891 0.1453 0.0199  0.0131  0.0189  197 GLY A N     
1492 C  CA    . GLY A 217 ? 0.2270 0.1919 0.1528 0.0019  0.0160  0.0069  197 GLY A CA    
1493 C  C     . GLY A 217 ? 0.2154 0.1997 0.1399 0.0020  0.0027  0.0194  197 GLY A C     
1494 O  O     . GLY A 217 ? 0.2251 0.2064 0.1417 -0.0058 -0.0032 0.0223  197 GLY A O     
1495 N  N     . PHE A 218 ? 0.2283 0.2081 0.1371 -0.0007 0.0109  0.0090  198 PHE A N     
1496 C  CA    . PHE A 218 ? 0.2231 0.1878 0.1309 0.0047  0.0062  0.0282  198 PHE A CA    
1497 C  C     . PHE A 218 ? 0.2145 0.1935 0.1394 -0.0051 0.0127  0.0321  198 PHE A C     
1498 O  O     . PHE A 218 ? 0.2475 0.1885 0.1248 0.0114  0.0228  0.0264  198 PHE A O     
1499 C  CB    . PHE A 218 ? 0.2194 0.1819 0.1337 -0.0053 0.0130  0.0294  198 PHE A CB    
1500 C  CG    . PHE A 218 ? 0.2275 0.1827 0.1354 -0.0092 0.0117  0.0232  198 PHE A CG    
1501 C  CD1   . PHE A 218 ? 0.2176 0.1879 0.1297 0.0103  0.0202  0.0296  198 PHE A CD1   
1502 C  CD2   . PHE A 218 ? 0.2641 0.2048 0.1749 -0.0029 -0.0248 0.0469  198 PHE A CD2   
1503 C  CE1   . PHE A 218 ? 0.2306 0.1997 0.1639 0.0134  0.0220  0.0192  198 PHE A CE1   
1504 C  CE2   . PHE A 218 ? 0.2870 0.2034 0.2009 0.0024  -0.0335 0.0475  198 PHE A CE2   
1505 C  CZ    . PHE A 218 ? 0.2684 0.2144 0.1933 0.0221  -0.0103 0.0321  198 PHE A CZ    
1506 N  N     . LEU A 219 ? 0.2099 0.2035 0.1474 0.0057  0.0129  0.0241  199 LEU A N     
1507 C  CA    . LEU A 219 ? 0.2136 0.2150 0.1594 0.0175  0.0111  0.0179  199 LEU A CA    
1508 C  C     . LEU A 219 ? 0.2320 0.2053 0.1625 0.0254  0.0166  0.0370  199 LEU A C     
1509 O  O     . LEU A 219 ? 0.2442 0.2106 0.1632 0.0218  0.0194  0.0391  199 LEU A O     
1510 C  CB    . LEU A 219 ? 0.2243 0.2266 0.1711 0.0359  0.0165  0.0164  199 LEU A CB    
1511 C  CG    . LEU A 219 ? 0.2292 0.2602 0.1934 0.0239  0.0073  0.0090  199 LEU A CG    
1512 C  CD1   . LEU A 219 ? 0.2394 0.2794 0.1972 0.0196  -0.0052 0.0100  199 LEU A CD1   
1513 C  CD2   . LEU A 219 ? 0.2174 0.2696 0.1991 0.0394  0.0166  0.0200  199 LEU A CD2   
1514 N  N     . LYS A 220 ? 0.2548 0.1907 0.1612 0.0197  0.0245  0.0370  200 LYS A N     
1515 C  CA    . LYS A 220 ? 0.2810 0.2005 0.1912 0.0083  0.0506  0.0182  200 LYS A CA    
1516 C  C     . LYS A 220 ? 0.2659 0.2019 0.1772 0.0212  0.0460  0.0294  200 LYS A C     
1517 O  O     . LYS A 220 ? 0.2839 0.2135 0.1841 0.0279  0.0337  0.0486  200 LYS A O     
1518 C  CB    . LYS A 220 ? 0.3404 0.2195 0.2409 -0.0005 0.0802  0.0067  200 LYS A CB    
1519 C  CG    . LYS A 220 ? 0.4260 0.2519 0.3002 0.0110  0.0838  0.0255  200 LYS A CG    
1520 C  CD    . LYS A 220 ? 0.5078 0.2963 0.3581 0.0384  0.0778  0.0246  200 LYS A CD    
1521 C  CE    . LYS A 220 ? 0.5668 0.3267 0.3921 0.0535  0.0761  0.0321  200 LYS A CE    
1522 N  NZ    . LYS A 220 ? 0.6069 0.3506 0.4141 0.0624  0.0816  0.0347  200 LYS A NZ    
1523 N  N     . ALA A 221 ? 0.2366 0.2175 0.1567 0.0355  0.0216  0.0371  201 ALA A N     
1524 C  CA    . ALA A 221 ? 0.2248 0.2104 0.1632 0.0212  0.0280  0.0300  201 ALA A CA    
1525 C  C     . ALA A 221 ? 0.2264 0.2120 0.1553 0.0288  0.0207  0.0522  201 ALA A C     
1526 O  O     . ALA A 221 ? 0.2318 0.2283 0.1609 0.0310  0.0283  0.0580  201 ALA A O     
1527 C  CB    . ALA A 221 ? 0.2096 0.2149 0.1719 0.0328  0.0288  0.0246  201 ALA A CB    
1528 N  N     . LEU A 222 ? 0.2197 0.2128 0.1495 0.0204  0.0130  0.0359  202 LEU A N     
1529 C  CA    . LEU A 222 ? 0.2146 0.2120 0.1554 0.0199  0.0158  0.0385  202 LEU A CA    
1530 C  C     . LEU A 222 ? 0.2516 0.2394 0.1604 0.0241  0.0234  0.0535  202 LEU A C     
1531 O  O     . LEU A 222 ? 0.2791 0.2628 0.1564 0.0354  0.0107  0.0595  202 LEU A O     
1532 C  CB    . LEU A 222 ? 0.2260 0.2131 0.1577 0.0191  0.0243  0.0067  202 LEU A CB    
1533 C  CG    . LEU A 222 ? 0.2195 0.2117 0.1556 0.0091  0.0196  0.0059  202 LEU A CG    
1534 C  CD1   . LEU A 222 ? 0.1999 0.2151 0.1747 -0.0088 0.0243  0.0062  202 LEU A CD1   
1535 C  CD2   . LEU A 222 ? 0.2580 0.2192 0.1663 -0.0033 0.0233  0.0076  202 LEU A CD2   
1536 N  N     . LYS A 223 ? 0.2610 0.2303 0.1663 0.0396  0.0187  0.0566  203 LYS A N     
1537 C  CA    . LYS A 223 ? 0.2904 0.2354 0.1918 0.0472  0.0142  0.0545  203 LYS A CA    
1538 C  C     . LYS A 223 ? 0.2979 0.2359 0.2050 0.0348  0.0310  0.0691  203 LYS A C     
1539 O  O     . LYS A 223 ? 0.3330 0.2597 0.2331 0.0291  0.0437  0.0838  203 LYS A O     
1540 C  CB    . LYS A 223 ? 0.3098 0.2609 0.2137 0.0576  0.0269  0.0649  203 LYS A CB    
1541 C  CG    . LYS A 223 ? 0.3335 0.3080 0.2210 0.0859  0.0431  0.0740  203 LYS A CG    
1542 C  CD    . LYS A 223 ? 0.3960 0.3598 0.2475 0.1156  0.0526  0.0633  203 LYS A CD    
1543 C  CE    . LYS A 223 ? 0.4815 0.3945 0.2701 0.1366  0.0311  0.0709  203 LYS A CE    
1544 N  NZ    . LYS A 223 ? 0.5258 0.4278 0.2787 0.1365  0.0294  0.0723  203 LYS A NZ    
1545 N  N     . GLY A 224 ? 0.2746 0.2293 0.1992 0.0174  0.0382  0.0558  204 GLY A N     
1546 C  CA    . GLY A 224 ? 0.2908 0.2503 0.2017 -0.0092 0.0492  0.0486  204 GLY A CA    
1547 C  C     . GLY A 224 ? 0.3350 0.2550 0.2169 -0.0362 0.0572  0.0599  204 GLY A C     
1548 O  O     . GLY A 224 ? 0.3851 0.2904 0.2315 -0.0514 0.0747  0.0471  204 GLY A O     
1549 N  N     . GLU A 225 ? 0.3291 0.2560 0.2142 -0.0246 0.0393  0.0614  205 GLU A N     
1550 C  CA    . GLU A 225 ? 0.3615 0.2583 0.2296 -0.0335 0.0297  0.0543  205 GLU A CA    
1551 C  C     . GLU A 225 ? 0.3752 0.2668 0.2240 -0.0421 0.0066  0.0388  205 GLU A C     
1552 O  O     . GLU A 225 ? 0.3324 0.2588 0.2298 -0.0288 -0.0006 0.0279  205 GLU A O     
1553 C  CB    . GLU A 225 ? 0.3907 0.2775 0.2558 0.0025  0.0233  0.0520  205 GLU A CB    
1554 C  CG    . GLU A 225 ? 0.4212 0.3077 0.2847 0.0259  0.0271  0.0529  205 GLU A CG    
1555 C  CD    . GLU A 225 ? 0.4419 0.3430 0.3160 0.0463  0.0407  0.0429  205 GLU A CD    
1556 O  OE1   . GLU A 225 ? 0.4637 0.3796 0.3394 0.0569  0.0493  0.0274  205 GLU A OE1   
1557 O  OE2   . GLU A 225 ? 0.4366 0.3275 0.3289 0.0462  0.0550  0.0412  205 GLU A OE2   
1558 N  N     . LYS A 226 ? 0.4339 0.2885 0.2251 -0.0557 -0.0041 0.0333  206 LYS A N     
1559 C  CA    . LYS A 226 ? 0.4933 0.3269 0.2454 -0.0656 -0.0165 0.0298  206 LYS A CA    
1560 C  C     . LYS A 226 ? 0.5288 0.3165 0.2589 -0.0490 -0.0206 0.0236  206 LYS A C     
1561 O  O     . LYS A 226 ? 0.5405 0.3378 0.2817 -0.0136 -0.0300 0.0186  206 LYS A O     
1562 C  CB    . LYS A 226 ? 0.5207 0.3658 0.2531 -0.0924 -0.0170 0.0323  206 LYS A CB    
1563 C  CG    . LYS A 226 ? 0.5245 0.3869 0.2520 -0.1205 -0.0080 0.0307  206 LYS A CG    
1564 N  N     . VAL A 227 ? 0.5399 0.2934 0.2456 -0.0681 -0.0129 0.0336  207 VAL A N     
1565 C  CA    . VAL A 227 ? 0.5720 0.3163 0.2681 -0.0784 -0.0063 0.0319  207 VAL A CA    
1566 C  C     . VAL A 227 ? 0.6481 0.3789 0.3075 -0.1079 0.0007  0.0277  207 VAL A C     
1567 O  O     . VAL A 227 ? 0.6501 0.3933 0.3132 -0.1113 0.0081  0.0199  207 VAL A O     
1568 C  CB    . VAL A 227 ? 0.5414 0.2859 0.2605 -0.0606 -0.0143 0.0289  207 VAL A CB    
1569 C  CG1   . VAL A 227 ? 0.5220 0.2773 0.2562 -0.0591 -0.0113 0.0173  207 VAL A CG1   
1570 C  CG2   . VAL A 227 ? 0.5407 0.2852 0.2652 -0.0501 -0.0071 0.0273  207 VAL A CG2   
1571 N  N     . GLU A 228 ? 0.7138 0.4158 0.3461 -0.1392 -0.0040 0.0305  208 GLU A N     
1572 C  CA    . GLU A 228 ? 0.7651 0.4666 0.3882 -0.1761 -0.0028 0.0200  208 GLU A CA    
1573 C  C     . GLU A 228 ? 0.7990 0.4969 0.4126 -0.2164 -0.0058 0.0131  208 GLU A C     
1574 O  O     . GLU A 228 ? 0.8004 0.4992 0.4163 -0.2361 -0.0148 0.0173  208 GLU A O     
1575 C  CB    . GLU A 228 ? 0.7730 0.4762 0.3986 -0.1732 0.0069  0.0155  208 GLU A CB    
1576 N  N     . ALA A 229 ? 0.8361 0.5256 0.4386 -0.2142 0.0064  0.0148  209 ALA A N     
1577 C  CA    . ALA A 229 ? 0.8662 0.5490 0.4667 -0.2197 0.0201  0.0147  209 ALA A CA    
1578 C  C     . ALA A 229 ? 0.8877 0.5584 0.4809 -0.2313 0.0154  0.0142  209 ALA A C     
1579 O  O     . ALA A 229 ? 0.9028 0.5562 0.4833 -0.2361 0.0162  0.0163  209 ALA A O     
1580 C  CB    . ALA A 229 ? 0.8654 0.5527 0.4753 -0.2261 0.0314  0.0154  209 ALA A CB    
1581 N  N     . LYS A 230 ? 0.8892 0.5686 0.4912 -0.2302 0.0087  0.0101  210 LYS A N     
1582 C  CA    . LYS A 230 ? 0.8927 0.5879 0.5051 -0.2172 0.0066  0.0119  210 LYS A CA    
1583 C  C     . LYS A 230 ? 0.8966 0.6075 0.5157 -0.2056 0.0048  0.0133  210 LYS A C     
1584 O  O     . LYS A 230 ? 0.8991 0.6190 0.5227 -0.1980 0.0034  0.0122  210 LYS A O     
1585 C  CB    . LYS A 230 ? 0.8930 0.5874 0.5060 -0.2148 0.0065  0.0101  210 LYS A CB    
1586 P  PB    . ADP B .   ? 0.2013 0.2568 0.1264 0.0067  -0.0191 -0.0200 301 ADP A PB    
1587 O  O1B   . ADP B .   ? 0.1937 0.2617 0.1415 0.0117  -0.0233 -0.0283 301 ADP A O1B   
1588 O  O2B   . ADP B .   ? 0.2360 0.2491 0.1476 -0.0007 -0.0005 -0.0225 301 ADP A O2B   
1589 O  O3B   . ADP B .   ? 0.1978 0.2528 0.1215 0.0083  -0.0189 -0.0191 301 ADP A O3B   
1590 P  PA    . ADP B .   ? 0.1647 0.2568 0.1261 -0.0158 -0.0054 -0.0251 301 ADP A PA    
1591 O  O1A   . ADP B .   ? 0.1734 0.2607 0.1395 -0.0135 -0.0101 -0.0245 301 ADP A O1A   
1592 O  O2A   . ADP B .   ? 0.1771 0.2420 0.1115 -0.0121 -0.0058 -0.0413 301 ADP A O2A   
1593 O  O3A   . ADP B .   ? 0.1899 0.2387 0.1251 -0.0074 -0.0102 -0.0165 301 ADP A O3A   
1594 O  "O5'" . ADP B .   ? 0.1529 0.2330 0.1217 -0.0220 -0.0079 -0.0314 301 ADP A "O5'" 
1595 C  "C5'" . ADP B .   ? 0.1603 0.2343 0.1259 -0.0119 -0.0083 -0.0208 301 ADP A "C5'" 
1596 C  "C4'" . ADP B .   ? 0.1668 0.2165 0.1277 -0.0177 -0.0146 -0.0197 301 ADP A "C4'" 
1597 O  "O4'" . ADP B .   ? 0.1681 0.2136 0.1415 -0.0171 -0.0193 -0.0174 301 ADP A "O4'" 
1598 C  "C3'" . ADP B .   ? 0.1630 0.2291 0.1283 -0.0157 -0.0144 -0.0256 301 ADP A "C3'" 
1599 O  "O3'" . ADP B .   ? 0.2039 0.2406 0.1336 0.0129  -0.0089 -0.0416 301 ADP A "O3'" 
1600 C  "C2'" . ADP B .   ? 0.1758 0.2334 0.1191 -0.0127 -0.0080 -0.0015 301 ADP A "C2'" 
1601 O  "O2'" . ADP B .   ? 0.1647 0.2138 0.1195 -0.0118 -0.0149 -0.0082 301 ADP A "O2'" 
1602 C  "C1'" . ADP B .   ? 0.1703 0.2216 0.1287 -0.0018 -0.0012 -0.0124 301 ADP A "C1'" 
1603 N  N9    . ADP B .   ? 0.1718 0.2232 0.1216 -0.0012 -0.0145 -0.0123 301 ADP A N9    
1604 C  C8    . ADP B .   ? 0.2039 0.2436 0.1380 -0.0131 -0.0234 0.0001  301 ADP A C8    
1605 N  N7    . ADP B .   ? 0.1986 0.2641 0.1383 -0.0115 -0.0311 0.0058  301 ADP A N7    
1606 C  C5    . ADP B .   ? 0.1747 0.2392 0.1421 -0.0003 -0.0059 0.0026  301 ADP A C5    
1607 C  C6    . ADP B .   ? 0.1758 0.2262 0.1507 0.0028  0.0002  0.0185  301 ADP A C6    
1608 N  N6    . ADP B .   ? 0.2090 0.2396 0.1684 0.0055  -0.0159 0.0424  301 ADP A N6    
1609 N  N1    . ADP B .   ? 0.1706 0.2277 0.1486 0.0009  -0.0065 0.0097  301 ADP A N1    
1610 C  C2    . ADP B .   ? 0.1702 0.2286 0.1440 -0.0061 0.0053  0.0016  301 ADP A C2    
1611 N  N3    . ADP B .   ? 0.1538 0.2359 0.1323 -0.0022 -0.0075 -0.0079 301 ADP A N3    
1612 C  C4    . ADP B .   ? 0.1552 0.2425 0.1287 -0.0010 -0.0085 -0.0102 301 ADP A C4    
1613 MG MG    . MG  C .   ? 0.1908 0.2731 0.1197 -0.0114 -0.0240 -0.0335 302 MG  A MG    
1614 MG MG    . MG  D .   ? 0.2015 0.3100 0.1399 0.0005  -0.0357 -0.0295 303 MG  A MG    
1615 C  C2    . PG4 E .   ? 0.6508 0.3985 0.6581 0.0738  -0.0180 -0.0885 304 PG4 A C2    
1616 O  O2    . PG4 E .   ? 0.6393 0.3810 0.6521 0.0851  -0.0248 -0.0879 304 PG4 A O2    
1617 C  C3    . PG4 E .   ? 0.6236 0.3583 0.6491 0.0716  -0.0346 -0.0848 304 PG4 A C3    
1618 C  C4    . PG4 E .   ? 0.6119 0.3435 0.6444 0.0596  -0.0406 -0.0785 304 PG4 A C4    
1619 O  O3    . PG4 E .   ? 0.5971 0.3325 0.6374 0.0405  -0.0549 -0.0771 304 PG4 A O3    
1620 C  C5    . PG4 E .   ? 0.5922 0.3264 0.6375 0.0491  -0.0543 -0.0740 304 PG4 A C5    
1621 C  C6    . PG4 E .   ? 0.5928 0.3335 0.6379 0.0529  -0.0529 -0.0726 304 PG4 A C6    
1622 O  O4    . PG4 E .   ? 0.6024 0.3385 0.6400 0.0661  -0.0492 -0.0786 304 PG4 A O4    
1623 C  C7    . PG4 E .   ? 0.6197 0.3619 0.6439 0.0644  -0.0422 -0.0831 304 PG4 A C7    
1624 C  C8    . PG4 E .   ? 0.6296 0.3758 0.6463 0.0789  -0.0303 -0.0867 304 PG4 A C8    
1625 O  O5    . PG4 E .   ? 0.6427 0.3869 0.6473 0.0996  -0.0273 -0.0905 304 PG4 A O5    
# 
