data_8VIQ
# 
_entry.id   8VIQ 
# 
_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   8VIQ         pdb_00008viq 10.2210/pdb8viq/pdb 
WWPDB D_1000280329 ?            ?                   
# 
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                        8VIQ 
_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 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   1   ? ? ?                             ? 
3 non-polymer syn 'MAGNESIUM ION'                               24.305    2   ? ? ?                             ? 
4 water       nat water                                         18.015    229 ? ? ?                             ? 
# 
_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 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
3 'MAGNESIUM ION'                               MG  
4 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   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 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
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  
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  ?   ?   ?   A . n 
A 1 20  HIS 20  0   ?   ?   ?   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 ANP ? ? ANP ? ? '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 ANP 1   301 1   ANP ANP A . 
C 3 MG  1   302 1   MG  MG  A . 
D 3 MG  1   303 2   MG  MG  A . 
E 4 HOH 1   401 201 HOH HOH A . 
E 4 HOH 2   402 133 HOH HOH A . 
E 4 HOH 3   403 101 HOH HOH A . 
E 4 HOH 4   404 202 HOH HOH A . 
E 4 HOH 5   405 113 HOH HOH A . 
E 4 HOH 6   406 148 HOH HOH A . 
E 4 HOH 7   407 199 HOH HOH A . 
E 4 HOH 8   408 57  HOH HOH A . 
E 4 HOH 9   409 8   HOH HOH A . 
E 4 HOH 10  410 155 HOH HOH A . 
E 4 HOH 11  411 221 HOH HOH A . 
E 4 HOH 12  412 79  HOH HOH A . 
E 4 HOH 13  413 196 HOH HOH A . 
E 4 HOH 14  414 104 HOH HOH A . 
E 4 HOH 15  415 194 HOH HOH A . 
E 4 HOH 16  416 215 HOH HOH A . 
E 4 HOH 17  417 46  HOH HOH A . 
E 4 HOH 18  418 31  HOH HOH A . 
E 4 HOH 19  419 22  HOH HOH A . 
E 4 HOH 20  420 88  HOH HOH A . 
E 4 HOH 21  421 222 HOH HOH A . 
E 4 HOH 22  422 19  HOH HOH A . 
E 4 HOH 23  423 166 HOH HOH A . 
E 4 HOH 24  424 138 HOH HOH A . 
E 4 HOH 25  425 151 HOH HOH A . 
E 4 HOH 26  426 34  HOH HOH A . 
E 4 HOH 27  427 4   HOH HOH A . 
E 4 HOH 28  428 6   HOH HOH A . 
E 4 HOH 29  429 53  HOH HOH A . 
E 4 HOH 30  430 183 HOH HOH A . 
E 4 HOH 31  431 84  HOH HOH A . 
E 4 HOH 32  432 167 HOH HOH A . 
E 4 HOH 33  433 125 HOH HOH A . 
E 4 HOH 34  434 186 HOH HOH A . 
E 4 HOH 35  435 56  HOH HOH A . 
E 4 HOH 36  436 59  HOH HOH A . 
E 4 HOH 37  437 150 HOH HOH A . 
E 4 HOH 38  438 23  HOH HOH A . 
E 4 HOH 39  439 117 HOH HOH A . 
E 4 HOH 40  440 71  HOH HOH A . 
E 4 HOH 41  441 74  HOH HOH A . 
E 4 HOH 42  442 39  HOH HOH A . 
E 4 HOH 43  443 44  HOH HOH A . 
E 4 HOH 44  444 86  HOH HOH A . 
E 4 HOH 45  445 80  HOH HOH A . 
E 4 HOH 46  446 177 HOH HOH A . 
E 4 HOH 47  447 198 HOH HOH A . 
E 4 HOH 48  448 48  HOH HOH A . 
E 4 HOH 49  449 64  HOH HOH A . 
E 4 HOH 50  450 168 HOH HOH A . 
E 4 HOH 51  451 72  HOH HOH A . 
E 4 HOH 52  452 78  HOH HOH A . 
E 4 HOH 53  453 76  HOH HOH A . 
E 4 HOH 54  454 90  HOH HOH A . 
E 4 HOH 55  455 5   HOH HOH A . 
E 4 HOH 56  456 12  HOH HOH A . 
E 4 HOH 57  457 176 HOH HOH A . 
E 4 HOH 58  458 7   HOH HOH A . 
E 4 HOH 59  459 216 HOH HOH A . 
E 4 HOH 60  460 14  HOH HOH A . 
E 4 HOH 61  461 38  HOH HOH A . 
E 4 HOH 62  462 188 HOH HOH A . 
E 4 HOH 63  463 124 HOH HOH A . 
E 4 HOH 64  464 2   HOH HOH A . 
E 4 HOH 65  465 18  HOH HOH A . 
E 4 HOH 66  466 110 HOH HOH A . 
E 4 HOH 67  467 75  HOH HOH A . 
E 4 HOH 68  468 108 HOH HOH A . 
E 4 HOH 69  469 129 HOH HOH A . 
E 4 HOH 70  470 20  HOH HOH A . 
E 4 HOH 71  471 191 HOH HOH A . 
E 4 HOH 72  472 49  HOH HOH A . 
E 4 HOH 73  473 153 HOH HOH A . 
E 4 HOH 74  474 35  HOH HOH A . 
E 4 HOH 75  475 62  HOH HOH A . 
E 4 HOH 76  476 224 HOH HOH A . 
E 4 HOH 77  477 146 HOH HOH A . 
E 4 HOH 78  478 120 HOH HOH A . 
E 4 HOH 79  479 37  HOH HOH A . 
E 4 HOH 80  480 33  HOH HOH A . 
E 4 HOH 81  481 10  HOH HOH A . 
E 4 HOH 82  482 116 HOH HOH A . 
E 4 HOH 83  483 161 HOH HOH A . 
E 4 HOH 84  484 164 HOH HOH A . 
E 4 HOH 85  485 204 HOH HOH A . 
E 4 HOH 86  486 11  HOH HOH A . 
E 4 HOH 87  487 27  HOH HOH A . 
E 4 HOH 88  488 143 HOH HOH A . 
E 4 HOH 89  489 9   HOH HOH A . 
E 4 HOH 90  490 93  HOH HOH A . 
E 4 HOH 91  491 29  HOH HOH A . 
E 4 HOH 92  492 55  HOH HOH A . 
E 4 HOH 93  493 68  HOH HOH A . 
E 4 HOH 94  494 107 HOH HOH A . 
E 4 HOH 95  495 132 HOH HOH A . 
E 4 HOH 96  496 92  HOH HOH A . 
E 4 HOH 97  497 47  HOH HOH A . 
E 4 HOH 98  498 97  HOH HOH A . 
E 4 HOH 99  499 73  HOH HOH A . 
E 4 HOH 100 500 141 HOH HOH A . 
E 4 HOH 101 501 111 HOH HOH A . 
E 4 HOH 102 502 15  HOH HOH A . 
E 4 HOH 103 503 118 HOH HOH A . 
E 4 HOH 104 504 197 HOH HOH A . 
E 4 HOH 105 505 26  HOH HOH A . 
E 4 HOH 106 506 36  HOH HOH A . 
E 4 HOH 107 507 140 HOH HOH A . 
E 4 HOH 108 508 208 HOH HOH A . 
E 4 HOH 109 509 54  HOH HOH A . 
E 4 HOH 110 510 61  HOH HOH A . 
E 4 HOH 111 511 82  HOH HOH A . 
E 4 HOH 112 512 98  HOH HOH A . 
E 4 HOH 113 513 50  HOH HOH A . 
E 4 HOH 114 514 147 HOH HOH A . 
E 4 HOH 115 515 16  HOH HOH A . 
E 4 HOH 116 516 13  HOH HOH A . 
E 4 HOH 117 517 28  HOH HOH A . 
E 4 HOH 118 518 226 HOH HOH A . 
E 4 HOH 119 519 52  HOH HOH A . 
E 4 HOH 120 520 40  HOH HOH A . 
E 4 HOH 121 521 30  HOH HOH A . 
E 4 HOH 122 522 42  HOH HOH A . 
E 4 HOH 123 523 200 HOH HOH A . 
E 4 HOH 124 524 58  HOH HOH A . 
E 4 HOH 125 525 91  HOH HOH A . 
E 4 HOH 126 526 41  HOH HOH A . 
E 4 HOH 127 527 85  HOH HOH A . 
E 4 HOH 128 528 32  HOH HOH A . 
E 4 HOH 129 529 131 HOH HOH A . 
E 4 HOH 130 530 96  HOH HOH A . 
E 4 HOH 131 531 162 HOH HOH A . 
E 4 HOH 132 532 21  HOH HOH A . 
E 4 HOH 133 533 170 HOH HOH A . 
E 4 HOH 134 534 179 HOH HOH A . 
E 4 HOH 135 535 223 HOH HOH A . 
E 4 HOH 136 536 24  HOH HOH A . 
E 4 HOH 137 537 152 HOH HOH A . 
E 4 HOH 138 538 174 HOH HOH A . 
E 4 HOH 139 539 127 HOH HOH A . 
E 4 HOH 140 540 156 HOH HOH A . 
E 4 HOH 141 541 25  HOH HOH A . 
E 4 HOH 142 542 77  HOH HOH A . 
E 4 HOH 143 543 160 HOH HOH A . 
E 4 HOH 144 544 112 HOH HOH A . 
E 4 HOH 145 545 154 HOH HOH A . 
E 4 HOH 146 546 121 HOH HOH A . 
E 4 HOH 147 547 43  HOH HOH A . 
E 4 HOH 148 548 60  HOH HOH A . 
E 4 HOH 149 549 67  HOH HOH A . 
E 4 HOH 150 550 66  HOH HOH A . 
E 4 HOH 151 551 102 HOH HOH A . 
E 4 HOH 152 552 182 HOH HOH A . 
E 4 HOH 153 553 136 HOH HOH A . 
E 4 HOH 154 554 171 HOH HOH A . 
E 4 HOH 155 555 145 HOH HOH A . 
E 4 HOH 156 556 229 HOH HOH A . 
E 4 HOH 157 557 17  HOH HOH A . 
E 4 HOH 158 558 81  HOH HOH A . 
E 4 HOH 159 559 181 HOH HOH A . 
E 4 HOH 160 560 100 HOH HOH A . 
E 4 HOH 161 561 139 HOH HOH A . 
E 4 HOH 162 562 149 HOH HOH A . 
E 4 HOH 163 563 128 HOH HOH A . 
E 4 HOH 164 564 165 HOH HOH A . 
E 4 HOH 165 565 173 HOH HOH A . 
E 4 HOH 166 566 126 HOH HOH A . 
E 4 HOH 167 567 45  HOH HOH A . 
E 4 HOH 168 568 206 HOH HOH A . 
E 4 HOH 169 569 123 HOH HOH A . 
E 4 HOH 170 570 169 HOH HOH A . 
E 4 HOH 171 571 144 HOH HOH A . 
E 4 HOH 172 572 115 HOH HOH A . 
E 4 HOH 173 573 130 HOH HOH A . 
E 4 HOH 174 574 122 HOH HOH A . 
E 4 HOH 175 575 87  HOH HOH A . 
E 4 HOH 176 576 163 HOH HOH A . 
E 4 HOH 177 577 106 HOH HOH A . 
E 4 HOH 178 578 142 HOH HOH A . 
E 4 HOH 179 579 187 HOH HOH A . 
E 4 HOH 180 580 217 HOH HOH A . 
E 4 HOH 181 581 189 HOH HOH A . 
E 4 HOH 182 582 103 HOH HOH A . 
E 4 HOH 183 583 119 HOH HOH A . 
E 4 HOH 184 584 180 HOH HOH A . 
E 4 HOH 185 585 172 HOH HOH A . 
E 4 HOH 186 586 228 HOH HOH A . 
E 4 HOH 187 587 94  HOH HOH A . 
E 4 HOH 188 588 175 HOH HOH A . 
E 4 HOH 189 589 137 HOH HOH A . 
E 4 HOH 190 590 193 HOH HOH A . 
E 4 HOH 191 591 184 HOH HOH A . 
E 4 HOH 192 592 207 HOH HOH A . 
E 4 HOH 193 593 134 HOH HOH A . 
E 4 HOH 194 594 89  HOH HOH A . 
E 4 HOH 195 595 203 HOH HOH A . 
E 4 HOH 196 596 63  HOH HOH A . 
E 4 HOH 197 597 220 HOH HOH A . 
E 4 HOH 198 598 157 HOH HOH A . 
E 4 HOH 199 599 213 HOH HOH A . 
E 4 HOH 200 600 214 HOH HOH A . 
E 4 HOH 201 601 209 HOH HOH A . 
E 4 HOH 202 602 51  HOH HOH A . 
E 4 HOH 203 603 99  HOH HOH A . 
E 4 HOH 204 604 195 HOH HOH A . 
E 4 HOH 205 605 205 HOH HOH A . 
E 4 HOH 206 606 219 HOH HOH A . 
E 4 HOH 207 607 158 HOH HOH A . 
E 4 HOH 208 608 114 HOH HOH A . 
E 4 HOH 209 609 95  HOH HOH A . 
E 4 HOH 210 610 218 HOH HOH A . 
E 4 HOH 211 611 65  HOH HOH A . 
E 4 HOH 212 612 69  HOH HOH A . 
E 4 HOH 213 613 105 HOH HOH A . 
E 4 HOH 214 614 70  HOH HOH A . 
E 4 HOH 215 615 190 HOH HOH A . 
E 4 HOH 216 616 210 HOH HOH A . 
E 4 HOH 217 617 1   HOH HOH A . 
E 4 HOH 218 618 135 HOH HOH A . 
E 4 HOH 219 619 211 HOH HOH A . 
E 4 HOH 220 620 178 HOH HOH A . 
E 4 HOH 221 621 212 HOH HOH A . 
E 4 HOH 222 622 83  HOH HOH A . 
E 4 HOH 223 623 159 HOH HOH A . 
E 4 HOH 224 624 109 HOH HOH A . 
E 4 HOH 225 625 227 HOH HOH A . 
E 4 HOH 226 626 225 HOH HOH A . 
E 4 HOH 227 627 185 HOH HOH A . 
E 4 HOH 228 628 192 HOH HOH A . 
E 4 HOH 229 629 3   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 LYS 4   ? CE  ? A LYS 24  CE  
2  1 Y 1 A LYS 4   ? NZ  ? A LYS 24  NZ  
3  1 Y 1 A LYS 73  ? CD  ? A LYS 93  CD  
4  1 Y 1 A LYS 73  ? CE  ? A LYS 93  CE  
5  1 Y 1 A LYS 73  ? NZ  ? A LYS 93  NZ  
6  1 Y 1 A ARG 80  ? CD  ? A ARG 100 CD  
7  1 Y 1 A ARG 80  ? NE  ? A ARG 100 NE  
8  1 Y 1 A ARG 80  ? CZ  ? A ARG 100 CZ  
9  1 Y 1 A ARG 80  ? NH1 ? A ARG 100 NH1 
10 1 Y 1 A ARG 80  ? NH2 ? A ARG 100 NH2 
11 1 Y 1 A GLU 111 ? CD  ? A GLU 131 CD  
12 1 Y 1 A GLU 111 ? OE1 ? A GLU 131 OE1 
13 1 Y 1 A GLU 111 ? OE2 ? A GLU 131 OE2 
14 1 Y 1 A LYS 122 ? CE  ? A LYS 142 CE  
15 1 Y 1 A LYS 122 ? NZ  ? A LYS 142 NZ  
16 1 Y 1 A LYS 203 ? CE  ? A LYS 223 CE  
17 1 Y 1 A LYS 203 ? NZ  ? A LYS 223 NZ  
18 1 Y 1 A GLU 208 ? CG  ? A GLU 228 CG  
19 1 Y 1 A GLU 208 ? CD  ? A GLU 228 CD  
20 1 Y 1 A GLU 208 ? OE1 ? A GLU 228 OE1 
21 1 Y 1 A GLU 208 ? OE2 ? A GLU 228 OE2 
22 1 Y 1 A LYS 210 ? CG  ? A LYS 230 CG  
23 1 Y 1 A LYS 210 ? CD  ? A LYS 230 CD  
24 1 Y 1 A LYS 210 ? CE  ? A LYS 230 CE  
25 1 Y 1 A LYS 210 ? NZ  ? A LYS 230 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.15_3460: ???)' 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                     8VIQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.728 
_cell.length_a_esd                 ? 
_cell.length_b                     56.433 
_cell.length_b_esd                 ? 
_cell.length_c                     81.803 
_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                         8VIQ 
_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                   8VIQ 
_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             1.99 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          38.10 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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 D9: 15% (w/v) PEG 6000, 100 mM MES pH 6.5, 5% (v/v) 2-methyl-2,4-pentanediol, Cryo: 85% crystallization solution and 15% (v/v) MPD, 2.5 mM MgCl2 and 2.5 mM AMP-PNP 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         2019-03-30 
_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                                       8VIQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.10 
_reflns.d_resolution_low                               46.45 
_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                                     81027 
_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                          12.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.061 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       512550 
_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                              0.056 
_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                                    1.10 
_reflns_shell.d_res_low                                     1.12 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           24635 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3948 
_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                               6.2 
_reflns_shell.pdbx_chi_squared                              1.02 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               1.237 
_reflns_shell.pdbx_Rpim_I_all                               0.492 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.675 
_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                                  1.133 
_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                                 8VIQ 
_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                            1.100 
_refine.ls_d_res_low                             34.065 
_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                     80922 
_refine.ls_number_reflns_R_free                  3958 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.94 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1262 
_refine.ls_R_factor_R_free                       0.1417 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1254 
_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                          1.01 
_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                 12.44 
_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                            0.09 
_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                       1.100 
_refine_hist.d_res_low                        34.065 
_refine_hist.number_atoms_solvent             229 
_refine_hist.number_atoms_total               1805 
_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        1543 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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 ? 1653 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.988 ? 2253 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.025 ? 963  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.067 ? 270  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006 ? 290  ? 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' 1.1000 1.1134 . . 134 2701 100.00 . . . . 0.2237 . . . . . . . . . . . 0.2234 
'X-RAY DIFFRACTION' 1.1134 1.1275 . . 147 2764 100.00 . . . . 0.2179 . . . . . . . . . . . 0.2484 
'X-RAY DIFFRACTION' 1.1275 1.1424 . . 126 2700 100.00 . . . . 0.1952 . . . . . . . . . . . 0.2038 
'X-RAY DIFFRACTION' 1.1424 1.1580 . . 146 2681 100.00 . . . . 0.1870 . . . . . . . . . . . 0.1871 
'X-RAY DIFFRACTION' 1.1580 1.1745 . . 148 2716 100.00 . . . . 0.1779 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 1.1745 1.1921 . . 149 2712 100.00 . . . . 0.1655 . . . . . . . . . . . 0.2023 
'X-RAY DIFFRACTION' 1.1921 1.2107 . . 132 2704 100.00 . . . . 0.1495 . . . . . . . . . . . 0.1698 
'X-RAY DIFFRACTION' 1.2107 1.2306 . . 128 2754 100.00 . . . . 0.1435 . . . . . . . . . . . 0.1780 
'X-RAY DIFFRACTION' 1.2306 1.2518 . . 160 2676 100.00 . . . . 0.1390 . . . . . . . . . . . 0.1503 
'X-RAY DIFFRACTION' 1.2518 1.2745 . . 157 2713 100.00 . . . . 0.1337 . . . . . . . . . . . 0.1492 
'X-RAY DIFFRACTION' 1.2745 1.2991 . . 148 2741 100.00 . . . . 0.1288 . . . . . . . . . . . 0.1536 
'X-RAY DIFFRACTION' 1.2991 1.3256 . . 139 2706 100.00 . . . . 0.1208 . . . . . . . . . . . 0.1388 
'X-RAY DIFFRACTION' 1.3256 1.3544 . . 146 2732 100.00 . . . . 0.1152 . . . . . . . . . . . 0.1516 
'X-RAY DIFFRACTION' 1.3544 1.3859 . . 145 2735 100.00 . . . . 0.1128 . . . . . . . . . . . 0.1313 
'X-RAY DIFFRACTION' 1.3859 1.4206 . . 141 2742 100.00 . . . . 0.1065 . . . . . . . . . . . 0.1082 
'X-RAY DIFFRACTION' 1.4206 1.4590 . . 159 2705 100.00 . . . . 0.0955 . . . . . . . . . . . 0.1128 
'X-RAY DIFFRACTION' 1.4590 1.5019 . . 141 2735 100.00 . . . . 0.0950 . . . . . . . . . . . 0.1222 
'X-RAY DIFFRACTION' 1.5019 1.5504 . . 144 2730 100.00 . . . . 0.0958 . . . . . . . . . . . 0.1146 
'X-RAY DIFFRACTION' 1.5504 1.6058 . . 127 2768 100.00 . . . . 0.0925 . . . . . . . . . . . 0.1195 
'X-RAY DIFFRACTION' 1.6058 1.6701 . . 127 2753 100.00 . . . . 0.1012 . . . . . . . . . . . 0.1110 
'X-RAY DIFFRACTION' 1.6701 1.7461 . . 136 2769 100.00 . . . . 0.1051 . . . . . . . . . . . 0.1232 
'X-RAY DIFFRACTION' 1.7461 1.8381 . . 141 2760 100.00 . . . . 0.1134 . . . . . . . . . . . 0.1346 
'X-RAY DIFFRACTION' 1.8381 1.9533 . . 127 2797 100.00 . . . . 0.1173 . . . . . . . . . . . 0.1455 
'X-RAY DIFFRACTION' 1.9533 2.1041 . . 126 2764 100.00 . . . . 0.1144 . . . . . . . . . . . 0.1185 
'X-RAY DIFFRACTION' 2.1041 2.3158 . . 157 2777 100.00 . . . . 0.1173 . . . . . . . . . . . 0.1198 
'X-RAY DIFFRACTION' 2.3158 2.6508 . . 133 2822 100.00 . . . . 0.1215 . . . . . . . . . . . 0.1228 
'X-RAY DIFFRACTION' 2.6508 3.3392 . . 140 2846 100.00 . . . . 0.1299 . . . . . . . . . . . 0.1494 
'X-RAY DIFFRACTION' 3.3392 34.065 . . 154 2961 100.00 . . . . 0.1403 . . . . . . . . . . . 0.1632 
# 
_struct.entry_id                     8VIQ 
_struct.title                        
'Crystal structure of the N-terminal domain of fatty acid kinase A (FakA) from Staphylococcus aureus (Mg and AMP-PNP)' 
_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        8VIQ 
_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 ? 
# 
_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              8VIQ 
_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 8VIQ MET A 1  ? UNP Q2FZ58 ? ? 'expression tag' -19 1  
1 8VIQ GLY A 2  ? UNP Q2FZ58 ? ? 'expression tag' -18 2  
1 8VIQ SER A 3  ? UNP Q2FZ58 ? ? 'expression tag' -17 3  
1 8VIQ SER A 4  ? UNP Q2FZ58 ? ? 'expression tag' -16 4  
1 8VIQ HIS A 5  ? UNP Q2FZ58 ? ? 'expression tag' -15 5  
1 8VIQ HIS A 6  ? UNP Q2FZ58 ? ? 'expression tag' -14 6  
1 8VIQ HIS A 7  ? UNP Q2FZ58 ? ? 'expression tag' -13 7  
1 8VIQ HIS A 8  ? UNP Q2FZ58 ? ? 'expression tag' -12 8  
1 8VIQ HIS A 9  ? UNP Q2FZ58 ? ? 'expression tag' -11 9  
1 8VIQ HIS A 10 ? UNP Q2FZ58 ? ? 'expression tag' -10 10 
1 8VIQ SER A 11 ? UNP Q2FZ58 ? ? 'expression tag' -9  11 
1 8VIQ SER A 12 ? UNP Q2FZ58 ? ? 'expression tag' -8  12 
1 8VIQ GLY A 13 ? UNP Q2FZ58 ? ? 'expression tag' -7  13 
1 8VIQ LEU A 14 ? UNP Q2FZ58 ? ? 'expression tag' -6  14 
1 8VIQ VAL A 15 ? UNP Q2FZ58 ? ? 'expression tag' -5  15 
1 8VIQ PRO A 16 ? UNP Q2FZ58 ? ? 'expression tag' -4  16 
1 8VIQ ARG A 17 ? UNP Q2FZ58 ? ? 'expression tag' -3  17 
1 8VIQ GLY A 18 ? UNP Q2FZ58 ? ? 'expression tag' -2  18 
1 8VIQ SER A 19 ? UNP Q2FZ58 ? ? 'expression tag' -1  19 
1 8VIQ 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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 27  ? ASN A 44  ? GLY A 7   ASN A 24  1 ? 18 
HELX_P HELX_P2  AA2 ASN A 44  ? LEU A 51  ? ASN A 24  LEU A 31  1 ? 8  
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 ? ? ? ? ? ? ? 2.174 ? ? 
metalc2  metalc ? ? A ASP 58 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASP 38  A MG  302 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc3  metalc ? ? A ASP 58 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 38  A MG  303 1_555 ? ? ? ? ? ? ? 2.593 ? ? 
metalc4  metalc ? ? A ASP 60 OD1 ? ? ? 1_555 C MG  . MG ? ? A ASP 40  A MG  302 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc5  metalc ? ? A ASP 60 OD2 ? ? ? 1_555 D MG  . MG ? ? A ASP 40  A MG  303 1_555 ? ? ? ? ? ? ? 2.476 ? ? 
metalc6  metalc ? ? B ANP .  O2B ? ? ? 1_555 C MG  . MG ? ? A ANP 301 A MG  302 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc7  metalc ? ? B ANP .  O1A ? ? ? 1_555 C MG  . MG ? ? A ANP 301 A MG  302 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc8  metalc ? ? B ANP .  O2B ? ? ? 1_555 D MG  . MG ? ? A ANP 301 A MG  303 1_555 ? ? ? ? ? ? ? 2.583 ? ? 
metalc9  metalc ? ? C MG  .  MG  ? ? ? 1_555 E HOH . O  ? ? A MG  302 A HOH 409 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc10 metalc ? ? D MG  .  MG  ? ? ? 1_555 E HOH . O  ? ? A MG  303 A HOH 451 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc11 metalc ? ? D MG  .  MG  ? ? ? 1_555 E HOH . O  ? ? A MG  303 A HOH 545 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc12 metalc ? ? D MG  .  MG  ? ? ? 1_555 E HOH . O  ? ? A MG  303 A HOH 574 1_555 ? ? ? ? ? ? ? 2.859 ? ? 
# 
_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 84.1  ? 
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 85.9  ? 
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 87.7  ? 
4  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 176.4 ? 
5  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 99.3  ? 
6  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 95.2  ? 
7  OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 86.4  ? 
8  OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 170.5 ? 
9  OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 92.3  ? 
10 O2B ? B ANP .  ? A ANP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O1A ? B ANP .  ? A ANP 301 ? 1_555 90.2  ? 
11 OD1 ? A ASN 52 ? A ASN 32  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? E HOH .  ? A HOH 409 ? 1_555 88.3  ? 
12 OD1 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? E HOH .  ? A HOH 409 ? 1_555 88.3  ? 
13 OD1 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? E HOH .  ? A HOH 409 ? 1_555 173.3 ? 
14 O2B ? B ANP .  ? A ANP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? E HOH .  ? A HOH 409 ? 1_555 90.7  ? 
15 O1A ? B ANP .  ? A ANP 301 ? 1_555 MG ? C MG . ? A MG 302 ? 1_555 O   ? E HOH .  ? A HOH 409 ? 1_555 90.8  ? 
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 92.6  ? 
17 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 75.2  ? 
18 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O2B ? B ANP .  ? A ANP 301 ? 1_555 86.4  ? 
19 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 451 ? 1_555 163.2 ? 
20 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 451 ? 1_555 85.4  ? 
21 O2B ? B ANP .  ? A ANP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 451 ? 1_555 88.0  ? 
22 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 545 ? 1_555 97.6  ? 
23 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 545 ? 1_555 163.9 ? 
24 O2B ? B ANP .  ? A ANP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 545 ? 1_555 108.2 ? 
25 O   ? E HOH .  ? A HOH 451 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 545 ? 1_555 88.3  ? 
26 OD2 ? A ASP 58 ? A ASP 38  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 574 ? 1_555 85.7  ? 
27 OD2 ? A ASP 60 ? A ASP 40  ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 574 ? 1_555 81.5  ? 
28 O2B ? B ANP .  ? A ANP 301 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 574 ? 1_555 157.0 ? 
29 O   ? E HOH .  ? A HOH 451 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 574 ? 1_555 110.3 ? 
30 O   ? E HOH .  ? A HOH 545 ? 1_555 MG ? D MG . ? A MG 303 ? 1_555 O   ? E HOH .  ? A HOH 574 ? 1_555 86.8  ? 
# 
_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       -3.78 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   2 
_struct_sheet.details          ? 
# 
_struct_sheet_order.sheet_id     AA1 
_struct_sheet_order.range_id_1   1 
_struct_sheet_order.range_id_2   2 
_struct_sheet_order.offset       ? 
_struct_sheet_order.sense        anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 25  ? ASN A 26  ? ILE A 5   ASN A 6   
AA1 2 GLU A 123 ? ILE A 124 ? GLU A 103 ILE A 104 
# 
_pdbx_struct_sheet_hbond.sheet_id                AA1 
_pdbx_struct_sheet_hbond.range_id_1              1 
_pdbx_struct_sheet_hbond.range_id_2              2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id   N 
_pdbx_struct_sheet_hbond.range_1_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_1_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_1_label_seq_id    25 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id    N 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id     5 
_pdbx_struct_sheet_hbond.range_2_label_atom_id   O 
_pdbx_struct_sheet_hbond.range_2_label_comp_id   ILE 
_pdbx_struct_sheet_hbond.range_2_label_asym_id   A 
_pdbx_struct_sheet_hbond.range_2_label_seq_id    124 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code    ? 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id    O 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id    ILE 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id    A 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id     104 
# 
_pdbx_entry_details.entry_id                   8VIQ 
_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             -150.33 
_pdbx_validate_torsion.psi             74.53 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 628 ? 5.90 . 
2 1 O ? A HOH 629 ? 7.76 . 
# 
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 SER -1  ? A SER 19  
20 1 Y 1 A HIS 0   ? A HIS 20  
21 1 Y 1 A VAL 211 ? A VAL 231 
22 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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MG  MG     MG N N 298 
PHE N      N  N N 299 
PHE CA     C  N S 300 
PHE C      C  N N 301 
PHE O      O  N N 302 
PHE CB     C  N N 303 
PHE CG     C  Y N 304 
PHE CD1    C  Y N 305 
PHE CD2    C  Y N 306 
PHE CE1    C  Y N 307 
PHE CE2    C  Y N 308 
PHE CZ     C  Y N 309 
PHE OXT    O  N N 310 
PHE H      H  N N 311 
PHE H2     H  N N 312 
PHE HA     H  N N 313 
PHE HB2    H  N N 314 
PHE HB3    H  N N 315 
PHE HD1    H  N N 316 
PHE HD2    H  N N 317 
PHE HE1    H  N N 318 
PHE HE2    H  N N 319 
PHE HZ     H  N N 320 
PHE HXT    H  N N 321 
PRO N      N  N N 322 
PRO CA     C  N S 323 
PRO C      C  N N 324 
PRO O      O  N N 325 
PRO CB     C  N N 326 
PRO CG     C  N N 327 
PRO CD     C  N N 328 
PRO OXT    O  N N 329 
PRO H      H  N N 330 
PRO HA     H  N N 331 
PRO HB2    H  N N 332 
PRO HB3    H  N N 333 
PRO HG2    H  N N 334 
PRO HG3    H  N N 335 
PRO HD2    H  N N 336 
PRO HD3    H  N N 337 
PRO HXT    H  N N 338 
SER N      N  N N 339 
SER CA     C  N S 340 
SER C      C  N N 341 
SER O      O  N N 342 
SER CB     C  N N 343 
SER OG     O  N N 344 
SER OXT    O  N N 345 
SER H      H  N N 346 
SER H2     H  N N 347 
SER HA     H  N N 348 
SER HB2    H  N N 349 
SER HB3    H  N N 350 
SER HG     H  N N 351 
SER HXT    H  N N 352 
THR N      N  N N 353 
THR CA     C  N S 354 
THR C      C  N N 355 
THR O      O  N N 356 
THR CB     C  N R 357 
THR OG1    O  N N 358 
THR CG2    C  N N 359 
THR OXT    O  N N 360 
THR H      H  N N 361 
THR H2     H  N N 362 
THR HA     H  N N 363 
THR HB     H  N N 364 
THR HG1    H  N N 365 
THR HG21   H  N N 366 
THR HG22   H  N N 367 
THR HG23   H  N N 368 
THR HXT    H  N N 369 
TYR N      N  N N 370 
TYR CA     C  N S 371 
TYR C      C  N N 372 
TYR O      O  N N 373 
TYR CB     C  N N 374 
TYR CG     C  Y N 375 
TYR CD1    C  Y N 376 
TYR CD2    C  Y N 377 
TYR CE1    C  Y N 378 
TYR CE2    C  Y N 379 
TYR CZ     C  Y N 380 
TYR OH     O  N N 381 
TYR OXT    O  N N 382 
TYR H      H  N N 383 
TYR H2     H  N N 384 
TYR HA     H  N N 385 
TYR HB2    H  N N 386 
TYR HB3    H  N N 387 
TYR HD1    H  N N 388 
TYR HD2    H  N N 389 
TYR HE1    H  N N 390 
TYR HE2    H  N N 391 
TYR HH     H  N N 392 
TYR HXT    H  N N 393 
VAL N      N  N N 394 
VAL CA     C  N S 395 
VAL C      C  N N 396 
VAL O      O  N N 397 
VAL CB     C  N N 398 
VAL CG1    C  N N 399 
VAL CG2    C  N N 400 
VAL OXT    O  N N 401 
VAL H      H  N N 402 
VAL H2     H  N N 403 
VAL HA     H  N N 404 
VAL HB     H  N N 405 
VAL HG11   H  N N 406 
VAL HG12   H  N N 407 
VAL HG13   H  N N 408 
VAL HG21   H  N N 409 
VAL HG22   H  N N 410 
VAL HG23   H  N N 411 
VAL HXT    H  N N 412 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TYR N     CA     sing N N 356 
TYR N     H      sing N N 357 
TYR N     H2     sing N N 358 
TYR CA    C      sing N N 359 
TYR CA    CB     sing N N 360 
TYR CA    HA     sing N N 361 
TYR C     O      doub N N 362 
TYR C     OXT    sing N N 363 
TYR CB    CG     sing N N 364 
TYR CB    HB2    sing N N 365 
TYR CB    HB3    sing N N 366 
TYR CG    CD1    doub Y N 367 
TYR CG    CD2    sing Y N 368 
TYR CD1   CE1    sing Y N 369 
TYR CD1   HD1    sing N N 370 
TYR CD2   CE2    doub Y N 371 
TYR CD2   HD2    sing N N 372 
TYR CE1   CZ     doub Y N 373 
TYR CE1   HE1    sing N N 374 
TYR CE2   CZ     sing Y N 375 
TYR CE2   HE2    sing N N 376 
TYR CZ    OH     sing N N 377 
TYR OH    HH     sing N N 378 
TYR OXT   HXT    sing N N 379 
VAL N     CA     sing N N 380 
VAL N     H      sing N N 381 
VAL N     H2     sing N N 382 
VAL CA    C      sing N N 383 
VAL CA    CB     sing N N 384 
VAL CA    HA     sing N N 385 
VAL C     O      doub N N 386 
VAL C     OXT    sing N N 387 
VAL CB    CG1    sing N N 388 
VAL CB    CG2    sing N N 389 
VAL CB    HB     sing N N 390 
VAL CG1   HG11   sing N N 391 
VAL CG1   HG12   sing N N 392 
VAL CG1   HG13   sing N N 393 
VAL CG2   HG21   sing N N 394 
VAL CG2   HG22   sing N N 395 
VAL CG2   HG23   sing N N 396 
VAL OXT   HXT    sing N N 397 
# 
_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                    8VIQ 
_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]   0.023404 
_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]   0.017720 
_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]   0.012224 
_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     . MET A 1 21  ? -21.427 2.642   -30.343 1.00 34.56 ? 1   MET A N     1 
ATOM   2    C  CA    . MET A 1 21  ? -21.489 1.395   -29.533 1.00 33.57 ? 1   MET A CA    1 
ATOM   3    C  C     . MET A 1 21  ? -20.208 0.581   -29.652 1.00 28.00 ? 1   MET A C     1 
ATOM   4    O  O     . MET A 1 21  ? -19.420 0.754   -30.576 1.00 28.73 ? 1   MET A O     1 
ATOM   5    C  CB    . MET A 1 21  ? -22.720 0.557   -29.913 1.00 37.70 ? 1   MET A CB    1 
ATOM   6    C  CG    . MET A 1 21  ? -22.573 -0.408  -31.086 1.00 41.61 ? 1   MET A CG    1 
ATOM   7    S  SD    . MET A 1 21  ? -23.559 -1.887  -30.730 1.00 44.67 ? 1   MET A SD    1 
ATOM   8    C  CE    . MET A 1 21  ? -23.037 -2.966  -32.057 1.00 45.34 ? 1   MET A CE    1 
ATOM   9    N  N     . ILE A 1 22  ? -20.014 -0.311  -28.693 1.00 22.19 ? 2   ILE A N     1 
ATOM   10   C  CA    . ILE A 1 22  ? -18.831 -1.154  -28.614 1.00 18.58 ? 2   ILE A CA    1 
ATOM   11   C  C     . ILE A 1 22  ? -19.311 -2.587  -28.775 1.00 17.66 ? 2   ILE A C     1 
ATOM   12   O  O     . ILE A 1 22  ? -19.940 -3.137  -27.865 1.00 17.97 ? 2   ILE A O     1 
ATOM   13   C  CB    . ILE A 1 22  ? -18.100 -0.968  -27.274 1.00 17.60 ? 2   ILE A CB    1 
ATOM   14   C  CG1   . ILE A 1 22  ? -17.564 0.461   -27.143 1.00 17.93 ? 2   ILE A CG1   1 
ATOM   15   C  CG2   . ILE A 1 22  ? -17.005 -2.011  -27.121 1.00 16.99 ? 2   ILE A CG2   1 
ATOM   16   C  CD1   . ILE A 1 22  ? -16.445 0.814   -28.118 1.00 18.12 ? 2   ILE A CD1   1 
ATOM   17   N  N     . SER A 1 23  ? -19.038 -3.197  -29.925 1.00 17.78 ? 3   SER A N     1 
ATOM   18   C  CA    A SER A 1 23  ? -19.428 -4.589  -30.103 0.50 18.31 ? 3   SER A CA    1 
ATOM   19   C  CA    B SER A 1 23  ? -19.411 -4.590  -30.144 0.50 18.12 ? 3   SER A CA    1 
ATOM   20   C  C     . SER A 1 23  ? -18.329 -5.558  -29.696 1.00 17.81 ? 3   SER A C     1 
ATOM   21   O  O     . SER A 1 23  ? -18.634 -6.690  -29.305 1.00 18.80 ? 3   SER A O     1 
ATOM   22   C  CB    A SER A 1 23  ? -19.854 -4.856  -31.548 0.50 19.92 ? 3   SER A CB    1 
ATOM   23   C  CB    B SER A 1 23  ? -19.679 -4.855  -31.628 0.50 19.41 ? 3   SER A CB    1 
ATOM   24   O  OG    A SER A 1 23  ? -18.744 -4.814  -32.417 0.50 21.47 ? 3   SER A OG    1 
ATOM   25   O  OG    B SER A 1 23  ? -20.569 -3.907  -32.167 0.50 20.88 ? 3   SER A OG    1 
ATOM   26   N  N     . LYS A 1 24  ? -17.072 -5.137  -29.748 1.00 16.24 ? 4   LYS A N     1 
ATOM   27   C  CA    . LYS A 1 24  ? -15.963 -5.997  -29.374 1.00 16.58 ? 4   LYS A CA    1 
ATOM   28   C  C     . LYS A 1 24  ? -14.922 -5.177  -28.628 1.00 15.11 ? 4   LYS A C     1 
ATOM   29   O  O     . LYS A 1 24  ? -14.726 -3.984  -28.902 1.00 15.09 ? 4   LYS A O     1 
ATOM   30   C  CB    . LYS A 1 24  ? -15.319 -6.654  -30.599 1.00 19.52 ? 4   LYS A CB    1 
ATOM   31   C  CG    . LYS A 1 24  ? -16.234 -7.643  -31.339 1.00 22.63 ? 4   LYS A CG    1 
ATOM   32   C  CD    . LYS A 1 24  ? -15.500 -8.349  -32.459 1.00 25.01 ? 4   LYS A CD    1 
ATOM   33   N  N     . ILE A 1 25  ? -14.257 -5.844  -27.684 1.00 14.01 ? 5   ILE A N     1 
ATOM   34   C  CA    . ILE A 1 25  ? -13.233 -5.245  -26.834 1.00 13.04 ? 5   ILE A CA    1 
ATOM   35   C  C     . ILE A 1 25  ? -11.910 -5.911  -27.181 1.00 12.88 ? 5   ILE A C     1 
ATOM   36   O  O     . ILE A 1 25  ? -11.714 -7.098  -26.891 1.00 13.21 ? 5   ILE A O     1 
ATOM   37   C  CB    . ILE A 1 25  ? -13.554 -5.445  -25.346 1.00 12.95 ? 5   ILE A CB    1 
ATOM   38   C  CG1   . ILE A 1 25  ? -14.913 -4.837  -24.989 1.00 13.77 ? 5   ILE A CG1   1 
ATOM   39   C  CG2   . ILE A 1 25  ? -12.444 -4.864  -24.485 1.00 13.15 ? 5   ILE A CG2   1 
ATOM   40   C  CD1   . ILE A 1 25  ? -15.394 -5.177  -23.582 1.00 14.26 ? 5   ILE A CD1   1 
ATOM   41   N  N     . ASN A 1 26  ? -11.005 -5.157  -27.811 1.00 12.68 ? 6   ASN A N     1 
ATOM   42   C  CA    . ASN A 1 26  ? -9.671  -5.640  -28.127 1.00 12.34 ? 6   ASN A CA    1 
ATOM   43   C  C     . ASN A 1 26  ? -8.718  -5.369  -26.959 1.00 12.39 ? 6   ASN A C     1 
ATOM   44   O  O     . ASN A 1 26  ? -9.102  -4.877  -25.897 1.00 12.27 ? 6   ASN A O     1 
ATOM   45   C  CB    . ASN A 1 26  ? -9.166  -5.096  -29.469 1.00 13.10 ? 6   ASN A CB    1 
ATOM   46   C  CG    . ASN A 1 26  ? -8.885  -3.602  -29.466 1.00 13.65 ? 6   ASN A CG    1 
ATOM   47   O  OD1   . ASN A 1 26  ? -8.548  -3.003  -28.446 1.00 13.26 ? 6   ASN A OD1   1 
ATOM   48   N  ND2   . ASN A 1 26  ? -9.012  -2.988  -30.644 1.00 15.75 ? 6   ASN A ND2   1 
ATOM   49   N  N     . GLY A 1 27  ? -7.452  -5.729  -27.139 1.00 12.24 ? 7   GLY A N     1 
ATOM   50   C  CA    . GLY A 1 27  ? -6.507  -5.606  -26.045 1.00 12.48 ? 7   GLY A CA    1 
ATOM   51   C  C     . GLY A 1 27  ? -6.260  -4.179  -25.601 1.00 11.74 ? 7   GLY A C     1 
ATOM   52   O  O     . GLY A 1 27  ? -6.025  -3.933  -24.417 1.00 12.27 ? 7   GLY A O     1 
ATOM   53   N  N     . LYS A 1 28  ? -6.280  -3.219  -26.533 1.00 11.89 ? 8   LYS A N     1 
ATOM   54   C  CA    . LYS A 1 28  ? -6.075  -1.828  -26.131 1.00 11.67 ? 8   LYS A CA    1 
ATOM   55   C  C     . LYS A 1 28  ? -7.292  -1.264  -25.408 1.00 11.45 ? 8   LYS A C     1 
ATOM   56   O  O     . LYS A 1 28  ? -7.143  -0.493  -24.452 1.00 11.81 ? 8   LYS A O     1 
ATOM   57   C  CB    . LYS A 1 28  ? -5.669  -0.954  -27.319 1.00 12.08 ? 8   LYS A CB    1 
ATOM   58   C  CG    . LYS A 1 28  ? -5.331  0.494   -26.945 1.00 12.76 ? 8   LYS A CG    1 
ATOM   59   C  CD    . LYS A 1 28  ? -4.389  0.605   -25.734 1.00 13.47 ? 8   LYS A CD    1 
ATOM   60   C  CE    . LYS A 1 28  ? -3.733  1.982   -25.604 1.00 14.05 ? 8   LYS A CE    1 
ATOM   61   N  NZ    . LYS A 1 28  ? -4.674  3.097   -25.392 1.00 14.03 ? 8   LYS A NZ    1 
ATOM   62   N  N     . LEU A 1 29  ? -8.503  -1.636  -25.822 1.00 11.19 ? 9   LEU A N     1 
ATOM   63   C  CA    . LEU A 1 29  ? -9.674  -1.193  -25.077 1.00 11.36 ? 9   LEU A CA    1 
ATOM   64   C  C     . LEU A 1 29  ? -9.681  -1.796  -23.670 1.00 11.44 ? 9   LEU A C     1 
ATOM   65   O  O     . LEU A 1 29  ? -10.001 -1.102  -22.700 1.00 11.47 ? 9   LEU A O     1 
ATOM   66   C  CB    . LEU A 1 29  ? -10.962 -1.497  -25.840 1.00 11.48 ? 9   LEU A CB    1 
ATOM   67   C  CG    . LEU A 1 29  ? -12.241 -0.913  -25.244 1.00 12.13 ? 9   LEU A CG    1 
ATOM   68   C  CD1   . LEU A 1 29  ? -12.133 0.551   -24.918 1.00 13.16 ? 9   LEU A CD1   1 
ATOM   69   C  CD2   . LEU A 1 29  ? -13.383 -1.169  -26.185 1.00 12.96 ? 9   LEU A CD2   1 
ATOM   70   N  N     . PHE A 1 30  ? -9.299  -3.069  -23.533 1.00 11.10 ? 10  PHE A N     1 
ATOM   71   C  CA    . PHE A 1 30  ? -9.184  -3.654  -22.196 1.00 11.20 ? 10  PHE A CA    1 
ATOM   72   C  C     . PHE A 1 30  ? -8.117  -2.934  -21.383 1.00 10.95 ? 10  PHE A C     1 
ATOM   73   O  O     . PHE A 1 30  ? -8.324  -2.649  -20.197 1.00 11.10 ? 10  PHE A O     1 
ATOM   74   C  CB    . PHE A 1 30  ? -8.926  -5.157  -22.288 1.00 11.28 ? 10  PHE A CB    1 
ATOM   75   C  CG    . PHE A 1 30  ? -8.992  -5.900  -20.958 1.00 12.21 ? 10  PHE A CG    1 
ATOM   76   C  CD1   . PHE A 1 30  ? -9.922  -5.560  -19.981 1.00 12.86 ? 10  PHE A CD1   1 
ATOM   77   C  CD2   . PHE A 1 30  ? -8.145  -6.978  -20.711 1.00 12.13 ? 10  PHE A CD2   1 
ATOM   78   C  CE1   . PHE A 1 30  ? -9.979  -6.269  -18.782 1.00 13.34 ? 10  PHE A CE1   1 
ATOM   79   C  CE2   . PHE A 1 30  ? -8.207  -7.692  -19.521 1.00 12.51 ? 10  PHE A CE2   1 
ATOM   80   C  CZ    . PHE A 1 30  ? -9.122  -7.335  -18.561 1.00 13.26 ? 10  PHE A CZ    1 
ATOM   81   N  N     . ALA A 1 31  ? -6.967  -2.627  -21.990 1.00 10.92 ? 11  ALA A N     1 
ATOM   82   C  CA    . ALA A 1 31  ? -5.952  -1.845  -21.292 1.00 11.20 ? 11  ALA A CA    1 
ATOM   83   C  C     . ALA A 1 31  ? -6.512  -0.511  -20.814 1.00 11.12 ? 11  ALA A C     1 
ATOM   84   O  O     . ALA A 1 31  ? -6.256  -0.097  -19.683 1.00 11.50 ? 11  ALA A O     1 
ATOM   85   C  CB    . ALA A 1 31  ? -4.728  -1.639  -22.182 1.00 11.88 ? 11  ALA A CB    1 
ATOM   86   N  N     . ASP A 1 32  ? -7.285  0.177   -21.658 1.00 11.60 ? 12  ASP A N     1 
ATOM   87   C  CA    . ASP A 1 32  ? -7.877  1.443   -21.244 1.00 11.56 ? 12  ASP A CA    1 
ATOM   88   C  C     . ASP A 1 32  ? -8.828  1.242   -20.063 1.00 10.86 ? 12  ASP A C     1 
ATOM   89   O  O     . ASP A 1 32  ? -8.874  2.067   -19.142 1.00 11.33 ? 12  ASP A O     1 
ATOM   90   C  CB    . ASP A 1 32  ? -8.657  2.082   -22.399 1.00 12.18 ? 12  ASP A CB    1 
ATOM   91   C  CG    . ASP A 1 32  ? -7.784  2.644   -23.504 1.00 12.85 ? 12  ASP A CG    1 
ATOM   92   O  OD1   . ASP A 1 32  ? -6.553  2.712   -23.357 1.00 13.67 ? 12  ASP A OD1   1 
ATOM   93   O  OD2   . ASP A 1 32  ? -8.366  3.038   -24.538 1.00 13.30 ? 12  ASP A OD2   1 
ATOM   94   N  N     . MET A 1 33  ? -9.630  0.171   -20.094 1.00 10.86 ? 13  MET A N     1 
ATOM   95   C  CA    . MET A 1 33  ? -10.508 -0.136  -18.966 1.00 10.90 ? 13  MET A CA    1 
ATOM   96   C  C     . MET A 1 33  ? -9.701  -0.295  -17.685 1.00 10.83 ? 13  MET A C     1 
ATOM   97   O  O     . MET A 1 33  ? -10.074 0.232   -16.632 1.00 11.14 ? 13  MET A O     1 
ATOM   98   C  CB    . MET A 1 33  ? -11.298 -1.407  -19.273 1.00 11.54 ? 13  MET A CB    1 
ATOM   99   C  CG    . MET A 1 33  ? -12.308 -1.247  -20.405 1.00 11.79 ? 13  MET A CG    1 
ATOM   100  S  SD    . MET A 1 33  ? -12.924 -2.794  -21.099 1.00 12.38 ? 13  MET A SD    1 
ATOM   101  C  CE    . MET A 1 33  ? -13.927 -3.399  -19.746 1.00 14.27 ? 13  MET A CE    1 
ATOM   102  N  N     . ILE A 1 34  ? -8.591  -1.019  -17.765 1.00 10.86 ? 14  ILE A N     1 
ATOM   103  C  CA    . ILE A 1 34  ? -7.723  -1.226  -16.610 1.00 10.96 ? 14  ILE A CA    1 
ATOM   104  C  C     . ILE A 1 34  ? -7.161  0.101   -16.116 1.00 11.23 ? 14  ILE A C     1 
ATOM   105  O  O     . ILE A 1 34  ? -7.146  0.380   -14.907 1.00 11.65 ? 14  ILE A O     1 
ATOM   106  C  CB    . ILE A 1 34  ? -6.613  -2.229  -16.983 1.00 11.39 ? 14  ILE A CB    1 
ATOM   107  C  CG1   . ILE A 1 34  ? -7.221  -3.622  -17.136 1.00 11.38 ? 14  ILE A CG1   1 
ATOM   108  C  CG2   . ILE A 1 34  ? -5.463  -2.201  -15.978 1.00 12.11 ? 14  ILE A CG2   1 
ATOM   109  C  CD1   . ILE A 1 34  ? -6.396  -4.558  -18.010 1.00 11.42 ? 14  ILE A CD1   1 
ATOM   110  N  N     . ILE A 1 35  ? -6.662  0.925   -17.043 1.00 11.41 ? 15  ILE A N     1 
ATOM   111  C  CA    . ILE A 1 35  ? -6.020  2.182   -16.675 1.00 11.96 ? 15  ILE A CA    1 
ATOM   112  C  C     . ILE A 1 35  ? -7.028  3.139   -16.047 1.00 11.37 ? 15  ILE A C     1 
ATOM   113  O  O     . ILE A 1 35  ? -6.758  3.757   -15.006 1.00 12.21 ? 15  ILE A O     1 
ATOM   114  C  CB    . ILE A 1 35  ? -5.316  2.790   -17.905 1.00 13.19 ? 15  ILE A CB    1 
ATOM   115  C  CG1   . ILE A 1 35  ? -4.136  1.901   -18.321 1.00 14.57 ? 15  ILE A CG1   1 
ATOM   116  C  CG2   . ILE A 1 35  ? -4.880  4.215   -17.616 1.00 14.87 ? 15  ILE A CG2   1 
ATOM   117  C  CD1   . ILE A 1 35  ? -3.654  2.111   -19.743 1.00 15.59 ? 15  ILE A CD1   1 
ATOM   118  N  N     . GLN A 1 36  ? -8.195  3.289   -16.677 1.00 11.32 ? 16  GLN A N     1 
ATOM   119  C  CA    . GLN A 1 36  ? -9.199  4.209   -16.144 1.00 11.98 ? 16  GLN A CA    1 
ATOM   120  C  C     . GLN A 1 36  ? -9.836  3.664   -14.869 1.00 11.58 ? 16  GLN A C     1 
ATOM   121  O  O     . GLN A 1 36  ? -10.142 4.432   -13.944 1.00 12.08 ? 16  GLN A O     1 
ATOM   122  C  CB    . GLN A 1 36  ? -10.264 4.524   -17.198 1.00 12.81 ? 16  GLN A CB    1 
ATOM   123  C  CG    . GLN A 1 36  ? -9.723  5.121   -18.507 1.00 13.70 ? 16  GLN A CG    1 
ATOM   124  C  CD    . GLN A 1 36  ? -8.709  6.221   -18.309 1.00 15.43 ? 16  GLN A CD    1 
ATOM   125  O  OE1   . GLN A 1 36  ? -8.904  7.112   -17.495 1.00 15.56 ? 16  GLN A OE1   1 
ATOM   126  N  NE2   . GLN A 1 36  ? -7.638  6.192   -19.101 1.00 17.49 ? 16  GLN A NE2   1 
ATOM   127  N  N     . GLY A 1 37  ? -10.049 2.343   -14.801 1.00 11.31 ? 17  GLY A N     1 
ATOM   128  C  CA    . GLY A 1 37  ? -10.509 1.739   -13.556 1.00 11.45 ? 17  GLY A CA    1 
ATOM   129  C  C     . GLY A 1 37  ? -9.532  1.955   -12.419 1.00 11.21 ? 17  GLY A C     1 
ATOM   130  O  O     . GLY A 1 37  ? -9.925  2.293   -11.294 1.00 11.81 ? 17  GLY A O     1 
ATOM   131  N  N     . ALA A 1 38  ? -8.240  1.791   -12.704 1.00 11.16 ? 18  ALA A N     1 
ATOM   132  C  CA    . ALA A 1 38  ? -7.217  2.036   -11.696 1.00 11.75 ? 18  ALA A CA    1 
ATOM   133  C  C     . ALA A 1 38  ? -7.215  3.494   -11.259 1.00 11.81 ? 18  ALA A C     1 
ATOM   134  O  O     . ALA A 1 38  ? -7.119  3.789   -10.066 1.00 12.60 ? 18  ALA A O     1 
ATOM   135  C  CB    . ALA A 1 38  ? -5.846  1.638   -12.232 1.00 12.48 ? 18  ALA A CB    1 
ATOM   136  N  N     . GLN A 1 39  ? -7.324  4.426   -12.211 1.00 12.13 ? 19  GLN A N     1 
ATOM   137  C  CA    . GLN A 1 39  ? -7.316  5.843   -11.846 1.00 12.47 ? 19  GLN A CA    1 
ATOM   138  C  C     . GLN A 1 39  ? -8.530  6.203   -10.998 1.00 12.91 ? 19  GLN A C     1 
ATOM   139  O  O     . GLN A 1 39  ? -8.426  6.981   -10.040 1.00 13.33 ? 19  GLN A O     1 
ATOM   140  C  CB    . GLN A 1 39  ? -7.263  6.741   -13.087 1.00 13.14 ? 19  GLN A CB    1 
ATOM   141  C  CG    . GLN A 1 39  ? -7.047  8.215   -12.733 1.00 15.64 ? 19  GLN A CG    1 
ATOM   142  C  CD    . GLN A 1 39  ? -5.720  8.450   -12.028 1.00 18.14 ? 19  GLN A CD    1 
ATOM   143  O  OE1   . GLN A 1 39  ? -4.662  8.154   -12.578 1.00 20.23 ? 19  GLN A OE1   1 
ATOM   144  N  NE2   . GLN A 1 39  ? -5.772  8.966   -10.806 1.00 18.85 ? 19  GLN A NE2   1 
ATOM   145  N  N     . ASN A 1 40  ? -9.696  5.664   -11.342 1.00 12.30 ? 20  ASN A N     1 
ATOM   146  C  CA    . ASN A 1 40  ? -10.891 5.988   -10.578 1.00 12.91 ? 20  ASN A CA    1 
ATOM   147  C  C     . ASN A 1 40  ? -10.796 5.428   -9.167  1.00 13.24 ? 20  ASN A C     1 
ATOM   148  O  O     . ASN A 1 40  ? -11.209 6.083   -8.208  1.00 14.47 ? 20  ASN A O     1 
ATOM   149  C  CB    . ASN A 1 40  ? -12.135 5.482   -11.292 1.00 13.76 ? 20  ASN A CB    1 
ATOM   150  C  CG    . ASN A 1 40  ? -13.382 6.164   -10.799 1.00 15.43 ? 20  ASN A CG    1 
ATOM   151  O  OD1   . ASN A 1 40  ? -13.449 7.393   -10.755 1.00 17.58 ? 20  ASN A OD1   1 
ATOM   152  N  ND2   . ASN A 1 40  ? -14.375 5.384   -10.419 1.00 15.00 ? 20  ASN A ND2   1 
ATOM   153  N  N     . LEU A 1 41  ? -10.255 4.220   -9.021  1.00 12.49 ? 21  LEU A N     1 
ATOM   154  C  CA    . LEU A 1 41  ? -10.017 3.664   -7.694  1.00 12.51 ? 21  LEU A CA    1 
ATOM   155  C  C     . LEU A 1 41  ? -9.017  4.513   -6.914  1.00 13.20 ? 21  LEU A C     1 
ATOM   156  O  O     . LEU A 1 41  ? -9.239  4.817   -5.734  1.00 14.30 ? 21  LEU A O     1 
ATOM   157  C  CB    . LEU A 1 41  ? -9.544  2.215   -7.816  1.00 12.41 ? 21  LEU A CB    1 
ATOM   158  C  CG    . LEU A 1 41  ? -9.147  1.524   -6.509  1.00 12.73 ? 21  LEU A CG    1 
ATOM   159  C  CD1   . LEU A 1 41  ? -10.310 1.467   -5.528  1.00 13.34 ? 21  LEU A CD1   1 
ATOM   160  C  CD2   . LEU A 1 41  ? -8.629  0.126   -6.802  1.00 13.19 ? 21  LEU A CD2   1 
ATOM   161  N  N     . SER A 1 42  ? -7.917  4.922   -7.559  1.00 13.83 ? 22  SER A N     1 
ATOM   162  C  CA    A SER A 1 42  ? -6.946  5.771   -6.881  0.50 14.59 ? 22  SER A CA    1 
ATOM   163  C  CA    B SER A 1 42  ? -6.936  5.785   -6.904  0.50 14.88 ? 22  SER A CA    1 
ATOM   164  C  C     . SER A 1 42  ? -7.596  7.053   -6.379  1.00 14.87 ? 22  SER A C     1 
ATOM   165  O  O     . SER A 1 42  ? -7.345  7.479   -5.243  1.00 16.03 ? 22  SER A O     1 
ATOM   166  C  CB    A SER A 1 42  ? -5.795  6.085   -7.830  0.50 14.94 ? 22  SER A CB    1 
ATOM   167  C  CB    B SER A 1 42  ? -5.835  6.157   -7.901  0.50 15.81 ? 22  SER A CB    1 
ATOM   168  O  OG    A SER A 1 42  ? -4.811  6.851   -7.166  0.50 15.33 ? 22  SER A OG    1 
ATOM   169  O  OG    B SER A 1 42  ? -5.012  5.058   -8.241  0.50 16.86 ? 22  SER A OG    1 
ATOM   170  N  N     . ASN A 1 43  ? -8.433  7.685   -7.212  1.00 15.44 ? 23  ASN A N     1 
ATOM   171  C  CA    . ASN A 1 43  ? -9.094  8.922   -6.807  1.00 16.19 ? 23  ASN A CA    1 
ATOM   172  C  C     . ASN A 1 43  ? -9.986  8.704   -5.593  1.00 16.73 ? 23  ASN A C     1 
ATOM   173  O  O     . ASN A 1 43  ? -10.199 9.632   -4.807  1.00 18.58 ? 23  ASN A O     1 
ATOM   174  C  CB    . ASN A 1 43  ? -9.947  9.479   -7.954  1.00 17.38 ? 23  ASN A CB    1 
ATOM   175  C  CG    . ASN A 1 43  ? -9.123  10.029  -9.107  1.00 17.47 ? 23  ASN A CG    1 
ATOM   176  O  OD1   . ASN A 1 43  ? -7.896  10.130  -9.034  1.00 18.01 ? 23  ASN A OD1   1 
ATOM   177  N  ND2   . ASN A 1 43  ? -9.802  10.388  -10.182 1.00 18.73 ? 23  ASN A ND2   1 
ATOM   178  N  N     . ASN A 1 44  ? -10.524 7.497   -5.439  1.00 16.08 ? 24  ASN A N     1 
ATOM   179  C  CA    . ASN A 1 44  ? -11.481 7.181   -4.392  1.00 16.18 ? 24  ASN A CA    1 
ATOM   180  C  C     . ASN A 1 44  ? -10.866 6.396   -3.247  1.00 15.70 ? 24  ASN A C     1 
ATOM   181  O  O     . ASN A 1 44  ? -11.593 5.967   -2.344  1.00 16.15 ? 24  ASN A O     1 
ATOM   182  C  CB    . ASN A 1 44  ? -12.645 6.394   -4.990  1.00 17.34 ? 24  ASN A CB    1 
ATOM   183  C  CG    . ASN A 1 44  ? -13.645 7.284   -5.679  1.00 19.05 ? 24  ASN A CG    1 
ATOM   184  O  OD1   . ASN A 1 44  ? -14.490 7.903   -5.030  1.00 21.40 ? 24  ASN A OD1   1 
ATOM   185  N  ND2   . ASN A 1 44  ? -13.555 7.364   -6.998  1.00 18.77 ? 24  ASN A ND2   1 
ATOM   186  N  N     . ALA A 1 45  ? -9.541  6.249   -3.227  1.00 15.32 ? 25  ALA A N     1 
ATOM   187  C  CA    . ALA A 1 45  ? -8.919  5.375   -2.240  1.00 15.53 ? 25  ALA A CA    1 
ATOM   188  C  C     . ALA A 1 45  ? -9.173  5.869   -0.822  1.00 15.73 ? 25  ALA A C     1 
ATOM   189  O  O     . ALA A 1 45  ? -9.441  5.066   0.077   1.00 16.05 ? 25  ALA A O     1 
ATOM   190  C  CB    . ALA A 1 45  ? -7.425  5.235   -2.521  1.00 16.60 ? 25  ALA A CB    1 
ATOM   191  N  N     . ASP A 1 46  ? -9.086  7.183   -0.594  1.00 16.77 ? 26  ASP A N     1 
ATOM   192  C  CA    . ASP A 1 46  ? -9.335  7.706   0.743   1.00 18.04 ? 26  ASP A CA    1 
ATOM   193  C  C     . ASP A 1 46  ? -10.784 7.476   1.156   1.00 16.90 ? 26  ASP A C     1 
ATOM   194  O  O     . ASP A 1 46  ? -11.058 7.154   2.318   1.00 17.71 ? 26  ASP A O     1 
ATOM   195  C  CB    . ASP A 1 46  ? -9.006  9.201   0.786   1.00 21.01 ? 26  ASP A CB    1 
ATOM   196  C  CG    . ASP A 1 46  ? -7.509  9.486   0.724   1.00 24.66 ? 26  ASP A CG    1 
ATOM   197  O  OD1   . ASP A 1 46  ? -6.689  8.573   0.972   1.00 26.41 ? 26  ASP A OD1   1 
ATOM   198  O  OD2   . ASP A 1 46  ? -7.155  10.651  0.448   1.00 26.66 ? 26  ASP A OD2   1 
ATOM   199  N  N     . LEU A 1 47  ? -11.731 7.683   0.238   1.00 17.10 ? 27  LEU A N     1 
ATOM   200  C  CA    . LEU A 1 47  ? -13.132 7.404   0.550   1.00 17.03 ? 27  LEU A CA    1 
ATOM   201  C  C     . LEU A 1 47  ? -13.332 5.938   0.925   1.00 16.30 ? 27  LEU A C     1 
ATOM   202  O  O     . LEU A 1 47  ? -14.023 5.626   1.904   1.00 16.62 ? 27  LEU A O     1 
ATOM   203  C  CB    . LEU A 1 47  ? -14.013 7.791   -0.638  1.00 18.96 ? 27  LEU A CB    1 
ATOM   204  C  CG    . LEU A 1 47  ? -15.482 7.372   -0.526  1.00 21.57 ? 27  LEU A CG    1 
ATOM   205  C  CD1   . LEU A 1 47  ? -16.137 7.876   0.754   1.00 23.80 ? 27  LEU A CD1   1 
ATOM   206  C  CD2   . LEU A 1 47  ? -16.255 7.834   -1.749  1.00 22.63 ? 27  LEU A CD2   1 
ATOM   207  N  N     . VAL A 1 48  ? -12.728 5.022   0.165   1.00 15.21 ? 28  VAL A N     1 
ATOM   208  C  CA    . VAL A 1 48  ? -12.878 3.599   0.450   1.00 14.97 ? 28  VAL A CA    1 
ATOM   209  C  C     . VAL A 1 48  ? -12.233 3.253   1.788   1.00 15.47 ? 28  VAL A C     1 
ATOM   210  O  O     . VAL A 1 48  ? -12.787 2.483   2.580   1.00 16.39 ? 28  VAL A O     1 
ATOM   211  C  CB    . VAL A 1 48  ? -12.328 2.772   -0.725  1.00 13.75 ? 28  VAL A CB    1 
ATOM   212  C  CG1   . VAL A 1 48  ? -12.347 1.289   -0.414  1.00 13.39 ? 28  VAL A CG1   1 
ATOM   213  C  CG2   . VAL A 1 48  ? -13.157 3.055   -1.970  1.00 14.23 ? 28  VAL A CG2   1 
ATOM   214  N  N     . ASP A 1 49  ? -11.074 3.850   2.078   1.00 15.54 ? 29  ASP A N     1 
ATOM   215  C  CA    . ASP A 1 49  ? -10.447 3.692   3.388   1.00 15.81 ? 29  ASP A CA    1 
ATOM   216  C  C     . ASP A 1 49  ? -11.379 4.130   4.513   1.00 15.51 ? 29  ASP A C     1 
ATOM   217  O  O     . ASP A 1 49  ? -11.450 3.468   5.549   1.00 16.00 ? 29  ASP A O     1 
ATOM   218  C  CB    . ASP A 1 49  ? -9.165  4.530   3.461   1.00 16.22 ? 29  ASP A CB    1 
ATOM   219  C  CG    . ASP A 1 49  ? -7.952  3.864   2.807   1.00 16.75 ? 29  ASP A CG    1 
ATOM   220  O  OD1   . ASP A 1 49  ? -8.040  2.685   2.408   1.00 17.44 ? 29  ASP A OD1   1 
ATOM   221  O  OD2   . ASP A 1 49  ? -6.893  4.540   2.709   1.00 17.83 ? 29  ASP A OD2   1 
ATOM   222  N  N     . SER A 1 50  ? -12.109 5.235   4.314   1.00 15.72 ? 30  SER A N     1 
ATOM   223  C  CA    . SER A 1 50  ? -12.951 5.798   5.365   1.00 16.53 ? 30  SER A CA    1 
ATOM   224  C  C     . SER A 1 50  ? -14.093 4.871   5.739   1.00 16.30 ? 30  SER A C     1 
ATOM   225  O  O     . SER A 1 50  ? -14.698 5.043   6.803   1.00 17.70 ? 30  SER A O     1 
ATOM   226  C  CB    . SER A 1 50  ? -13.498 7.157   4.925   1.00 17.18 ? 30  SER A CB    1 
ATOM   227  O  OG    . SER A 1 50  ? -14.637 7.035   4.082   1.00 19.19 ? 30  SER A OG    1 
ATOM   228  N  N     . LEU A 1 51  ? -14.378 3.877   4.907   1.00 15.07 ? 31  LEU A N     1 
ATOM   229  C  CA    . LEU A 1 51  ? -15.469 2.955   5.147   1.00 14.69 ? 31  LEU A CA    1 
ATOM   230  C  C     . LEU A 1 51  ? -15.024 1.646   5.776   1.00 13.36 ? 31  LEU A C     1 
ATOM   231  O  O     . LEU A 1 51  ? -15.877 0.854   6.165   1.00 13.03 ? 31  LEU A O     1 
ATOM   232  C  CB    . LEU A 1 51  ? -16.170 2.633   3.820   1.00 16.14 ? 31  LEU A CB    1 
ATOM   233  C  CG    . LEU A 1 51  ? -16.722 3.825   3.045   1.00 17.66 ? 31  LEU A CG    1 
ATOM   234  C  CD1   . LEU A 1 51  ? -17.347 3.336   1.743   1.00 19.12 ? 31  LEU A CD1   1 
ATOM   235  C  CD2   . LEU A 1 51  ? -17.722 4.583   3.887   1.00 18.55 ? 31  LEU A CD2   1 
ATOM   236  N  N     . ASN A 1 52  ? -13.728 1.378   5.864   1.00 12.92 ? 32  ASN A N     1 
ATOM   237  C  CA    . ASN A 1 52  ? -13.249 0.034   6.202   1.00 12.50 ? 32  ASN A CA    1 
ATOM   238  C  C     . ASN A 1 52  ? -13.425 -0.236  7.690   1.00 12.87 ? 32  ASN A C     1 
ATOM   239  O  O     . ASN A 1 52  ? -12.639 0.221   8.519   1.00 14.59 ? 32  ASN A O     1 
ATOM   240  C  CB    . ASN A 1 52  ? -11.804 -0.127  5.746   1.00 13.36 ? 32  ASN A CB    1 
ATOM   241  C  CG    . ASN A 1 52  ? -11.205 -1.491  6.074   1.00 12.37 ? 32  ASN A CG    1 
ATOM   242  O  OD1   . ASN A 1 52  ? -9.987  -1.602  6.205   1.00 12.83 ? 32  ASN A OD1   1 
ATOM   243  N  ND2   . ASN A 1 52  ? -12.035 -2.536  6.135   1.00 12.45 ? 32  ASN A ND2   1 
ATOM   244  N  N     . VAL A 1 53  ? -14.456 -1.013  8.012   1.00 13.54 ? 33  VAL A N     1 
ATOM   245  C  CA    . VAL A 1 53  ? -14.753 -1.420  9.379   1.00 15.38 ? 33  VAL A CA    1 
ATOM   246  C  C     . VAL A 1 53  ? -14.646 -2.920  9.585   1.00 15.78 ? 33  VAL A C     1 
ATOM   247  O  O     . VAL A 1 53  ? -14.640 -3.364  10.746  1.00 18.40 ? 33  VAL A O     1 
ATOM   248  C  CB    . VAL A 1 53  ? -16.147 -0.932  9.828   1.00 16.83 ? 33  VAL A CB    1 
ATOM   249  C  CG1   . VAL A 1 53  ? -16.208 0.574   9.773   1.00 17.64 ? 33  VAL A CG1   1 
ATOM   250  C  CG2   . VAL A 1 53  ? -17.243 -1.583  8.984   1.00 17.06 ? 33  VAL A CG2   1 
ATOM   251  N  N     . TYR A 1 54  ? -14.554 -3.713  8.516   1.00 16.19 ? 34  TYR A N     1 
ATOM   252  C  CA    . TYR A 1 54  ? -14.629 -5.169  8.564   1.00 16.13 ? 34  TYR A CA    1 
ATOM   253  C  C     . TYR A 1 54  ? -13.556 -5.783  7.673   1.00 14.94 ? 34  TYR A C     1 
ATOM   254  O  O     . TYR A 1 54  ? -13.349 -5.299  6.553   1.00 15.02 ? 34  TYR A O     1 
ATOM   255  C  CB    . TYR A 1 54  ? -16.022 -5.633  8.074   1.00 17.64 ? 34  TYR A CB    1 
ATOM   256  C  CG    . TYR A 1 54  ? -16.072 -7.101  7.803   1.00 18.96 ? 34  TYR A CG    1 
ATOM   257  C  CD1   . TYR A 1 54  ? -16.350 -7.989  8.823   1.00 21.58 ? 34  TYR A CD1   1 
ATOM   258  C  CD2   . TYR A 1 54  ? -15.822 -7.611  6.529   1.00 21.42 ? 34  TYR A CD2   1 
ATOM   259  C  CE1   . TYR A 1 54  ? -16.355 -9.331  8.605   1.00 23.51 ? 34  TYR A CE1   1 
ATOM   260  C  CE2   . TYR A 1 54  ? -15.835 -8.959  6.306   1.00 23.34 ? 34  TYR A CE2   1 
ATOM   261  C  CZ    . TYR A 1 54  ? -16.099 -9.813  7.350   1.00 24.90 ? 34  TYR A CZ    1 
ATOM   262  O  OH    . TYR A 1 54  ? -16.122 -11.166 7.127   1.00 28.23 ? 34  TYR A OH    1 
ATOM   263  N  N     . PRO A 1 55  ? -12.893 -6.885  8.100   1.00 14.42 ? 35  PRO A N     1 
ATOM   264  C  CA    . PRO A 1 55  ? -12.997 -7.588  9.394   1.00 14.65 ? 35  PRO A CA    1 
ATOM   265  C  C     . PRO A 1 55  ? -12.523 -6.760  10.594  1.00 14.72 ? 35  PRO A C     1 
ATOM   266  O  O     . PRO A 1 55  ? -13.162 -6.758  11.643  1.00 17.03 ? 35  PRO A O     1 
ATOM   267  C  CB    . PRO A 1 55  ? -12.124 -8.833  9.188   1.00 15.25 ? 35  PRO A CB    1 
ATOM   268  C  CG    . PRO A 1 55  ? -12.184 -9.068  7.690   1.00 15.90 ? 35  PRO A CG    1 
ATOM   269  C  CD    . PRO A 1 55  ? -12.171 -7.692  7.093   1.00 15.09 ? 35  PRO A CD    1 
ATOM   270  N  N     . VAL A 1 56  ? -11.418 -6.049  10.428  1.00 13.17 ? 36  VAL A N     1 
ATOM   271  C  CA    . VAL A 1 56  ? -10.889 -5.146  11.445  1.00 13.13 ? 36  VAL A CA    1 
ATOM   272  C  C     . VAL A 1 56  ? -11.079 -3.733  10.918  1.00 12.50 ? 36  VAL A C     1 
ATOM   273  O  O     . VAL A 1 56  ? -10.840 -3.482  9.724   1.00 12.34 ? 36  VAL A O     1 
ATOM   274  C  CB    . VAL A 1 56  ? -9.402  -5.423  11.704  1.00 14.32 ? 36  VAL A CB    1 
ATOM   275  C  CG1   . VAL A 1 56  ? -8.821  -4.437  12.736  1.00 14.54 ? 36  VAL A CG1   1 
ATOM   276  C  CG2   . VAL A 1 56  ? -9.199  -6.848  12.161  1.00 15.94 ? 36  VAL A CG2   1 
ATOM   277  N  N     . PRO A 1 57  ? -11.455 -2.777  11.762  1.00 12.07 ? 37  PRO A N     1 
ATOM   278  C  CA    . PRO A 1 57  ? -11.640 -1.402  11.279  1.00 12.56 ? 37  PRO A CA    1 
ATOM   279  C  C     . PRO A 1 57  ? -10.319 -0.646  11.188  1.00 13.08 ? 37  PRO A C     1 
ATOM   280  O  O     . PRO A 1 57  ? -10.089 0.342   11.894  1.00 14.98 ? 37  PRO A O     1 
ATOM   281  C  CB    . PRO A 1 57  ? -12.595 -0.820  12.329  1.00 13.53 ? 37  PRO A CB    1 
ATOM   282  C  CG    . PRO A 1 57  ? -12.187 -1.508  13.611  1.00 13.19 ? 37  PRO A CG    1 
ATOM   283  C  CD    . PRO A 1 57  ? -11.934 -2.933  13.154  1.00 13.14 ? 37  PRO A CD    1 
ATOM   284  N  N     . ASP A 1 58  ? -9.433  -1.120  10.313  1.00 13.33 ? 38  ASP A N     1 
ATOM   285  C  CA    . ASP A 1 58  ? -8.110  -0.538  10.165  1.00 14.68 ? 38  ASP A CA    1 
ATOM   286  C  C     . ASP A 1 58  ? -8.003  0.467   9.016   1.00 15.18 ? 38  ASP A C     1 
ATOM   287  O  O     . ASP A 1 58  ? -6.920  1.007   8.793   1.00 17.25 ? 38  ASP A O     1 
ATOM   288  C  CB    . ASP A 1 58  ? -7.026  -1.630  10.100  1.00 15.03 ? 38  ASP A CB    1 
ATOM   289  C  CG    . ASP A 1 58  ? -7.323  -2.720  9.079   1.00 15.61 ? 38  ASP A CG    1 
ATOM   290  O  OD1   . ASP A 1 58  ? -8.106  -2.476  8.150   1.00 14.57 ? 38  ASP A OD1   1 
ATOM   291  O  OD2   . ASP A 1 58  ? -6.754  -3.825  9.209   1.00 16.16 ? 38  ASP A OD2   1 
ATOM   292  N  N     . GLY A 1 59  ? -9.105  0.791   8.346   1.00 15.30 ? 39  GLY A N     1 
ATOM   293  C  CA    . GLY A 1 59  ? -9.138  1.969   7.489   1.00 16.48 ? 39  GLY A CA    1 
ATOM   294  C  C     . GLY A 1 59  ? -8.206  1.926   6.297   1.00 16.09 ? 39  GLY A C     1 
ATOM   295  O  O     . GLY A 1 59  ? -7.666  2.972   5.910   1.00 17.37 ? 39  GLY A O     1 
ATOM   296  N  N     . ASP A 1 60  ? -8.028  0.745   5.674   1.00 15.49 ? 40  ASP A N     1 
ATOM   297  C  CA    . ASP A 1 60  ? -7.009  0.578   4.640   1.00 15.74 ? 40  ASP A CA    1 
ATOM   298  C  C     . ASP A 1 60  ? -7.471  -0.139  3.370   1.00 14.03 ? 40  ASP A C     1 
ATOM   299  O  O     . ASP A 1 60  ? -6.640  -0.408  2.497   1.00 14.58 ? 40  ASP A O     1 
ATOM   300  C  CB    . ASP A 1 60  ? -5.783  -0.162  5.197   1.00 16.47 ? 40  ASP A CB    1 
ATOM   301  C  CG    . ASP A 1 60  ? -6.109  -1.571  5.678   1.00 17.16 ? 40  ASP A CG    1 
ATOM   302  O  OD1   . ASP A 1 60  ? -7.250  -2.036  5.481   1.00 14.56 ? 40  ASP A OD1   1 
ATOM   303  O  OD2   . ASP A 1 60  ? -5.228  -2.219  6.289   1.00 20.14 ? 40  ASP A OD2   1 
ATOM   304  N  N     . THR A 1 61  ? -8.756  -0.442  3.222   1.00 13.01 ? 41  THR A N     1 
ATOM   305  C  CA    . THR A 1 61  ? -9.188  -1.192  2.048   1.00 12.05 ? 41  THR A CA    1 
ATOM   306  C  C     . THR A 1 61  ? -8.854  -0.453  0.764   1.00 12.22 ? 41  THR A C     1 
ATOM   307  O  O     . THR A 1 61  ? -8.434  -1.070  -0.230  1.00 12.21 ? 41  THR A O     1 
ATOM   308  C  CB    . THR A 1 61  ? -10.696 -1.383  2.089   1.00 11.39 ? 41  THR A CB    1 
ATOM   309  O  OG1   . THR A 1 61  ? -11.075 -1.992  3.328   1.00 11.58 ? 41  THR A OG1   1 
ATOM   310  C  CG2   . THR A 1 61  ? -11.174 -2.226  0.908   1.00 11.37 ? 41  THR A CG2   1 
ATOM   311  N  N     . GLY A 1 62  ? -9.097  0.858   0.743   1.00 12.64 ? 42  GLY A N     1 
ATOM   312  C  CA    . GLY A 1 62  ? -8.832  1.628   -0.460  1.00 13.64 ? 42  GLY A CA    1 
ATOM   313  C  C     . GLY A 1 62  ? -7.369  1.619   -0.835  1.00 14.67 ? 42  GLY A C     1 
ATOM   314  O  O     . GLY A 1 62  ? -7.014  1.420   -1.999  1.00 14.72 ? 42  GLY A O     1 
ATOM   315  N  N     . THR A 1 63  ? -6.499  1.830   0.149   1.00 15.47 ? 43  THR A N     1 
ATOM   316  C  CA    . THR A 1 63  ? -5.065  1.765   -0.095  1.00 16.67 ? 43  THR A CA    1 
ATOM   317  C  C     . THR A 1 63  ? -4.646  0.383   -0.588  1.00 15.46 ? 43  THR A C     1 
ATOM   318  O  O     . THR A 1 63  ? -3.872  0.265   -1.550  1.00 16.04 ? 43  THR A O     1 
ATOM   319  C  CB    . THR A 1 63  ? -4.322  2.151   1.182   1.00 19.17 ? 43  THR A CB    1 
ATOM   320  O  OG1   . THR A 1 63  ? -4.585  3.529   1.485   1.00 21.27 ? 43  THR A OG1   1 
ATOM   321  C  CG2   . THR A 1 63  ? -2.822  1.948   1.014   1.00 20.15 ? 43  THR A CG2   1 
ATOM   322  N  N     . ASN A 1 64  ? -5.171  -0.676  0.036   1.00 14.16 ? 44  ASN A N     1 
ATOM   323  C  CA    . ASN A 1 64  ? -4.803  -2.033  -0.360  1.00 13.40 ? 44  ASN A CA    1 
ATOM   324  C  C     . ASN A 1 64  ? -5.234  -2.322  -1.794  1.00 12.83 ? 44  ASN A C     1 
ATOM   325  O  O     . ASN A 1 64  ? -4.459  -2.849  -2.602  1.00 13.12 ? 44  ASN A O     1 
ATOM   326  C  CB    . ASN A 1 64  ? -5.440  -3.049  0.591   1.00 13.78 ? 44  ASN A CB    1 
ATOM   327  C  CG    . ASN A 1 64  ? -4.779  -3.066  1.952   1.00 14.77 ? 44  ASN A CG    1 
ATOM   328  O  OD1   . ASN A 1 64  ? -3.657  -2.588  2.114   1.00 16.26 ? 44  ASN A OD1   1 
ATOM   329  N  ND2   . ASN A 1 64  ? -5.459  -3.647  2.930   1.00 14.70 ? 44  ASN A ND2   1 
ATOM   330  N  N     . MET A 1 65  ? -6.483  -1.999  -2.122  1.00 11.93 ? 45  MET A N     1 
ATOM   331  C  CA    . MET A 1 65  ? -6.966  -2.241  -3.477  1.00 11.27 ? 45  MET A CA    1 
ATOM   332  C  C     . MET A 1 65  ? -6.237  -1.365  -4.484  1.00 11.87 ? 45  MET A C     1 
ATOM   333  O  O     . MET A 1 65  ? -5.906  -1.822  -5.582  1.00 12.25 ? 45  MET A O     1 
ATOM   334  C  CB    . MET A 1 65  ? -8.475  -2.017  -3.539  1.00 11.30 ? 45  MET A CB    1 
ATOM   335  C  CG    . MET A 1 65  ? -9.267  -3.052  -2.760  1.00 11.09 ? 45  MET A CG    1 
ATOM   336  S  SD    . MET A 1 65  ? -11.055 -2.853  -2.854  1.00 11.01 ? 45  MET A SD    1 
ATOM   337  C  CE    . MET A 1 65  ? -11.381 -3.463  -4.508  1.00 11.93 ? 45  MET A CE    1 
ATOM   338  N  N     . ASN A 1 66  ? -5.980  -0.108  -4.130  1.00 12.40 ? 46  ASN A N     1 
ATOM   339  C  CA    . ASN A 1 66  ? -5.266  0.800   -5.020  1.00 13.61 ? 46  ASN A CA    1 
ATOM   340  C  C     . ASN A 1 66  ? -3.869  0.283   -5.325  1.00 13.65 ? 46  ASN A C     1 
ATOM   341  O  O     . ASN A 1 66  ? -3.451  0.259   -6.486  1.00 14.09 ? 46  ASN A O     1 
ATOM   342  C  CB    . ASN A 1 66  ? -5.210  2.183   -4.368  1.00 14.90 ? 46  ASN A CB    1 
ATOM   343  C  CG    . ASN A 1 66  ? -4.602  3.253   -5.259  1.00 17.21 ? 46  ASN A CG    1 
ATOM   344  O  OD1   . ASN A 1 66  ? -4.636  3.176   -6.470  1.00 17.83 ? 46  ASN A OD1   1 
ATOM   345  N  ND2   . ASN A 1 66  ? -4.075  4.288   -4.639  1.00 19.83 ? 46  ASN A ND2   1 
ATOM   346  N  N     . LEU A 1 67  ? -3.130  -0.147  -4.301  1.00 14.16 ? 47  LEU A N     1 
ATOM   347  C  CA    . LEU A 1 67  ? -1.791  -0.673  -4.541  1.00 14.96 ? 47  LEU A CA    1 
ATOM   348  C  C     . LEU A 1 67  ? -1.838  -1.904  -5.435  1.00 14.20 ? 47  LEU A C     1 
ATOM   349  O  O     . LEU A 1 67  ? -0.998  -2.068  -6.329  1.00 14.62 ? 47  LEU A O     1 
ATOM   350  C  CB    . LEU A 1 67  ? -1.109  -1.006  -3.216  1.00 17.12 ? 47  LEU A CB    1 
ATOM   351  C  CG    . LEU A 1 67  ? -0.703  0.211   -2.395  1.00 19.49 ? 47  LEU A CG    1 
ATOM   352  C  CD1   . LEU A 1 67  ? -0.272  -0.209  -0.991  1.00 21.15 ? 47  LEU A CD1   1 
ATOM   353  C  CD2   . LEU A 1 67  ? 0.408   1.013   -3.082  1.00 21.05 ? 47  LEU A CD2   1 
ATOM   354  N  N     . THR A 1 68  ? -2.816  -2.786  -5.205  1.00 13.47 ? 48  THR A N     1 
ATOM   355  C  CA    . THR A 1 68  ? -2.938  -3.999  -6.013  1.00 13.16 ? 48  THR A CA    1 
ATOM   356  C  C     . THR A 1 68  ? -3.242  -3.646  -7.467  1.00 12.86 ? 48  THR A C     1 
ATOM   357  O  O     . THR A 1 68  ? -2.583  -4.125  -8.403  1.00 13.13 ? 48  THR A O     1 
ATOM   358  C  CB    . THR A 1 68  ? -4.061  -4.873  -5.434  1.00 13.48 ? 48  THR A CB    1 
ATOM   359  O  OG1   . THR A 1 68  ? -3.784  -5.190  -4.058  1.00 14.24 ? 48  THR A OG1   1 
ATOM   360  C  CG2   . THR A 1 68  ? -4.227  -6.158  -6.228  1.00 13.68 ? 48  THR A CG2   1 
ATOM   361  N  N     . MET A 1 69  ? -4.268  -2.824  -7.669  1.00 12.68 ? 49  MET A N     1 
ATOM   362  C  CA    . MET A 1 69  ? -4.670  -2.430  -9.012  1.00 13.25 ? 49  MET A CA    1 
ATOM   363  C  C     . MET A 1 69  ? -3.553  -1.677  -9.720  1.00 13.96 ? 49  MET A C     1 
ATOM   364  O  O     . MET A 1 69  ? -3.346  -1.856  -10.926 1.00 14.53 ? 49  MET A O     1 
ATOM   365  C  CB    . MET A 1 69  ? -5.931  -1.577  -8.910  1.00 13.86 ? 49  MET A CB    1 
ATOM   366  C  CG    . MET A 1 69  ? -6.622  -1.344  -10.214 1.00 14.37 ? 49  MET A CG    1 
ATOM   367  S  SD    . MET A 1 69  ? -7.406  -2.830  -10.854 1.00 13.91 ? 49  MET A SD    1 
ATOM   368  C  CE    . MET A 1 69  ? -8.023  -2.080  -12.358 1.00 14.07 ? 49  MET A CE    1 
ATOM   369  N  N     . THR A 1 70  ? -2.808  -0.845  -8.987  1.00 14.44 ? 50  THR A N     1 
ATOM   370  C  CA    . THR A 1 70  ? -1.697  -0.104  -9.583  1.00 15.41 ? 50  THR A CA    1 
ATOM   371  C  C     . THR A 1 70  ? -0.624  -1.046  -10.116 1.00 15.13 ? 50  THR A C     1 
ATOM   372  O  O     . THR A 1 70  ? -0.048  -0.800  -11.181 1.00 15.53 ? 50  THR A O     1 
ATOM   373  C  CB    . THR A 1 70  ? -1.105  0.864   -8.554  1.00 18.45 ? 50  THR A CB    1 
ATOM   374  O  OG1   . THR A 1 70  ? -2.067  1.883   -8.264  1.00 20.10 ? 50  THR A OG1   1 
ATOM   375  C  CG2   . THR A 1 70  ? 0.164   1.514   -9.078  1.00 19.50 ? 50  THR A CG2   1 
ATOM   376  N  N     . SER A 1 71  ? -0.350  -2.137  -9.397  1.00 15.03 ? 51  SER A N     1 
ATOM   377  C  CA    . SER A 1 71  ? 0.614   -3.125  -9.877  1.00 15.88 ? 51  SER A CA    1 
ATOM   378  C  C     . SER A 1 71  ? 0.149   -3.737  -11.192 1.00 15.05 ? 51  SER A C     1 
ATOM   379  O  O     . SER A 1 71  ? 0.945   -3.925  -12.116 1.00 15.88 ? 51  SER A O     1 
ATOM   380  C  CB    . SER A 1 71  ? 0.806   -4.208  -8.813  1.00 16.69 ? 51  SER A CB    1 
ATOM   381  O  OG    . SER A 1 71  ? 1.806   -5.156  -9.169  1.00 19.10 ? 51  SER A OG    1 
ATOM   382  N  N     . GLY A 1 72  ? -1.138  -4.047  -11.306 1.00 13.89 ? 52  GLY A N     1 
ATOM   383  C  CA    . GLY A 1 72  ? -1.651  -4.517  -12.582 1.00 13.71 ? 52  GLY A CA    1 
ATOM   384  C  C     . GLY A 1 72  ? -1.560  -3.465  -13.673 1.00 13.33 ? 52  GLY A C     1 
ATOM   385  O  O     . GLY A 1 72  ? -1.153  -3.765  -14.799 1.00 13.98 ? 52  GLY A O     1 
ATOM   386  N  N     . ARG A 1 73  ? -1.941  -2.222  -13.349 1.00 13.84 ? 53  ARG A N     1 
ATOM   387  C  CA    A ARG A 1 73  ? -1.919  -1.141  -14.328 0.50 14.04 ? 53  ARG A CA    1 
ATOM   388  C  CA    B ARG A 1 73  ? -1.919  -1.149  -14.337 0.50 15.05 ? 53  ARG A CA    1 
ATOM   389  C  C     . ARG A 1 73  ? -0.511  -0.906  -14.852 1.00 14.74 ? 53  ARG A C     1 
ATOM   390  O  O     . ARG A 1 73  ? -0.316  -0.693  -16.053 1.00 15.24 ? 53  ARG A O     1 
ATOM   391  C  CB    A ARG A 1 73  ? -2.482  0.125   -13.671 0.50 14.31 ? 53  ARG A CB    1 
ATOM   392  C  CB    B ARG A 1 73  ? -2.467  0.157   -13.753 0.50 17.26 ? 53  ARG A CB    1 
ATOM   393  C  CG    A ARG A 1 73  ? -2.479  1.375   -14.540 0.50 15.00 ? 53  ARG A CG    1 
ATOM   394  C  CG    B ARG A 1 73  ? -2.044  1.396   -14.577 0.50 19.82 ? 53  ARG A CG    1 
ATOM   395  C  CD    A ARG A 1 73  ? -2.556  2.671   -13.709 0.50 15.82 ? 53  ARG A CD    1 
ATOM   396  C  CD    B ARG A 1 73  ? -2.633  2.699   -14.072 0.50 22.19 ? 53  ARG A CD    1 
ATOM   397  N  NE    A ARG A 1 73  ? -2.301  3.843   -14.550 0.50 15.84 ? 53  ARG A NE    1 
ATOM   398  N  NE    B ARG A 1 73  ? -2.030  3.132   -12.816 0.50 23.80 ? 53  ARG A NE    1 
ATOM   399  C  CZ    A ARG A 1 73  ? -2.964  4.991   -14.484 0.50 16.87 ? 53  ARG A CZ    1 
ATOM   400  C  CZ    B ARG A 1 73  ? -0.792  3.608   -12.679 0.50 24.52 ? 53  ARG A CZ    1 
ATOM   401  N  NH1   A ARG A 1 73  ? -3.948  5.148   -13.615 0.50 18.05 ? 53  ARG A NH1   1 
ATOM   402  N  NH1   B ARG A 1 73  ? 0.019   3.719   -13.723 0.50 25.15 ? 53  ARG A NH1   1 
ATOM   403  N  NH2   A ARG A 1 73  ? -2.638  5.982   -15.300 0.50 17.13 ? 53  ARG A NH2   1 
ATOM   404  N  NH2   B ARG A 1 73  ? -0.364  3.977   -11.481 0.50 24.68 ? 53  ARG A NH2   1 
ATOM   405  N  N     . GLU A 1 74  ? 0.478   -0.909  -13.958 1.00 15.16 ? 54  GLU A N     1 
ATOM   406  C  CA    . GLU A 1 74  ? 1.847   -0.642  -14.374 1.00 17.09 ? 54  GLU A CA    1 
ATOM   407  C  C     . GLU A 1 74  ? 2.346   -1.708  -15.335 1.00 16.79 ? 54  GLU A C     1 
ATOM   408  O  O     . GLU A 1 74  ? 3.012   -1.390  -16.329 1.00 17.30 ? 54  GLU A O     1 
ATOM   409  C  CB    . GLU A 1 74  ? 2.747   -0.536  -13.142 1.00 19.73 ? 54  GLU A CB    1 
ATOM   410  C  CG    . GLU A 1 74  ? 2.519   0.745   -12.339 1.00 24.02 ? 54  GLU A CG    1 
ATOM   411  C  CD    . GLU A 1 74  ? 3.318   0.819   -11.042 1.00 27.53 ? 54  GLU A CD    1 
ATOM   412  O  OE1   . GLU A 1 74  ? 3.800   -0.228  -10.558 1.00 29.04 ? 54  GLU A OE1   1 
ATOM   413  O  OE2   . GLU A 1 74  ? 3.448   1.933   -10.490 1.00 29.02 ? 54  GLU A OE2   1 
ATOM   414  N  N     . GLU A 1 75  ? 2.032   -2.976  -15.069 1.00 16.00 ? 55  GLU A N     1 
ATOM   415  C  CA    . GLU A 1 75  ? 2.452   -4.030  -15.986 1.00 16.66 ? 55  GLU A CA    1 
ATOM   416  C  C     . GLU A 1 75  ? 1.812   -3.831  -17.353 1.00 15.87 ? 55  GLU A C     1 
ATOM   417  O  O     . GLU A 1 75  ? 2.469   -3.986  -18.387 1.00 16.19 ? 55  GLU A O     1 
ATOM   418  C  CB    . GLU A 1 75  ? 2.074   -5.404  -15.429 1.00 19.21 ? 55  GLU A CB    1 
ATOM   419  C  CG    . GLU A 1 75  ? 2.894   -5.869  -14.245 1.00 23.17 ? 55  GLU A CG    1 
ATOM   420  C  CD    . GLU A 1 75  ? 4.374   -5.988  -14.549 1.00 26.64 ? 55  GLU A CD    1 
ATOM   421  O  OE1   . GLU A 1 75  ? 5.159   -5.361  -13.818 1.00 28.95 ? 55  GLU A OE1   1 
ATOM   422  O  OE2   . GLU A 1 75  ? 4.750   -6.695  -15.515 1.00 28.41 ? 55  GLU A OE2   1 
ATOM   423  N  N     . VAL A 1 76  ? 0.529   -3.474  -17.373 1.00 14.51 ? 56  VAL A N     1 
ATOM   424  C  CA    . VAL A 1 76  ? -0.197  -3.259  -18.622 1.00 14.30 ? 56  VAL A CA    1 
ATOM   425  C  C     . VAL A 1 76  ? 0.396   -2.092  -19.407 1.00 15.52 ? 56  VAL A C     1 
ATOM   426  O  O     . VAL A 1 76  ? 0.637   -2.197  -20.616 1.00 16.05 ? 56  VAL A O     1 
ATOM   427  C  CB    . VAL A 1 76  ? -1.684  -3.049  -18.289 1.00 13.67 ? 56  VAL A CB    1 
ATOM   428  C  CG1   . VAL A 1 76  ? -2.427  -2.398  -19.439 1.00 14.26 ? 56  VAL A CG1   1 
ATOM   429  C  CG2   . VAL A 1 76  ? -2.287  -4.386  -17.900 1.00 14.03 ? 56  VAL A CG2   1 
ATOM   430  N  N     . GLU A 1 77  ? 0.642   -0.961  -18.739 1.00 16.17 ? 57  GLU A N     1 
ATOM   431  C  CA    . GLU A 1 77  ? 1.142   0.210   -19.458 1.00 17.77 ? 57  GLU A CA    1 
ATOM   432  C  C     . GLU A 1 77  ? 2.506   -0.050  -20.078 1.00 19.04 ? 57  GLU A C     1 
ATOM   433  O  O     . GLU A 1 77  ? 2.856   0.566   -21.092 1.00 20.71 ? 57  GLU A O     1 
ATOM   434  C  CB    . GLU A 1 77  ? 1.226   1.411   -18.516 1.00 19.02 ? 57  GLU A CB    1 
ATOM   435  C  CG    . GLU A 1 77  ? -0.134  1.984   -18.185 1.00 20.66 ? 57  GLU A CG    1 
ATOM   436  C  CD    . GLU A 1 77  ? -0.091  3.087   -17.142 1.00 23.58 ? 57  GLU A CD    1 
ATOM   437  O  OE1   . GLU A 1 77  ? 0.853   3.108   -16.324 1.00 24.97 ? 57  GLU A OE1   1 
ATOM   438  O  OE2   . GLU A 1 77  ? -1.018  3.922   -17.121 1.00 24.64 ? 57  GLU A OE2   1 
ATOM   439  N  N     . ASN A 1 78  ? 3.292   -0.940  -19.484 1.00 19.11 ? 58  ASN A N     1 
ATOM   440  C  CA    . ASN A 1 78  ? 4.616   -1.252  -19.998 1.00 20.98 ? 58  ASN A CA    1 
ATOM   441  C  C     . ASN A 1 78  ? 4.608   -2.364  -21.037 1.00 19.87 ? 58  ASN A C     1 
ATOM   442  O  O     . ASN A 1 78  ? 5.643   -2.611  -21.663 1.00 20.84 ? 58  ASN A O     1 
ATOM   443  C  CB    . ASN A 1 78  ? 5.540   -1.632  -18.836 1.00 24.21 ? 58  ASN A CB    1 
ATOM   444  C  CG    . ASN A 1 78  ? 6.006   -0.422  -18.041 1.00 28.56 ? 58  ASN A CG    1 
ATOM   445  O  OD1   . ASN A 1 78  ? 6.264   0.641   -18.607 1.00 30.95 ? 58  ASN A OD1   1 
ATOM   446  N  ND2   . ASN A 1 78  ? 6.118   -0.580  -16.726 1.00 29.89 ? 58  ASN A ND2   1 
ATOM   447  N  N     . ASN A 1 79  ? 3.477   -3.036  -21.245 1.00 18.31 ? 59  ASN A N     1 
ATOM   448  C  CA    A ASN A 1 79  ? 3.392   -4.177  -22.142 0.50 18.04 ? 59  ASN A CA    1 
ATOM   449  C  CA    B ASN A 1 79  ? 3.419   -4.131  -22.211 0.50 18.56 ? 59  ASN A CA    1 
ATOM   450  C  C     . ASN A 1 79  ? 2.001   -4.208  -22.780 1.00 16.98 ? 59  ASN A C     1 
ATOM   451  O  O     . ASN A 1 79  ? 1.207   -5.090  -22.480 1.00 17.62 ? 59  ASN A O     1 
ATOM   452  C  CB    A ASN A 1 79  ? 3.619   -5.493  -21.389 0.50 19.23 ? 59  ASN A CB    1 
ATOM   453  C  CB    B ASN A 1 79  ? 3.870   -5.472  -21.627 0.50 20.79 ? 59  ASN A CB    1 
ATOM   454  C  CG    A ASN A 1 79  ? 4.946   -5.545  -20.663 0.50 20.40 ? 59  ASN A CG    1 
ATOM   455  C  CG    B ASN A 1 79  ? 4.113   -6.515  -22.704 0.50 22.51 ? 59  ASN A CG    1 
ATOM   456  O  OD1   A ASN A 1 79  ? 5.984   -5.791  -21.272 0.50 21.39 ? 59  ASN A OD1   1 
ATOM   457  O  OD1   B ASN A 1 79  ? 4.214   -6.185  -23.885 0.50 23.72 ? 59  ASN A OD1   1 
ATOM   458  N  ND2   A ASN A 1 79  ? 4.916   -5.344  -19.351 0.50 20.75 ? 59  ASN A ND2   1 
ATOM   459  N  ND2   B ASN A 1 79  ? 4.200   -7.778  -22.303 0.50 23.19 ? 59  ASN A ND2   1 
ATOM   460  N  N     . LEU A 1 80  ? 1.697   -3.249  -23.657 1.00 15.29 ? 60  LEU A N     1 
ATOM   461  C  CA    . LEU A 1 80  ? 0.406   -3.214  -24.325 1.00 15.11 ? 60  LEU A CA    1 
ATOM   462  C  C     . LEU A 1 80  ? 0.367   -4.226  -25.468 1.00 15.52 ? 60  LEU A C     1 
ATOM   463  O  O     . LEU A 1 80  ? 1.397   -4.633  -26.010 1.00 16.87 ? 60  LEU A O     1 
ATOM   464  C  CB    . LEU A 1 80  ? 0.125   -1.810  -24.866 1.00 14.93 ? 60  LEU A CB    1 
ATOM   465  C  CG    . LEU A 1 80  ? -0.046  -0.712  -23.807 1.00 15.53 ? 60  LEU A CG    1 
ATOM   466  C  CD1   . LEU A 1 80  ? -0.064  0.650   -24.462 1.00 16.86 ? 60  LEU A CD1   1 
ATOM   467  C  CD2   . LEU A 1 80  ? -1.315  -0.931  -22.997 1.00 15.72 ? 60  LEU A CD2   1 
ATOM   468  N  N     . SER A 1 81  ? -0.852  -4.624  -25.837 1.00 15.73 ? 61  SER A N     1 
ATOM   469  C  CA    . SER A 1 81  ? -1.067  -5.576  -26.921 1.00 15.25 ? 61  SER A CA    1 
ATOM   470  C  C     . SER A 1 81  ? -2.437  -5.349  -27.544 1.00 15.41 ? 61  SER A C     1 
ATOM   471  O  O     . SER A 1 81  ? -3.389  -4.980  -26.859 1.00 16.35 ? 61  SER A O     1 
ATOM   472  C  CB    . SER A 1 81  ? -0.999  -7.023  -26.412 1.00 15.96 ? 61  SER A CB    1 
ATOM   473  O  OG    . SER A 1 81  ? -1.344  -7.937  -27.436 1.00 16.37 ? 61  SER A OG    1 
ATOM   474  N  N     . LYS A 1 82  ? -2.532  -5.596  -28.855 1.00 15.48 ? 62  LYS A N     1 
ATOM   475  C  CA    . LYS A 1 82  ? -3.827  -5.587  -29.522 1.00 15.96 ? 62  LYS A CA    1 
ATOM   476  C  C     . LYS A 1 82  ? -4.670  -6.790  -29.117 1.00 13.94 ? 62  LYS A C     1 
ATOM   477  O  O     . LYS A 1 82  ? -5.880  -6.800  -29.357 1.00 15.21 ? 62  LYS A O     1 
ATOM   478  C  CB    . LYS A 1 82  ? -3.641  -5.576  -31.046 1.00 17.53 ? 62  LYS A CB    1 
ATOM   479  C  CG    . LYS A 1 82  ? -3.183  -6.901  -31.641 1.00 19.54 ? 62  LYS A CG    1 
ATOM   480  C  CD    . LYS A 1 82  ? -2.860  -6.798  -33.125 1.00 21.88 ? 62  LYS A CD    1 
ATOM   481  C  CE    . LYS A 1 82  ? -2.122  -8.054  -33.593 1.00 23.97 ? 62  LYS A CE    1 
ATOM   482  N  NZ    . LYS A 1 82  ? -1.771  -8.000  -35.037 1.00 25.22 ? 62  LYS A NZ    1 
ATOM   483  N  N     . ASN A 1 83  ? -4.043  -7.824  -28.556 1.00 14.03 ? 63  ASN A N     1 
ATOM   484  C  CA    . ASN A 1 83  ? -4.681  -9.106  -28.282 1.00 14.18 ? 63  ASN A CA    1 
ATOM   485  C  C     . ASN A 1 83  ? -5.139  -9.125  -26.825 1.00 13.17 ? 63  ASN A C     1 
ATOM   486  O  O     . ASN A 1 83  ? -4.314  -9.044  -25.908 1.00 13.37 ? 63  ASN A O     1 
ATOM   487  C  CB    . ASN A 1 83  ? -3.666  -10.221 -28.542 1.00 15.02 ? 63  ASN A CB    1 
ATOM   488  C  CG    . ASN A 1 83  ? -4.236  -11.600 -28.350 1.00 16.63 ? 63  ASN A CG    1 
ATOM   489  O  OD1   . ASN A 1 83  ? -4.393  -12.065 -27.221 1.00 17.01 ? 63  ASN A OD1   1 
ATOM   490  N  ND2   . ASN A 1 83  ? -4.522  -12.282 -29.453 1.00 17.63 ? 63  ASN A ND2   1 
ATOM   491  N  N     . ILE A 1 84  ? -6.451  -9.239  -26.613 1.00 13.04 ? 64  ILE A N     1 
ATOM   492  C  CA    . ILE A 1 84  ? -6.979  -9.097  -25.258 1.00 12.62 ? 64  ILE A CA    1 
ATOM   493  C  C     . ILE A 1 84  ? -6.486  -10.222 -24.352 1.00 12.54 ? 64  ILE A C     1 
ATOM   494  O  O     . ILE A 1 84  ? -6.240  -10.002 -23.164 1.00 12.65 ? 64  ILE A O     1 
ATOM   495  C  CB    . ILE A 1 84  ? -8.518  -8.976  -25.250 1.00 12.64 ? 64  ILE A CB    1 
ATOM   496  C  CG1   . ILE A 1 84  ? -8.981  -8.414  -23.901 1.00 12.93 ? 64  ILE A CG1   1 
ATOM   497  C  CG2   . ILE A 1 84  ? -9.195  -10.293 -25.594 1.00 12.97 ? 64  ILE A CG2   1 
ATOM   498  C  CD1   . ILE A 1 84  ? -10.472 -8.237  -23.776 1.00 13.15 ? 64  ILE A CD1   1 
ATOM   499  N  N     . GLY A 1 85  ? -6.348  -11.440 -24.879 1.00 12.57 ? 65  GLY A N     1 
ATOM   500  C  CA    . GLY A 1 85  ? -5.894  -12.543 -24.044 1.00 12.97 ? 65  GLY A CA    1 
ATOM   501  C  C     . GLY A 1 85  ? -4.489  -12.330 -23.522 1.00 13.01 ? 65  GLY A C     1 
ATOM   502  O  O     . GLY A 1 85  ? -4.205  -12.583 -22.340 1.00 13.15 ? 65  GLY A O     1 
ATOM   503  N  N     . GLU A 1 86  ? -3.592  -11.850 -24.389 1.00 13.59 ? 66  GLU A N     1 
ATOM   504  C  CA    . GLU A 1 86  ? -2.230  -11.545 -23.964 1.00 14.12 ? 66  GLU A CA    1 
ATOM   505  C  C     . GLU A 1 86  ? -2.204  -10.392 -22.975 1.00 13.35 ? 66  GLU A C     1 
ATOM   506  O  O     . GLU A 1 86  ? -1.480  -10.441 -21.973 1.00 13.71 ? 66  GLU A O     1 
ATOM   507  C  CB    . GLU A 1 86  ? -1.354  -11.230 -25.180 1.00 18.21 ? 66  GLU A CB    1 
ATOM   508  C  CG    . GLU A 1 86  ? -1.011  -12.456 -26.004 1.00 23.64 ? 66  GLU A CG    1 
ATOM   509  C  CD    . GLU A 1 86  ? -0.324  -13.540 -25.186 1.00 27.97 ? 66  GLU A CD    1 
ATOM   510  O  OE1   . GLU A 1 86  ? 0.567   -13.203 -24.372 1.00 28.90 ? 66  GLU A OE1   1 
ATOM   511  O  OE2   . GLU A 1 86  ? -0.693  -14.727 -25.340 1.00 30.11 ? 66  GLU A OE2   1 
ATOM   512  N  N     . LEU A 1 87  ? -2.984  -9.347  -23.239 1.00 12.65 ? 67  LEU A N     1 
ATOM   513  C  CA    . LEU A 1 87  ? -3.043  -8.221  -22.313 1.00 12.60 ? 67  LEU A CA    1 
ATOM   514  C  C     . LEU A 1 87  ? -3.560  -8.680  -20.955 1.00 12.29 ? 67  LEU A C     1 
ATOM   515  O  O     . LEU A 1 87  ? -3.056  -8.253  -19.910 1.00 12.60 ? 67  LEU A O     1 
ATOM   516  C  CB    . LEU A 1 87  ? -3.908  -7.112  -22.918 1.00 13.05 ? 67  LEU A CB    1 
ATOM   517  C  CG    . LEU A 1 87  ? -3.777  -5.680  -22.385 1.00 13.42 ? 67  LEU A CG    1 
ATOM   518  C  CD1   . LEU A 1 87  ? -4.551  -5.478  -21.076 1.00 13.17 ? 67  LEU A CD1   1 
ATOM   519  C  CD2   . LEU A 1 87  ? -2.320  -5.259  -22.230 1.00 14.76 ? 67  LEU A CD2   1 
ATOM   520  N  N     . GLY A 1 88  ? -4.542  -9.572  -20.953 1.00 12.14 ? 68  GLY A N     1 
ATOM   521  C  CA    . GLY A 1 88  ? -5.048  -10.104 -19.700 1.00 12.27 ? 68  GLY A CA    1 
ATOM   522  C  C     . GLY A 1 88  ? -4.010  -10.893 -18.921 1.00 12.42 ? 68  GLY A C     1 
ATOM   523  O  O     . GLY A 1 88  ? -3.988  -10.844 -17.690 1.00 12.56 ? 68  GLY A O     1 
ATOM   524  N  N     . LYS A 1 89  ? -3.149  -11.647 -19.614 1.00 13.03 ? 69  LYS A N     1 
ATOM   525  C  CA    . LYS A 1 89  ? -2.076  -12.349 -18.909 1.00 13.73 ? 69  LYS A CA    1 
ATOM   526  C  C     . LYS A 1 89  ? -1.165  -11.358 -18.202 1.00 13.15 ? 69  LYS A C     1 
ATOM   527  O  O     . LYS A 1 89  ? -0.747  -11.582 -17.062 1.00 13.90 ? 69  LYS A O     1 
ATOM   528  C  CB    . LYS A 1 89  ? -1.264  -13.192 -19.894 1.00 14.95 ? 69  LYS A CB    1 
ATOM   529  C  CG    . LYS A 1 89  ? -1.976  -14.412 -20.444 1.00 17.16 ? 69  LYS A CG    1 
ATOM   530  C  CD    . LYS A 1 89  ? -1.133  -15.128 -21.501 1.00 20.18 ? 69  LYS A CD    1 
ATOM   531  C  CE    . LYS A 1 89  ? -1.950  -16.161 -22.257 1.00 22.62 ? 69  LYS A CE    1 
ATOM   532  N  NZ    . LYS A 1 89  ? -1.179  -16.786 -23.360 1.00 24.62 ? 69  LYS A NZ    1 
ATOM   533  N  N     . THR A 1 90  ? -0.857  -10.249 -18.871 1.00 12.91 ? 70  THR A N     1 
ATOM   534  C  CA    . THR A 1 90  ? -0.021  -9.205  -18.294 1.00 13.14 ? 70  THR A CA    1 
ATOM   535  C  C     . THR A 1 90  ? -0.689  -8.574  -17.080 1.00 12.52 ? 70  THR A C     1 
ATOM   536  O  O     . THR A 1 90  ? -0.058  -8.401  -16.032 1.00 12.73 ? 70  THR A O     1 
ATOM   537  C  CB    . THR A 1 90  ? 0.252   -8.165  -19.386 1.00 13.93 ? 70  THR A CB    1 
ATOM   538  O  OG1   . THR A 1 90  ? 0.992   -8.798  -20.441 1.00 15.14 ? 70  THR A OG1   1 
ATOM   539  C  CG2   . THR A 1 90  ? 1.007   -6.967  -18.859 1.00 15.07 ? 70  THR A CG2   1 
ATOM   540  N  N     . PHE A 1 91  ? -1.966  -8.217  -17.205 1.00 11.98 ? 71  PHE A N     1 
ATOM   541  C  CA    . PHE A 1 91  ? -2.703  -7.628  -16.086 1.00 12.13 ? 71  PHE A CA    1 
ATOM   542  C  C     . PHE A 1 91  ? -2.768  -8.586  -14.901 1.00 11.91 ? 71  PHE A C     1 
ATOM   543  O  O     . PHE A 1 91  ? -2.494  -8.203  -13.758 1.00 12.54 ? 71  PHE A O     1 
ATOM   544  C  CB    . PHE A 1 91  ? -4.115  -7.301  -16.577 1.00 11.90 ? 71  PHE A CB    1 
ATOM   545  C  CG    . PHE A 1 91  ? -5.018  -6.659  -15.552 1.00 11.75 ? 71  PHE A CG    1 
ATOM   546  C  CD1   . PHE A 1 91  ? -4.578  -5.627  -14.736 1.00 12.38 ? 71  PHE A CD1   1 
ATOM   547  C  CD2   . PHE A 1 91  ? -6.335  -7.070  -15.439 1.00 12.06 ? 71  PHE A CD2   1 
ATOM   548  C  CE1   . PHE A 1 91  ? -5.445  -5.022  -13.825 1.00 12.74 ? 71  PHE A CE1   1 
ATOM   549  C  CE2   . PHE A 1 91  ? -7.194  -6.469  -14.536 1.00 12.66 ? 71  PHE A CE2   1 
ATOM   550  C  CZ    . PHE A 1 91  ? -6.746  -5.442  -13.731 1.00 12.92 ? 71  PHE A CZ    1 
ATOM   551  N  N     . SER A 1 92  ? -3.149  -9.840  -15.166 1.00 12.45 ? 72  SER A N     1 
ATOM   552  C  CA    . SER A 1 92  ? -3.276  -10.855 -14.126 1.00 13.50 ? 72  SER A CA    1 
ATOM   553  C  C     . SER A 1 92  ? -1.968  -11.017 -13.365 1.00 13.34 ? 72  SER A C     1 
ATOM   554  O  O     . SER A 1 92  ? -1.956  -11.046 -12.127 1.00 13.90 ? 72  SER A O     1 
ATOM   555  C  CB    . SER A 1 92  ? -3.706  -12.167 -14.797 1.00 15.79 ? 72  SER A CB    1 
ATOM   556  O  OG    . SER A 1 92  ? -3.813  -13.237 -13.884 1.00 17.05 ? 72  SER A OG    1 
ATOM   557  N  N     . LYS A 1 93  ? -0.856  -11.140 -14.085 1.00 13.80 ? 73  LYS A N     1 
ATOM   558  C  CA    . LYS A 1 93  ? 0.436   -11.297 -13.427 1.00 15.07 ? 73  LYS A CA    1 
ATOM   559  C  C     . LYS A 1 93  ? 0.738   -10.102 -12.535 1.00 14.14 ? 73  LYS A C     1 
ATOM   560  O  O     . LYS A 1 93  ? 1.195   -10.266 -11.398 1.00 14.66 ? 73  LYS A O     1 
ATOM   561  C  CB    . LYS A 1 93  ? 1.541   -11.487 -14.466 1.00 17.77 ? 73  LYS A CB    1 
ATOM   562  C  CG    . LYS A 1 93  ? 2.955   -11.345 -13.916 1.00 19.93 ? 73  LYS A CG    1 
ATOM   563  N  N     . GLY A 1 94  ? 0.477   -8.889  -13.023 1.00 13.47 ? 74  GLY A N     1 
ATOM   564  C  CA    . GLY A 1 94  ? 0.745   -7.715  -12.219 1.00 13.92 ? 74  GLY A CA    1 
ATOM   565  C  C     . GLY A 1 94  ? -0.076  -7.688  -10.944 1.00 13.36 ? 74  GLY A C     1 
ATOM   566  O  O     . GLY A 1 94  ? 0.431   -7.346  -9.870  1.00 14.27 ? 74  GLY A O     1 
ATOM   567  N  N     . LEU A 1 95  ? -1.361  -8.033  -11.037 1.00 12.05 ? 75  LEU A N     1 
ATOM   568  C  CA    . LEU A 1 95  ? -2.190  -8.054  -9.835  1.00 12.14 ? 75  LEU A CA    1 
ATOM   569  C  C     . LEU A 1 95  ? -1.694  -9.091  -8.840  1.00 12.06 ? 75  LEU A C     1 
ATOM   570  O  O     . LEU A 1 95  ? -1.661  -8.843  -7.629  1.00 12.63 ? 75  LEU A O     1 
ATOM   571  C  CB    . LEU A 1 95  ? -3.635  -8.391  -10.180 1.00 12.19 ? 75  LEU A CB    1 
ATOM   572  C  CG    . LEU A 1 95  ? -4.403  -7.391  -11.028 1.00 12.12 ? 75  LEU A CG    1 
ATOM   573  C  CD1   . LEU A 1 95  ? -5.708  -8.023  -11.473 1.00 13.84 ? 75  LEU A CD1   1 
ATOM   574  C  CD2   . LEU A 1 95  ? -4.667  -6.104  -10.292 1.00 12.97 ? 75  LEU A CD2   1 
ATOM   575  N  N     . LEU A 1 96  ? -1.369  -10.286 -9.324  1.00 11.88 ? 76  LEU A N     1 
ATOM   576  C  CA    . LEU A 1 96  ? -1.094  -11.401 -8.430  1.00 12.31 ? 76  LEU A CA    1 
ATOM   577  C  C     . LEU A 1 96  ? 0.240   -11.252 -7.714  1.00 14.06 ? 76  LEU A C     1 
ATOM   578  O  O     . LEU A 1 96  ? 0.424   -11.822 -6.638  1.00 16.03 ? 76  LEU A O     1 
ATOM   579  C  CB    . LEU A 1 96  ? -1.161  -12.723 -9.198  1.00 12.47 ? 76  LEU A CB    1 
ATOM   580  C  CG    . LEU A 1 96  ? -2.581  -13.100 -9.627  1.00 12.44 ? 76  LEU A CG    1 
ATOM   581  C  CD1   . LEU A 1 96  ? -2.534  -14.095 -10.772 1.00 13.06 ? 76  LEU A CD1   1 
ATOM   582  C  CD2   . LEU A 1 96  ? -3.384  -13.639 -8.461  1.00 13.14 ? 76  LEU A CD2   1 
ATOM   583  N  N     . MET A 1 97  ? 1.195   -10.523 -8.271  1.00 14.89 ? 77  MET A N     1 
ATOM   584  C  CA    A MET A 1 97  ? 2.431   -10.310 -7.526  0.50 17.26 ? 77  MET A CA    1 
ATOM   585  C  CA    B MET A 1 97  ? 2.466   -10.264 -7.608  0.50 16.79 ? 77  MET A CA    1 
ATOM   586  C  C     . MET A 1 97  ? 2.459   -8.966  -6.804  1.00 17.24 ? 77  MET A C     1 
ATOM   587  O  O     . MET A 1 97  ? 3.501   -8.592  -6.251  1.00 19.33 ? 77  MET A O     1 
ATOM   588  C  CB    A MET A 1 97  ? 3.680   -10.558 -8.371  0.50 20.73 ? 77  MET A CB    1 
ATOM   589  C  CB    B MET A 1 97  ? 3.597   -10.257 -8.637  0.50 19.89 ? 77  MET A CB    1 
ATOM   590  C  CG    A MET A 1 97  ? 3.790   -9.758  -9.611  0.50 23.13 ? 77  MET A CG    1 
ATOM   591  C  CG    B MET A 1 97  ? 3.664   -9.028  -9.477  0.50 23.37 ? 77  MET A CG    1 
ATOM   592  S  SD    A MET A 1 97  ? 5.208   -10.313 -10.578 0.50 25.13 ? 77  MET A SD    1 
ATOM   593  S  SD    B MET A 1 97  ? 5.161   -9.122  -10.458 0.50 26.72 ? 77  MET A SD    1 
ATOM   594  C  CE    A MET A 1 97  ? 4.740   -11.998 -10.973 0.50 23.06 ? 77  MET A CE    1 
ATOM   595  C  CE    B MET A 1 97  ? 4.891   -7.797  -11.634 0.50 26.40 ? 77  MET A CE    1 
ATOM   596  N  N     . GLY A 1 98  ? 1.320   -8.270  -6.732  1.00 17.83 ? 78  GLY A N     1 
ATOM   597  C  CA    . GLY A 1 98  ? 1.222   -7.029  -5.988  1.00 17.78 ? 78  GLY A CA    1 
ATOM   598  C  C     . GLY A 1 98  ? -0.004  -6.971  -5.101  1.00 17.04 ? 78  GLY A C     1 
ATOM   599  O  O     . GLY A 1 98  ? -0.409  -5.890  -4.674  1.00 17.94 ? 78  GLY A O     1 
ATOM   600  N  N     . ALA A 1 99  ? -0.605  -8.126  -4.818  1.00 17.81 ? 79  ALA A N     1 
ATOM   601  C  CA    . ALA A 1 99  ? -1.868  -8.156  -4.094  1.00 17.97 ? 79  ALA A CA    1 
ATOM   602  C  C     . ALA A 1 99  ? -1.627  -7.850  -2.623  1.00 18.87 ? 79  ALA A C     1 
ATOM   603  O  O     . ALA A 1 99  ? -0.754  -8.450  -1.993  1.00 21.75 ? 79  ALA A O     1 
ATOM   604  C  CB    . ALA A 1 99  ? -2.544  -9.517  -4.274  1.00 17.86 ? 79  ALA A CB    1 
ATOM   605  N  N     . ARG A 1 100 ? -2.389  -6.892  -2.094  1.00 17.16 ? 80  ARG A N     1 
ATOM   606  C  CA    . ARG A 1 100 ? -2.250  -6.406  -0.728  1.00 17.61 ? 80  ARG A CA    1 
ATOM   607  C  C     . ARG A 1 100 ? -3.592  -6.508  -0.015  1.00 16.31 ? 80  ARG A C     1 
ATOM   608  O  O     . ARG A 1 100 ? -4.601  -6.006  -0.516  1.00 15.68 ? 80  ARG A O     1 
ATOM   609  C  CB    . ARG A 1 100 ? -1.811  -4.933  -0.725  1.00 19.25 ? 80  ARG A CB    1 
ATOM   610  C  CG    . ARG A 1 100 ? -0.444  -4.662  -1.341  1.00 20.82 ? 80  ARG A CG    1 
ATOM   611  N  N     . GLY A 1 101 ? -3.591  -7.116  1.171   1.00 16.62 ? 81  GLY A N     1 
ATOM   612  C  CA    . GLY A 1 101 ? -4.767  -7.150  2.018   1.00 15.84 ? 81  GLY A CA    1 
ATOM   613  C  C     . GLY A 1 101 ? -5.809  -8.144  1.539   1.00 14.31 ? 81  GLY A C     1 
ATOM   614  O  O     . GLY A 1 101 ? -5.744  -8.677  0.433   1.00 14.61 ? 81  GLY A O     1 
ATOM   615  N  N     . ASN A 1 102 ? -6.817  -8.381  2.383   1.00 13.54 ? 82  ASN A N     1 
ATOM   616  C  CA    . ASN A 1 102 ? -7.880  -9.287  1.967   1.00 13.28 ? 82  ASN A CA    1 
ATOM   617  C  C     . ASN A 1 102 ? -8.511  -8.793  0.682   1.00 11.97 ? 82  ASN A C     1 
ATOM   618  O  O     . ASN A 1 102 ? -8.841  -9.587  -0.205  1.00 12.02 ? 82  ASN A O     1 
ATOM   619  C  CB    . ASN A 1 102 ? -8.986  -9.386  3.021   1.00 14.54 ? 82  ASN A CB    1 
ATOM   620  C  CG    . ASN A 1 102 ? -8.538  -10.049 4.303   1.00 17.38 ? 82  ASN A CG    1 
ATOM   621  O  OD1   . ASN A 1 102 ? -7.487  -9.736  4.849   1.00 18.62 ? 82  ASN A OD1   1 
ATOM   622  N  ND2   . ASN A 1 102 ? -9.358  -10.945 4.811   1.00 21.19 ? 82  ASN A ND2   1 
ATOM   623  N  N     . SER A 1 103 ? -8.720  -7.478  0.585   1.00 11.32 ? 83  SER A N     1 
ATOM   624  C  CA    . SER A 1 103 ? -9.424  -6.934  -0.568  1.00 10.89 ? 83  SER A CA    1 
ATOM   625  C  C     . SER A 1 103 ? -8.581  -7.003  -1.830  1.00 11.17 ? 83  SER A C     1 
ATOM   626  O  O     . SER A 1 103 ? -9.111  -7.270  -2.912  1.00 11.04 ? 83  SER A O     1 
ATOM   627  C  CB    . SER A 1 103 ? -9.861  -5.501  -0.286  1.00 11.26 ? 83  SER A CB    1 
ATOM   628  O  OG    . SER A 1 103 ? -8.755  -4.643  -0.039  1.00 11.29 ? 83  SER A OG    1 
ATOM   629  N  N     . GLY A 1 104 ? -7.281  -6.732  -1.717  1.00 11.25 ? 84  GLY A N     1 
ATOM   630  C  CA    . GLY A 1 104 ? -6.416  -6.832  -2.880  1.00 11.46 ? 84  GLY A CA    1 
ATOM   631  C  C     . GLY A 1 104 ? -6.247  -8.263  -3.350  1.00 11.03 ? 84  GLY A C     1 
ATOM   632  O  O     . GLY A 1 104 ? -6.218  -8.536  -4.555  1.00 11.08 ? 84  GLY A O     1 
ATOM   633  N  N     . VAL A 1 105 ? -6.121  -9.199  -2.412  1.00 11.08 ? 85  VAL A N     1 
ATOM   634  C  CA    . VAL A 1 105 ? -6.077  -10.605 -2.791  1.00 11.17 ? 85  VAL A CA    1 
ATOM   635  C  C     . VAL A 1 105 ? -7.359  -10.994 -3.523  1.00 10.39 ? 85  VAL A C     1 
ATOM   636  O  O     . VAL A 1 105 ? -7.315  -11.574 -4.614  1.00 10.63 ? 85  VAL A O     1 
ATOM   637  C  CB    . VAL A 1 105 ? -5.804  -11.489 -1.562  1.00 12.40 ? 85  VAL A CB    1 
ATOM   638  C  CG1   . VAL A 1 105 ? -5.972  -12.953 -1.923  1.00 13.31 ? 85  VAL A CG1   1 
ATOM   639  C  CG2   . VAL A 1 105 ? -4.392  -11.240 -1.033  1.00 13.58 ? 85  VAL A CG2   1 
ATOM   640  N  N     . ILE A 1 106 ? -8.521  -10.636 -2.979  1.00 10.43 ? 86  ILE A N     1 
ATOM   641  C  CA    . ILE A 1 106 ? -9.763  -10.995 -3.654  1.00 10.25 ? 86  ILE A CA    1 
ATOM   642  C  C     . ILE A 1 106 ? -9.837  -10.335 -5.028  1.00 10.04 ? 86  ILE A C     1 
ATOM   643  O  O     . ILE A 1 106 ? -10.227 -10.974 -6.011  1.00 10.22 ? 86  ILE A O     1 
ATOM   644  C  CB    . ILE A 1 106 ? -10.996 -10.698 -2.781  1.00 11.05 ? 86  ILE A CB    1 
ATOM   645  C  CG1   . ILE A 1 106 ? -11.009 -11.615 -1.553  1.00 12.03 ? 86  ILE A CG1   1 
ATOM   646  C  CG2   . ILE A 1 106 ? -12.264 -10.879 -3.604  1.00 11.76 ? 86  ILE A CG2   1 
ATOM   647  C  CD1   . ILE A 1 106 ? -11.971 -11.182 -0.438  1.00 13.60 ? 86  ILE A CD1   1 
ATOM   648  N  N     . LEU A 1 107 ? -9.474  -9.049  -5.126  1.00 10.24 ? 87  LEU A N     1 
ATOM   649  C  CA    . LEU A 1 107 ? -9.483  -8.362  -6.417  1.00 9.93  ? 87  LEU A CA    1 
ATOM   650  C  C     . LEU A 1 107 ? -8.604  -9.088  -7.427  1.00 9.75  ? 87  LEU A C     1 
ATOM   651  O  O     . LEU A 1 107 ? -8.995  -9.281  -8.589  1.00 10.27 ? 87  LEU A O     1 
ATOM   652  C  CB    . LEU A 1 107 ? -9.020  -6.920  -6.229  1.00 10.81 ? 87  LEU A CB    1 
ATOM   653  C  CG    . LEU A 1 107 ? -9.025  -6.045  -7.478  1.00 12.15 ? 87  LEU A CG    1 
ATOM   654  C  CD1   . LEU A 1 107 ? -10.434 -5.788  -7.955  1.00 13.22 ? 87  LEU A CD1   1 
ATOM   655  C  CD2   . LEU A 1 107 ? -8.326  -4.729  -7.185  1.00 13.08 ? 87  LEU A CD2   1 
ATOM   656  N  N     . SER A 1 108 ? -7.405  -9.483  -7.003  1.00 9.83  ? 88  SER A N     1 
ATOM   657  C  CA    . SER A 1 108 ? -6.499  -10.207 -7.888  1.00 10.46 ? 88  SER A CA    1 
ATOM   658  C  C     . SER A 1 108 ? -7.076  -11.542 -8.327  1.00 10.66 ? 88  SER A C     1 
ATOM   659  O  O     . SER A 1 108 ? -6.832  -11.971 -9.460  1.00 10.71 ? 88  SER A O     1 
ATOM   660  C  CB    . SER A 1 108 ? -5.126  -10.388 -7.238  1.00 10.85 ? 88  SER A CB    1 
ATOM   661  O  OG    . SER A 1 108 ? -5.122  -11.368 -6.215  1.00 11.14 ? 88  SER A OG    1 
ATOM   662  N  N     . GLN A 1 109 ? -7.829  -12.217 -7.459  1.00 10.04 ? 89  GLN A N     1 
ATOM   663  C  CA    . GLN A 1 109 ? -8.415  -13.507 -7.812  1.00 10.31 ? 89  GLN A CA    1 
ATOM   664  C  C     . GLN A 1 109 ? -9.618  -13.347 -8.745  1.00 10.22 ? 89  GLN A C     1 
ATOM   665  O  O     . GLN A 1 109 ? -9.789  -14.138 -9.687  1.00 10.68 ? 89  GLN A O     1 
ATOM   666  C  CB    . GLN A 1 109 ? -8.776  -14.289 -6.548  1.00 10.06 ? 89  GLN A CB    1 
ATOM   667  C  CG    . GLN A 1 109 ? -7.551  -14.647 -5.706  1.00 11.00 ? 89  GLN A CG    1 
ATOM   668  C  CD    . GLN A 1 109 ? -6.630  -15.645 -6.387  1.00 10.84 ? 89  GLN A CD    1 
ATOM   669  O  OE1   . GLN A 1 109 ? -7.081  -16.498 -7.159  1.00 11.62 ? 89  GLN A OE1   1 
ATOM   670  N  NE2   . GLN A 1 109 ? -5.330  -15.546 -6.116  1.00 11.34 ? 89  GLN A NE2   1 
ATOM   671  N  N     . LEU A 1 110 ? -10.453 -12.327 -8.507  1.00 10.08 ? 90  LEU A N     1 
ATOM   672  C  CA    . LEU A 1 110 ? -11.521 -11.993 -9.447  1.00 10.22 ? 90  LEU A CA    1 
ATOM   673  C  C     . LEU A 1 110 ? -10.956 -11.812 -10.849 1.00 10.31 ? 90  LEU A C     1 
ATOM   674  O  O     . LEU A 1 110 ? -11.470 -12.370 -11.826 1.00 11.14 ? 90  LEU A O     1 
ATOM   675  C  CB    . LEU A 1 110 ? -12.248 -10.719 -9.010  1.00 10.26 ? 90  LEU A CB    1 
ATOM   676  C  CG    . LEU A 1 110 ? -13.189 -10.792 -7.806  1.00 10.48 ? 90  LEU A CG    1 
ATOM   677  C  CD1   . LEU A 1 110 ? -13.579 -9.393  -7.363  1.00 11.24 ? 90  LEU A CD1   1 
ATOM   678  C  CD2   . LEU A 1 110 ? -14.420 -11.605 -8.133  1.00 10.75 ? 90  LEU A CD2   1 
ATOM   679  N  N     . PHE A 1 111 ? -9.888  -11.038 -10.968 1.00 10.17 ? 91  PHE A N     1 
ATOM   680  C  CA    . PHE A 1 111 ? -9.351  -10.777 -12.295 1.00 10.33 ? 91  PHE A CA    1 
ATOM   681  C  C     . PHE A 1 111 ? -8.486  -11.912 -12.815 1.00 10.52 ? 91  PHE A C     1 
ATOM   682  O  O     . PHE A 1 111 ? -8.390  -12.071 -14.033 1.00 11.22 ? 91  PHE A O     1 
ATOM   683  C  CB    . PHE A 1 111 ? -8.737  -9.381  -12.372 1.00 11.23 ? 91  PHE A CB    1 
ATOM   684  C  CG    . PHE A 1 111 ? -9.799  -8.323  -12.505 1.00 12.16 ? 91  PHE A CG    1 
ATOM   685  C  CD1   . PHE A 1 111 ? -10.543 -8.237  -13.674 1.00 12.44 ? 91  PHE A CD1   1 
ATOM   686  C  CD2   . PHE A 1 111 ? -10.130 -7.492  -11.459 1.00 13.98 ? 91  PHE A CD2   1 
ATOM   687  C  CE1   . PHE A 1 111 ? -11.562 -7.316  -13.809 1.00 13.82 ? 91  PHE A CE1   1 
ATOM   688  C  CE2   . PHE A 1 111 ? -11.150 -6.560  -11.600 1.00 15.85 ? 91  PHE A CE2   1 
ATOM   689  C  CZ    . PHE A 1 111 ? -11.861 -6.480  -12.776 1.00 15.53 ? 91  PHE A CZ    1 
ATOM   690  N  N     . ARG A 1 112 ? -7.924  -12.755 -11.943 1.00 10.90 ? 92  ARG A N     1 
ATOM   691  C  CA    . ARG A 1 112 ? -7.260  -13.954 -12.435 1.00 11.58 ? 92  ARG A CA    1 
ATOM   692  C  C     . ARG A 1 112 ? -8.250  -14.813 -13.205 1.00 11.16 ? 92  ARG A C     1 
ATOM   693  O  O     . ARG A 1 112 ? -7.966  -15.272 -14.313 1.00 11.63 ? 92  ARG A O     1 
ATOM   694  C  CB    . ARG A 1 112 ? -6.622  -14.749 -11.292 1.00 11.52 ? 92  ARG A CB    1 
ATOM   695  C  CG    . ARG A 1 112 ? -6.003  -16.053 -11.783 1.00 12.00 ? 92  ARG A CG    1 
ATOM   696  C  CD    . ARG A 1 112 ? -5.253  -16.783 -10.741 1.00 12.41 ? 92  ARG A CD    1 
ATOM   697  N  NE    . ARG A 1 112 ? -6.008  -17.370 -9.654  1.00 11.76 ? 92  ARG A NE    1 
ATOM   698  C  CZ    . ARG A 1 112 ? -6.298  -18.664 -9.543  1.00 11.99 ? 92  ARG A CZ    1 
ATOM   699  N  NH1   . ARG A 1 112 ? -6.075  -19.518 -10.537 1.00 12.99 ? 92  ARG A NH1   1 
ATOM   700  N  NH2   . ARG A 1 112 ? -6.826  -19.100 -8.412  1.00 12.54 ? 92  ARG A NH2   1 
ATOM   701  N  N     . GLY A 1 113 ? -9.421  -15.054 -12.625 1.00 11.61 ? 93  GLY A N     1 
ATOM   702  C  CA    . GLY A 1 113 ? -10.411 -15.876 -13.295 1.00 11.39 ? 93  GLY A CA    1 
ATOM   703  C  C     . GLY A 1 113 ? -10.977 -15.221 -14.541 1.00 11.22 ? 93  GLY A C     1 
ATOM   704  O  O     . GLY A 1 113 ? -11.187 -15.886 -15.557 1.00 12.22 ? 93  GLY A O     1 
ATOM   705  N  N     . PHE A 1 114 ? -11.224 -13.912 -14.477 1.00 10.98 ? 94  PHE A N     1 
ATOM   706  C  CA    . PHE A 1 114 ? -11.686 -13.158 -15.641 1.00 10.90 ? 94  PHE A CA    1 
ATOM   707  C  C     . PHE A 1 114 ? -10.705 -13.308 -16.798 1.00 10.83 ? 94  PHE A C     1 
ATOM   708  O  O     . PHE A 1 114 ? -11.086 -13.646 -17.926 1.00 11.96 ? 94  PHE A O     1 
ATOM   709  C  CB    . PHE A 1 114 ? -11.837 -11.685 -15.216 1.00 11.27 ? 94  PHE A CB    1 
ATOM   710  C  CG    . PHE A 1 114 ? -12.325 -10.742 -16.303 1.00 11.02 ? 94  PHE A CG    1 
ATOM   711  C  CD1   . PHE A 1 114 ? -11.498 -10.339 -17.348 1.00 11.69 ? 94  PHE A CD1   1 
ATOM   712  C  CD2   . PHE A 1 114 ? -13.595 -10.206 -16.230 1.00 11.58 ? 94  PHE A CD2   1 
ATOM   713  C  CE1   . PHE A 1 114 ? -11.957 -9.454  -18.319 1.00 12.40 ? 94  PHE A CE1   1 
ATOM   714  C  CE2   . PHE A 1 114 ? -14.051 -9.319  -17.191 1.00 12.36 ? 94  PHE A CE2   1 
ATOM   715  C  CZ    . PHE A 1 114 ? -13.226 -8.953  -18.237 1.00 12.64 ? 94  PHE A CZ    1 
ATOM   716  N  N     . CYS A 1 115 ? -9.425  -13.075 -16.529 1.00 10.87 ? 95  CYS A N     1 
ATOM   717  C  CA    . CYS A 1 115 ? -8.445  -13.070 -17.605 1.00 11.47 ? 95  CYS A CA    1 
ATOM   718  C  C     . CYS A 1 115 ? -8.169  -14.483 -18.109 1.00 11.66 ? 95  CYS A C     1 
ATOM   719  O  O     . CYS A 1 115 ? -7.989  -14.689 -19.317 1.00 12.30 ? 95  CYS A O     1 
ATOM   720  C  CB    . CYS A 1 115 ? -7.171  -12.371 -17.143 1.00 12.11 ? 95  CYS A CB    1 
ATOM   721  S  SG    . CYS A 1 115 ? -7.304  -10.621 -16.821 1.00 12.12 ? 95  CYS A SG    1 
ATOM   722  N  N     . LYS A 1 116 ? -8.170  -15.481 -17.218 1.00 11.90 ? 96  LYS A N     1 
ATOM   723  C  CA    . LYS A 1 116 ? -7.978  -16.853 -17.670 1.00 13.00 ? 96  LYS A CA    1 
ATOM   724  C  C     . LYS A 1 116 ? -9.044  -17.229 -18.689 1.00 13.23 ? 96  LYS A C     1 
ATOM   725  O  O     . LYS A 1 116 ? -8.771  -17.943 -19.661 1.00 14.25 ? 96  LYS A O     1 
ATOM   726  C  CB    . LYS A 1 116 ? -7.988  -17.808 -16.476 1.00 13.69 ? 96  LYS A CB    1 
ATOM   727  C  CG    . LYS A 1 116 ? -7.882  -19.278 -16.848 1.00 15.58 ? 96  LYS A CG    1 
ATOM   728  C  CD    . LYS A 1 116 ? -6.530  -19.608 -17.471 1.00 19.04 ? 96  LYS A CD    1 
ATOM   729  C  CE    . LYS A 1 116 ? -6.373  -21.099 -17.703 1.00 22.38 ? 96  LYS A CE    1 
ATOM   730  N  NZ    . LYS A 1 116 ? -5.070  -21.418 -18.353 1.00 24.77 ? 96  LYS A NZ    1 
ATOM   731  N  N     . ASN A 1 117 ? -10.266 -16.750 -18.482 1.00 12.72 ? 97  ASN A N     1 
ATOM   732  C  CA    . ASN A 1 117 ? -11.376 -17.105 -19.342 1.00 13.37 ? 97  ASN A CA    1 
ATOM   733  C  C     . ASN A 1 117 ? -11.210 -16.602 -20.766 1.00 14.52 ? 97  ASN A C     1 
ATOM   734  O  O     . ASN A 1 117 ? -11.853 -17.147 -21.669 1.00 16.71 ? 97  ASN A O     1 
ATOM   735  C  CB    . ASN A 1 117 ? -12.666 -16.532 -18.765 1.00 13.72 ? 97  ASN A CB    1 
ATOM   736  C  CG    . ASN A 1 117 ? -13.881 -17.194 -19.345 1.00 15.60 ? 97  ASN A CG    1 
ATOM   737  O  OD1   . ASN A 1 117 ? -14.043 -18.405 -19.237 1.00 17.74 ? 97  ASN A OD1   1 
ATOM   738  N  ND2   . ASN A 1 117 ? -14.741 -16.412 -19.973 1.00 16.03 ? 97  ASN A ND2   1 
ATOM   739  N  N     . ILE A 1 118 ? -10.384 -15.580 -20.986 1.00 13.95 ? 98  ILE A N     1 
ATOM   740  C  CA    . ILE A 1 118 ? -10.216 -14.965 -22.298 1.00 14.52 ? 98  ILE A CA    1 
ATOM   741  C  C     . ILE A 1 118 ? -8.801  -15.115 -22.833 1.00 14.27 ? 98  ILE A C     1 
ATOM   742  O  O     . ILE A 1 118 ? -8.449  -14.461 -23.816 1.00 14.91 ? 98  ILE A O     1 
ATOM   743  C  CB    . ILE A 1 118 ? -10.630 -13.480 -22.283 1.00 15.54 ? 98  ILE A CB    1 
ATOM   744  C  CG1   . ILE A 1 118 ? -9.717  -12.656 -21.355 1.00 16.01 ? 98  ILE A CG1   1 
ATOM   745  C  CG2   . ILE A 1 118 ? -12.077 -13.368 -21.886 1.00 17.86 ? 98  ILE A CG2   1 
ATOM   746  C  CD1   . ILE A 1 118 ? -9.979  -11.170 -21.374 1.00 17.20 ? 98  ILE A CD1   1 
ATOM   747  N  N     . GLU A 1 119 ? -8.002  -16.007 -22.243 1.00 15.65 ? 99  GLU A N     1 
ATOM   748  C  CA    A GLU A 1 119 ? -6.571  -16.044 -22.531 0.50 17.75 ? 99  GLU A CA    1 
ATOM   749  C  CA    B GLU A 1 119 ? -6.570  -16.026 -22.530 0.50 17.18 ? 99  GLU A CA    1 
ATOM   750  C  C     . GLU A 1 119 ? -6.265  -16.288 -24.002 1.00 18.30 ? 99  GLU A C     1 
ATOM   751  O  O     . GLU A 1 119 ? -5.218  -15.852 -24.494 1.00 19.47 ? 99  GLU A O     1 
ATOM   752  C  CB    A GLU A 1 119 ? -5.912  -17.143 -21.702 0.50 19.82 ? 99  GLU A CB    1 
ATOM   753  C  CB    B GLU A 1 119 ? -5.861  -17.051 -21.635 0.50 18.24 ? 99  GLU A CB    1 
ATOM   754  C  CG    A GLU A 1 119 ? -5.155  -16.631 -20.507 0.50 21.33 ? 99  GLU A CG    1 
ATOM   755  C  CG    B GLU A 1 119 ? -6.281  -18.504 -21.871 0.50 18.83 ? 99  GLU A CG    1 
ATOM   756  C  CD    A GLU A 1 119 ? -4.405  -17.728 -19.776 0.50 22.50 ? 99  GLU A CD    1 
ATOM   757  C  CD    B GLU A 1 119 ? -5.448  -19.521 -21.095 0.50 20.46 ? 99  GLU A CD    1 
ATOM   758  O  OE1   A GLU A 1 119 ? -3.811  -17.436 -18.718 0.50 22.54 ? 99  GLU A OE1   1 
ATOM   759  O  OE1   B GLU A 1 119 ? -4.389  -19.148 -20.547 0.50 21.24 ? 99  GLU A OE1   1 
ATOM   760  O  OE2   A GLU A 1 119 ? -4.402  -18.879 -20.262 0.50 23.36 ? 99  GLU A OE2   1 
ATOM   761  O  OE2   B GLU A 1 119 ? -5.848  -20.706 -21.043 0.50 21.11 ? 99  GLU A OE2   1 
ATOM   762  N  N     . SER A 1 120 ? -7.138  -16.987 -24.726 1.00 19.36 ? 100 SER A N     1 
ATOM   763  C  CA    A SER A 1 120 ? -6.882  -17.337 -26.119 0.50 20.71 ? 100 SER A CA    1 
ATOM   764  C  CA    B SER A 1 120 ? -6.860  -17.321 -26.118 0.50 20.56 ? 100 SER A CA    1 
ATOM   765  C  C     . SER A 1 120 ? -7.574  -16.413 -27.114 1.00 20.11 ? 100 SER A C     1 
ATOM   766  O  O     . SER A 1 120 ? -7.489  -16.653 -28.327 1.00 21.95 ? 100 SER A O     1 
ATOM   767  C  CB    A SER A 1 120 ? -7.319  -18.779 -26.388 0.50 22.69 ? 100 SER A CB    1 
ATOM   768  C  CB    B SER A 1 120 ? -7.196  -18.787 -26.394 0.50 22.29 ? 100 SER A CB    1 
ATOM   769  O  OG    A SER A 1 120 ? -8.731  -18.873 -26.390 0.50 23.97 ? 100 SER A OG    1 
ATOM   770  O  OG    B SER A 1 120 ? -6.415  -19.635 -25.576 0.50 23.25 ? 100 SER A OG    1 
ATOM   771  N  N     . GLU A 1 121 ? -8.250  -15.371 -26.641 1.00 17.27 ? 101 GLU A N     1 
ATOM   772  C  CA    . GLU A 1 121 ? -9.004  -14.483 -27.513 1.00 16.40 ? 101 GLU A CA    1 
ATOM   773  C  C     . GLU A 1 121 ? -8.175  -13.275 -27.918 1.00 16.01 ? 101 GLU A C     1 
ATOM   774  O  O     . GLU A 1 121 ? -7.315  -12.813 -27.167 1.00 16.37 ? 101 GLU A O     1 
ATOM   775  C  CB    . GLU A 1 121 ? -10.250 -13.955 -26.800 1.00 18.18 ? 101 GLU A CB    1 
ATOM   776  C  CG    . GLU A 1 121 ? -11.076 -15.004 -26.123 1.00 21.73 ? 101 GLU A CG    1 
ATOM   777  C  CD    . GLU A 1 121 ? -11.561 -16.057 -27.063 1.00 25.87 ? 101 GLU A CD    1 
ATOM   778  O  OE1   . GLU A 1 121 ? -11.903 -15.719 -28.219 1.00 26.68 ? 101 GLU A OE1   1 
ATOM   779  O  OE2   . GLU A 1 121 ? -11.601 -17.227 -26.629 1.00 28.79 ? 101 GLU A OE2   1 
ATOM   780  N  N     . SER A 1 122 ? -8.466  -12.745 -29.110 1.00 15.65 ? 102 SER A N     1 
ATOM   781  C  CA    . SER A 1 122 ? -7.925  -11.451 -29.515 1.00 15.98 ? 102 SER A CA    1 
ATOM   782  C  C     . SER A 1 122 ? -8.858  -10.300 -29.152 1.00 14.47 ? 102 SER A C     1 
ATOM   783  O  O     . SER A 1 122 ? -8.384  -9.207  -28.830 1.00 14.70 ? 102 SER A O     1 
ATOM   784  C  CB    . SER A 1 122 ? -7.614  -11.445 -31.016 1.00 18.47 ? 102 SER A CB    1 
ATOM   785  O  OG    . SER A 1 122 ? -8.744  -11.827 -31.768 1.00 20.82 ? 102 SER A OG    1 
ATOM   786  N  N     . GLU A 1 123 ? -10.171 -10.519 -29.205 1.00 14.36 ? 103 GLU A N     1 
ATOM   787  C  CA    . GLU A 1 123 ? -11.160 -9.546  -28.755 1.00 14.55 ? 103 GLU A CA    1 
ATOM   788  C  C     . GLU A 1 123 ? -12.349 -10.327 -28.223 1.00 14.57 ? 103 GLU A C     1 
ATOM   789  O  O     . GLU A 1 123 ? -12.522 -11.505 -28.542 1.00 16.37 ? 103 GLU A O     1 
ATOM   790  C  CB    . GLU A 1 123 ? -11.565 -8.555  -29.864 1.00 16.55 ? 103 GLU A CB    1 
ATOM   791  C  CG    . GLU A 1 123 ? -12.338 -9.136  -31.025 1.00 20.51 ? 103 GLU A CG    1 
ATOM   792  C  CD    . GLU A 1 123 ? -11.500 -10.045 -31.893 1.00 24.02 ? 103 GLU A CD    1 
ATOM   793  O  OE1   . GLU A 1 123 ? -11.970 -11.167 -32.178 1.00 26.52 ? 103 GLU A OE1   1 
ATOM   794  O  OE2   . GLU A 1 123 ? -10.379 -9.650  -32.293 1.00 24.53 ? 103 GLU A OE2   1 
ATOM   795  N  N     . ILE A 1 124 ? -13.171 -9.673  -27.403 1.00 13.60 ? 104 ILE A N     1 
ATOM   796  C  CA    . ILE A 1 124 ? -14.343 -10.331 -26.833 1.00 14.00 ? 104 ILE A CA    1 
ATOM   797  C  C     . ILE A 1 124 ? -15.599 -9.503  -27.072 1.00 13.69 ? 104 ILE A C     1 
ATOM   798  O  O     . ILE A 1 124 ? -15.551 -8.269  -27.158 1.00 15.29 ? 104 ILE A O     1 
ATOM   799  C  CB    . ILE A 1 124 ? -14.179 -10.661 -25.328 1.00 14.13 ? 104 ILE A CB    1 
ATOM   800  C  CG1   . ILE A 1 124 ? -14.125 -9.389  -24.477 1.00 13.97 ? 104 ILE A CG1   1 
ATOM   801  C  CG2   . ILE A 1 124 ? -12.938 -11.508 -25.112 1.00 15.12 ? 104 ILE A CG2   1 
ATOM   802  C  CD1   . ILE A 1 124 ? -14.034 -9.656  -22.986 1.00 14.39 ? 104 ILE A CD1   1 
ATOM   803  N  N     . ASN A 1 125 ? -16.740 -10.196 -27.152 1.00 14.24 ? 105 ASN A N     1 
ATOM   804  C  CA    . ASN A 1 125 ? -18.037 -9.555  -27.274 1.00 14.71 ? 105 ASN A CA    1 
ATOM   805  C  C     . ASN A 1 125 ? -18.689 -9.427  -25.894 1.00 13.80 ? 105 ASN A C     1 
ATOM   806  O  O     . ASN A 1 125 ? -18.110 -9.780  -24.855 1.00 13.87 ? 105 ASN A O     1 
ATOM   807  C  CB    . ASN A 1 125 ? -18.916 -10.291 -28.293 1.00 16.04 ? 105 ASN A CB    1 
ATOM   808  C  CG    . ASN A 1 125 ? -19.315 -11.682 -27.845 1.00 17.61 ? 105 ASN A CG    1 
ATOM   809  O  OD1   . ASN A 1 125 ? -19.157 -12.048 -26.691 1.00 17.54 ? 105 ASN A OD1   1 
ATOM   810  N  ND2   . ASN A 1 125 ? -19.857 -12.464 -28.768 1.00 19.53 ? 105 ASN A ND2   1 
ATOM   811  N  N     . SER A 1 126 ? -19.918 -8.905  -25.885 1.00 14.73 ? 106 SER A N     1 
ATOM   812  C  CA    . SER A 1 126 ? -20.587 -8.626  -24.615 1.00 14.89 ? 106 SER A CA    1 
ATOM   813  C  C     . SER A 1 126 ? -20.884 -9.906  -23.842 1.00 14.40 ? 106 SER A C     1 
ATOM   814  O  O     . SER A 1 126 ? -20.794 -9.924  -22.610 1.00 13.82 ? 106 SER A O     1 
ATOM   815  C  CB    . SER A 1 126 ? -21.870 -7.824  -24.841 1.00 16.00 ? 106 SER A CB    1 
ATOM   816  O  OG    . SER A 1 126 ? -22.783 -8.553  -25.640 1.00 17.18 ? 106 SER A OG    1 
ATOM   817  N  N     . LYS A 1 127 ? -21.247 -10.981 -24.536 1.00 15.06 ? 107 LYS A N     1 
ATOM   818  C  CA    . LYS A 1 127 ? -21.523 -12.240 -23.854 1.00 15.58 ? 107 LYS A CA    1 
ATOM   819  C  C     . LYS A 1 127 ? -20.268 -12.796 -23.188 1.00 14.64 ? 107 LYS A C     1 
ATOM   820  O  O     . LYS A 1 127 ? -20.322 -13.279 -22.049 1.00 14.48 ? 107 LYS A O     1 
ATOM   821  C  CB    . LYS A 1 127 ? -22.140 -13.236 -24.838 1.00 18.39 ? 107 LYS A CB    1 
ATOM   822  C  CG    . LYS A 1 127 ? -23.578 -12.863 -25.213 1.00 21.76 ? 107 LYS A CG    1 
ATOM   823  C  CD    . LYS A 1 127 ? -24.137 -13.724 -26.343 1.00 26.06 ? 107 LYS A CD    1 
ATOM   824  C  CE    . LYS A 1 127 ? -25.368 -13.088 -27.021 1.00 28.84 ? 107 LYS A CE    1 
ATOM   825  N  NZ    . LYS A 1 127 ? -25.250 -11.613 -27.302 1.00 31.12 ? 107 LYS A NZ    1 
ATOM   826  N  N     . LEU A 1 128 ? -19.123 -12.725 -23.871 1.00 14.12 ? 108 LEU A N     1 
ATOM   827  C  CA    . LEU A 1 128 ? -17.887 -13.218 -23.279 1.00 13.96 ? 108 LEU A CA    1 
ATOM   828  C  C     . LEU A 1 128 ? -17.398 -12.302 -22.161 1.00 12.92 ? 108 LEU A C     1 
ATOM   829  O  O     . LEU A 1 128 ? -16.804 -12.783 -21.188 1.00 13.22 ? 108 LEU A O     1 
ATOM   830  C  CB    . LEU A 1 128 ? -16.829 -13.400 -24.360 1.00 16.20 ? 108 LEU A CB    1 
ATOM   831  C  CG    . LEU A 1 128 ? -15.558 -14.152 -23.990 1.00 19.01 ? 108 LEU A CG    1 
ATOM   832  C  CD1   . LEU A 1 128 ? -15.831 -15.381 -23.141 1.00 20.33 ? 108 LEU A CD1   1 
ATOM   833  C  CD2   . LEU A 1 128 ? -14.874 -14.541 -25.284 1.00 20.37 ? 108 LEU A CD2   1 
ATOM   834  N  N     . LEU A 1 129 ? -17.634 -10.991 -22.265 1.00 12.69 ? 109 LEU A N     1 
ATOM   835  C  CA    . LEU A 1 129 ? -17.365 -10.098 -21.140 1.00 12.17 ? 109 LEU A CA    1 
ATOM   836  C  C     . LEU A 1 129 ? -18.136 -10.557 -19.906 1.00 12.07 ? 109 LEU A C     1 
ATOM   837  O  O     . LEU A 1 129 ? -17.568 -10.707 -18.815 1.00 11.83 ? 109 LEU A O     1 
ATOM   838  C  CB    . LEU A 1 129 ? -17.748 -8.667  -21.518 1.00 12.45 ? 109 LEU A CB    1 
ATOM   839  C  CG    . LEU A 1 129 ? -17.561 -7.623  -20.417 1.00 12.75 ? 109 LEU A CG    1 
ATOM   840  C  CD1   . LEU A 1 129 ? -16.107 -7.554  -19.968 1.00 13.26 ? 109 LEU A CD1   1 
ATOM   841  C  CD2   . LEU A 1 129 ? -18.051 -6.259  -20.871 1.00 13.93 ? 109 LEU A CD2   1 
ATOM   842  N  N     . ALA A 1 130 ? -19.437 -10.812 -20.069 1.00 12.56 ? 110 ALA A N     1 
ATOM   843  C  CA    . ALA A 1 130 ? -20.251 -11.248 -18.941 1.00 12.64 ? 110 ALA A CA    1 
ATOM   844  C  C     . ALA A 1 130 ? -19.756 -12.580 -18.386 1.00 12.51 ? 110 ALA A C     1 
ATOM   845  O  O     . ALA A 1 130 ? -19.655 -12.765 -17.163 1.00 12.45 ? 110 ALA A O     1 
ATOM   846  C  CB    . ALA A 1 130 ? -21.706 -11.345 -19.390 1.00 13.15 ? 110 ALA A CB    1 
ATOM   847  N  N     . GLU A 1 131 ? -19.464 -13.534 -19.269 1.00 12.59 ? 111 GLU A N     1 
ATOM   848  C  CA    . GLU A 1 131 ? -18.978 -14.836 -18.831 1.00 13.26 ? 111 GLU A CA    1 
ATOM   849  C  C     . GLU A 1 131 ? -17.661 -14.714 -18.077 1.00 12.45 ? 111 GLU A C     1 
ATOM   850  O  O     . GLU A 1 131 ? -17.393 -15.490 -17.147 1.00 12.82 ? 111 GLU A O     1 
ATOM   851  C  CB    . GLU A 1 131 ? -18.785 -15.750 -20.038 1.00 15.44 ? 111 GLU A CB    1 
ATOM   852  C  CG    . GLU A 1 131 ? -18.467 -17.176 -19.656 1.00 18.91 ? 111 GLU A CG    1 
ATOM   853  N  N     . SER A 1 132 ? -16.839 -13.734 -18.446 1.00 12.30 ? 112 SER A N     1 
ATOM   854  C  CA    . SER A 1 132 ? -15.548 -13.558 -17.796 1.00 12.22 ? 112 SER A CA    1 
ATOM   855  C  C     . SER A 1 132 ? -15.714 -12.967 -16.400 1.00 11.47 ? 112 SER A C     1 
ATOM   856  O  O     . SER A 1 132 ? -15.009 -13.368 -15.467 1.00 11.53 ? 112 SER A O     1 
ATOM   857  C  CB    . SER A 1 132 ? -14.638 -12.714 -18.686 1.00 12.93 ? 112 SER A CB    1 
ATOM   858  O  OG    . SER A 1 132 ? -14.447 -13.369 -19.939 1.00 14.05 ? 112 SER A OG    1 
ATOM   859  N  N     . PHE A 1 133 ? -16.657 -12.041 -16.219 1.00 10.98 ? 113 PHE A N     1 
ATOM   860  C  CA    . PHE A 1 133 ? -16.983 -11.614 -14.862 1.00 10.87 ? 113 PHE A CA    1 
ATOM   861  C  C     . PHE A 1 133 ? -17.403 -12.816 -14.013 1.00 10.86 ? 113 PHE A C     1 
ATOM   862  O  O     . PHE A 1 133 ? -16.960 -12.974 -12.873 1.00 10.79 ? 113 PHE A O     1 
ATOM   863  C  CB    . PHE A 1 133 ? -18.067 -10.532 -14.867 1.00 11.19 ? 113 PHE A CB    1 
ATOM   864  C  CG    . PHE A 1 133 ? -17.576 -9.149  -15.254 1.00 11.21 ? 113 PHE A CG    1 
ATOM   865  C  CD1   . PHE A 1 133 ? -16.594 -8.517  -14.504 1.00 11.90 ? 113 PHE A CD1   1 
ATOM   866  C  CD2   . PHE A 1 133 ? -18.111 -8.466  -16.349 1.00 11.73 ? 113 PHE A CD2   1 
ATOM   867  C  CE1   . PHE A 1 133 ? -16.155 -7.253  -14.829 1.00 12.37 ? 113 PHE A CE1   1 
ATOM   868  C  CE2   . PHE A 1 133 ? -17.674 -7.197  -16.669 1.00 12.09 ? 113 PHE A CE2   1 
ATOM   869  C  CZ    . PHE A 1 133 ? -16.693 -6.589  -15.906 1.00 12.49 ? 113 PHE A CZ    1 
ATOM   870  N  N     . GLN A 1 134 ? -18.272 -13.676 -14.550 1.00 11.11 ? 114 GLN A N     1 
ATOM   871  C  CA    . GLN A 1 134 ? -18.724 -14.840 -13.794 1.00 11.37 ? 114 GLN A CA    1 
ATOM   872  C  C     . GLN A 1 134 ? -17.569 -15.773 -13.459 1.00 11.16 ? 114 GLN A C     1 
ATOM   873  O  O     . GLN A 1 134 ? -17.493 -16.301 -12.344 1.00 11.85 ? 114 GLN A O     1 
ATOM   874  C  CB    . GLN A 1 134 ? -19.817 -15.561 -14.580 1.00 13.19 ? 114 GLN A CB    1 
ATOM   875  C  CG    . GLN A 1 134 ? -20.357 -16.800 -13.889 1.00 16.34 ? 114 GLN A CG    1 
ATOM   876  C  CD    . GLN A 1 134 ? -20.982 -16.495 -12.555 1.00 20.32 ? 114 GLN A CD    1 
ATOM   877  O  OE1   . GLN A 1 134 ? -21.621 -15.455 -12.385 1.00 22.16 ? 114 GLN A OE1   1 
ATOM   878  N  NE2   . GLN A 1 134 ? -20.813 -17.403 -11.596 1.00 22.71 ? 114 GLN A NE2   1 
ATOM   879  N  N     . ALA A 1 135 ? -16.669 -16.009 -14.414 1.00 11.73 ? 115 ALA A N     1 
ATOM   880  C  CA    . ALA A 1 135 ? -15.514 -16.863 -14.144 1.00 12.21 ? 115 ALA A CA    1 
ATOM   881  C  C     . ALA A 1 135 ? -14.674 -16.294 -13.009 1.00 11.20 ? 115 ALA A C     1 
ATOM   882  O  O     . ALA A 1 135 ? -14.159 -17.043 -12.168 1.00 12.25 ? 115 ALA A O     1 
ATOM   883  C  CB    . ALA A 1 135 ? -14.676 -17.033 -15.412 1.00 12.89 ? 115 ALA A CB    1 
ATOM   884  N  N     . GLY A 1 136 ? -14.536 -14.968 -12.964 1.00 11.27 ? 116 GLY A N     1 
ATOM   885  C  CA    . GLY A 1 136 ? -13.814 -14.343 -11.870 1.00 10.79 ? 116 GLY A CA    1 
ATOM   886  C  C     . GLY A 1 136 ? -14.480 -14.553 -10.527 1.00 10.37 ? 116 GLY A C     1 
ATOM   887  O  O     . GLY A 1 136 ? -13.804 -14.795 -9.527  1.00 10.73 ? 116 GLY A O     1 
ATOM   888  N  N     . VAL A 1 137 ? -15.809 -14.465 -10.481 1.00 10.29 ? 117 VAL A N     1 
ATOM   889  C  CA    . VAL A 1 137 ? -16.531 -14.734 -9.239  1.00 10.79 ? 117 VAL A CA    1 
ATOM   890  C  C     . VAL A 1 137 ? -16.232 -16.139 -8.740  1.00 10.70 ? 117 VAL A C     1 
ATOM   891  O  O     . VAL A 1 137 ? -16.001 -16.360 -7.542  1.00 11.42 ? 117 VAL A O     1 
ATOM   892  C  CB    . VAL A 1 137 ? -18.043 -14.520 -9.446  1.00 11.48 ? 117 VAL A CB    1 
ATOM   893  C  CG1   . VAL A 1 137 ? -18.834 -15.026 -8.259  1.00 12.60 ? 117 VAL A CG1   1 
ATOM   894  C  CG2   . VAL A 1 137 ? -18.332 -13.055 -9.697  1.00 11.74 ? 117 VAL A CG2   1 
ATOM   895  N  N     . GLU A 1 138 ? -16.271 -17.115 -9.643  1.00 11.28 ? 118 GLU A N     1 
ATOM   896  C  CA    A GLU A 1 138 ? -16.020 -18.493 -9.242  0.50 12.44 ? 118 GLU A CA    1 
ATOM   897  C  CA    B GLU A 1 138 ? -16.021 -18.491 -9.236  0.50 12.45 ? 118 GLU A CA    1 
ATOM   898  C  C     . GLU A 1 138 ? -14.616 -18.649 -8.674  1.00 11.90 ? 118 GLU A C     1 
ATOM   899  O  O     . GLU A 1 138 ? -14.424 -19.299 -7.639  1.00 12.66 ? 118 GLU A O     1 
ATOM   900  C  CB    A GLU A 1 138 ? -16.233 -19.429 -10.429 0.50 15.21 ? 118 GLU A CB    1 
ATOM   901  C  CB    B GLU A 1 138 ? -16.260 -19.425 -10.420 0.50 15.21 ? 118 GLU A CB    1 
ATOM   902  C  CG    A GLU A 1 138 ? -17.667 -19.470 -10.946 0.50 19.24 ? 118 GLU A CG    1 
ATOM   903  C  CG    B GLU A 1 138 ? -17.704 -19.405 -10.901 0.50 19.27 ? 118 GLU A CG    1 
ATOM   904  C  CD    A GLU A 1 138 ? -18.645 -20.098 -9.968  0.50 22.72 ? 118 GLU A CD    1 
ATOM   905  C  CD    B GLU A 1 138 ? -18.038 -20.543 -11.833 0.50 22.75 ? 118 GLU A CD    1 
ATOM   906  O  OE1   A GLU A 1 138 ? -18.203 -20.791 -9.028  0.50 24.00 ? 118 GLU A OE1   1 
ATOM   907  O  OE1   B GLU A 1 138 ? -17.370 -21.597 -11.756 0.50 24.13 ? 118 GLU A OE1   1 
ATOM   908  O  OE2   A GLU A 1 138 ? -19.866 -19.900 -10.154 0.50 24.47 ? 118 GLU A OE2   1 
ATOM   909  O  OE2   B GLU A 1 138 ? -18.977 -20.381 -12.643 0.50 24.41 ? 118 GLU A OE2   1 
ATOM   910  N  N     . THR A 1 139 ? -13.619 -18.068 -9.342  1.00 11.69 ? 119 THR A N     1 
ATOM   911  C  CA    . THR A 1 139 ? -12.246 -18.151 -8.853  1.00 11.48 ? 119 THR A CA    1 
ATOM   912  C  C     . THR A 1 139 ? -12.121 -17.530 -7.466  1.00 11.50 ? 119 THR A C     1 
ATOM   913  O  O     . THR A 1 139 ? -11.485 -18.100 -6.574  1.00 12.10 ? 119 THR A O     1 
ATOM   914  C  CB    . THR A 1 139 ? -11.310 -17.475 -9.862  1.00 11.99 ? 119 THR A CB    1 
ATOM   915  O  OG1   . THR A 1 139 ? -11.449 -18.125 -11.130 1.00 13.02 ? 119 THR A OG1   1 
ATOM   916  C  CG2   . THR A 1 139 ? -9.875  -17.526 -9.407  1.00 12.28 ? 119 THR A CG2   1 
ATOM   917  N  N     . ALA A 1 140 ? -12.712 -16.354 -7.268  1.00 11.40 ? 120 ALA A N     1 
ATOM   918  C  CA    . ALA A 1 140 ? -12.554 -15.651 -6.006  1.00 11.44 ? 120 ALA A CA    1 
ATOM   919  C  C     . ALA A 1 140 ? -13.247 -16.386 -4.869  1.00 11.16 ? 120 ALA A C     1 
ATOM   920  O  O     . ALA A 1 140 ? -12.696 -16.484 -3.766  1.00 12.06 ? 120 ALA A O     1 
ATOM   921  C  CB    . ALA A 1 140 ? -13.081 -14.226 -6.139  1.00 12.05 ? 120 ALA A CB    1 
ATOM   922  N  N     . TYR A 1 141 ? -14.465 -16.897 -5.098  1.00 11.79 ? 121 TYR A N     1 
ATOM   923  C  CA    . TYR A 1 141 ? -15.141 -17.651 -4.043  1.00 12.23 ? 121 TYR A CA    1 
ATOM   924  C  C     . TYR A 1 141 ? -14.328 -18.878 -3.644  1.00 12.96 ? 121 TYR A C     1 
ATOM   925  O  O     . TYR A 1 141 ? -14.216 -19.199 -2.455  1.00 14.66 ? 121 TYR A O     1 
ATOM   926  C  CB    . TYR A 1 141 ? -16.557 -18.066 -4.458  1.00 12.80 ? 121 TYR A CB    1 
ATOM   927  C  CG    . TYR A 1 141 ? -17.635 -17.108 -4.003  1.00 12.39 ? 121 TYR A CG    1 
ATOM   928  C  CD1   . TYR A 1 141 ? -17.960 -15.999 -4.759  1.00 11.93 ? 121 TYR A CD1   1 
ATOM   929  C  CD2   . TYR A 1 141 ? -18.318 -17.301 -2.808  1.00 13.30 ? 121 TYR A CD2   1 
ATOM   930  C  CE1   . TYR A 1 141 ? -18.938 -15.114 -4.350  1.00 12.49 ? 121 TYR A CE1   1 
ATOM   931  C  CE2   . TYR A 1 141 ? -19.297 -16.415 -2.391  1.00 13.76 ? 121 TYR A CE2   1 
ATOM   932  C  CZ    . TYR A 1 141 ? -19.604 -15.323 -3.173  1.00 13.10 ? 121 TYR A CZ    1 
ATOM   933  O  OH    . TYR A 1 141 ? -20.562 -14.412 -2.812  1.00 14.59 ? 121 TYR A OH    1 
ATOM   934  N  N     . LYS A 1 142 ? -13.745 -19.573 -4.626  1.00 12.71 ? 122 LYS A N     1 
ATOM   935  C  CA    . LYS A 1 142 ? -12.960 -20.763 -4.321  1.00 13.52 ? 122 LYS A CA    1 
ATOM   936  C  C     . LYS A 1 142 ? -11.674 -20.421 -3.573  1.00 13.44 ? 122 LYS A C     1 
ATOM   937  O  O     . LYS A 1 142 ? -11.169 -21.250 -2.809  1.00 14.91 ? 122 LYS A O     1 
ATOM   938  C  CB    . LYS A 1 142 ? -12.637 -21.538 -5.598  1.00 15.57 ? 122 LYS A CB    1 
ATOM   939  C  CG    . LYS A 1 142 ? -13.815 -22.245 -6.229  1.00 18.60 ? 122 LYS A CG    1 
ATOM   940  C  CD    . LYS A 1 142 ? -13.420 -22.913 -7.541  1.00 21.04 ? 122 LYS A CD    1 
ATOM   941  N  N     . ALA A 1 143 ? -11.133 -19.217 -3.788  1.00 12.89 ? 123 ALA A N     1 
ATOM   942  C  CA    . ALA A 1 143 ? -9.882  -18.799 -3.159  1.00 12.95 ? 123 ALA A CA    1 
ATOM   943  C  C     . ALA A 1 143 ? -10.039 -18.445 -1.684  1.00 13.06 ? 123 ALA A C     1 
ATOM   944  O  O     . ALA A 1 143 ? -9.053  -18.506 -0.945  1.00 13.90 ? 123 ALA A O     1 
ATOM   945  C  CB    . ALA A 1 143 ? -9.321  -17.583 -3.897  1.00 13.31 ? 123 ALA A CB    1 
ATOM   946  N  N     . VAL A 1 144 ? -11.235 -18.064 -1.253  1.00 13.59 ? 124 VAL A N     1 
ATOM   947  C  CA    . VAL A 1 144 ? -11.498 -17.621 0.110   1.00 13.29 ? 124 VAL A CA    1 
ATOM   948  C  C     . VAL A 1 144 ? -12.011 -18.818 0.898   1.00 14.42 ? 124 VAL A C     1 
ATOM   949  O  O     . VAL A 1 144 ? -13.059 -19.380 0.562   1.00 15.83 ? 124 VAL A O     1 
ATOM   950  C  CB    . VAL A 1 144 ? -12.516 -16.469 0.113   1.00 13.20 ? 124 VAL A CB    1 
ATOM   951  C  CG1   . VAL A 1 144 ? -12.868 -16.069 1.533   1.00 13.74 ? 124 VAL A CG1   1 
ATOM   952  C  CG2   . VAL A 1 144 ? -11.973 -15.277 -0.683  1.00 13.06 ? 124 VAL A CG2   1 
ATOM   953  N  N     . MET A 1 145 ? -11.293 -19.211 1.953   1.00 14.87 ? 125 MET A N     1 
ATOM   954  C  CA    . MET A 1 145 ? -11.662 -20.432 2.665   1.00 15.68 ? 125 MET A CA    1 
ATOM   955  C  C     . MET A 1 145 ? -13.033 -20.316 3.308   1.00 16.75 ? 125 MET A C     1 
ATOM   956  O  O     . MET A 1 145 ? -13.800 -21.285 3.316   1.00 18.60 ? 125 MET A O     1 
ATOM   957  C  CB    . MET A 1 145 ? -10.609 -20.783 3.716   1.00 15.34 ? 125 MET A CB    1 
ATOM   958  C  CG    . MET A 1 145 ? -9.393  -21.419 3.085   1.00 15.96 ? 125 MET A CG    1 
ATOM   959  S  SD    . MET A 1 145 ? -8.163  -21.944 4.277   1.00 17.06 ? 125 MET A SD    1 
ATOM   960  C  CE    . MET A 1 145 ? -7.536  -20.369 4.799   1.00 17.77 ? 125 MET A CE    1 
ATOM   961  N  N     . LYS A 1 146 ? -13.351 -19.154 3.878   1.00 16.64 ? 126 LYS A N     1 
ATOM   962  C  CA    . LYS A 1 146 ? -14.619 -18.922 4.566   1.00 18.23 ? 126 LYS A CA    1 
ATOM   963  C  C     . LYS A 1 146 ? -15.252 -17.640 4.041   1.00 16.81 ? 126 LYS A C     1 
ATOM   964  O  O     . LYS A 1 146 ? -15.202 -16.589 4.698   1.00 17.28 ? 126 LYS A O     1 
ATOM   965  C  CB    . LYS A 1 146 ? -14.404 -18.853 6.078   1.00 21.10 ? 126 LYS A CB    1 
ATOM   966  C  CG    . LYS A 1 146 ? -13.630 -20.030 6.664   1.00 24.70 ? 126 LYS A CG    1 
ATOM   967  C  CD    . LYS A 1 146 ? -14.449 -20.748 7.691   1.00 26.68 ? 126 LYS A CD    1 
ATOM   968  C  CE    . LYS A 1 146 ? -13.632 -21.779 8.426   1.00 28.59 ? 126 LYS A CE    1 
ATOM   969  N  NZ    . LYS A 1 146 ? -14.141 -23.141 8.147   1.00 30.14 ? 126 LYS A NZ    1 
ATOM   970  N  N     . PRO A 1 147 ? -15.886 -17.699 2.870   1.00 16.77 ? 127 PRO A N     1 
ATOM   971  C  CA    . PRO A 1 147 ? -16.547 -16.509 2.328   1.00 15.91 ? 127 PRO A CA    1 
ATOM   972  C  C     . PRO A 1 147 ? -17.658 -16.016 3.242   1.00 14.84 ? 127 PRO A C     1 
ATOM   973  O  O     . PRO A 1 147 ? -18.389 -16.806 3.847   1.00 16.65 ? 127 PRO A O     1 
ATOM   974  C  CB    . PRO A 1 147 ? -17.114 -16.996 0.988   1.00 17.38 ? 127 PRO A CB    1 
ATOM   975  C  CG    . PRO A 1 147 ? -16.407 -18.259 0.653   1.00 18.61 ? 127 PRO A CG    1 
ATOM   976  C  CD    . PRO A 1 147 ? -15.962 -18.859 1.955   1.00 18.05 ? 127 PRO A CD    1 
ATOM   977  N  N     . VAL A 1 148 ? -17.781 -14.693 3.324   1.00 13.30 ? 128 VAL A N     1 
ATOM   978  C  CA    . VAL A 1 148 ? -18.822 -14.012 4.088   1.00 13.35 ? 128 VAL A CA    1 
ATOM   979  C  C     . VAL A 1 148 ? -19.591 -13.123 3.119   1.00 12.58 ? 128 VAL A C     1 
ATOM   980  O  O     . VAL A 1 148 ? -18.995 -12.463 2.260   1.00 13.01 ? 128 VAL A O     1 
ATOM   981  C  CB    . VAL A 1 148 ? -18.178 -13.203 5.238   1.00 14.67 ? 128 VAL A CB    1 
ATOM   982  C  CG1   . VAL A 1 148 ? -19.173 -12.269 5.918   1.00 15.18 ? 128 VAL A CG1   1 
ATOM   983  C  CG2   . VAL A 1 148 ? -17.568 -14.168 6.262   1.00 15.76 ? 128 VAL A CG2   1 
ATOM   984  N  N     . GLU A 1 149 ? -20.916 -13.130 3.233   1.00 12.00 ? 129 GLU A N     1 
ATOM   985  C  CA    . GLU A 1 149 ? -21.778 -12.324 2.380   1.00 11.84 ? 129 GLU A CA    1 
ATOM   986  C  C     . GLU A 1 149 ? -21.905 -10.901 2.925   1.00 11.61 ? 129 GLU A C     1 
ATOM   987  O  O     . GLU A 1 149 ? -21.678 -10.631 4.115   1.00 12.36 ? 129 GLU A O     1 
ATOM   988  C  CB    . GLU A 1 149 ? -23.150 -12.973 2.217   1.00 13.54 ? 129 GLU A CB    1 
ATOM   989  C  CG    . GLU A 1 149 ? -23.086 -14.314 1.484   1.00 14.94 ? 129 GLU A CG    1 
ATOM   990  C  CD    . GLU A 1 149 ? -22.601 -14.198 0.042   1.00 16.98 ? 129 GLU A CD    1 
ATOM   991  O  OE1   . GLU A 1 149 ? -23.049 -13.278 -0.677  1.00 16.95 ? 129 GLU A OE1   1 
ATOM   992  O  OE2   . GLU A 1 149 ? -21.782 -15.042 -0.392  1.00 18.74 ? 129 GLU A OE2   1 
ATOM   993  N  N     . GLY A 1 150 ? -22.258 -9.982  2.031   1.00 11.24 ? 130 GLY A N     1 
ATOM   994  C  CA    . GLY A 1 150 ? -22.250 -8.569  2.347   1.00 11.31 ? 130 GLY A CA    1 
ATOM   995  C  C     . GLY A 1 150 ? -20.947 -7.889  2.014   1.00 10.92 ? 130 GLY A C     1 
ATOM   996  O  O     . GLY A 1 150 ? -20.640 -6.839  2.584   1.00 11.71 ? 130 GLY A O     1 
ATOM   997  N  N     . THR A 1 151 ? -20.183 -8.455  1.086   1.00 10.72 ? 131 THR A N     1 
ATOM   998  C  CA    . THR A 1 151 ? -18.795 -8.089  0.884   1.00 10.68 ? 131 THR A CA    1 
ATOM   999  C  C     . THR A 1 151 ? -18.496 -7.901  -0.602  1.00 10.41 ? 131 THR A C     1 
ATOM   1000 O  O     . THR A 1 151 ? -19.390 -7.957  -1.460  1.00 10.52 ? 131 THR A O     1 
ATOM   1001 C  CB    . THR A 1 151 ? -17.915 -9.233  1.390   1.00 11.61 ? 131 THR A CB    1 
ATOM   1002 O  OG1   . THR A 1 151 ? -18.259 -10.395 0.618   1.00 11.35 ? 131 THR A OG1   1 
ATOM   1003 C  CG2   . THR A 1 151 ? -18.092 -9.490  2.891   1.00 12.51 ? 131 THR A CG2   1 
ATOM   1004 N  N     . ILE A 1 152 ? -17.211 -7.734  -0.926  1.00 9.98  ? 132 ILE A N     1 
ATOM   1005 C  CA    . ILE A 1 152 ? -16.798 -7.636  -2.322  1.00 9.59  ? 132 ILE A CA    1 
ATOM   1006 C  C     . ILE A 1 152 ? -17.225 -8.874  -3.097  1.00 9.36  ? 132 ILE A C     1 
ATOM   1007 O  O     . ILE A 1 152 ? -17.523 -8.782  -4.293  1.00 9.98  ? 132 ILE A O     1 
ATOM   1008 C  CB    . ILE A 1 152 ? -15.277 -7.388  -2.395  1.00 9.99  ? 132 ILE A CB    1 
ATOM   1009 C  CG1   . ILE A 1 152 ? -14.839 -7.056  -3.834  1.00 10.56 ? 132 ILE A CG1   1 
ATOM   1010 C  CG2   . ILE A 1 152 ? -14.471 -8.575  -1.827  1.00 10.29 ? 132 ILE A CG2   1 
ATOM   1011 C  CD1   . ILE A 1 152 ? -13.364 -6.689  -3.942  1.00 10.84 ? 132 ILE A CD1   1 
ATOM   1012 N  N     . LEU A 1 153 ? -17.227 -10.050 -2.464  1.00 9.43  ? 133 LEU A N     1 
ATOM   1013 C  CA    . LEU A 1 153 ? -17.662 -11.262 -3.162  1.00 9.92  ? 133 LEU A CA    1 
ATOM   1014 C  C     . LEU A 1 153 ? -19.121 -11.159 -3.586  1.00 10.06 ? 133 LEU A C     1 
ATOM   1015 O  O     . LEU A 1 153 ? -19.475 -11.504 -4.719  1.00 10.42 ? 133 LEU A O     1 
ATOM   1016 C  CB    . LEU A 1 153 ? -17.464 -12.490 -2.278  1.00 10.69 ? 133 LEU A CB    1 
ATOM   1017 C  CG    . LEU A 1 153 ? -16.027 -12.939 -2.039  1.00 11.72 ? 133 LEU A CG    1 
ATOM   1018 C  CD1   . LEU A 1 153 ? -16.026 -14.218 -1.197  1.00 12.75 ? 133 LEU A CD1   1 
ATOM   1019 C  CD2   . LEU A 1 153 ? -15.273 -13.155 -3.344  1.00 13.13 ? 133 LEU A CD2   1 
ATOM   1020 N  N     . THR A 1 154 ? -19.982 -10.686 -2.688  1.00 10.02 ? 134 THR A N     1 
ATOM   1021 C  CA    . THR A 1 154 ? -21.400 -10.547 -2.994  1.00 10.79 ? 134 THR A CA    1 
ATOM   1022 C  C     . THR A 1 154 ? -21.611 -9.572  -4.143  1.00 10.24 ? 134 THR A C     1 
ATOM   1023 O  O     . THR A 1 154 ? -22.386 -9.836  -5.073  1.00 10.42 ? 134 THR A O     1 
ATOM   1024 C  CB    . THR A 1 154 ? -22.153 -10.036 -1.758  1.00 11.75 ? 134 THR A CB    1 
ATOM   1025 O  OG1   . THR A 1 154 ? -21.861 -10.866 -0.629  1.00 12.00 ? 134 THR A OG1   1 
ATOM   1026 C  CG2   . THR A 1 154 ? -23.650 -10.000 -2.009  1.00 13.97 ? 134 THR A CG2   1 
ATOM   1027 N  N     . VAL A 1 155 ? -20.952 -8.418  -4.077  1.00 10.14 ? 135 VAL A N     1 
ATOM   1028 C  CA    . VAL A 1 155 ? -21.113 -7.409  -5.116  1.00 10.22 ? 135 VAL A CA    1 
ATOM   1029 C  C     . VAL A 1 155 ? -20.644 -7.954  -6.457  1.00 9.89  ? 135 VAL A C     1 
ATOM   1030 O  O     . VAL A 1 155 ? -21.318 -7.787  -7.485  1.00 10.22 ? 135 VAL A O     1 
ATOM   1031 C  CB    . VAL A 1 155 ? -20.381 -6.113  -4.718  1.00 10.31 ? 135 VAL A CB    1 
ATOM   1032 C  CG1   . VAL A 1 155 ? -20.425 -5.070  -5.842  1.00 11.27 ? 135 VAL A CG1   1 
ATOM   1033 C  CG2   . VAL A 1 155 ? -20.981 -5.539  -3.427  1.00 10.95 ? 135 VAL A CG2   1 
ATOM   1034 N  N     . ALA A 1 156 ? -19.490 -8.629  -6.477  1.00 9.82  ? 136 ALA A N     1 
ATOM   1035 C  CA    . ALA A 1 156 ? -19.008 -9.214  -7.725  1.00 9.88  ? 136 ALA A CA    1 
ATOM   1036 C  C     . ALA A 1 156 ? -19.987 -10.251 -8.259  1.00 10.01 ? 136 ALA A C     1 
ATOM   1037 O  O     . ALA A 1 156 ? -20.242 -10.305 -9.469  1.00 10.15 ? 136 ALA A O     1 
ATOM   1038 C  CB    . ALA A 1 156 ? -17.621 -9.817  -7.509  1.00 10.41 ? 136 ALA A CB    1 
ATOM   1039 N  N     . LYS A 1 157 ? -20.507 -11.105 -7.375  1.00 10.19 ? 137 LYS A N     1 
ATOM   1040 C  CA    . LYS A 1 157 ? -21.449 -12.150 -7.773  1.00 10.33 ? 137 LYS A CA    1 
ATOM   1041 C  C     . LYS A 1 157 ? -22.714 -11.555 -8.382  1.00 10.67 ? 137 LYS A C     1 
ATOM   1042 O  O     . LYS A 1 157 ? -23.171 -11.986 -9.452  1.00 11.07 ? 137 LYS A O     1 
ATOM   1043 C  CB    . LYS A 1 157 ? -21.797 -12.991 -6.539  1.00 11.81 ? 137 LYS A CB    1 
ATOM   1044 C  CG    . LYS A 1 157 ? -22.811 -14.093 -6.792  1.00 14.39 ? 137 LYS A CG    1 
ATOM   1045 C  CD    . LYS A 1 157 ? -23.144 -14.872 -5.509  1.00 18.36 ? 137 LYS A CD    1 
ATOM   1046 C  CE    . LYS A 1 157 ? -23.619 -13.988 -4.322  1.00 22.17 ? 137 LYS A CE    1 
ATOM   1047 N  NZ    . LYS A 1 157 ? -24.944 -13.279 -4.496  1.00 24.68 ? 137 LYS A NZ    1 
ATOM   1048 N  N     . ASP A 1 158 ? -23.292 -10.556 -7.718  1.00 10.75 ? 138 ASP A N     1 
ATOM   1049 C  CA    . ASP A 1 158 ? -24.519 -9.943  -8.214  1.00 11.20 ? 138 ASP A CA    1 
ATOM   1050 C  C     . ASP A 1 158 ? -24.265 -9.191  -9.515  1.00 11.39 ? 138 ASP A C     1 
ATOM   1051 O  O     . ASP A 1 158 ? -25.110 -9.199  -10.424 1.00 12.17 ? 138 ASP A O     1 
ATOM   1052 C  CB    . ASP A 1 158 ? -25.105 -9.021  -7.141  1.00 11.56 ? 138 ASP A CB    1 
ATOM   1053 C  CG    . ASP A 1 158 ? -25.681 -9.781  -5.955  1.00 12.91 ? 138 ASP A CG    1 
ATOM   1054 O  OD1   . ASP A 1 158 ? -26.029 -10.972 -6.109  1.00 15.96 ? 138 ASP A OD1   1 
ATOM   1055 O  OD2   . ASP A 1 158 ? -25.791 -9.183  -4.862  1.00 12.95 ? 138 ASP A OD2   1 
ATOM   1056 N  N     . ALA A 1 159 ? -23.100 -8.553  -9.633  1.00 11.15 ? 139 ALA A N     1 
ATOM   1057 C  CA    . ALA A 1 159 ? -22.745 -7.871  -10.871 1.00 11.06 ? 139 ALA A CA    1 
ATOM   1058 C  C     . ALA A 1 159 ? -22.637 -8.855  -12.029 1.00 11.06 ? 139 ALA A C     1 
ATOM   1059 O  O     . ALA A 1 159 ? -23.089 -8.569  -13.146 1.00 11.84 ? 139 ALA A O     1 
ATOM   1060 C  CB    . ALA A 1 159 ? -21.422 -7.129  -10.682 1.00 11.93 ? 139 ALA A CB    1 
ATOM   1061 N  N     . ALA A 1 160 ? -22.023 -10.017 -11.793 1.00 10.96 ? 140 ALA A N     1 
ATOM   1062 C  CA    . ALA A 1 160 ? -21.821 -10.986 -12.865 1.00 11.51 ? 140 ALA A CA    1 
ATOM   1063 C  C     . ALA A 1 160 ? -23.135 -11.630 -13.283 1.00 11.85 ? 140 ALA A C     1 
ATOM   1064 O  O     . ALA A 1 160 ? -23.344 -11.913 -14.466 1.00 12.19 ? 140 ALA A O     1 
ATOM   1065 C  CB    . ALA A 1 160 ? -20.819 -12.043 -12.415 1.00 11.43 ? 140 ALA A CB    1 
ATOM   1066 N  N     . GLN A 1 161 ? -24.028 -11.891 -12.330 1.00 12.36 ? 141 GLN A N     1 
ATOM   1067 C  CA    . GLN A 1 161 ? -25.319 -12.456 -12.692 1.00 13.64 ? 141 GLN A CA    1 
ATOM   1068 C  C     . GLN A 1 161 ? -26.095 -11.477 -13.561 1.00 13.68 ? 141 GLN A C     1 
ATOM   1069 O  O     . GLN A 1 161 ? -26.715 -11.861 -14.564 1.00 14.68 ? 141 GLN A O     1 
ATOM   1070 C  CB    . GLN A 1 161 ? -26.103 -12.802 -11.429 1.00 15.66 ? 141 GLN A CB    1 
ATOM   1071 C  CG    . GLN A 1 161 ? -27.431 -13.463 -11.752 1.00 20.51 ? 141 GLN A CG    1 
ATOM   1072 C  CD    . GLN A 1 161 ? -27.246 -14.670 -12.653 1.00 26.24 ? 141 GLN A CD    1 
ATOM   1073 O  OE1   . GLN A 1 161 ? -26.298 -15.435 -12.477 1.00 29.65 ? 141 GLN A OE1   1 
ATOM   1074 N  NE2   . GLN A 1 161 ? -28.137 -14.842 -13.624 1.00 28.73 ? 141 GLN A NE2   1 
ATOM   1075 N  N     . ALA A 1 162 ? -26.061 -10.199 -13.192 1.00 13.37 ? 142 ALA A N     1 
ATOM   1076 C  CA    . ALA A 1 162 ? -26.677 -9.163  -14.009 1.00 13.82 ? 142 ALA A CA    1 
ATOM   1077 C  C     . ALA A 1 162 ? -26.042 -9.104  -15.394 1.00 13.44 ? 142 ALA A C     1 
ATOM   1078 O  O     . ALA A 1 162 ? -26.742 -8.974  -16.410 1.00 14.77 ? 142 ALA A O     1 
ATOM   1079 C  CB    . ALA A 1 162 ? -26.538 -7.821  -13.293 1.00 14.91 ? 142 ALA A CB    1 
ATOM   1080 N  N     . ALA A 1 163 ? -24.718 -9.217  -15.465 1.00 12.50 ? 143 ALA A N     1 
ATOM   1081 C  CA    . ALA A 1 163 ? -24.037 -9.163  -16.749 1.00 12.36 ? 143 ALA A CA    1 
ATOM   1082 C  C     . ALA A 1 163 ? -24.526 -10.269 -17.670 1.00 12.21 ? 143 ALA A C     1 
ATOM   1083 O  O     . ALA A 1 163 ? -24.791 -10.038 -18.856 1.00 13.03 ? 143 ALA A O     1 
ATOM   1084 C  CB    . ALA A 1 163 ? -22.532 -9.304  -16.530 1.00 12.73 ? 143 ALA A CB    1 
ATOM   1085 N  N     . ILE A 1 164 ? -24.626 -11.490 -17.146 1.00 12.28 ? 144 ILE A N     1 
ATOM   1086 C  CA    A ILE A 1 164 ? -25.039 -12.632 -17.960 0.50 13.88 ? 144 ILE A CA    1 
ATOM   1087 C  CA    B ILE A 1 164 ? -25.031 -12.618 -17.979 0.50 13.47 ? 144 ILE A CA    1 
ATOM   1088 C  C     . ILE A 1 164 ? -26.452 -12.420 -18.481 1.00 14.21 ? 144 ILE A C     1 
ATOM   1089 O  O     . ILE A 1 164 ? -26.751 -12.662 -19.656 1.00 15.45 ? 144 ILE A O     1 
ATOM   1090 C  CB    A ILE A 1 164 ? -24.937 -13.932 -17.138 0.50 15.44 ? 144 ILE A CB    1 
ATOM   1091 C  CB    B ILE A 1 164 ? -24.873 -13.940 -17.204 0.50 14.31 ? 144 ILE A CB    1 
ATOM   1092 C  CG1   A ILE A 1 164 ? -23.479 -14.250 -16.793 0.50 16.62 ? 144 ILE A CG1   1 
ATOM   1093 C  CG1   B ILE A 1 164 ? -23.393 -14.316 -17.103 0.50 14.92 ? 144 ILE A CG1   1 
ATOM   1094 C  CG2   A ILE A 1 164 ? -25.602 -15.106 -17.869 0.50 15.89 ? 144 ILE A CG2   1 
ATOM   1095 C  CG2   B ILE A 1 164 ? -25.697 -15.066 -17.850 0.50 15.06 ? 144 ILE A CG2   1 
ATOM   1096 C  CD1   A ILE A 1 164 ? -22.677 -14.770 -17.953 0.50 17.74 ? 144 ILE A CD1   1 
ATOM   1097 C  CD1   B ILE A 1 164 ? -23.128 -15.468 -16.176 0.50 15.23 ? 144 ILE A CD1   1 
ATOM   1098 N  N     . GLU A 1 165 ? -27.353 -11.983 -17.604 1.00 14.87 ? 145 GLU A N     1 
ATOM   1099 C  CA    . GLU A 1 165 ? -28.742 -11.807 -18.010 1.00 16.54 ? 145 GLU A CA    1 
ATOM   1100 C  C     . GLU A 1 165 ? -28.848 -10.765 -19.110 1.00 16.81 ? 145 GLU A C     1 
ATOM   1101 O  O     . GLU A 1 165 ? -29.550 -10.963 -20.109 1.00 18.39 ? 145 GLU A O     1 
ATOM   1102 C  CB    . GLU A 1 165 ? -29.585 -11.369 -16.814 1.00 18.39 ? 145 GLU A CB    1 
ATOM   1103 C  CG    . GLU A 1 165 ? -29.921 -12.464 -15.851 1.00 22.87 ? 145 GLU A CG    1 
ATOM   1104 C  CD    . GLU A 1 165 ? -30.825 -11.997 -14.728 1.00 26.63 ? 145 GLU A CD    1 
ATOM   1105 O  OE1   . GLU A 1 165 ? -31.566 -11.004 -14.923 1.00 27.51 ? 145 GLU A OE1   1 
ATOM   1106 O  OE2   . GLU A 1 165 ? -30.809 -12.648 -13.662 1.00 28.86 ? 145 GLU A OE2   1 
ATOM   1107 N  N     . LYS A 1 166 ? -28.159 -9.642  -18.937 1.00 16.25 ? 146 LYS A N     1 
ATOM   1108 C  CA    . LYS A 1 166 ? -28.291 -8.517  -19.854 1.00 16.83 ? 146 LYS A CA    1 
ATOM   1109 C  C     . LYS A 1 166 ? -27.593 -8.787  -21.178 1.00 16.98 ? 146 LYS A C     1 
ATOM   1110 O  O     . LYS A 1 166 ? -28.093 -8.392  -22.237 1.00 17.69 ? 146 LYS A O     1 
ATOM   1111 C  CB    . LYS A 1 166 ? -27.697 -7.275  -19.189 1.00 17.18 ? 146 LYS A CB    1 
ATOM   1112 C  CG    . LYS A 1 166 ? -27.790 -5.997  -20.007 1.00 18.95 ? 146 LYS A CG    1 
ATOM   1113 C  CD    . LYS A 1 166 ? -29.219 -5.493  -20.123 1.00 21.48 ? 146 LYS A CD    1 
ATOM   1114 C  CE    . LYS A 1 166 ? -29.238 -4.106  -20.731 1.00 23.72 ? 146 LYS A CE    1 
ATOM   1115 N  NZ    . LYS A 1 166 ? -30.607 -3.689  -21.117 1.00 26.02 ? 146 LYS A NZ    1 
ATOM   1116 N  N     . ALA A 1 167 ? -26.426 -9.432  -21.145 1.00 16.55 ? 147 ALA A N     1 
ATOM   1117 C  CA    . ALA A 1 167 ? -25.656 -9.634  -22.362 1.00 17.65 ? 147 ALA A CA    1 
ATOM   1118 C  C     . ALA A 1 167 ? -26.381 -10.544 -23.326 1.00 20.05 ? 147 ALA A C     1 
ATOM   1119 O  O     . ALA A 1 167 ? -26.127 -10.491 -24.530 1.00 20.72 ? 147 ALA A O     1 
ATOM   1120 C  CB    . ALA A 1 167 ? -24.291 -10.236 -22.037 1.00 17.15 ? 147 ALA A CB    1 
ATOM   1121 N  N     . ASN A 1 168 ? -27.291 -11.368 -22.826 1.00 22.28 ? 148 ASN A N     1 
ATOM   1122 C  CA    . ASN A 1 168 ? -28.008 -12.279 -23.701 1.00 25.30 ? 148 ASN A CA    1 
ATOM   1123 C  C     . ASN A 1 168 ? -28.855 -11.544 -24.728 1.00 26.59 ? 148 ASN A C     1 
ATOM   1124 O  O     . ASN A 1 168 ? -29.226 -12.146 -25.740 1.00 28.14 ? 148 ASN A O     1 
ATOM   1125 C  CB    . ASN A 1 168 ? -28.866 -13.192 -22.838 1.00 27.68 ? 148 ASN A CB    1 
ATOM   1126 C  CG    . ASN A 1 168 ? -29.463 -14.309 -23.609 1.00 30.19 ? 148 ASN A CG    1 
ATOM   1127 O  OD1   . ASN A 1 168 ? -28.826 -14.872 -24.493 1.00 31.92 ? 148 ASN A OD1   1 
ATOM   1128 N  ND2   . ASN A 1 168 ? -30.703 -14.652 -23.283 1.00 30.95 ? 148 ASN A ND2   1 
ATOM   1129 N  N     . ASN A 1 169 ? -29.166 -10.261 -24.505 1.00 26.68 ? 149 ASN A N     1 
ATOM   1130 C  CA    . ASN A 1 169 ? -29.951 -9.471  -25.448 1.00 27.60 ? 149 ASN A CA    1 
ATOM   1131 C  C     . ASN A 1 169 ? -29.336 -8.107  -25.745 1.00 25.64 ? 149 ASN A C     1 
ATOM   1132 O  O     . ASN A 1 169 ? -30.004 -7.255  -26.348 1.00 26.25 ? 149 ASN A O     1 
ATOM   1133 C  CB    . ASN A 1 169 ? -31.372 -9.277  -24.908 1.00 30.96 ? 149 ASN A CB    1 
ATOM   1134 C  CG    . ASN A 1 169 ? -31.379 -8.637  -23.534 1.00 33.64 ? 149 ASN A CG    1 
ATOM   1135 O  OD1   . ASN A 1 169 ? -31.307 -7.416  -23.410 1.00 34.43 ? 149 ASN A OD1   1 
ATOM   1136 N  ND2   . ASN A 1 169 ? -31.448 -9.462  -22.489 1.00 35.07 ? 149 ASN A ND2   1 
ATOM   1137 N  N     . THR A 1 170 ? -28.086 -7.876  -25.352 1.00 23.26 ? 150 THR A N     1 
ATOM   1138 C  CA    . THR A 1 170 ? -27.452 -6.566  -25.446 1.00 22.37 ? 150 THR A CA    1 
ATOM   1139 C  C     . THR A 1 170 ? -26.073 -6.757  -26.063 1.00 21.59 ? 150 THR A C     1 
ATOM   1140 O  O     . THR A 1 170 ? -25.162 -7.266  -25.402 1.00 22.23 ? 150 THR A O     1 
ATOM   1141 C  CB    . THR A 1 170 ? -27.335 -5.937  -24.054 1.00 22.27 ? 150 THR A CB    1 
ATOM   1142 O  OG1   . THR A 1 170 ? -28.635 -5.843  -23.458 1.00 22.85 ? 150 THR A OG1   1 
ATOM   1143 C  CG2   . THR A 1 170 ? -26.708 -4.553  -24.130 1.00 22.92 ? 150 THR A CG2   1 
ATOM   1144 N  N     . GLU A 1 171 ? -25.928 -6.356  -27.330 1.00 20.90 ? 151 GLU A N     1 
ATOM   1145 C  CA    . GLU A 1 171 ? -24.640 -6.432  -28.011 1.00 21.40 ? 151 GLU A CA    1 
ATOM   1146 C  C     . GLU A 1 171 ? -23.690 -5.322  -27.568 1.00 19.19 ? 151 GLU A C     1 
ATOM   1147 O  O     . GLU A 1 171 ? -22.473 -5.528  -27.550 1.00 18.92 ? 151 GLU A O     1 
ATOM   1148 C  CB    . GLU A 1 171 ? -24.858 -6.369  -29.529 1.00 25.10 ? 151 GLU A CB    1 
ATOM   1149 C  CG    . GLU A 1 171 ? -23.590 -6.455  -30.364 1.00 28.67 ? 151 GLU A CG    1 
ATOM   1150 C  CD    . GLU A 1 171 ? -23.842 -6.216  -31.854 1.00 31.35 ? 151 GLU A CD    1 
ATOM   1151 O  OE1   . GLU A 1 171 ? -25.018 -6.227  -32.283 1.00 32.51 ? 151 GLU A OE1   1 
ATOM   1152 O  OE2   . GLU A 1 171 ? -22.862 -6.006  -32.603 1.00 32.34 ? 151 GLU A OE2   1 
ATOM   1153 N  N     . ASP A 1 172 ? -24.213 -4.152  -27.209 1.00 17.81 ? 152 ASP A N     1 
ATOM   1154 C  CA    . ASP A 1 172 ? -23.372 -3.002  -26.908 1.00 17.22 ? 152 ASP A CA    1 
ATOM   1155 C  C     . ASP A 1 172 ? -22.742 -3.161  -25.527 1.00 15.63 ? 152 ASP A C     1 
ATOM   1156 O  O     . ASP A 1 172 ? -23.443 -3.230  -24.508 1.00 15.84 ? 152 ASP A O     1 
ATOM   1157 C  CB    . ASP A 1 172 ? -24.197 -1.721  -26.958 1.00 18.37 ? 152 ASP A CB    1 
ATOM   1158 C  CG    . ASP A 1 172 ? -23.409 -0.494  -26.523 1.00 19.25 ? 152 ASP A CG    1 
ATOM   1159 O  OD1   . ASP A 1 172 ? -24.059 0.472   -26.067 1.00 20.83 ? 152 ASP A OD1   1 
ATOM   1160 O  OD2   . ASP A 1 172 ? -22.159 -0.483  -26.649 1.00 18.64 ? 152 ASP A OD2   1 
ATOM   1161 N  N     . CYS A 1 173 ? -21.414 -3.191  -25.493 1.00 14.28 ? 153 CYS A N     1 
ATOM   1162 C  CA    . CYS A 1 173 ? -20.716 -3.329  -24.219 1.00 13.71 ? 153 CYS A CA    1 
ATOM   1163 C  C     . CYS A 1 173 ? -20.874 -2.097  -23.331 1.00 13.60 ? 153 CYS A C     1 
ATOM   1164 O  O     . CYS A 1 173 ? -20.752 -2.217  -22.108 1.00 13.75 ? 153 CYS A O     1 
ATOM   1165 C  CB    . CYS A 1 173 ? -19.239 -3.644  -24.446 1.00 14.11 ? 153 CYS A CB    1 
ATOM   1166 S  SG    . CYS A 1 173 ? -18.919 -5.274  -25.168 1.00 15.05 ? 153 CYS A SG    1 
ATOM   1167 N  N     . ILE A 1 174 ? -21.112 -0.910  -23.899 1.00 13.79 ? 154 ILE A N     1 
ATOM   1168 C  CA    . ILE A 1 174 ? -21.383 0.264   -23.063 1.00 14.77 ? 154 ILE A CA    1 
ATOM   1169 C  C     . ILE A 1 174 ? -22.684 0.070   -22.287 1.00 14.90 ? 154 ILE A C     1 
ATOM   1170 O  O     . ILE A 1 174 ? -22.724 0.188   -21.055 1.00 14.99 ? 154 ILE A O     1 
ATOM   1171 C  CB    . ILE A 1 174 ? -21.418 1.550   -23.914 1.00 15.36 ? 154 ILE A CB    1 
ATOM   1172 C  CG1   . ILE A 1 174 ? -20.040 1.839   -24.518 1.00 15.98 ? 154 ILE A CG1   1 
ATOM   1173 C  CG2   . ILE A 1 174 ? -21.901 2.735   -23.072 1.00 16.40 ? 154 ILE A CG2   1 
ATOM   1174 C  CD1   . ILE A 1 174 ? -20.033 2.941   -25.555 1.00 17.19 ? 154 ILE A CD1   1 
ATOM   1175 N  N     . GLU A 1 175 ? -23.768 -0.222  -23.005 1.00 15.76 ? 155 GLU A N     1 
ATOM   1176 C  CA    . GLU A 1 175 ? -25.056 -0.476  -22.374 1.00 16.46 ? 155 GLU A CA    1 
ATOM   1177 C  C     . GLU A 1 175 ? -24.952 -1.606  -21.359 1.00 15.51 ? 155 GLU A C     1 
ATOM   1178 O  O     . GLU A 1 175 ? -25.518 -1.528  -20.257 1.00 15.72 ? 155 GLU A O     1 
ATOM   1179 C  CB    . GLU A 1 175 ? -26.089 -0.814  -23.452 1.00 18.41 ? 155 GLU A CB    1 
ATOM   1180 C  CG    . GLU A 1 175 ? -27.492 -1.012  -22.917 1.00 20.69 ? 155 GLU A CG    1 
ATOM   1181 C  CD    . GLU A 1 175 ? -28.516 -1.376  -23.980 1.00 23.83 ? 155 GLU A CD    1 
ATOM   1182 O  OE1   . GLU A 1 175 ? -28.219 -1.253  -25.194 1.00 25.13 ? 155 GLU A OE1   1 
ATOM   1183 O  OE2   . GLU A 1 175 ? -29.626 -1.796  -23.577 1.00 25.29 ? 155 GLU A OE2   1 
ATOM   1184 N  N     . LEU A 1 176 ? -24.237 -2.675  -21.710 1.00 14.33 ? 156 LEU A N     1 
ATOM   1185 C  CA    . LEU A 1 176 ? -24.048 -3.765  -20.760 1.00 13.93 ? 156 LEU A CA    1 
ATOM   1186 C  C     . LEU A 1 176 ? -23.354 -3.274  -19.493 1.00 13.46 ? 156 LEU A C     1 
ATOM   1187 O  O     . LEU A 1 176 ? -23.803 -3.553  -18.372 1.00 13.56 ? 156 LEU A O     1 
ATOM   1188 C  CB    . LEU A 1 176 ? -23.241 -4.889  -21.405 1.00 14.20 ? 156 LEU A CB    1 
ATOM   1189 C  CG    . LEU A 1 176 ? -22.873 -6.040  -20.471 1.00 14.82 ? 156 LEU A CG    1 
ATOM   1190 C  CD1   . LEU A 1 176 ? -24.125 -6.681  -19.889 1.00 15.96 ? 156 LEU A CD1   1 
ATOM   1191 C  CD2   . LEU A 1 176 ? -21.992 -7.077  -21.148 1.00 15.62 ? 156 LEU A CD2   1 
ATOM   1192 N  N     . MET A 1 177 ? -22.236 -2.562  -19.645 1.00 12.85 ? 157 MET A N     1 
ATOM   1193 C  CA    . MET A 1 177 ? -21.477 -2.133  -18.475 1.00 12.68 ? 157 MET A CA    1 
ATOM   1194 C  C     . MET A 1 177 ? -22.288 -1.169  -17.619 1.00 12.65 ? 157 MET A C     1 
ATOM   1195 O  O     . MET A 1 177 ? -22.202 -1.205  -16.386 1.00 12.66 ? 157 MET A O     1 
ATOM   1196 C  CB    . MET A 1 177 ? -20.135 -1.530  -18.902 1.00 12.77 ? 157 MET A CB    1 
ATOM   1197 C  CG    . MET A 1 177 ? -19.141 -1.407  -17.762 1.00 13.05 ? 157 MET A CG    1 
ATOM   1198 S  SD    . MET A 1 177 ? -18.489 -3.020  -17.265 1.00 12.89 ? 157 MET A SD    1 
ATOM   1199 C  CE    . MET A 1 177 ? -18.337 -2.790  -15.499 1.00 13.25 ? 157 MET A CE    1 
ATOM   1200 N  N     . GLU A 1 178 ? -23.080 -0.297  -18.252 1.00 13.17 ? 158 GLU A N     1 
ATOM   1201 C  CA    . GLU A 1 178 ? -23.962 0.589   -17.497 1.00 14.16 ? 158 GLU A CA    1 
ATOM   1202 C  C     . GLU A 1 178 ? -24.905 -0.208  -16.619 1.00 14.14 ? 158 GLU A C     1 
ATOM   1203 O  O     . GLU A 1 178 ? -25.105 0.128   -15.446 1.00 14.43 ? 158 GLU A O     1 
ATOM   1204 C  CB    . GLU A 1 178 ? -24.752 1.478   -18.462 1.00 16.32 ? 158 GLU A CB    1 
ATOM   1205 C  CG    . GLU A 1 178 ? -23.917 2.640   -18.993 1.00 19.41 ? 158 GLU A CG    1 
ATOM   1206 C  CD    . GLU A 1 178 ? -24.541 3.403   -20.139 1.00 23.78 ? 158 GLU A CD    1 
ATOM   1207 O  OE1   . GLU A 1 178 ? -25.469 2.882   -20.792 1.00 25.38 ? 158 GLU A OE1   1 
ATOM   1208 O  OE2   . GLU A 1 178 ? -24.077 4.533   -20.400 1.00 25.97 ? 158 GLU A OE2   1 
ATOM   1209 N  N     . TYR A 1 179 ? -25.484 -1.274  -17.169 1.00 13.95 ? 159 TYR A N     1 
ATOM   1210 C  CA    . TYR A 1 179 ? -26.405 -2.111  -16.402 1.00 13.83 ? 159 TYR A CA    1 
ATOM   1211 C  C     . TYR A 1 179 ? -25.692 -2.847  -15.278 1.00 13.08 ? 159 TYR A C     1 
ATOM   1212 O  O     . TYR A 1 179 ? -26.223 -2.961  -14.162 1.00 13.51 ? 159 TYR A O     1 
ATOM   1213 C  CB    . TYR A 1 179 ? -27.069 -3.112  -17.344 1.00 14.59 ? 159 TYR A CB    1 
ATOM   1214 C  CG    . TYR A 1 179 ? -28.118 -3.980  -16.685 1.00 15.15 ? 159 TYR A CG    1 
ATOM   1215 C  CD1   . TYR A 1 179 ? -29.374 -3.475  -16.384 1.00 17.20 ? 159 TYR A CD1   1 
ATOM   1216 C  CD2   . TYR A 1 179 ? -27.853 -5.306  -16.365 1.00 14.95 ? 159 TYR A CD2   1 
ATOM   1217 C  CE1   . TYR A 1 179 ? -30.331 -4.262  -15.797 1.00 17.99 ? 159 TYR A CE1   1 
ATOM   1218 C  CE2   . TYR A 1 179 ? -28.816 -6.107  -15.780 1.00 15.63 ? 159 TYR A CE2   1 
ATOM   1219 C  CZ    . TYR A 1 179 ? -30.050 -5.576  -15.494 1.00 17.82 ? 159 TYR A CZ    1 
ATOM   1220 O  OH    . TYR A 1 179 ? -31.020 -6.364  -14.909 1.00 19.54 ? 159 TYR A OH    1 
ATOM   1221 N  N     . ILE A 1 180 ? -24.509 -3.386  -15.566 1.00 12.27 ? 160 ILE A N     1 
ATOM   1222 C  CA    . ILE A 1 180 ? -23.714 -4.027  -14.525 1.00 12.36 ? 160 ILE A CA    1 
ATOM   1223 C  C     . ILE A 1 180 ? -23.496 -3.075  -13.357 1.00 12.10 ? 160 ILE A C     1 
ATOM   1224 O  O     . ILE A 1 180 ? -23.605 -3.463  -12.188 1.00 12.48 ? 160 ILE A O     1 
ATOM   1225 C  CB    . ILE A 1 180 ? -22.377 -4.526  -15.103 1.00 12.03 ? 160 ILE A CB    1 
ATOM   1226 C  CG1   . ILE A 1 180 ? -22.617 -5.644  -16.122 1.00 12.33 ? 160 ILE A CG1   1 
ATOM   1227 C  CG2   . ILE A 1 180 ? -21.444 -4.989  -13.992 1.00 12.65 ? 160 ILE A CG2   1 
ATOM   1228 C  CD1   . ILE A 1 180 ? -21.369 -6.053  -16.885 1.00 13.24 ? 160 ILE A CD1   1 
ATOM   1229 N  N     . ILE A 1 181 ? -23.173 -1.817  -13.656 1.00 12.45 ? 161 ILE A N     1 
ATOM   1230 C  CA    . ILE A 1 181 ? -22.932 -0.838  -12.603 1.00 12.15 ? 161 ILE A CA    1 
ATOM   1231 C  C     . ILE A 1 181 ? -24.205 -0.547  -11.819 1.00 12.61 ? 161 ILE A C     1 
ATOM   1232 O  O     . ILE A 1 181 ? -24.167 -0.453  -10.587 1.00 12.64 ? 161 ILE A O     1 
ATOM   1233 C  CB    . ILE A 1 181 ? -22.273 0.430   -13.179 1.00 12.75 ? 161 ILE A CB    1 
ATOM   1234 C  CG1   . ILE A 1 181 ? -20.829 0.111   -13.584 1.00 13.39 ? 161 ILE A CG1   1 
ATOM   1235 C  CG2   . ILE A 1 181 ? -22.330 1.609   -12.201 1.00 13.53 ? 161 ILE A CG2   1 
ATOM   1236 C  CD1   . ILE A 1 181 ? -20.254 1.089   -14.574 1.00 14.28 ? 161 ILE A CD1   1 
ATOM   1237 N  N     . VAL A 1 182 ? -25.351 -0.418  -12.494 1.00 12.94 ? 162 VAL A N     1 
ATOM   1238 C  CA    . VAL A 1 182 ? -26.604 -0.223  -11.760 1.00 13.64 ? 162 VAL A CA    1 
ATOM   1239 C  C     . VAL A 1 182 ? -26.813 -1.362  -10.770 1.00 12.53 ? 162 VAL A C     1 
ATOM   1240 O  O     . VAL A 1 182 ? -27.133 -1.148  -9.591  1.00 13.29 ? 162 VAL A O     1 
ATOM   1241 C  CB    . VAL A 1 182 ? -27.798 -0.109  -12.729 1.00 15.65 ? 162 VAL A CB    1 
ATOM   1242 C  CG1   . VAL A 1 182 ? -29.121 -0.202  -11.961 1.00 17.01 ? 162 VAL A CG1   1 
ATOM   1243 C  CG2   . VAL A 1 182 ? -27.719 1.177   -13.517 1.00 17.17 ? 162 VAL A CG2   1 
ATOM   1244 N  N     . LYS A 1 183 ? -26.652 -2.597  -11.247 1.00 12.78 ? 163 LYS A N     1 
ATOM   1245 C  CA    . LYS A 1 183 ? -26.949 -3.750  -10.408 1.00 12.56 ? 163 LYS A CA    1 
ATOM   1246 C  C     . LYS A 1 183 ? -25.878 -3.969  -9.346  1.00 12.21 ? 163 LYS A C     1 
ATOM   1247 O  O     . LYS A 1 183 ? -26.184 -4.427  -8.233  1.00 12.82 ? 163 LYS A O     1 
ATOM   1248 C  CB    . LYS A 1 183 ? -27.154 -4.977  -11.289 1.00 13.67 ? 163 LYS A CB    1 
ATOM   1249 C  CG    . LYS A 1 183 ? -28.403 -4.860  -12.174 1.00 16.50 ? 163 LYS A CG    1 
ATOM   1250 C  CD    . LYS A 1 183 ? -29.636 -5.001  -11.308 1.00 19.95 ? 163 LYS A CD    1 
ATOM   1251 C  CE    . LYS A 1 183 ? -30.920 -4.758  -12.032 1.00 22.39 ? 163 LYS A CE    1 
ATOM   1252 N  NZ    . LYS A 1 183 ? -32.006 -4.806  -11.017 1.00 23.89 ? 163 LYS A NZ    1 
ATOM   1253 N  N     . ALA A 1 184 ? -24.624 -3.659  -9.663  1.00 11.53 ? 164 ALA A N     1 
ATOM   1254 C  CA    . ALA A 1 184 ? -23.568 -3.736  -8.662  1.00 11.54 ? 164 ALA A CA    1 
ATOM   1255 C  C     . ALA A 1 184 ? -23.797 -2.717  -7.555  1.00 11.40 ? 164 ALA A C     1 
ATOM   1256 O  O     . ALA A 1 184 ? -23.572 -3.006  -6.373  1.00 11.56 ? 164 ALA A O     1 
ATOM   1257 C  CB    . ALA A 1 184 ? -22.202 -3.522  -9.316  1.00 11.75 ? 164 ALA A CB    1 
ATOM   1258 N  N     . ASN A 1 185 ? -24.241 -1.514  -7.918  1.00 11.54 ? 165 ASN A N     1 
ATOM   1259 C  CA    . ASN A 1 185 ? -24.574 -0.525  -6.903  1.00 12.27 ? 165 ASN A CA    1 
ATOM   1260 C  C     . ASN A 1 185 ? -25.743 -0.971  -6.035  1.00 11.80 ? 165 ASN A C     1 
ATOM   1261 O  O     . ASN A 1 185 ? -25.730 -0.748  -4.822  1.00 12.36 ? 165 ASN A O     1 
ATOM   1262 C  CB    . ASN A 1 185 ? -24.860 0.821   -7.548  1.00 14.35 ? 165 ASN A CB    1 
ATOM   1263 C  CG    . ASN A 1 185 ? -23.615 1.656   -7.679  1.00 18.06 ? 165 ASN A CG    1 
ATOM   1264 O  OD1   . ASN A 1 185 ? -22.828 1.768   -6.727  1.00 19.45 ? 165 ASN A OD1   1 
ATOM   1265 N  ND2   . ASN A 1 185 ? -23.420 2.249   -8.846  1.00 20.41 ? 165 ASN A ND2   1 
ATOM   1266 N  N     . GLU A 1 186 ? -26.780 -1.569  -6.628  1.00 12.12 ? 166 GLU A N     1 
ATOM   1267 C  CA    . GLU A 1 186 ? -27.868 -2.095  -5.803  1.00 12.39 ? 166 GLU A CA    1 
ATOM   1268 C  C     . GLU A 1 186 ? -27.347 -3.124  -4.810  1.00 11.60 ? 166 GLU A C     1 
ATOM   1269 O  O     . GLU A 1 186 ? -27.704 -3.099  -3.624  1.00 12.28 ? 166 GLU A O     1 
ATOM   1270 C  CB    . GLU A 1 186 ? -28.964 -2.697  -6.679  1.00 13.78 ? 166 GLU A CB    1 
ATOM   1271 C  CG    . GLU A 1 186 ? -29.763 -1.630  -7.419  1.00 16.15 ? 166 GLU A CG    1 
ATOM   1272 C  CD    . GLU A 1 186 ? -30.750 -2.185  -8.424  1.00 19.56 ? 166 GLU A CD    1 
ATOM   1273 O  OE1   . GLU A 1 186 ? -30.911 -3.418  -8.500  1.00 20.69 ? 166 GLU A OE1   1 
ATOM   1274 O  OE2   . GLU A 1 186 ? -31.384 -1.372  -9.133  1.00 22.33 ? 166 GLU A OE2   1 
ATOM   1275 N  N     . SER A 1 187 ? -26.484 -4.026  -5.274  1.00 11.10 ? 167 SER A N     1 
ATOM   1276 C  CA    . SER A 1 187 ? -25.891 -5.018  -4.386  1.00 11.05 ? 167 SER A CA    1 
ATOM   1277 C  C     . SER A 1 187 ? -25.074 -4.354  -3.285  1.00 10.52 ? 167 SER A C     1 
ATOM   1278 O  O     . SER A 1 187 ? -25.194 -4.709  -2.103  1.00 10.99 ? 167 SER A O     1 
ATOM   1279 C  CB    . SER A 1 187 ? -25.037 -5.976  -5.216  1.00 11.81 ? 167 SER A CB    1 
ATOM   1280 O  OG    . SER A 1 187 ? -24.414 -6.943  -4.402  1.00 11.96 ? 167 SER A OG    1 
ATOM   1281 N  N     . LEU A 1 188 ? -24.250 -3.371  -3.646  1.00 10.75 ? 168 LEU A N     1 
ATOM   1282 C  CA    . LEU A 1 188 ? -23.456 -2.666  -2.652  1.00 10.77 ? 168 LEU A CA    1 
ATOM   1283 C  C     . LEU A 1 188 ? -24.342 -2.015  -1.598  1.00 10.38 ? 168 LEU A C     1 
ATOM   1284 O  O     . LEU A 1 188 ? -24.056 -2.087  -0.395  1.00 10.92 ? 168 LEU A O     1 
ATOM   1285 C  CB    . LEU A 1 188 ? -22.590 -1.624  -3.345  1.00 11.06 ? 168 LEU A CB    1 
ATOM   1286 C  CG    . LEU A 1 188 ? -21.687 -0.800  -2.428  1.00 11.99 ? 168 LEU A CG    1 
ATOM   1287 C  CD1   . LEU A 1 188 ? -20.728 -1.691  -1.644  1.00 12.09 ? 168 LEU A CD1   1 
ATOM   1288 C  CD2   . LEU A 1 188 ? -20.937 0.234   -3.244  1.00 13.47 ? 168 LEU A CD2   1 
ATOM   1289 N  N     . GLU A 1 189 ? -25.413 -1.353  -2.029  1.00 11.20 ? 169 GLU A N     1 
ATOM   1290 C  CA    . GLU A 1 189 ? -26.309 -0.715  -1.079  1.00 12.28 ? 169 GLU A CA    1 
ATOM   1291 C  C     . GLU A 1 189 ? -27.012 -1.727  -0.188  1.00 12.51 ? 169 GLU A C     1 
ATOM   1292 O  O     . GLU A 1 189 ? -27.456 -1.368  0.906   1.00 14.16 ? 169 GLU A O     1 
ATOM   1293 C  CB    . GLU A 1 189 ? -27.319 0.158   -1.821  1.00 14.04 ? 169 GLU A CB    1 
ATOM   1294 C  CG    . GLU A 1 189 ? -26.685 1.376   -2.496  1.00 17.66 ? 169 GLU A CG    1 
ATOM   1295 C  CD    . GLU A 1 189 ? -25.830 2.218   -1.545  1.00 23.24 ? 169 GLU A CD    1 
ATOM   1296 O  OE1   . GLU A 1 189 ? -26.340 2.616   -0.479  1.00 25.62 ? 169 GLU A OE1   1 
ATOM   1297 O  OE2   . GLU A 1 189 ? -24.643 2.473   -1.866  1.00 26.37 ? 169 GLU A OE2   1 
ATOM   1298 N  N     . ASN A 1 190 ? -27.111 -2.977  -0.617  1.00 11.87 ? 170 ASN A N     1 
ATOM   1299 C  CA    . ASN A 1 190 ? -27.711 -4.029  0.181   1.00 12.33 ? 170 ASN A CA    1 
ATOM   1300 C  C     . ASN A 1 190 ? -26.732 -4.697  1.136   1.00 11.52 ? 170 ASN A C     1 
ATOM   1301 O  O     . ASN A 1 190 ? -27.180 -5.457  2.009   1.00 12.14 ? 170 ASN A O     1 
ATOM   1302 C  CB    . ASN A 1 190 ? -28.315 -5.087  -0.750  1.00 13.68 ? 170 ASN A CB    1 
ATOM   1303 C  CG    . ASN A 1 190 ? -29.164 -6.094  -0.011  1.00 14.54 ? 170 ASN A CG    1 
ATOM   1304 O  OD1   . ASN A 1 190 ? -30.133 -5.732  0.639   1.00 15.65 ? 170 ASN A OD1   1 
ATOM   1305 N  ND2   . ASN A 1 190 ? -28.820 -7.360  -0.130  1.00 15.15 ? 170 ASN A ND2   1 
ATOM   1306 N  N     . THR A 1 191 ? -25.425 -4.453  1.006   1.00 10.97 ? 171 THR A N     1 
ATOM   1307 C  CA    . THR A 1 191 ? -24.459 -5.132  1.870   1.00 10.70 ? 171 THR A CA    1 
ATOM   1308 C  C     . THR A 1 191 ? -24.770 -4.981  3.357   1.00 11.01 ? 171 THR A C     1 
ATOM   1309 O  O     . THR A 1 191 ? -24.596 -5.969  4.093   1.00 11.24 ? 171 THR A O     1 
ATOM   1310 C  CB    . THR A 1 191 ? -22.988 -4.794  1.548   1.00 10.71 ? 171 THR A CB    1 
ATOM   1311 O  OG1   . THR A 1 191 ? -22.735 -3.387  1.621   1.00 11.02 ? 171 THR A OG1   1 
ATOM   1312 C  CG2   . THR A 1 191 ? -22.578 -5.317  0.180   1.00 11.24 ? 171 THR A CG2   1 
ATOM   1313 N  N     . PRO A 1 192 ? -25.231 -3.830  3.865   1.00 11.39 ? 172 PRO A N     1 
ATOM   1314 C  CA    . PRO A 1 192 ? -25.540 -3.761  5.304   1.00 11.97 ? 172 PRO A CA    1 
ATOM   1315 C  C     . PRO A 1 192 ? -26.662 -4.672  5.742   1.00 11.46 ? 172 PRO A C     1 
ATOM   1316 O  O     . PRO A 1 192 ? -26.772 -4.942  6.943   1.00 12.77 ? 172 PRO A O     1 
ATOM   1317 C  CB    . PRO A 1 192 ? -25.904 -2.289  5.532   1.00 13.19 ? 172 PRO A CB    1 
ATOM   1318 C  CG    . PRO A 1 192 ? -25.320 -1.546  4.358   1.00 13.66 ? 172 PRO A CG    1 
ATOM   1319 C  CD    . PRO A 1 192 ? -25.372 -2.515  3.209   1.00 12.32 ? 172 PRO A CD    1 
ATOM   1320 N  N     . ASN A 1 193 ? -27.504 -5.136  4.825   1.00 11.31 ? 173 ASN A N     1 
ATOM   1321 C  CA    . ASN A 1 193 ? -28.556 -6.081  5.173   1.00 11.30 ? 173 ASN A CA    1 
ATOM   1322 C  C     . ASN A 1 193 ? -28.060 -7.513  5.276   1.00 11.25 ? 173 ASN A C     1 
ATOM   1323 O  O     . ASN A 1 193 ? -28.824 -8.385  5.703   1.00 12.36 ? 173 ASN A O     1 
ATOM   1324 C  CB    . ASN A 1 193 ? -29.693 -5.991  4.169   1.00 12.22 ? 173 ASN A CB    1 
ATOM   1325 C  CG    . ASN A 1 193 ? -30.295 -4.621  4.127   1.00 13.88 ? 173 ASN A CG    1 
ATOM   1326 O  OD1   . ASN A 1 193 ? -30.515 -3.996  5.165   1.00 15.22 ? 173 ASN A OD1   1 
ATOM   1327 N  ND2   . ASN A 1 193 ? -30.530 -4.119  2.919   1.00 14.95 ? 173 ASN A ND2   1 
ATOM   1328 N  N     . LEU A 1 194 ? -26.804 -7.774  4.932   1.00 11.00 ? 174 LEU A N     1 
ATOM   1329 C  CA    . LEU A 1 194 ? -26.212 -9.099  5.045   1.00 10.96 ? 174 LEU A CA    1 
ATOM   1330 C  C     . LEU A 1 194 ? -25.153 -9.198  6.133   1.00 10.98 ? 174 LEU A C     1 
ATOM   1331 O  O     . LEU A 1 194 ? -24.942 -10.291 6.663   1.00 11.20 ? 174 LEU A O     1 
ATOM   1332 C  CB    . LEU A 1 194 ? -25.575 -9.484  3.703   1.00 11.15 ? 174 LEU A CB    1 
ATOM   1333 C  CG    . LEU A 1 194 ? -26.571 -9.814  2.589   1.00 11.65 ? 174 LEU A CG    1 
ATOM   1334 C  CD1   . LEU A 1 194 ? -25.934 -9.622  1.213   1.00 12.77 ? 174 LEU A CD1   1 
ATOM   1335 C  CD2   . LEU A 1 194 ? -27.082 -11.236 2.742   1.00 12.00 ? 174 LEU A CD2   1 
ATOM   1336 N  N     . LEU A 1 195 ? -24.470 -8.099  6.450   1.00 11.94 ? 175 LEU A N     1 
ATOM   1337 C  CA    . LEU A 1 195 ? -23.304 -8.091  7.332   1.00 12.66 ? 175 LEU A CA    1 
ATOM   1338 C  C     . LEU A 1 195 ? -23.599 -7.074  8.427   1.00 13.44 ? 175 LEU A C     1 
ATOM   1339 O  O     . LEU A 1 195 ? -23.650 -5.870  8.169   1.00 13.81 ? 175 LEU A O     1 
ATOM   1340 C  CB    . LEU A 1 195 ? -22.040 -7.756  6.525   1.00 13.19 ? 175 LEU A CB    1 
ATOM   1341 C  CG    . LEU A 1 195 ? -20.711 -7.694  7.270   1.00 13.72 ? 175 LEU A CG    1 
ATOM   1342 C  CD1   . LEU A 1 195 ? -20.431 -8.979  8.011   1.00 14.63 ? 175 LEU A CD1   1 
ATOM   1343 C  CD2   . LEU A 1 195 ? -19.575 -7.396  6.296   1.00 14.07 ? 175 LEU A CD2   1 
ATOM   1344 N  N     . ALA A 1 196 ? -23.803 -7.568  9.653   1.00 13.48 ? 176 ALA A N     1 
ATOM   1345 C  CA    . ALA A 1 196 ? -24.369 -6.740  10.717  1.00 14.19 ? 176 ALA A CA    1 
ATOM   1346 C  C     . ALA A 1 196 ? -23.530 -5.498  11.009  1.00 13.25 ? 176 ALA A C     1 
ATOM   1347 O  O     . ALA A 1 196 ? -24.082 -4.415  11.243  1.00 14.09 ? 176 ALA A O     1 
ATOM   1348 C  CB    . ALA A 1 196 ? -24.494 -7.569  11.992  1.00 15.62 ? 176 ALA A CB    1 
ATOM   1349 N  N     . VAL A 1 197 ? -22.204 -5.640  11.060  1.00 12.18 ? 177 VAL A N     1 
ATOM   1350 C  CA    . VAL A 1 197 ? -21.374 -4.509  11.459  1.00 12.19 ? 177 VAL A CA    1 
ATOM   1351 C  C     . VAL A 1 197 ? -21.559 -3.334  10.510  1.00 12.17 ? 177 VAL A C     1 
ATOM   1352 O  O     . VAL A 1 197 ? -21.449 -2.172  10.918  1.00 12.58 ? 177 VAL A O     1 
ATOM   1353 C  CB    . VAL A 1 197 ? -19.896 -4.931  11.604  1.00 13.74 ? 177 VAL A CB    1 
ATOM   1354 C  CG1   . VAL A 1 197 ? -19.298 -5.355  10.266  1.00 14.25 ? 177 VAL A CG1   1 
ATOM   1355 C  CG2   . VAL A 1 197 ? -19.066 -3.816  12.262  1.00 15.65 ? 177 VAL A CG2   1 
ATOM   1356 N  N     . LEU A 1 198 ? -21.817 -3.602  9.227   1.00 11.91 ? 178 LEU A N     1 
ATOM   1357 C  CA    . LEU A 1 198 ? -22.029 -2.513  8.280   1.00 12.04 ? 178 LEU A CA    1 
ATOM   1358 C  C     . LEU A 1 198 ? -23.266 -1.706  8.651   1.00 12.73 ? 178 LEU A C     1 
ATOM   1359 O  O     . LEU A 1 198 ? -23.252 -0.472  8.624   1.00 13.33 ? 178 LEU A O     1 
ATOM   1360 C  CB    . LEU A 1 198 ? -22.179 -3.078  6.870   1.00 11.89 ? 178 LEU A CB    1 
ATOM   1361 C  CG    . LEU A 1 198 ? -21.008 -3.873  6.305   1.00 11.57 ? 178 LEU A CG    1 
ATOM   1362 C  CD1   . LEU A 1 198 ? -21.342 -4.316  4.872   1.00 11.75 ? 178 LEU A CD1   1 
ATOM   1363 C  CD2   . LEU A 1 198 ? -19.731 -3.094  6.328   1.00 12.80 ? 178 LEU A CD2   1 
ATOM   1364 N  N     . LYS A 1 199 ? -24.360 -2.394  8.970   1.00 12.78 ? 179 LYS A N     1 
ATOM   1365 C  CA    . LYS A 1 199 ? -25.587 -1.708  9.361   1.00 13.99 ? 179 LYS A CA    1 
ATOM   1366 C  C     . LYS A 1 199 ? -25.418 -0.983  10.684  1.00 13.90 ? 179 LYS A C     1 
ATOM   1367 O  O     . LYS A 1 199 ? -25.900 0.143   10.843  1.00 14.88 ? 179 LYS A O     1 
ATOM   1368 C  CB    . LYS A 1 199 ? -26.724 -2.716  9.475   1.00 15.82 ? 179 LYS A CB    1 
ATOM   1369 C  CG    . LYS A 1 199 ? -28.071 -2.086  9.796   1.00 19.12 ? 179 LYS A CG    1 
ATOM   1370 C  CD    . LYS A 1 199 ? -29.230 -3.042  9.574   1.00 22.95 ? 179 LYS A CD    1 
ATOM   1371 C  CE    . LYS A 1 199 ? -29.735 -2.972  8.148   1.00 25.67 ? 179 LYS A CE    1 
ATOM   1372 N  NZ    . LYS A 1 199 ? -30.929 -3.852  7.917   1.00 26.92 ? 179 LYS A NZ    1 
ATOM   1373 N  N     . GLU A 1 200 ? -24.745 -1.617  11.647  1.00 13.53 ? 180 GLU A N     1 
ATOM   1374 C  CA    . GLU A 1 200 ? -24.592 -1.012  12.964  1.00 14.61 ? 180 GLU A CA    1 
ATOM   1375 C  C     . GLU A 1 200 ? -23.741 0.250   12.896  1.00 14.18 ? 180 GLU A C     1 
ATOM   1376 O  O     . GLU A 1 200 ? -24.041 1.249   13.566  1.00 14.72 ? 180 GLU A O     1 
ATOM   1377 C  CB    . GLU A 1 200 ? -23.999 -2.039  13.933  1.00 17.37 ? 180 GLU A CB    1 
ATOM   1378 C  CG    . GLU A 1 200 ? -24.932 -3.213  14.213  1.00 20.49 ? 180 GLU A CG    1 
ATOM   1379 C  CD    . GLU A 1 200 ? -24.220 -4.484  14.688  1.00 24.08 ? 180 GLU A CD    1 
ATOM   1380 O  OE1   . GLU A 1 200 ? -22.971 -4.590  14.611  1.00 26.22 ? 180 GLU A OE1   1 
ATOM   1381 O  OE2   . GLU A 1 200 ? -24.930 -5.395  15.146  1.00 25.19 ? 180 GLU A OE2   1 
ATOM   1382 N  N     . VAL A 1 201 ? -22.674 0.225   12.100  1.00 13.82 ? 181 VAL A N     1 
ATOM   1383 C  CA    . VAL A 1 201 ? -21.819 1.398   11.979  1.00 14.54 ? 181 VAL A CA    1 
ATOM   1384 C  C     . VAL A 1 201 ? -22.448 2.433   11.062  1.00 14.53 ? 181 VAL A C     1 
ATOM   1385 O  O     . VAL A 1 201 ? -22.320 3.637   11.301  1.00 17.20 ? 181 VAL A O     1 
ATOM   1386 C  CB    . VAL A 1 201 ? -20.409 0.995   11.514  1.00 14.47 ? 181 VAL A CB    1 
ATOM   1387 C  CG1   . VAL A 1 201 ? -19.578 2.233   11.229  1.00 15.77 ? 181 VAL A CG1   1 
ATOM   1388 C  CG2   . VAL A 1 201 ? -19.728 0.115   12.542  1.00 14.16 ? 181 VAL A CG2   1 
ATOM   1389 N  N     . GLY A 1 202 ? -23.122 1.986   10.002  1.00 14.46 ? 182 GLY A N     1 
ATOM   1390 C  CA    . GLY A 1 202 ? -23.741 2.866   9.036   1.00 15.05 ? 182 GLY A CA    1 
ATOM   1391 C  C     . GLY A 1 202 ? -22.951 3.078   7.759   1.00 15.05 ? 182 GLY A C     1 
ATOM   1392 O  O     . GLY A 1 202 ? -22.929 4.193   7.237   1.00 17.23 ? 182 GLY A O     1 
ATOM   1393 N  N     . VAL A 1 203 ? -22.314 2.027   7.237   1.00 13.63 ? 183 VAL A N     1 
ATOM   1394 C  CA    . VAL A 1 203 ? -21.531 2.104   6.007   1.00 13.24 ? 183 VAL A CA    1 
ATOM   1395 C  C     . VAL A 1 203 ? -21.891 0.942   5.092   1.00 12.78 ? 183 VAL A C     1 
ATOM   1396 O  O     . VAL A 1 203 ? -22.417 -0.076  5.532   1.00 14.45 ? 183 VAL A O     1 
ATOM   1397 C  CB    . VAL A 1 203 ? -20.012 2.082   6.290   1.00 14.02 ? 183 VAL A CB    1 
ATOM   1398 C  CG1   . VAL A 1 203 ? -19.589 3.334   7.032   1.00 15.15 ? 183 VAL A CG1   1 
ATOM   1399 C  CG2   . VAL A 1 203 ? -19.608 0.836   7.091   1.00 14.43 ? 183 VAL A CG2   1 
ATOM   1400 N  N     . VAL A 1 204 ? -21.583 1.095   3.803   1.00 12.04 ? 184 VAL A N     1 
ATOM   1401 C  CA    . VAL A 1 204 ? -21.582 -0.044  2.891   1.00 11.56 ? 184 VAL A CA    1 
ATOM   1402 C  C     . VAL A 1 204 ? -20.215 -0.724  2.956   1.00 11.25 ? 184 VAL A C     1 
ATOM   1403 O  O     . VAL A 1 204 ? -19.264 -0.197  3.546   1.00 12.32 ? 184 VAL A O     1 
ATOM   1404 C  CB    . VAL A 1 204 ? -21.947 0.351   1.448   1.00 12.32 ? 184 VAL A CB    1 
ATOM   1405 C  CG1   . VAL A 1 204 ? -23.346 0.968   1.412   1.00 13.31 ? 184 VAL A CG1   1 
ATOM   1406 C  CG2   . VAL A 1 204 ? -20.881 1.265   0.818   1.00 13.13 ? 184 VAL A CG2   1 
ATOM   1407 N  N     . ASP A 1 205 ? -20.088 -1.883  2.315   1.00 10.80 ? 185 ASP A N     1 
ATOM   1408 C  CA    . ASP A 1 205 ? -18.831 -2.610  2.359   1.00 11.02 ? 185 ASP A CA    1 
ATOM   1409 C  C     . ASP A 1 205 ? -17.727 -1.894  1.584   1.00 11.04 ? 185 ASP A C     1 
ATOM   1410 O  O     . ASP A 1 205 ? -17.890 -1.566  0.410   1.00 11.06 ? 185 ASP A O     1 
ATOM   1411 C  CB    . ASP A 1 205 ? -18.991 -4.001  1.767   1.00 10.78 ? 185 ASP A CB    1 
ATOM   1412 C  CG    . ASP A 1 205 ? -17.736 -4.798  1.933   1.00 11.25 ? 185 ASP A CG    1 
ATOM   1413 O  OD1   . ASP A 1 205 ? -17.375 -5.087  3.102   1.00 12.17 ? 185 ASP A OD1   1 
ATOM   1414 O  OD2   . ASP A 1 205 ? -17.089 -5.089  0.898   1.00 11.33 ? 185 ASP A OD2   1 
ATOM   1415 N  N     . SER A 1 206 ? -16.565 -1.741  2.214   1.00 10.82 ? 186 SER A N     1 
ATOM   1416 C  CA    A SER A 1 206 ? -15.472 -1.019  1.575   0.50 10.32 ? 186 SER A CA    1 
ATOM   1417 C  CA    B SER A 1 206 ? -15.449 -1.036  1.592   0.50 11.88 ? 186 SER A CA    1 
ATOM   1418 C  C     . SER A 1 206 ? -14.927 -1.771  0.364   1.00 10.45 ? 186 SER A C     1 
ATOM   1419 O  O     . SER A 1 206 ? -14.634 -1.155  -0.664  1.00 11.10 ? 186 SER A O     1 
ATOM   1420 C  CB    A SER A 1 206 ? -14.363 -0.739  2.592   0.50 9.88  ? 186 SER A CB    1 
ATOM   1421 C  CB    B SER A 1 206 ? -14.317 -0.890  2.607   0.50 14.51 ? 186 SER A CB    1 
ATOM   1422 O  OG    A SER A 1 206 ? -13.920 -1.934  3.232   0.50 9.01  ? 186 SER A OG    1 
ATOM   1423 O  OG    B SER A 1 206 ? -14.477 0.272   3.375   0.50 16.74 ? 186 SER A OG    1 
ATOM   1424 N  N     . GLY A 1 207 ? -14.740 -3.087  0.469   1.00 10.48 ? 187 GLY A N     1 
ATOM   1425 C  CA    . GLY A 1 207 ? -14.248 -3.834  -0.679  1.00 10.12 ? 187 GLY A CA    1 
ATOM   1426 C  C     . GLY A 1 207 ? -15.182 -3.713  -1.861  1.00 9.84  ? 187 GLY A C     1 
ATOM   1427 O  O     . GLY A 1 207 ? -14.746 -3.500  -2.996  1.00 10.40 ? 187 GLY A O     1 
ATOM   1428 N  N     . GLY A 1 208 ? -16.479 -3.840  -1.619  1.00 9.98  ? 188 GLY A N     1 
ATOM   1429 C  CA    . GLY A 1 208 ? -17.435 -3.663  -2.695  1.00 10.50 ? 188 GLY A CA    1 
ATOM   1430 C  C     . GLY A 1 208 ? -17.396 -2.273  -3.296  1.00 10.27 ? 188 GLY A C     1 
ATOM   1431 O  O     . GLY A 1 208 ? -17.539 -2.115  -4.510  1.00 10.55 ? 188 GLY A O     1 
ATOM   1432 N  N     . LYS A 1 209 ? -17.233 -1.246  -2.457  1.00 10.61 ? 189 LYS A N     1 
ATOM   1433 C  CA    . LYS A 1 209 ? -17.139 0.111   -2.978  1.00 11.11 ? 189 LYS A CA    1 
ATOM   1434 C  C     . LYS A 1 209 ? -15.910 0.268   -3.870  1.00 10.84 ? 189 LYS A C     1 
ATOM   1435 O  O     . LYS A 1 209 ? -15.984 0.879   -4.943  1.00 11.20 ? 189 LYS A O     1 
ATOM   1436 C  CB    . LYS A 1 209 ? -17.111 1.118   -1.824  1.00 11.73 ? 189 LYS A CB    1 
ATOM   1437 C  CG    . LYS A 1 209 ? -17.068 2.576   -2.282  1.00 13.94 ? 189 LYS A CG    1 
ATOM   1438 C  CD    . LYS A 1 209 ? -18.327 2.991   -3.004  1.00 17.91 ? 189 LYS A CD    1 
ATOM   1439 C  CE    . LYS A 1 209 ? -18.309 4.449   -3.409  1.00 21.83 ? 189 LYS A CE    1 
ATOM   1440 N  NZ    . LYS A 1 209 ? -19.624 4.814   -3.988  1.00 23.95 ? 189 LYS A NZ    1 
ATOM   1441 N  N     . GLY A 1 210 ? -14.773 -0.295  -3.461  1.00 10.47 ? 190 GLY A N     1 
ATOM   1442 C  CA    . GLY A 1 210 ? -13.593 -0.254  -4.317  1.00 10.63 ? 190 GLY A CA    1 
ATOM   1443 C  C     . GLY A 1 210 ? -13.821 -0.928  -5.656  1.00 10.09 ? 190 GLY A C     1 
ATOM   1444 O  O     . GLY A 1 210 ? -13.383 -0.431  -6.695  1.00 10.76 ? 190 GLY A O     1 
ATOM   1445 N  N     . LEU A 1 211 ? -14.490 -2.080  -5.647  1.00 10.13 ? 191 LEU A N     1 
ATOM   1446 C  CA    . LEU A 1 211 ? -14.801 -2.770  -6.894  1.00 10.19 ? 191 LEU A CA    1 
ATOM   1447 C  C     . LEU A 1 211 ? -15.678 -1.905  -7.793  1.00 10.27 ? 191 LEU A C     1 
ATOM   1448 O  O     . LEU A 1 211 ? -15.443 -1.820  -9.007  1.00 10.88 ? 191 LEU A O     1 
ATOM   1449 C  CB    . LEU A 1 211 ? -15.477 -4.106  -6.590  1.00 10.45 ? 191 LEU A CB    1 
ATOM   1450 C  CG    . LEU A 1 211 ? -15.717 -4.995  -7.801  1.00 10.85 ? 191 LEU A CG    1 
ATOM   1451 C  CD1   . LEU A 1 211 ? -14.403 -5.437  -8.451  1.00 11.87 ? 191 LEU A CD1   1 
ATOM   1452 C  CD2   . LEU A 1 211 ? -16.548 -6.203  -7.414  1.00 11.82 ? 191 LEU A CD2   1 
ATOM   1453 N  N     . LEU A 1 212 ? -16.689 -1.251  -7.221  1.00 10.58 ? 192 LEU A N     1 
ATOM   1454 C  CA    . LEU A 1 212 ? -17.532 -0.358  -8.007  1.00 11.28 ? 192 LEU A CA    1 
ATOM   1455 C  C     . LEU A 1 212 ? -16.704 0.743   -8.651  1.00 11.06 ? 192 LEU A C     1 
ATOM   1456 O  O     . LEU A 1 212 ? -16.946 1.117   -9.801  1.00 11.48 ? 192 LEU A O     1 
ATOM   1457 C  CB    . LEU A 1 212 ? -18.636 0.243   -7.136  1.00 12.73 ? 192 LEU A CB    1 
ATOM   1458 C  CG    . LEU A 1 212 ? -20.043 -0.330  -7.282  1.00 14.71 ? 192 LEU A CG    1 
ATOM   1459 C  CD1   . LEU A 1 212 ? -20.611 -0.057  -8.680  1.00 14.47 ? 192 LEU A CD1   1 
ATOM   1460 C  CD2   . LEU A 1 212 ? -19.983 -1.807  -6.948  1.00 15.38 ? 192 LEU A CD2   1 
ATOM   1461 N  N     . CYS A 1 213 ? -15.727 1.285   -7.928  1.00 11.40 ? 193 CYS A N     1 
ATOM   1462 C  CA    . CYS A 1 213 ? -14.891 2.332   -8.506  1.00 12.09 ? 193 CYS A CA    1 
ATOM   1463 C  C     . CYS A 1 213 ? -14.143 1.820   -9.728  1.00 11.15 ? 193 CYS A C     1 
ATOM   1464 O  O     . CYS A 1 213 ? -14.016 2.536   -10.732 1.00 11.67 ? 193 CYS A O     1 
ATOM   1465 C  CB    . CYS A 1 213 ? -13.916 2.864   -7.457  1.00 13.91 ? 193 CYS A CB    1 
ATOM   1466 S  SG    . CYS A 1 213 ? -14.691 3.765   -6.104  1.00 16.80 ? 193 CYS A SG    1 
ATOM   1467 N  N     . VAL A 1 214 ? -13.640 0.586   -9.671  1.00 10.55 ? 194 VAL A N     1 
ATOM   1468 C  CA    . VAL A 1 214 ? -12.986 0.007   -10.843 1.00 10.72 ? 194 VAL A CA    1 
ATOM   1469 C  C     . VAL A 1 214 ? -13.975 -0.098  -11.994 1.00 10.67 ? 194 VAL A C     1 
ATOM   1470 O  O     . VAL A 1 214 ? -13.676 0.291   -13.130 1.00 11.09 ? 194 VAL A O     1 
ATOM   1471 C  CB    . VAL A 1 214 ? -12.357 -1.354  -10.490 1.00 11.02 ? 194 VAL A CB    1 
ATOM   1472 C  CG1   . VAL A 1 214 ? -11.850 -2.069  -11.729 1.00 11.94 ? 194 VAL A CG1   1 
ATOM   1473 C  CG2   . VAL A 1 214 ? -11.237 -1.175  -9.469  1.00 11.75 ? 194 VAL A CG2   1 
ATOM   1474 N  N     . TYR A 1 215 ? -15.175 -0.617  -11.718 1.00 10.26 ? 195 TYR A N     1 
ATOM   1475 C  CA    . TYR A 1 215 ? -16.170 -0.793  -12.771 1.00 10.63 ? 195 TYR A CA    1 
ATOM   1476 C  C     . TYR A 1 215 ? -16.572 0.538   -13.400 1.00 10.89 ? 195 TYR A C     1 
ATOM   1477 O  O     . TYR A 1 215 ? -16.793 0.612   -14.617 1.00 11.32 ? 195 TYR A O     1 
ATOM   1478 C  CB    . TYR A 1 215 ? -17.390 -1.509  -12.196 1.00 10.64 ? 195 TYR A CB    1 
ATOM   1479 C  CG    . TYR A 1 215 ? -17.205 -2.985  -11.880 1.00 11.28 ? 195 TYR A CG    1 
ATOM   1480 C  CD1   . TYR A 1 215 ? -16.022 -3.666  -12.158 1.00 11.52 ? 195 TYR A CD1   1 
ATOM   1481 C  CD2   . TYR A 1 215 ? -18.233 -3.698  -11.291 1.00 12.13 ? 195 TYR A CD2   1 
ATOM   1482 C  CE1   . TYR A 1 215 ? -15.885 -5.021  -11.859 1.00 12.28 ? 195 TYR A CE1   1 
ATOM   1483 C  CE2   . TYR A 1 215 ? -18.106 -5.053  -10.992 1.00 12.91 ? 195 TYR A CE2   1 
ATOM   1484 C  CZ    . TYR A 1 215 ? -16.936 -5.713  -11.283 1.00 12.63 ? 195 TYR A CZ    1 
ATOM   1485 O  OH    . TYR A 1 215 ? -16.817 -7.058  -10.972 1.00 13.63 ? 195 TYR A OH    1 
ATOM   1486 N  N     . GLU A 1 216 ? -16.703 1.592   -12.592 1.00 11.07 ? 196 GLU A N     1 
ATOM   1487 C  CA    . GLU A 1 216 ? -17.029 2.905   -13.140 1.00 12.14 ? 196 GLU A CA    1 
ATOM   1488 C  C     . GLU A 1 216 ? -15.948 3.383   -14.106 1.00 12.22 ? 196 GLU A C     1 
ATOM   1489 O  O     . GLU A 1 216 ? -16.250 3.995   -15.139 1.00 12.80 ? 196 GLU A O     1 
ATOM   1490 C  CB    . GLU A 1 216 ? -17.247 3.902   -12.003 1.00 14.67 ? 196 GLU A CB    1 
ATOM   1491 C  CG    . GLU A 1 216 ? -18.538 3.646   -11.222 1.00 18.63 ? 196 GLU A CG    1 
ATOM   1492 C  CD    . GLU A 1 216 ? -18.561 4.319   -9.863  1.00 25.19 ? 196 GLU A CD    1 
ATOM   1493 O  OE1   . GLU A 1 216 ? -17.543 4.942   -9.485  1.00 27.71 ? 196 GLU A OE1   1 
ATOM   1494 O  OE2   . GLU A 1 216 ? -19.597 4.235   -9.168  1.00 28.49 ? 196 GLU A OE2   1 
ATOM   1495 N  N     . GLY A 1 217 ? -14.684 3.109   -13.797 1.00 11.49 ? 197 GLY A N     1 
ATOM   1496 C  CA    . GLY A 1 217 ? -13.622 3.421   -14.739 1.00 11.57 ? 197 GLY A CA    1 
ATOM   1497 C  C     . GLY A 1 217 ? -13.672 2.574   -15.998 1.00 11.19 ? 197 GLY A C     1 
ATOM   1498 O  O     . GLY A 1 217 ? -13.366 3.064   -17.092 1.00 12.24 ? 197 GLY A O     1 
ATOM   1499 N  N     . PHE A 1 218 ? -14.041 1.295   -15.870 1.00 11.06 ? 198 PHE A N     1 
ATOM   1500 C  CA    . PHE A 1 218 ? -14.243 0.463   -17.052 1.00 11.08 ? 198 PHE A CA    1 
ATOM   1501 C  C     . PHE A 1 218 ? -15.227 1.147   -18.002 1.00 11.17 ? 198 PHE A C     1 
ATOM   1502 O  O     . PHE A 1 218 ? -15.020 1.183   -19.216 1.00 11.58 ? 198 PHE A O     1 
ATOM   1503 C  CB    . PHE A 1 218 ? -14.810 -0.911  -16.655 1.00 11.16 ? 198 PHE A CB    1 
ATOM   1504 C  CG    . PHE A 1 218 ? -13.796 -1.926  -16.158 1.00 11.35 ? 198 PHE A CG    1 
ATOM   1505 C  CD1   . PHE A 1 218 ? -12.514 -1.584  -15.765 1.00 11.44 ? 198 PHE A CD1   1 
ATOM   1506 C  CD2   . PHE A 1 218 ? -14.165 -3.256  -16.084 1.00 12.63 ? 198 PHE A CD2   1 
ATOM   1507 C  CE1   . PHE A 1 218 ? -11.617 -2.558  -15.339 1.00 12.24 ? 198 PHE A CE1   1 
ATOM   1508 C  CE2   . PHE A 1 218 ? -13.286 -4.223  -15.646 1.00 13.45 ? 198 PHE A CE2   1 
ATOM   1509 C  CZ    . PHE A 1 218 ? -12.010 -3.868  -15.279 1.00 12.86 ? 198 PHE A CZ    1 
ATOM   1510 N  N     . LEU A 1 219 ? -16.337 1.655   -17.462 1.00 11.77 ? 199 LEU A N     1 
ATOM   1511 C  CA    . LEU A 1 219 ? -17.347 2.292   -18.301 1.00 11.90 ? 199 LEU A CA    1 
ATOM   1512 C  C     . LEU A 1 219 ? -16.785 3.521   -18.997 1.00 11.97 ? 199 LEU A C     1 
ATOM   1513 O  O     . LEU A 1 219 ? -17.033 3.735   -20.191 1.00 12.69 ? 199 LEU A O     1 
ATOM   1514 C  CB    . LEU A 1 219 ? -18.561 2.653   -17.456 1.00 12.64 ? 199 LEU A CB    1 
ATOM   1515 C  CG    . LEU A 1 219 ? -19.658 3.409   -18.197 1.00 14.83 ? 199 LEU A CG    1 
ATOM   1516 C  CD1   . LEU A 1 219 ? -20.185 2.614   -19.384 1.00 15.89 ? 199 LEU A CD1   1 
ATOM   1517 C  CD2   . LEU A 1 219 ? -20.786 3.771   -17.235 1.00 15.70 ? 199 LEU A CD2   1 
ATOM   1518 N  N     . LYS A 1 220 ? -16.044 4.362   -18.270 1.00 12.46 ? 200 LYS A N     1 
ATOM   1519 C  CA    A LYS A 1 220 ? -15.442 5.534   -18.900 0.50 13.31 ? 200 LYS A CA    1 
ATOM   1520 C  CA    B LYS A 1 220 ? -15.453 5.534   -18.909 0.50 13.34 ? 200 LYS A CA    1 
ATOM   1521 C  C     . LYS A 1 220 ? -14.599 5.131   -20.103 1.00 12.72 ? 200 LYS A C     1 
ATOM   1522 O  O     . LYS A 1 220 ? -14.689 5.741   -21.180 1.00 13.09 ? 200 LYS A O     1 
ATOM   1523 C  CB    A LYS A 1 220 ? -14.594 6.297   -17.885 0.50 15.34 ? 200 LYS A CB    1 
ATOM   1524 C  CB    B LYS A 1 220 ? -14.635 6.327   -17.895 0.50 15.44 ? 200 LYS A CB    1 
ATOM   1525 C  CG    A LYS A 1 220 ? -15.399 6.978   -16.802 0.50 17.81 ? 200 LYS A CG    1 
ATOM   1526 C  CG    B LYS A 1 220 ? -15.484 7.024   -16.852 0.50 17.94 ? 200 LYS A CG    1 
ATOM   1527 C  CD    A LYS A 1 220 ? -15.818 8.376   -17.196 0.50 20.33 ? 200 LYS A CD    1 
ATOM   1528 C  CD    B LYS A 1 220 ? -15.848 8.440   -17.259 0.50 20.54 ? 200 LYS A CD    1 
ATOM   1529 C  CE    A LYS A 1 220 ? -16.499 9.074   -16.032 0.50 21.76 ? 200 LYS A CE    1 
ATOM   1530 C  CE    B LYS A 1 220 ? -14.654 9.375   -17.140 0.50 22.03 ? 200 LYS A CE    1 
ATOM   1531 N  NZ    A LYS A 1 220 ? -16.804 10.501  -16.310 0.50 22.45 ? 200 LYS A NZ    1 
ATOM   1532 N  NZ    B LYS A 1 220 ? -15.029 10.813  -17.092 0.50 23.22 ? 200 LYS A NZ    1 
ATOM   1533 N  N     . ALA A 1 221 ? -13.777 4.094   -19.939 1.00 12.50 ? 201 ALA A N     1 
ATOM   1534 C  CA    . ALA A 1 221 ? -12.918 3.653   -21.034 1.00 12.12 ? 201 ALA A CA    1 
ATOM   1535 C  C     . ALA A 1 221 ? -13.728 3.140   -22.216 1.00 11.92 ? 201 ALA A C     1 
ATOM   1536 O  O     . ALA A 1 221 ? -13.376 3.399   -23.372 1.00 12.08 ? 201 ALA A O     1 
ATOM   1537 C  CB    . ALA A 1 221 ? -11.982 2.560   -20.533 1.00 12.74 ? 201 ALA A CB    1 
ATOM   1538 N  N     . LEU A 1 222 ? -14.801 2.388   -21.953 1.00 12.09 ? 202 LEU A N     1 
ATOM   1539 C  CA    . LEU A 1 222 ? -15.640 1.882   -23.032 1.00 12.39 ? 202 LEU A CA    1 
ATOM   1540 C  C     . LEU A 1 222 ? -16.244 3.025   -23.837 1.00 12.85 ? 202 LEU A C     1 
ATOM   1541 O  O     . LEU A 1 222 ? -16.466 2.878   -25.043 1.00 14.02 ? 202 LEU A O     1 
ATOM   1542 C  CB    . LEU A 1 222 ? -16.739 0.986   -22.460 1.00 12.06 ? 202 LEU A CB    1 
ATOM   1543 C  CG    . LEU A 1 222 ? -16.252 -0.382  -21.988 1.00 12.11 ? 202 LEU A CG    1 
ATOM   1544 C  CD1   . LEU A 1 222 ? -17.315 -1.068  -21.149 1.00 13.79 ? 202 LEU A CD1   1 
ATOM   1545 C  CD2   . LEU A 1 222 ? -15.858 -1.254  -23.152 1.00 13.49 ? 202 LEU A CD2   1 
ATOM   1546 N  N     . LYS A 1 223 ? -16.520 4.160   -23.189 1.00 13.21 ? 203 LYS A N     1 
ATOM   1547 C  CA    . LYS A 1 223 ? -17.045 5.352   -23.844 1.00 14.14 ? 203 LYS A CA    1 
ATOM   1548 C  C     . LYS A 1 223 ? -15.952 6.205   -24.482 1.00 14.13 ? 203 LYS A C     1 
ATOM   1549 O  O     . LYS A 1 223 ? -16.258 7.272   -25.032 1.00 15.49 ? 203 LYS A O     1 
ATOM   1550 C  CB    . LYS A 1 223 ? -17.810 6.202   -22.830 1.00 15.23 ? 203 LYS A CB    1 
ATOM   1551 C  CG    . LYS A 1 223 ? -19.060 5.543   -22.293 1.00 16.41 ? 203 LYS A CG    1 
ATOM   1552 C  CD    . LYS A 1 223 ? -19.653 6.356   -21.146 1.00 17.95 ? 203 LYS A CD    1 
ATOM   1553 N  N     . GLY A 1 224 ? -14.696 5.770   -24.439 1.00 14.19 ? 204 GLY A N     1 
ATOM   1554 C  CA    . GLY A 1 224 ? -13.603 6.556   -24.987 1.00 14.54 ? 204 GLY A CA    1 
ATOM   1555 C  C     . GLY A 1 224 ? -13.271 7.791   -24.190 1.00 15.02 ? 204 GLY A C     1 
ATOM   1556 O  O     . GLY A 1 224 ? -12.775 8.774   -24.756 1.00 17.63 ? 204 GLY A O     1 
ATOM   1557 N  N     . GLU A 1 225 ? -13.523 7.763   -22.885 1.00 13.98 ? 205 GLU A N     1 
ATOM   1558 C  CA    . GLU A 1 225 ? -13.324 8.889   -21.988 1.00 14.55 ? 205 GLU A CA    1 
ATOM   1559 C  C     . GLU A 1 225 ? -12.206 8.577   -21.006 1.00 15.05 ? 205 GLU A C     1 
ATOM   1560 O  O     . GLU A 1 225 ? -11.768 7.430   -20.848 1.00 15.04 ? 205 GLU A O     1 
ATOM   1561 C  CB    . GLU A 1 225 ? -14.624 9.226   -21.244 1.00 15.20 ? 205 GLU A CB    1 
ATOM   1562 C  CG    . GLU A 1 225 ? -15.741 9.662   -22.194 1.00 16.25 ? 205 GLU A CG    1 
ATOM   1563 C  CD    . GLU A 1 225 ? -17.081 9.915   -21.515 1.00 17.73 ? 205 GLU A CD    1 
ATOM   1564 O  OE1   . GLU A 1 225 ? -17.108 10.162  -20.292 1.00 19.60 ? 205 GLU A OE1   1 
ATOM   1565 O  OE2   . GLU A 1 225 ? -18.110 9.855   -22.215 1.00 18.76 ? 205 GLU A OE2   1 
ATOM   1566 N  N     . LYS A 1 226 ? -11.761 9.627   -20.329 1.00 16.77 ? 206 LYS A N     1 
ATOM   1567 C  CA    . LYS A 1 226 ? -10.657 9.539   -19.391 1.00 19.12 ? 206 LYS A CA    1 
ATOM   1568 C  C     . LYS A 1 226 ? -11.110 10.011  -18.018 1.00 19.87 ? 206 LYS A C     1 
ATOM   1569 O  O     . LYS A 1 226 ? -11.847 10.992  -17.894 1.00 21.23 ? 206 LYS A O     1 
ATOM   1570 C  CB    . LYS A 1 226 ? -9.471  10.398  -19.850 1.00 22.77 ? 206 LYS A CB    1 
ATOM   1571 C  CG    . LYS A 1 226 ? -8.929  10.034  -21.222 1.00 25.41 ? 206 LYS A CG    1 
ATOM   1572 C  CD    . LYS A 1 226 ? -8.185  8.708   -21.210 1.00 27.61 ? 206 LYS A CD    1 
ATOM   1573 C  CE    . LYS A 1 226 ? -7.792  8.260   -22.618 1.00 28.81 ? 206 LYS A CE    1 
ATOM   1574 N  NZ    . LYS A 1 226 ? -7.355  6.824   -22.683 1.00 29.30 ? 206 LYS A NZ    1 
ATOM   1575 N  N     . VAL A 1 227 ? -10.662 9.301   -16.992 1.00 19.06 ? 207 VAL A N     1 
ATOM   1576 C  CA    . VAL A 1 227 ? -10.866 9.713   -15.610 1.00 19.77 ? 207 VAL A CA    1 
ATOM   1577 C  C     . VAL A 1 227 ? -9.843  10.794  -15.280 1.00 23.21 ? 207 VAL A C     1 
ATOM   1578 O  O     . VAL A 1 227 ? -8.637  10.604  -15.473 1.00 23.97 ? 207 VAL A O     1 
ATOM   1579 C  CB    . VAL A 1 227 ? -10.717 8.501   -14.675 1.00 18.25 ? 207 VAL A CB    1 
ATOM   1580 C  CG1   . VAL A 1 227 ? -10.755 8.922   -13.222 1.00 18.23 ? 207 VAL A CG1   1 
ATOM   1581 C  CG2   . VAL A 1 227 ? -11.809 7.479   -14.941 1.00 18.56 ? 207 VAL A CG2   1 
ATOM   1582 N  N     . GLU A 1 228 ? -10.313 11.931  -14.781 1.00 25.45 ? 208 GLU A N     1 
ATOM   1583 C  CA    . GLU A 1 228 ? -9.392  12.991  -14.387 1.00 27.83 ? 208 GLU A CA    1 
ATOM   1584 C  C     . GLU A 1 228 ? -8.619  12.558  -13.148 1.00 29.67 ? 208 GLU A C     1 
ATOM   1585 O  O     . GLU A 1 228 ? -9.198  12.034  -12.197 1.00 29.89 ? 208 GLU A O     1 
ATOM   1586 C  CB    . GLU A 1 228 ? -10.158 14.279  -14.088 1.00 28.81 ? 208 GLU A CB    1 
ATOM   1587 N  N     . ALA A 1 229 ? -7.308  12.776  -13.151 1.00 32.40 ? 209 ALA A N     1 
ATOM   1588 C  CA    . ALA A 1 229 ? -6.480  12.358  -12.026 1.00 35.41 ? 209 ALA A CA    1 
ATOM   1589 C  C     . ALA A 1 229 ? -6.550  13.380  -10.898 1.00 37.13 ? 209 ALA A C     1 
ATOM   1590 O  O     . ALA A 1 229 ? -6.327  14.574  -11.119 1.00 37.34 ? 209 ALA A O     1 
ATOM   1591 C  CB    . ALA A 1 229 ? -5.031  12.198  -12.480 1.00 36.19 ? 209 ALA A CB    1 
ATOM   1592 N  N     . LYS A 1 230 ? -6.847  12.910  -9.687  1.00 38.30 ? 210 LYS A N     1 
ATOM   1593 C  CA    . LYS A 1 230 ? -6.850  13.775  -8.509  1.00 40.15 ? 210 LYS A CA    1 
ATOM   1594 C  C     . LYS A 1 230 ? -5.465  13.780  -7.869  1.00 41.29 ? 210 LYS A C     1 
ATOM   1595 O  O     . LYS A 1 230 ? -4.461  13.975  -8.553  1.00 41.94 ? 210 LYS A O     1 
ATOM   1596 C  CB    . LYS A 1 230 ? -7.889  13.311  -7.488  1.00 40.57 ? 210 LYS A CB    1 
HETATM 1597 P  PG    . ANP B 2 .   ? -8.258  -7.310  8.289   1.00 15.29 ? 301 ANP A PG    1 
HETATM 1598 O  O1G   . ANP B 2 .   ? -9.585  -6.621  8.371   1.00 14.87 ? 301 ANP A O1G   1 
HETATM 1599 O  O2G   . ANP B 2 .   ? -7.177  -6.423  9.013   1.00 16.46 ? 301 ANP A O2G   1 
HETATM 1600 O  O3G   . ANP B 2 .   ? -8.211  -8.762  8.871   1.00 16.78 ? 301 ANP A O3G   1 
HETATM 1601 P  PB    . ANP B 2 .   ? -7.484  -6.309  5.633   1.00 13.58 ? 301 ANP A PB    1 
HETATM 1602 O  O1B   . ANP B 2 .   ? -6.292  -6.695  4.789   1.00 15.45 ? 301 ANP A O1B   1 
HETATM 1603 O  O2B   . ANP B 2 .   ? -7.367  -4.945  6.320   1.00 13.74 ? 301 ANP A O2B   1 
HETATM 1604 N  N3B   . ANP B 2 .   ? -7.797  -7.543  6.696   1.00 14.63 ? 301 ANP A N3B   1 
HETATM 1605 P  PA    . ANP B 2 .   ? -9.089  -5.071  3.648   1.00 11.34 ? 301 ANP A PA    1 
HETATM 1606 O  O1A   . ANP B 2 .   ? -9.361  -3.846  4.444   1.00 11.69 ? 301 ANP A O1A   1 
HETATM 1607 O  O2A   . ANP B 2 .   ? -8.040  -5.001  2.542   1.00 12.06 ? 301 ANP A O2A   1 
HETATM 1608 O  O3A   . ANP B 2 .   ? -8.750  -6.271  4.646   1.00 12.48 ? 301 ANP A O3A   1 
HETATM 1609 O  "O5'" . ANP B 2 .   ? -10.416 -5.560  2.973   1.00 11.18 ? 301 ANP A "O5'" 1 
HETATM 1610 C  "C5'" . ANP B 2 .   ? -11.673 -5.625  3.660   1.00 11.56 ? 301 ANP A "C5'" 1 
HETATM 1611 C  "C4'" . ANP B 2 .   ? -12.693 -6.134  2.681   1.00 11.56 ? 301 ANP A "C4'" 1 
HETATM 1612 O  "O4'" . ANP B 2 .   ? -12.330 -7.470  2.282   1.00 11.61 ? 301 ANP A "O4'" 1 
HETATM 1613 C  "C3'" . ANP B 2 .   ? -14.110 -6.262  3.217   1.00 11.42 ? 301 ANP A "C3'" 1 
HETATM 1614 O  "O3'" . ANP B 2 .   ? -14.766 -5.001  3.198   1.00 12.00 ? 301 ANP A "O3'" 1 
HETATM 1615 C  "C2'" . ANP B 2 .   ? -14.710 -7.327  2.300   1.00 11.05 ? 301 ANP A "C2'" 1 
HETATM 1616 O  "O2'" . ANP B 2 .   ? -15.097 -6.777  1.052   1.00 10.73 ? 301 ANP A "O2'" 1 
HETATM 1617 C  "C1'" . ANP B 2 .   ? -13.498 -8.224  2.019   1.00 11.15 ? 301 ANP A "C1'" 1 
HETATM 1618 N  N9    . ANP B 2 .   ? -13.444 -9.443  2.805   1.00 11.60 ? 301 ANP A N9    1 
HETATM 1619 C  C8    . ANP B 2 .   ? -12.694 -9.710  3.924   1.00 13.82 ? 301 ANP A C8    1 
HETATM 1620 N  N7    . ANP B 2 .   ? -12.867 -10.916 4.410   1.00 14.05 ? 301 ANP A N7    1 
HETATM 1621 C  C5    . ANP B 2 .   ? -13.812 -11.474 3.553   1.00 12.66 ? 301 ANP A C5    1 
HETATM 1622 C  C6    . ANP B 2 .   ? -14.439 -12.740 3.528   1.00 12.90 ? 301 ANP A C6    1 
HETATM 1623 N  N6    . ANP B 2 .   ? -14.195 -13.713 4.408   1.00 14.40 ? 301 ANP A N6    1 
HETATM 1624 N  N1    . ANP B 2 .   ? -15.337 -12.971 2.545   1.00 12.10 ? 301 ANP A N1    1 
HETATM 1625 C  C2    . ANP B 2 .   ? -15.580 -12.004 1.653   1.00 11.92 ? 301 ANP A C2    1 
HETATM 1626 N  N3    . ANP B 2 .   ? -15.045 -10.785 1.569   1.00 11.31 ? 301 ANP A N3    1 
HETATM 1627 C  C4    . ANP B 2 .   ? -14.171 -10.580 2.564   1.00 11.51 ? 301 ANP A C4    1 
HETATM 1628 MG MG    . MG  C 3 .   ? -8.612  -3.283  6.312   1.00 12.65 ? 302 MG  A MG    1 
HETATM 1629 MG MG    . MG  D 3 .   ? -5.053  -4.447  7.354   1.00 20.86 ? 303 MG  A MG    1 
HETATM 1630 O  O     . HOH E 4 .   ? 2.606   3.960   -10.815 1.00 62.22 ? 401 HOH A O     1 
HETATM 1631 O  O     . HOH E 4 .   ? -9.407  -7.633  -32.536 1.00 37.12 ? 402 HOH A O     1 
HETATM 1632 O  O     . HOH E 4 .   ? -23.921 2.720   -4.828  1.00 39.47 ? 403 HOH A O     1 
HETATM 1633 O  O     . HOH E 4 .   ? -14.627 -12.836 8.047   1.00 51.79 ? 404 HOH A O     1 
HETATM 1634 O  O     . HOH E 4 .   ? -17.836 -19.590 -14.634 1.00 33.00 ? 405 HOH A O     1 
HETATM 1635 O  O     . HOH E 4 .   ? -18.418 4.232   -7.027  1.00 40.38 ? 406 HOH A O     1 
HETATM 1636 O  O     . HOH E 4 .   ? -2.690  6.484   -5.889  1.00 46.48 ? 407 HOH A O     1 
HETATM 1637 O  O     . HOH E 4 .   ? -22.616 -14.675 -10.219 1.00 21.82 ? 408 HOH A O     1 
HETATM 1638 O  O     . HOH E 4 .   ? -10.112 -4.368  7.271   1.00 13.32 ? 409 HOH A O     1 
HETATM 1639 O  O     . HOH E 4 .   ? -3.095  -3.095  -25.124 1.00 36.51 ? 410 HOH A O     1 
HETATM 1640 O  O     . HOH E 4 .   ? -27.956 2.363   -20.177 1.00 47.71 ? 411 HOH A O     1 
HETATM 1641 O  O     . HOH E 4 .   ? -6.442  6.902   3.736   1.00 34.34 ? 412 HOH A O     1 
HETATM 1642 O  O     . HOH E 4 .   ? -14.962 -8.432  12.576  1.00 44.77 ? 413 HOH A O     1 
HETATM 1643 O  O     . HOH E 4 .   ? -30.637 -11.816 -11.173 1.00 49.88 ? 414 HOH A O     1 
HETATM 1644 O  O     . HOH E 4 .   ? -26.481 -16.983 -14.597 1.00 39.88 ? 415 HOH A O     1 
HETATM 1645 O  O     . HOH E 4 .   ? -16.808 8.198   5.023   1.00 42.75 ? 416 HOH A O     1 
HETATM 1646 O  O     . HOH E 4 .   ? -6.987  8.758   -16.382 1.00 25.51 ? 417 HOH A O     1 
HETATM 1647 O  O     . HOH E 4 .   ? -17.918 9.535   -24.827 1.00 21.10 ? 418 HOH A O     1 
HETATM 1648 O  O     . HOH E 4 .   ? -14.517 -8.309  -11.399 1.00 18.08 ? 419 HOH A O     1 
HETATM 1649 O  O     . HOH E 4 .   ? -30.967 1.233   -8.848  1.00 35.42 ? 420 HOH A O     1 
HETATM 1650 O  O     . HOH E 4 .   ? 4.042   0.812   -23.465 1.00 41.25 ? 421 HOH A O     1 
HETATM 1651 O  O     . HOH E 4 .   ? -4.657  -15.012 -18.005 1.00 17.67 ? 422 HOH A O     1 
HETATM 1652 O  O     . HOH E 4 .   ? -8.891  12.662  0.169   1.00 52.89 ? 423 HOH A O     1 
HETATM 1653 O  O     . HOH E 4 .   ? -8.391  -10.099 11.180  1.00 35.90 ? 424 HOH A O     1 
HETATM 1654 O  O     . HOH E 4 .   ? 1.299   -3.835  -4.563  1.00 38.71 ? 425 HOH A O     1 
HETATM 1655 O  O     . HOH E 4 .   ? -7.465  5.215   -25.804 1.00 18.54 ? 426 HOH A O     1 
HETATM 1656 O  O     . HOH E 4 .   ? -20.964 -7.605  -28.305 1.00 17.30 ? 427 HOH A O     1 
HETATM 1657 O  O     . HOH E 4 .   ? -17.138 -1.235  5.055   1.00 12.49 ? 428 HOH A O     1 
HETATM 1658 O  O     . HOH E 4 .   ? -27.244 -6.265  14.105  1.00 19.88 ? 429 HOH A O     1 
HETATM 1659 O  O     . HOH E 4 .   ? -30.149 -1.018  -21.049 1.00 43.12 ? 430 HOH A O     1 
HETATM 1660 O  O     . HOH E 4 .   ? -30.165 -8.798  -14.124 1.00 21.28 ? 431 HOH A O     1 
HETATM 1661 O  O     . HOH E 4 .   ? 1.189   -8.255  -28.313 1.00 52.26 ? 432 HOH A O     1 
HETATM 1662 O  O     . HOH E 4 .   ? -3.029  5.052   -24.517 1.00 31.20 ? 433 HOH A O     1 
HETATM 1663 O  O     . HOH E 4 .   ? -5.174  -11.316 -11.492 1.00 56.35 ? 434 HOH A O     1 
HETATM 1664 O  O     . HOH E 4 .   ? -12.639 9.917   -10.216 1.00 24.79 ? 435 HOH A O     1 
HETATM 1665 O  O     . HOH E 4 .   ? -5.078  -4.643  11.169  1.00 27.72 ? 436 HOH A O     1 
HETATM 1666 O  O     . HOH E 4 .   ? 2.635   -8.563  -15.813 1.00 57.67 ? 437 HOH A O     1 
HETATM 1667 O  O     . HOH E 4 .   ? -14.221 -21.438 -0.763  1.00 32.53 ? 438 HOH A O     1 
HETATM 1668 O  O     . HOH E 4 .   ? -13.943 -13.733 -29.151 1.00 43.40 ? 439 HOH A O     1 
HETATM 1669 O  O     . HOH E 4 .   ? -9.827  -18.040 -24.046 1.00 25.42 ? 440 HOH A O     1 
HETATM 1670 O  O     . HOH E 4 .   ? -32.841 -5.784  0.387   1.00 26.96 ? 441 HOH A O     1 
HETATM 1671 O  O     . HOH E 4 .   ? -5.732  1.820   -8.569  1.00 17.76 ? 442 HOH A O     1 
HETATM 1672 O  O     . HOH E 4 .   ? 0.440   -7.681  -22.883 1.00 17.64 ? 443 HOH A O     1 
HETATM 1673 O  O     . HOH E 4 .   ? -4.350  -14.777 -26.880 1.00 29.84 ? 444 HOH A O     1 
HETATM 1674 O  O     . HOH E 4 .   ? -19.006 9.563   -18.415 1.00 38.18 ? 445 HOH A O     1 
HETATM 1675 O  O     . HOH E 4 .   ? -9.836  -19.872 -21.292 1.00 46.05 ? 446 HOH A O     1 
HETATM 1676 O  O     . HOH E 4 .   ? -0.063  -5.939  -35.635 1.00 37.18 ? 447 HOH A O     1 
HETATM 1677 O  O     . HOH E 4 .   ? 1.104   -11.633 -22.185 1.00 28.10 ? 448 HOH A O     1 
HETATM 1678 O  O     . HOH E 4 .   ? 3.370   -4.228  -27.877 1.00 31.19 ? 449 HOH A O     1 
HETATM 1679 O  O     . HOH E 4 .   ? -26.896 -12.689 -8.079  1.00 42.69 ? 450 HOH A O     1 
HETATM 1680 O  O     . HOH E 4 .   ? -4.062  -5.151  5.268   1.00 30.16 ? 451 HOH A O     1 
HETATM 1681 O  O     . HOH E 4 .   ? -8.796  -11.233 7.802   1.00 38.17 ? 452 HOH A O     1 
HETATM 1682 O  O     . HOH E 4 .   ? -27.262 1.626   8.962   1.00 31.25 ? 453 HOH A O     1 
HETATM 1683 O  O     . HOH E 4 .   ? 1.592   -1.117  -6.281  1.00 29.14 ? 454 HOH A O     1 
HETATM 1684 O  O     . HOH E 4 .   ? -9.834  -20.277 -6.968  1.00 14.03 ? 455 HOH A O     1 
HETATM 1685 O  O     . HOH E 4 .   ? -5.681  -13.377 -20.079 1.00 14.51 ? 456 HOH A O     1 
HETATM 1686 O  O     . HOH E 4 .   ? -1.554  5.186   -19.519 1.00 41.93 ? 457 HOH A O     1 
HETATM 1687 O  O     . HOH E 4 .   ? -27.779 -8.839  -9.796  1.00 16.87 ? 458 HOH A O     1 
HETATM 1688 O  O     . HOH E 4 .   ? -15.471 12.290  -19.389 1.00 32.61 ? 459 HOH A O     1 
HETATM 1689 O  O     . HOH E 4 .   ? -22.556 -11.817 6.457   1.00 14.56 ? 460 HOH A O     1 
HETATM 1690 O  O     . HOH E 4 .   ? -9.924  5.829   -22.162 1.00 20.20 ? 461 HOH A O     1 
HETATM 1691 O  O     . HOH E 4 .   ? -21.386 -17.727 0.182   1.00 45.89 ? 462 HOH A O     1 
HETATM 1692 O  O     . HOH E 4 .   ? -2.533  -1.736  5.839   1.00 42.08 ? 463 HOH A O     1 
HETATM 1693 O  O     . HOH E 4 .   ? -10.848 4.256   -24.290 1.00 14.82 ? 464 HOH A O     1 
HETATM 1694 O  O     . HOH E 4 .   ? -12.172 -2.955  -29.272 1.00 14.24 ? 465 HOH A O     1 
HETATM 1695 O  O     . HOH E 4 .   ? -7.858  5.442   7.168   1.00 36.61 ? 466 HOH A O     1 
HETATM 1696 O  O     . HOH E 4 .   ? -25.100 -13.810 -21.574 1.00 28.20 ? 467 HOH A O     1 
HETATM 1697 O  O     . HOH E 4 .   ? -5.707  9.617   -7.399  1.00 34.18 ? 468 HOH A O     1 
HETATM 1698 O  O     . HOH E 4 .   ? -22.511 -10.623 -27.477 1.00 28.28 ? 469 HOH A O     1 
HETATM 1699 O  O     . HOH E 4 .   ? -30.240 -2.160  -2.960  1.00 22.34 ? 470 HOH A O     1 
HETATM 1700 O  O     . HOH E 4 .   ? -4.861  7.734   -4.007  1.00 43.16 ? 471 HOH A O     1 
HETATM 1701 O  O     . HOH E 4 .   ? -24.882 2.835   -14.819 1.00 25.44 ? 472 HOH A O     1 
HETATM 1702 O  O     . HOH E 4 .   ? -20.583 3.359   -6.276  1.00 39.32 ? 473 HOH A O     1 
HETATM 1703 O  O     . HOH E 4 .   ? -28.162 1.297   -8.712  1.00 20.61 ? 474 HOH A O     1 
HETATM 1704 O  O     . HOH E 4 .   ? -26.808 0.626   -26.708 1.00 28.01 ? 475 HOH A O     1 
HETATM 1705 O  O     . HOH E 4 .   ? -17.154 7.268   -5.603  1.00 49.80 ? 476 HOH A O     1 
HETATM 1706 O  O     . HOH E 4 .   ? -19.558 7.611   -4.061  1.00 43.72 ? 477 HOH A O     1 
HETATM 1707 O  O     . HOH E 4 .   ? 3.531   -1.798  -8.256  1.00 38.99 ? 478 HOH A O     1 
HETATM 1708 O  O     . HOH E 4 .   ? -27.973 -0.314  -19.652 1.00 25.47 ? 479 HOH A O     1 
HETATM 1709 O  O     . HOH E 4 .   ? -18.378 5.831   -15.067 1.00 18.26 ? 480 HOH A O     1 
HETATM 1710 O  O     . HOH E 4 .   ? -15.937 -10.759 -11.472 1.00 12.99 ? 481 HOH A O     1 
HETATM 1711 O  O     . HOH E 4 .   ? -1.359  -16.912 -17.437 1.00 42.60 ? 482 HOH A O     1 
HETATM 1712 O  O     . HOH E 4 .   ? -30.594 -4.482  -24.955 1.00 43.30 ? 483 HOH A O     1 
HETATM 1713 O  O     . HOH E 4 .   ? -33.939 -10.520 -13.483 1.00 45.41 ? 484 HOH A O     1 
HETATM 1714 O  O     . HOH E 4 .   ? -3.772  -13.385 -4.777  1.00 12.75 ? 485 HOH A O     1 
HETATM 1715 O  O     . HOH E 4 .   ? -18.326 -9.418  -11.344 1.00 12.66 ? 486 HOH A O     1 
HETATM 1716 O  O     . HOH E 4 .   ? -5.301  -15.158 -15.325 1.00 14.40 ? 487 HOH A O     1 
HETATM 1717 O  O     . HOH E 4 .   ? -5.977  5.942   0.229   1.00 33.23 ? 488 HOH A O     1 
HETATM 1718 O  O     . HOH E 4 .   ? -16.950 4.585   -27.250 1.00 21.66 ? 489 HOH A O     1 
HETATM 1719 O  O     . HOH E 4 .   ? -12.083 -12.675 6.492   1.00 28.32 ? 490 HOH A O     1 
HETATM 1720 O  O     . HOH E 4 .   ? -13.222 -19.539 -13.140 1.00 19.34 ? 491 HOH A O     1 
HETATM 1721 O  O     . HOH E 4 .   ? -18.257 -18.174 -16.821 1.00 22.61 ? 492 HOH A O     1 
HETATM 1722 O  O     . HOH E 4 .   ? -0.161  -5.929  -30.385 1.00 26.12 ? 493 HOH A O     1 
HETATM 1723 O  O     . HOH E 4 .   ? -23.696 3.239   -26.613 1.00 48.83 ? 494 HOH A O     1 
HETATM 1724 O  O     . HOH E 4 .   ? -15.189 8.434   -12.750 1.00 46.10 ? 495 HOH A O     1 
HETATM 1725 O  O     . HOH E 4 .   ? -3.696  4.057   -10.696 1.00 33.57 ? 496 HOH A O     1 
HETATM 1726 O  O     . HOH E 4 .   ? -6.144  4.619   -21.275 1.00 21.58 ? 497 HOH A O     1 
HETATM 1727 O  O     . HOH E 4 .   ? -32.053 -7.599  -10.411 1.00 34.82 ? 498 HOH A O     1 
HETATM 1728 O  O     . HOH E 4 .   ? -27.111 1.259   1.985   1.00 28.42 ? 499 HOH A O     1 
HETATM 1729 O  O     . HOH E 4 .   ? -4.325  8.585   -15.387 1.00 33.96 ? 500 HOH A O     1 
HETATM 1730 O  O     . HOH E 4 .   ? 3.797   -4.265  -11.549 1.00 33.91 ? 501 HOH A O     1 
HETATM 1731 O  O     . HOH E 4 .   ? -1.313  -14.641 -13.869 1.00 19.84 ? 502 HOH A O     1 
HETATM 1732 O  O     . HOH E 4 .   ? -28.277 -5.982  -28.933 1.00 34.92 ? 503 HOH A O     1 
HETATM 1733 O  O     . HOH E 4 .   ? -2.353  -0.578  3.693   1.00 47.59 ? 504 HOH A O     1 
HETATM 1734 O  O     . HOH E 4 .   ? -6.284  -19.314 -13.395 1.00 15.62 ? 505 HOH A O     1 
HETATM 1735 O  O     . HOH E 4 .   ? -22.601 -14.771 -21.130 1.00 32.66 ? 506 HOH A O     1 
HETATM 1736 O  O     . HOH E 4 .   ? -10.312 -20.766 -11.050 1.00 42.43 ? 507 HOH A O     1 
HETATM 1737 O  O     . HOH E 4 .   ? -14.111 9.503   -27.211 1.00 33.09 ? 508 HOH A O     1 
HETATM 1738 O  O     . HOH E 4 .   ? -30.499 -6.031  -7.333  1.00 33.25 ? 509 HOH A O     1 
HETATM 1739 O  O     . HOH E 4 .   ? -6.821  -7.059  -32.084 1.00 19.76 ? 510 HOH A O     1 
HETATM 1740 O  O     . HOH E 4 .   ? -10.828 -13.759 -30.445 1.00 29.75 ? 511 HOH A O     1 
HETATM 1741 O  O     . HOH E 4 .   ? -16.462 13.295  -17.520 1.00 35.78 ? 512 HOH A O     1 
HETATM 1742 O  O     . HOH E 4 .   ? -5.782  4.249   -27.812 1.00 17.23 ? 513 HOH A O     1 
HETATM 1743 O  O     . HOH E 4 .   ? -5.257  4.091   7.076   1.00 44.76 ? 514 HOH A O     1 
HETATM 1744 O  O     . HOH E 4 .   ? -11.240 -18.760 -15.163 1.00 19.76 ? 515 HOH A O     1 
HETATM 1745 O  O     . HOH E 4 .   ? -15.039 -3.058  5.666   1.00 14.46 ? 516 HOH A O     1 
HETATM 1746 O  O     . HOH E 4 .   ? -22.925 -10.186 10.562  1.00 14.75 ? 517 HOH A O     1 
HETATM 1747 O  O     . HOH E 4 .   ? -20.628 -15.147 -27.950 1.00 42.35 ? 518 HOH A O     1 
HETATM 1748 O  O     . HOH E 4 .   ? -10.122 -4.633  -32.772 1.00 20.31 ? 519 HOH A O     1 
HETATM 1749 O  O     . HOH E 4 .   ? -21.045 -8.278  11.524  1.00 16.87 ? 520 HOH A O     1 
HETATM 1750 O  O     . HOH E 4 .   ? -11.301 -17.237 4.682   1.00 18.02 ? 521 HOH A O     1 
HETATM 1751 O  O     . HOH E 4 .   ? -26.022 -7.375  -1.243  1.00 24.01 ? 522 HOH A O     1 
HETATM 1752 O  O     . HOH E 4 .   ? -0.458  -10.597 -35.294 1.00 45.00 ? 523 HOH A O     1 
HETATM 1753 O  O     . HOH E 4 .   ? 3.828   -1.616  -24.810 1.00 21.31 ? 524 HOH A O     1 
HETATM 1754 O  O     . HOH E 4 .   ? -4.024  -10.971 -32.019 1.00 23.72 ? 525 HOH A O     1 
HETATM 1755 O  O     . HOH E 4 .   ? -22.424 -14.394 5.398   1.00 13.60 ? 526 HOH A O     1 
HETATM 1756 O  O     . HOH E 4 .   ? -0.580  -14.434 -16.431 1.00 32.76 ? 527 HOH A O     1 
HETATM 1757 O  O     . HOH E 4 .   ? -14.512 -15.607 7.372   1.00 29.73 ? 528 HOH A O     1 
HETATM 1758 O  O     . HOH E 4 .   ? 6.380   -3.109  -24.459 1.00 52.28 ? 529 HOH A O     1 
HETATM 1759 O  O     . HOH E 4 .   ? -5.766  -14.881 -30.022 1.00 26.47 ? 530 HOH A O     1 
HETATM 1760 O  O     . HOH E 4 .   ? -3.854  -0.775  8.447   1.00 35.26 ? 531 HOH A O     1 
HETATM 1761 O  O     . HOH E 4 .   ? -16.771 -17.932 -21.460 1.00 26.27 ? 532 HOH A O     1 
HETATM 1762 O  O     . HOH E 4 .   ? -8.217  -16.181 0.652   1.00 48.66 ? 533 HOH A O     1 
HETATM 1763 O  O     . HOH E 4 .   ? -19.987 -11.386 -31.507 1.00 43.63 ? 534 HOH A O     1 
HETATM 1764 O  O     . HOH E 4 .   ? -1.671  4.703   -7.503  1.00 44.43 ? 535 HOH A O     1 
HETATM 1765 O  O     . HOH E 4 .   ? -11.177 9.510   -2.010  1.00 22.71 ? 536 HOH A O     1 
HETATM 1766 O  O     . HOH E 4 .   ? -9.709  7.889   4.837   1.00 44.72 ? 537 HOH A O     1 
HETATM 1767 O  O     . HOH E 4 .   ? -4.620  -8.897  5.827   1.00 46.21 ? 538 HOH A O     1 
HETATM 1768 O  O     . HOH E 4 .   ? -13.486 10.183  -3.425  1.00 49.15 ? 539 HOH A O     1 
HETATM 1769 O  O     . HOH E 4 .   ? -21.688 4.166   -1.958  1.00 37.24 ? 540 HOH A O     1 
HETATM 1770 O  O     . HOH E 4 .   ? -6.865  -22.029 -8.885  1.00 17.23 ? 541 HOH A O     1 
HETATM 1771 O  O     . HOH E 4 .   ? -16.291 -12.959 -28.149 1.00 23.78 ? 542 HOH A O     1 
HETATM 1772 O  O     . HOH E 4 .   ? -16.202 7.740   -27.966 1.00 45.42 ? 543 HOH A O     1 
HETATM 1773 O  O     . HOH E 4 .   ? -3.012  -19.199 -16.452 1.00 40.25 ? 544 HOH A O     1 
HETATM 1774 O  O     . HOH E 4 .   ? -4.296  -6.297  8.261   1.00 43.40 ? 545 HOH A O     1 
HETATM 1775 O  O     . HOH E 4 .   ? -27.064 -3.335  -27.513 1.00 30.96 ? 546 HOH A O     1 
HETATM 1776 O  O     . HOH E 4 .   ? -5.280  8.035   -19.105 1.00 36.60 ? 547 HOH A O     1 
HETATM 1777 O  O     . HOH E 4 .   ? -7.910  9.008   -2.654  1.00 27.12 ? 548 HOH A O     1 
HETATM 1778 O  O     . HOH E 4 .   ? -12.201 -19.944 -17.449 1.00 32.91 ? 549 HOH A O     1 
HETATM 1779 O  O     . HOH E 4 .   ? -8.557  -18.015 2.165   1.00 33.29 ? 550 HOH A O     1 
HETATM 1780 O  O     . HOH E 4 .   ? -16.687 -2.569  -31.693 1.00 30.30 ? 551 HOH A O     1 
HETATM 1781 O  O     . HOH E 4 .   ? -15.245 9.226   -8.652  1.00 53.09 ? 552 HOH A O     1 
HETATM 1782 O  O     . HOH E 4 .   ? -31.304 -13.598 -20.523 1.00 37.12 ? 553 HOH A O     1 
HETATM 1783 O  O     . HOH E 4 .   ? 1.718   3.130   -22.214 1.00 40.81 ? 554 HOH A O     1 
HETATM 1784 O  O     . HOH E 4 .   ? -1.475  -9.113  2.050   1.00 53.55 ? 555 HOH A O     1 
HETATM 1785 O  O     . HOH E 4 .   ? -16.611 -19.880 -18.474 1.00 49.41 ? 556 HOH A O     1 
HETATM 1786 O  O     . HOH E 4 .   ? -21.311 4.076   3.156   1.00 17.10 ? 557 HOH A O     1 
HETATM 1787 O  O     . HOH E 4 .   ? -12.969 12.315  -21.166 1.00 23.50 ? 558 HOH A O     1 
HETATM 1788 O  O     . HOH E 4 .   ? 0.360   -10.880 -3.531  1.00 41.60 ? 559 HOH A O     1 
HETATM 1789 O  O     . HOH E 4 .   ? -4.122  4.976   -1.620  1.00 31.62 ? 560 HOH A O     1 
HETATM 1790 O  O     . HOH E 4 .   ? -10.708 -12.752 2.592   1.00 36.99 ? 561 HOH A O     1 
HETATM 1791 O  O     . HOH E 4 .   ? -4.540  -7.060  10.648  1.00 48.74 ? 562 HOH A O     1 
HETATM 1792 O  O     . HOH E 4 .   ? -31.446 -3.043  -0.511  1.00 40.71 ? 563 HOH A O     1 
HETATM 1793 O  O     . HOH E 4 .   ? -4.318  3.479   4.689   1.00 47.70 ? 564 HOH A O     1 
HETATM 1794 O  O     . HOH E 4 .   ? -12.836 -24.006 -2.959  1.00 43.10 ? 565 HOH A O     1 
HETATM 1795 O  O     . HOH E 4 .   ? -12.607 -20.325 -21.397 1.00 55.84 ? 566 HOH A O     1 
HETATM 1796 O  O     . HOH E 4 .   ? -9.044  -19.152 -13.062 1.00 23.40 ? 567 HOH A O     1 
HETATM 1797 O  O     . HOH E 4 .   ? -25.339 0.980   6.514   1.00 21.27 ? 568 HOH A O     1 
HETATM 1798 O  O     . HOH E 4 .   ? -21.276 -7.354  14.230  1.00 32.02 ? 569 HOH A O     1 
HETATM 1799 O  O     . HOH E 4 .   ? -26.335 3.191   -9.983  1.00 43.85 ? 570 HOH A O     1 
HETATM 1800 O  O     . HOH E 4 .   ? 2.160   -8.607  -24.863 1.00 36.69 ? 571 HOH A O     1 
HETATM 1801 O  O     . HOH E 4 .   ? -28.164 1.539   -6.011  1.00 32.56 ? 572 HOH A O     1 
HETATM 1802 O  O     . HOH E 4 .   ? -26.412 -12.127 -1.559  1.00 35.53 ? 573 HOH A O     1 
HETATM 1803 O  O     . HOH E 4 .   ? -3.128  -3.064  8.952   1.00 48.03 ? 574 HOH A O     1 
HETATM 1804 O  O     . HOH E 4 .   ? -15.328 -20.654 -14.438 1.00 34.19 ? 575 HOH A O     1 
HETATM 1805 O  O     . HOH E 4 .   ? -28.939 -10.742 -8.087  1.00 37.17 ? 576 HOH A O     1 
HETATM 1806 O  O     . HOH E 4 .   ? -28.626 0.367   -17.003 1.00 29.90 ? 577 HOH A O     1 
HETATM 1807 O  O     . HOH E 4 .   ? -17.979 -15.331 -27.680 1.00 42.01 ? 578 HOH A O     1 
HETATM 1808 O  O     . HOH E 4 .   ? -16.247 -11.599 -30.485 1.00 43.89 ? 579 HOH A O     1 
HETATM 1809 O  O     . HOH E 4 .   ? -11.413 -6.304  14.823  1.00 29.99 ? 580 HOH A O     1 
HETATM 1810 O  O     . HOH E 4 .   ? -10.585 -14.518 4.449   1.00 52.54 ? 581 HOH A O     1 
HETATM 1811 O  O     . HOH E 4 .   ? -13.385 12.345  -23.834 1.00 37.01 ? 582 HOH A O     1 
HETATM 1812 O  O     . HOH E 4 .   ? -23.849 4.190   3.605   1.00 48.13 ? 583 HOH A O     1 
HETATM 1813 O  O     . HOH E 4 .   ? -12.803 -21.630 -10.916 1.00 47.60 ? 584 HOH A O     1 
HETATM 1814 O  O     . HOH E 4 .   ? -8.360  -13.170 0.994   1.00 41.56 ? 585 HOH A O     1 
HETATM 1815 O  O     . HOH E 4 .   ? -22.087 -9.676  -30.132 1.00 45.73 ? 586 HOH A O     1 
HETATM 1816 O  O     . HOH E 4 .   ? -16.926 -6.895  12.730  1.00 32.01 ? 587 HOH A O     1 
HETATM 1817 O  O     . HOH E 4 .   ? -27.708 3.060   -16.468 1.00 53.83 ? 588 HOH A O     1 
HETATM 1818 O  O     . HOH E 4 .   ? -17.496 7.908   -13.250 1.00 39.58 ? 589 HOH A O     1 
HETATM 1819 O  O     . HOH E 4 .   ? -26.629 3.638   -5.225  1.00 48.54 ? 590 HOH A O     1 
HETATM 1820 O  O     . HOH E 4 .   ? -25.328 3.876   -12.079 1.00 38.84 ? 591 HOH A O     1 
HETATM 1821 O  O     . HOH E 4 .   ? -18.868 -11.708 10.117  1.00 39.06 ? 592 HOH A O     1 
HETATM 1822 O  O     . HOH E 4 .   ? -9.334  -15.781 3.047   1.00 43.73 ? 593 HOH A O     1 
HETATM 1823 O  O     . HOH E 4 .   ? -9.723  -21.978 -8.886  1.00 37.51 ? 594 HOH A O     1 
HETATM 1824 O  O     . HOH E 4 .   ? -4.406  -17.711 -14.606 1.00 16.73 ? 595 HOH A O     1 
HETATM 1825 O  O     . HOH E 4 .   ? -3.521  5.683   -21.268 1.00 36.76 ? 596 HOH A O     1 
HETATM 1826 O  O     . HOH E 4 .   ? -28.173 -5.539  11.588  1.00 40.87 ? 597 HOH A O     1 
HETATM 1827 O  O     . HOH E 4 .   ? -9.002  4.907   9.460   1.00 33.10 ? 598 HOH A O     1 
HETATM 1828 O  O     . HOH E 4 .   ? -15.671 9.266   7.566   1.00 23.76 ? 599 HOH A O     1 
HETATM 1829 O  O     . HOH E 4 .   ? -13.637 10.674  6.068   1.00 49.32 ? 600 HOH A O     1 
HETATM 1830 O  O     . HOH E 4 .   ? -5.989  -12.686 1.885   1.00 41.92 ? 601 HOH A O     1 
HETATM 1831 O  O     . HOH E 4 .   ? -29.961 -9.087  -11.452 1.00 24.21 ? 602 HOH A O     1 
HETATM 1832 O  O     . HOH E 4 .   ? -25.661 2.396   4.223   1.00 33.89 ? 603 HOH A O     1 
HETATM 1833 O  O     . HOH E 4 .   ? -22.371 -19.053 -15.247 1.00 50.56 ? 604 HOH A O     1 
HETATM 1834 O  O     . HOH E 4 .   ? -2.173  -17.137 -13.087 1.00 16.97 ? 605 HOH A O     1 
HETATM 1835 O  O     . HOH E 4 .   ? -32.531 -3.162  -4.493  1.00 42.04 ? 606 HOH A O     1 
HETATM 1836 O  O     . HOH E 4 .   ? -20.835 -18.172 -17.348 1.00 33.25 ? 607 HOH A O     1 
HETATM 1837 O  O     . HOH E 4 .   ? -30.064 0.576   -4.178  1.00 45.18 ? 608 HOH A O     1 
HETATM 1838 O  O     . HOH E 4 .   ? -19.395 7.070   -17.326 1.00 31.45 ? 609 HOH A O     1 
HETATM 1839 O  O     . HOH E 4 .   ? -10.591 -20.494 7.895   1.00 44.34 ? 610 HOH A O     1 
HETATM 1840 O  O     . HOH E 4 .   ? -20.427 4.817   -13.635 1.00 31.20 ? 611 HOH A O     1 
HETATM 1841 O  O     . HOH E 4 .   ? 0.995   -14.789 -12.032 1.00 37.86 ? 612 HOH A O     1 
HETATM 1842 O  O     . HOH E 4 .   ? -22.117 -17.258 -19.772 1.00 49.48 ? 613 HOH A O     1 
HETATM 1843 O  O     . HOH E 4 .   ? -10.182 -18.225 7.109   1.00 28.33 ? 614 HOH A O     1 
HETATM 1844 O  O     . HOH E 4 .   ? -11.102 -12.515 8.880   1.00 51.59 ? 615 HOH A O     1 
HETATM 1845 O  O     . HOH E 4 .   ? -10.646 -10.680 12.509  1.00 58.57 ? 616 HOH A O     1 
HETATM 1846 O  O     . HOH E 4 .   ? -5.536  -18.604 2.337   1.00 25.81 ? 617 HOH A O     1 
HETATM 1847 O  O     . HOH E 4 .   ? -20.648 5.093   0.706   1.00 41.46 ? 618 HOH A O     1 
HETATM 1848 O  O     . HOH E 4 .   ? -19.814 -19.577 -0.454  1.00 39.55 ? 619 HOH A O     1 
HETATM 1849 O  O     . HOH E 4 .   ? -12.096 -16.872 8.596   1.00 47.40 ? 620 HOH A O     1 
HETATM 1850 O  O     . HOH E 4 .   ? -0.175  -16.161 -9.077  1.00 17.60 ? 621 HOH A O     1 
HETATM 1851 O  O     . HOH E 4 .   ? -18.499 -8.972  11.816  1.00 29.80 ? 622 HOH A O     1 
HETATM 1852 O  O     . HOH E 4 .   ? -18.386 -7.052  14.841  1.00 45.01 ? 623 HOH A O     1 
HETATM 1853 O  O     . HOH E 4 .   ? -23.017 4.914   -14.899 1.00 41.46 ? 624 HOH A O     1 
HETATM 1854 O  O     . HOH E 4 .   ? -12.694 -18.762 10.813  1.00 56.00 ? 625 HOH A O     1 
HETATM 1855 O  O     . HOH E 4 .   ? -22.027 -17.076 -25.579 1.00 49.07 ? 626 HOH A O     1 
HETATM 1856 O  O     . HOH E 4 .   ? -21.782 -9.937  14.995  1.00 39.75 ? 627 HOH A O     1 
HETATM 1857 O  O     . HOH E 4 .   ? -31.154 -0.157  -15.984 1.00 56.90 ? 628 HOH A O     1 
HETATM 1858 O  O     . HOH E 4 .   ? -6.557  -21.527 8.010   1.00 15.86 ? 629 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     . MET A 21  ? 0.5654 0.4537 0.2941 0.0444  0.0272  0.1113  1   MET A N     
2    C  CA    . MET A 21  ? 0.5435 0.4522 0.2797 0.0407  0.0305  0.1066  1   MET A CA    
3    C  C     . MET A 21  ? 0.4346 0.3863 0.2430 0.0340  0.0317  0.1044  1   MET A C     
4    O  O     . MET A 21  ? 0.4493 0.3891 0.2531 0.0446  0.0430  0.1143  1   MET A O     
5    C  CB    . MET A 21  ? 0.6228 0.5093 0.3004 0.0466  0.0367  0.1047  1   MET A CB    
6    C  CG    . MET A 21  ? 0.6972 0.5594 0.3246 0.0538  0.0408  0.1008  1   MET A CG    
7    S  SD    . MET A 21  ? 0.7544 0.6015 0.3412 0.0602  0.0467  0.0957  1   MET A SD    
8    C  CE    . MET A 21  ? 0.7684 0.6118 0.3425 0.0591  0.0480  0.0907  1   MET A CE    
9    N  N     . ILE A 22  ? 0.3156 0.3224 0.2052 0.0137  0.0126  0.0888  2   ILE A N     
10   C  CA    . ILE A 22  ? 0.2429 0.2809 0.1821 -0.0108 0.0124  0.0592  2   ILE A CA    
11   C  C     . ILE A 22  ? 0.2319 0.2653 0.1738 -0.0186 -0.0125 0.0492  2   ILE A C     
12   O  O     . ILE A 22  ? 0.2404 0.2663 0.1760 -0.0423 0.0069  0.0346  2   ILE A O     
13   C  CB    . ILE A 22  ? 0.2222 0.2679 0.1788 -0.0409 0.0131  0.0372  2   ILE A CB    
14   C  CG1   . ILE A 22  ? 0.2288 0.2648 0.1875 -0.0487 0.0353  0.0327  2   ILE A CG1   
15   C  CG2   . ILE A 22  ? 0.2072 0.2717 0.1665 -0.0418 -0.0091 0.0318  2   ILE A CG2   
16   C  CD1   . ILE A 22  ? 0.2317 0.2669 0.1897 -0.0404 0.0383  0.0318  2   ILE A CD1   
17   N  N     . SER A 23  ? 0.2341 0.2631 0.1782 -0.0133 -0.0372 0.0454  3   SER A N     
18   C  CA    A SER A 23  ? 0.2353 0.2692 0.1911 -0.0164 -0.0424 0.0346  3   SER A CA    
19   C  CA    B SER A 23  ? 0.2333 0.2651 0.1901 -0.0102 -0.0435 0.0330  3   SER A CA    
20   C  C     . SER A 23  ? 0.2267 0.2537 0.1963 -0.0180 -0.0390 0.0347  3   SER A C     
21   O  O     . SER A 23  ? 0.2293 0.2536 0.2314 -0.0338 -0.0283 0.0368  3   SER A O     
22   C  CB    A SER A 23  ? 0.2542 0.2994 0.2032 -0.0186 -0.0457 0.0277  3   SER A CB    
23   C  CB    B SER A 23  ? 0.2483 0.2878 0.2014 -0.0001 -0.0508 0.0212  3   SER A CB    
24   O  OG    A SER A 23  ? 0.2831 0.3193 0.2133 -0.0229 -0.0397 0.0258  3   SER A OG    
25   O  OG    B SER A 23  ? 0.2790 0.3003 0.2141 0.0081  -0.0493 0.0122  3   SER A OG    
26   N  N     . LYS A 24  ? 0.2034 0.2300 0.1838 -0.0090 -0.0430 0.0176  4   LYS A N     
27   C  CA    . LYS A 24  ? 0.2241 0.2206 0.1854 -0.0137 -0.0380 0.0102  4   LYS A CA    
28   C  C     . LYS A 24  ? 0.2125 0.1846 0.1771 -0.0129 -0.0239 0.0258  4   LYS A C     
29   O  O     . LYS A 24  ? 0.2058 0.1851 0.1823 -0.0085 -0.0324 0.0325  4   LYS A O     
30   C  CB    . LYS A 24  ? 0.2739 0.2634 0.2043 -0.0141 -0.0450 -0.0173 4   LYS A CB    
31   C  CG    . LYS A 24  ? 0.3242 0.3004 0.2350 -0.0150 -0.0504 -0.0275 4   LYS A CG    
32   C  CD    . LYS A 24  ? 0.3693 0.3199 0.2611 -0.0225 -0.0390 -0.0222 4   LYS A CD    
33   N  N     . ILE A 25  ? 0.1927 0.1718 0.1677 -0.0034 -0.0227 0.0244  5   ILE A N     
34   C  CA    . ILE A 25  ? 0.1882 0.1560 0.1513 -0.0073 -0.0173 0.0134  5   ILE A CA    
35   C  C     . ILE A 25  ? 0.1962 0.1425 0.1509 -0.0044 -0.0185 0.0150  5   ILE A C     
36   O  O     . ILE A 25  ? 0.2132 0.1366 0.1521 -0.0019 -0.0092 0.0171  5   ILE A O     
37   C  CB    . ILE A 25  ? 0.1822 0.1581 0.1517 -0.0094 -0.0025 0.0241  5   ILE A CB    
38   C  CG1   . ILE A 25  ? 0.1854 0.1709 0.1670 -0.0068 0.0071  0.0264  5   ILE A CG1   
39   C  CG2   . ILE A 25  ? 0.1946 0.1577 0.1474 -0.0052 0.0016  0.0178  5   ILE A CG2   
40   C  CD1   . ILE A 25  ? 0.1831 0.1842 0.1743 -0.0072 -0.0009 0.0204  5   ILE A CD1   
41   N  N     . ASN A 26  ? 0.1922 0.1482 0.1414 -0.0039 0.0018  0.0113  6   ASN A N     
42   C  CA    . ASN A 26  ? 0.1922 0.1416 0.1352 -0.0064 -0.0009 0.0066  6   ASN A CA    
43   C  C     . ASN A 26  ? 0.1971 0.1376 0.1360 0.0070  -0.0044 0.0013  6   ASN A C     
44   O  O     . ASN A 26  ? 0.1948 0.1385 0.1327 0.0041  0.0040  0.0001  6   ASN A O     
45   C  CB    . ASN A 26  ? 0.2227 0.1445 0.1306 -0.0019 0.0038  -0.0011 6   ASN A CB    
46   C  CG    . ASN A 26  ? 0.2339 0.1530 0.1319 0.0010  0.0039  0.0058  6   ASN A CG    
47   O  OD1   . ASN A 26  ? 0.2238 0.1470 0.1331 0.0003  -0.0048 0.0034  6   ASN A OD1   
48   N  ND2   . ASN A 26  ? 0.2759 0.1813 0.1414 -0.0251 -0.0079 0.0105  6   ASN A ND2   
49   N  N     . GLY A 27  ? 0.1888 0.1423 0.1339 0.0137  -0.0038 0.0003  7   GLY A N     
50   C  CA    . GLY A 27  ? 0.1865 0.1461 0.1417 0.0090  0.0098  0.0011  7   GLY A CA    
51   C  C     . GLY A 27  ? 0.1714 0.1428 0.1318 0.0158  0.0223  0.0066  7   GLY A C     
52   O  O     . GLY A 27  ? 0.1921 0.1540 0.1204 0.0182  0.0168  0.0036  7   GLY A O     
53   N  N     . LYS A 28  ? 0.1808 0.1419 0.1289 0.0121  0.0182  0.0100  8   LYS A N     
54   C  CA    . LYS A 28  ? 0.1747 0.1445 0.1241 0.0064  0.0080  0.0172  8   LYS A CA    
55   C  C     . LYS A 28  ? 0.1736 0.1390 0.1226 0.0095  0.0033  0.0268  8   LYS A C     
56   O  O     . LYS A 28  ? 0.1944 0.1355 0.1188 0.0018  0.0177  0.0131  8   LYS A O     
57   C  CB    . LYS A 28  ? 0.1695 0.1559 0.1336 -0.0027 0.0124  0.0136  8   LYS A CB    
58   C  CG    . LYS A 28  ? 0.1767 0.1655 0.1426 -0.0032 0.0042  0.0192  8   LYS A CG    
59   C  CD    . LYS A 28  ? 0.1888 0.1688 0.1542 -0.0069 0.0020  0.0125  8   LYS A CD    
60   C  CE    . LYS A 28  ? 0.1894 0.1793 0.1652 -0.0185 0.0111  0.0105  8   LYS A CE    
61   N  NZ    . LYS A 28  ? 0.1873 0.1814 0.1642 -0.0259 0.0056  0.0141  8   LYS A NZ    
62   N  N     . LEU A 29  ? 0.1660 0.1422 0.1171 0.0121  0.0076  0.0155  9   LEU A N     
63   C  CA    . LEU A 29  ? 0.1719 0.1326 0.1270 0.0100  0.0047  0.0166  9   LEU A CA    
64   C  C     . LEU A 29  ? 0.1789 0.1280 0.1278 0.0069  0.0025  0.0112  9   LEU A C     
65   O  O     . LEU A 29  ? 0.1833 0.1299 0.1228 0.0150  0.0154  0.0096  9   LEU A O     
66   C  CB    . LEU A 29  ? 0.1716 0.1350 0.1294 0.0005  0.0047  0.0180  9   LEU A CB    
67   C  CG    . LEU A 29  ? 0.1670 0.1478 0.1461 0.0065  0.0038  0.0149  9   LEU A CG    
68   C  CD1   . LEU A 29  ? 0.1674 0.1562 0.1765 0.0187  0.0124  -0.0006 9   LEU A CD1   
69   C  CD2   . LEU A 29  ? 0.1850 0.1633 0.1443 0.0012  0.0068  0.0195  9   LEU A CD2   
70   N  N     . PHE A 30  ? 0.1799 0.1248 0.1168 0.0120  0.0079  0.0162  10  PHE A N     
71   C  CA    . PHE A 30  ? 0.1779 0.1237 0.1241 0.0041  0.0050  0.0159  10  PHE A CA    
72   C  C     . PHE A 30  ? 0.1647 0.1240 0.1272 0.0046  0.0079  0.0190  10  PHE A C     
73   O  O     . PHE A 30  ? 0.1726 0.1285 0.1206 0.0090  0.0102  0.0145  10  PHE A O     
74   C  CB    . PHE A 30  ? 0.1806 0.1223 0.1258 0.0027  0.0052  0.0145  10  PHE A CB    
75   C  CG    . PHE A 30  ? 0.1937 0.1247 0.1455 -0.0033 0.0043  0.0147  10  PHE A CG    
76   C  CD1   . PHE A 30  ? 0.1985 0.1382 0.1519 0.0058  0.0145  0.0287  10  PHE A CD1   
77   C  CD2   . PHE A 30  ? 0.1915 0.1201 0.1494 0.0021  -0.0094 0.0133  10  PHE A CD2   
78   C  CE1   . PHE A 30  ? 0.1980 0.1489 0.1600 0.0052  0.0075  0.0267  10  PHE A CE1   
79   C  CE2   . PHE A 30  ? 0.1901 0.1245 0.1608 0.0081  -0.0124 0.0272  10  PHE A CE2   
80   C  CZ    . PHE A 30  ? 0.1971 0.1426 0.1643 -0.0086 -0.0068 0.0259  10  PHE A CZ    
81   N  N     . ALA A 31  ? 0.1693 0.1250 0.1208 0.0017  0.0116  0.0132  11  ALA A N     
82   C  CA    . ALA A 31  ? 0.1694 0.1244 0.1318 0.0001  0.0140  0.0153  11  ALA A CA    
83   C  C     . ALA A 31  ? 0.1695 0.1271 0.1260 0.0055  0.0164  0.0096  11  ALA A C     
84   O  O     . ALA A 31  ? 0.1707 0.1376 0.1287 0.0078  0.0135  0.0058  11  ALA A O     
85   C  CB    . ALA A 31  ? 0.1690 0.1447 0.1378 -0.0011 0.0207  0.0143  11  ALA A CB    
86   N  N     . ASP A 32  ? 0.1874 0.1248 0.1287 0.0148  0.0154  0.0128  12  ASP A N     
87   C  CA    . ASP A 32  ? 0.1840 0.1296 0.1258 0.0112  0.0112  0.0252  12  ASP A CA    
88   C  C     . ASP A 32  ? 0.1636 0.1229 0.1261 0.0076  0.0115  0.0219  12  ASP A C     
89   O  O     . ASP A 32  ? 0.1727 0.1241 0.1338 0.0028  0.0114  0.0107  12  ASP A O     
90   C  CB    . ASP A 32  ? 0.1857 0.1420 0.1351 0.0133  0.0218  0.0265  12  ASP A CB    
91   C  CG    . ASP A 32  ? 0.1861 0.1517 0.1504 0.0164  0.0209  0.0313  12  ASP A CG    
92   O  OD1   . ASP A 32  ? 0.1896 0.1675 0.1621 0.0003  0.0222  0.0322  12  ASP A OD1   
93   O  OD2   . ASP A 32  ? 0.1955 0.1587 0.1513 0.0078  0.0181  0.0354  12  ASP A OD2   
94   N  N     . MET A 33  ? 0.1713 0.1194 0.1221 0.0049  0.0044  0.0146  13  MET A N     
95   C  CA    . MET A 33  ? 0.1612 0.1228 0.1302 0.0006  0.0184  0.0143  13  MET A CA    
96   C  C     . MET A 33  ? 0.1595 0.1266 0.1256 0.0031  0.0099  0.0152  13  MET A C     
97   O  O     . MET A 33  ? 0.1720 0.1214 0.1299 -0.0031 0.0192  0.0065  13  MET A O     
98   C  CB    . MET A 33  ? 0.1708 0.1382 0.1296 0.0014  0.0154  0.0151  13  MET A CB    
99   C  CG    . MET A 33  ? 0.1756 0.1329 0.1396 0.0054  0.0061  0.0145  13  MET A CG    
100  S  SD    . MET A 33  ? 0.1762 0.1491 0.1452 0.0045  -0.0009 -0.0031 13  MET A SD    
101  C  CE    . MET A 33  ? 0.2118 0.1695 0.1609 -0.0131 0.0141  -0.0105 13  MET A CE    
102  N  N     . ILE A 34  ? 0.1612 0.1291 0.1221 0.0090  0.0079  0.0145  14  ILE A N     
103  C  CA    . ILE A 34  ? 0.1648 0.1252 0.1266 0.0083  0.0103  0.0169  14  ILE A CA    
104  C  C     . ILE A 34  ? 0.1625 0.1287 0.1354 0.0020  0.0135  0.0155  14  ILE A C     
105  O  O     . ILE A 34  ? 0.1656 0.1444 0.1327 0.0004  0.0103  0.0115  14  ILE A O     
106  C  CB    . ILE A 34  ? 0.1675 0.1320 0.1332 0.0090  0.0136  0.0168  14  ILE A CB    
107  C  CG1   . ILE A 34  ? 0.1732 0.1171 0.1423 0.0112  0.0026  0.0041  14  ILE A CG1   
108  C  CG2   . ILE A 34  ? 0.1701 0.1454 0.1446 0.0059  -0.0055 0.0107  14  ILE A CG2   
109  C  CD1   . ILE A 34  ? 0.1668 0.1191 0.1478 0.0001  0.0024  0.0050  14  ILE A CD1   
110  N  N     . ILE A 35  ? 0.1546 0.1352 0.1436 -0.0070 0.0188  0.0073  15  ILE A N     
111  C  CA    . ILE A 35  ? 0.1558 0.1459 0.1525 -0.0108 0.0184  0.0098  15  ILE A CA    
112  C  C     . ILE A 35  ? 0.1536 0.1338 0.1444 -0.0144 0.0212  0.0053  15  ILE A C     
113  O  O     . ILE A 35  ? 0.1772 0.1353 0.1514 -0.0183 0.0125  -0.0007 15  ILE A O     
114  C  CB    . ILE A 35  ? 0.1669 0.1706 0.1637 -0.0325 0.0318  0.0116  15  ILE A CB    
115  C  CG1   . ILE A 35  ? 0.1858 0.1958 0.1722 -0.0204 0.0338  0.0058  15  ILE A CG1   
116  C  CG2   . ILE A 35  ? 0.2122 0.1786 0.1741 -0.0446 0.0260  0.0185  15  ILE A CG2   
117  C  CD1   . ILE A 35  ? 0.2066 0.2097 0.1759 -0.0222 0.0398  0.0140  15  ILE A CD1   
118  N  N     . GLN A 36  ? 0.1615 0.1186 0.1500 -0.0128 0.0171  0.0074  16  GLN A N     
119  C  CA    . GLN A 36  ? 0.1748 0.1302 0.1502 -0.0063 0.0157  0.0106  16  GLN A CA    
120  C  C     . GLN A 36  ? 0.1742 0.1156 0.1501 -0.0067 0.0181  0.0075  16  GLN A C     
121  O  O     . GLN A 36  ? 0.1906 0.1131 0.1551 -0.0017 0.0308  0.0011  16  GLN A O     
122  C  CB    . GLN A 36  ? 0.1902 0.1337 0.1630 -0.0055 0.0138  0.0181  16  GLN A CB    
123  C  CG    . GLN A 36  ? 0.2174 0.1260 0.1773 -0.0079 0.0119  0.0230  16  GLN A CG    
124  C  CD    . GLN A 36  ? 0.2378 0.1523 0.1962 -0.0107 0.0169  0.0268  16  GLN A CD    
125  O  OE1   . GLN A 36  ? 0.2371 0.1397 0.2146 -0.0219 0.0072  0.0224  16  GLN A OE1   
126  N  NE2   . GLN A 36  ? 0.2557 0.1931 0.2156 -0.0304 0.0293  0.0201  16  GLN A NE2   
127  N  N     . GLY A 37  ? 0.1685 0.1162 0.1449 -0.0106 0.0189  0.0069  17  GLY A N     
128  C  CA    . GLY A 37  ? 0.1674 0.1203 0.1475 -0.0194 0.0134  0.0103  17  GLY A CA    
129  C  C     . GLY A 37  ? 0.1560 0.1225 0.1472 -0.0056 0.0094  0.0059  17  GLY A C     
130  O  O     . GLY A 37  ? 0.1711 0.1309 0.1468 -0.0162 0.0217  -0.0022 17  GLY A O     
131  N  N     . ALA A 38  ? 0.1553 0.1268 0.1419 -0.0147 0.0135  0.0032  18  ALA A N     
132  C  CA    . ALA A 38  ? 0.1579 0.1350 0.1534 -0.0192 0.0029  0.0096  18  ALA A CA    
133  C  C     . ALA A 38  ? 0.1662 0.1270 0.1557 -0.0207 0.0188  0.0042  18  ALA A C     
134  O  O     . ALA A 38  ? 0.1938 0.1336 0.1513 -0.0189 0.0164  -0.0056 18  ALA A O     
135  C  CB    . ALA A 38  ? 0.1630 0.1502 0.1609 -0.0175 -0.0037 0.0038  18  ALA A CB    
136  N  N     . GLN A 39  ? 0.1808 0.1174 0.1628 -0.0238 0.0169  0.0031  19  GLN A N     
137  C  CA    . GLN A 39  ? 0.1805 0.1209 0.1724 -0.0376 0.0165  0.0079  19  GLN A CA    
138  C  C     . GLN A 39  ? 0.1884 0.1281 0.1739 -0.0306 0.0197  0.0085  19  GLN A C     
139  O  O     . GLN A 39  ? 0.2018 0.1265 0.1781 -0.0289 0.0190  -0.0086 19  GLN A O     
140  C  CB    . GLN A 39  ? 0.1911 0.1236 0.1846 -0.0341 0.0259  0.0168  19  GLN A CB    
141  C  CG    . GLN A 39  ? 0.2257 0.1552 0.2132 -0.0432 0.0405  0.0056  19  GLN A CG    
142  C  CD    . GLN A 39  ? 0.2520 0.1953 0.2419 -0.0568 0.0521  -0.0154 19  GLN A CD    
143  O  OE1   . GLN A 39  ? 0.2715 0.2379 0.2592 -0.0622 0.0547  -0.0307 19  GLN A OE1   
144  N  NE2   . GLN A 39  ? 0.2650 0.1975 0.2539 -0.0732 0.0469  -0.0276 19  GLN A NE2   
145  N  N     . ASN A 40  ? 0.1805 0.1109 0.1758 -0.0158 0.0204  0.0013  20  ASN A N     
146  C  CA    . ASN A 40  ? 0.1818 0.1157 0.1929 -0.0124 0.0266  0.0005  20  ASN A CA    
147  C  C     . ASN A 40  ? 0.2034 0.1151 0.1844 -0.0290 0.0288  -0.0080 20  ASN A C     
148  O  O     . ASN A 40  ? 0.2330 0.1298 0.1870 -0.0109 0.0440  -0.0173 20  ASN A O     
149  C  CB    . ASN A 40  ? 0.1828 0.1244 0.2154 -0.0120 0.0364  0.0081  20  ASN A CB    
150  C  CG    . ASN A 40  ? 0.2104 0.1222 0.2536 -0.0126 0.0257  -0.0041 20  ASN A CG    
151  O  OD1   . ASN A 40  ? 0.2441 0.1280 0.2961 -0.0077 0.0238  -0.0131 20  ASN A OD1   
152  N  ND2   . ASN A 40  ? 0.1935 0.1282 0.2481 -0.0057 0.0493  -0.0018 20  ASN A ND2   
153  N  N     . LEU A 41  ? 0.1924 0.1175 0.1645 -0.0207 0.0324  -0.0038 21  LEU A N     
154  C  CA    . LEU A 41  ? 0.1908 0.1245 0.1599 -0.0266 0.0250  -0.0072 21  LEU A CA    
155  C  C     . LEU A 41  ? 0.1973 0.1406 0.1638 -0.0349 0.0322  -0.0216 21  LEU A C     
156  O  O     . LEU A 41  ? 0.2297 0.1528 0.1607 -0.0430 0.0341  -0.0262 21  LEU A O     
157  C  CB    . LEU A 41  ? 0.1885 0.1293 0.1536 -0.0240 0.0148  -0.0053 21  LEU A CB    
158  C  CG    . LEU A 41  ? 0.1884 0.1387 0.1566 -0.0305 0.0053  0.0044  21  LEU A CG    
159  C  CD1   . LEU A 41  ? 0.1936 0.1514 0.1621 -0.0336 0.0090  0.0092  21  LEU A CD1   
160  C  CD2   . LEU A 41  ? 0.1888 0.1508 0.1615 -0.0261 -0.0084 0.0170  21  LEU A CD2   
161  N  N     . SER A 42  ? 0.2060 0.1490 0.1706 -0.0533 0.0279  -0.0205 22  SER A N     
162  C  CA    A SER A 42  ? 0.2150 0.1591 0.1802 -0.0580 0.0299  -0.0252 22  SER A CA    
163  C  CA    B SER A 42  ? 0.2243 0.1598 0.1812 -0.0567 0.0263  -0.0219 22  SER A CA    
164  C  C     . SER A 42  ? 0.2338 0.1482 0.1829 -0.0673 0.0341  -0.0273 22  SER A C     
165  O  O     . SER A 42  ? 0.2579 0.1627 0.1886 -0.0647 0.0220  -0.0310 22  SER A O     
166  C  CB    A SER A 42  ? 0.2059 0.1758 0.1858 -0.0686 0.0250  -0.0261 22  SER A CB    
167  C  CB    B SER A 42  ? 0.2325 0.1789 0.1893 -0.0626 0.0134  -0.0162 22  SER A CB    
168  O  OG    A SER A 42  ? 0.1998 0.1949 0.1878 -0.0776 0.0224  -0.0322 22  SER A OG    
169  O  OG    B SER A 42  ? 0.2468 0.1994 0.1945 -0.0655 0.0050  -0.0167 22  SER A OG    
170  N  N     . ASN A 43  ? 0.2452 0.1436 0.1980 -0.0623 0.0430  -0.0297 23  ASN A N     
171  C  CA    . ASN A 43  ? 0.2646 0.1373 0.2134 -0.0572 0.0490  -0.0283 23  ASN A CA    
172  C  C     . ASN A 43  ? 0.2754 0.1407 0.2194 -0.0492 0.0574  -0.0337 23  ASN A C     
173  O  O     . ASN A 43  ? 0.3051 0.1628 0.2380 -0.0515 0.0716  -0.0440 23  ASN A O     
174  C  CB    . ASN A 43  ? 0.2911 0.1448 0.2244 -0.0491 0.0468  -0.0184 23  ASN A CB    
175  C  CG    . ASN A 43  ? 0.2865 0.1421 0.2352 -0.0432 0.0455  -0.0079 23  ASN A CG    
176  O  OD1   . ASN A 43  ? 0.2978 0.1443 0.2421 -0.0508 0.0453  -0.0037 23  ASN A OD1   
177  N  ND2   . ASN A 43  ? 0.3067 0.1591 0.2459 -0.0379 0.0372  0.0012  23  ASN A ND2   
178  N  N     . ASN A 44  ? 0.2535 0.1444 0.2130 -0.0513 0.0603  -0.0291 24  ASN A N     
179  C  CA    . ASN A 44  ? 0.2457 0.1589 0.2103 -0.0469 0.0557  -0.0290 24  ASN A CA    
180  C  C     . ASN A 44  ? 0.2455 0.1563 0.1945 -0.0456 0.0461  -0.0346 24  ASN A C     
181  O  O     . ASN A 44  ? 0.2524 0.1685 0.1925 -0.0509 0.0485  -0.0361 24  ASN A O     
182  C  CB    . ASN A 44  ? 0.2479 0.1938 0.2170 -0.0320 0.0597  -0.0300 24  ASN A CB    
183  C  CG    . ASN A 44  ? 0.2661 0.2251 0.2326 -0.0025 0.0596  -0.0361 24  ASN A CG    
184  O  OD1   . ASN A 44  ? 0.2881 0.2762 0.2488 0.0315  0.0643  -0.0495 24  ASN A OD1   
185  N  ND2   . ASN A 44  ? 0.2694 0.2094 0.2345 0.0011  0.0534  -0.0232 24  ASN A ND2   
186  N  N     . ALA A 45  ? 0.2378 0.1555 0.1889 -0.0471 0.0384  -0.0262 25  ALA A N     
187  C  CA    . ALA A 45  ? 0.2367 0.1634 0.1900 -0.0497 0.0397  -0.0277 25  ALA A CA    
188  C  C     . ALA A 45  ? 0.2400 0.1663 0.1914 -0.0737 0.0345  -0.0372 25  ALA A C     
189  O  O     . ALA A 45  ? 0.2473 0.1781 0.1845 -0.0624 0.0385  -0.0330 25  ALA A O     
190  C  CB    . ALA A 45  ? 0.2431 0.1883 0.1995 -0.0392 0.0351  -0.0183 25  ALA A CB    
191  N  N     . ASP A 46  ? 0.2770 0.1664 0.1936 -0.0723 0.0340  -0.0340 26  ASP A N     
192  C  CA    . ASP A 46  ? 0.2980 0.1756 0.2119 -0.0875 0.0351  -0.0558 26  ASP A CA    
193  C  C     . ASP A 46  ? 0.2870 0.1557 0.1994 -0.0677 0.0350  -0.0516 26  ASP A C     
194  O  O     . ASP A 46  ? 0.2992 0.1763 0.1973 -0.0601 0.0265  -0.0444 26  ASP A O     
195  C  CB    . ASP A 46  ? 0.3464 0.2052 0.2468 -0.1077 0.0367  -0.0538 26  ASP A CB    
196  C  CG    . ASP A 46  ? 0.4077 0.2356 0.2938 -0.1254 0.0264  -0.0383 26  ASP A CG    
197  O  OD1   . ASP A 46  ? 0.4248 0.2652 0.3133 -0.1264 0.0115  -0.0331 26  ASP A OD1   
198  O  OD2   . ASP A 46  ? 0.4423 0.2571 0.3137 -0.1255 0.0260  -0.0227 26  ASP A OD2   
199  N  N     . LEU A 47  ? 0.2804 0.1584 0.2108 -0.0547 0.0449  -0.0430 27  LEU A N     
200  C  CA    . LEU A 47  ? 0.2718 0.1606 0.2146 -0.0289 0.0490  -0.0410 27  LEU A CA    
201  C  C     . LEU A 47  ? 0.2601 0.1550 0.2042 -0.0354 0.0555  -0.0377 27  LEU A C     
202  O  O     . LEU A 47  ? 0.2546 0.1706 0.2061 -0.0313 0.0492  -0.0434 27  LEU A O     
203  C  CB    . LEU A 47  ? 0.2897 0.2006 0.2302 -0.0162 0.0496  -0.0269 27  LEU A CB    
204  C  CG    . LEU A 47  ? 0.3183 0.2504 0.2507 -0.0138 0.0415  -0.0128 27  LEU A CG    
205  C  CD1   . LEU A 47  ? 0.3564 0.2802 0.2676 -0.0189 0.0388  -0.0192 27  LEU A CD1   
206  C  CD2   . LEU A 47  ? 0.3277 0.2756 0.2565 -0.0140 0.0303  0.0004  27  LEU A CD2   
207  N  N     . VAL A 48  ? 0.2451 0.1523 0.1804 -0.0485 0.0541  -0.0402 28  VAL A N     
208  C  CA    . VAL A 48  ? 0.2374 0.1554 0.1761 -0.0554 0.0402  -0.0293 28  VAL A CA    
209  C  C     . VAL A 48  ? 0.2503 0.1696 0.1678 -0.0677 0.0403  -0.0295 28  VAL A C     
210  O  O     . VAL A 48  ? 0.2591 0.1926 0.1711 -0.0885 0.0385  -0.0272 28  VAL A O     
211  C  CB    . VAL A 48  ? 0.2047 0.1503 0.1674 -0.0478 0.0204  -0.0210 28  VAL A CB    
212  C  CG1   . VAL A 48  ? 0.1980 0.1441 0.1667 -0.0377 0.0123  -0.0145 28  VAL A CG1   
213  C  CG2   . VAL A 48  ? 0.2151 0.1542 0.1712 -0.0367 0.0179  -0.0283 28  VAL A CG2   
214  N  N     . ASP A 49  ? 0.2422 0.1869 0.1614 -0.0636 0.0340  -0.0327 29  ASP A N     
215  C  CA    . ASP A 49  ? 0.2400 0.1921 0.1686 -0.0545 0.0261  -0.0232 29  ASP A CA    
216  C  C     . ASP A 49  ? 0.2201 0.1981 0.1712 -0.0322 0.0204  -0.0181 29  ASP A C     
217  O  O     . ASP A 49  ? 0.2181 0.2153 0.1745 -0.0372 0.0024  -0.0246 29  ASP A O     
218  C  CB    . ASP A 49  ? 0.2400 0.2008 0.1754 -0.0637 0.0367  -0.0282 29  ASP A CB    
219  C  CG    . ASP A 49  ? 0.2434 0.2032 0.1897 -0.0767 0.0321  -0.0381 29  ASP A CG    
220  O  OD1   . ASP A 49  ? 0.2723 0.2069 0.1835 -0.0755 0.0325  -0.0437 29  ASP A OD1   
221  O  OD2   . ASP A 49  ? 0.2506 0.2235 0.2032 -0.0761 0.0303  -0.0416 29  ASP A OD2   
222  N  N     . SER A 50  ? 0.2367 0.1872 0.1735 -0.0338 0.0266  -0.0289 30  SER A N     
223  C  CA    . SER A 50  ? 0.2524 0.1878 0.1878 -0.0197 0.0320  -0.0325 30  SER A CA    
224  C  C     . SER A 50  ? 0.2411 0.1911 0.1873 -0.0197 0.0287  -0.0289 30  SER A C     
225  O  O     . SER A 50  ? 0.2521 0.2122 0.2083 -0.0140 0.0367  -0.0307 30  SER A O     
226  C  CB    . SER A 50  ? 0.2632 0.1911 0.1987 -0.0189 0.0197  -0.0326 30  SER A CB    
227  O  OG    . SER A 50  ? 0.3099 0.2035 0.2155 -0.0046 0.0228  -0.0287 30  SER A OG    
228  N  N     . LEU A 51  ? 0.2224 0.1769 0.1734 -0.0294 0.0281  -0.0250 31  LEU A N     
229  C  CA    . LEU A 51  ? 0.2166 0.1693 0.1721 -0.0300 0.0223  -0.0154 31  LEU A CA    
230  C  C     . LEU A 51  ? 0.1939 0.1642 0.1497 -0.0277 0.0048  -0.0260 31  LEU A C     
231  O  O     . LEU A 51  ? 0.1791 0.1583 0.1575 -0.0209 0.0017  -0.0090 31  LEU A O     
232  C  CB    . LEU A 51  ? 0.2308 0.1814 0.2010 -0.0190 0.0021  0.0096  31  LEU A CB    
233  C  CG    . LEU A 51  ? 0.2403 0.2073 0.2236 -0.0202 -0.0110 0.0270  31  LEU A CG    
234  C  CD1   . LEU A 51  ? 0.2658 0.2258 0.2349 -0.0241 -0.0272 0.0291  31  LEU A CD1   
235  C  CD2   . LEU A 51  ? 0.2343 0.2278 0.2426 -0.0074 -0.0075 0.0355  31  LEU A CD2   
236  N  N     . ASN A 52  ? 0.1787 0.1717 0.1404 -0.0248 0.0078  -0.0246 32  ASN A N     
237  C  CA    . ASN A 52  ? 0.1632 0.1760 0.1358 -0.0058 -0.0041 -0.0298 32  ASN A CA    
238  C  C     . ASN A 52  ? 0.1702 0.1818 0.1369 0.0057  -0.0167 -0.0246 32  ASN A C     
239  O  O     . ASN A 52  ? 0.2352 0.1686 0.1503 -0.0026 -0.0272 -0.0209 32  ASN A O     
240  C  CB    . ASN A 52  ? 0.1734 0.1869 0.1473 -0.0127 -0.0013 -0.0341 32  ASN A CB    
241  C  CG    . ASN A 52  ? 0.1480 0.1888 0.1334 -0.0236 -0.0005 -0.0342 32  ASN A CG    
242  O  OD1   . ASN A 52  ? 0.1444 0.2035 0.1396 -0.0230 0.0026  -0.0422 32  ASN A OD1   
243  N  ND2   . ASN A 52  ? 0.1467 0.1947 0.1318 -0.0117 0.0110  -0.0225 32  ASN A ND2   
244  N  N     . VAL A 53  ? 0.1515 0.2313 0.1317 -0.0040 -0.0150 -0.0034 33  VAL A N     
245  C  CA    . VAL A 53  ? 0.1703 0.2822 0.1320 0.0074  0.0000  0.0150  33  VAL A CA    
246  C  C     . VAL A 53  ? 0.1697 0.2884 0.1415 -0.0103 -0.0017 0.0356  33  VAL A C     
247  O  O     . VAL A 53  ? 0.2259 0.3272 0.1462 -0.0408 -0.0147 0.0337  33  VAL A O     
248  C  CB    . VAL A 53  ? 0.1760 0.3199 0.1436 0.0213  0.0028  0.0142  33  VAL A CB    
249  C  CG1   . VAL A 53  ? 0.1837 0.3291 0.1575 0.0522  0.0069  -0.0024 33  VAL A CG1   
250  C  CG2   . VAL A 53  ? 0.1714 0.3324 0.1445 0.0229  0.0028  0.0156  33  VAL A CG2   
251  N  N     . TYR A 54  ? 0.1839 0.2649 0.1663 0.0037  0.0182  0.0358  34  TYR A N     
252  C  CA    . TYR A 54  ? 0.1781 0.2564 0.1785 -0.0090 0.0212  0.0267  34  TYR A CA    
253  C  C     . TYR A 54  ? 0.1627 0.2328 0.1723 -0.0012 -0.0008 0.0080  34  TYR A C     
254  O  O     . TYR A 54  ? 0.1627 0.2365 0.1713 -0.0113 -0.0116 0.0239  34  TYR A O     
255  C  CB    . TYR A 54  ? 0.1775 0.2886 0.2040 -0.0052 0.0120  0.0272  34  TYR A CB    
256  C  CG    . TYR A 54  ? 0.1521 0.3142 0.2541 -0.0285 -0.0007 0.0337  34  TYR A CG    
257  C  CD1   . TYR A 54  ? 0.1916 0.3252 0.3031 -0.0479 -0.0291 0.0428  34  TYR A CD1   
258  C  CD2   . TYR A 54  ? 0.1879 0.3283 0.2976 -0.0328 -0.0057 0.0167  34  TYR A CD2   
259  C  CE1   . TYR A 54  ? 0.2253 0.3292 0.3387 -0.0678 -0.0486 0.0361  34  TYR A CE1   
260  C  CE2   . TYR A 54  ? 0.2165 0.3347 0.3356 -0.0487 -0.0186 0.0049  34  TYR A CE2   
261  C  CZ    . TYR A 54  ? 0.2490 0.3300 0.3671 -0.0584 -0.0438 0.0135  34  TYR A CZ    
262  O  OH    . TYR A 54  ? 0.3204 0.3405 0.4117 -0.0441 -0.0569 0.0042  34  TYR A OH    
263  N  N     . PRO A 55  ? 0.1780 0.2047 0.1653 -0.0143 -0.0007 -0.0104 35  PRO A N     
264  C  CA    . PRO A 55  ? 0.1920 0.2022 0.1624 -0.0061 0.0056  -0.0107 35  PRO A CA    
265  C  C     . PRO A 55  ? 0.2032 0.2071 0.1489 -0.0066 0.0130  -0.0109 35  PRO A C     
266  O  O     . PRO A 55  ? 0.2232 0.2597 0.1643 -0.0222 0.0258  -0.0165 35  PRO A O     
267  C  CB    . PRO A 55  ? 0.2074 0.1995 0.1724 -0.0080 -0.0068 -0.0122 35  PRO A CB    
268  C  CG    . PRO A 55  ? 0.2199 0.2083 0.1760 -0.0054 -0.0146 -0.0121 35  PRO A CG    
269  C  CD    . PRO A 55  ? 0.2046 0.2022 0.1665 -0.0081 -0.0124 -0.0151 35  PRO A CD    
270  N  N     . VAL A 56  ? 0.1984 0.1617 0.1404 -0.0077 0.0178  -0.0212 36  VAL A N     
271  C  CA    . VAL A 56  ? 0.2005 0.1573 0.1410 0.0065  -0.0009 -0.0255 36  VAL A CA    
272  C  C     . VAL A 56  ? 0.1890 0.1569 0.1293 0.0001  -0.0003 -0.0177 36  VAL A C     
273  O  O     . VAL A 56  ? 0.1936 0.1523 0.1231 -0.0055 0.0044  -0.0106 36  VAL A O     
274  C  CB    . VAL A 56  ? 0.2278 0.1646 0.1515 0.0181  -0.0189 -0.0232 36  VAL A CB    
275  C  CG1   . VAL A 56  ? 0.2296 0.1718 0.1509 0.0169  -0.0296 -0.0218 36  VAL A CG1   
276  C  CG2   . VAL A 56  ? 0.2691 0.1712 0.1654 0.0285  -0.0248 -0.0181 36  VAL A CG2   
277  N  N     . PRO A 57  ? 0.1860 0.1492 0.1233 0.0014  -0.0007 -0.0197 37  PRO A N     
278  C  CA    . PRO A 57  ? 0.2013 0.1527 0.1232 0.0030  -0.0161 -0.0216 37  PRO A CA    
279  C  C     . PRO A 57  ? 0.2157 0.1656 0.1158 -0.0195 -0.0093 -0.0219 37  PRO A C     
280  O  O     . PRO A 57  ? 0.2552 0.1759 0.1381 -0.0434 0.0109  -0.0345 37  PRO A O     
281  C  CB    . PRO A 57  ? 0.2130 0.1716 0.1297 0.0080  -0.0093 -0.0283 37  PRO A CB    
282  C  CG    . PRO A 57  ? 0.1967 0.1726 0.1320 -0.0063 -0.0043 -0.0258 37  PRO A CG    
283  C  CD    . PRO A 57  ? 0.2054 0.1654 0.1284 -0.0078 0.0120  -0.0233 37  PRO A CD    
284  N  N     . ASP A 58  ? 0.2063 0.1719 0.1283 -0.0276 -0.0139 -0.0249 38  ASP A N     
285  C  CA    . ASP A 58  ? 0.2102 0.2122 0.1355 -0.0459 -0.0100 -0.0316 38  ASP A CA    
286  C  C     . ASP A 58  ? 0.2046 0.2231 0.1490 -0.0656 -0.0004 -0.0345 38  ASP A C     
287  O  O     . ASP A 58  ? 0.2160 0.2684 0.1712 -0.0713 -0.0157 -0.0262 38  ASP A O     
288  C  CB    . ASP A 58  ? 0.2003 0.2325 0.1383 -0.0335 -0.0072 -0.0357 38  ASP A CB    
289  C  CG    . ASP A 58  ? 0.2040 0.2415 0.1476 -0.0197 -0.0073 -0.0369 38  ASP A CG    
290  O  OD1   . ASP A 58  ? 0.1802 0.2371 0.1364 -0.0456 -0.0061 -0.0368 38  ASP A OD1   
291  O  OD2   . ASP A 58  ? 0.2198 0.2451 0.1489 -0.0111 -0.0207 -0.0473 38  ASP A OD2   
292  N  N     . GLY A 59  ? 0.2358 0.1981 0.1473 -0.0565 0.0052  -0.0370 39  GLY A N     
293  C  CA    . GLY A 59  ? 0.2703 0.1899 0.1661 -0.0536 0.0016  -0.0316 39  GLY A CA    
294  C  C     . GLY A 59  ? 0.2618 0.1885 0.1610 -0.0676 -0.0067 -0.0224 39  GLY A C     
295  O  O     . GLY A 59  ? 0.2931 0.1922 0.1747 -0.0741 -0.0064 -0.0232 39  GLY A O     
296  N  N     . ASP A 60  ? 0.2378 0.1991 0.1515 -0.0688 -0.0062 -0.0279 40  ASP A N     
297  C  CA    . ASP A 60  ? 0.2069 0.2334 0.1578 -0.0605 -0.0017 -0.0144 40  ASP A CA    
298  C  C     . ASP A 60  ? 0.1750 0.2159 0.1422 -0.0547 -0.0009 -0.0175 40  ASP A C     
299  O  O     . ASP A 60  ? 0.1679 0.2384 0.1478 -0.0500 0.0026  -0.0124 40  ASP A O     
300  C  CB    . ASP A 60  ? 0.1828 0.2673 0.1756 -0.0656 -0.0070 -0.0102 40  ASP A CB    
301  C  CG    . ASP A 60  ? 0.1835 0.2880 0.1803 -0.0437 -0.0256 0.0009  40  ASP A CG    
302  O  OD1   . ASP A 60  ? 0.1585 0.2442 0.1506 -0.0509 -0.0023 -0.0319 40  ASP A OD1   
303  O  OD2   . ASP A 60  ? 0.1966 0.3367 0.2320 -0.0351 -0.0337 0.0251  40  ASP A OD2   
304  N  N     . THR A 61  ? 0.1706 0.1888 0.1348 -0.0517 0.0095  -0.0317 41  THR A N     
305  C  CA    . THR A 61  ? 0.1675 0.1604 0.1299 -0.0377 0.0058  -0.0275 41  THR A CA    
306  C  C     . THR A 61  ? 0.1684 0.1595 0.1364 -0.0347 0.0056  -0.0221 41  THR A C     
307  O  O     . THR A 61  ? 0.1582 0.1694 0.1364 -0.0286 -0.0009 -0.0179 41  THR A O     
308  C  CB    . THR A 61  ? 0.1545 0.1504 0.1278 -0.0226 0.0052  -0.0144 41  THR A CB    
309  O  OG1   . THR A 61  ? 0.1652 0.1429 0.1319 -0.0180 0.0134  -0.0157 41  THR A OG1   
310  C  CG2   . THR A 61  ? 0.1500 0.1560 0.1261 -0.0122 0.0026  -0.0226 41  THR A CG2   
311  N  N     . GLY A 62  ? 0.1824 0.1575 0.1404 -0.0374 0.0245  -0.0293 42  GLY A N     
312  C  CA    . GLY A 62  ? 0.2045 0.1612 0.1524 -0.0340 0.0213  -0.0232 42  GLY A CA    
313  C  C     . GLY A 62  ? 0.2115 0.1823 0.1635 -0.0524 0.0239  -0.0198 42  GLY A C     
314  O  O     . GLY A 62  ? 0.2108 0.1926 0.1560 -0.0507 0.0344  -0.0171 42  GLY A O     
315  N  N     . THR A 63  ? 0.1953 0.2086 0.1838 -0.0656 0.0175  -0.0225 43  THR A N     
316  C  CA    . THR A 63  ? 0.1961 0.2345 0.2026 -0.0776 0.0094  -0.0283 43  THR A CA    
317  C  C     . THR A 63  ? 0.1829 0.2324 0.1722 -0.0656 0.0127  -0.0193 43  THR A C     
318  O  O     . THR A 63  ? 0.1874 0.2496 0.1723 -0.0629 0.0200  -0.0190 43  THR A O     
319  C  CB    . THR A 63  ? 0.2266 0.2523 0.2496 -0.0990 0.0091  -0.0516 43  THR A CB    
320  O  OG1   . THR A 63  ? 0.2532 0.2681 0.2869 -0.1034 0.0156  -0.0596 43  THR A OG1   
321  C  CG2   . THR A 63  ? 0.2373 0.2722 0.2562 -0.0977 0.0089  -0.0532 43  THR A CG2   
322  N  N     . ASN A 64  ? 0.1675 0.2149 0.1555 -0.0601 -0.0026 -0.0216 44  ASN A N     
323  C  CA    . ASN A 64  ? 0.1515 0.2149 0.1426 -0.0363 0.0065  -0.0084 44  ASN A CA    
324  C  C     . ASN A 64  ? 0.1418 0.2079 0.1377 -0.0306 0.0070  -0.0062 44  ASN A C     
325  O  O     . ASN A 64  ? 0.1388 0.2181 0.1414 -0.0093 0.0056  -0.0065 44  ASN A O     
326  C  CB    . ASN A 64  ? 0.1476 0.2373 0.1388 -0.0266 -0.0063 -0.0009 44  ASN A CB    
327  C  CG    . ASN A 64  ? 0.1482 0.2641 0.1489 -0.0425 -0.0042 0.0013  44  ASN A CG    
328  O  OD1   . ASN A 64  ? 0.1588 0.3028 0.1564 -0.0557 -0.0160 0.0049  44  ASN A OD1   
329  N  ND2   . ASN A 64  ? 0.1506 0.2650 0.1429 -0.0210 -0.0075 -0.0029 44  ASN A ND2   
330  N  N     . MET A 65  ? 0.1413 0.1834 0.1286 -0.0342 0.0050  -0.0145 45  MET A N     
331  C  CA    . MET A 65  ? 0.1402 0.1571 0.1307 -0.0299 0.0060  -0.0119 45  MET A CA    
332  C  C     . MET A 65  ? 0.1484 0.1644 0.1381 -0.0369 0.0092  -0.0059 45  MET A C     
333  O  O     . MET A 65  ? 0.1557 0.1737 0.1360 -0.0315 0.0100  -0.0139 45  MET A O     
334  C  CB    . MET A 65  ? 0.1499 0.1482 0.1313 -0.0256 0.0035  -0.0099 45  MET A CB    
335  C  CG    . MET A 65  ? 0.1550 0.1365 0.1298 -0.0175 0.0052  -0.0022 45  MET A CG    
336  S  SD    . MET A 65  ? 0.1427 0.1374 0.1382 -0.0147 0.0050  -0.0031 45  MET A SD    
337  C  CE    . MET A 65  ? 0.1498 0.1544 0.1491 -0.0257 0.0022  -0.0061 45  MET A CE    
338  N  N     . ASN A 66  ? 0.1645 0.1670 0.1397 -0.0444 0.0140  -0.0070 46  ASN A N     
339  C  CA    . ASN A 66  ? 0.1889 0.1733 0.1550 -0.0551 0.0116  -0.0079 46  ASN A CA    
340  C  C     . ASN A 66  ? 0.1761 0.1839 0.1588 -0.0525 0.0150  -0.0096 46  ASN A C     
341  O  O     . ASN A 66  ? 0.1863 0.1953 0.1538 -0.0511 0.0226  -0.0039 46  ASN A O     
342  C  CB    . ASN A 66  ? 0.2112 0.1828 0.1721 -0.0655 0.0100  -0.0078 46  ASN A CB    
343  C  CG    . ASN A 66  ? 0.2573 0.2050 0.1917 -0.0783 0.0206  -0.0171 46  ASN A CG    
344  O  OD1   . ASN A 66  ? 0.2794 0.2190 0.1790 -0.0623 0.0290  -0.0181 46  ASN A OD1   
345  N  ND2   . ASN A 66  ? 0.3048 0.2284 0.2204 -0.1094 0.0130  -0.0110 46  ASN A ND2   
346  N  N     . LEU A 67  ? 0.1604 0.2127 0.1650 -0.0520 0.0138  -0.0128 47  LEU A N     
347  C  CA    . LEU A 67  ? 0.1541 0.2393 0.1750 -0.0505 0.0007  -0.0180 47  LEU A CA    
348  C  C     . LEU A 67  ? 0.1477 0.2247 0.1671 -0.0300 0.0032  -0.0067 47  LEU A C     
349  O  O     . LEU A 67  ? 0.1427 0.2325 0.1802 -0.0356 0.0170  -0.0118 47  LEU A O     
350  C  CB    . LEU A 67  ? 0.1788 0.2761 0.1957 -0.0382 -0.0051 -0.0433 47  LEU A CB    
351  C  CG    . LEU A 67  ? 0.2109 0.3054 0.2241 -0.0424 -0.0028 -0.0563 47  LEU A CG    
352  C  CD1   . LEU A 67  ? 0.2541 0.3212 0.2282 -0.0207 -0.0189 -0.0610 47  LEU A CD1   
353  C  CD2   . LEU A 67  ? 0.2410 0.3143 0.2444 -0.0598 0.0128  -0.0632 47  LEU A CD2   
354  N  N     . THR A 68  ? 0.1412 0.2148 0.1556 -0.0352 0.0038  0.0025  48  THR A N     
355  C  CA    . THR A 68  ? 0.1483 0.1996 0.1521 -0.0249 0.0066  -0.0013 48  THR A CA    
356  C  C     . THR A 68  ? 0.1458 0.1941 0.1488 -0.0239 0.0179  -0.0028 48  THR A C     
357  O  O     . THR A 68  ? 0.1491 0.2011 0.1487 -0.0158 0.0118  -0.0015 48  THR A O     
358  C  CB    . THR A 68  ? 0.1617 0.1975 0.1528 -0.0242 0.0023  0.0027  48  THR A CB    
359  O  OG1   . THR A 68  ? 0.1835 0.2082 0.1495 -0.0258 -0.0004 0.0084  48  THR A OG1   
360  C  CG2   . THR A 68  ? 0.1748 0.1866 0.1584 -0.0161 -0.0017 0.0103  48  THR A CG2   
361  N  N     . MET A 69  ? 0.1451 0.1896 0.1470 -0.0192 0.0082  -0.0063 49  MET A N     
362  C  CA    . MET A 69  ? 0.1677 0.1838 0.1519 -0.0055 0.0081  -0.0099 49  MET A CA    
363  C  C     . MET A 69  ? 0.1850 0.1903 0.1549 -0.0103 0.0141  -0.0090 49  MET A C     
364  O  O     . MET A 69  ? 0.1963 0.2103 0.1457 -0.0170 0.0163  -0.0144 49  MET A O     
365  C  CB    . MET A 69  ? 0.1865 0.1816 0.1584 -0.0002 0.0062  -0.0099 49  MET A CB    
366  C  CG    . MET A 69  ? 0.2017 0.1724 0.1718 0.0109  0.0039  0.0003  49  MET A CG    
367  S  SD    . MET A 69  ? 0.1862 0.1565 0.1858 0.0068  -0.0110 -0.0130 49  MET A SD    
368  C  CE    . MET A 69  ? 0.1897 0.1597 0.1852 0.0089  -0.0032 0.0194  49  MET A CE    
369  N  N     . THR A 70  ? 0.1897 0.1938 0.1651 -0.0287 0.0265  -0.0065 50  THR A N     
370  C  CA    . THR A 70  ? 0.2024 0.2003 0.1829 -0.0493 0.0385  -0.0156 50  THR A CA    
371  C  C     . THR A 70  ? 0.1813 0.2160 0.1775 -0.0553 0.0196  -0.0136 50  THR A C     
372  O  O     . THR A 70  ? 0.1846 0.2346 0.1710 -0.0555 0.0243  -0.0043 50  THR A O     
373  C  CB    . THR A 70  ? 0.2557 0.2242 0.2210 -0.0715 0.0653  -0.0253 50  THR A CB    
374  O  OG1   . THR A 70  ? 0.2993 0.2307 0.2339 -0.0632 0.0782  -0.0187 50  THR A OG1   
375  C  CG2   . THR A 70  ? 0.2651 0.2425 0.2333 -0.0754 0.0728  -0.0395 50  THR A CG2   
376  N  N     . SER A 71  ? 0.1588 0.2381 0.1741 -0.0464 0.0196  -0.0144 51  SER A N     
377  C  CA    . SER A 71  ? 0.1609 0.2525 0.1900 -0.0344 0.0191  -0.0222 51  SER A CA    
378  C  C     . SER A 71  ? 0.1486 0.2397 0.1836 -0.0323 0.0269  -0.0222 51  SER A C     
379  O  O     . SER A 71  ? 0.1463 0.2643 0.1928 -0.0243 0.0262  -0.0235 51  SER A O     
380  C  CB    . SER A 71  ? 0.1541 0.2694 0.2105 -0.0207 0.0035  -0.0412 51  SER A CB    
381  O  OG    . SER A 71  ? 0.1953 0.2909 0.2394 -0.0245 0.0050  -0.0400 51  SER A OG    
382  N  N     . GLY A 72  ? 0.1471 0.2144 0.1661 -0.0269 0.0122  -0.0135 52  GLY A N     
383  C  CA    . GLY A 72  ? 0.1586 0.1951 0.1671 -0.0288 0.0064  -0.0092 52  GLY A CA    
384  C  C     . GLY A 72  ? 0.1545 0.1886 0.1636 -0.0280 0.0225  -0.0027 52  GLY A C     
385  O  O     . GLY A 72  ? 0.1707 0.2014 0.1589 -0.0184 0.0198  -0.0176 52  GLY A O     
386  N  N     . ARG A 73  ? 0.1709 0.1874 0.1676 -0.0188 0.0183  0.0017  53  ARG A N     
387  C  CA    A ARG A 73  ? 0.1767 0.1832 0.1735 -0.0219 0.0193  -0.0004 53  ARG A CA    
388  C  CA    B ARG A 73  ? 0.1917 0.2007 0.1794 -0.0271 0.0129  0.0011  53  ARG A CA    
389  C  C     . ARG A 73  ? 0.1824 0.2005 0.1770 -0.0343 0.0155  -0.0061 53  ARG A C     
390  O  O     . ARG A 73  ? 0.2038 0.2051 0.1700 -0.0289 0.0310  0.0035  53  ARG A O     
391  C  CB    A ARG A 73  ? 0.1887 0.1788 0.1763 0.0018  0.0199  0.0009  53  ARG A CB    
392  C  CB    B ARG A 73  ? 0.2317 0.2303 0.1937 -0.0155 0.0014  0.0060  53  ARG A CB    
393  C  CG    A ARG A 73  ? 0.2081 0.1761 0.1857 0.0173  0.0215  0.0018  53  ARG A CG    
394  C  CG    B ARG A 73  ? 0.2806 0.2610 0.2116 -0.0074 -0.0055 0.0136  53  ARG A CG    
395  C  CD    A ARG A 73  ? 0.2220 0.1757 0.2033 -0.0013 0.0348  0.0030  53  ARG A CD    
396  C  CD    B ARG A 73  ? 0.3207 0.2854 0.2369 -0.0272 -0.0118 0.0244  53  ARG A CD    
397  N  NE    A ARG A 73  ? 0.2107 0.1750 0.2160 -0.0127 0.0430  0.0036  53  ARG A NE    
398  N  NE    B ARG A 73  ? 0.3495 0.3039 0.2508 -0.0449 -0.0155 0.0243  53  ARG A NE    
399  C  CZ    A ARG A 73  ? 0.2141 0.1970 0.2298 -0.0318 0.0433  0.0140  53  ARG A CZ    
400  C  CZ    B ARG A 73  ? 0.3643 0.3104 0.2569 -0.0542 -0.0134 0.0156  53  ARG A CZ    
401  N  NH1   A ARG A 73  ? 0.2134 0.2321 0.2404 0.0052  0.0658  0.0340  53  ARG A NH1   
402  N  NH1   B ARG A 73  ? 0.3781 0.3151 0.2624 -0.0575 -0.0089 0.0068  53  ARG A NH1   
403  N  NH2   A ARG A 73  ? 0.2371 0.1812 0.2326 -0.0636 0.0220  0.0078  53  ARG A NH2   
404  N  NH2   B ARG A 73  ? 0.3682 0.3143 0.2553 -0.0465 -0.0186 0.0121  53  ARG A NH2   
405  N  N     . GLU A 74  ? 0.1679 0.2248 0.1833 -0.0407 0.0235  -0.0088 54  GLU A N     
406  C  CA    . GLU A 74  ? 0.1773 0.2668 0.2053 -0.0651 0.0258  -0.0213 54  GLU A CA    
407  C  C     . GLU A 74  ? 0.1675 0.2673 0.2032 -0.0492 0.0269  -0.0167 54  GLU A C     
408  O  O     . GLU A 74  ? 0.1764 0.2789 0.2020 -0.0432 0.0410  -0.0060 54  GLU A O     
409  C  CB    . GLU A 74  ? 0.2064 0.3171 0.2263 -0.0792 0.0307  -0.0355 54  GLU A CB    
410  C  CG    . GLU A 74  ? 0.2847 0.3659 0.2621 -0.0750 0.0281  -0.0462 54  GLU A CG    
411  C  CD    . GLU A 74  ? 0.3465 0.4101 0.2894 -0.0664 0.0197  -0.0507 54  GLU A CD    
412  O  OE1   . GLU A 74  ? 0.3675 0.4404 0.2954 -0.0432 0.0050  -0.0459 54  GLU A OE1   
413  O  OE2   . GLU A 74  ? 0.3711 0.4262 0.3053 -0.0806 0.0265  -0.0553 54  GLU A OE2   
414  N  N     . GLU A 75  ? 0.1520 0.2607 0.1953 -0.0289 0.0205  -0.0157 55  GLU A N     
415  C  CA    . GLU A 75  ? 0.1528 0.2705 0.2099 -0.0163 0.0128  -0.0106 55  GLU A CA    
416  C  C     . GLU A 75  ? 0.1570 0.2494 0.1966 -0.0085 0.0163  -0.0139 55  GLU A C     
417  O  O     . GLU A 75  ? 0.1622 0.2586 0.1943 -0.0094 0.0397  -0.0263 55  GLU A O     
418  C  CB    . GLU A 75  ? 0.1865 0.3078 0.2357 -0.0026 -0.0087 -0.0025 55  GLU A CB    
419  C  CG    . GLU A 75  ? 0.2437 0.3670 0.2695 -0.0019 -0.0061 0.0002  55  GLU A CG    
420  C  CD    . GLU A 75  ? 0.2818 0.4234 0.3070 -0.0041 -0.0041 -0.0047 55  GLU A CD    
421  O  OE1   . GLU A 75  ? 0.3254 0.4458 0.3288 0.0081  0.0022  -0.0045 55  GLU A OE1   
422  O  OE2   . GLU A 75  ? 0.3005 0.4494 0.3298 -0.0127 -0.0115 -0.0053 55  GLU A OE2   
423  N  N     . VAL A 76  ? 0.1501 0.2256 0.1757 -0.0102 0.0169  -0.0023 56  VAL A N     
424  C  CA    . VAL A 76  ? 0.1622 0.2104 0.1709 -0.0198 0.0219  -0.0005 56  VAL A CA    
425  C  C     . VAL A 76  ? 0.1904 0.2229 0.1764 -0.0261 0.0290  0.0086  56  VAL A C     
426  O  O     . VAL A 76  ? 0.2099 0.2303 0.1697 -0.0219 0.0403  0.0154  56  VAL A O     
427  C  CB    . VAL A 76  ? 0.1608 0.1907 0.1679 -0.0197 0.0233  0.0008  56  VAL A CB    
428  C  CG1   . VAL A 76  ? 0.1953 0.1828 0.1637 -0.0158 0.0095  0.0164  56  VAL A CG1   
429  C  CG2   . VAL A 76  ? 0.1657 0.1898 0.1774 -0.0166 0.0267  0.0034  56  VAL A CG2   
430  N  N     . GLU A 77  ? 0.2114 0.2202 0.1829 -0.0480 0.0393  0.0112  57  GLU A N     
431  C  CA    . GLU A 77  ? 0.2270 0.2404 0.2079 -0.0533 0.0515  0.0032  57  GLU A CA    
432  C  C     . GLU A 77  ? 0.2420 0.2687 0.2127 -0.0757 0.0612  -0.0053 57  GLU A C     
433  O  O     . GLU A 77  ? 0.2894 0.2827 0.2148 -0.0815 0.0663  0.0067  57  GLU A O     
434  C  CB    . GLU A 77  ? 0.2328 0.2491 0.2409 -0.0511 0.0536  0.0002  57  GLU A CB    
435  C  CG    . GLU A 77  ? 0.2527 0.2675 0.2650 -0.0351 0.0611  -0.0024 57  GLU A CG    
436  C  CD    . GLU A 77  ? 0.3055 0.2910 0.2994 -0.0381 0.0541  -0.0083 57  GLU A CD    
437  O  OE1   . GLU A 77  ? 0.3321 0.3100 0.3066 -0.0411 0.0462  -0.0139 57  GLU A OE1   
438  O  OE2   . GLU A 77  ? 0.3253 0.2998 0.3111 -0.0403 0.0653  -0.0048 57  GLU A OE2   
439  N  N     . ASN A 78  ? 0.2087 0.3001 0.2172 -0.0739 0.0572  -0.0196 58  ASN A N     
440  C  CA    . ASN A 78  ? 0.2191 0.3395 0.2387 -0.0634 0.0580  -0.0287 58  ASN A CA    
441  C  C     . ASN A 78  ? 0.1959 0.3244 0.2346 -0.0399 0.0554  -0.0205 58  ASN A C     
442  O  O     . ASN A 78  ? 0.1929 0.3521 0.2469 -0.0384 0.0552  -0.0265 58  ASN A O     
443  C  CB    . ASN A 78  ? 0.2718 0.3817 0.2664 -0.0641 0.0528  -0.0395 58  ASN A CB    
444  C  CG    . ASN A 78  ? 0.3657 0.4202 0.2991 -0.0670 0.0518  -0.0345 58  ASN A CG    
445  O  OD1   . ASN A 78  ? 0.4172 0.4399 0.3189 -0.0615 0.0437  -0.0361 58  ASN A OD1   
446  N  ND2   . ASN A 78  ? 0.3877 0.4360 0.3121 -0.0735 0.0548  -0.0280 58  ASN A ND2   
447  N  N     . ASN A 79  ? 0.1895 0.2843 0.2220 -0.0317 0.0486  -0.0010 59  ASN A N     
448  C  CA    A ASN A 79  ? 0.1880 0.2704 0.2268 -0.0051 0.0488  0.0013  59  ASN A CA    
449  C  CA    B ASN A 79  ? 0.2106 0.2686 0.2261 -0.0145 0.0404  0.0054  59  ASN A CA    
450  C  C     . ASN A 79  ? 0.1863 0.2459 0.2128 -0.0083 0.0454  0.0073  59  ASN A C     
451  O  O     . ASN A 79  ? 0.2006 0.2460 0.2227 -0.0162 0.0317  0.0302  59  ASN A O     
452  C  CB    A ASN A 79  ? 0.1927 0.2888 0.2492 0.0242  0.0458  0.0007  59  ASN A CB    
453  C  CB    B ASN A 79  ? 0.2591 0.2832 0.2477 -0.0023 0.0237  0.0113  59  ASN A CB    
454  C  CG    A ASN A 79  ? 0.1943 0.3076 0.2733 0.0432  0.0381  -0.0038 59  ASN A CG    
455  C  CG    B ASN A 79  ? 0.2956 0.2946 0.2651 0.0102  0.0132  0.0084  59  ASN A CG    
456  O  OD1   A ASN A 79  ? 0.2049 0.3252 0.2828 0.0459  0.0431  -0.0039 59  ASN A OD1   
457  O  OD1   B ASN A 79  ? 0.3224 0.3051 0.2736 0.0227  0.0092  -0.0003 59  ASN A OD1   
458  N  ND2   A ASN A 79  ? 0.1888 0.3128 0.2868 0.0445  0.0260  -0.0021 59  ASN A ND2   
459  N  ND2   B ASN A 79  ? 0.3080 0.2990 0.2741 0.0086  0.0043  0.0098  59  ASN A ND2   
460  N  N     . LEU A 80  ? 0.1829 0.2141 0.1839 -0.0249 0.0333  0.0045  60  LEU A N     
461  C  CA    . LEU A 80  ? 0.1887 0.2031 0.1822 -0.0198 0.0356  -0.0014 60  LEU A CA    
462  C  C     . LEU A 80  ? 0.1946 0.2080 0.1871 -0.0037 0.0367  -0.0164 60  LEU A C     
463  O  O     . LEU A 80  ? 0.2128 0.2302 0.1981 -0.0029 0.0485  -0.0290 60  LEU A O     
464  C  CB    . LEU A 80  ? 0.1897 0.2014 0.1760 -0.0179 0.0353  0.0048  60  LEU A CB    
465  C  CG    . LEU A 80  ? 0.2024 0.1991 0.1884 -0.0168 0.0346  0.0047  60  LEU A CG    
466  C  CD1   . LEU A 80  ? 0.2298 0.2054 0.2054 -0.0209 0.0444  0.0009  60  LEU A CD1   
467  C  CD2   . LEU A 80  ? 0.2109 0.1999 0.1866 -0.0098 0.0272  0.0095  60  LEU A CD2   
468  N  N     . SER A 81  ? 0.1994 0.2071 0.1913 -0.0091 0.0253  -0.0104 61  SER A N     
469  C  CA    . SER A 81  ? 0.1998 0.1951 0.1846 -0.0159 0.0277  -0.0072 61  SER A CA    
470  C  C     . SER A 81  ? 0.2109 0.1848 0.1898 -0.0020 0.0234  -0.0125 61  SER A C     
471  O  O     . SER A 81  ? 0.2129 0.2026 0.2057 -0.0061 0.0256  -0.0151 61  SER A O     
472  C  CB    . SER A 81  ? 0.2112 0.1933 0.2018 -0.0168 0.0158  -0.0051 61  SER A CB    
473  O  OG    . SER A 81  ? 0.2177 0.1931 0.2111 -0.0024 0.0160  -0.0011 61  SER A OG    
474  N  N     . LYS A 82  ? 0.2337 0.1751 0.1792 -0.0105 0.0240  -0.0049 62  LYS A N     
475  C  CA    . LYS A 82  ? 0.2525 0.1800 0.1738 -0.0098 0.0160  -0.0006 62  LYS A CA    
476  C  C     . LYS A 82  ? 0.2080 0.1694 0.1525 0.0003  0.0130  0.0023  62  LYS A C     
477  O  O     . LYS A 82  ? 0.2252 0.1906 0.1622 0.0208  0.0147  -0.0088 62  LYS A O     
478  C  CB    . LYS A 82  ? 0.3077 0.1871 0.1712 -0.0328 0.0237  -0.0024 62  LYS A CB    
479  C  CG    . LYS A 82  ? 0.3731 0.2028 0.1664 -0.0483 0.0476  -0.0090 62  LYS A CG    
480  C  CD    . LYS A 82  ? 0.4281 0.2280 0.1752 -0.0382 0.0605  -0.0145 62  LYS A CD    
481  C  CE    . LYS A 82  ? 0.4688 0.2550 0.1870 -0.0228 0.0539  -0.0121 62  LYS A CE    
482  N  NZ    . LYS A 82  ? 0.4853 0.2737 0.1993 -0.0116 0.0600  -0.0061 62  LYS A NZ    
483  N  N     . ASN A 83  ? 0.2197 0.1728 0.1406 -0.0079 0.0104  0.0118  63  ASN A N     
484  C  CA    . ASN A 83  ? 0.2273 0.1681 0.1435 0.0037  0.0165  0.0063  63  ASN A CA    
485  C  C     . ASN A 83  ? 0.2045 0.1631 0.1330 0.0021  0.0101  0.0058  63  ASN A C     
486  O  O     . ASN A 83  ? 0.1941 0.1707 0.1434 -0.0028 0.0140  -0.0005 63  ASN A O     
487  C  CB    . ASN A 83  ? 0.2470 0.1705 0.1530 -0.0033 0.0293  -0.0059 63  ASN A CB    
488  C  CG    . ASN A 83  ? 0.2777 0.1864 0.1677 -0.0061 0.0199  -0.0056 63  ASN A CG    
489  O  OD1   . ASN A 83  ? 0.2822 0.1959 0.1684 -0.0252 0.0263  -0.0011 63  ASN A OD1   
490  N  ND2   . ASN A 83  ? 0.2991 0.1961 0.1748 0.0025  0.0193  -0.0052 63  ASN A ND2   
491  N  N     . ILE A 84  ? 0.2016 0.1604 0.1335 0.0023  0.0048  0.0067  64  ILE A N     
492  C  CA    . ILE A 84  ? 0.2029 0.1401 0.1366 -0.0049 0.0155  0.0114  64  ILE A CA    
493  C  C     . ILE A 84  ? 0.1994 0.1347 0.1424 0.0101  0.0186  0.0031  64  ILE A C     
494  O  O     . ILE A 84  ? 0.1917 0.1535 0.1354 0.0117  0.0194  0.0009  64  ILE A O     
495  C  CB    . ILE A 84  ? 0.2105 0.1352 0.1344 -0.0047 0.0050  0.0109  64  ILE A CB    
496  C  CG1   . ILE A 84  ? 0.2181 0.1346 0.1387 -0.0058 0.0082  0.0074  64  ILE A CG1   
497  C  CG2   . ILE A 84  ? 0.2171 0.1419 0.1337 -0.0056 0.0101  0.0096  64  ILE A CG2   
498  C  CD1   . ILE A 84  ? 0.2232 0.1352 0.1410 0.0088  0.0018  0.0038  64  ILE A CD1   
499  N  N     . GLY A 85  ? 0.1964 0.1397 0.1417 0.0057  0.0068  0.0067  65  GLY A N     
500  C  CA    . GLY A 85  ? 0.1935 0.1478 0.1513 0.0084  0.0211  0.0073  65  GLY A CA    
501  C  C     . GLY A 85  ? 0.1917 0.1541 0.1485 0.0165  0.0249  0.0066  65  GLY A C     
502  O  O     . GLY A 85  ? 0.1947 0.1575 0.1475 0.0221  0.0203  0.0096  65  GLY A O     
503  N  N     . GLU A 86  ? 0.1987 0.1702 0.1473 0.0110  0.0255  0.0019  66  GLU A N     
504  C  CA    . GLU A 86  ? 0.1882 0.1825 0.1659 0.0283  0.0373  -0.0034 66  GLU A CA    
505  C  C     . GLU A 86  ? 0.1785 0.1708 0.1579 0.0215  0.0269  0.0035  66  GLU A C     
506  O  O     . GLU A 86  ? 0.1752 0.1775 0.1683 0.0191  0.0195  0.0059  66  GLU A O     
507  C  CB    . GLU A 86  ? 0.2567 0.2397 0.1954 0.0352  0.0420  -0.0177 66  GLU A CB    
508  C  CG    . GLU A 86  ? 0.3483 0.3096 0.2403 0.0419  0.0292  -0.0221 66  GLU A CG    
509  C  CD    . GLU A 86  ? 0.4235 0.3608 0.2785 0.0507  0.0222  -0.0233 66  GLU A CD    
510  O  OE1   . GLU A 86  ? 0.4179 0.3854 0.2949 0.0592  0.0165  -0.0192 66  GLU A OE1   
511  O  OE2   . GLU A 86  ? 0.4674 0.3817 0.2949 0.0511  0.0230  -0.0191 66  GLU A OE2   
512  N  N     . LEU A 87  ? 0.1717 0.1608 0.1481 0.0187  0.0200  0.0018  67  LEU A N     
513  C  CA    . LEU A 87  ? 0.1775 0.1520 0.1491 0.0165  0.0168  0.0091  67  LEU A CA    
514  C  C     . LEU A 87  ? 0.1708 0.1527 0.1434 0.0137  0.0133  0.0015  67  LEU A C     
515  O  O     . LEU A 87  ? 0.1807 0.1501 0.1478 -0.0019 0.0121  0.0130  67  LEU A O     
516  C  CB    . LEU A 87  ? 0.1858 0.1511 0.1590 0.0020  0.0131  0.0133  67  LEU A CB    
517  C  CG    . LEU A 87  ? 0.1857 0.1561 0.1683 0.0043  0.0190  0.0002  67  LEU A CG    
518  C  CD1   . LEU A 87  ? 0.1750 0.1530 0.1723 0.0143  0.0219  0.0045  67  LEU A CD1   
519  C  CD2   . LEU A 87  ? 0.2089 0.1691 0.1830 0.0070  0.0216  -0.0025 67  LEU A CD2   
520  N  N     . GLY A 88  ? 0.1704 0.1540 0.1368 0.0051  0.0160  0.0044  68  GLY A N     
521  C  CA    . GLY A 88  ? 0.1703 0.1534 0.1427 0.0036  0.0121  0.0033  68  GLY A CA    
522  C  C     . GLY A 88  ? 0.1699 0.1550 0.1472 0.0004  0.0125  0.0045  68  GLY A C     
523  O  O     . GLY A 88  ? 0.1786 0.1611 0.1375 0.0059  0.0155  0.0086  68  GLY A O     
524  N  N     . LYS A 89  ? 0.1832 0.1578 0.1541 0.0125  0.0067  0.0096  69  LYS A N     
525  C  CA    . LYS A 89  ? 0.1834 0.1693 0.1689 0.0073  0.0067  0.0090  69  LYS A CA    
526  C  C     . LYS A 89  ? 0.1671 0.1695 0.1632 0.0177  0.0093  0.0171  69  LYS A C     
527  O  O     . LYS A 89  ? 0.1796 0.1836 0.1648 0.0202  0.0044  0.0241  69  LYS A O     
528  C  CB    . LYS A 89  ? 0.2010 0.1791 0.1879 0.0264  0.0220  -0.0047 69  LYS A CB    
529  C  CG    . LYS A 89  ? 0.2408 0.1964 0.2150 0.0279  0.0302  -0.0204 69  LYS A CG    
530  C  CD    . LYS A 89  ? 0.3029 0.2233 0.2406 0.0287  0.0406  -0.0312 69  LYS A CD    
531  C  CE    . LYS A 89  ? 0.3517 0.2485 0.2594 0.0391  0.0542  -0.0381 69  LYS A CE    
532  N  NZ    . LYS A 89  ? 0.3875 0.2746 0.2732 0.0415  0.0543  -0.0391 69  LYS A NZ    
533  N  N     . THR A 90  ? 0.1652 0.1635 0.1617 0.0115  0.0134  0.0119  70  THR A N     
534  C  CA    . THR A 90  ? 0.1676 0.1719 0.1599 0.0000  0.0189  0.0079  70  THR A CA    
535  C  C     . THR A 90  ? 0.1607 0.1667 0.1481 -0.0024 0.0155  0.0084  70  THR A C     
536  O  O     . THR A 90  ? 0.1536 0.1802 0.1501 0.0053  0.0093  0.0084  70  THR A O     
537  C  CB    . THR A 90  ? 0.1678 0.1858 0.1758 0.0020  0.0333  0.0045  70  THR A CB    
538  O  OG1   . THR A 90  ? 0.1945 0.2002 0.1804 0.0067  0.0429  0.0014  70  THR A OG1   
539  C  CG2   . THR A 90  ? 0.1908 0.1958 0.1860 -0.0079 0.0265  -0.0019 70  THR A CG2   
540  N  N     . PHE A 91  ? 0.1582 0.1593 0.1378 -0.0001 0.0142  0.0090  71  PHE A N     
541  C  CA    . PHE A 91  ? 0.1700 0.1534 0.1373 0.0036  0.0132  0.0077  71  PHE A CA    
542  C  C     . PHE A 91  ? 0.1634 0.1502 0.1389 0.0072  0.0065  0.0099  71  PHE A C     
543  O  O     . PHE A 91  ? 0.1731 0.1630 0.1405 0.0052  0.0047  0.0089  71  PHE A O     
544  C  CB    . PHE A 91  ? 0.1631 0.1480 0.1412 0.0061  0.0119  0.0102  71  PHE A CB    
545  C  CG    . PHE A 91  ? 0.1668 0.1376 0.1422 0.0092  0.0058  0.0114  71  PHE A CG    
546  C  CD1   . PHE A 91  ? 0.1724 0.1537 0.1443 0.0105  0.0093  0.0097  71  PHE A CD1   
547  C  CD2   . PHE A 91  ? 0.1772 0.1371 0.1439 -0.0022 -0.0004 0.0204  71  PHE A CD2   
548  C  CE1   . PHE A 91  ? 0.1890 0.1559 0.1391 0.0139  0.0132  0.0192  71  PHE A CE1   
549  C  CE2   . PHE A 91  ? 0.1829 0.1489 0.1493 0.0050  0.0182  0.0309  71  PHE A CE2   
550  C  CZ    . PHE A 91  ? 0.1948 0.1540 0.1420 0.0204  0.0238  0.0269  71  PHE A CZ    
551  N  N     . SER A 92  ? 0.1812 0.1476 0.1441 -0.0096 0.0095  0.0132  72  SER A N     
552  C  CA    . SER A 92  ? 0.1925 0.1592 0.1611 -0.0184 0.0077  0.0229  72  SER A CA    
553  C  C     . SER A 92  ? 0.1848 0.1642 0.1579 -0.0126 0.0015  0.0151  72  SER A C     
554  O  O     . SER A 92  ? 0.2143 0.1636 0.1503 -0.0191 -0.0044 0.0221  72  SER A O     
555  C  CB    . SER A 92  ? 0.2495 0.1721 0.1784 -0.0354 0.0002  0.0398  72  SER A CB    
556  O  OG    . SER A 92  ? 0.2788 0.1869 0.1823 -0.0331 -0.0087 0.0313  72  SER A OG    
557  N  N     . LYS A 93  ? 0.1778 0.1762 0.1704 0.0157  0.0048  0.0082  73  LYS A N     
558  C  CA    . LYS A 93  ? 0.1839 0.2003 0.1884 0.0218  -0.0023 0.0140  73  LYS A CA    
559  C  C     . LYS A 93  ? 0.1686 0.1923 0.1761 0.0007  0.0125  0.0214  73  LYS A C     
560  O  O     . LYS A 93  ? 0.1739 0.2100 0.1731 -0.0049 -0.0054 0.0249  73  LYS A O     
561  C  CB    . LYS A 93  ? 0.2081 0.2467 0.2206 0.0449  -0.0106 -0.0068 73  LYS A CB    
562  C  CG    . LYS A 93  ? 0.2338 0.2853 0.2379 0.0421  -0.0061 -0.0098 73  LYS A CG    
563  N  N     . GLY A 94  ? 0.1534 0.1802 0.1783 0.0048  0.0132  0.0232  74  GLY A N     
564  C  CA    . GLY A 94  ? 0.1646 0.1801 0.1841 0.0026  0.0125  0.0183  74  GLY A CA    
565  C  C     . GLY A 94  ? 0.1617 0.1767 0.1693 -0.0044 0.0040  0.0112  74  GLY A C     
566  O  O     . GLY A 94  ? 0.1640 0.2033 0.1748 -0.0250 0.0038  -0.0038 74  GLY A O     
567  N  N     . LEU A 95  ? 0.1464 0.1565 0.1550 -0.0045 0.0075  0.0075  75  LEU A N     
568  C  CA    . LEU A 95  ? 0.1561 0.1499 0.1553 -0.0124 0.0072  0.0131  75  LEU A CA    
569  C  C     . LEU A 95  ? 0.1546 0.1482 0.1556 -0.0103 0.0011  0.0120  75  LEU A C     
570  O  O     . LEU A 95  ? 0.1586 0.1590 0.1622 -0.0028 -0.0100 0.0097  75  LEU A O     
571  C  CB    . LEU A 95  ? 0.1517 0.1533 0.1581 -0.0116 0.0031  0.0133  75  LEU A CB    
572  C  CG    . LEU A 95  ? 0.1496 0.1534 0.1576 -0.0133 0.0096  0.0157  75  LEU A CG    
573  C  CD1   . LEU A 95  ? 0.1715 0.1775 0.1768 -0.0224 -0.0051 0.0327  75  LEU A CD1   
574  C  CD2   . LEU A 95  ? 0.1621 0.1751 0.1554 0.0119  0.0034  -0.0019 75  LEU A CD2   
575  N  N     . LEU A 96  ? 0.1615 0.1355 0.1543 0.0022  -0.0003 0.0184  76  LEU A N     
576  C  CA    . LEU A 96  ? 0.1432 0.1581 0.1665 -0.0058 0.0022  0.0146  76  LEU A CA    
577  C  C     . LEU A 96  ? 0.1458 0.2023 0.1859 -0.0184 -0.0061 0.0088  76  LEU A C     
578  O  O     . LEU A 96  ? 0.1708 0.2559 0.1824 -0.0269 -0.0203 0.0234  76  LEU A O     
579  C  CB    . LEU A 96  ? 0.1553 0.1518 0.1667 -0.0057 0.0091  0.0179  76  LEU A CB    
580  C  CG    . LEU A 96  ? 0.1676 0.1445 0.1606 0.0013  0.0039  0.0130  76  LEU A CG    
581  C  CD1   . LEU A 96  ? 0.1828 0.1510 0.1627 0.0001  0.0051  0.0027  76  LEU A CD1   
582  C  CD2   . LEU A 96  ? 0.1837 0.1525 0.1632 -0.0036 0.0145  0.0117  76  LEU A CD2   
583  N  N     . MET A 97  ? 0.1325 0.2069 0.2265 -0.0007 0.0033  -0.0027 77  MET A N     
584  C  CA    A MET A 97  ? 0.1443 0.2472 0.2642 -0.0055 0.0038  -0.0060 77  MET A CA    
585  C  CA    B MET A 97  ? 0.1352 0.2401 0.2625 0.0037  0.0103  -0.0151 77  MET A CA    
586  C  C     . MET A 97  ? 0.1409 0.2392 0.2750 -0.0017 -0.0054 -0.0234 77  MET A C     
587  O  O     . MET A 97  ? 0.1868 0.2475 0.3003 -0.0059 -0.0071 -0.0209 77  MET A O     
588  C  CB    A MET A 97  ? 0.1922 0.3022 0.2931 -0.0133 0.0118  0.0004  77  MET A CB    
589  C  CB    B MET A 97  ? 0.1786 0.2852 0.2919 0.0106  0.0220  -0.0269 77  MET A CB    
590  C  CG    A MET A 97  ? 0.2234 0.3478 0.3075 -0.0140 0.0228  0.0123  77  MET A CG    
591  C  CG    B MET A 97  ? 0.2418 0.3305 0.3157 0.0136  0.0292  -0.0336 77  MET A CG    
592  S  SD    A MET A 97  ? 0.2548 0.3837 0.3163 -0.0193 0.0547  0.0187  77  MET A SD    
593  S  SD    B MET A 97  ? 0.3088 0.3671 0.3394 0.0063  0.0388  -0.0330 77  MET A SD    
594  C  CE    A MET A 97  ? 0.2056 0.3740 0.2965 -0.0158 0.1016  0.0108  77  MET A CE    
595  C  CE    B MET A 97  ? 0.3000 0.3690 0.3342 0.0022  0.0400  -0.0281 77  MET A CE    
596  N  N     . GLY A 98  ? 0.1734 0.2299 0.2742 -0.0131 0.0018  -0.0404 78  GLY A N     
597  C  CA    . GLY A 98  ? 0.1850 0.2309 0.2595 -0.0019 0.0002  -0.0405 78  GLY A CA    
598  C  C     . GLY A 98  ? 0.1803 0.2337 0.2334 0.0131  -0.0091 -0.0328 78  GLY A C     
599  O  O     . GLY A 98  ? 0.2195 0.2297 0.2322 0.0278  -0.0137 -0.0290 78  GLY A O     
600  N  N     . ALA A 99  ? 0.1739 0.2660 0.2367 0.0096  -0.0018 -0.0371 79  ALA A N     
601  C  CA    . ALA A 99  ? 0.1715 0.2935 0.2179 0.0150  -0.0096 -0.0190 79  ALA A CA    
602  C  C     . ALA A 99  ? 0.1850 0.3208 0.2111 0.0326  -0.0277 -0.0103 79  ALA A C     
603  O  O     . ALA A 99  ? 0.2221 0.3633 0.2410 0.0591  -0.0417 -0.0175 79  ALA A O     
604  C  CB    . ALA A 99  ? 0.1703 0.2935 0.2149 0.0033  -0.0074 -0.0044 79  ALA A CB    
605  N  N     . ARG A 100 ? 0.1589 0.3147 0.1782 0.0132  -0.0135 -0.0069 80  ARG A N     
606  C  CA    . ARG A 100 ? 0.1791 0.3094 0.1805 -0.0076 -0.0126 -0.0104 80  ARG A CA    
607  C  C     . ARG A 100 ? 0.1696 0.2806 0.1696 -0.0058 -0.0090 -0.0258 80  ARG A C     
608  O  O     . ARG A 100 ? 0.1795 0.2459 0.1704 -0.0082 -0.0088 -0.0278 80  ARG A O     
609  C  CB    . ARG A 100 ? 0.2134 0.3216 0.1965 -0.0247 -0.0176 -0.0080 80  ARG A CB    
610  C  CG    . ARG A 100 ? 0.2461 0.3339 0.2111 -0.0194 -0.0186 -0.0045 80  ARG A CG    
611  N  N     . GLY A 101 ? 0.1771 0.2844 0.1699 -0.0040 -0.0105 -0.0139 81  GLY A N     
612  C  CA    . GLY A 101 ? 0.1858 0.2566 0.1593 0.0002  -0.0084 -0.0088 81  GLY A CA    
613  C  C     . GLY A 101 ? 0.1760 0.2171 0.1506 0.0177  -0.0080 -0.0014 81  GLY A C     
614  O  O     . GLY A 101 ? 0.1948 0.2146 0.1456 0.0295  -0.0018 -0.0184 81  GLY A O     
615  N  N     . ASN A 102 ? 0.1767 0.1943 0.1434 0.0129  -0.0021 0.0018  82  ASN A N     
616  C  CA    . ASN A 102 ? 0.1830 0.1779 0.1438 0.0089  0.0069  0.0098  82  ASN A CA    
617  C  C     . ASN A 102 ? 0.1711 0.1559 0.1277 0.0154  0.0080  -0.0011 82  ASN A C     
618  O  O     . ASN A 102 ? 0.1734 0.1478 0.1356 0.0122  0.0010  0.0014  82  ASN A O     
619  C  CB    . ASN A 102 ? 0.1998 0.1950 0.1576 -0.0046 -0.0021 0.0201  82  ASN A CB    
620  C  CG    . ASN A 102 ? 0.2241 0.2478 0.1885 -0.0015 0.0034  0.0267  82  ASN A CG    
621  O  OD1   . ASN A 102 ? 0.2370 0.2638 0.2067 0.0329  -0.0057 0.0282  82  ASN A OD1   
622  N  ND2   . ASN A 102 ? 0.2834 0.3006 0.2211 -0.0085 -0.0282 0.0504  82  ASN A ND2   
623  N  N     . SER A 103 ? 0.1567 0.1433 0.1302 0.0000  0.0005  -0.0108 83  SER A N     
624  C  CA    . SER A 103 ? 0.1478 0.1376 0.1282 0.0049  0.0097  -0.0057 83  SER A CA    
625  C  C     . SER A 103 ? 0.1557 0.1349 0.1339 0.0051  0.0049  -0.0137 83  SER A C     
626  O  O     . SER A 103 ? 0.1504 0.1347 0.1343 0.0066  0.0016  -0.0136 83  SER A O     
627  C  CB    . SER A 103 ? 0.1473 0.1450 0.1354 0.0064  0.0029  -0.0109 83  SER A CB    
628  O  OG    . SER A 103 ? 0.1479 0.1438 0.1373 -0.0001 -0.0022 -0.0164 83  SER A OG    
629  N  N     . GLY A 104 ? 0.1485 0.1413 0.1376 -0.0009 0.0011  -0.0109 84  GLY A N     
630  C  CA    . GLY A 104 ? 0.1426 0.1450 0.1477 -0.0073 0.0143  -0.0128 84  GLY A CA    
631  C  C     . GLY A 104 ? 0.1283 0.1480 0.1428 -0.0042 0.0057  -0.0062 84  GLY A C     
632  O  O     . GLY A 104 ? 0.1390 0.1492 0.1329 -0.0060 0.0082  -0.0135 84  GLY A O     
633  N  N     . VAL A 105 ? 0.1375 0.1411 0.1422 0.0142  0.0036  -0.0060 85  VAL A N     
634  C  CA    . VAL A 105 ? 0.1300 0.1398 0.1544 0.0231  0.0005  0.0064  85  VAL A CA    
635  C  C     . VAL A 105 ? 0.1184 0.1314 0.1451 0.0065  0.0010  0.0125  85  VAL A C     
636  O  O     . VAL A 105 ? 0.1402 0.1332 0.1306 0.0086  -0.0033 -0.0064 85  VAL A O     
637  C  CB    . VAL A 105 ? 0.1510 0.1622 0.1581 0.0306  -0.0079 0.0015  85  VAL A CB    
638  C  CG1   . VAL A 105 ? 0.1790 0.1694 0.1572 0.0302  -0.0152 0.0160  85  VAL A CG1   
639  C  CG2   . VAL A 105 ? 0.1658 0.1791 0.1710 0.0372  -0.0161 -0.0092 85  VAL A CG2   
640  N  N     . ILE A 106 ? 0.1240 0.1273 0.1451 -0.0031 0.0056  0.0082  86  ILE A N     
641  C  CA    . ILE A 106 ? 0.1183 0.1210 0.1502 0.0068  0.0081  0.0058  86  ILE A CA    
642  C  C     . ILE A 106 ? 0.1197 0.1226 0.1392 0.0155  0.0112  0.0043  86  ILE A C     
643  O  O     . ILE A 106 ? 0.1294 0.1203 0.1385 0.0011  0.0039  -0.0015 86  ILE A O     
644  C  CB    . ILE A 106 ? 0.1325 0.1331 0.1542 0.0025  0.0147  0.0042  86  ILE A CB    
645  C  CG1   . ILE A 106 ? 0.1523 0.1507 0.1540 0.0003  0.0135  0.0090  86  ILE A CG1   
646  C  CG2   . ILE A 106 ? 0.1339 0.1455 0.1675 -0.0082 0.0114  -0.0081 86  ILE A CG2   
647  C  CD1   . ILE A 106 ? 0.1758 0.1730 0.1678 0.0051  0.0213  0.0108  86  ILE A CD1   
648  N  N     . LEU A 107 ? 0.1434 0.1155 0.1302 -0.0015 0.0057  0.0005  87  LEU A N     
649  C  CA    . LEU A 107 ? 0.1413 0.1008 0.1353 -0.0003 0.0053  -0.0008 87  LEU A CA    
650  C  C     . LEU A 107 ? 0.1331 0.1051 0.1323 -0.0041 0.0041  0.0028  87  LEU A C     
651  O  O     . LEU A 107 ? 0.1451 0.1113 0.1338 -0.0019 -0.0021 0.0067  87  LEU A O     
652  C  CB    . LEU A 107 ? 0.1522 0.1124 0.1462 0.0074  0.0026  0.0008  87  LEU A CB    
653  C  CG    . LEU A 107 ? 0.1851 0.1207 0.1556 0.0028  -0.0094 0.0062  87  LEU A CG    
654  C  CD1   . LEU A 107 ? 0.2067 0.1313 0.1642 0.0060  -0.0230 0.0029  87  LEU A CD1   
655  C  CD2   . LEU A 107 ? 0.1959 0.1319 0.1694 -0.0128 -0.0032 0.0083  87  LEU A CD2   
656  N  N     . SER A 108 ? 0.1282 0.1108 0.1346 0.0067  0.0018  -0.0004 88  SER A N     
657  C  CA    . SER A 108 ? 0.1337 0.1253 0.1383 0.0000  0.0057  0.0044  88  SER A CA    
658  C  C     . SER A 108 ? 0.1457 0.1263 0.1330 -0.0002 0.0021  0.0073  88  SER A C     
659  O  O     . SER A 108 ? 0.1437 0.1360 0.1271 -0.0059 0.0033  -0.0018 88  SER A O     
660  C  CB    . SER A 108 ? 0.1334 0.1337 0.1449 0.0017  0.0014  0.0060  88  SER A CB    
661  O  OG    . SER A 108 ? 0.1402 0.1382 0.1450 0.0125  0.0045  0.0075  88  SER A OG    
662  N  N     . GLN A 109 ? 0.1374 0.1133 0.1306 -0.0019 0.0044  0.0085  89  GLN A N     
663  C  CA    . GLN A 109 ? 0.1403 0.1109 0.1405 0.0049  0.0072  0.0106  89  GLN A CA    
664  C  C     . GLN A 109 ? 0.1443 0.1073 0.1367 0.0050  0.0100  0.0054  89  GLN A C     
665  O  O     . GLN A 109 ? 0.1480 0.1165 0.1415 0.0102  0.0022  0.0070  89  GLN A O     
666  C  CB    . GLN A 109 ? 0.1268 0.1086 0.1466 0.0141  -0.0010 0.0137  89  GLN A CB    
667  C  CG    . GLN A 109 ? 0.1443 0.1227 0.1509 0.0127  0.0031  0.0124  89  GLN A CG    
668  C  CD    . GLN A 109 ? 0.1443 0.1200 0.1475 0.0141  0.0046  0.0128  89  GLN A CD    
669  O  OE1   . GLN A 109 ? 0.1580 0.1307 0.1527 0.0120  -0.0043 -0.0045 89  GLN A OE1   
670  N  NE2   . GLN A 109 ? 0.1499 0.1312 0.1497 0.0187  -0.0016 0.0081  89  GLN A NE2   
671  N  N     . LEU A 110 ? 0.1349 0.1142 0.1338 0.0045  -0.0002 0.0008  90  LEU A N     
672  C  CA    . LEU A 110 ? 0.1377 0.1121 0.1387 0.0007  -0.0129 0.0070  90  LEU A CA    
673  C  C     . LEU A 110 ? 0.1382 0.1168 0.1368 -0.0036 -0.0089 0.0086  90  LEU A C     
674  O  O     . LEU A 110 ? 0.1534 0.1374 0.1324 -0.0168 0.0001  0.0011  90  LEU A O     
675  C  CB    . LEU A 110 ? 0.1302 0.1113 0.1486 -0.0051 -0.0135 0.0085  90  LEU A CB    
676  C  CG    . LEU A 110 ? 0.1270 0.1194 0.1517 0.0032  -0.0028 0.0025  90  LEU A CG    
677  C  CD1   . LEU A 110 ? 0.1283 0.1326 0.1661 0.0054  0.0083  0.0004  90  LEU A CD1   
678  C  CD2   . LEU A 110 ? 0.1347 0.1221 0.1517 -0.0016 0.0011  -0.0009 90  LEU A CD2   
679  N  N     . PHE A 111 ? 0.1397 0.1141 0.1328 -0.0076 -0.0061 0.0082  91  PHE A N     
680  C  CA    . PHE A 111 ? 0.1392 0.1157 0.1377 -0.0048 0.0002  0.0100  91  PHE A CA    
681  C  C     . PHE A 111 ? 0.1447 0.1122 0.1429 0.0037  0.0077  0.0015  91  PHE A C     
682  O  O     . PHE A 111 ? 0.1623 0.1247 0.1394 0.0050  0.0043  0.0007  91  PHE A O     
683  C  CB    . PHE A 111 ? 0.1570 0.1253 0.1446 -0.0079 0.0045  0.0083  91  PHE A CB    
684  C  CG    . PHE A 111 ? 0.1883 0.1267 0.1471 0.0013  0.0193  0.0166  91  PHE A CG    
685  C  CD1   . PHE A 111 ? 0.1989 0.1245 0.1494 0.0082  0.0013  0.0184  91  PHE A CD1   
686  C  CD2   . PHE A 111 ? 0.2310 0.1475 0.1527 0.0424  0.0049  0.0172  91  PHE A CD2   
687  C  CE1   . PHE A 111 ? 0.2091 0.1489 0.1672 0.0045  0.0026  0.0301  91  PHE A CE1   
688  C  CE2   . PHE A 111 ? 0.2578 0.1751 0.1694 0.0492  0.0176  0.0149  91  PHE A CE2   
689  C  CZ    . PHE A 111 ? 0.2460 0.1670 0.1773 0.0267  0.0177  0.0288  91  PHE A CZ    
690  N  N     . ARG A 112 ? 0.1479 0.1208 0.1455 0.0156  0.0034  0.0041  92  ARG A N     
691  C  CA    . ARG A 112 ? 0.1595 0.1304 0.1499 0.0236  0.0057  0.0080  92  ARG A CA    
692  C  C     . ARG A 112 ? 0.1598 0.1208 0.1433 0.0180  0.0002  0.0139  92  ARG A C     
693  O  O     . ARG A 112 ? 0.1706 0.1315 0.1398 0.0081  0.0060  -0.0011 92  ARG A O     
694  C  CB    . ARG A 112 ? 0.1504 0.1408 0.1464 0.0254  0.0087  0.0115  92  ARG A CB    
695  C  CG    . ARG A 112 ? 0.1551 0.1475 0.1534 0.0316  0.0144  0.0132  92  ARG A CG    
696  C  CD    . ARG A 112 ? 0.1621 0.1380 0.1714 0.0173  0.0189  0.0124  92  ARG A CD    
697  N  NE    . ARG A 112 ? 0.1578 0.1247 0.1645 0.0314  0.0006  0.0043  92  ARG A NE    
698  C  CZ    . ARG A 112 ? 0.1606 0.1264 0.1684 0.0289  0.0000  0.0015  92  ARG A CZ    
699  N  NH1   . ARG A 112 ? 0.1831 0.1318 0.1785 0.0114  0.0118  -0.0027 92  ARG A NH1   
700  N  NH2   . ARG A 112 ? 0.1742 0.1330 0.1695 0.0228  0.0010  0.0063  92  ARG A NH2   
701  N  N     . GLY A 113 ? 0.1661 0.1339 0.1412 0.0098  0.0039  0.0157  93  GLY A N     
702  C  CA    . GLY A 113 ? 0.1561 0.1295 0.1471 -0.0008 0.0027  0.0069  93  GLY A CA    
703  C  C     . GLY A 113 ? 0.1591 0.1197 0.1476 -0.0017 0.0049  -0.0045 93  GLY A C     
704  O  O     . GLY A 113 ? 0.1805 0.1219 0.1619 0.0037  0.0033  -0.0061 93  GLY A O     
705  N  N     . PHE A 114 ? 0.1566 0.1224 0.1380 0.0074  0.0006  0.0030  94  PHE A N     
706  C  CA    . PHE A 114 ? 0.1484 0.1230 0.1428 -0.0061 -0.0038 0.0084  94  PHE A CA    
707  C  C     . PHE A 114 ? 0.1557 0.1186 0.1372 0.0061  -0.0056 0.0046  94  PHE A C     
708  O  O     . PHE A 114 ? 0.1789 0.1377 0.1377 -0.0042 -0.0080 0.0043  94  PHE A O     
709  C  CB    . PHE A 114 ? 0.1475 0.1303 0.1506 -0.0027 0.0077  0.0108  94  PHE A CB    
710  C  CG    . PHE A 114 ? 0.1454 0.1211 0.1521 -0.0100 -0.0040 0.0085  94  PHE A CG    
711  C  CD1   . PHE A 114 ? 0.1505 0.1347 0.1591 -0.0102 0.0041  0.0140  94  PHE A CD1   
712  C  CD2   . PHE A 114 ? 0.1541 0.1283 0.1578 -0.0083 0.0007  0.0137  94  PHE A CD2   
713  C  CE1   . PHE A 114 ? 0.1584 0.1471 0.1655 -0.0045 0.0073  0.0225  94  PHE A CE1   
714  C  CE2   . PHE A 114 ? 0.1591 0.1437 0.1668 -0.0045 -0.0011 0.0246  94  PHE A CE2   
715  C  CZ    . PHE A 114 ? 0.1631 0.1491 0.1682 -0.0008 -0.0143 0.0270  94  PHE A CZ    
716  N  N     . CYS A 115 ? 0.1505 0.1241 0.1383 -0.0025 -0.0012 0.0061  95  CYS A N     
717  C  CA    . CYS A 115 ? 0.1556 0.1319 0.1484 -0.0013 0.0139  0.0087  95  CYS A CA    
718  C  C     . CYS A 115 ? 0.1723 0.1246 0.1463 -0.0045 0.0099  0.0016  95  CYS A C     
719  O  O     . CYS A 115 ? 0.1915 0.1387 0.1373 -0.0044 0.0140  -0.0015 95  CYS A O     
720  C  CB    . CYS A 115 ? 0.1622 0.1470 0.1509 -0.0019 0.0183  0.0085  95  CYS A CB    
721  S  SG    . CYS A 115 ? 0.1812 0.1262 0.1530 -0.0016 0.0207  0.0029  95  CYS A SG    
722  N  N     . LYS A 116 ? 0.1906 0.1154 0.1460 0.0070  0.0088  -0.0006 96  LYS A N     
723  C  CA    . LYS A 116 ? 0.2065 0.1224 0.1650 0.0068  0.0039  0.0062  96  LYS A CA    
724  C  C     . LYS A 116 ? 0.2117 0.1310 0.1600 0.0121  0.0028  -0.0072 96  LYS A C     
725  O  O     . LYS A 116 ? 0.2320 0.1459 0.1636 0.0175  0.0034  -0.0216 96  LYS A O     
726  C  CB    . LYS A 116 ? 0.2236 0.1186 0.1780 0.0185  0.0093  0.0102  96  LYS A CB    
727  C  CG    . LYS A 116 ? 0.2672 0.1324 0.1923 0.0178  0.0106  0.0080  96  LYS A CG    
728  C  CD    . LYS A 116 ? 0.3332 0.1689 0.2212 0.0476  0.0198  -0.0046 96  LYS A CD    
729  C  CE    . LYS A 116 ? 0.3920 0.2077 0.2508 0.0669  0.0191  -0.0087 96  LYS A CE    
730  N  NZ    . LYS A 116 ? 0.4265 0.2413 0.2735 0.0794  0.0212  -0.0046 96  LYS A NZ    
731  N  N     . ASN A 117 ? 0.1955 0.1326 0.1552 -0.0027 0.0021  -0.0049 97  ASN A N     
732  C  CA    . ASN A 117 ? 0.2039 0.1446 0.1596 -0.0077 0.0028  -0.0080 97  ASN A CA    
733  C  C     . ASN A 117 ? 0.2393 0.1564 0.1559 -0.0061 -0.0026 -0.0129 97  ASN A C     
734  O  O     . ASN A 117 ? 0.2723 0.1959 0.1669 -0.0291 -0.0162 -0.0161 97  ASN A O     
735  C  CB    . ASN A 117 ? 0.1976 0.1481 0.1755 -0.0082 0.0074  -0.0010 97  ASN A CB    
736  C  CG    . ASN A 117 ? 0.2265 0.1655 0.2006 -0.0157 0.0107  -0.0131 97  ASN A CG    
737  O  OD1   . ASN A 117 ? 0.2504 0.1838 0.2400 -0.0372 0.0066  -0.0062 97  ASN A OD1   
738  N  ND2   . ASN A 117 ? 0.2240 0.1917 0.1935 -0.0054 -0.0065 -0.0329 97  ASN A ND2   
739  N  N     . ILE A 118 ? 0.2313 0.1513 0.1475 0.0011  0.0049  0.0010  98  ILE A N     
740  C  CA    . ILE A 118 ? 0.2304 0.1679 0.1533 0.0151  0.0096  0.0104  98  ILE A CA    
741  C  C     . ILE A 118 ? 0.2234 0.1542 0.1647 0.0150  0.0204  0.0001  98  ILE A C     
742  O  O     . ILE A 118 ? 0.2463 0.1554 0.1648 0.0049  0.0281  -0.0029 98  ILE A O     
743  C  CB    . ILE A 118 ? 0.2462 0.1829 0.1613 0.0383  0.0143  0.0234  98  ILE A CB    
744  C  CG1   . ILE A 118 ? 0.2824 0.1649 0.1610 0.0362  0.0151  0.0110  98  ILE A CG1   
745  C  CG2   . ILE A 118 ? 0.2647 0.2254 0.1883 0.0453  0.0277  0.0453  98  ILE A CG2   
746  C  CD1   . ILE A 118 ? 0.3029 0.1771 0.1735 0.0333  0.0262  0.0188  98  ILE A CD1   
747  N  N     . GLU A 119 ? 0.2385 0.1665 0.1897 0.0278  0.0317  0.0080  99  GLU A N     
748  C  CA    A GLU A 119 ? 0.2803 0.1808 0.2133 0.0366  0.0405  0.0180  99  GLU A CA    
749  C  CA    B GLU A 119 ? 0.2705 0.1711 0.2112 0.0430  0.0382  0.0170  99  GLU A CA    
750  C  C     . GLU A 119 ? 0.2954 0.1810 0.2190 0.0455  0.0462  0.0114  99  GLU A C     
751  O  O     . GLU A 119 ? 0.2898 0.2057 0.2441 0.0433  0.0579  0.0150  99  GLU A O     
752  C  CB    A GLU A 119 ? 0.3241 0.1978 0.2313 0.0367  0.0407  0.0296  99  GLU A CB    
753  C  CB    B GLU A 119 ? 0.2957 0.1710 0.2261 0.0535  0.0349  0.0259  99  GLU A CB    
754  C  CG    A GLU A 119 ? 0.3663 0.2037 0.2402 0.0415  0.0391  0.0270  99  GLU A CG    
755  C  CG    B GLU A 119 ? 0.3182 0.1667 0.2305 0.0676  0.0319  0.0188  99  GLU A CG    
756  C  CD    A GLU A 119 ? 0.4011 0.2039 0.2499 0.0382  0.0311  0.0203  99  GLU A CD    
757  C  CD    B GLU A 119 ? 0.3570 0.1777 0.2428 0.0719  0.0250  0.0160  99  GLU A CD    
758  O  OE1   A GLU A 119 ? 0.4132 0.1918 0.2514 0.0215  0.0339  0.0119  99  GLU A OE1   
759  O  OE1   B GLU A 119 ? 0.3722 0.1937 0.2411 0.0870  0.0166  0.0060  99  GLU A OE1   
760  O  OE2   A GLU A 119 ? 0.4176 0.2173 0.2528 0.0454  0.0239  0.0184  99  GLU A OE2   
761  O  OE2   B GLU A 119 ? 0.3763 0.1743 0.2515 0.0719  0.0268  0.0317  99  GLU A OE2   
762  N  N     . SER A 120 ? 0.3413 0.1828 0.2116 0.0640  0.0440  -0.0128 100 SER A N     
763  C  CA    A SER A 120 ? 0.3738 0.1971 0.2158 0.0631  0.0410  -0.0169 100 SER A CA    
764  C  CA    B SER A 120 ? 0.3745 0.1934 0.2135 0.0708  0.0376  -0.0165 100 SER A CA    
765  C  C     . SER A 120 ? 0.3624 0.2001 0.2015 0.0629  0.0383  -0.0206 100 SER A C     
766  O  O     . SER A 120 ? 0.4015 0.2262 0.2065 0.0772  0.0409  -0.0263 100 SER A O     
767  C  CB    A SER A 120 ? 0.4090 0.2172 0.2361 0.0529  0.0396  -0.0181 100 SER A CB    
768  C  CB    B SER A 120 ? 0.4121 0.2058 0.2288 0.0757  0.0297  -0.0173 100 SER A CB    
769  O  OG    A SER A 120 ? 0.4286 0.2313 0.2507 0.0426  0.0402  -0.0173 100 SER A OG    
770  O  OG    B SER A 120 ? 0.4321 0.2136 0.2379 0.0814  0.0239  -0.0144 100 SER A OG    
771  N  N     . GLU A 121 ? 0.3053 0.1710 0.1799 0.0369  0.0269  -0.0138 101 GLU A N     
772  C  CA    . GLU A 121 ? 0.2801 0.1746 0.1682 0.0225  0.0162  -0.0142 101 GLU A CA    
773  C  C     . GLU A 121 ? 0.2634 0.1869 0.1579 0.0126  0.0142  -0.0187 101 GLU A C     
774  O  O     . GLU A 121 ? 0.2607 0.1993 0.1621 0.0070  -0.0051 -0.0184 101 GLU A O     
775  C  CB    . GLU A 121 ? 0.3068 0.1910 0.1929 0.0056  0.0179  -0.0091 101 GLU A CB    
776  C  CG    . GLU A 121 ? 0.3630 0.2352 0.2274 -0.0151 0.0204  -0.0110 101 GLU A CG    
777  C  CD    . GLU A 121 ? 0.4291 0.2877 0.2663 -0.0355 0.0126  -0.0076 101 GLU A CD    
778  O  OE1   . GLU A 121 ? 0.4247 0.3106 0.2785 -0.0475 -0.0120 -0.0212 101 GLU A OE1   
779  O  OE2   . GLU A 121 ? 0.4846 0.3186 0.2905 -0.0477 0.0160  -0.0036 101 GLU A OE2   
780  N  N     . SER A 122 ? 0.2527 0.1884 0.1536 0.0130  0.0159  -0.0173 102 SER A N     
781  C  CA    . SER A 122 ? 0.2465 0.2023 0.1582 0.0048  0.0077  -0.0073 102 SER A CA    
782  C  C     . SER A 122 ? 0.2250 0.1813 0.1435 0.0019  0.0022  -0.0010 102 SER A C     
783  O  O     . SER A 122 ? 0.2284 0.1894 0.1408 -0.0102 -0.0021 0.0060  102 SER A O     
784  C  CB    . SER A 122 ? 0.2815 0.2462 0.1740 0.0093  0.0131  -0.0104 102 SER A CB    
785  O  OG    . SER A 122 ? 0.3256 0.2869 0.1786 0.0142  0.0135  -0.0124 102 SER A OG    
786  N  N     . GLU A 123 ? 0.2240 0.1703 0.1514 0.0012  0.0000  -0.0008 103 GLU A N     
787  C  CA    . GLU A 123 ? 0.2264 0.1738 0.1526 -0.0068 -0.0076 0.0044  103 GLU A CA    
788  C  C     . GLU A 123 ? 0.2164 0.1661 0.1713 -0.0205 -0.0157 -0.0052 103 GLU A C     
789  O  O     . GLU A 123 ? 0.2384 0.1812 0.2025 -0.0302 0.0051  -0.0190 103 GLU A O     
790  C  CB    . GLU A 123 ? 0.2633 0.2042 0.1613 0.0024  0.0005  0.0129  103 GLU A CB    
791  C  CG    . GLU A 123 ? 0.3470 0.2408 0.1913 0.0134  -0.0011 -0.0004 103 GLU A CG    
792  C  CD    . GLU A 123 ? 0.4238 0.2643 0.2246 0.0065  0.0027  -0.0138 103 GLU A CD    
793  O  OE1   . GLU A 123 ? 0.4702 0.2870 0.2504 -0.0044 -0.0011 -0.0335 103 GLU A OE1   
794  O  OE2   . GLU A 123 ? 0.4310 0.2838 0.2171 0.0262  0.0217  0.0005  103 GLU A OE2   
795  N  N     . ILE A 124 ? 0.2017 0.1535 0.1615 -0.0135 -0.0128 0.0049  104 ILE A N     
796  C  CA    . ILE A 124 ? 0.2003 0.1642 0.1672 -0.0239 -0.0091 0.0062  104 ILE A CA    
797  C  C     . ILE A 124 ? 0.1955 0.1666 0.1582 -0.0305 -0.0173 0.0113  104 ILE A C     
798  O  O     . ILE A 124 ? 0.2173 0.1828 0.1810 -0.0327 -0.0249 0.0221  104 ILE A O     
799  C  CB    . ILE A 124 ? 0.2014 0.1663 0.1693 -0.0042 -0.0055 0.0119  104 ILE A CB    
800  C  CG1   . ILE A 124 ? 0.1984 0.1832 0.1491 -0.0010 -0.0021 0.0110  104 ILE A CG1   
801  C  CG2   . ILE A 124 ? 0.2197 0.1724 0.1824 0.0038  0.0019  0.0067  104 ILE A CG2   
802  C  CD1   . ILE A 124 ? 0.1911 0.1999 0.1556 0.0008  0.0001  0.0180  104 ILE A CD1   
803  N  N     . ASN A 125 ? 0.2073 0.1830 0.1509 -0.0248 -0.0074 0.0026  105 ASN A N     
804  C  CA    . ASN A 125 ? 0.2058 0.2014 0.1517 -0.0289 -0.0123 0.0048  105 ASN A CA    
805  C  C     . ASN A 125 ? 0.1929 0.1842 0.1474 -0.0346 -0.0183 0.0055  105 ASN A C     
806  O  O     . ASN A 125 ? 0.1924 0.1862 0.1483 -0.0297 -0.0179 0.0097  105 ASN A O     
807  C  CB    . ASN A 125 ? 0.2240 0.2235 0.1619 -0.0395 -0.0185 0.0004  105 ASN A CB    
808  C  CG    . ASN A 125 ? 0.2580 0.2356 0.1753 -0.0488 -0.0291 -0.0128 105 ASN A CG    
809  O  OD1   . ASN A 125 ? 0.2703 0.2287 0.1674 -0.0467 -0.0312 0.0003  105 ASN A OD1   
810  N  ND2   . ASN A 125 ? 0.3032 0.2530 0.1859 -0.0507 -0.0412 -0.0229 105 ASN A ND2   
811  N  N     . SER A 126 ? 0.2093 0.1958 0.1545 -0.0273 -0.0299 0.0064  106 SER A N     
812  C  CA    . SER A 126 ? 0.2034 0.2044 0.1578 -0.0243 -0.0325 0.0083  106 SER A CA    
813  C  C     . SER A 126 ? 0.1934 0.1961 0.1577 -0.0339 -0.0274 0.0080  106 SER A C     
814  O  O     . SER A 126 ? 0.1846 0.1937 0.1468 -0.0288 -0.0165 0.0064  106 SER A O     
815  C  CB    . SER A 126 ? 0.2134 0.2283 0.1663 -0.0138 -0.0352 0.0081  106 SER A CB    
816  O  OG    . SER A 126 ? 0.2216 0.2468 0.1842 -0.0112 -0.0386 0.0137  106 SER A OG    
817  N  N     . LYS A 127 ? 0.2000 0.2023 0.1699 -0.0463 -0.0293 0.0086  107 LYS A N     
818  C  CA    . LYS A 127 ? 0.2068 0.2051 0.1802 -0.0539 -0.0345 -0.0088 107 LYS A CA    
819  C  C     . LYS A 127 ? 0.2082 0.1893 0.1588 -0.0475 -0.0166 -0.0063 107 LYS A C     
820  O  O     . LYS A 127 ? 0.2142 0.1851 0.1510 -0.0516 -0.0149 0.0019  107 LYS A O     
821  C  CB    . LYS A 127 ? 0.2340 0.2466 0.2181 -0.0662 -0.0476 -0.0206 107 LYS A CB    
822  C  CG    . LYS A 127 ? 0.2750 0.3034 0.2483 -0.0726 -0.0644 -0.0331 107 LYS A CG    
823  C  CD    . LYS A 127 ? 0.3491 0.3626 0.2784 -0.0596 -0.0668 -0.0271 107 LYS A CD    
824  C  CE    . LYS A 127 ? 0.4063 0.3947 0.2947 -0.0532 -0.0628 -0.0237 107 LYS A CE    
825  N  NZ    . LYS A 127 ? 0.4445 0.4330 0.3051 -0.0427 -0.0504 -0.0104 107 LYS A NZ    
826  N  N     . LEU A 128 ? 0.2075 0.1772 0.1517 -0.0305 -0.0132 0.0038  108 LEU A N     
827  C  CA    . LEU A 128 ? 0.2067 0.1696 0.1542 -0.0333 -0.0004 -0.0020 108 LEU A CA    
828  C  C     . LEU A 128 ? 0.1909 0.1625 0.1373 -0.0317 -0.0015 -0.0054 108 LEU A C     
829  O  O     . LEU A 128 ? 0.1993 0.1684 0.1348 -0.0102 -0.0098 -0.0006 108 LEU A O     
830  C  CB    . LEU A 128 ? 0.2448 0.1931 0.1774 -0.0195 0.0003  0.0011  108 LEU A CB    
831  C  CG    . LEU A 128 ? 0.2822 0.2263 0.2139 -0.0284 -0.0014 0.0077  108 LEU A CG    
832  C  CD1   . LEU A 128 ? 0.3035 0.2401 0.2286 -0.0322 -0.0064 0.0053  108 LEU A CD1   
833  C  CD2   . LEU A 128 ? 0.3057 0.2389 0.2293 -0.0185 0.0113  0.0081  108 LEU A CD2   
834  N  N     . LEU A 129 ? 0.1856 0.1620 0.1346 -0.0234 -0.0079 0.0018  109 LEU A N     
835  C  CA    . LEU A 129 ? 0.1751 0.1500 0.1374 -0.0235 -0.0077 0.0065  109 LEU A CA    
836  C  C     . LEU A 129 ? 0.1625 0.1566 0.1396 -0.0262 -0.0074 0.0102  109 LEU A C     
837  O  O     . LEU A 129 ? 0.1596 0.1501 0.1398 -0.0186 -0.0124 0.0076  109 LEU A O     
838  C  CB    . LEU A 129 ? 0.1691 0.1546 0.1493 -0.0157 -0.0104 0.0113  109 LEU A CB    
839  C  CG    . LEU A 129 ? 0.1716 0.1507 0.1622 -0.0138 -0.0111 0.0106  109 LEU A CG    
840  C  CD1   . LEU A 129 ? 0.1824 0.1543 0.1672 -0.0175 -0.0175 0.0140  109 LEU A CD1   
841  C  CD2   . LEU A 129 ? 0.1853 0.1647 0.1794 -0.0199 -0.0095 0.0089  109 LEU A CD2   
842  N  N     . ALA A 130 ? 0.1662 0.1621 0.1487 -0.0375 -0.0170 0.0123  110 ALA A N     
843  C  CA    . ALA A 130 ? 0.1686 0.1611 0.1506 -0.0371 -0.0121 0.0083  110 ALA A CA    
844  C  C     . ALA A 130 ? 0.1675 0.1508 0.1569 -0.0315 -0.0163 0.0006  110 ALA A C     
845  O  O     . ALA A 130 ? 0.1655 0.1542 0.1534 -0.0259 -0.0108 0.0103  110 ALA A O     
846  C  CB    . ALA A 130 ? 0.1732 0.1710 0.1553 -0.0318 -0.0078 0.0095  110 ALA A CB    
847  N  N     . GLU A 131 ? 0.1810 0.1416 0.1558 -0.0344 -0.0125 -0.0065 111 GLU A N     
848  C  CA    . GLU A 131 ? 0.2023 0.1426 0.1591 -0.0338 -0.0166 -0.0106 111 GLU A CA    
849  C  C     . GLU A 131 ? 0.1935 0.1267 0.1529 -0.0213 -0.0045 -0.0034 111 GLU A C     
850  O  O     . GLU A 131 ? 0.2042 0.1272 0.1558 -0.0223 -0.0142 0.0007  111 GLU A O     
851  C  CB    . GLU A 131 ? 0.2304 0.1728 0.1833 -0.0444 -0.0339 -0.0180 111 GLU A CB    
852  C  CG    . GLU A 131 ? 0.2963 0.2055 0.2168 -0.0287 -0.0148 -0.0223 111 GLU A CG    
853  N  N     . SER A 132 ? 0.1866 0.1259 0.1548 -0.0210 -0.0056 -0.0017 112 SER A N     
854  C  CA    . SER A 132 ? 0.1770 0.1413 0.1460 -0.0084 -0.0082 0.0006  112 SER A CA    
855  C  C     . SER A 132 ? 0.1606 0.1325 0.1425 -0.0097 -0.0059 -0.0063 112 SER A C     
856  O  O     . SER A 132 ? 0.1645 0.1237 0.1500 -0.0074 -0.0098 -0.0005 112 SER A O     
857  C  CB    . SER A 132 ? 0.1761 0.1766 0.1386 -0.0068 0.0030  -0.0057 112 SER A CB    
858  O  OG    . SER A 132 ? 0.1910 0.1981 0.1446 0.0038  0.0004  -0.0063 112 SER A OG    
859  N  N     . PHE A 133 ? 0.1482 0.1286 0.1403 -0.0107 -0.0105 0.0003  113 PHE A N     
860  C  CA    . PHE A 133 ? 0.1511 0.1189 0.1430 -0.0122 -0.0047 0.0045  113 PHE A CA    
861  C  C     . PHE A 133 ? 0.1471 0.1168 0.1485 -0.0122 -0.0059 0.0040  113 PHE A C     
862  O  O     . PHE A 133 ? 0.1566 0.1196 0.1337 -0.0005 -0.0065 0.0032  113 PHE A O     
863  C  CB    . PHE A 133 ? 0.1584 0.1229 0.1440 -0.0144 -0.0064 0.0082  113 PHE A CB    
864  C  CG    . PHE A 133 ? 0.1554 0.1273 0.1434 -0.0042 0.0012  0.0061  113 PHE A CG    
865  C  CD1   . PHE A 133 ? 0.1730 0.1325 0.1466 -0.0093 -0.0077 -0.0005 113 PHE A CD1   
866  C  CD2   . PHE A 133 ? 0.1623 0.1368 0.1468 -0.0006 0.0007  0.0150  113 PHE A CD2   
867  C  CE1   . PHE A 133 ? 0.1975 0.1245 0.1481 -0.0155 -0.0151 0.0057  113 PHE A CE1   
868  C  CE2   . PHE A 133 ? 0.1781 0.1333 0.1481 -0.0041 -0.0047 0.0228  113 PHE A CE2   
869  C  CZ    . PHE A 133 ? 0.1959 0.1268 0.1518 -0.0095 0.0005  0.0130  113 PHE A CZ    
870  N  N     . GLN A 134 ? 0.1523 0.1181 0.1518 -0.0177 -0.0065 0.0036  114 GLN A N     
871  C  CA    . GLN A 134 ? 0.1538 0.1087 0.1695 -0.0274 -0.0116 0.0005  114 GLN A CA    
872  C  C     . GLN A 134 ? 0.1517 0.1144 0.1578 -0.0160 -0.0045 -0.0067 114 GLN A C     
873  O  O     . GLN A 134 ? 0.1680 0.1180 0.1643 -0.0173 -0.0153 0.0045  114 GLN A O     
874  C  CB    . GLN A 134 ? 0.1736 0.1298 0.1978 -0.0289 -0.0173 -0.0011 114 GLN A CB    
875  C  CG    . GLN A 134 ? 0.2263 0.1595 0.2349 -0.0429 -0.0142 0.0060  114 GLN A CG    
876  C  CD    . GLN A 134 ? 0.2929 0.2039 0.2751 -0.0391 0.0072  0.0110  114 GLN A CD    
877  O  OE1   . GLN A 134 ? 0.3196 0.2274 0.2952 -0.0262 0.0183  0.0091  114 GLN A OE1   
878  N  NE2   . GLN A 134 ? 0.3357 0.2425 0.2847 -0.0340 0.0041  0.0159  114 GLN A NE2   
879  N  N     . ALA A 135 ? 0.1694 0.1185 0.1578 -0.0129 -0.0045 -0.0095 115 ALA A N     
880  C  CA    . ALA A 135 ? 0.1720 0.1283 0.1635 -0.0066 -0.0061 -0.0101 115 ALA A CA    
881  C  C     . ALA A 135 ? 0.1514 0.1166 0.1576 -0.0003 0.0016  -0.0072 115 ALA A C     
882  O  O     . ALA A 135 ? 0.1858 0.1200 0.1596 0.0105  0.0019  -0.0033 115 ALA A O     
883  C  CB    . ALA A 135 ? 0.1857 0.1358 0.1683 -0.0053 -0.0029 -0.0148 115 ALA A CB    
884  N  N     . GLY A 136 ? 0.1565 0.1181 0.1538 -0.0013 0.0052  0.0009  116 GLY A N     
885  C  CA    . GLY A 136 ? 0.1473 0.1169 0.1459 -0.0177 -0.0072 -0.0027 116 GLY A CA    
886  C  C     . GLY A 136 ? 0.1361 0.1078 0.1499 -0.0044 -0.0023 0.0023  116 GLY A C     
887  O  O     . GLY A 136 ? 0.1444 0.1098 0.1536 -0.0004 -0.0080 0.0058  116 GLY A O     
888  N  N     . VAL A 137 ? 0.1345 0.1112 0.1455 -0.0095 -0.0006 0.0092  117 VAL A N     
889  C  CA    . VAL A 137 ? 0.1333 0.1205 0.1562 -0.0035 0.0003  0.0051  117 VAL A CA    
890  C  C     . VAL A 137 ? 0.1306 0.1159 0.1600 -0.0050 -0.0030 0.0066  117 VAL A C     
891  O  O     . VAL A 137 ? 0.1405 0.1375 0.1558 0.0014  -0.0025 0.0212  117 VAL A O     
892  C  CB    . VAL A 137 ? 0.1395 0.1357 0.1609 -0.0041 0.0074  0.0090  117 VAL A CB    
893  C  CG1   . VAL A 137 ? 0.1520 0.1443 0.1826 -0.0060 0.0017  0.0188  117 VAL A CG1   
894  C  CG2   . VAL A 137 ? 0.1459 0.1458 0.1544 0.0079  0.0055  0.0027  117 VAL A CG2   
895  N  N     . GLU A 138 ? 0.1434 0.1082 0.1771 -0.0166 -0.0087 0.0090  118 GLU A N     
896  C  CA    A GLU A 138 ? 0.1551 0.1219 0.1957 -0.0203 -0.0040 0.0085  118 GLU A CA    
897  C  CA    B GLU A 138 ? 0.1687 0.1106 0.1938 -0.0167 -0.0049 0.0098  118 GLU A CA    
898  C  C     . GLU A 138 ? 0.1523 0.1144 0.1854 -0.0045 0.0009  0.0072  118 GLU A C     
899  O  O     . GLU A 138 ? 0.1745 0.1254 0.1809 -0.0062 0.0008  0.0210  118 GLU A O     
900  C  CB    A GLU A 138 ? 0.1904 0.1596 0.2279 -0.0247 -0.0203 0.0037  118 GLU A CB    
901  C  CB    B GLU A 138 ? 0.2272 0.1282 0.2225 -0.0150 -0.0223 0.0068  118 GLU A CB    
902  C  CG    A GLU A 138 ? 0.2500 0.2209 0.2600 -0.0303 -0.0300 0.0044  118 GLU A CG    
903  C  CG    B GLU A 138 ? 0.3028 0.1782 0.2512 -0.0211 -0.0330 0.0083  118 GLU A CG    
904  C  CD    A GLU A 138 ? 0.2966 0.2734 0.2932 -0.0356 -0.0307 0.0082  118 GLU A CD    
905  C  CD    B GLU A 138 ? 0.3650 0.2184 0.2811 -0.0276 -0.0354 0.0138  118 GLU A CD    
906  O  OE1   A GLU A 138 ? 0.3196 0.2866 0.3056 -0.0553 -0.0293 0.0099  118 GLU A OE1   
907  O  OE1   B GLU A 138 ? 0.3955 0.2250 0.2964 -0.0225 -0.0330 0.0033  118 GLU A OE1   
908  O  OE2   A GLU A 138 ? 0.3206 0.3022 0.3068 -0.0228 -0.0226 0.0109  118 GLU A OE2   
909  O  OE2   B GLU A 138 ? 0.3915 0.2451 0.2909 -0.0348 -0.0351 0.0288  118 GLU A OE2   
910  N  N     . THR A 139 ? 0.1525 0.1171 0.1745 0.0015  -0.0040 0.0064  119 THR A N     
911  C  CA    . THR A 139 ? 0.1490 0.1200 0.1672 0.0081  -0.0015 0.0110  119 THR A CA    
912  C  C     . THR A 139 ? 0.1529 0.1205 0.1635 0.0104  -0.0088 0.0088  119 THR A C     
913  O  O     . THR A 139 ? 0.1544 0.1375 0.1679 0.0109  -0.0124 0.0182  119 THR A O     
914  C  CB    . THR A 139 ? 0.1591 0.1325 0.1642 0.0043  -0.0034 0.0055  119 THR A CB    
915  O  OG1   . THR A 139 ? 0.1757 0.1561 0.1629 0.0017  -0.0100 0.0113  119 THR A OG1   
916  C  CG2   . THR A 139 ? 0.1623 0.1361 0.1681 0.0072  0.0001  0.0043  119 THR A CG2   
917  N  N     . ALA A 140 ? 0.1552 0.1189 0.1590 0.0035  -0.0116 0.0059  120 ALA A N     
918  C  CA    . ALA A 140 ? 0.1521 0.1231 0.1594 0.0024  -0.0147 -0.0046 120 ALA A CA    
919  C  C     . ALA A 140 ? 0.1347 0.1278 0.1616 0.0086  -0.0029 0.0040  120 ALA A C     
920  O  O     . ALA A 140 ? 0.1518 0.1425 0.1638 -0.0028 -0.0083 0.0095  120 ALA A O     
921  C  CB    . ALA A 140 ? 0.1668 0.1240 0.1670 0.0021  -0.0110 -0.0007 120 ALA A CB    
922  N  N     . TYR A 141 ? 0.1517 0.1388 0.1576 -0.0014 -0.0107 0.0145  121 TYR A N     
923  C  CA    . TYR A 141 ? 0.1498 0.1460 0.1689 0.0022  0.0053  0.0134  121 TYR A CA    
924  C  C     . TYR A 141 ? 0.1668 0.1495 0.1761 0.0154  0.0100  0.0173  121 TYR A C     
925  O  O     . TYR A 141 ? 0.2072 0.1646 0.1850 0.0327  0.0119  0.0323  121 TYR A O     
926  C  CB    . TYR A 141 ? 0.1557 0.1453 0.1854 -0.0017 0.0058  0.0183  121 TYR A CB    
927  C  CG    . TYR A 141 ? 0.1425 0.1397 0.1886 -0.0150 0.0021  0.0167  121 TYR A CG    
928  C  CD1   . TYR A 141 ? 0.1395 0.1380 0.1757 0.0014  0.0004  0.0163  121 TYR A CD1   
929  C  CD2   . TYR A 141 ? 0.1630 0.1464 0.1962 -0.0061 0.0070  0.0246  121 TYR A CD2   
930  C  CE1   . TYR A 141 ? 0.1501 0.1398 0.1845 0.0050  -0.0037 0.0126  121 TYR A CE1   
931  C  CE2   . TYR A 141 ? 0.1611 0.1603 0.2013 -0.0003 0.0190  0.0174  121 TYR A CE2   
932  C  CZ    . TYR A 141 ? 0.1431 0.1544 0.2002 0.0045  0.0067  0.0125  121 TYR A CZ    
933  O  OH    . TYR A 141 ? 0.1656 0.1683 0.2206 0.0001  0.0099  0.0015  121 TYR A OH    
934  N  N     . LYS A 142 ? 0.1670 0.1364 0.1796 0.0150  0.0082  0.0254  122 LYS A N     
935  C  CA    . LYS A 142 ? 0.1720 0.1382 0.2035 0.0114  0.0044  0.0248  122 LYS A CA    
936  C  C     . LYS A 142 ? 0.1675 0.1472 0.1958 0.0274  0.0078  0.0356  122 LYS A C     
937  O  O     . LYS A 142 ? 0.1904 0.1605 0.2154 0.0312  0.0085  0.0470  122 LYS A O     
938  C  CB    . LYS A 142 ? 0.1989 0.1516 0.2411 -0.0006 0.0077  0.0069  122 LYS A CB    
939  C  CG    . LYS A 142 ? 0.2430 0.1952 0.2686 -0.0015 0.0115  -0.0064 122 LYS A CG    
940  C  CD    . LYS A 142 ? 0.2870 0.2275 0.2849 -0.0084 0.0109  -0.0237 122 LYS A CD    
941  N  N     . ALA A 143 ? 0.1606 0.1473 0.1820 0.0313  -0.0094 0.0235  123 ALA A N     
942  C  CA    . ALA A 143 ? 0.1599 0.1578 0.1745 0.0285  -0.0053 0.0137  123 ALA A CA    
943  C  C     . ALA A 143 ? 0.1560 0.1633 0.1768 0.0368  -0.0180 0.0201  123 ALA A C     
944  O  O     . ALA A 143 ? 0.1647 0.1865 0.1768 0.0233  -0.0210 0.0153  123 ALA A O     
945  C  CB    . ALA A 143 ? 0.1562 0.1779 0.1717 0.0114  -0.0084 0.0026  123 ALA A CB    
946  N  N     . VAL A 144 ? 0.1645 0.1842 0.1679 0.0269  -0.0271 0.0131  124 VAL A N     
947  C  CA    . VAL A 144 ? 0.1615 0.1742 0.1693 0.0151  -0.0191 0.0225  124 VAL A CA    
948  C  C     . VAL A 144 ? 0.1838 0.1741 0.1901 0.0163  -0.0262 0.0371  124 VAL A C     
949  O  O     . VAL A 144 ? 0.2057 0.1786 0.2172 0.0053  -0.0316 0.0391  124 VAL A O     
950  C  CB    . VAL A 144 ? 0.1705 0.1696 0.1614 0.0148  -0.0055 0.0222  124 VAL A CB    
951  C  CG1   . VAL A 144 ? 0.1824 0.1757 0.1641 0.0120  0.0054  0.0201  124 VAL A CG1   
952  C  CG2   . VAL A 144 ? 0.1713 0.1689 0.1561 0.0095  0.0094  0.0151  124 VAL A CG2   
953  N  N     . MET A 145 ? 0.1878 0.1809 0.1963 0.0227  -0.0220 0.0362  125 MET A N     
954  C  CA    . MET A 145 ? 0.1826 0.1932 0.2201 0.0344  -0.0155 0.0546  125 MET A CA    
955  C  C     . MET A 145 ? 0.1758 0.1924 0.2684 0.0309  -0.0203 0.0780  125 MET A C     
956  O  O     . MET A 145 ? 0.2026 0.2018 0.3023 0.0057  -0.0198 0.0757  125 MET A O     
957  C  CB    . MET A 145 ? 0.1710 0.2145 0.1972 0.0462  -0.0055 0.0501  125 MET A CB    
958  C  CG    . MET A 145 ? 0.1855 0.2349 0.1860 0.0631  0.0055  0.0405  125 MET A CG    
959  S  SD    . MET A 145 ? 0.1998 0.2580 0.1905 0.0779  0.0094  0.0421  125 MET A SD    
960  C  CE    . MET A 145 ? 0.2015 0.2727 0.2011 0.0507  -0.0048 0.0561  125 MET A CE    
961  N  N     . LYS A 146 ? 0.1589 0.1939 0.2796 0.0445  -0.0003 0.0912  126 LYS A N     
962  C  CA    . LYS A 146 ? 0.1921 0.2093 0.2913 0.0480  0.0270  0.1039  126 LYS A CA    
963  C  C     . LYS A 146 ? 0.1623 0.1862 0.2900 0.0236  0.0241  0.0907  126 LYS A C     
964  O  O     . LYS A 146 ? 0.1650 0.2093 0.2821 0.0246  0.0315  0.0961  126 LYS A O     
965  C  CB    . LYS A 146 ? 0.2595 0.2366 0.3056 0.0696  0.0475  0.1225  126 LYS A CB    
966  C  CG    . LYS A 146 ? 0.3320 0.2745 0.3319 0.0687  0.0358  0.1190  126 LYS A CG    
967  C  CD    . LYS A 146 ? 0.3716 0.2899 0.3523 0.0623  0.0280  0.1151  126 LYS A CD    
968  C  CE    . LYS A 146 ? 0.4048 0.3124 0.3691 0.0368  0.0241  0.1137  126 LYS A CE    
969  N  NZ    . LYS A 146 ? 0.4242 0.3373 0.3837 0.0164  0.0211  0.1028  126 LYS A NZ    
970  N  N     . PRO A 147 ? 0.1767 0.1647 0.2958 0.0178  0.0090  0.0726  127 PRO A N     
971  C  CA    . PRO A 147 ? 0.1722 0.1498 0.2825 0.0221  0.0124  0.0717  127 PRO A CA    
972  C  C     . PRO A 147 ? 0.1427 0.1515 0.2696 -0.0031 0.0239  0.0621  127 PRO A C     
973  O  O     . PRO A 147 ? 0.1819 0.1605 0.2904 -0.0051 0.0413  0.0648  127 PRO A O     
974  C  CB    . PRO A 147 ? 0.2120 0.1573 0.2910 0.0206  0.0057  0.0584  127 PRO A CB    
975  C  CG    . PRO A 147 ? 0.2249 0.1788 0.3033 0.0182  -0.0022 0.0462  127 PRO A CG    
976  C  CD    . PRO A 147 ? 0.2028 0.1742 0.3089 0.0162  -0.0038 0.0536  127 PRO A CD    
977  N  N     . VAL A 148 ? 0.1266 0.1492 0.2297 0.0026  0.0262  0.0602  128 VAL A N     
978  C  CA    . VAL A 148 ? 0.1302 0.1692 0.2079 0.0043  0.0239  0.0493  128 VAL A CA    
979  C  C     . VAL A 148 ? 0.1382 0.1541 0.1855 0.0039  0.0104  0.0439  128 VAL A C     
980  O  O     . VAL A 148 ? 0.1451 0.1572 0.1921 -0.0037 0.0179  0.0572  128 VAL A O     
981  C  CB    . VAL A 148 ? 0.1549 0.2011 0.2011 0.0033  0.0073  0.0464  128 VAL A CB    
982  C  CG1   . VAL A 148 ? 0.1726 0.2118 0.1926 -0.0064 0.0003  0.0376  128 VAL A CG1   
983  C  CG2   . VAL A 148 ? 0.1849 0.2162 0.1979 0.0079  -0.0020 0.0489  128 VAL A CG2   
984  N  N     . GLU A 149 ? 0.1320 0.1487 0.1752 -0.0011 0.0130  0.0453  129 GLU A N     
985  C  CA    . GLU A 149 ? 0.1326 0.1544 0.1629 0.0010  0.0063  0.0395  129 GLU A CA    
986  C  C     . GLU A 149 ? 0.1350 0.1588 0.1472 0.0050  0.0028  0.0368  129 GLU A C     
987  O  O     . GLU A 149 ? 0.1626 0.1694 0.1378 0.0083  0.0087  0.0256  129 GLU A O     
988  C  CB    . GLU A 149 ? 0.1588 0.1654 0.1903 -0.0194 -0.0012 0.0345  129 GLU A CB    
989  C  CG    . GLU A 149 ? 0.1793 0.1737 0.2149 -0.0368 -0.0016 0.0358  129 GLU A CG    
990  C  CD    . GLU A 149 ? 0.2206 0.1940 0.2307 -0.0216 0.0004  0.0223  129 GLU A CD    
991  O  OE1   . GLU A 149 ? 0.2161 0.2041 0.2239 -0.0347 -0.0031 0.0324  129 GLU A OE1   
992  O  OE2   . GLU A 149 ? 0.2445 0.2112 0.2563 -0.0130 0.0230  0.0331  129 GLU A OE2   
993  N  N     . GLY A 150 ? 0.1316 0.1540 0.1414 -0.0016 0.0072  0.0241  130 GLY A N     
994  C  CA    . GLY A 150 ? 0.1361 0.1522 0.1416 -0.0075 0.0114  0.0178  130 GLY A CA    
995  C  C     . GLY A 150 ? 0.1345 0.1462 0.1341 -0.0170 -0.0020 0.0075  130 GLY A C     
996  O  O     . GLY A 150 ? 0.1439 0.1514 0.1496 -0.0088 0.0189  0.0103  130 GLY A O     
997  N  N     . THR A 151 ? 0.1339 0.1435 0.1299 -0.0178 0.0071  -0.0019 131 THR A N     
998  C  CA    . THR A 151 ? 0.1357 0.1380 0.1320 -0.0174 0.0004  0.0051  131 THR A CA    
999  C  C     . THR A 151 ? 0.1412 0.1229 0.1315 -0.0115 0.0000  0.0010  131 THR A C     
1000 O  O     . THR A 151 ? 0.1385 0.1289 0.1322 -0.0090 -0.0025 0.0018  131 THR A O     
1001 C  CB    . THR A 151 ? 0.1529 0.1484 0.1397 -0.0165 0.0033  0.0107  131 THR A CB    
1002 O  OG1   . THR A 151 ? 0.1476 0.1341 0.1497 -0.0118 0.0074  0.0196  131 THR A OG1   
1003 C  CG2   . THR A 151 ? 0.1594 0.1744 0.1415 -0.0101 0.0121  0.0202  131 THR A CG2   
1004 N  N     . ILE A 152 ? 0.1306 0.1270 0.1215 -0.0093 -0.0012 -0.0015 132 ILE A N     
1005 C  CA    . ILE A 152 ? 0.1330 0.1147 0.1167 0.0020  0.0017  0.0055  132 ILE A CA    
1006 C  C     . ILE A 152 ? 0.1230 0.1043 0.1281 -0.0112 0.0071  0.0047  132 ILE A C     
1007 O  O     . ILE A 152 ? 0.1377 0.1178 0.1236 -0.0087 -0.0067 0.0065  132 ILE A O     
1008 C  CB    . ILE A 152 ? 0.1348 0.1206 0.1242 -0.0059 0.0093  0.0081  132 ILE A CB    
1009 C  CG1   . ILE A 152 ? 0.1422 0.1277 0.1315 -0.0117 0.0101  0.0051  132 ILE A CG1   
1010 C  CG2   . ILE A 152 ? 0.1399 0.1251 0.1259 -0.0098 0.0088  0.0045  132 ILE A CG2   
1011 C  CD1   . ILE A 152 ? 0.1393 0.1328 0.1398 -0.0169 0.0159  0.0015  132 ILE A CD1   
1012 N  N     . LEU A 153 ? 0.1307 0.1003 0.1275 -0.0108 0.0014  0.0068  133 LEU A N     
1013 C  CA    . LEU A 153 ? 0.1329 0.1049 0.1392 -0.0026 0.0039  0.0047  133 LEU A CA    
1014 C  C     . LEU A 153 ? 0.1340 0.1096 0.1386 -0.0098 -0.0003 0.0163  133 LEU A C     
1015 O  O     . LEU A 153 ? 0.1403 0.1191 0.1368 -0.0104 -0.0070 0.0093  133 LEU A O     
1016 C  CB    . LEU A 153 ? 0.1346 0.1112 0.1604 -0.0017 -0.0043 -0.0005 133 LEU A CB    
1017 C  CG    . LEU A 153 ? 0.1473 0.1192 0.1787 -0.0048 -0.0076 0.0077  133 LEU A CG    
1018 C  CD1   . LEU A 153 ? 0.1663 0.1284 0.1897 0.0010  -0.0105 0.0213  133 LEU A CD1   
1019 C  CD2   . LEU A 153 ? 0.1615 0.1423 0.1950 0.0086  -0.0007 -0.0002 133 LEU A CD2   
1020 N  N     . THR A 154 ? 0.1274 0.1253 0.1282 -0.0032 0.0011  0.0152  134 THR A N     
1021 C  CA    . THR A 154 ? 0.1423 0.1342 0.1335 -0.0062 0.0066  0.0124  134 THR A CA    
1022 C  C     . THR A 154 ? 0.1235 0.1291 0.1364 -0.0143 -0.0003 0.0074  134 THR A C     
1023 O  O     . THR A 154 ? 0.1315 0.1300 0.1345 -0.0134 -0.0037 0.0098  134 THR A O     
1024 C  CB    . THR A 154 ? 0.1431 0.1640 0.1394 0.0002  0.0083  0.0265  134 THR A CB    
1025 O  OG1   . THR A 154 ? 0.1567 0.1580 0.1415 -0.0103 0.0045  0.0267  134 THR A OG1   
1026 C  CG2   . THR A 154 ? 0.1615 0.2192 0.1499 0.0014  0.0172  0.0399  134 THR A CG2   
1027 N  N     . VAL A 155 ? 0.1307 0.1254 0.1291 -0.0127 0.0007  0.0048  135 VAL A N     
1028 C  CA    . VAL A 155 ? 0.1285 0.1233 0.1367 -0.0045 0.0003  0.0092  135 VAL A CA    
1029 C  C     . VAL A 155 ? 0.1211 0.1221 0.1326 -0.0017 0.0066  0.0159  135 VAL A C     
1030 O  O     . VAL A 155 ? 0.1320 0.1269 0.1295 -0.0040 -0.0067 0.0102  135 VAL A O     
1031 C  CB    . VAL A 155 ? 0.1268 0.1192 0.1456 -0.0107 0.0015  0.0081  135 VAL A CB    
1032 C  CG1   . VAL A 155 ? 0.1591 0.1148 0.1543 -0.0100 0.0001  0.0060  135 VAL A CG1   
1033 C  CG2   . VAL A 155 ? 0.1407 0.1284 0.1471 0.0046  0.0004  -0.0130 135 VAL A CG2   
1034 N  N     . ALA A 156 ? 0.1247 0.1165 0.1320 -0.0049 -0.0016 0.0091  136 ALA A N     
1035 C  CA    . ALA A 156 ? 0.1285 0.1167 0.1303 -0.0107 0.0001  -0.0020 136 ALA A CA    
1036 C  C     . ALA A 156 ? 0.1270 0.1152 0.1380 -0.0090 0.0036  0.0046  136 ALA A C     
1037 O  O     . ALA A 156 ? 0.1248 0.1238 0.1370 -0.0082 -0.0027 0.0052  136 ALA A O     
1038 C  CB    . ALA A 156 ? 0.1300 0.1263 0.1394 -0.0129 0.0075  -0.0087 136 ALA A CB    
1039 N  N     . LYS A 157 ? 0.1304 0.1151 0.1416 -0.0153 0.0017  0.0041  137 LYS A N     
1040 C  CA    . LYS A 157 ? 0.1313 0.1099 0.1511 -0.0146 -0.0068 0.0077  137 LYS A CA    
1041 C  C     . LYS A 157 ? 0.1363 0.1189 0.1501 -0.0141 -0.0040 0.0034  137 LYS A C     
1042 O  O     . LYS A 157 ? 0.1476 0.1227 0.1503 -0.0170 -0.0168 0.0013  137 LYS A O     
1043 C  CB    . LYS A 157 ? 0.1451 0.1341 0.1696 -0.0161 -0.0037 0.0129  137 LYS A CB    
1044 C  CG    . LYS A 157 ? 0.1793 0.1675 0.2000 -0.0406 -0.0168 0.0294  137 LYS A CG    
1045 C  CD    . LYS A 157 ? 0.2483 0.2090 0.2403 -0.0666 -0.0234 0.0385  137 LYS A CD    
1046 C  CE    . LYS A 157 ? 0.3164 0.2543 0.2716 -0.0522 -0.0256 0.0437  137 LYS A CE    
1047 N  NZ    . LYS A 157 ? 0.3699 0.2781 0.2899 -0.0485 -0.0329 0.0452  137 LYS A NZ    
1048 N  N     . ASP A 158 ? 0.1336 0.1236 0.1512 -0.0060 -0.0043 0.0002  138 ASP A N     
1049 C  CA    . ASP A 158 ? 0.1279 0.1418 0.1558 -0.0047 -0.0119 -0.0068 138 ASP A CA    
1050 C  C     . ASP A 158 ? 0.1298 0.1488 0.1544 -0.0018 -0.0147 -0.0057 138 ASP A C     
1051 O  O     . ASP A 158 ? 0.1328 0.1704 0.1593 -0.0053 -0.0203 -0.0025 138 ASP A O     
1052 C  CB    . ASP A 158 ? 0.1264 0.1509 0.1621 -0.0080 -0.0046 0.0006  138 ASP A CB    
1053 C  CG    . ASP A 158 ? 0.1618 0.1555 0.1731 -0.0304 0.0045  -0.0021 138 ASP A CG    
1054 O  OD1   . ASP A 158 ? 0.2354 0.1839 0.1871 -0.0604 0.0276  -0.0052 138 ASP A OD1   
1055 O  OD2   . ASP A 158 ? 0.1560 0.1626 0.1736 -0.0215 0.0114  -0.0020 138 ASP A OD2   
1056 N  N     . ALA A 159 ? 0.1381 0.1433 0.1423 0.0009  -0.0174 0.0059  139 ALA A N     
1057 C  CA    . ALA A 159 ? 0.1539 0.1219 0.1445 0.0012  -0.0166 0.0065  139 ALA A CA    
1058 C  C     . ALA A 159 ? 0.1507 0.1283 0.1413 -0.0063 -0.0126 0.0014  139 ALA A C     
1059 O  O     . ALA A 159 ? 0.1583 0.1490 0.1427 -0.0064 -0.0276 0.0060  139 ALA A O     
1060 C  CB    . ALA A 159 ? 0.1805 0.1259 0.1467 -0.0104 -0.0137 0.0111  139 ALA A CB    
1061 N  N     . ALA A 160 ? 0.1488 0.1303 0.1373 -0.0013 -0.0119 0.0040  140 ALA A N     
1062 C  CA    . ALA A 160 ? 0.1527 0.1417 0.1431 -0.0072 -0.0077 0.0021  140 ALA A CA    
1063 C  C     . ALA A 160 ? 0.1498 0.1480 0.1523 -0.0144 -0.0159 -0.0002 140 ALA A C     
1064 O  O     . ALA A 160 ? 0.1574 0.1597 0.1462 -0.0084 -0.0219 -0.0039 140 ALA A O     
1065 C  CB    . ALA A 160 ? 0.1478 0.1463 0.1402 -0.0102 -0.0031 -0.0079 140 ALA A CB    
1066 N  N     . GLN A 161 ? 0.1460 0.1657 0.1579 -0.0217 -0.0233 -0.0019 141 GLN A N     
1067 C  CA    . GLN A 161 ? 0.1536 0.1869 0.1779 -0.0343 -0.0118 0.0043  141 GLN A CA    
1068 C  C     . GLN A 161 ? 0.1442 0.2040 0.1715 -0.0276 -0.0215 -0.0022 141 GLN A C     
1069 O  O     . GLN A 161 ? 0.1571 0.2248 0.1757 -0.0226 -0.0326 -0.0100 141 GLN A O     
1070 C  CB    . GLN A 161 ? 0.1634 0.2142 0.2175 -0.0443 -0.0232 0.0094  141 GLN A CB    
1071 C  CG    . GLN A 161 ? 0.2414 0.2596 0.2782 -0.0497 -0.0277 0.0038  141 GLN A CG    
1072 C  CD    . GLN A 161 ? 0.3491 0.2938 0.3543 -0.0572 -0.0378 -0.0025 141 GLN A CD    
1073 O  OE1   . GLN A 161 ? 0.4178 0.3063 0.4023 -0.0436 -0.0279 -0.0012 141 GLN A OE1   
1074 N  NE2   . GLN A 161 ? 0.3954 0.3211 0.3750 -0.0664 -0.0422 -0.0089 141 GLN A NE2   
1075 N  N     . ALA A 162 ? 0.1466 0.2002 0.1612 -0.0093 -0.0292 0.0001  142 ALA A N     
1076 C  CA    . ALA A 162 ? 0.1613 0.2027 0.1611 0.0115  -0.0322 0.0061  142 ALA A CA    
1077 C  C     . ALA A 162 ? 0.1652 0.1899 0.1557 0.0030  -0.0386 -0.0033 142 ALA A C     
1078 O  O     . ALA A 162 ? 0.1811 0.2156 0.1645 0.0031  -0.0456 0.0006  142 ALA A O     
1079 C  CB    . ALA A 162 ? 0.1770 0.2169 0.1726 0.0273  -0.0216 0.0089  142 ALA A CB    
1080 N  N     . ALA A 163 ? 0.1525 0.1671 0.1556 -0.0171 -0.0275 -0.0034 143 ALA A N     
1081 C  CA    . ALA A 163 ? 0.1599 0.1525 0.1571 -0.0175 -0.0254 -0.0008 143 ALA A CA    
1082 C  C     . ALA A 163 ? 0.1547 0.1572 0.1520 -0.0339 -0.0217 -0.0020 143 ALA A C     
1083 O  O     . ALA A 163 ? 0.1659 0.1813 0.1478 -0.0342 -0.0227 0.0048  143 ALA A O     
1084 C  CB    . ALA A 163 ? 0.1767 0.1500 0.1568 -0.0221 -0.0106 0.0031  143 ALA A CB    
1085 N  N     . ILE A 164 ? 0.1605 0.1510 0.1551 -0.0415 -0.0148 -0.0054 144 ILE A N     
1086 C  CA    A ILE A 164 ? 0.1763 0.1758 0.1754 -0.0434 -0.0224 -0.0088 144 ILE A CA    
1087 C  CA    B ILE A 164 ? 0.1725 0.1676 0.1718 -0.0489 -0.0199 -0.0056 144 ILE A CA    
1088 C  C     . ILE A 164 ? 0.1709 0.1967 0.1724 -0.0521 -0.0188 -0.0035 144 ILE A C     
1089 O  O     . ILE A 164 ? 0.2008 0.2243 0.1619 -0.0536 -0.0306 -0.0111 144 ILE A O     
1090 C  CB    A ILE A 164 ? 0.2038 0.1845 0.1983 -0.0435 -0.0298 -0.0172 144 ILE A CB    
1091 C  CB    B ILE A 164 ? 0.1935 0.1620 0.1883 -0.0592 -0.0218 -0.0077 144 ILE A CB    
1092 C  CG1   A ILE A 164 ? 0.2282 0.1966 0.2068 -0.0419 -0.0303 -0.0225 144 ILE A CG1   
1093 C  CG1   B ILE A 164 ? 0.2123 0.1619 0.1926 -0.0596 -0.0265 -0.0059 144 ILE A CG1   
1094 C  CG2   A ILE A 164 ? 0.2111 0.1847 0.2080 -0.0431 -0.0410 -0.0160 144 ILE A CG2   
1095 C  CG2   B ILE A 164 ? 0.2090 0.1643 0.1988 -0.0602 -0.0276 -0.0061 144 ILE A CG2   
1096 C  CD1   A ILE A 164 ? 0.2467 0.2105 0.2167 -0.0433 -0.0239 -0.0236 144 ILE A CD1   
1097 C  CD1   B ILE A 164 ? 0.2203 0.1634 0.1951 -0.0606 -0.0331 -0.0046 144 ILE A CD1   
1098 N  N     . GLU A 165 ? 0.1590 0.2278 0.1782 -0.0511 -0.0173 0.0140  145 GLU A N     
1099 C  CA    . GLU A 165 ? 0.1629 0.2685 0.1971 -0.0511 -0.0231 0.0242  145 GLU A CA    
1100 C  C     . GLU A 165 ? 0.1697 0.2838 0.1851 -0.0508 -0.0344 0.0228  145 GLU A C     
1101 O  O     . GLU A 165 ? 0.1960 0.3146 0.1883 -0.0515 -0.0502 0.0192  145 GLU A O     
1102 C  CB    . GLU A 165 ? 0.1633 0.3044 0.2310 -0.0498 -0.0191 0.0415  145 GLU A CB    
1103 C  CG    . GLU A 165 ? 0.2496 0.3488 0.2706 -0.0466 -0.0107 0.0431  145 GLU A CG    
1104 C  CD    . GLU A 165 ? 0.3328 0.3768 0.3024 -0.0494 0.0122  0.0444  145 GLU A CD    
1105 O  OE1   . GLU A 165 ? 0.3450 0.3766 0.3237 -0.0536 0.0216  0.0391  145 GLU A OE1   
1106 O  OE2   . GLU A 165 ? 0.3807 0.4019 0.3138 -0.0485 0.0211  0.0422  145 GLU A OE2   
1107 N  N     . LYS A 166 ? 0.1662 0.2741 0.1771 -0.0538 -0.0436 0.0259  146 LYS A N     
1108 C  CA    . LYS A 166 ? 0.1822 0.2808 0.1765 -0.0422 -0.0425 0.0309  146 LYS A CA    
1109 C  C     . LYS A 166 ? 0.1849 0.2930 0.1673 -0.0508 -0.0424 0.0263  146 LYS A C     
1110 O  O     . LYS A 166 ? 0.1881 0.3101 0.1740 -0.0342 -0.0464 0.0311  146 LYS A O     
1111 C  CB    . LYS A 166 ? 0.1813 0.2784 0.1929 -0.0273 -0.0554 0.0294  146 LYS A CB    
1112 C  CG    . LYS A 166 ? 0.2039 0.2935 0.2229 -0.0135 -0.0521 0.0355  146 LYS A CG    
1113 C  CD    . LYS A 166 ? 0.2429 0.3206 0.2527 0.0061  -0.0669 0.0425  146 LYS A CD    
1114 C  CE    . LYS A 166 ? 0.2726 0.3501 0.2785 0.0232  -0.0775 0.0466  146 LYS A CE    
1115 N  NZ    . LYS A 166 ? 0.3096 0.3763 0.3028 0.0333  -0.0721 0.0453  146 LYS A NZ    
1116 N  N     . ALA A 167 ? 0.1877 0.2858 0.1555 -0.0576 -0.0301 0.0199  147 ALA A N     
1117 C  CA    . ALA A 167 ? 0.2132 0.2908 0.1668 -0.0676 -0.0247 0.0055  147 ALA A CA    
1118 C  C     . ALA A 167 ? 0.2561 0.3219 0.1836 -0.0898 -0.0342 -0.0025 147 ALA A C     
1119 O  O     . ALA A 167 ? 0.2714 0.3386 0.1774 -0.0784 -0.0309 0.0020  147 ALA A O     
1120 C  CB    . ALA A 167 ? 0.2083 0.2775 0.1657 -0.0591 -0.0257 -0.0006 147 ALA A CB    
1121 N  N     . ASN A 168 ? 0.3005 0.3458 0.2002 -0.1177 -0.0464 -0.0123 148 ASN A N     
1122 C  CA    . ASN A 168 ? 0.3495 0.3838 0.2281 -0.1299 -0.0572 -0.0181 148 ASN A CA    
1123 C  C     . ASN A 168 ? 0.3399 0.4196 0.2508 -0.1190 -0.0755 -0.0144 148 ASN A C     
1124 O  O     . ASN A 168 ? 0.3761 0.4366 0.2566 -0.1015 -0.0928 -0.0276 148 ASN A O     
1125 C  CB    . ASN A 168 ? 0.4089 0.3947 0.2480 -0.1420 -0.0491 -0.0272 148 ASN A CB    
1126 C  CG    . ASN A 168 ? 0.4770 0.4011 0.2690 -0.1299 -0.0326 -0.0301 148 ASN A CG    
1127 O  OD1   . ASN A 168 ? 0.5152 0.4163 0.2812 -0.1014 -0.0211 -0.0315 148 ASN A OD1   
1128 N  ND2   . ASN A 168 ? 0.4981 0.3948 0.2831 -0.1398 -0.0213 -0.0301 148 ASN A ND2   
1129 N  N     . ASN A 169 ? 0.3129 0.4370 0.2638 -0.1171 -0.0668 0.0027  149 ASN A N     
1130 C  CA    . ASN A 169 ? 0.3052 0.4583 0.2853 -0.0820 -0.0636 0.0158  149 ASN A CA    
1131 C  C     . ASN A 169 ? 0.2615 0.4461 0.2666 -0.0499 -0.0811 0.0287  149 ASN A C     
1132 O  O     . ASN A 169 ? 0.2613 0.4536 0.2825 -0.0400 -0.0940 0.0304  149 ASN A O     
1133 C  CB    . ASN A 169 ? 0.3676 0.4890 0.3199 -0.0686 -0.0417 0.0235  149 ASN A CB    
1134 C  CG    . ASN A 169 ? 0.4199 0.5131 0.3452 -0.0509 -0.0287 0.0255  149 ASN A CG    
1135 O  OD1   . ASN A 169 ? 0.4293 0.5221 0.3566 -0.0509 -0.0273 0.0346  149 ASN A OD1   
1136 N  ND2   . ASN A 169 ? 0.4499 0.5260 0.3567 -0.0459 -0.0182 0.0173  149 ASN A ND2   
1137 N  N     . THR A 170 ? 0.2135 0.4271 0.2431 -0.0409 -0.0711 0.0376  150 THR A N     
1138 C  CA    . THR A 170 ? 0.2058 0.4093 0.2349 -0.0205 -0.0518 0.0461  150 THR A CA    
1139 C  C     . THR A 170 ? 0.1987 0.3989 0.2228 -0.0116 -0.0500 0.0551  150 THR A C     
1140 O  O     . THR A 170 ? 0.2038 0.4092 0.2316 0.0128  -0.0368 0.0656  150 THR A O     
1141 C  CB    . THR A 170 ? 0.2076 0.3998 0.2389 -0.0200 -0.0348 0.0460  150 THR A CB    
1142 O  OG1   . THR A 170 ? 0.2239 0.4047 0.2396 -0.0231 -0.0322 0.0470  150 THR A OG1   
1143 C  CG2   . THR A 170 ? 0.2284 0.3934 0.2492 -0.0244 -0.0212 0.0441  150 THR A CG2   
1144 N  N     . GLU A 171 ? 0.2026 0.3852 0.2062 -0.0328 -0.0634 0.0451  151 GLU A N     
1145 C  CA    . GLU A 171 ? 0.2341 0.3851 0.1938 -0.0374 -0.0614 0.0336  151 GLU A CA    
1146 C  C     . GLU A 171 ? 0.2192 0.3340 0.1759 -0.0218 -0.0540 0.0382  151 GLU A C     
1147 O  O     . GLU A 171 ? 0.2186 0.3177 0.1825 -0.0145 -0.0391 0.0330  151 GLU A O     
1148 C  CB    . GLU A 171 ? 0.2982 0.4419 0.2134 -0.0471 -0.0607 0.0221  151 GLU A CB    
1149 C  CG    . GLU A 171 ? 0.3588 0.4919 0.2387 -0.0511 -0.0519 0.0094  151 GLU A CG    
1150 C  CD    . GLU A 171 ? 0.3975 0.5365 0.2572 -0.0479 -0.0448 0.0045  151 GLU A CD    
1151 O  OE1   . GLU A 171 ? 0.4139 0.5570 0.2644 -0.0464 -0.0547 0.0032  151 GLU A OE1   
1152 O  OE2   . GLU A 171 ? 0.4147 0.5499 0.2643 -0.0482 -0.0305 -0.0016 151 GLU A OE2   
1153 N  N     . ASP A 172 ? 0.2091 0.3077 0.1597 -0.0155 -0.0496 0.0391  152 ASP A N     
1154 C  CA    . ASP A 172 ? 0.2159 0.2750 0.1632 -0.0080 -0.0331 0.0447  152 ASP A CA    
1155 C  C     . ASP A 172 ? 0.2005 0.2431 0.1502 -0.0123 -0.0137 0.0464  152 ASP A C     
1156 O  O     . ASP A 172 ? 0.1845 0.2646 0.1528 -0.0123 -0.0124 0.0399  152 ASP A O     
1157 C  CB    . ASP A 172 ? 0.2372 0.2773 0.1836 0.0053  -0.0317 0.0516  152 ASP A CB    
1158 C  CG    . ASP A 172 ? 0.2479 0.2792 0.2042 0.0119  -0.0232 0.0473  152 ASP A CG    
1159 O  OD1   . ASP A 172 ? 0.2641 0.3008 0.2267 0.0117  -0.0208 0.0365  152 ASP A OD1   
1160 O  OD2   . ASP A 172 ? 0.2526 0.2591 0.1966 0.0075  -0.0285 0.0573  152 ASP A OD2   
1161 N  N     . CYS A 173 ? 0.1780 0.2175 0.1469 -0.0128 -0.0116 0.0413  153 CYS A N     
1162 C  CA    . CYS A 173 ? 0.1727 0.1941 0.1541 -0.0026 -0.0081 0.0433  153 CYS A CA    
1163 C  C     . CYS A 173 ? 0.1697 0.1878 0.1592 0.0063  -0.0086 0.0457  153 CYS A C     
1164 O  O     . CYS A 173 ? 0.1785 0.1951 0.1490 0.0061  -0.0086 0.0350  153 CYS A O     
1165 C  CB    . CYS A 173 ? 0.1857 0.1859 0.1644 -0.0060 -0.0070 0.0311  153 CYS A CB    
1166 S  SG    . CYS A 173 ? 0.2000 0.1934 0.1783 -0.0099 -0.0069 0.0166  153 CYS A SG    
1167 N  N     . ILE A 174 ? 0.1766 0.1825 0.1649 0.0116  0.0028  0.0477  154 ILE A N     
1168 C  CA    . ILE A 174 ? 0.1962 0.1863 0.1788 0.0161  0.0006  0.0534  154 ILE A CA    
1169 C  C     . ILE A 174 ? 0.1911 0.2001 0.1751 0.0140  -0.0042 0.0605  154 ILE A C     
1170 O  O     . ILE A 174 ? 0.2034 0.1983 0.1680 0.0099  0.0038  0.0525  154 ILE A O     
1171 C  CB    . ILE A 174 ? 0.2028 0.1889 0.1920 0.0188  0.0014  0.0510  154 ILE A CB    
1172 C  CG1   . ILE A 174 ? 0.2129 0.1899 0.2044 0.0141  0.0048  0.0504  154 ILE A CG1   
1173 C  CG2   . ILE A 174 ? 0.2217 0.1967 0.2049 0.0221  -0.0014 0.0474  154 ILE A CG2   
1174 C  CD1   . ILE A 174 ? 0.2462 0.1947 0.2121 0.0155  0.0154  0.0588  154 ILE A CD1   
1175 N  N     . GLU A 175 ? 0.1895 0.2278 0.1814 0.0114  -0.0120 0.0632  155 GLU A N     
1176 C  CA    . GLU A 175 ? 0.1798 0.2520 0.1936 0.0116  -0.0185 0.0675  155 GLU A CA    
1177 C  C     . GLU A 175 ? 0.1716 0.2447 0.1732 0.0085  -0.0090 0.0584  155 GLU A C     
1178 O  O     . GLU A 175 ? 0.1756 0.2456 0.1762 0.0120  -0.0019 0.0469  155 GLU A O     
1179 C  CB    . GLU A 175 ? 0.1834 0.2941 0.2219 0.0045  -0.0206 0.0772  155 GLU A CB    
1180 C  CG    . GLU A 175 ? 0.1901 0.3436 0.2524 0.0090  -0.0258 0.0739  155 GLU A CG    
1181 C  CD    . GLU A 175 ? 0.2254 0.3982 0.2817 -0.0070 -0.0267 0.0745  155 GLU A CD    
1182 O  OE1   . GLU A 175 ? 0.2476 0.4206 0.2866 -0.0111 -0.0455 0.0745  155 GLU A OE1   
1183 O  OE2   . GLU A 175 ? 0.2314 0.4241 0.3052 -0.0042 -0.0336 0.0714  155 GLU A OE2   
1184 N  N     . LEU A 176 ? 0.1610 0.2255 0.1580 -0.0027 -0.0098 0.0511  156 LEU A N     
1185 C  CA    . LEU A 176 ? 0.1658 0.2035 0.1600 -0.0140 -0.0112 0.0414  156 LEU A CA    
1186 C  C     . LEU A 176 ? 0.1679 0.1869 0.1566 -0.0038 -0.0076 0.0393  156 LEU A C     
1187 O  O     . LEU A 176 ? 0.1735 0.1926 0.1491 -0.0146 -0.0023 0.0424  156 LEU A O     
1188 C  CB    . LEU A 176 ? 0.1855 0.1904 0.1638 -0.0177 -0.0132 0.0323  156 LEU A CB    
1189 C  CG    . LEU A 176 ? 0.2028 0.1892 0.1710 -0.0192 -0.0131 0.0283  156 LEU A CG    
1190 C  CD1   . LEU A 176 ? 0.2135 0.2050 0.1880 -0.0258 -0.0168 0.0216  156 LEU A CD1   
1191 C  CD2   . LEU A 176 ? 0.2254 0.1880 0.1799 -0.0129 -0.0155 0.0237  156 LEU A CD2   
1192 N  N     . MET A 177 ? 0.1537 0.1831 0.1516 -0.0102 -0.0034 0.0304  157 MET A N     
1193 C  CA    . MET A 177 ? 0.1604 0.1679 0.1534 -0.0107 0.0012  0.0304  157 MET A CA    
1194 C  C     . MET A 177 ? 0.1659 0.1550 0.1596 -0.0057 0.0068  0.0459  157 MET A C     
1195 O  O     . MET A 177 ? 0.1747 0.1617 0.1447 -0.0095 0.0103  0.0309  157 MET A O     
1196 C  CB    . MET A 177 ? 0.1641 0.1654 0.1557 0.0025  0.0092  0.0192  157 MET A CB    
1197 C  CG    . MET A 177 ? 0.1779 0.1611 0.1570 -0.0099 0.0053  0.0082  157 MET A CG    
1198 S  SD    . MET A 177 ? 0.1834 0.1530 0.1535 0.0048  -0.0094 0.0168  157 MET A SD    
1199 C  CE    . MET A 177 ? 0.1820 0.1571 0.1643 -0.0046 -0.0112 0.0176  157 MET A CE    
1200 N  N     . GLU A 178 ? 0.1704 0.1606 0.1695 0.0110  0.0021  0.0495  158 GLU A N     
1201 C  CA    . GLU A 178 ? 0.1870 0.1673 0.1837 0.0119  0.0076  0.0575  158 GLU A CA    
1202 C  C     . GLU A 178 ? 0.1779 0.1833 0.1762 0.0195  0.0132  0.0427  158 GLU A C     
1203 O  O     . GLU A 178 ? 0.1827 0.1970 0.1684 0.0186  0.0142  0.0371  158 GLU A O     
1204 C  CB    . GLU A 178 ? 0.2299 0.1823 0.2081 0.0243  0.0155  0.0695  158 GLU A CB    
1205 C  CG    . GLU A 178 ? 0.2733 0.2174 0.2468 0.0322  0.0150  0.0711  158 GLU A CG    
1206 C  CD    . GLU A 178 ? 0.3492 0.2629 0.2914 0.0317  -0.0013 0.0632  158 GLU A CD    
1207 O  OE1   . GLU A 178 ? 0.3751 0.2899 0.2991 0.0325  -0.0305 0.0633  158 GLU A OE1   
1208 O  OE2   . GLU A 178 ? 0.3958 0.2745 0.3163 0.0357  -0.0005 0.0605  158 GLU A OE2   
1209 N  N     . TYR A 179 ? 0.1612 0.1965 0.1723 0.0085  0.0161  0.0367  159 TYR A N     
1210 C  CA    . TYR A 179 ? 0.1598 0.1974 0.1684 0.0003  -0.0012 0.0334  159 TYR A CA    
1211 C  C     . TYR A 179 ? 0.1628 0.1815 0.1528 -0.0090 -0.0032 0.0260  159 TYR A C     
1212 O  O     . TYR A 179 ? 0.1539 0.1977 0.1619 -0.0128 0.0067  0.0256  159 TYR A O     
1213 C  CB    . TYR A 179 ? 0.1571 0.2130 0.1842 -0.0056 -0.0097 0.0329  159 TYR A CB    
1214 C  CG    . TYR A 179 ? 0.1471 0.2279 0.2005 -0.0063 -0.0158 0.0368  159 TYR A CG    
1215 C  CD1   . TYR A 179 ? 0.1751 0.2493 0.2290 -0.0125 0.0003  0.0341  159 TYR A CD1   
1216 C  CD2   . TYR A 179 ? 0.1433 0.2294 0.1954 -0.0100 -0.0177 0.0426  159 TYR A CD2   
1217 C  CE1   . TYR A 179 ? 0.1802 0.2611 0.2421 -0.0031 0.0014  0.0399  159 TYR A CE1   
1218 C  CE2   . TYR A 179 ? 0.1498 0.2415 0.2025 -0.0132 -0.0140 0.0444  159 TYR A CE2   
1219 C  CZ    . TYR A 179 ? 0.1816 0.2620 0.2336 -0.0145 -0.0001 0.0511  159 TYR A CZ    
1220 O  OH    . TYR A 179 ? 0.1907 0.2894 0.2621 -0.0276 0.0063  0.0497  159 TYR A OH    
1221 N  N     . ILE A 180 ? 0.1555 0.1685 0.1422 0.0043  0.0037  0.0320  160 ILE A N     
1222 C  CA    . ILE A 180 ? 0.1675 0.1543 0.1477 -0.0092 -0.0001 0.0280  160 ILE A CA    
1223 C  C     . ILE A 180 ? 0.1648 0.1489 0.1461 -0.0007 0.0032  0.0188  160 ILE A C     
1224 O  O     . ILE A 180 ? 0.1852 0.1561 0.1327 0.0019  0.0086  0.0284  160 ILE A O     
1225 C  CB    . ILE A 180 ? 0.1685 0.1394 0.1493 -0.0058 -0.0006 0.0236  160 ILE A CB    
1226 C  CG1   . ILE A 180 ? 0.1781 0.1333 0.1571 0.0021  0.0008  0.0198  160 ILE A CG1   
1227 C  CG2   . ILE A 180 ? 0.1745 0.1471 0.1591 -0.0016 -0.0107 0.0196  160 ILE A CG2   
1228 C  CD1   . ILE A 180 ? 0.1952 0.1392 0.1685 -0.0085 0.0010  0.0256  160 ILE A CD1   
1229 N  N     . ILE A 181 ? 0.1673 0.1513 0.1544 0.0040  0.0027  0.0249  161 ILE A N     
1230 C  CA    . ILE A 181 ? 0.1599 0.1431 0.1588 0.0053  0.0024  0.0234  161 ILE A CA    
1231 C  C     . ILE A 181 ? 0.1577 0.1566 0.1648 0.0065  0.0114  0.0230  161 ILE A C     
1232 O  O     . ILE A 181 ? 0.1668 0.1559 0.1576 -0.0053 0.0108  0.0194  161 ILE A O     
1233 C  CB    . ILE A 181 ? 0.1668 0.1516 0.1661 -0.0037 0.0071  0.0266  161 ILE A CB    
1234 C  CG1   . ILE A 181 ? 0.1757 0.1671 0.1659 -0.0074 0.0036  0.0219  161 ILE A CG1   
1235 C  CG2   . ILE A 181 ? 0.1817 0.1549 0.1775 -0.0054 0.0167  0.0256  161 ILE A CG2   
1236 C  CD1   . ILE A 181 ? 0.1889 0.1764 0.1772 -0.0067 0.0032  0.0225  161 ILE A CD1   
1237 N  N     . VAL A 182 ? 0.1566 0.1695 0.1657 0.0145  0.0145  0.0292  162 VAL A N     
1238 C  CA    . VAL A 182 ? 0.1601 0.1838 0.1742 0.0182  0.0094  0.0332  162 VAL A CA    
1239 C  C     . VAL A 182 ? 0.1431 0.1722 0.1609 0.0043  0.0101  0.0284  162 VAL A C     
1240 O  O     . VAL A 182 ? 0.1559 0.1874 0.1616 0.0133  0.0159  0.0283  162 VAL A O     
1241 C  CB    . VAL A 182 ? 0.1793 0.2256 0.1898 0.0345  0.0091  0.0437  162 VAL A CB    
1242 C  CG1   . VAL A 182 ? 0.1893 0.2567 0.2003 0.0309  0.0067  0.0348  162 VAL A CG1   
1243 C  CG2   . VAL A 182 ? 0.2152 0.2355 0.2017 0.0491  0.0164  0.0513  162 VAL A CG2   
1244 N  N     . LYS A 183 ? 0.1664 0.1609 0.1584 -0.0049 0.0070  0.0233  163 LYS A N     
1245 C  CA    . LYS A 183 ? 0.1547 0.1641 0.1584 -0.0136 0.0006  0.0225  163 LYS A CA    
1246 C  C     . LYS A 183 ? 0.1523 0.1661 0.1454 -0.0045 0.0029  0.0150  163 LYS A C     
1247 O  O     . LYS A 183 ? 0.1753 0.1705 0.1411 -0.0198 0.0056  0.0220  163 LYS A O     
1248 C  CB    . LYS A 183 ? 0.1504 0.1824 0.1867 -0.0182 -0.0101 0.0066  163 LYS A CB    
1249 C  CG    . LYS A 183 ? 0.1733 0.2276 0.2261 -0.0035 -0.0104 -0.0084 163 LYS A CG    
1250 C  CD    . LYS A 183 ? 0.1991 0.2881 0.2709 -0.0047 -0.0027 -0.0249 163 LYS A CD    
1251 C  CE    . LYS A 183 ? 0.2219 0.3233 0.3055 -0.0096 0.0018  -0.0218 163 LYS A CE    
1252 N  NZ    . LYS A 183 ? 0.2380 0.3445 0.3250 -0.0101 0.0070  -0.0204 163 LYS A NZ    
1253 N  N     . ALA A 184 ? 0.1429 0.1465 0.1488 0.0013  0.0004  0.0114  164 ALA A N     
1254 C  CA    . ALA A 184 ? 0.1534 0.1312 0.1538 0.0058  0.0028  0.0109  164 ALA A CA    
1255 C  C     . ALA A 184 ? 0.1500 0.1330 0.1500 0.0014  0.0083  0.0098  164 ALA A C     
1256 O  O     . ALA A 184 ? 0.1477 0.1509 0.1408 0.0056  0.0120  0.0149  164 ALA A O     
1257 C  CB    . ALA A 184 ? 0.1500 0.1409 0.1557 0.0073  -0.0033 0.0078  164 ALA A CB    
1258 N  N     . ASN A 185 ? 0.1567 0.1266 0.1551 0.0012  0.0074  0.0095  165 ASN A N     
1259 C  CA    . ASN A 185 ? 0.1679 0.1266 0.1718 -0.0003 0.0148  0.0160  165 ASN A CA    
1260 C  C     . ASN A 185 ? 0.1476 0.1375 0.1631 0.0025  0.0122  0.0184  165 ASN A C     
1261 O  O     . ASN A 185 ? 0.1743 0.1411 0.1541 0.0087  0.0197  0.0076  165 ASN A O     
1262 C  CB    . ASN A 185 ? 0.2182 0.1364 0.1908 -0.0061 0.0149  0.0098  165 ASN A CB    
1263 C  CG    . ASN A 185 ? 0.2672 0.1938 0.2250 -0.0040 0.0206  0.0105  165 ASN A CG    
1264 O  OD1   . ASN A 185 ? 0.2694 0.2204 0.2493 -0.0093 0.0194  0.0009  165 ASN A OD1   
1265 N  ND2   . ASN A 185 ? 0.3219 0.2147 0.2387 -0.0027 0.0254  0.0185  165 ASN A ND2   
1266 N  N     . GLU A 186 ? 0.1452 0.1561 0.1591 0.0032  0.0045  0.0155  166 GLU A N     
1267 C  CA    . GLU A 186 ? 0.1380 0.1727 0.1602 0.0000  0.0122  0.0137  166 GLU A CA    
1268 C  C     . GLU A 186 ? 0.1380 0.1491 0.1536 -0.0005 0.0110  0.0115  166 GLU A C     
1269 O  O     . GLU A 186 ? 0.1459 0.1579 0.1627 0.0149  0.0196  0.0155  166 GLU A O     
1270 C  CB    . GLU A 186 ? 0.1379 0.2056 0.1799 0.0198  -0.0035 0.0263  166 GLU A CB    
1271 C  CG    . GLU A 186 ? 0.1642 0.2438 0.2056 0.0229  0.0031  0.0391  166 GLU A CG    
1272 C  CD    . GLU A 186 ? 0.2160 0.2876 0.2395 0.0275  -0.0235 0.0422  166 GLU A CD    
1273 O  OE1   . GLU A 186 ? 0.2283 0.3078 0.2502 0.0102  -0.0432 0.0292  166 GLU A OE1   
1274 O  OE2   . GLU A 186 ? 0.2642 0.3168 0.2674 0.0362  -0.0438 0.0425  166 GLU A OE2   
1275 N  N     . SER A 187 ? 0.1404 0.1399 0.1414 -0.0072 0.0138  0.0138  167 SER A N     
1276 C  CA    . SER A 187 ? 0.1416 0.1270 0.1515 -0.0100 0.0033  0.0075  167 SER A CA    
1277 C  C     . SER A 187 ? 0.1409 0.1147 0.1442 -0.0058 0.0084  0.0036  167 SER A C     
1278 O  O     . SER A 187 ? 0.1485 0.1253 0.1438 -0.0142 0.0058  0.0088  167 SER A O     
1279 C  CB    . SER A 187 ? 0.1648 0.1283 0.1556 -0.0090 -0.0023 0.0063  167 SER A CB    
1280 O  OG    . SER A 187 ? 0.1713 0.1312 0.1518 -0.0041 -0.0040 0.0091  167 SER A OG    
1281 N  N     . LEU A 188 ? 0.1481 0.1241 0.1361 -0.0110 0.0079  0.0107  168 LEU A N     
1282 C  CA    . LEU A 188 ? 0.1465 0.1211 0.1417 -0.0110 0.0063  0.0076  168 LEU A CA    
1283 C  C     . LEU A 188 ? 0.1339 0.1224 0.1380 -0.0145 0.0099  0.0028  168 LEU A C     
1284 O  O     . LEU A 188 ? 0.1456 0.1306 0.1388 -0.0043 0.0112  -0.0011 168 LEU A O     
1285 C  CB    . LEU A 188 ? 0.1458 0.1304 0.1440 -0.0040 0.0081  0.0115  168 LEU A CB    
1286 C  CG    . LEU A 188 ? 0.1655 0.1326 0.1575 -0.0241 0.0167  0.0034  168 LEU A CG    
1287 C  CD1   . LEU A 188 ? 0.1590 0.1424 0.1579 -0.0118 0.0088  -0.0081 168 LEU A CD1   
1288 C  CD2   . LEU A 188 ? 0.2021 0.1476 0.1621 -0.0389 0.0150  0.0019  168 LEU A CD2   
1289 N  N     . GLU A 189 ? 0.1459 0.1381 0.1414 0.0038  0.0101  0.0079  169 GLU A N     
1290 C  CA    . GLU A 189 ? 0.1620 0.1505 0.1542 0.0169  0.0204  0.0043  169 GLU A CA    
1291 C  C     . GLU A 189 ? 0.1525 0.1708 0.1519 0.0089  0.0173  0.0023  169 GLU A C     
1292 O  O     . GLU A 189 ? 0.1869 0.1860 0.1649 0.0167  0.0279  -0.0094 169 GLU A O     
1293 C  CB    . GLU A 189 ? 0.1912 0.1592 0.1830 0.0334  0.0184  0.0102  169 GLU A CB    
1294 C  CG    . GLU A 189 ? 0.2699 0.1853 0.2159 0.0346  0.0131  0.0220  169 GLU A CG    
1295 C  CD    . GLU A 189 ? 0.3684 0.2484 0.2662 0.0125  0.0137  0.0265  169 GLU A CD    
1296 O  OE1   . GLU A 189 ? 0.4153 0.2652 0.2930 0.0209  0.0084  0.0182  169 GLU A OE1   
1297 O  OE2   . GLU A 189 ? 0.4211 0.2857 0.2952 -0.0016 0.0047  0.0276  169 GLU A OE2   
1298 N  N     . ASN A 190 ? 0.1427 0.1654 0.1428 -0.0101 0.0136  0.0076  170 ASN A N     
1299 C  CA    . ASN A 190 ? 0.1466 0.1738 0.1481 -0.0221 0.0011  0.0092  170 ASN A CA    
1300 C  C     . ASN A 190 ? 0.1428 0.1548 0.1403 -0.0209 0.0024  0.0100  170 ASN A C     
1301 O  O     . ASN A 190 ? 0.1528 0.1675 0.1410 -0.0333 -0.0011 0.0106  170 ASN A O     
1302 C  CB    . ASN A 190 ? 0.1627 0.1990 0.1580 -0.0422 -0.0086 0.0183  170 ASN A CB    
1303 C  CG    . ASN A 190 ? 0.1670 0.2208 0.1645 -0.0389 -0.0059 0.0238  170 ASN A CG    
1304 O  OD1   . ASN A 190 ? 0.1738 0.2468 0.1739 -0.0483 0.0092  0.0104  170 ASN A OD1   
1305 N  ND2   . ASN A 190 ? 0.1706 0.2268 0.1781 -0.0333 0.0055  0.0436  170 ASN A ND2   
1306 N  N     . THR A 191 ? 0.1399 0.1412 0.1357 -0.0130 0.0050  0.0091  171 THR A N     
1307 C  CA    . THR A 191 ? 0.1403 0.1293 0.1369 -0.0129 -0.0020 0.0070  171 THR A CA    
1308 C  C     . THR A 191 ? 0.1366 0.1347 0.1472 -0.0178 0.0008  0.0062  171 THR A C     
1309 O  O     . THR A 191 ? 0.1469 0.1377 0.1425 -0.0177 0.0057  0.0114  171 THR A O     
1310 C  CB    . THR A 191 ? 0.1474 0.1256 0.1338 -0.0093 0.0035  0.0078  171 THR A CB    
1311 O  OG1   . THR A 191 ? 0.1460 0.1278 0.1451 -0.0127 0.0023  0.0139  171 THR A OG1   
1312 C  CG2   . THR A 191 ? 0.1592 0.1360 0.1319 -0.0049 -0.0029 0.0116  171 THR A CG2   
1313 N  N     . PRO A 192 ? 0.1539 0.1359 0.1430 -0.0195 0.0029  0.0011  172 PRO A N     
1314 C  CA    . PRO A 192 ? 0.1662 0.1449 0.1437 -0.0220 0.0059  -0.0063 172 PRO A CA    
1315 C  C     . PRO A 192 ? 0.1507 0.1427 0.1419 -0.0206 0.0115  -0.0056 172 PRO A C     
1316 O  O     . PRO A 192 ? 0.1706 0.1737 0.1410 -0.0432 0.0124  -0.0027 172 PRO A O     
1317 C  CB    . PRO A 192 ? 0.1996 0.1483 0.1535 -0.0266 0.0073  -0.0042 172 PRO A CB    
1318 C  CG    . PRO A 192 ? 0.2083 0.1507 0.1599 -0.0159 0.0083  -0.0024 172 PRO A CG    
1319 C  CD    . PRO A 192 ? 0.1728 0.1387 0.1565 -0.0120 0.0122  -0.0045 172 PRO A CD    
1320 N  N     . ASN A 193 ? 0.1420 0.1412 0.1466 -0.0224 0.0026  0.0007  173 ASN A N     
1321 C  CA    . ASN A 193 ? 0.1358 0.1453 0.1482 -0.0141 0.0081  0.0056  173 ASN A CA    
1322 C  C     . ASN A 193 ? 0.1357 0.1459 0.1459 -0.0177 0.0067  0.0109  173 ASN A C     
1323 O  O     . ASN A 193 ? 0.1452 0.1531 0.1712 -0.0186 0.0129  0.0198  173 ASN A O     
1324 C  CB    . ASN A 193 ? 0.1486 0.1498 0.1659 -0.0066 -0.0021 0.0075  173 ASN A CB    
1325 C  CG    . ASN A 193 ? 0.1702 0.1721 0.1852 -0.0005 -0.0016 -0.0032 173 ASN A CG    
1326 O  OD1   . ASN A 193 ? 0.1871 0.1890 0.2021 0.0135  0.0049  -0.0129 173 ASN A OD1   
1327 N  ND2   . ASN A 193 ? 0.1954 0.1784 0.1943 0.0014  -0.0129 0.0043  173 ASN A ND2   
1328 N  N     . LEU A 194 ? 0.1398 0.1367 0.1412 -0.0171 0.0046  0.0032  174 LEU A N     
1329 C  CA    . LEU A 194 ? 0.1355 0.1398 0.1411 -0.0181 0.0037  0.0082  174 LEU A CA    
1330 C  C     . LEU A 194 ? 0.1418 0.1310 0.1443 -0.0327 0.0000  0.0079  174 LEU A C     
1331 O  O     . LEU A 194 ? 0.1470 0.1349 0.1437 -0.0250 -0.0077 0.0097  174 LEU A O     
1332 C  CB    . LEU A 194 ? 0.1350 0.1516 0.1369 -0.0219 0.0021  0.0063  174 LEU A CB    
1333 C  CG    . LEU A 194 ? 0.1413 0.1624 0.1388 -0.0098 0.0009  0.0028  174 LEU A CG    
1334 C  CD1   . LEU A 194 ? 0.1689 0.1743 0.1421 -0.0163 0.0013  0.0040  174 LEU A CD1   
1335 C  CD2   . LEU A 194 ? 0.1429 0.1674 0.1458 -0.0177 -0.0087 -0.0039 174 LEU A CD2   
1336 N  N     . LEU A 195 ? 0.1609 0.1328 0.1600 -0.0263 -0.0153 0.0178  175 LEU A N     
1337 C  CA    . LEU A 195 ? 0.1680 0.1395 0.1735 -0.0282 -0.0222 0.0130  175 LEU A CA    
1338 C  C     . LEU A 195 ? 0.1805 0.1492 0.1809 -0.0275 -0.0263 0.0083  175 LEU A C     
1339 O  O     . LEU A 195 ? 0.2034 0.1418 0.1795 -0.0242 -0.0302 0.0005  175 LEU A O     
1340 C  CB    . LEU A 195 ? 0.1602 0.1628 0.1782 -0.0294 -0.0140 0.0215  175 LEU A CB    
1341 C  CG    . LEU A 195 ? 0.1710 0.1775 0.1726 -0.0154 0.0007  0.0151  175 LEU A CG    
1342 C  CD1   . LEU A 195 ? 0.1906 0.1877 0.1777 -0.0119 0.0094  0.0263  175 LEU A CD1   
1343 C  CD2   . LEU A 195 ? 0.1710 0.1850 0.1784 -0.0215 0.0133  0.0139  175 LEU A CD2   
1344 N  N     . ALA A 196 ? 0.1766 0.1577 0.1778 -0.0317 -0.0020 -0.0002 176 ALA A N     
1345 C  CA    . ALA A 196 ? 0.1753 0.1828 0.1812 -0.0401 0.0038  -0.0049 176 ALA A CA    
1346 C  C     . ALA A 196 ? 0.1619 0.1730 0.1685 -0.0316 0.0113  -0.0093 176 ALA A C     
1347 O  O     . ALA A 196 ? 0.1796 0.1781 0.1775 -0.0202 0.0127  -0.0155 176 ALA A O     
1348 C  CB    . ALA A 196 ? 0.2064 0.1968 0.1903 -0.0418 0.0216  -0.0073 176 ALA A CB    
1349 N  N     . VAL A 197 ? 0.1528 0.1629 0.1470 -0.0280 0.0041  -0.0103 177 VAL A N     
1350 C  CA    . VAL A 197 ? 0.1599 0.1612 0.1421 -0.0210 0.0038  -0.0063 177 VAL A CA    
1351 C  C     . VAL A 197 ? 0.1744 0.1468 0.1409 -0.0147 0.0072  -0.0177 177 VAL A C     
1352 O  O     . VAL A 197 ? 0.1836 0.1548 0.1396 -0.0275 0.0097  -0.0163 177 VAL A O     
1353 C  CB    . VAL A 197 ? 0.1833 0.1774 0.1616 -0.0183 -0.0106 -0.0059 177 VAL A CB    
1354 C  CG1   . VAL A 197 ? 0.1888 0.1875 0.1650 -0.0125 0.0110  -0.0030 177 VAL A CG1   
1355 C  CG2   . VAL A 197 ? 0.2058 0.1999 0.1891 -0.0066 -0.0146 -0.0123 177 VAL A CG2   
1356 N  N     . LEU A 198 ? 0.1693 0.1471 0.1361 -0.0173 0.0042  -0.0111 178 LEU A N     
1357 C  CA    . LEU A 198 ? 0.1703 0.1484 0.1388 -0.0069 0.0111  -0.0094 178 LEU A CA    
1358 C  C     . LEU A 198 ? 0.1846 0.1590 0.1400 -0.0073 0.0118  -0.0205 178 LEU A C     
1359 O  O     . LEU A 198 ? 0.2007 0.1607 0.1450 0.0053  0.0241  -0.0255 178 LEU A O     
1360 C  CB    . LEU A 198 ? 0.1641 0.1544 0.1332 -0.0002 0.0130  -0.0090 178 LEU A CB    
1361 C  CG    . LEU A 198 ? 0.1566 0.1479 0.1352 -0.0009 0.0115  0.0021  178 LEU A CG    
1362 C  CD1   . LEU A 198 ? 0.1661 0.1460 0.1346 -0.0030 0.0104  0.0009  178 LEU A CD1   
1363 C  CD2   . LEU A 198 ? 0.1585 0.1678 0.1600 -0.0055 0.0149  0.0022  178 LEU A CD2   
1364 N  N     . LYS A 199 ? 0.1746 0.1719 0.1391 -0.0080 0.0015  -0.0161 179 LYS A N     
1365 C  CA    . LYS A 199 ? 0.1764 0.1913 0.1637 -0.0057 0.0052  -0.0339 179 LYS A CA    
1366 C  C     . LYS A 199 ? 0.1859 0.1850 0.1571 -0.0036 0.0118  -0.0421 179 LYS A C     
1367 O  O     . LYS A 199 ? 0.2018 0.1905 0.1732 -0.0016 0.0130  -0.0434 179 LYS A O     
1368 C  CB    . LYS A 199 ? 0.1714 0.2249 0.2047 -0.0084 0.0038  -0.0472 179 LYS A CB    
1369 C  CG    . LYS A 199 ? 0.2035 0.2769 0.2460 -0.0110 0.0061  -0.0498 179 LYS A CG    
1370 C  CD    . LYS A 199 ? 0.2639 0.3296 0.2786 -0.0188 0.0155  -0.0491 179 LYS A CD    
1371 C  CE    . LYS A 199 ? 0.3083 0.3675 0.2997 -0.0344 0.0171  -0.0429 179 LYS A CE    
1372 N  NZ    . LYS A 199 ? 0.3281 0.3861 0.3087 -0.0472 0.0253  -0.0360 179 LYS A NZ    
1373 N  N     . GLU A 200 ? 0.1798 0.1919 0.1423 -0.0147 -0.0034 -0.0361 180 GLU A N     
1374 C  CA    . GLU A 200 ? 0.2025 0.2053 0.1472 -0.0318 -0.0009 -0.0333 180 GLU A CA    
1375 C  C     . GLU A 200 ? 0.1861 0.1963 0.1562 -0.0210 0.0040  -0.0403 180 GLU A C     
1376 O  O     . GLU A 200 ? 0.1845 0.2064 0.1684 -0.0174 0.0022  -0.0506 180 GLU A O     
1377 C  CB    . GLU A 200 ? 0.2539 0.2392 0.1670 -0.0535 -0.0199 -0.0104 180 GLU A CB    
1378 C  CG    . GLU A 200 ? 0.3057 0.2815 0.1912 -0.0673 -0.0236 0.0153  180 GLU A CG    
1379 C  CD    . GLU A 200 ? 0.3442 0.3366 0.2341 -0.0735 -0.0185 0.0289  180 GLU A CD    
1380 O  OE1   . GLU A 200 ? 0.3750 0.3679 0.2535 -0.0622 -0.0035 0.0247  180 GLU A OE1   
1381 O  OE2   . GLU A 200 ? 0.3620 0.3494 0.2456 -0.0732 -0.0243 0.0504  180 GLU A OE2   
1382 N  N     . VAL A 201 ? 0.1848 0.1816 0.1588 -0.0216 0.0096  -0.0267 181 VAL A N     
1383 C  CA    . VAL A 201 ? 0.1999 0.1750 0.1776 -0.0079 -0.0051 -0.0252 181 VAL A CA    
1384 C  C     . VAL A 201 ? 0.2063 0.1641 0.1817 -0.0101 0.0018  -0.0218 181 VAL A C     
1385 O  O     . VAL A 201 ? 0.2622 0.1796 0.2116 0.0009  -0.0197 -0.0107 181 VAL A O     
1386 C  CB    . VAL A 201 ? 0.1977 0.1673 0.1849 -0.0100 -0.0005 -0.0152 181 VAL A CB    
1387 C  CG1   . VAL A 201 ? 0.2134 0.1801 0.2056 -0.0090 0.0064  -0.0129 181 VAL A CG1   
1388 C  CG2   . VAL A 201 ? 0.1781 0.1753 0.1846 -0.0065 -0.0162 -0.0218 181 VAL A CG2   
1389 N  N     . GLY A 202 ? 0.2001 0.1766 0.1726 0.0070  0.0095  -0.0133 182 GLY A N     
1390 C  CA    . GLY A 202 ? 0.2097 0.1857 0.1764 0.0019  0.0079  -0.0124 182 GLY A CA    
1391 C  C     . GLY A 202 ? 0.2286 0.1690 0.1742 0.0057  0.0117  -0.0081 182 GLY A C     
1392 O  O     . GLY A 202 ? 0.2760 0.1875 0.1911 0.0328  0.0278  -0.0065 182 GLY A O     
1393 N  N     . VAL A 203 ? 0.2013 0.1535 0.1632 0.0057  0.0252  -0.0161 183 VAL A N     
1394 C  CA    . VAL A 203 ? 0.1968 0.1442 0.1622 -0.0130 0.0118  -0.0222 183 VAL A CA    
1395 C  C     . VAL A 203 ? 0.1889 0.1404 0.1563 -0.0237 0.0139  -0.0179 183 VAL A C     
1396 O  O     . VAL A 203 ? 0.2325 0.1569 0.1596 -0.0460 0.0096  -0.0155 183 VAL A O     
1397 C  CB    . VAL A 203 ? 0.2052 0.1586 0.1691 -0.0295 0.0107  -0.0267 183 VAL A CB    
1398 C  CG1   . VAL A 203 ? 0.2387 0.1609 0.1760 -0.0432 0.0071  -0.0358 183 VAL A CG1   
1399 C  CG2   . VAL A 203 ? 0.1964 0.1736 0.1785 -0.0110 0.0086  -0.0229 183 VAL A CG2   
1400 N  N     . VAL A 204 ? 0.1788 0.1250 0.1535 -0.0087 0.0148  -0.0058 184 VAL A N     
1401 C  CA    . VAL A 204 ? 0.1555 0.1310 0.1527 -0.0114 0.0135  -0.0113 184 VAL A CA    
1402 C  C     . VAL A 204 ? 0.1422 0.1369 0.1483 -0.0146 0.0051  -0.0036 184 VAL A C     
1403 O  O     . VAL A 204 ? 0.1618 0.1436 0.1628 -0.0180 0.0017  -0.0105 184 VAL A O     
1404 C  CB    . VAL A 204 ? 0.1702 0.1350 0.1629 -0.0087 -0.0029 -0.0113 184 VAL A CB    
1405 C  CG1   . VAL A 204 ? 0.1783 0.1466 0.1809 0.0098  -0.0080 -0.0075 184 VAL A CG1   
1406 C  CG2   . VAL A 204 ? 0.1960 0.1433 0.1595 -0.0150 -0.0020 -0.0013 184 VAL A CG2   
1407 N  N     . ASP A 205 ? 0.1421 0.1289 0.1392 -0.0048 0.0115  -0.0104 185 ASP A N     
1408 C  CA    . ASP A 205 ? 0.1445 0.1394 0.1349 -0.0110 0.0084  -0.0103 185 ASP A CA    
1409 C  C     . ASP A 205 ? 0.1410 0.1375 0.1407 -0.0231 0.0141  -0.0080 185 ASP A C     
1410 O  O     . ASP A 205 ? 0.1466 0.1414 0.1324 -0.0118 0.0052  -0.0008 185 ASP A O     
1411 C  CB    . ASP A 205 ? 0.1309 0.1401 0.1387 -0.0079 0.0144  -0.0064 185 ASP A CB    
1412 C  CG    . ASP A 205 ? 0.1517 0.1437 0.1322 -0.0076 0.0167  0.0036  185 ASP A CG    
1413 O  OD1   . ASP A 205 ? 0.1614 0.1610 0.1398 -0.0047 0.0124  0.0092  185 ASP A OD1   
1414 O  OD2   . ASP A 205 ? 0.1581 0.1392 0.1333 -0.0051 0.0135  0.0011  185 ASP A OD2   
1415 N  N     . SER A 206 ? 0.1365 0.1363 0.1382 -0.0159 0.0087  -0.0043 186 SER A N     
1416 C  CA    A SER A 206 ? 0.1384 0.1249 0.1288 -0.0154 0.0032  -0.0113 186 SER A CA    
1417 C  CA    B SER A 206 ? 0.1598 0.1447 0.1468 -0.0139 0.0033  -0.0127 186 SER A CA    
1418 C  C     . SER A 206 ? 0.1388 0.1294 0.1289 -0.0178 0.0052  -0.0153 186 SER A C     
1419 O  O     . SER A 206 ? 0.1601 0.1281 0.1336 -0.0242 0.0128  -0.0045 186 SER A O     
1420 C  CB    A SER A 206 ? 0.1349 0.1203 0.1203 -0.0192 0.0026  -0.0155 186 SER A CB    
1421 C  CB    B SER A 206 ? 0.2015 0.1778 0.1721 -0.0118 0.0011  -0.0202 186 SER A CB    
1422 O  OG    A SER A 206 ? 0.1138 0.1220 0.1067 -0.0197 -0.0065 -0.0093 186 SER A OG    
1423 O  OG    B SER A 206 ? 0.2380 0.2071 0.1911 -0.0045 -0.0083 -0.0203 186 SER A OG    
1424 N  N     . GLY A 207 ? 0.1474 0.1262 0.1245 -0.0206 0.0113  -0.0101 187 GLY A N     
1425 C  CA    . GLY A 207 ? 0.1385 0.1242 0.1217 -0.0097 0.0009  -0.0093 187 GLY A CA    
1426 C  C     . GLY A 207 ? 0.1414 0.1139 0.1187 -0.0106 -0.0071 -0.0051 187 GLY A C     
1427 O  O     . GLY A 207 ? 0.1479 0.1294 0.1180 -0.0157 0.0071  -0.0016 187 GLY A O     
1428 N  N     . GLY A 208 ? 0.1346 0.1232 0.1215 -0.0080 0.0078  -0.0048 188 GLY A N     
1429 C  CA    . GLY A 208 ? 0.1357 0.1307 0.1325 -0.0160 0.0059  -0.0100 188 GLY A CA    
1430 C  C     . GLY A 208 ? 0.1308 0.1237 0.1357 -0.0117 0.0103  -0.0069 188 GLY A C     
1431 O  O     . GLY A 208 ? 0.1451 0.1257 0.1300 -0.0160 0.0084  -0.0003 188 GLY A O     
1432 N  N     . LYS A 209 ? 0.1488 0.1159 0.1384 -0.0154 0.0107  0.0022  189 LYS A N     
1433 C  CA    . LYS A 209 ? 0.1558 0.1176 0.1486 -0.0234 0.0153  -0.0061 189 LYS A CA    
1434 C  C     . LYS A 209 ? 0.1515 0.1203 0.1401 -0.0128 0.0137  -0.0038 189 LYS A C     
1435 O  O     . LYS A 209 ? 0.1639 0.1205 0.1412 -0.0116 0.0178  0.0088  189 LYS A O     
1436 C  CB    . LYS A 209 ? 0.1603 0.1211 0.1642 -0.0174 0.0134  -0.0098 189 LYS A CB    
1437 C  CG    . LYS A 209 ? 0.1958 0.1332 0.2008 -0.0021 0.0075  -0.0064 189 LYS A CG    
1438 C  CD    . LYS A 209 ? 0.2749 0.1506 0.2549 0.0073  -0.0225 -0.0093 189 LYS A CD    
1439 C  CE    . LYS A 209 ? 0.3462 0.1921 0.2913 0.0135  -0.0507 -0.0078 189 LYS A CE    
1440 N  NZ    . LYS A 209 ? 0.3840 0.2110 0.3150 0.0358  -0.0694 -0.0127 189 LYS A NZ    
1441 N  N     . GLY A 210 ? 0.1470 0.1157 0.1349 -0.0161 0.0150  -0.0038 190 GLY A N     
1442 C  CA    . GLY A 210 ? 0.1401 0.1225 0.1414 -0.0124 0.0151  -0.0026 190 GLY A CA    
1443 C  C     . GLY A 210 ? 0.1363 0.1155 0.1314 -0.0145 0.0097  0.0013  190 GLY A C     
1444 O  O     . GLY A 210 ? 0.1549 0.1253 0.1287 -0.0226 0.0159  0.0027  190 GLY A O     
1445 N  N     . LEU A 211 ? 0.1468 0.1105 0.1276 -0.0158 0.0094  0.0017  191 LEU A N     
1446 C  CA    . LEU A 211 ? 0.1481 0.1069 0.1322 -0.0145 0.0041  -0.0034 191 LEU A CA    
1447 C  C     . LEU A 211 ? 0.1482 0.1100 0.1321 -0.0189 0.0066  -0.0010 191 LEU A C     
1448 O  O     . LEU A 211 ? 0.1692 0.1123 0.1317 -0.0117 0.0081  0.0055  191 LEU A O     
1449 C  CB    . LEU A 211 ? 0.1561 0.1100 0.1308 -0.0099 0.0061  -0.0015 191 LEU A CB    
1450 C  CG    . LEU A 211 ? 0.1674 0.1085 0.1363 -0.0211 -0.0049 -0.0005 191 LEU A CG    
1451 C  CD1   . LEU A 211 ? 0.1776 0.1209 0.1526 -0.0114 0.0070  -0.0133 191 LEU A CD1   
1452 C  CD2   . LEU A 211 ? 0.1897 0.1187 0.1406 -0.0314 -0.0018 0.0063  191 LEU A CD2   
1453 N  N     . LEU A 212 ? 0.1469 0.1198 0.1354 -0.0116 0.0072  0.0028  192 LEU A N     
1454 C  CA    . LEU A 212 ? 0.1388 0.1393 0.1504 -0.0142 0.0131  0.0034  192 LEU A CA    
1455 C  C     . LEU A 212 ? 0.1499 0.1238 0.1465 -0.0043 0.0183  0.0059  192 LEU A C     
1456 O  O     . LEU A 212 ? 0.1596 0.1376 0.1390 0.0041  0.0104  0.0187  192 LEU A O     
1457 C  CB    . LEU A 212 ? 0.1515 0.1647 0.1674 -0.0095 0.0139  0.0061  192 LEU A CB    
1458 C  CG    . LEU A 212 ? 0.1902 0.1741 0.1948 -0.0029 0.0016  0.0048  192 LEU A CG    
1459 C  CD1   . LEU A 212 ? 0.1835 0.1682 0.1979 -0.0012 -0.0190 0.0031  192 LEU A CD1   
1460 C  CD2   . LEU A 212 ? 0.1958 0.1787 0.2097 -0.0217 0.0078  0.0096  192 LEU A CD2   
1461 N  N     . CYS A 213 ? 0.1729 0.1147 0.1456 -0.0088 0.0125  0.0099  193 CYS A N     
1462 C  CA    . CYS A 213 ? 0.1998 0.1149 0.1448 -0.0229 0.0098  0.0052  193 CYS A CA    
1463 C  C     . CYS A 213 ? 0.1751 0.1075 0.1409 -0.0163 0.0143  0.0089  193 CYS A C     
1464 O  O     . CYS A 213 ? 0.1740 0.1213 0.1482 -0.0074 0.0146  0.0190  193 CYS A O     
1465 C  CB    . CYS A 213 ? 0.2427 0.1291 0.1569 -0.0446 0.0160  -0.0020 193 CYS A CB    
1466 S  SG    . CYS A 213 ? 0.3204 0.1421 0.1760 -0.0582 0.0358  -0.0142 193 CYS A SG    
1467 N  N     . VAL A 214 ? 0.1616 0.1080 0.1314 -0.0186 0.0098  0.0079  194 VAL A N     
1468 C  CA    . VAL A 214 ? 0.1544 0.1197 0.1334 -0.0140 0.0098  0.0122  194 VAL A CA    
1469 C  C     . VAL A 214 ? 0.1499 0.1192 0.1364 -0.0090 0.0149  0.0056  194 VAL A C     
1470 O  O     . VAL A 214 ? 0.1605 0.1218 0.1391 0.0001  0.0174  0.0184  194 VAL A O     
1471 C  CB    . VAL A 214 ? 0.1502 0.1286 0.1398 -0.0074 0.0073  0.0112  194 VAL A CB    
1472 C  CG1   . VAL A 214 ? 0.1676 0.1418 0.1441 0.0006  0.0140  0.0109  194 VAL A CG1   
1473 C  CG2   . VAL A 214 ? 0.1598 0.1370 0.1497 -0.0093 0.0018  0.0039  194 VAL A CG2   
1474 N  N     . TYR A 215 ? 0.1466 0.1138 0.1294 -0.0032 0.0095  0.0066  195 TYR A N     
1475 C  CA    . TYR A 215 ? 0.1506 0.1150 0.1381 -0.0088 0.0060  0.0045  195 TYR A CA    
1476 C  C     . TYR A 215 ? 0.1573 0.1187 0.1379 -0.0063 0.0128  0.0151  195 TYR A C     
1477 O  O     . TYR A 215 ? 0.1644 0.1287 0.1371 -0.0007 0.0059  0.0212  195 TYR A O     
1478 C  CB    . TYR A 215 ? 0.1456 0.1217 0.1368 -0.0066 0.0024  0.0112  195 TYR A CB    
1479 C  CG    . TYR A 215 ? 0.1586 0.1254 0.1445 -0.0234 0.0056  0.0116  195 TYR A CG    
1480 C  CD1   . TYR A 215 ? 0.1737 0.1146 0.1495 -0.0144 0.0081  0.0121  195 TYR A CD1   
1481 C  CD2   . TYR A 215 ? 0.1561 0.1341 0.1705 -0.0260 -0.0059 0.0086  195 TYR A CD2   
1482 C  CE1   . TYR A 215 ? 0.1853 0.1205 0.1609 -0.0100 0.0022  0.0032  195 TYR A CE1   
1483 C  CE2   . TYR A 215 ? 0.1756 0.1383 0.1766 -0.0350 -0.0177 0.0145  195 TYR A CE2   
1484 C  CZ    . TYR A 215 ? 0.2010 0.1155 0.1634 -0.0250 -0.0136 0.0056  195 TYR A CZ    
1485 O  OH    . TYR A 215 ? 0.2317 0.1160 0.1704 -0.0329 -0.0305 0.0069  195 TYR A OH    
1486 N  N     . GLU A 216 ? 0.1626 0.1153 0.1427 0.0040  0.0169  0.0133  196 GLU A N     
1487 C  CA    . GLU A 216 ? 0.1828 0.1179 0.1604 0.0137  0.0210  0.0117  196 GLU A CA    
1488 C  C     . GLU A 216 ? 0.1836 0.1225 0.1581 0.0077  0.0137  0.0192  196 GLU A C     
1489 O  O     . GLU A 216 ? 0.1941 0.1325 0.1595 0.0227  0.0130  0.0317  196 GLU A O     
1490 C  CB    . GLU A 216 ? 0.2295 0.1413 0.1865 0.0304  0.0352  0.0074  196 GLU A CB    
1491 C  CG    . GLU A 216 ? 0.2946 0.1984 0.2148 0.0680  0.0526  0.0073  196 GLU A CG    
1492 C  CD    . GLU A 216 ? 0.4161 0.2780 0.2628 0.0597  0.0522  -0.0126 196 GLU A CD    
1493 O  OE1   . GLU A 216 ? 0.4711 0.2987 0.2831 0.0537  0.0496  -0.0227 196 GLU A OE1   
1494 O  OE2   . GLU A 216 ? 0.4773 0.3223 0.2828 0.0686  0.0510  -0.0170 196 GLU A OE2   
1495 N  N     . GLY A 217 ? 0.1718 0.1122 0.1526 -0.0017 0.0142  0.0150  197 GLY A N     
1496 C  CA    . GLY A 217 ? 0.1690 0.1151 0.1553 0.0050  0.0096  0.0177  197 GLY A CA    
1497 C  C     . GLY A 217 ? 0.1607 0.1138 0.1507 0.0009  0.0168  0.0274  197 GLY A C     
1498 O  O     . GLY A 217 ? 0.1774 0.1262 0.1616 0.0020  0.0193  0.0278  197 GLY A O     
1499 N  N     . PHE A 218 ? 0.1690 0.1155 0.1358 0.0028  0.0182  0.0188  198 PHE A N     
1500 C  CA    . PHE A 218 ? 0.1710 0.1130 0.1371 0.0092  0.0122  0.0244  198 PHE A CA    
1501 C  C     . PHE A 218 ? 0.1643 0.1203 0.1401 0.0034  0.0190  0.0287  198 PHE A C     
1502 O  O     . PHE A 218 ? 0.1835 0.1228 0.1337 0.0038  0.0148  0.0236  198 PHE A O     
1503 C  CB    . PHE A 218 ? 0.1642 0.1180 0.1417 0.0006  0.0057  0.0172  198 PHE A CB    
1504 C  CG    . PHE A 218 ? 0.1748 0.1145 0.1418 -0.0029 0.0117  0.0226  198 PHE A CG    
1505 C  CD1   . PHE A 218 ? 0.1820 0.1150 0.1376 0.0102  0.0144  0.0105  198 PHE A CD1   
1506 C  CD2   . PHE A 218 ? 0.1910 0.1186 0.1704 -0.0027 -0.0015 0.0232  198 PHE A CD2   
1507 C  CE1   . PHE A 218 ? 0.1846 0.1280 0.1524 0.0101  0.0104  0.0114  198 PHE A CE1   
1508 C  CE2   . PHE A 218 ? 0.2100 0.1175 0.1833 -0.0022 -0.0018 0.0281  198 PHE A CE2   
1509 C  CZ    . PHE A 218 ? 0.1952 0.1243 0.1691 0.0058  0.0043  0.0219  198 PHE A CZ    
1510 N  N     . LEU A 219 ? 0.1668 0.1411 0.1394 0.0104  0.0197  0.0247  199 LEU A N     
1511 C  CA    . LEU A 219 ? 0.1656 0.1327 0.1539 0.0219  0.0166  0.0300  199 LEU A CA    
1512 C  C     . LEU A 219 ? 0.1697 0.1275 0.1574 0.0271  0.0156  0.0345  199 LEU A C     
1513 O  O     . LEU A 219 ? 0.1777 0.1478 0.1568 0.0224  0.0193  0.0441  199 LEU A O     
1514 C  CB    . LEU A 219 ? 0.1605 0.1490 0.1708 0.0132  0.0170  0.0288  199 LEU A CB    
1515 C  CG    . LEU A 219 ? 0.1866 0.1874 0.1896 0.0230  0.0149  0.0230  199 LEU A CG    
1516 C  CD1   . LEU A 219 ? 0.1986 0.2092 0.1961 0.0170  0.0176  0.0193  199 LEU A CD1   
1517 C  CD2   . LEU A 219 ? 0.1866 0.2072 0.2028 0.0311  0.0263  0.0197  199 LEU A CD2   
1518 N  N     . LYS A 220 ? 0.1903 0.1220 0.1611 0.0117  0.0226  0.0323  200 LYS A N     
1519 C  CA    A LYS A 220 ? 0.2072 0.1275 0.1712 0.0149  0.0249  0.0305  200 LYS A CA    
1520 C  CA    B LYS A 220 ? 0.2055 0.1283 0.1730 0.0162  0.0256  0.0322  200 LYS A CA    
1521 C  C     . LYS A 220 ? 0.1953 0.1254 0.1625 0.0250  0.0197  0.0283  200 LYS A C     
1522 O  O     . LYS A 220 ? 0.1977 0.1345 0.1651 0.0275  0.0282  0.0433  200 LYS A O     
1523 C  CB    A LYS A 220 ? 0.2546 0.1365 0.1916 0.0024  0.0370  0.0154  200 LYS A CB    
1524 C  CB    B LYS A 220 ? 0.2505 0.1393 0.1968 0.0034  0.0386  0.0199  200 LYS A CB    
1525 C  CG    A LYS A 220 ? 0.3057 0.1527 0.2182 0.0105  0.0414  0.0050  200 LYS A CG    
1526 C  CG    B LYS A 220 ? 0.2997 0.1555 0.2264 0.0077  0.0456  0.0109  200 LYS A CG    
1527 C  CD    A LYS A 220 ? 0.3512 0.1812 0.2402 0.0193  0.0379  0.0043  200 LYS A CD    
1528 C  CD    B LYS A 220 ? 0.3444 0.1844 0.2516 0.0117  0.0468  0.0078  200 LYS A CD    
1529 C  CE    A LYS A 220 ? 0.3798 0.1983 0.2485 0.0182  0.0352  0.0049  200 LYS A CE    
1530 C  CE    B LYS A 220 ? 0.3748 0.1983 0.2639 0.0025  0.0512  0.0069  200 LYS A CE    
1531 N  NZ    A LYS A 220 ? 0.3940 0.2066 0.2525 0.0202  0.0327  0.0060  200 LYS A NZ    
1532 N  NZ    B LYS A 220 ? 0.3962 0.2110 0.2753 -0.0035 0.0515  0.0095  200 LYS A NZ    
1533 N  N     . ALA A 221 ? 0.2001 0.1198 0.1551 0.0209  0.0214  0.0273  201 ALA A N     
1534 C  CA    . ALA A 221 ? 0.1823 0.1222 0.1559 0.0091  0.0248  0.0250  201 ALA A CA    
1535 C  C     . ALA A 221 ? 0.1705 0.1309 0.1516 0.0188  0.0082  0.0257  201 ALA A C     
1536 O  O     . ALA A 221 ? 0.1757 0.1379 0.1454 0.0191  0.0141  0.0276  201 ALA A O     
1537 C  CB    . ALA A 221 ? 0.1804 0.1403 0.1635 0.0104  0.0198  0.0275  201 ALA A CB    
1538 N  N     . LEU A 222 ? 0.1701 0.1391 0.1502 0.0070  0.0048  0.0237  202 LEU A N     
1539 C  CA    . LEU A 222 ? 0.1720 0.1442 0.1545 0.0108  0.0025  0.0340  202 LEU A CA    
1540 C  C     . LEU A 222 ? 0.1843 0.1476 0.1563 0.0191  0.0112  0.0398  202 LEU A C     
1541 O  O     . LEU A 222 ? 0.2073 0.1674 0.1578 0.0217  0.0036  0.0438  202 LEU A O     
1542 C  CB    . LEU A 222 ? 0.1583 0.1444 0.1554 -0.0010 0.0069  0.0236  202 LEU A CB    
1543 C  CG    . LEU A 222 ? 0.1621 0.1389 0.1591 -0.0039 0.0158  0.0206  202 LEU A CG    
1544 C  CD1   . LEU A 222 ? 0.2022 0.1523 0.1694 -0.0105 0.0197  0.0228  202 LEU A CD1   
1545 C  CD2   . LEU A 222 ? 0.1928 0.1506 0.1690 0.0043  0.0084  0.0198  202 LEU A CD2   
1546 N  N     . LYS A 223 ? 0.1894 0.1479 0.1646 0.0259  0.0077  0.0388  203 LYS A N     
1547 C  CA    . LYS A 223 ? 0.2045 0.1478 0.1850 0.0241  0.0182  0.0390  203 LYS A CA    
1548 C  C     . LYS A 223 ? 0.2087 0.1525 0.1756 0.0241  0.0160  0.0486  203 LYS A C     
1549 O  O     . LYS A 223 ? 0.2316 0.1651 0.1917 0.0336  0.0124  0.0574  203 LYS A O     
1550 C  CB    . LYS A 223 ? 0.2024 0.1668 0.2095 0.0291  0.0263  0.0352  203 LYS A CB    
1551 C  CG    . LYS A 223 ? 0.2143 0.1841 0.2249 0.0293  0.0295  0.0399  203 LYS A CG    
1552 C  CD    . LYS A 223 ? 0.2347 0.1985 0.2487 0.0416  0.0394  0.0407  203 LYS A CD    
1553 N  N     . GLY A 224 ? 0.2112 0.1586 0.1695 0.0108  0.0234  0.0378  204 GLY A N     
1554 C  CA    . GLY A 224 ? 0.2150 0.1609 0.1765 0.0124  0.0382  0.0346  204 GLY A CA    
1555 C  C     . GLY A 224 ? 0.2289 0.1590 0.1829 -0.0002 0.0326  0.0486  204 GLY A C     
1556 O  O     . GLY A 224 ? 0.2922 0.1787 0.1988 -0.0313 0.0426  0.0458  204 GLY A O     
1557 N  N     . GLU A 225 ? 0.2049 0.1440 0.1822 0.0176  0.0207  0.0501  205 GLU A N     
1558 C  CA    . GLU A 225 ? 0.2094 0.1474 0.1960 0.0073  0.0129  0.0392  205 GLU A CA    
1559 C  C     . GLU A 225 ? 0.2176 0.1493 0.2051 0.0168  -0.0001 0.0319  205 GLU A C     
1560 O  O     . GLU A 225 ? 0.2062 0.1530 0.2122 0.0248  0.0036  0.0356  205 GLU A O     
1561 C  CB    . GLU A 225 ? 0.2167 0.1513 0.2095 0.0318  0.0058  0.0333  205 GLU A CB    
1562 C  CG    . GLU A 225 ? 0.2254 0.1670 0.2250 0.0431  0.0061  0.0351  205 GLU A CG    
1563 C  CD    . GLU A 225 ? 0.2466 0.1850 0.2419 0.0359  0.0116  0.0264  205 GLU A CD    
1564 O  OE1   . GLU A 225 ? 0.2690 0.2273 0.2486 0.0434  0.0257  0.0203  205 GLU A OE1   
1565 O  OE2   . GLU A 225 ? 0.2685 0.1874 0.2570 0.0277  0.0065  0.0198  205 GLU A OE2   
1566 N  N     . LYS A 226 ? 0.2544 0.1642 0.2186 0.0145  -0.0140 0.0307  206 LYS A N     
1567 C  CA    . LYS A 226 ? 0.3001 0.1931 0.2332 0.0119  -0.0237 0.0191  206 LYS A CA    
1568 C  C     . LYS A 226 ? 0.3239 0.1966 0.2345 0.0285  -0.0211 0.0066  206 LYS A C     
1569 O  O     . LYS A 226 ? 0.3470 0.2167 0.2430 0.0423  -0.0291 0.0030  206 LYS A O     
1570 C  CB    . LYS A 226 ? 0.3566 0.2448 0.2638 -0.0048 -0.0247 0.0182  206 LYS A CB    
1571 C  CG    . LYS A 226 ? 0.4051 0.2732 0.2873 -0.0139 -0.0201 0.0210  206 LYS A CG    
1572 C  CD    . LYS A 226 ? 0.4491 0.2903 0.3096 -0.0086 -0.0132 0.0240  206 LYS A CD    
1573 C  CE    . LYS A 226 ? 0.4730 0.2946 0.3269 -0.0026 0.0022  0.0255  206 LYS A CE    
1574 N  NZ    . LYS A 226 ? 0.4760 0.3010 0.3361 -0.0008 0.0098  0.0298  206 LYS A NZ    
1575 N  N     . VAL A 227 ? 0.3177 0.1815 0.2251 0.0192  -0.0206 0.0003  207 VAL A N     
1576 C  CA    . VAL A 227 ? 0.3321 0.1797 0.2393 0.0058  -0.0114 -0.0007 207 VAL A CA    
1577 C  C     . VAL A 227 ? 0.4092 0.2088 0.2638 -0.0258 -0.0073 -0.0062 207 VAL A C     
1578 O  O     . VAL A 227 ? 0.4000 0.2381 0.2725 -0.0714 0.0142  -0.0160 207 VAL A O     
1579 C  CB    . VAL A 227 ? 0.2787 0.1778 0.2367 0.0059  -0.0063 0.0083  207 VAL A CB    
1580 C  CG1   . VAL A 227 ? 0.2660 0.1889 0.2376 -0.0033 -0.0039 0.0102  207 VAL A CG1   
1581 C  CG2   . VAL A 227 ? 0.2692 0.1923 0.2438 0.0022  -0.0051 0.0006  207 VAL A CG2   
1582 N  N     . GLU A 228 ? 0.4827 0.2070 0.2775 -0.0301 -0.0283 -0.0006 208 GLU A N     
1583 C  CA    . GLU A 228 ? 0.5486 0.2138 0.2952 -0.0563 -0.0406 0.0037  208 GLU A CA    
1584 C  C     . GLU A 228 ? 0.5917 0.2309 0.3047 -0.1022 -0.0505 0.0257  208 GLU A C     
1585 O  O     . GLU A 228 ? 0.5910 0.2523 0.2922 -0.1153 -0.0546 0.0503  208 GLU A O     
1586 C  CB    . GLU A 228 ? 0.5696 0.2222 0.3027 -0.0405 -0.0378 -0.0065 208 GLU A CB    
1587 N  N     . ALA A 229 ? 0.6453 0.2574 0.3284 -0.1155 -0.0507 0.0225  209 ALA A N     
1588 C  CA    . ALA A 229 ? 0.6926 0.2946 0.3584 -0.1293 -0.0521 0.0156  209 ALA A CA    
1589 C  C     . ALA A 229 ? 0.7238 0.3148 0.3722 -0.1476 -0.0633 0.0136  209 ALA A C     
1590 O  O     . ALA A 229 ? 0.7312 0.3111 0.3764 -0.1564 -0.0684 0.0139  209 ALA A O     
1591 C  CB    . ALA A 229 ? 0.6984 0.3070 0.3695 -0.1287 -0.0453 0.0127  209 ALA A CB    
1592 N  N     . LYS A 230 ? 0.7410 0.3336 0.3807 -0.1514 -0.0712 0.0084  210 LYS A N     
1593 C  CA    . LYS A 230 ? 0.7600 0.3709 0.3945 -0.1427 -0.0733 0.0107  210 LYS A CA    
1594 C  C     . LYS A 230 ? 0.7681 0.3953 0.4054 -0.1384 -0.0755 0.0153  210 LYS A C     
1595 O  O     . LYS A 230 ? 0.7752 0.4065 0.4119 -0.1402 -0.0768 0.0211  210 LYS A O     
1596 C  CB    . LYS A 230 ? 0.7675 0.3769 0.3970 -0.1399 -0.0734 0.0086  210 LYS A CB    
1597 P  PG    . ANP B .   ? 0.2136 0.2188 0.1484 0.0026  -0.0164 -0.0074 301 ANP A PG    
1598 O  O1G   . ANP B .   ? 0.1867 0.2124 0.1660 0.0170  -0.0079 -0.0075 301 ANP A O1G   
1599 O  O2G   . ANP B .   ? 0.2332 0.2291 0.1633 0.0103  -0.0413 -0.0219 301 ANP A O2G   
1600 O  O3G   . ANP B .   ? 0.2431 0.2295 0.1652 0.0085  -0.0077 -0.0043 301 ANP A O3G   
1601 P  PB    . ANP B .   ? 0.1591 0.2181 0.1387 0.0132  -0.0109 -0.0097 301 ANP A PB    
1602 O  O1B   . ANP B .   ? 0.1639 0.2669 0.1560 0.0272  -0.0082 -0.0252 301 ANP A O1B   
1603 O  O2B   . ANP B .   ? 0.1595 0.2279 0.1349 -0.0079 -0.0161 -0.0136 301 ANP A O2B   
1604 N  N3B   . ANP B .   ? 0.1887 0.2212 0.1459 0.0213  -0.0150 -0.0029 301 ANP A N3B   
1605 P  PA    . ANP B .   ? 0.1418 0.1683 0.1209 -0.0113 -0.0029 -0.0167 301 ANP A PA    
1606 O  O1A   . ANP B .   ? 0.1449 0.1710 0.1281 -0.0207 -0.0045 -0.0338 301 ANP A O1A   
1607 O  O2A   . ANP B .   ? 0.1465 0.1876 0.1239 -0.0139 0.0071  -0.0174 301 ANP A O2A   
1608 O  O3A   . ANP B .   ? 0.1497 0.1945 0.1298 -0.0001 -0.0093 -0.0130 301 ANP A O3A   
1609 O  "O5'" . ANP B .   ? 0.1349 0.1622 0.1277 -0.0156 0.0027  -0.0163 301 ANP A "O5'" 
1610 C  "C5'" . ANP B .   ? 0.1465 0.1612 0.1314 -0.0060 0.0006  -0.0126 301 ANP A "C5'" 
1611 C  "C4'" . ANP B .   ? 0.1493 0.1569 0.1331 -0.0094 -0.0072 -0.0139 301 ANP A "C4'" 
1612 O  "O4'" . ANP B .   ? 0.1443 0.1579 0.1391 -0.0105 -0.0008 -0.0140 301 ANP A "O4'" 
1613 C  "C3'" . ANP B .   ? 0.1460 0.1515 0.1367 -0.0128 -0.0006 -0.0072 301 ANP A "C3'" 
1614 O  "O3'" . ANP B .   ? 0.1532 0.1612 0.1414 -0.0103 0.0025  -0.0164 301 ANP A "O3'" 
1615 C  "C2'" . ANP B .   ? 0.1430 0.1510 0.1260 -0.0103 0.0020  -0.0015 301 ANP A "C2'" 
1616 O  "O2'" . ANP B .   ? 0.1404 0.1406 0.1268 -0.0029 -0.0013 -0.0012 301 ANP A "O2'" 
1617 C  "C1'" . ANP B .   ? 0.1367 0.1540 0.1331 -0.0125 0.0040  -0.0008 301 ANP A "C1'" 
1618 N  N9    . ANP B .   ? 0.1454 0.1624 0.1328 0.0007  -0.0077 0.0040  301 ANP A N9    
1619 C  C8    . ANP B .   ? 0.1841 0.1893 0.1516 -0.0044 -0.0204 -0.0057 301 ANP A C8    
1620 N  N7    . ANP B .   ? 0.1888 0.1914 0.1536 0.0002  -0.0327 0.0087  301 ANP A N7    
1621 C  C5    . ANP B .   ? 0.1617 0.1730 0.1465 -0.0004 -0.0058 0.0136  301 ANP A C5    
1622 C  C6    . ANP B .   ? 0.1649 0.1673 0.1581 0.0048  0.0039  0.0299  301 ANP A C6    
1623 N  N6    . ANP B .   ? 0.1964 0.1798 0.1708 0.0090  -0.0064 0.0385  301 ANP A N6    
1624 N  N1    . ANP B .   ? 0.1428 0.1492 0.1678 0.0037  0.0103  0.0250  301 ANP A N1    
1625 C  C2    . ANP B .   ? 0.1446 0.1491 0.1594 -0.0057 0.0024  0.0253  301 ANP A C2    
1626 N  N3    . ANP B .   ? 0.1344 0.1498 0.1457 -0.0065 -0.0055 0.0221  301 ANP A N3    
1627 C  C4    . ANP B .   ? 0.1339 0.1646 0.1388 -0.0022 0.0012  0.0114  301 ANP A C4    
1628 MG MG    . MG  C .   ? 0.1576 0.1995 0.1235 -0.0215 -0.0096 -0.0264 302 MG  A MG    
1629 MG MG    . MG  D .   ? 0.2165 0.3858 0.1901 -0.0253 0.0156  -0.0425 303 MG  A MG    
1630 O  O     . HOH E .   ? 0.8770 0.4272 1.0598 0.0148  0.5369  0.0575  401 HOH A O     
1631 O  O     . HOH E .   ? 0.4109 0.7786 0.2208 -0.1773 -0.0070 0.0585  402 HOH A O     
1632 O  O     . HOH E .   ? 0.4047 0.3830 0.7119 0.0273  0.1329  0.2663  403 HOH A O     
1633 O  O     . HOH E .   ? 0.8322 0.5597 0.5759 -0.1374 -0.3857 0.0284  404 HOH A O     
1634 O  O     . HOH E .   ? 0.5127 0.3190 0.4220 -0.0091 -0.0625 0.0103  405 HOH A O     
1635 O  O     . HOH E .   ? 0.5696 0.5837 0.3808 -0.0756 -0.0011 -0.0012 406 HOH A O     
1636 O  O     . HOH E .   ? 0.3989 0.7566 0.6105 -0.1308 -0.0833 0.3202  407 HOH A O     
1637 O  O     . HOH E .   ? 0.3858 0.1838 0.2595 0.0361  0.0093  -0.0159 408 HOH A O     
1638 O  O     . HOH E .   ? 0.1678 0.2105 0.1279 -0.0330 -0.0005 -0.0269 409 HOH A O     
1639 O  O     . HOH E .   ? 0.3832 0.7096 0.2946 -0.1182 -0.0351 0.2077  410 HOH A O     
1640 O  O     . HOH E .   ? 0.4045 0.6741 0.7343 0.0165  -0.0929 0.2996  411 HOH A O     
1641 O  O     . HOH E .   ? 0.4248 0.2702 0.6097 -0.0981 -0.0218 -0.1595 412 HOH A O     
1642 O  O     . HOH E .   ? 0.5969 0.6391 0.4652 -0.2309 0.1297  0.1532  413 HOH A O     
1643 O  O     . HOH E .   ? 0.8076 0.5610 0.5265 -0.3332 0.2883  -0.1438 414 HOH A O     
1644 O  O     . HOH E .   ? 0.5598 0.5998 0.3557 -0.0546 0.1624  -0.1731 415 HOH A O     
1645 O  O     . HOH E .   ? 0.4574 0.5984 0.5683 0.0208  0.1897  -0.1874 416 HOH A O     
1646 O  O     . HOH E .   ? 0.3316 0.3209 0.3169 -0.1030 0.0286  -0.0703 417 HOH A O     
1647 O  O     . HOH E .   ? 0.3092 0.2069 0.2856 0.0618  -0.0045 0.0418  418 HOH A O     
1648 O  O     . HOH E .   ? 0.2700 0.1761 0.2407 0.0084  -0.0248 0.0076  419 HOH A O     
1649 O  O     . HOH E .   ? 0.2893 0.5579 0.4987 0.1270  -0.0194 0.1282  420 HOH A O     
1650 O  O     . HOH E .   ? 0.5303 0.7868 0.2501 -0.2326 0.0627  -0.0034 421 HOH A O     
1651 O  O     . HOH E .   ? 0.2411 0.2437 0.1868 0.0188  0.0212  0.0351  422 HOH A O     
1652 O  O     . HOH E .   ? 0.5758 0.3504 1.0833 -0.0602 -0.2944 0.1380  423 HOH A O     
1653 O  O     . HOH E .   ? 0.8595 0.2821 0.2226 0.1203  -0.0292 -0.0068 424 HOH A O     
1654 O  O     . HOH E .   ? 0.5338 0.4507 0.4864 0.1874  0.0262  -0.0970 425 HOH A O     
1655 O  O     . HOH E .   ? 0.2555 0.1987 0.2503 -0.0209 0.0379  0.0432  426 HOH A O     
1656 O  O     . HOH E .   ? 0.2397 0.2447 0.1728 -0.0249 -0.0287 0.0335  427 HOH A O     
1657 O  O     . HOH E .   ? 0.1575 0.1761 0.1409 -0.0194 0.0169  -0.0086 428 HOH A O     
1658 O  O     . HOH E .   ? 0.2902 0.1995 0.2656 -0.0040 0.0611  -0.0315 429 HOH A O     
1659 O  O     . HOH E .   ? 0.4177 0.4107 0.8102 0.0381  0.0115  0.1164  430 HOH A O     
1660 O  O     . HOH E .   ? 0.2067 0.3577 0.2443 -0.0239 -0.0086 0.0442  431 HOH A O     
1661 O  O     . HOH E .   ? 0.4145 0.9454 0.6258 0.2777  -0.0737 -0.1461 432 HOH A O     
1662 O  O     . HOH E .   ? 0.4014 0.3894 0.3948 -0.2116 0.0494  -0.0923 433 HOH A O     
1663 O  O     . HOH E .   ? 0.6680 0.7897 0.6832 -0.3062 0.2222  0.1311  434 HOH A O     
1664 O  O     . HOH E .   ? 0.3748 0.1597 0.4073 -0.0161 0.0472  -0.0202 435 HOH A O     
1665 O  O     . HOH E .   ? 0.3494 0.4893 0.2145 0.1666  -0.0935 -0.1141 436 HOH A O     
1666 O  O     . HOH E .   ? 0.5931 1.1084 0.4896 0.2276  -0.1907 0.0591  437 HOH A O     
1667 O  O     . HOH E .   ? 0.6195 0.3341 0.2825 -0.1289 0.0532  0.0151  438 HOH A O     
1668 O  O     . HOH E .   ? 0.5180 0.5564 0.5745 -0.2767 0.1237  -0.2233 439 HOH A O     
1669 O  O     . HOH E .   ? 0.3522 0.2998 0.3140 -0.0495 0.0184  -0.0899 440 HOH A O     
1670 O  O     . HOH E .   ? 0.3769 0.3357 0.3117 -0.0540 -0.0453 0.0799  441 HOH A O     
1671 O  O     . HOH E .   ? 0.2831 0.1803 0.2116 -0.0252 -0.0396 -0.0100 442 HOH A O     
1672 O  O     . HOH E .   ? 0.2216 0.2617 0.1870 -0.0047 0.0418  0.0122  443 HOH A O     
1673 O  O     . HOH E .   ? 0.5698 0.2241 0.3398 0.0658  0.2124  -0.0078 444 HOH A O     
1674 O  O     . HOH E .   ? 0.5136 0.5583 0.3786 0.2635  0.1773  0.2157  445 HOH A O     
1675 O  O     . HOH E .   ? 0.6122 0.4646 0.6729 -0.0165 -0.0285 -0.3229 446 HOH A O     
1676 O  O     . HOH E .   ? 0.6347 0.3552 0.4228 0.1938  0.2094  0.1629  447 HOH A O     
1677 O  O     . HOH E .   ? 0.2720 0.3736 0.4219 0.0725  0.0803  0.0343  448 HOH A O     
1678 O  O     . HOH E .   ? 0.3018 0.5041 0.3791 0.1408  0.0810  0.1674  449 HOH A O     
1679 O  O     . HOH E .   ? 0.4156 0.7562 0.4500 -0.2801 0.1343  -0.2212 450 HOH A O     
1680 O  O     . HOH E .   ? 0.2328 0.7260 0.1870 -0.0165 -0.0070 -0.0418 451 HOH A O     
1681 O  O     . HOH E .   ? 0.7888 0.4048 0.2565 -0.0794 -0.0961 0.0927  452 HOH A O     
1682 O  O     . HOH E .   ? 0.4448 0.3035 0.4391 0.0463  -0.1174 0.0411  453 HOH A O     
1683 O  O     . HOH E .   ? 0.2377 0.5516 0.3181 -0.1563 0.0748  -0.1267 454 HOH A O     
1684 O  O     . HOH E .   ? 0.1703 0.1516 0.2112 0.0093  -0.0197 0.0069  455 HOH A O     
1685 O  O     . HOH E .   ? 0.2164 0.1835 0.1513 -0.0107 0.0240  0.0063  456 HOH A O     
1686 O  O     . HOH E .   ? 0.6141 0.4935 0.4856 -0.2771 0.1304  0.0142  457 HOH A O     
1687 O  O     . HOH E .   ? 0.1582 0.2589 0.2239 -0.0079 -0.0251 0.0041  458 HOH A O     
1688 O  O     . HOH E .   ? 0.4591 0.4419 0.3381 0.2547  -0.1340 -0.1275 459 HOH A O     
1689 O  O     . HOH E .   ? 0.1895 0.1728 0.1908 -0.0069 0.0055  0.0222  460 HOH A O     
1690 O  O     . HOH E .   ? 0.2222 0.2681 0.2773 -0.0013 0.0455  0.0033  461 HOH A O     
1691 O  O     . HOH E .   ? 0.6076 0.3502 0.7856 -0.0041 0.2828  0.1669  462 HOH A O     
1692 O  O     . HOH E .   ? 0.3033 0.7386 0.5569 -0.1197 -0.0020 0.1994  463 HOH A O     
1693 O  O     . HOH E .   ? 0.1980 0.1827 0.1825 0.0047  0.0165  0.0505  464 HOH A O     
1694 O  O     . HOH E .   ? 0.2215 0.1552 0.1644 0.0040  0.0052  0.0282  465 HOH A O     
1695 O  O     . HOH E .   ? 0.7081 0.3165 0.3665 -0.1204 -0.0238 -0.1306 466 HOH A O     
1696 O  O     . HOH E .   ? 0.5557 0.2544 0.2613 -0.0907 0.0875  -0.0352 467 HOH A O     
1697 O  O     . HOH E .   ? 0.3843 0.6023 0.3122 -0.2314 -0.0081 0.0623  468 HOH A O     
1698 O  O     . HOH E .   ? 0.3941 0.4020 0.2783 -0.0961 0.0315  -0.0458 469 HOH A O     
1699 O  O     . HOH E .   ? 0.2052 0.3459 0.2978 0.0701  0.0493  0.0427  470 HOH A O     
1700 O  O     . HOH E .   ? 0.3037 0.7458 0.5905 -0.1400 -0.0573 0.1499  471 HOH A O     
1701 O  O     . HOH E .   ? 0.3621 0.2473 0.3574 0.0444  0.0416  0.0586  472 HOH A O     
1702 O  O     . HOH E .   ? 0.3591 0.3555 0.7794 -0.0622 0.0855  -0.2579 473 HOH A O     
1703 O  O     . HOH E .   ? 0.2805 0.2270 0.2757 0.0533  0.0088  -0.0026 474 HOH A O     
1704 O  O     . HOH E .   ? 0.2712 0.4859 0.3072 0.0260  -0.0244 0.1055  475 HOH A O     
1705 O  O     . HOH E .   ? 0.3625 0.5438 0.9858 -0.0773 -0.0355 0.2375  476 HOH A O     
1706 O  O     . HOH E .   ? 0.6826 0.2449 0.7338 -0.0034 -0.2356 0.0559  477 HOH A O     
1707 O  O     . HOH E .   ? 0.5476 0.4597 0.4742 -0.1969 0.0233  -0.0035 478 HOH A O     
1708 O  O     . HOH E .   ? 0.2132 0.4370 0.3175 0.0864  -0.0050 0.0875  479 HOH A O     
1709 O  O     . HOH E .   ? 0.2733 0.1910 0.2296 0.0522  0.0134  0.0450  480 HOH A O     
1710 O  O     . HOH E .   ? 0.1823 0.1379 0.1734 -0.0130 -0.0054 -0.0071 481 HOH A O     
1711 O  O     . HOH E .   ? 0.8102 0.4121 0.3963 0.1373  -0.0555 -0.0455 482 HOH A O     
1712 O  O     . HOH E .   ? 0.3317 0.5238 0.7896 0.1005  -0.1699 -0.0148 483 HOH A O     
1713 O  O     . HOH E .   ? 0.3245 0.5303 0.8705 -0.0822 -0.1010 0.1395  484 HOH A O     
1714 O  O     . HOH E .   ? 0.1487 0.1616 0.1742 0.0114  -0.0130 0.0109  485 HOH A O     
1715 O  O     . HOH E .   ? 0.1849 0.1416 0.1544 -0.0130 0.0205  -0.0011 486 HOH A O     
1716 O  O     . HOH E .   ? 0.1921 0.1790 0.1759 0.0121  0.0047  0.0177  487 HOH A O     
1717 O  O     . HOH E .   ? 0.3981 0.4514 0.4129 -0.0475 0.0062  0.0063  488 HOH A O     
1718 O  O     . HOH E .   ? 0.3666 0.2673 0.1891 0.0693  0.0332  0.0790  489 HOH A O     
1719 O  O     . HOH E .   ? 0.5761 0.2716 0.2281 0.0555  -0.1017 0.0517  490 HOH A O     
1720 O  O     . HOH E .   ? 0.3018 0.1761 0.2569 0.0224  -0.0015 -0.0232 491 HOH A O     
1721 O  O     . HOH E .   ? 0.3205 0.2098 0.3288 -0.0482 -0.0360 0.0059  492 HOH A O     
1722 O  O     . HOH E .   ? 0.3809 0.2775 0.3339 -0.0920 0.1625  -0.0887 493 HOH A O     
1723 O  O     . HOH E .   ? 0.4695 0.6770 0.7090 0.1083  -0.2038 0.1325  494 HOH A O     
1724 O  O     . HOH E .   ? 0.4877 0.5568 0.7072 0.1023  -0.0880 0.1087  495 HOH A O     
1725 O  O     . HOH E .   ? 0.3255 0.6646 0.2855 -0.2180 0.0851  -0.1828 496 HOH A O     
1726 O  O     . HOH E .   ? 0.3122 0.2795 0.2283 -0.0593 0.0476  -0.0307 497 HOH A O     
1727 O  O     . HOH E .   ? 0.3776 0.5501 0.3952 -0.1274 -0.0803 0.1767  498 HOH A O     
1728 O  O     . HOH E .   ? 0.4118 0.3168 0.3511 0.0989  0.0040  -0.0915 499 HOH A O     
1729 O  O     . HOH E .   ? 0.3355 0.4597 0.4952 -0.1176 -0.0235 0.1255  500 HOH A O     
1730 O  O     . HOH E .   ? 0.3021 0.6072 0.3791 -0.0087 0.1099  0.0213  501 HOH A O     
1731 O  O     . HOH E .   ? 0.3232 0.2162 0.2146 0.0195  0.0408  0.0090  502 HOH A O     
1732 O  O     . HOH E .   ? 0.4103 0.5795 0.3372 0.0172  -0.1766 0.0532  503 HOH A O     
1733 O  O     . HOH E .   ? 0.3316 0.7733 0.7032 -0.0356 0.0837  -0.2042 504 HOH A O     
1734 O  O     . HOH E .   ? 0.2390 0.1865 0.1680 0.0312  -0.0188 0.0073  505 HOH A O     
1735 O  O     . HOH E .   ? 0.5298 0.4504 0.2606 -0.2839 0.0834  -0.0854 506 HOH A O     
1736 O  O     . HOH E .   ? 0.6750 0.3548 0.5822 0.2220  -0.1322 -0.1465 507 HOH A O     
1737 O  O     . HOH E .   ? 0.6825 0.3157 0.2591 0.1845  0.0055  0.0555  508 HOH A O     
1738 O  O     . HOH E .   ? 0.2691 0.7182 0.2761 0.1667  0.0578  0.1615  509 HOH A O     
1739 O  O     . HOH E .   ? 0.2851 0.2261 0.2398 0.0077  -0.0125 -0.0081 510 HOH A O     
1740 O  O     . HOH E .   ? 0.3286 0.5482 0.2535 -0.1063 -0.0271 -0.0964 511 HOH A O     
1741 O  O     . HOH E .   ? 0.5991 0.2987 0.4616 0.0824  -0.2613 0.0304  512 HOH A O     
1742 O  O     . HOH E .   ? 0.2085 0.2809 0.1651 -0.0164 -0.0099 0.0160  513 HOH A O     
1743 O  O     . HOH E .   ? 0.5282 0.6282 0.5443 -0.2224 -0.2096 0.1793  514 HOH A O     
1744 O  O     . HOH E .   ? 0.2628 0.1756 0.3124 0.0159  0.0115  -0.0256 515 HOH A O     
1745 O  O     . HOH E .   ? 0.2029 0.2107 0.1359 0.0007  -0.0197 -0.0133 516 HOH A O     
1746 O  O     . HOH E .   ? 0.2312 0.1666 0.1628 -0.0232 0.0076  0.0157  517 HOH A O     
1747 O  O     . HOH E .   ? 0.6588 0.4503 0.5001 -0.1112 0.2273  -0.1136 518 HOH A O     
1748 O  O     . HOH E .   ? 0.3592 0.2189 0.1937 0.0122  -0.0087 0.0001  519 HOH A O     
1749 O  O     . HOH E .   ? 0.2412 0.1873 0.2125 -0.0297 -0.0062 0.0183  520 HOH A O     
1750 O  O     . HOH E .   ? 0.2344 0.2388 0.2117 -0.0107 0.0006  0.0345  521 HOH A O     
1751 O  O     . HOH E .   ? 0.4793 0.1766 0.2564 0.0245  0.1209  0.0298  522 HOH A O     
1752 O  O     . HOH E .   ? 0.7557 0.4384 0.5155 0.2203  0.0525  0.0348  523 HOH A O     
1753 O  O     . HOH E .   ? 0.2024 0.3958 0.2116 -0.0667 -0.0219 0.0700  524 HOH A O     
1754 O  O     . HOH E .   ? 0.3554 0.3285 0.2175 -0.0499 0.0007  0.0559  525 HOH A O     
1755 O  O     . HOH E .   ? 0.1672 0.1726 0.1768 -0.0142 0.0052  0.0364  526 HOH A O     
1756 O  O     . HOH E .   ? 0.6333 0.3303 0.2812 0.1802  0.1430  0.1082  527 HOH A O     
1757 O  O     . HOH E .   ? 0.4812 0.3417 0.3065 0.0180  -0.1410 0.0755  528 HOH A O     
1758 O  O     . HOH E .   ? 0.6894 0.6958 0.6010 0.1405  0.3653  0.0250  529 HOH A O     
1759 O  O     . HOH E .   ? 0.4280 0.2444 0.3334 -0.0246 0.0722  -0.0459 530 HOH A O     
1760 O  O     . HOH E .   ? 0.3138 0.6995 0.3264 -0.0536 -0.0984 -0.1118 531 HOH A O     
1761 O  O     . HOH E .   ? 0.4143 0.2796 0.3043 -0.0097 -0.1005 -0.1208 532 HOH A O     
1762 O  O     . HOH E .   ? 0.4335 0.8486 0.5668 0.0016  -0.1930 0.2508  533 HOH A O     
1763 O  O     . HOH E .   ? 0.8377 0.5746 0.2454 -0.1466 -0.0977 0.0083  534 HOH A O     
1764 O  O     . HOH E .   ? 0.5878 0.5572 0.5432 -0.2312 0.0471  -0.1789 535 HOH A O     
1765 O  O     . HOH E .   ? 0.4313 0.1924 0.2394 -0.0892 0.0609  -0.0229 536 HOH A O     
1766 O  O     . HOH E .   ? 0.7117 0.4707 0.5167 -0.1465 -0.0796 -0.2437 537 HOH A O     
1767 O  O     . HOH E .   ? 0.3764 0.7572 0.6220 0.0386  0.0276  0.1601  538 HOH A O     
1768 O  O     . HOH E .   ? 0.5641 0.3411 0.9623 0.0434  0.3431  -0.0491 539 HOH A O     
1769 O  O     . HOH E .   ? 0.5060 0.4285 0.4804 0.0345  -0.1877 -0.0389 540 HOH A O     
1770 O  O     . HOH E .   ? 0.2632 0.1579 0.2336 0.0161  -0.0676 0.0175  541 HOH A O     
1771 O  O     . HOH E .   ? 0.4163 0.2323 0.2551 -0.0586 -0.0134 -0.0390 542 HOH A O     
1772 O  O     . HOH E .   ? 0.6039 0.5829 0.5389 -0.0523 -0.0769 0.1782  543 HOH A O     
1773 O  O     . HOH E .   ? 0.3522 0.7811 0.3960 0.0491  0.0680  -0.2431 544 HOH A O     
1774 O  O     . HOH E .   ? 0.7186 0.5801 0.3504 0.2604  0.1262  0.0652  545 HOH A O     
1775 O  O     . HOH E .   ? 0.2233 0.4498 0.5032 -0.0557 -0.0694 0.1590  546 HOH A O     
1776 O  O     . HOH E .   ? 0.3428 0.4200 0.6277 -0.1675 0.1132  0.0100  547 HOH A O     
1777 O  O     . HOH E .   ? 0.5348 0.2558 0.2397 -0.1779 0.0663  -0.0217 548 HOH A O     
1778 O  O     . HOH E .   ? 0.7444 0.2070 0.2992 -0.0049 -0.0783 0.0211  549 HOH A O     
1779 O  O     . HOH E .   ? 0.3742 0.3142 0.5765 -0.1161 -0.2434 0.1872  550 HOH A O     
1780 O  O     . HOH E .   ? 0.3012 0.5918 0.2582 -0.1757 0.0340  0.0501  551 HOH A O     
1781 O  O     . HOH E .   ? 0.7893 0.8205 0.4074 0.3238  -0.0057 -0.0616 552 HOH A O     
1782 O  O     . HOH E .   ? 0.5659 0.5259 0.3184 0.1691  0.0969  0.0663  553 HOH A O     
1783 O  O     . HOH E .   ? 0.6736 0.3893 0.4878 -0.1718 -0.0929 -0.0298 554 HOH A O     
1784 O  O     . HOH E .   ? 0.5620 1.1109 0.3616 0.4163  0.0243  0.0622  555 HOH A O     
1785 O  O     . HOH E .   ? 0.6478 0.4818 0.7478 -0.1878 -0.2381 0.1631  556 HOH A O     
1786 O  O     . HOH E .   ? 0.2710 0.1515 0.2270 -0.0025 0.0021  -0.0013 557 HOH A O     
1787 O  O     . HOH E .   ? 0.3356 0.1819 0.3755 0.0135  -0.0867 0.0087  558 HOH A O     
1788 O  O     . HOH E .   ? 0.3876 0.4632 0.7299 0.2049  -0.0152 0.1312  559 HOH A O     
1789 O  O     . HOH E .   ? 0.4821 0.4671 0.2521 -0.2454 -0.0164 -0.0410 560 HOH A O     
1790 O  O     . HOH E .   ? 0.6575 0.4368 0.3109 -0.1010 0.0998  -0.0823 561 HOH A O     
1791 O  O     . HOH E .   ? 0.7106 0.6397 0.5016 0.0744  0.2089  0.0820  562 HOH A O     
1792 O  O     . HOH E .   ? 0.5140 0.6926 0.3403 0.2055  0.1573  0.1309  563 HOH A O     
1793 O  O     . HOH E .   ? 0.8745 0.5981 0.3396 -0.0289 0.1021  0.0560  564 HOH A O     
1794 O  O     . HOH E .   ? 0.3892 0.4517 0.7969 0.0321  -0.0895 0.2968  565 HOH A O     
1795 O  O     . HOH E .   ? 0.6703 0.4104 1.0409 -0.1894 0.0965  -0.1248 566 HOH A O     
1796 O  O     . HOH E .   ? 0.2368 0.2661 0.3863 0.0428  0.0160  0.0651  567 HOH A O     
1797 O  O     . HOH E .   ? 0.2553 0.2143 0.3385 -0.0019 -0.0335 -0.0477 568 HOH A O     
1798 O  O     . HOH E .   ? 0.5140 0.5232 0.1795 -0.1512 -0.0052 -0.0092 569 HOH A O     
1799 O  O     . HOH E .   ? 0.9155 0.3594 0.3913 0.0065  0.0365  0.0426  570 HOH A O     
1800 O  O     . HOH E .   ? 0.4533 0.5490 0.3917 0.0923  0.1868  -0.0673 571 HOH A O     
1801 O  O     . HOH E .   ? 0.5356 0.4183 0.2832 0.1401  0.0298  -0.0270 572 HOH A O     
1802 O  O     . HOH E .   ? 0.5971 0.4884 0.2645 -0.3156 0.0736  -0.0726 573 HOH A O     
1803 O  O     . HOH E .   ? 0.3856 0.4965 0.9428 0.0931  -0.0356 0.1350  574 HOH A O     
1804 O  O     . HOH E .   ? 0.4154 0.2374 0.6464 -0.0074 -0.1722 -0.0676 575 HOH A O     
1805 O  O     . HOH E .   ? 0.5627 0.3254 0.5240 -0.1387 0.0339  0.1235  576 HOH A O     
1806 O  O     . HOH E .   ? 0.3604 0.4434 0.3321 0.1315  0.0266  0.0709  577 HOH A O     
1807 O  O     . HOH E .   ? 0.6017 0.3455 0.6488 -0.1703 -0.2437 0.0882  578 HOH A O     
1808 O  O     . HOH E .   ? 0.9612 0.3592 0.3474 0.0858  0.1363  0.0123  579 HOH A O     
1809 O  O     . HOH E .   ? 0.3990 0.4188 0.3217 0.1339  0.1182  0.0594  580 HOH A O     
1810 O  O     . HOH E .   ? 0.9660 0.3899 0.6404 0.1228  -0.4362 -0.0511 581 HOH A O     
1811 O  O     . HOH E .   ? 0.3878 0.5481 0.4704 0.1852  0.0556  0.2484  582 HOH A O     
1812 O  O     . HOH E .   ? 0.8390 0.3254 0.6644 -0.1067 -0.0567 -0.1576 583 HOH A O     
1813 O  O     . HOH E .   ? 0.4059 0.4970 0.9058 0.1401  -0.2058 -0.0948 584 HOH A O     
1814 O  O     . HOH E .   ? 0.4240 0.8085 0.3464 -0.1605 0.1516  -0.1172 585 HOH A O     
1815 O  O     . HOH E .   ? 0.5619 0.5121 0.6636 -0.0556 -0.2890 0.0329  586 HOH A O     
1816 O  O     . HOH E .   ? 0.4631 0.3538 0.3993 0.0143  -0.1615 -0.0475 587 HOH A O     
1817 O  O     . HOH E .   ? 1.0919 0.5260 0.4277 0.2638  0.1875  0.1464  588 HOH A O     
1818 O  O     . HOH E .   ? 0.4322 0.3321 0.7394 0.0669  0.0647  -0.0466 589 HOH A O     
1819 O  O     . HOH E .   ? 0.5065 0.5358 0.8022 0.0819  -0.1846 -0.1879 590 HOH A O     
1820 O  O     . HOH E .   ? 0.4546 0.4373 0.5836 -0.0238 0.0934  -0.1332 591 HOH A O     
1821 O  O     . HOH E .   ? 0.5261 0.4768 0.4811 -0.1219 -0.2863 0.1187  592 HOH A O     
1822 O  O     . HOH E .   ? 0.4127 0.8151 0.4336 0.1685  0.1038  -0.0068 593 HOH A O     
1823 O  O     . HOH E .   ? 0.5008 0.3985 0.5261 -0.0201 0.0022  -0.2692 594 HOH A O     
1824 O  O     . HOH E .   ? 0.2294 0.1988 0.2076 0.0308  -0.0200 -0.0054 595 HOH A O     
1825 O  O     . HOH E .   ? 0.3114 0.5032 0.5823 -0.1623 -0.0593 0.2190  596 HOH A O     
1826 O  O     . HOH E .   ? 0.7912 0.5027 0.2590 0.1969  0.0666  0.0943  597 HOH A O     
1827 O  O     . HOH E .   ? 0.6104 0.4294 0.2180 0.0860  0.0954  0.0054  598 HOH A O     
1828 O  O     . HOH E .   ? 0.4226 0.2511 0.2290 0.0276  -0.0204 -0.0116 599 HOH A O     
1829 O  O     . HOH E .   ? 1.0519 0.5033 0.3188 -0.0912 0.1248  0.0466  600 HOH A O     
1830 O  O     . HOH E .   ? 0.3953 0.7377 0.4598 0.2183  0.1305  0.3077  601 HOH A O     
1831 O  O     . HOH E .   ? 0.2234 0.4416 0.2548 -0.0143 -0.0284 -0.0317 602 HOH A O     
1832 O  O     . HOH E .   ? 0.5808 0.3464 0.3603 0.0969  0.0322  0.0055  603 HOH A O     
1833 O  O     . HOH E .   ? 0.3843 1.0975 0.4393 -0.1852 -0.0896 0.2926  604 HOH A O     
1834 O  O     . HOH E .   ? 0.2723 0.1930 0.1795 0.0094  -0.0322 0.0212  605 HOH A O     
1835 O  O     . HOH E .   ? 0.5089 0.6381 0.4504 -0.2422 0.0609  0.0062  606 HOH A O     
1836 O  O     . HOH E .   ? 0.3433 0.3810 0.5391 -0.0713 -0.0723 -0.0233 607 HOH A O     
1837 O  O     . HOH E .   ? 0.6981 0.5142 0.5042 0.3238  -0.1149 0.0239  608 HOH A O     
1838 O  O     . HOH E .   ? 0.4603 0.3401 0.3944 0.0564  -0.0497 0.1607  609 HOH A O     
1839 O  O     . HOH E .   ? 0.6405 0.5780 0.4664 -0.0240 -0.0268 -0.0170 610 HOH A O     
1840 O  O     . HOH E .   ? 0.4865 0.2944 0.4046 -0.0440 0.1996  -0.0006 611 HOH A O     
1841 O  O     . HOH E .   ? 0.4705 0.3228 0.6454 0.0572  -0.1414 -0.0903 612 HOH A O     
1842 O  O     . HOH E .   ? 0.8148 0.3005 0.7648 -0.1243 -0.1413 -0.0793 613 HOH A O     
1843 O  O     . HOH E .   ? 0.4583 0.3484 0.2698 -0.0116 -0.0492 0.0805  614 HOH A O     
1844 O  O     . HOH E .   ? 0.9662 0.3982 0.5957 -0.1858 -0.3935 0.1435  615 HOH A O     
1845 O  O     . HOH E .   ? 0.9243 0.6654 0.6355 -0.0641 0.0676  0.3796  616 HOH A O     
1846 O  O     . HOH E .   ? 0.1793 0.6130 0.1883 -0.0636 -0.0248 0.0704  617 HOH A O     
1847 O  O     . HOH E .   ? 0.5914 0.3949 0.5891 0.0736  -0.0640 0.1194  618 HOH A O     
1848 O  O     . HOH E .   ? 0.4744 0.4401 0.5882 -0.1580 0.0321  0.1753  619 HOH A O     
1849 O  O     . HOH E .   ? 0.6067 0.8154 0.3791 0.1955  -0.0483 0.0955  620 HOH A O     
1850 O  O     . HOH E .   ? 0.2969 0.1877 0.1842 0.0255  -0.0310 0.0303  621 HOH A O     
1851 O  O     . HOH E .   ? 0.3752 0.4005 0.3565 0.0502  -0.0949 0.0036  622 HOH A O     
1852 O  O     . HOH E .   ? 0.5146 0.6949 0.5008 -0.0512 -0.1763 0.1107  623 HOH A O     
1853 O  O     . HOH E .   ? 0.4379 0.4953 0.6419 0.0459  0.2874  -0.0210 624 HOH A O     
1854 O  O     . HOH E .   ? 0.6629 0.9513 0.5134 0.3167  -0.2351 -0.0548 625 HOH A O     
1855 O  O     . HOH E .   ? 0.8124 0.5545 0.4978 0.2402  -0.2498 -0.1918 626 HOH A O     
1856 O  O     . HOH E .   ? 0.6562 0.4280 0.4262 -0.2029 -0.1322 0.0328  627 HOH A O     
1857 O  O     . HOH E .   ? 0.6461 0.8257 0.6900 0.3907  0.2110  0.1109  628 HOH A O     
1858 O  O     . HOH E .   ? 0.2007 0.2148 0.1870 0.0164  0.0019  0.0416  629 HOH A O     
# 
