data_9JGC
# 
_entry.id   9JGC 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9JGC         pdb_00009jgc 10.2210/pdb9jgc/pdb 
WWPDB D_1300051275 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               '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 2 'Structure model' citation_author 
# 
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.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9JGC 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              spkanaujia@gmail.com 
_pdbx_contact_author.name_first         Shankar 
_pdbx_contact_author.name_last          Kanaujia 
_pdbx_contact_author.name_mi            P. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-9179-5723 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Saha, S.'       1 0000-0001-9937-2629 
'Kanaujia, S.P.' 2 0000-0001-9179-5723 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Febs J.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1742-464X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            292 
_citation.language                  ? 
_citation.page_first                2338 
_citation.page_last                 2358 
_citation.title                     
;Structural analysis of the ribosome assembly factor Nep1, an N1-specific pseudouridine methyltransferase, reveals mechanistic insights.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1111/febs.70005 
_citation.pdbx_database_id_PubMed   39918246 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Saha, S.'       1 ? 
primary 'Kanaujia, S.P.' 2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribosomal RNA small subunit methyltransferase Nep1' 26926.430 1   2.1.1.- ? ? ? 
2 non-polymer syn 'CHLORIDE ION'                                       35.453    1   ?       ? ? ? 
3 non-polymer syn ADENOSINE                                            267.241   1   ?       ? ? ? 
4 non-polymer syn 'SULFATE ION'                                        96.063    1   ?       ? ? ? 
5 non-polymer syn 'SULFITE ION'                                        80.063    2   ?       ? ? ? 
6 non-polymer syn 1,2-ETHANEDIOL                                       62.068    6   ?       ? ? ? 
7 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                              106.120   1   ?       ? ? ? 
8 water       nat water                                                18.015    141 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '16S rRNA (pseudouridine-N1-)-methyltransferase Nep1' 
# 
_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       
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_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 'CHLORIDE ION'          CL  
3 ADENOSINE               ADN 
4 'SULFATE ION'           SO4 
5 'SULFITE ION'           SO3 
6 1,2-ETHANEDIOL          EDO 
7 'DI(HYDROXYETHYL)ETHER' PEG 
8 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   GLU n 
1 3   GLU n 
1 4   LYS n 
1 5   LYS n 
1 6   ARG n 
1 7   LEU n 
1 8   HIS n 
1 9   LEU n 
1 10  ILE n 
1 11  ILE n 
1 12  ALA n 
1 13  ASP n 
1 14  ALA n 
1 15  GLU n 
1 16  LEU n 
1 17  GLU n 
1 18  THR n 
1 19  VAL n 
1 20  PRO n 
1 21  PRO n 
1 22  GLU n 
1 23  ILE n 
1 24  LEU n 
1 25  ASP n 
1 26  HIS n 
1 27  PRO n 
1 28  ALA n 
1 29  ILE n 
1 30  VAL n 
1 31  ASN n 
1 32  TYR n 
1 33  ALA n 
1 34  LYS n 
1 35  ARG n 
1 36  ARG n 
1 37  LYS n 
1 38  LYS n 
1 39  ARG n 
1 40  PRO n 
1 41  GLU n 
1 42  LYS n 
1 43  ILE n 
1 44  ILE n 
1 45  LEU n 
1 46  ASP n 
1 47  SER n 
1 48  THR n 
1 49  TYR n 
1 50  HIS n 
1 51  HIS n 
1 52  ALA n 
1 53  ALA n 
1 54  LEU n 
1 55  ARG n 
1 56  GLN n 
1 57  LEU n 
1 58  GLU n 
1 59  ASP n 
1 60  GLY n 
1 61  GLU n 
1 62  ARG n 
1 63  ARG n 
1 64  GLY n 
1 65  ARG n 
1 66  PRO n 
1 67  ASP n 
1 68  ILE n 
1 69  VAL n 
1 70  HIS n 
1 71  ILE n 
1 72  CYS n 
1 73  LEU n 
1 74  LEU n 
1 75  ASN n 
1 76  ALA n 
1 77  LEU n 
1 78  ASP n 
1 79  SER n 
1 80  ILE n 
1 81  LEU n 
1 82  ASN n 
1 83  LYS n 
1 84  GLU n 
1 85  ASP n 
1 86  ARG n 
1 87  LEU n 
1 88  ARG n 
1 89  VAL n 
1 90  TYR n 
1 91  VAL n 
1 92  HIS n 
1 93  THR n 
1 94  ARG n 
1 95  ASN n 
1 96  ASP n 
1 97  TYR n 
1 98  VAL n 
1 99  ILE n 
1 100 TYR n 
1 101 ILE n 
1 102 LYS n 
1 103 PRO n 
1 104 GLU n 
1 105 THR n 
1 106 ARG n 
1 107 LEU n 
1 108 PRO n 
1 109 ARG n 
1 110 ASN n 
1 111 TYR n 
1 112 ASN n 
1 113 ARG n 
1 114 PHE n 
1 115 ILE n 
1 116 GLY n 
1 117 LEU n 
1 118 MET n 
1 119 GLU n 
1 120 ASN n 
1 121 LEU n 
1 122 PHE n 
1 123 GLU n 
1 124 LYS n 
1 125 GLY n 
1 126 ALA n 
1 127 VAL n 
1 128 PRO n 
1 129 GLU n 
1 130 ASP n 
1 131 LEU n 
1 132 GLU n 
1 133 LEU n 
1 134 LEU n 
1 135 ARG n 
1 136 MET n 
1 137 GLU n 
1 138 LYS n 
1 139 LYS n 
1 140 THR n 
1 141 LEU n 
1 142 ASN n 
1 143 GLU n 
1 144 LEU n 
1 145 ILE n 
1 146 GLU n 
1 147 GLU n 
1 148 ILE n 
1 149 ASN n 
1 150 PRO n 
1 151 ASP n 
1 152 VAL n 
1 153 VAL n 
1 154 PHE n 
1 155 ILE n 
1 156 MET n 
1 157 HIS n 
1 158 GLU n 
1 159 GLU n 
1 160 GLY n 
1 161 GLU n 
1 162 LEU n 
1 163 MET n 
1 164 ILE n 
1 165 PRO n 
1 166 LYS n 
1 167 ASN n 
1 168 PHE n 
1 169 GLY n 
1 170 LYS n 
1 171 LEU n 
1 172 LEU n 
1 173 ASP n 
1 174 LYS n 
1 175 PHE n 
1 176 LYS n 
1 177 LYS n 
1 178 PRO n 
1 179 THR n 
1 180 VAL n 
1 181 ILE n 
1 182 VAL n 
1 183 GLY n 
1 184 GLY n 
1 185 PHE n 
1 186 PRO n 
1 187 HIS n 
1 188 GLY n 
1 189 ASP n 
1 190 PHE n 
1 191 LYS n 
1 192 SER n 
1 193 LYS n 
1 194 VAL n 
1 195 ASP n 
1 196 GLY n 
1 197 VAL n 
1 198 LYS n 
1 199 ILE n 
1 200 SER n 
1 201 LEU n 
1 202 TYR n 
1 203 ARG n 
1 204 GLU n 
1 205 PRO n 
1 206 LEU n 
1 207 MET n 
1 208 ALA n 
1 209 TRP n 
1 210 THR n 
1 211 ILE n 
1 212 VAL n 
1 213 ASN n 
1 214 GLU n 
1 215 VAL n 
1 216 ILE n 
1 217 VAL n 
1 218 SER n 
1 219 TYR n 
1 220 GLU n 
1 221 TRP n 
1 222 GLU n 
1 223 VAL n 
1 224 ILE n 
1 225 LYS n 
1 226 LYS n 
1 227 PHE n 
1 228 LYS n 
1 229 SER 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                   229 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nep1, PH1379' 
_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      'Pyrococcus horikoshii OT3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     70601 
_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              Rosetta 
_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 
ADN non-polymer         . ADENOSINE               ?                 'C10 H13 N5 O4'  267.241 
ALA 'L-peptide linking' y ALANINE                 ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ?                 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'          ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE                ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL          'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                 'C4 H10 O3'      106.120 
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 
SO3 non-polymer         . 'SULFITE ION'           ?                 'O3 S -2'        80.063  
SO4 non-polymer         . 'SULFATE ION'           ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE               ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLU 2   2   2   GLU GLU A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ARG 6   6   6   ARG ARG A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   HIS 8   8   8   HIS HIS A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ILE 10  10  10  ILE ILE A . n 
A 1 11  ILE 11  11  11  ILE ILE A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLU 15  15  15  GLU GLU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  LEU 24  24  24  LEU LEU A . n 
A 1 25  ASP 25  25  25  ASP ASP A . n 
A 1 26  HIS 26  26  26  HIS HIS A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  TYR 32  32  32  TYR TYR A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  ARG 35  35  35  ARG ARG A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  LYS 38  38  38  LYS LYS A . n 
A 1 39  ARG 39  39  39  ARG ARG A . n 
A 1 40  PRO 40  40  40  PRO PRO A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  LYS 42  42  42  LYS LYS A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASP 46  46  46  ASP ASP A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ARG 63  63  63  ARG ARG A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  ARG 65  65  65  ARG ARG A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  VAL 69  69  69  VAL VAL A . n 
A 1 70  HIS 70  70  70  HIS HIS A . n 
A 1 71  ILE 71  71  71  ILE ILE A . n 
A 1 72  CYS 72  72  72  CYS CYS A . n 
A 1 73  LEU 73  73  73  LEU LEU A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  ASP 78  78  78  ASP ASP A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  ASN 82  82  82  ASN ASN A . n 
A 1 83  LYS 83  83  83  LYS LYS A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  ARG 86  86  86  ARG ARG A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  HIS 92  92  92  HIS HIS A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  TYR 97  97  97  TYR TYR A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 ILE 101 101 101 ILE ILE A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 LEU 107 107 107 LEU LEU A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ASN 110 110 110 ASN ASN A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 ASN 112 112 112 ASN ASN A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 GLY 116 116 116 GLY GLY A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 MET 118 118 118 MET MET A . n 
A 1 119 GLU 119 119 119 GLU GLU A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 PRO 128 128 128 PRO PRO A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 LEU 131 131 131 LEU LEU A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLU 143 143 143 GLU GLU A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 ASN 149 149 149 ASN ASN A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 ASP 151 151 151 ASP ASP A . n 
A 1 152 VAL 152 152 152 VAL VAL A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 PHE 154 154 154 PHE PHE A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 MET 156 156 156 MET MET A . n 
A 1 157 HIS 157 157 157 HIS HIS A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 GLU 159 159 159 GLU GLU A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 MET 163 163 163 MET MET A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 LYS 170 170 170 LYS LYS A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ASP 173 173 173 ASP ASP A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 PRO 178 178 178 PRO PRO A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 VAL 182 182 182 VAL VAL A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 GLY 184 184 184 GLY GLY A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 PRO 186 186 186 PRO PRO A . n 
A 1 187 HIS 187 187 187 HIS HIS A . n 
A 1 188 GLY 188 188 188 GLY GLY A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 PHE 190 190 190 PHE PHE A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 SER 192 192 192 SER SER A . n 
A 1 193 LYS 193 193 193 LYS LYS A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 LYS 198 198 198 LYS LYS A . n 
A 1 199 ILE 199 199 199 ILE ILE A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 ARG 203 203 203 ARG ARG A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 LEU 206 206 206 LEU LEU A . n 
A 1 207 MET 207 207 207 MET MET A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 TRP 209 209 209 TRP TRP A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ILE 211 211 211 ILE ILE A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 GLU 214 214 214 GLU GLU A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ILE 216 216 216 ILE ILE A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 TYR 219 219 219 TYR TYR A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 TRP 221 221 221 TRP TRP A . n 
A 1 222 GLU 222 222 222 GLU GLU A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ILE 224 224 224 ILE ILE A . n 
A 1 225 LYS 225 225 225 LYS LYS A . n 
A 1 226 LYS 226 226 226 LYS LYS A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 LYS 228 228 ?   ?   ?   A . n 
A 1 229 SER 229 229 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ADN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ADN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CL  1   301 1   CL  CL  A . 
C 3 ADN 1   302 2   ADN ADN A . 
D 4 SO4 1   303 3   SO4 SO4 A . 
E 5 SO3 1   304 4   SO3 SO3 A . 
F 5 SO3 1   305 5   SO3 SO3 A . 
G 6 EDO 1   306 6   EDO EDO A . 
H 6 EDO 1   307 7   EDO EDO A . 
I 6 EDO 1   308 8   EDO EDO A . 
J 6 EDO 1   309 9   EDO EDO A . 
K 6 EDO 1   310 10  EDO EDO A . 
L 6 EDO 1   311 11  EDO EDO A . 
M 7 PEG 1   312 12  PEG PEG A . 
N 8 HOH 1   401 35  HOH HOH A . 
N 8 HOH 2   402 97  HOH HOH A . 
N 8 HOH 3   403 46  HOH HOH A . 
N 8 HOH 4   404 132 HOH HOH A . 
N 8 HOH 5   405 87  HOH HOH A . 
N 8 HOH 6   406 76  HOH HOH A . 
N 8 HOH 7   407 126 HOH HOH A . 
N 8 HOH 8   408 89  HOH HOH A . 
N 8 HOH 9   409 73  HOH HOH A . 
N 8 HOH 10  410 22  HOH HOH A . 
N 8 HOH 11  411 136 HOH HOH A . 
N 8 HOH 12  412 39  HOH HOH A . 
N 8 HOH 13  413 38  HOH HOH A . 
N 8 HOH 14  414 20  HOH HOH A . 
N 8 HOH 15  415 11  HOH HOH A . 
N 8 HOH 16  416 114 HOH HOH A . 
N 8 HOH 17  417 70  HOH HOH A . 
N 8 HOH 18  418 100 HOH HOH A . 
N 8 HOH 19  419 61  HOH HOH A . 
N 8 HOH 20  420 21  HOH HOH A . 
N 8 HOH 21  421 42  HOH HOH A . 
N 8 HOH 22  422 10  HOH HOH A . 
N 8 HOH 23  423 131 HOH HOH A . 
N 8 HOH 24  424 52  HOH HOH A . 
N 8 HOH 25  425 9   HOH HOH A . 
N 8 HOH 26  426 25  HOH HOH A . 
N 8 HOH 27  427 19  HOH HOH A . 
N 8 HOH 28  428 71  HOH HOH A . 
N 8 HOH 29  429 60  HOH HOH A . 
N 8 HOH 30  430 129 HOH HOH A . 
N 8 HOH 31  431 57  HOH HOH A . 
N 8 HOH 32  432 49  HOH HOH A . 
N 8 HOH 33  433 30  HOH HOH A . 
N 8 HOH 34  434 106 HOH HOH A . 
N 8 HOH 35  435 101 HOH HOH A . 
N 8 HOH 36  436 125 HOH HOH A . 
N 8 HOH 37  437 119 HOH HOH A . 
N 8 HOH 38  438 50  HOH HOH A . 
N 8 HOH 39  439 116 HOH HOH A . 
N 8 HOH 40  440 27  HOH HOH A . 
N 8 HOH 41  441 51  HOH HOH A . 
N 8 HOH 42  442 83  HOH HOH A . 
N 8 HOH 43  443 69  HOH HOH A . 
N 8 HOH 44  444 77  HOH HOH A . 
N 8 HOH 45  445 68  HOH HOH A . 
N 8 HOH 46  446 3   HOH HOH A . 
N 8 HOH 47  447 98  HOH HOH A . 
N 8 HOH 48  448 63  HOH HOH A . 
N 8 HOH 49  449 81  HOH HOH A . 
N 8 HOH 50  450 7   HOH HOH A . 
N 8 HOH 51  451 47  HOH HOH A . 
N 8 HOH 52  452 138 HOH HOH A . 
N 8 HOH 53  453 82  HOH HOH A . 
N 8 HOH 54  454 16  HOH HOH A . 
N 8 HOH 55  455 14  HOH HOH A . 
N 8 HOH 56  456 24  HOH HOH A . 
N 8 HOH 57  457 26  HOH HOH A . 
N 8 HOH 58  458 99  HOH HOH A . 
N 8 HOH 59  459 44  HOH HOH A . 
N 8 HOH 60  460 18  HOH HOH A . 
N 8 HOH 61  461 86  HOH HOH A . 
N 8 HOH 62  462 102 HOH HOH A . 
N 8 HOH 63  463 8   HOH HOH A . 
N 8 HOH 64  464 103 HOH HOH A . 
N 8 HOH 65  465 113 HOH HOH A . 
N 8 HOH 66  466 13  HOH HOH A . 
N 8 HOH 67  467 65  HOH HOH A . 
N 8 HOH 68  468 96  HOH HOH A . 
N 8 HOH 69  469 90  HOH HOH A . 
N 8 HOH 70  470 75  HOH HOH A . 
N 8 HOH 71  471 95  HOH HOH A . 
N 8 HOH 72  472 5   HOH HOH A . 
N 8 HOH 73  473 109 HOH HOH A . 
N 8 HOH 74  474 107 HOH HOH A . 
N 8 HOH 75  475 45  HOH HOH A . 
N 8 HOH 76  476 6   HOH HOH A . 
N 8 HOH 77  477 4   HOH HOH A . 
N 8 HOH 78  478 134 HOH HOH A . 
N 8 HOH 79  479 128 HOH HOH A . 
N 8 HOH 80  480 53  HOH HOH A . 
N 8 HOH 81  481 105 HOH HOH A . 
N 8 HOH 82  482 36  HOH HOH A . 
N 8 HOH 83  483 80  HOH HOH A . 
N 8 HOH 84  484 2   HOH HOH A . 
N 8 HOH 85  485 28  HOH HOH A . 
N 8 HOH 86  486 15  HOH HOH A . 
N 8 HOH 87  487 121 HOH HOH A . 
N 8 HOH 88  488 23  HOH HOH A . 
N 8 HOH 89  489 54  HOH HOH A . 
N 8 HOH 90  490 141 HOH HOH A . 
N 8 HOH 91  491 17  HOH HOH A . 
N 8 HOH 92  492 12  HOH HOH A . 
N 8 HOH 93  493 115 HOH HOH A . 
N 8 HOH 94  494 118 HOH HOH A . 
N 8 HOH 95  495 94  HOH HOH A . 
N 8 HOH 96  496 137 HOH HOH A . 
N 8 HOH 97  497 110 HOH HOH A . 
N 8 HOH 98  498 31  HOH HOH A . 
N 8 HOH 99  499 64  HOH HOH A . 
N 8 HOH 100 500 133 HOH HOH A . 
N 8 HOH 101 501 122 HOH HOH A . 
N 8 HOH 102 502 1   HOH HOH A . 
N 8 HOH 103 503 124 HOH HOH A . 
N 8 HOH 104 504 93  HOH HOH A . 
N 8 HOH 105 505 104 HOH HOH A . 
N 8 HOH 106 506 29  HOH HOH A . 
N 8 HOH 107 507 40  HOH HOH A . 
N 8 HOH 108 508 108 HOH HOH A . 
N 8 HOH 109 509 66  HOH HOH A . 
N 8 HOH 110 510 33  HOH HOH A . 
N 8 HOH 111 511 92  HOH HOH A . 
N 8 HOH 112 512 79  HOH HOH A . 
N 8 HOH 113 513 78  HOH HOH A . 
N 8 HOH 114 514 111 HOH HOH A . 
N 8 HOH 115 515 135 HOH HOH A . 
N 8 HOH 116 516 43  HOH HOH A . 
N 8 HOH 117 517 48  HOH HOH A . 
N 8 HOH 118 518 67  HOH HOH A . 
N 8 HOH 119 519 84  HOH HOH A . 
N 8 HOH 120 520 41  HOH HOH A . 
N 8 HOH 121 521 123 HOH HOH A . 
N 8 HOH 122 522 62  HOH HOH A . 
N 8 HOH 123 523 32  HOH HOH A . 
N 8 HOH 124 524 55  HOH HOH A . 
N 8 HOH 125 525 85  HOH HOH A . 
N 8 HOH 126 526 59  HOH HOH A . 
N 8 HOH 127 527 56  HOH HOH A . 
N 8 HOH 128 528 34  HOH HOH A . 
N 8 HOH 129 529 112 HOH HOH A . 
N 8 HOH 130 530 74  HOH HOH A . 
N 8 HOH 131 531 117 HOH HOH A . 
N 8 HOH 132 532 130 HOH HOH A . 
N 8 HOH 133 533 120 HOH HOH A . 
N 8 HOH 134 534 72  HOH HOH A . 
N 8 HOH 135 535 37  HOH HOH A . 
N 8 HOH 136 536 127 HOH HOH A . 
N 8 HOH 137 537 140 HOH HOH A . 
N 8 HOH 138 538 139 HOH HOH A . 
N 8 HOH 139 539 58  HOH HOH A . 
N 8 HOH 140 540 88  HOH HOH A . 
N 8 HOH 141 541 91  HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data collection' ? ? ? ? ? ? ? ? ? ? ? HKL-3000    ? ? ? 3000     1 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? 7.4.0    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.9    3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? 2.8.3    4 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? 0.9.4.1  6 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 4.2      7 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JGC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.410 
_cell.length_a_esd                 ? 
_cell.length_b                     113.410 
_cell.length_b_esd                 ? 
_cell.length_c                     102.180 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        18 
_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                         9JGC 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3 2' 
_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                   9JGC 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47 
_exptl_crystal.description                  Trigonal 
_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          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_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    '0.1M sodium chloride, 0.1M HEPES pH 7.5, 1.6M ammonium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      'VariMax HF' 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JGC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.01 
_reflns.d_resolution_low                               70.81 
_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                                     17065 
_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                                14.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.02 
_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                                0.100 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       246585 
_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                              0.096 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.01 
_reflns_shell.d_res_low                                     2.06 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           16745 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1245 
_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                               13.4 
_reflns_shell.pdbx_chi_squared                              0.92 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     6.0 
_reflns_shell.pdbx_Rrim_I_all                               0.504 
_reflns_shell.pdbx_Rpim_I_all                               0.137 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.965 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.484 
_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]                            -1.00 
_refine.aniso_B[1][2]                            -0.50 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -1.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            3.24 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.296 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JGC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.01 
_refine.ls_d_res_low                             70.81 
_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                     16216 
_refine.ls_number_reflns_R_free                  848 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    100.00 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16042 
_refine.ls_R_factor_R_free                       0.20933 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15792 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.166 
_refine.pdbx_overall_ESU_R_Free                  0.153 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             6.720 
_refine.overall_SU_ML                            0.099 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.01 
_refine_hist.d_res_low                        70.81 
_refine_hist.number_atoms_solvent             141 
_refine_hist.number_atoms_total               2076 
_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        1871 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         64 
_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' ? 0.008  0.012  1973 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  1953 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.472  1.672  2650 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.515  1.582  4509 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.553  5.000  227  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.899 5.000  16   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.192 10.000 373  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.074  0.200  294  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  2209 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  420  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.779  1.701  905  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.765  1.701  905  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.857  3.041  1130 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.856  3.043  1131 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.002  2.256  1068 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.001  2.260  1069 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.732  3.866  1520 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.890  19.66  2289 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.870  19.18  2262 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.01 
_refine_ls_shell.d_res_low                        2.058 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             49 
_refine_ls_shell.number_reflns_R_work             1195 
_refine_ls_shell.percent_reflns_obs               100.00 
_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                  0.181 
_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                  0.233 
# 
_struct.entry_id                     9JGC 
_struct.title                        'Crystal structure of Nep1 in complex with adenosine from Pyrococcus horikoshii OT3' 
_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        9JGC 
_struct_keywords.text            
;Conserved arginine residues, Globular loop extension, Inter-subunit interactions, Nep1, N1-pseudouridine methyltransferase, Trefoil knot, TRANSFERASE
;
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 6 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 7 ? 
N N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NEP1_PYRHO 
_struct_ref.pdbx_db_accession          O50087 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MEEKKRLHLIIADAELETVPPEILDHPAIVNYAKRRKKRPEKIILDSTYHHAALRQLEDGERRGRPDIVHICLLNALDSI
LNKEDRLRVYVHTRNDYVIYIKPETRLPRNYNRFIGLMENLFEKGAVPEDLELLRMEKKTLNELIEEINPDVVFIMHEEG
ELMIPKNFGKLLDKFKKPTVIVGGFPHGDFKSKVDGVKISLYREPLMAWTIVNEVIVSYEWEVIKKFKS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JGC 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 229 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O50087 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  229 
_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       229 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 8880  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  18930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z                  1.0000000000  0.0000000000  0.0000000000 0.0000000000  0.0000000000  
1.0000000000 0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 12_555 -x+2/3,-x+y+1/3,-z+1/3 -0.5000000000 -0.8660254038 0.0000000000 56.7050000000 -0.8660254038 
0.5000000000 0.0000000000 32.7386470144 0.0000000000 0.0000000000 -1.0000000000 34.0600000000 
# 
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 PRO A 20  ? LEU A 24  ? PRO A 20  LEU A 24  5 ? 5  
HELX_P HELX_P2  AA2 HIS A 26  ? LYS A 37  ? HIS A 26  LYS A 37  1 ? 12 
HELX_P HELX_P3  AA3 ARG A 39  ? ILE A 43  ? ARG A 39  ILE A 43  5 ? 5  
HELX_P HELX_P4  AA4 ASP A 46  ? ARG A 55  ? ASP A 46  ARG A 55  1 ? 10 
HELX_P HELX_P5  AA5 ARG A 65  ? ASP A 78  ? ARG A 65  ASP A 78  1 ? 14 
HELX_P HELX_P6  AA6 SER A 79  ? GLU A 84  ? SER A 79  GLU A 84  1 ? 6  
HELX_P HELX_P7  AA7 ASN A 110 ? GLY A 125 ? ASN A 110 GLY A 125 1 ? 16 
HELX_P HELX_P8  AA8 THR A 140 ? ASN A 149 ? THR A 140 ASN A 149 1 ? 10 
HELX_P HELX_P9  AA9 ILE A 164 ? ASP A 173 ? ILE A 164 ASP A 173 1 ? 10 
HELX_P HELX_P10 AB1 MET A 207 ? ILE A 224 ? MET A 207 ILE A 224 1 ? 18 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          VAL 
_struct_mon_prot_cis.label_seq_id           127 
_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           VAL 
_struct_mon_prot_cis.auth_seq_id            127 
_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    128 
_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     128 
_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       -17.09 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? 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 ALA A 126 ? VAL A 127 ? ALA A 126 VAL A 127 
AA1 2 LEU A 134 ? LYS A 138 ? LEU A 134 LYS A 138 
AA1 3 TYR A 97  ? ILE A 101 ? TYR A 97  ILE A 101 
AA1 4 LEU A 87  ? THR A 93  ? LEU A 87  THR A 93  
AA1 5 LEU A 7   ? ALA A 14  ? LEU A 7   ALA A 14  
AA1 6 THR A 179 ? GLY A 183 ? THR A 179 GLY A 183 
AA1 7 VAL A 153 ? MET A 156 ? VAL A 153 MET A 156 
AA1 8 VAL A 197 ? SER A 200 ? VAL A 197 SER A 200 
AA1 9 GLU A 161 ? LEU A 162 ? GLU A 161 LEU A 162 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 127 ? N VAL A 127 O LEU A 134 ? O LEU A 134 
AA1 2 3 O ARG A 135 ? O ARG A 135 N TYR A 100 ? N TYR A 100 
AA1 3 4 O ILE A 99  ? O ILE A 99  N VAL A 91  ? N VAL A 91  
AA1 4 5 O ARG A 88  ? O ARG A 88  N LEU A 9   ? N LEU A 9   
AA1 5 6 N ILE A 10  ? N ILE A 10  O VAL A 180 ? O VAL A 180 
AA1 6 7 O THR A 179 ? O THR A 179 N PHE A 154 ? N PHE A 154 
AA1 7 8 N VAL A 153 ? N VAL A 153 O VAL A 197 ? O VAL A 197 
AA1 8 9 O LYS A 198 ? O LYS A 198 N GLU A 161 ? N GLU A 161 
# 
_pdbx_entry_details.entry_id                   9JGC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 434 ? ? O A HOH 481 ? ? 2.10 
2 1 OE2 A GLU 2   ? ? O A HOH 401 ? ? 2.18 
3 1 O   A HOH 467 ? ? O A HOH 521 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 445 ? ? 1_555 O A HOH 445 ? ? 12_555 1.83 
2 1 O A HOH 537 ? ? 1_555 O A HOH 537 ? ? 5_555  2.10 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE A ARG 109 ? ? CZ A ARG 109 ? ? NH1 A ARG 109 ? ? 116.51 120.30 -3.79 0.50 N 
2 1 NE A ARG 109 ? ? CZ A ARG 109 ? ? NH2 A ARG 109 ? ? 123.37 120.30 3.07  0.50 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 139 ? ? -172.86 134.26 
2 1 LYS A 177 ? ? -148.44 52.76  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 62  ? ? 0.095 'SIDE CHAIN' 
2 1 ARG A 65  ? ? 0.090 'SIDE CHAIN' 
3 1 ARG A 109 ? ? 0.206 'SIDE CHAIN' 
4 1 ARG A 203 ? ? 0.161 'SIDE CHAIN' 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 501 ? N HOH . 
2 1 A HOH 512 ? N HOH . 
3 1 A HOH 529 ? N HOH . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         18.8420 
_pdbx_refine_tls.origin_y         8.3209 
_pdbx_refine_tls.origin_z         18.9153 
_pdbx_refine_tls.T[1][1]          0.0669 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0188 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0221 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1177 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0013 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0155 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.8002 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.2277 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1134 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.4032 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.1403 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.3401 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0127 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1337 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0430 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0058 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0338 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0570 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0061 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0614 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0211 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     2 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     227 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 1   ? A MET 1   
2 1 Y 1 A LYS 228 ? A LYS 228 
3 1 Y 1 A SER 229 ? A SER 229 
# 
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 
ADN "O5'"  O  N N 1   
ADN "C5'"  C  N N 2   
ADN "C4'"  C  N R 3   
ADN "O4'"  O  N N 4   
ADN "C3'"  C  N S 5   
ADN "O3'"  O  N N 6   
ADN "C2'"  C  N R 7   
ADN "O2'"  O  N N 8   
ADN "C1'"  C  N R 9   
ADN N9     N  Y N 10  
ADN C8     C  Y N 11  
ADN N7     N  Y N 12  
ADN C5     C  Y N 13  
ADN C6     C  Y N 14  
ADN N6     N  N N 15  
ADN N1     N  Y N 16  
ADN C2     C  Y N 17  
ADN N3     N  Y N 18  
ADN C4     C  Y N 19  
ADN "HO5'" H  N N 20  
ADN "H5'1" H  N N 21  
ADN "H5'2" H  N N 22  
ADN "H4'"  H  N N 23  
ADN "H3'"  H  N N 24  
ADN "HO3'" H  N N 25  
ADN "H2'"  H  N N 26  
ADN "HO2'" H  N N 27  
ADN "H1'"  H  N N 28  
ADN H8     H  N N 29  
ADN HN61   H  N N 30  
ADN HN62   H  N N 31  
ADN H2     H  N N 32  
ALA N      N  N N 33  
ALA CA     C  N S 34  
ALA C      C  N N 35  
ALA O      O  N N 36  
ALA CB     C  N N 37  
ALA OXT    O  N N 38  
ALA H      H  N N 39  
ALA H2     H  N N 40  
ALA HA     H  N N 41  
ALA HB1    H  N N 42  
ALA HB2    H  N N 43  
ALA HB3    H  N N 44  
ALA HXT    H  N N 45  
ARG N      N  N N 46  
ARG CA     C  N S 47  
ARG C      C  N N 48  
ARG O      O  N N 49  
ARG CB     C  N N 50  
ARG CG     C  N N 51  
ARG CD     C  N N 52  
ARG NE     N  N N 53  
ARG CZ     C  N N 54  
ARG NH1    N  N N 55  
ARG NH2    N  N N 56  
ARG OXT    O  N N 57  
ARG H      H  N N 58  
ARG H2     H  N N 59  
ARG HA     H  N N 60  
ARG HB2    H  N N 61  
ARG HB3    H  N N 62  
ARG HG2    H  N N 63  
ARG HG3    H  N N 64  
ARG HD2    H  N N 65  
ARG HD3    H  N N 66  
ARG HE     H  N N 67  
ARG HH11   H  N N 68  
ARG HH12   H  N N 69  
ARG HH21   H  N N 70  
ARG HH22   H  N N 71  
ARG HXT    H  N N 72  
ASN N      N  N N 73  
ASN CA     C  N S 74  
ASN C      C  N N 75  
ASN O      O  N N 76  
ASN CB     C  N N 77  
ASN CG     C  N N 78  
ASN OD1    O  N N 79  
ASN ND2    N  N N 80  
ASN OXT    O  N N 81  
ASN H      H  N N 82  
ASN H2     H  N N 83  
ASN HA     H  N N 84  
ASN HB2    H  N N 85  
ASN HB3    H  N N 86  
ASN HD21   H  N N 87  
ASN HD22   H  N N 88  
ASN HXT    H  N N 89  
ASP N      N  N N 90  
ASP CA     C  N S 91  
ASP C      C  N N 92  
ASP O      O  N N 93  
ASP CB     C  N N 94  
ASP CG     C  N N 95  
ASP OD1    O  N N 96  
ASP OD2    O  N N 97  
ASP OXT    O  N N 98  
ASP H      H  N N 99  
ASP H2     H  N N 100 
ASP HA     H  N N 101 
ASP HB2    H  N N 102 
ASP HB3    H  N N 103 
ASP HD2    H  N N 104 
ASP HXT    H  N N 105 
CL  CL     CL N N 106 
CYS N      N  N N 107 
CYS CA     C  N R 108 
CYS C      C  N N 109 
CYS O      O  N N 110 
CYS CB     C  N N 111 
CYS SG     S  N N 112 
CYS OXT    O  N N 113 
CYS H      H  N N 114 
CYS H2     H  N N 115 
CYS HA     H  N N 116 
CYS HB2    H  N N 117 
CYS HB3    H  N N 118 
CYS HG     H  N N 119 
CYS HXT    H  N N 120 
EDO C1     C  N N 121 
EDO O1     O  N N 122 
EDO C2     C  N N 123 
EDO O2     O  N N 124 
EDO H11    H  N N 125 
EDO H12    H  N N 126 
EDO HO1    H  N N 127 
EDO H21    H  N N 128 
EDO H22    H  N N 129 
EDO HO2    H  N N 130 
GLN N      N  N N 131 
GLN CA     C  N S 132 
GLN C      C  N N 133 
GLN O      O  N N 134 
GLN CB     C  N N 135 
GLN CG     C  N N 136 
GLN CD     C  N N 137 
GLN OE1    O  N N 138 
GLN NE2    N  N N 139 
GLN OXT    O  N N 140 
GLN H      H  N N 141 
GLN H2     H  N N 142 
GLN HA     H  N N 143 
GLN HB2    H  N N 144 
GLN HB3    H  N N 145 
GLN HG2    H  N N 146 
GLN HG3    H  N N 147 
GLN HE21   H  N N 148 
GLN HE22   H  N N 149 
GLN HXT    H  N N 150 
GLU N      N  N N 151 
GLU CA     C  N S 152 
GLU C      C  N N 153 
GLU O      O  N N 154 
GLU CB     C  N N 155 
GLU CG     C  N N 156 
GLU CD     C  N N 157 
GLU OE1    O  N N 158 
GLU OE2    O  N N 159 
GLU OXT    O  N N 160 
GLU H      H  N N 161 
GLU H2     H  N N 162 
GLU HA     H  N N 163 
GLU HB2    H  N N 164 
GLU HB3    H  N N 165 
GLU HG2    H  N N 166 
GLU HG3    H  N N 167 
GLU HE2    H  N N 168 
GLU HXT    H  N N 169 
GLY N      N  N N 170 
GLY CA     C  N N 171 
GLY C      C  N N 172 
GLY O      O  N N 173 
GLY OXT    O  N N 174 
GLY H      H  N N 175 
GLY H2     H  N N 176 
GLY HA2    H  N N 177 
GLY HA3    H  N N 178 
GLY HXT    H  N N 179 
HIS N      N  N N 180 
HIS CA     C  N S 181 
HIS C      C  N N 182 
HIS O      O  N N 183 
HIS CB     C  N N 184 
HIS CG     C  Y N 185 
HIS ND1    N  Y N 186 
HIS CD2    C  Y N 187 
HIS CE1    C  Y N 188 
HIS NE2    N  Y N 189 
HIS OXT    O  N N 190 
HIS H      H  N N 191 
HIS H2     H  N N 192 
HIS HA     H  N N 193 
HIS HB2    H  N N 194 
HIS HB3    H  N N 195 
HIS HD1    H  N N 196 
HIS HD2    H  N N 197 
HIS HE1    H  N N 198 
HIS HE2    H  N N 199 
HIS HXT    H  N N 200 
HOH O      O  N N 201 
HOH H1     H  N N 202 
HOH H2     H  N N 203 
ILE N      N  N N 204 
ILE CA     C  N S 205 
ILE C      C  N N 206 
ILE O      O  N N 207 
ILE CB     C  N S 208 
ILE CG1    C  N N 209 
ILE CG2    C  N N 210 
ILE CD1    C  N N 211 
ILE OXT    O  N N 212 
ILE H      H  N N 213 
ILE H2     H  N N 214 
ILE HA     H  N N 215 
ILE HB     H  N N 216 
ILE HG12   H  N N 217 
ILE HG13   H  N N 218 
ILE HG21   H  N N 219 
ILE HG22   H  N N 220 
ILE HG23   H  N N 221 
ILE HD11   H  N N 222 
ILE HD12   H  N N 223 
ILE HD13   H  N N 224 
ILE HXT    H  N N 225 
LEU N      N  N N 226 
LEU CA     C  N S 227 
LEU C      C  N N 228 
LEU O      O  N N 229 
LEU CB     C  N N 230 
LEU CG     C  N N 231 
LEU CD1    C  N N 232 
LEU CD2    C  N N 233 
LEU OXT    O  N N 234 
LEU H      H  N N 235 
LEU H2     H  N N 236 
LEU HA     H  N N 237 
LEU HB2    H  N N 238 
LEU HB3    H  N N 239 
LEU HG     H  N N 240 
LEU HD11   H  N N 241 
LEU HD12   H  N N 242 
LEU HD13   H  N N 243 
LEU HD21   H  N N 244 
LEU HD22   H  N N 245 
LEU HD23   H  N N 246 
LEU HXT    H  N N 247 
LYS N      N  N N 248 
LYS CA     C  N S 249 
LYS C      C  N N 250 
LYS O      O  N N 251 
LYS CB     C  N N 252 
LYS CG     C  N N 253 
LYS CD     C  N N 254 
LYS CE     C  N N 255 
LYS NZ     N  N N 256 
LYS OXT    O  N N 257 
LYS H      H  N N 258 
LYS H2     H  N N 259 
LYS HA     H  N N 260 
LYS HB2    H  N N 261 
LYS HB3    H  N N 262 
LYS HG2    H  N N 263 
LYS HG3    H  N N 264 
LYS HD2    H  N N 265 
LYS HD3    H  N N 266 
LYS HE2    H  N N 267 
LYS HE3    H  N N 268 
LYS HZ1    H  N N 269 
LYS HZ2    H  N N 270 
LYS HZ3    H  N N 271 
LYS HXT    H  N N 272 
MET N      N  N N 273 
MET CA     C  N S 274 
MET C      C  N N 275 
MET O      O  N N 276 
MET CB     C  N N 277 
MET CG     C  N N 278 
MET SD     S  N N 279 
MET CE     C  N N 280 
MET OXT    O  N N 281 
MET H      H  N N 282 
MET H2     H  N N 283 
MET HA     H  N N 284 
MET HB2    H  N N 285 
MET HB3    H  N N 286 
MET HG2    H  N N 287 
MET HG3    H  N N 288 
MET HE1    H  N N 289 
MET HE2    H  N N 290 
MET HE3    H  N N 291 
MET HXT    H  N N 292 
PEG C1     C  N N 293 
PEG O1     O  N N 294 
PEG C2     C  N N 295 
PEG O2     O  N N 296 
PEG C3     C  N N 297 
PEG C4     C  N N 298 
PEG O4     O  N N 299 
PEG H11    H  N N 300 
PEG H12    H  N N 301 
PEG HO1    H  N N 302 
PEG H21    H  N N 303 
PEG H22    H  N N 304 
PEG H31    H  N N 305 
PEG H32    H  N N 306 
PEG H41    H  N N 307 
PEG H42    H  N N 308 
PEG HO4    H  N N 309 
PHE N      N  N N 310 
PHE CA     C  N S 311 
PHE C      C  N N 312 
PHE O      O  N N 313 
PHE CB     C  N N 314 
PHE CG     C  Y N 315 
PHE CD1    C  Y N 316 
PHE CD2    C  Y N 317 
PHE CE1    C  Y N 318 
PHE CE2    C  Y N 319 
PHE CZ     C  Y N 320 
PHE OXT    O  N N 321 
PHE H      H  N N 322 
PHE H2     H  N N 323 
PHE HA     H  N N 324 
PHE HB2    H  N N 325 
PHE HB3    H  N N 326 
PHE HD1    H  N N 327 
PHE HD2    H  N N 328 
PHE HE1    H  N N 329 
PHE HE2    H  N N 330 
PHE HZ     H  N N 331 
PHE HXT    H  N N 332 
PRO N      N  N N 333 
PRO CA     C  N S 334 
PRO C      C  N N 335 
PRO O      O  N N 336 
PRO CB     C  N N 337 
PRO CG     C  N N 338 
PRO CD     C  N N 339 
PRO OXT    O  N N 340 
PRO H      H  N N 341 
PRO HA     H  N N 342 
PRO HB2    H  N N 343 
PRO HB3    H  N N 344 
PRO HG2    H  N N 345 
PRO HG3    H  N N 346 
PRO HD2    H  N N 347 
PRO HD3    H  N N 348 
PRO HXT    H  N N 349 
SER N      N  N N 350 
SER CA     C  N S 351 
SER C      C  N N 352 
SER O      O  N N 353 
SER CB     C  N N 354 
SER OG     O  N N 355 
SER OXT    O  N N 356 
SER H      H  N N 357 
SER H2     H  N N 358 
SER HA     H  N N 359 
SER HB2    H  N N 360 
SER HB3    H  N N 361 
SER HG     H  N N 362 
SER HXT    H  N N 363 
SO3 S      S  N N 364 
SO3 O1     O  N N 365 
SO3 O2     O  N N 366 
SO3 O3     O  N N 367 
SO4 S      S  N N 368 
SO4 O1     O  N N 369 
SO4 O2     O  N N 370 
SO4 O3     O  N N 371 
SO4 O4     O  N N 372 
THR N      N  N N 373 
THR CA     C  N S 374 
THR C      C  N N 375 
THR O      O  N N 376 
THR CB     C  N R 377 
THR OG1    O  N N 378 
THR CG2    C  N N 379 
THR OXT    O  N N 380 
THR H      H  N N 381 
THR H2     H  N N 382 
THR HA     H  N N 383 
THR HB     H  N N 384 
THR HG1    H  N N 385 
THR HG21   H  N N 386 
THR HG22   H  N N 387 
THR HG23   H  N N 388 
THR HXT    H  N N 389 
TRP N      N  N N 390 
TRP CA     C  N S 391 
TRP C      C  N N 392 
TRP O      O  N N 393 
TRP CB     C  N N 394 
TRP CG     C  Y N 395 
TRP CD1    C  Y N 396 
TRP CD2    C  Y N 397 
TRP NE1    N  Y N 398 
TRP CE2    C  Y N 399 
TRP CE3    C  Y N 400 
TRP CZ2    C  Y N 401 
TRP CZ3    C  Y N 402 
TRP CH2    C  Y N 403 
TRP OXT    O  N N 404 
TRP H      H  N N 405 
TRP H2     H  N N 406 
TRP HA     H  N N 407 
TRP HB2    H  N N 408 
TRP HB3    H  N N 409 
TRP HD1    H  N N 410 
TRP HE1    H  N N 411 
TRP HE3    H  N N 412 
TRP HZ2    H  N N 413 
TRP HZ3    H  N N 414 
TRP HH2    H  N N 415 
TRP HXT    H  N N 416 
TYR N      N  N N 417 
TYR CA     C  N S 418 
TYR C      C  N N 419 
TYR O      O  N N 420 
TYR CB     C  N N 421 
TYR CG     C  Y N 422 
TYR CD1    C  Y N 423 
TYR CD2    C  Y N 424 
TYR CE1    C  Y N 425 
TYR CE2    C  Y N 426 
TYR CZ     C  Y N 427 
TYR OH     O  N N 428 
TYR OXT    O  N N 429 
TYR H      H  N N 430 
TYR H2     H  N N 431 
TYR HA     H  N N 432 
TYR HB2    H  N N 433 
TYR HB3    H  N N 434 
TYR HD1    H  N N 435 
TYR HD2    H  N N 436 
TYR HE1    H  N N 437 
TYR HE2    H  N N 438 
TYR HH     H  N N 439 
TYR HXT    H  N N 440 
VAL N      N  N N 441 
VAL CA     C  N S 442 
VAL C      C  N N 443 
VAL O      O  N N 444 
VAL CB     C  N N 445 
VAL CG1    C  N N 446 
VAL CG2    C  N N 447 
VAL OXT    O  N N 448 
VAL H      H  N N 449 
VAL H2     H  N N 450 
VAL HA     H  N N 451 
VAL HB     H  N N 452 
VAL HG11   H  N N 453 
VAL HG12   H  N N 454 
VAL HG13   H  N N 455 
VAL HG21   H  N N 456 
VAL HG22   H  N N 457 
VAL HG23   H  N N 458 
VAL HXT    H  N N 459 
# 
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 
ADN "O5'" "C5'"  sing N N 1   
ADN "O5'" "HO5'" sing N N 2   
ADN "C5'" "C4'"  sing N N 3   
ADN "C5'" "H5'1" sing N N 4   
ADN "C5'" "H5'2" sing N N 5   
ADN "C4'" "O4'"  sing N N 6   
ADN "C4'" "C3'"  sing N N 7   
ADN "C4'" "H4'"  sing N N 8   
ADN "O4'" "C1'"  sing N N 9   
ADN "C3'" "O3'"  sing N N 10  
ADN "C3'" "C2'"  sing N N 11  
ADN "C3'" "H3'"  sing N N 12  
ADN "O3'" "HO3'" sing N N 13  
ADN "C2'" "O2'"  sing N N 14  
ADN "C2'" "C1'"  sing N N 15  
ADN "C2'" "H2'"  sing N N 16  
ADN "O2'" "HO2'" sing N N 17  
ADN "C1'" N9     sing N N 18  
ADN "C1'" "H1'"  sing N N 19  
ADN N9    C8     sing Y N 20  
ADN N9    C4     sing Y N 21  
ADN C8    N7     doub Y N 22  
ADN C8    H8     sing N N 23  
ADN N7    C5     sing Y N 24  
ADN C5    C6     sing Y N 25  
ADN C5    C4     doub Y N 26  
ADN C6    N6     sing N N 27  
ADN C6    N1     doub Y N 28  
ADN N6    HN61   sing N N 29  
ADN N6    HN62   sing N N 30  
ADN N1    C2     sing Y N 31  
ADN C2    N3     doub Y N 32  
ADN C2    H2     sing N N 33  
ADN N3    C4     sing Y N 34  
ALA N     CA     sing N N 35  
ALA N     H      sing N N 36  
ALA N     H2     sing N N 37  
ALA CA    C      sing N N 38  
ALA CA    CB     sing N N 39  
ALA CA    HA     sing N N 40  
ALA C     O      doub N N 41  
ALA C     OXT    sing N N 42  
ALA CB    HB1    sing N N 43  
ALA CB    HB2    sing N N 44  
ALA CB    HB3    sing N N 45  
ALA OXT   HXT    sing N N 46  
ARG N     CA     sing N N 47  
ARG N     H      sing N N 48  
ARG N     H2     sing N N 49  
ARG CA    C      sing N N 50  
ARG CA    CB     sing N N 51  
ARG CA    HA     sing N N 52  
ARG C     O      doub N N 53  
ARG C     OXT    sing N N 54  
ARG CB    CG     sing N N 55  
ARG CB    HB2    sing N N 56  
ARG CB    HB3    sing N N 57  
ARG CG    CD     sing N N 58  
ARG CG    HG2    sing N N 59  
ARG CG    HG3    sing N N 60  
ARG CD    NE     sing N N 61  
ARG CD    HD2    sing N N 62  
ARG CD    HD3    sing N N 63  
ARG NE    CZ     sing N N 64  
ARG NE    HE     sing N N 65  
ARG CZ    NH1    sing N N 66  
ARG CZ    NH2    doub N N 67  
ARG NH1   HH11   sing N N 68  
ARG NH1   HH12   sing N N 69  
ARG NH2   HH21   sing N N 70  
ARG NH2   HH22   sing N N 71  
ARG OXT   HXT    sing N N 72  
ASN N     CA     sing N N 73  
ASN N     H      sing N N 74  
ASN N     H2     sing N N 75  
ASN CA    C      sing N N 76  
ASN CA    CB     sing N N 77  
ASN CA    HA     sing N N 78  
ASN C     O      doub N N 79  
ASN C     OXT    sing N N 80  
ASN CB    CG     sing N N 81  
ASN CB    HB2    sing N N 82  
ASN CB    HB3    sing N N 83  
ASN CG    OD1    doub N N 84  
ASN CG    ND2    sing N N 85  
ASN ND2   HD21   sing N N 86  
ASN ND2   HD22   sing N N 87  
ASN OXT   HXT    sing N N 88  
ASP N     CA     sing N N 89  
ASP N     H      sing N N 90  
ASP N     H2     sing N N 91  
ASP CA    C      sing N N 92  
ASP CA    CB     sing N N 93  
ASP CA    HA     sing N N 94  
ASP C     O      doub N N 95  
ASP C     OXT    sing N N 96  
ASP CB    CG     sing N N 97  
ASP CB    HB2    sing N N 98  
ASP CB    HB3    sing N N 99  
ASP CG    OD1    doub N N 100 
ASP CG    OD2    sing N N 101 
ASP OD2   HD2    sing N N 102 
ASP OXT   HXT    sing N N 103 
CYS N     CA     sing N N 104 
CYS N     H      sing N N 105 
CYS N     H2     sing N N 106 
CYS CA    C      sing N N 107 
CYS CA    CB     sing N N 108 
CYS CA    HA     sing N N 109 
CYS C     O      doub N N 110 
CYS C     OXT    sing N N 111 
CYS CB    SG     sing N N 112 
CYS CB    HB2    sing N N 113 
CYS CB    HB3    sing N N 114 
CYS SG    HG     sing N N 115 
CYS OXT   HXT    sing N N 116 
EDO C1    O1     sing N N 117 
EDO C1    C2     sing N N 118 
EDO C1    H11    sing N N 119 
EDO C1    H12    sing N N 120 
EDO O1    HO1    sing N N 121 
EDO C2    O2     sing N N 122 
EDO C2    H21    sing N N 123 
EDO C2    H22    sing N N 124 
EDO O2    HO2    sing N N 125 
GLN N     CA     sing N N 126 
GLN N     H      sing N N 127 
GLN N     H2     sing N N 128 
GLN CA    C      sing N N 129 
GLN CA    CB     sing N N 130 
GLN CA    HA     sing N N 131 
GLN C     O      doub N N 132 
GLN C     OXT    sing N N 133 
GLN CB    CG     sing N N 134 
GLN CB    HB2    sing N N 135 
GLN CB    HB3    sing N N 136 
GLN CG    CD     sing N N 137 
GLN CG    HG2    sing N N 138 
GLN CG    HG3    sing N N 139 
GLN CD    OE1    doub N N 140 
GLN CD    NE2    sing N N 141 
GLN NE2   HE21   sing N N 142 
GLN NE2   HE22   sing N N 143 
GLN OXT   HXT    sing N N 144 
GLU N     CA     sing N N 145 
GLU N     H      sing N N 146 
GLU N     H2     sing N N 147 
GLU CA    C      sing N N 148 
GLU CA    CB     sing N N 149 
GLU CA    HA     sing N N 150 
GLU C     O      doub N N 151 
GLU C     OXT    sing N N 152 
GLU CB    CG     sing N N 153 
GLU CB    HB2    sing N N 154 
GLU CB    HB3    sing N N 155 
GLU CG    CD     sing N N 156 
GLU CG    HG2    sing N N 157 
GLU CG    HG3    sing N N 158 
GLU CD    OE1    doub N N 159 
GLU CD    OE2    sing N N 160 
GLU OE2   HE2    sing N N 161 
GLU OXT   HXT    sing N N 162 
GLY N     CA     sing N N 163 
GLY N     H      sing N N 164 
GLY N     H2     sing N N 165 
GLY CA    C      sing N N 166 
GLY CA    HA2    sing N N 167 
GLY CA    HA3    sing N N 168 
GLY C     O      doub N N 169 
GLY C     OXT    sing N N 170 
GLY OXT   HXT    sing N N 171 
HIS N     CA     sing N N 172 
HIS N     H      sing N N 173 
HIS N     H2     sing N N 174 
HIS CA    C      sing N N 175 
HIS CA    CB     sing N N 176 
HIS CA    HA     sing N N 177 
HIS C     O      doub N N 178 
HIS C     OXT    sing N N 179 
HIS CB    CG     sing N N 180 
HIS CB    HB2    sing N N 181 
HIS CB    HB3    sing N N 182 
HIS CG    ND1    sing Y N 183 
HIS CG    CD2    doub Y N 184 
HIS ND1   CE1    doub Y N 185 
HIS ND1   HD1    sing N N 186 
HIS CD2   NE2    sing Y N 187 
HIS CD2   HD2    sing N N 188 
HIS CE1   NE2    sing Y N 189 
HIS CE1   HE1    sing N N 190 
HIS NE2   HE2    sing N N 191 
HIS OXT   HXT    sing N N 192 
HOH O     H1     sing N N 193 
HOH O     H2     sing N N 194 
ILE N     CA     sing N N 195 
ILE N     H      sing N N 196 
ILE N     H2     sing N N 197 
ILE CA    C      sing N N 198 
ILE CA    CB     sing N N 199 
ILE CA    HA     sing N N 200 
ILE C     O      doub N N 201 
ILE C     OXT    sing N N 202 
ILE CB    CG1    sing N N 203 
ILE CB    CG2    sing N N 204 
ILE CB    HB     sing N N 205 
ILE CG1   CD1    sing N N 206 
ILE CG1   HG12   sing N N 207 
ILE CG1   HG13   sing N N 208 
ILE CG2   HG21   sing N N 209 
ILE CG2   HG22   sing N N 210 
ILE CG2   HG23   sing N N 211 
ILE CD1   HD11   sing N N 212 
ILE CD1   HD12   sing N N 213 
ILE CD1   HD13   sing N N 214 
ILE OXT   HXT    sing N N 215 
LEU N     CA     sing N N 216 
LEU N     H      sing N N 217 
LEU N     H2     sing N N 218 
LEU CA    C      sing N N 219 
LEU CA    CB     sing N N 220 
LEU CA    HA     sing N N 221 
LEU C     O      doub N N 222 
LEU C     OXT    sing N N 223 
LEU CB    CG     sing N N 224 
LEU CB    HB2    sing N N 225 
LEU CB    HB3    sing N N 226 
LEU CG    CD1    sing N N 227 
LEU CG    CD2    sing N N 228 
LEU CG    HG     sing N N 229 
LEU CD1   HD11   sing N N 230 
LEU CD1   HD12   sing N N 231 
LEU CD1   HD13   sing N N 232 
LEU CD2   HD21   sing N N 233 
LEU CD2   HD22   sing N N 234 
LEU CD2   HD23   sing N N 235 
LEU OXT   HXT    sing N N 236 
LYS N     CA     sing N N 237 
LYS N     H      sing N N 238 
LYS N     H2     sing N N 239 
LYS CA    C      sing N N 240 
LYS CA    CB     sing N N 241 
LYS CA    HA     sing N N 242 
LYS C     O      doub N N 243 
LYS C     OXT    sing N N 244 
LYS CB    CG     sing N N 245 
LYS CB    HB2    sing N N 246 
LYS CB    HB3    sing N N 247 
LYS CG    CD     sing N N 248 
LYS CG    HG2    sing N N 249 
LYS CG    HG3    sing N N 250 
LYS CD    CE     sing N N 251 
LYS CD    HD2    sing N N 252 
LYS CD    HD3    sing N N 253 
LYS CE    NZ     sing N N 254 
LYS CE    HE2    sing N N 255 
LYS CE    HE3    sing N N 256 
LYS NZ    HZ1    sing N N 257 
LYS NZ    HZ2    sing N N 258 
LYS NZ    HZ3    sing N N 259 
LYS OXT   HXT    sing N N 260 
MET N     CA     sing N N 261 
MET N     H      sing N N 262 
MET N     H2     sing N N 263 
MET CA    C      sing N N 264 
MET CA    CB     sing N N 265 
MET CA    HA     sing N N 266 
MET C     O      doub N N 267 
MET C     OXT    sing N N 268 
MET CB    CG     sing N N 269 
MET CB    HB2    sing N N 270 
MET CB    HB3    sing N N 271 
MET CG    SD     sing N N 272 
MET CG    HG2    sing N N 273 
MET CG    HG3    sing N N 274 
MET SD    CE     sing N N 275 
MET CE    HE1    sing N N 276 
MET CE    HE2    sing N N 277 
MET CE    HE3    sing N N 278 
MET OXT   HXT    sing N N 279 
PEG C1    O1     sing N N 280 
PEG C1    C2     sing N N 281 
PEG C1    H11    sing N N 282 
PEG C1    H12    sing N N 283 
PEG O1    HO1    sing N N 284 
PEG C2    O2     sing N N 285 
PEG C2    H21    sing N N 286 
PEG C2    H22    sing N N 287 
PEG O2    C3     sing N N 288 
PEG C3    C4     sing N N 289 
PEG C3    H31    sing N N 290 
PEG C3    H32    sing N N 291 
PEG C4    O4     sing N N 292 
PEG C4    H41    sing N N 293 
PEG C4    H42    sing N N 294 
PEG O4    HO4    sing N N 295 
PHE N     CA     sing N N 296 
PHE N     H      sing N N 297 
PHE N     H2     sing N N 298 
PHE CA    C      sing N N 299 
PHE CA    CB     sing N N 300 
PHE CA    HA     sing N N 301 
PHE C     O      doub N N 302 
PHE C     OXT    sing N N 303 
PHE CB    CG     sing N N 304 
PHE CB    HB2    sing N N 305 
PHE CB    HB3    sing N N 306 
PHE CG    CD1    doub Y N 307 
PHE CG    CD2    sing Y N 308 
PHE CD1   CE1    sing Y N 309 
PHE CD1   HD1    sing N N 310 
PHE CD2   CE2    doub Y N 311 
PHE CD2   HD2    sing N N 312 
PHE CE1   CZ     doub Y N 313 
PHE CE1   HE1    sing N N 314 
PHE CE2   CZ     sing Y N 315 
PHE CE2   HE2    sing N N 316 
PHE CZ    HZ     sing N N 317 
PHE OXT   HXT    sing N N 318 
PRO N     CA     sing N N 319 
PRO N     CD     sing N N 320 
PRO N     H      sing N N 321 
PRO CA    C      sing N N 322 
PRO CA    CB     sing N N 323 
PRO CA    HA     sing N N 324 
PRO C     O      doub N N 325 
PRO C     OXT    sing N N 326 
PRO CB    CG     sing N N 327 
PRO CB    HB2    sing N N 328 
PRO CB    HB3    sing N N 329 
PRO CG    CD     sing N N 330 
PRO CG    HG2    sing N N 331 
PRO CG    HG3    sing N N 332 
PRO CD    HD2    sing N N 333 
PRO CD    HD3    sing N N 334 
PRO OXT   HXT    sing N N 335 
SER N     CA     sing N N 336 
SER N     H      sing N N 337 
SER N     H2     sing N N 338 
SER CA    C      sing N N 339 
SER CA    CB     sing N N 340 
SER CA    HA     sing N N 341 
SER C     O      doub N N 342 
SER C     OXT    sing N N 343 
SER CB    OG     sing N N 344 
SER CB    HB2    sing N N 345 
SER CB    HB3    sing N N 346 
SER OG    HG     sing N N 347 
SER OXT   HXT    sing N N 348 
SO3 S     O1     doub N N 349 
SO3 S     O2     sing N N 350 
SO3 S     O3     sing N N 351 
SO4 S     O1     doub N N 352 
SO4 S     O2     doub N N 353 
SO4 S     O3     sing N N 354 
SO4 S     O4     sing N N 355 
THR N     CA     sing N N 356 
THR N     H      sing N N 357 
THR N     H2     sing N N 358 
THR CA    C      sing N N 359 
THR CA    CB     sing N N 360 
THR CA    HA     sing N N 361 
THR C     O      doub N N 362 
THR C     OXT    sing N N 363 
THR CB    OG1    sing N N 364 
THR CB    CG2    sing N N 365 
THR CB    HB     sing N N 366 
THR OG1   HG1    sing N N 367 
THR CG2   HG21   sing N N 368 
THR CG2   HG22   sing N N 369 
THR CG2   HG23   sing N N 370 
THR OXT   HXT    sing N N 371 
TRP N     CA     sing N N 372 
TRP N     H      sing N N 373 
TRP N     H2     sing N N 374 
TRP CA    C      sing N N 375 
TRP CA    CB     sing N N 376 
TRP CA    HA     sing N N 377 
TRP C     O      doub N N 378 
TRP C     OXT    sing N N 379 
TRP CB    CG     sing N N 380 
TRP CB    HB2    sing N N 381 
TRP CB    HB3    sing N N 382 
TRP CG    CD1    doub Y N 383 
TRP CG    CD2    sing Y N 384 
TRP CD1   NE1    sing Y N 385 
TRP CD1   HD1    sing N N 386 
TRP CD2   CE2    doub Y N 387 
TRP CD2   CE3    sing Y N 388 
TRP NE1   CE2    sing Y N 389 
TRP NE1   HE1    sing N N 390 
TRP CE2   CZ2    sing Y N 391 
TRP CE3   CZ3    doub Y N 392 
TRP CE3   HE3    sing N N 393 
TRP CZ2   CH2    doub Y N 394 
TRP CZ2   HZ2    sing N N 395 
TRP CZ3   CH2    sing Y N 396 
TRP CZ3   HZ3    sing N N 397 
TRP CH2   HH2    sing N N 398 
TRP OXT   HXT    sing N N 399 
TYR N     CA     sing N N 400 
TYR N     H      sing N N 401 
TYR N     H2     sing N N 402 
TYR CA    C      sing N N 403 
TYR CA    CB     sing N N 404 
TYR CA    HA     sing N N 405 
TYR C     O      doub N N 406 
TYR C     OXT    sing N N 407 
TYR CB    CG     sing N N 408 
TYR CB    HB2    sing N N 409 
TYR CB    HB3    sing N N 410 
TYR CG    CD1    doub Y N 411 
TYR CG    CD2    sing Y N 412 
TYR CD1   CE1    sing Y N 413 
TYR CD1   HD1    sing N N 414 
TYR CD2   CE2    doub Y N 415 
TYR CD2   HD2    sing N N 416 
TYR CE1   CZ     doub Y N 417 
TYR CE1   HE1    sing N N 418 
TYR CE2   CZ     sing Y N 419 
TYR CE2   HE2    sing N N 420 
TYR CZ    OH     sing N N 421 
TYR OH    HH     sing N N 422 
TYR OXT   HXT    sing N N 423 
VAL N     CA     sing N N 424 
VAL N     H      sing N N 425 
VAL N     H2     sing N N 426 
VAL CA    C      sing N N 427 
VAL CA    CB     sing N N 428 
VAL CA    HA     sing N N 429 
VAL C     O      doub N N 430 
VAL C     OXT    sing N N 431 
VAL CB    CG1    sing N N 432 
VAL CB    CG2    sing N N 433 
VAL CB    HB     sing N N 434 
VAL CG1   HG11   sing N N 435 
VAL CG1   HG12   sing N N 436 
VAL CG1   HG13   sing N N 437 
VAL CG2   HG21   sing N N 438 
VAL CG2   HG22   sing N N 439 
VAL CG2   HG23   sing N N 440 
VAL OXT   HXT    sing N N 441 
# 
_pdbx_audit_support.funding_organization   'Department of Biotechnology (DBT, India)' 
_pdbx_audit_support.country                India 
_pdbx_audit_support.grant_number           BT/PR51982/NER/95/2011/2023 
_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   9JGB 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JGC 
_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]   0.008818 
_atom_sites.fract_transf_matrix[1][2]   0.005091 
_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]   0.010182 
_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]   0.009787 
_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  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLU A 1 2   ? 9.486  18.725  36.980 1.00 71.89 ? 2   GLU A N     1 
ATOM   2    C  CA    . GLU A 1 2   ? 8.828  18.039  35.833 1.00 73.23 ? 2   GLU A CA    1 
ATOM   3    C  C     . GLU A 1 2   ? 7.557  18.772  35.394 1.00 73.35 ? 2   GLU A C     1 
ATOM   4    O  O     . GLU A 1 2   ? 6.619  18.146  34.902 1.00 75.78 ? 2   GLU A O     1 
ATOM   5    C  CB    . GLU A 1 2   ? 8.523  16.582  36.191 1.00 78.94 ? 2   GLU A CB    1 
ATOM   6    C  CG    . GLU A 1 2   ? 9.629  15.613  35.806 1.00 82.84 ? 2   GLU A CG    1 
ATOM   7    C  CD    . GLU A 1 2   ? 9.148  14.218  35.438 1.00 87.36 ? 2   GLU A CD    1 
ATOM   8    O  OE1   . GLU A 1 2   ? 7.943  13.927  35.623 1.00 84.18 ? 2   GLU A OE1   1 
ATOM   9    O  OE2   . GLU A 1 2   ? 9.977  13.428  34.945 1.00 91.31 ? 2   GLU A OE2   1 
ATOM   10   N  N     . GLU A 1 3   ? 7.534  20.104  35.539 1.00 70.07 ? 3   GLU A N     1 
ATOM   11   C  CA    . GLU A 1 3   ? 6.443  20.918  35.020 1.00 60.33 ? 3   GLU A CA    1 
ATOM   12   C  C     . GLU A 1 3   ? 6.997  22.029  34.119 1.00 50.26 ? 3   GLU A C     1 
ATOM   13   O  O     . GLU A 1 3   ? 6.251  22.558  33.301 1.00 48.44 ? 3   GLU A O     1 
ATOM   14   C  CB    . GLU A 1 3   ? 5.580  21.393  36.198 1.00 64.48 ? 3   GLU A CB    1 
ATOM   15   C  CG    . GLU A 1 3   ? 4.882  22.725  35.992 1.00 65.46 ? 3   GLU A CG    1 
ATOM   16   C  CD    . GLU A 1 3   ? 3.441  22.762  36.467 1.00 74.92 ? 3   GLU A CD    1 
ATOM   17   O  OE1   . GLU A 1 3   ? 2.914  23.882  36.660 1.00 74.64 ? 3   GLU A OE1   1 
ATOM   18   O  OE2   . GLU A 1 3   ? 2.834  21.674  36.596 1.00 81.09 ? 3   GLU A OE2   1 
ATOM   19   N  N     . LYS A 1 4   ? 8.296  22.368  34.217 1.00 42.97 ? 4   LYS A N     1 
ATOM   20   C  CA    . LYS A 1 4   ? 8.888  23.361  33.327 1.00 38.57 ? 4   LYS A CA    1 
ATOM   21   C  C     . LYS A 1 4   ? 8.840  22.820  31.890 1.00 34.16 ? 4   LYS A C     1 
ATOM   22   O  O     . LYS A 1 4   ? 8.776  21.616  31.683 1.00 31.79 ? 4   LYS A O     1 
ATOM   23   C  CB    . LYS A 1 4   ? 10.323 23.713  33.737 1.00 38.80 ? 4   LYS A CB    1 
ATOM   24   C  CG    . LYS A 1 4   ? 11.376 22.654  33.431 1.00 38.13 ? 4   LYS A CG    1 
ATOM   25   C  CD    . LYS A 1 4   ? 12.784 22.977  33.931 1.00 38.80 ? 4   LYS A CD    1 
ATOM   26   C  CE    . LYS A 1 4   ? 12.839 23.071  35.440 1.00 41.51 ? 4   LYS A CE    1 
ATOM   27   N  NZ    . LYS A 1 4   ? 14.122 22.572  36.002 1.00 41.61 ? 4   LYS A NZ    1 
ATOM   28   N  N     . LYS A 1 5   ? 8.861  23.718  30.911 1.00 31.89 ? 5   LYS A N     1 
ATOM   29   C  CA    . LYS A 1 5   ? 8.994  23.346  29.516 1.00 30.54 ? 5   LYS A CA    1 
ATOM   30   C  C     . LYS A 1 5   ? 10.308 22.586  29.333 1.00 28.60 ? 5   LYS A C     1 
ATOM   31   O  O     . LYS A 1 5   ? 11.349 23.001  29.852 1.00 28.36 ? 5   LYS A O     1 
ATOM   32   C  CB    . LYS A 1 5   ? 9.017  24.590  28.619 1.00 32.05 ? 5   LYS A CB    1 
ATOM   33   C  CG    . LYS A 1 5   ? 7.758  25.442  28.634 1.00 35.36 ? 5   LYS A CG    1 
ATOM   34   C  CD    . LYS A 1 5   ? 7.936  26.713  27.833 1.00 38.15 ? 5   LYS A CD    1 
ATOM   35   C  CE    . LYS A 1 5   ? 6.600  27.310  27.446 1.00 42.88 ? 5   LYS A CE    1 
ATOM   36   N  NZ    . LYS A 1 5   ? 6.763  28.724  27.054 1.00 47.60 ? 5   LYS A NZ    1 
ATOM   37   N  N     . ARG A 1 6   ? 10.224 21.490  28.573 1.00 26.42 ? 6   ARG A N     1 
ATOM   38   C  CA    . ARG A 1 6   ? 11.367 20.712  28.130 1.00 24.36 ? 6   ARG A CA    1 
ATOM   39   C  C     . ARG A 1 6   ? 11.069 20.174  26.737 1.00 23.36 ? 6   ARG A C     1 
ATOM   40   O  O     . ARG A 1 6   ? 9.908  19.948  26.372 1.00 23.60 ? 6   ARG A O     1 
ATOM   41   C  CB    . ARG A 1 6   ? 11.701 19.535  29.049 1.00 24.06 ? 6   ARG A CB    1 
ATOM   42   C  CG    . ARG A 1 6   ? 11.995 19.918  30.494 1.00 24.98 ? 6   ARG A CG    1 
ATOM   43   C  CD    . ARG A 1 6   ? 12.586 18.744  31.237 1.00 25.29 ? 6   ARG A CD    1 
ATOM   44   N  NE    . ARG A 1 6   ? 12.818 19.099  32.630 1.00 26.30 ? 6   ARG A NE    1 
ATOM   45   C  CZ    . ARG A 1 6   ? 11.972 18.824  33.603 1.00 28.23 ? 6   ARG A CZ    1 
ATOM   46   N  NH1   . ARG A 1 6   ? 10.801 18.289  33.325 1.00 28.42 ? 6   ARG A NH1   1 
ATOM   47   N  NH2   . ARG A 1 6   ? 12.290 19.126  34.846 1.00 30.55 ? 6   ARG A NH2   1 
ATOM   48   N  N     . LEU A 1 7   ? 12.134 20.032  25.952 1.00 22.86 ? 7   LEU A N     1 
ATOM   49   C  CA    . LEU A 1 7   ? 12.097 19.268  24.714 1.00 22.10 ? 7   LEU A CA    1 
ATOM   50   C  C     . LEU A 1 7   ? 12.317 17.782  25.000 1.00 21.96 ? 7   LEU A C     1 
ATOM   51   O  O     . LEU A 1 7   ? 13.261 17.408  25.706 1.00 22.09 ? 7   LEU A O     1 
ATOM   52   C  CB    . LEU A 1 7   ? 13.220 19.796  23.824 1.00 22.75 ? 7   LEU A CB    1 
ATOM   53   C  CG    . LEU A 1 7   ? 13.502 19.002  22.546 1.00 21.93 ? 7   LEU A CG    1 
ATOM   54   C  CD1   . LEU A 1 7   ? 12.308 19.041  21.623 1.00 22.40 ? 7   LEU A CD1   1 
ATOM   55   C  CD2   . LEU A 1 7   ? 14.733 19.567  21.853 1.00 23.06 ? 7   LEU A CD2   1 
ATOM   56   N  N     . HIS A 1 8   ? 11.471 16.945  24.396 1.00 21.65 ? 8   HIS A N     1 
ATOM   57   C  CA    . HIS A 1 8   ? 11.616 15.502  24.419 1.00 20.89 ? 8   HIS A CA    1 
ATOM   58   C  C     . HIS A 1 8   ? 12.061 15.069  23.031 1.00 20.23 ? 8   HIS A C     1 
ATOM   59   O  O     . HIS A 1 8   ? 11.265 15.098  22.082 1.00 19.79 ? 8   HIS A O     1 
ATOM   60   C  CB    . HIS A 1 8   ? 10.311 14.848  24.882 1.00 21.47 ? 8   HIS A CB    1 
ATOM   61   C  CG    . HIS A 1 8   ? 10.053 15.185  26.316 1.00 23.31 ? 8   HIS A CG    1 
ATOM   62   N  ND1   . HIS A 1 8   ? 10.121 14.247  27.314 1.00 22.80 ? 8   HIS A ND1   1 
ATOM   63   C  CD2   . HIS A 1 8   ? 9.817  16.359  26.921 1.00 24.22 ? 8   HIS A CD2   1 
ATOM   64   C  CE1   . HIS A 1 8   ? 9.888  14.831  28.488 1.00 24.05 ? 8   HIS A CE1   1 
ATOM   65   N  NE2   . HIS A 1 8   ? 9.715  16.119  28.285 1.00 24.37 ? 8   HIS A NE2   1 
ATOM   66   N  N     . LEU A 1 9   ? 13.338 14.662  22.934 1.00 19.09 ? 9   LEU A N     1 
ATOM   67   C  CA    . LEU A 1 9   ? 13.935 14.370  21.649 1.00 18.86 ? 9   LEU A CA    1 
ATOM   68   C  C     . LEU A 1 9   ? 14.104 12.868  21.494 1.00 18.84 ? 9   LEU A C     1 
ATOM   69   O  O     . LEU A 1 9   ? 14.740 12.227  22.327 1.00 19.02 ? 9   LEU A O     1 
ATOM   70   C  CB    . LEU A 1 9   ? 15.289 15.067  21.572 1.00 20.05 ? 9   LEU A CB    1 
ATOM   71   C  CG    . LEU A 1 9   ? 16.172 14.698  20.391 1.00 20.54 ? 9   LEU A CG    1 
ATOM   72   C  CD1   . LEU A 1 9   ? 15.572 15.227  19.105 1.00 20.41 ? 9   LEU A CD1   1 
ATOM   73   C  CD2   . LEU A 1 9   ? 17.579 15.248  20.604 1.00 22.50 ? 9   LEU A CD2   1 
ATOM   74   N  N     . ILE A 1 10  ? 13.567 12.320  20.397 1.00 18.46 ? 10  ILE A N     1 
ATOM   75   C  CA    . ILE A 1 10  ? 13.629 10.900  20.140 1.00 17.26 ? 10  ILE A CA    1 
ATOM   76   C  C     . ILE A 1 10  ? 14.445 10.697  18.884 1.00 17.63 ? 10  ILE A C     1 
ATOM   77   O  O     . ILE A 1 10  ? 14.090 11.213  17.817 1.00 17.14 ? 10  ILE A O     1 
ATOM   78   C  CB    . ILE A 1 10  ? 12.237 10.258  20.028 1.00 18.00 ? 10  ILE A CB    1 
ATOM   79   C  CG1   . ILE A 1 10  ? 11.302 10.593  21.182 1.00 19.68 ? 10  ILE A CG1   1 
ATOM   80   C  CG2   . ILE A 1 10  ? 12.380 8.741   19.866 1.00 18.46 ? 10  ILE A CG2   1 
ATOM   81   C  CD1   . ILE A 1 10  ? 9.824  10.266  20.869 1.00 19.59 ? 10  ILE A CD1   1 
ATOM   82   N  N     . ILE A 1 11  ? 15.557 9.969   19.021 1.00 17.62 ? 11  ILE A N     1 
ATOM   83   C  CA    . ILE A 1 11  ? 16.270 9.447   17.877 1.00 17.42 ? 11  ILE A CA    1 
ATOM   84   C  C     . ILE A 1 11  ? 15.617 8.103   17.526 1.00 17.37 ? 11  ILE A C     1 
ATOM   85   O  O     . ILE A 1 11  ? 15.805 7.131   18.261 1.00 17.03 ? 11  ILE A O     1 
ATOM   86   C  CB    . ILE A 1 11  ? 17.778 9.274   18.196 1.00 18.66 ? 11  ILE A CB    1 
ATOM   87   C  CG1   . ILE A 1 11  ? 18.410 10.523  18.800 1.00 20.78 ? 11  ILE A CG1   1 
ATOM   88   C  CG2   . ILE A 1 11  ? 18.533 8.802   16.964 1.00 19.02 ? 11  ILE A CG2   1 
ATOM   89   C  CD1   . ILE A 1 11  ? 18.259 11.739  17.927 1.00 21.00 ? 11  ILE A CD1   1 
ATOM   90   N  N     . ALA A 1 12  ? 14.912 8.029   16.380 1.00 16.93 ? 12  ALA A N     1 
ATOM   91   C  CA    . ALA A 1 12  ? 13.930 6.975   16.173 1.00 17.13 ? 12  ALA A CA    1 
ATOM   92   C  C     . ALA A 1 12  ? 14.331 6.079   15.013 1.00 16.57 ? 12  ALA A C     1 
ATOM   93   O  O     . ALA A 1 12  ? 15.036 6.487   14.097 1.00 16.19 ? 12  ALA A O     1 
ATOM   94   C  CB    . ALA A 1 12  ? 12.576 7.595   15.921 1.00 18.28 ? 12  ALA A CB    1 
ATOM   95   N  N     . ASP A 1 13  ? 13.806 4.852   15.034 1.00 16.82 ? 13  ASP A N     1 
ATOM   96   C  CA    . ASP A 1 13  ? 14.089 3.865   14.007 1.00 17.65 ? 13  ASP A CA    1 
ATOM   97   C  C     . ASP A 1 13  ? 15.612 3.764   13.849 1.00 17.97 ? 13  ASP A C     1 
ATOM   98   O  O     . ASP A 1 13  ? 16.138 3.534   12.759 1.00 18.48 ? 13  ASP A O     1 
ATOM   99   C  CB    . ASP A 1 13  ? 13.392 4.244   12.689 1.00 18.27 ? 13  ASP A CB    1 
ATOM   100  C  CG    . ASP A 1 13  ? 11.879 4.070   12.643 1.00 19.49 ? 13  ASP A CG    1 
ATOM   101  O  OD1   . ASP A 1 13  ? 11.328 3.367   13.513 1.00 20.38 ? 13  ASP A OD1   1 
ATOM   102  O  OD2   . ASP A 1 13  ? 11.246 4.687   11.737 1.00 20.29 ? 13  ASP A OD2   1 
ATOM   103  N  N     . ALA A 1 14  ? 16.317 3.829   14.967 1.00 16.71 ? 14  ALA A N     1 
ATOM   104  C  CA    . ALA A 1 14  ? 17.768 3.890   14.937 1.00 18.09 ? 14  ALA A CA    1 
ATOM   105  C  C     . ALA A 1 14  ? 18.376 2.570   14.485 1.00 19.26 ? 14  ALA A C     1 
ATOM   106  O  O     . ALA A 1 14  ? 17.889 1.514   14.880 1.00 19.64 ? 14  ALA A O     1 
ATOM   107  C  CB    . ALA A 1 14  ? 18.275 4.277   16.308 1.00 19.33 ? 14  ALA A CB    1 
ATOM   108  N  N     . GLU A 1 15  ? 19.474 2.654   13.706 1.00 18.35 ? 15  GLU A N     1 
ATOM   109  C  CA    . GLU A 1 15  ? 20.193 1.486   13.225 1.00 18.90 ? 15  GLU A CA    1 
ATOM   110  C  C     . GLU A 1 15  ? 21.179 0.974   14.284 1.00 18.45 ? 15  GLU A C     1 
ATOM   111  O  O     . GLU A 1 15  ? 22.386 0.900   14.058 1.00 19.80 ? 15  GLU A O     1 
ATOM   112  C  CB    . GLU A 1 15  ? 20.806 1.845   11.869 1.00 20.21 ? 15  GLU A CB    1 
ATOM   113  C  CG    . GLU A 1 15  ? 19.716 2.110   10.814 1.00 20.97 ? 15  GLU A CG    1 
ATOM   114  C  CD    . GLU A 1 15  ? 18.759 0.989   10.413 1.00 22.90 ? 15  GLU A CD    1 
ATOM   115  O  OE1   . GLU A 1 15  ? 17.849 1.213   9.539  1.00 25.06 ? 15  GLU A OE1   1 
ATOM   116  O  OE2   . GLU A 1 15  ? 18.902 -0.111  10.895 1.00 23.59 ? 15  GLU A OE2   1 
ATOM   117  N  N     . LEU A 1 16  ? 20.617 0.649   15.448 1.00 17.17 ? 16  LEU A N     1 
ATOM   118  C  CA    . LEU A 1 16  ? 21.320 0.140   16.612 1.00 16.93 ? 16  LEU A CA    1 
ATOM   119  C  C     . LEU A 1 16  ? 20.693 -1.193  17.008 1.00 17.18 ? 16  LEU A C     1 
ATOM   120  O  O     . LEU A 1 16  ? 19.543 -1.227  17.477 1.00 18.42 ? 16  LEU A O     1 
ATOM   121  C  CB    . LEU A 1 16  ? 21.142 1.152   17.724 1.00 16.59 ? 16  LEU A CB    1 
ATOM   122  C  CG    . LEU A 1 16  ? 21.805 0.788   19.045 1.00 17.38 ? 16  LEU A CG    1 
ATOM   123  C  CD1   . LEU A 1 16  ? 23.310 0.755   18.875 1.00 18.20 ? 16  LEU A CD1   1 
ATOM   124  C  CD2   . LEU A 1 16  ? 21.364 1.783   20.118 1.00 17.19 ? 16  LEU A CD2   1 
ATOM   125  N  N     . GLU A 1 17  ? 21.445 -2.279  16.785 1.00 17.38 ? 17  GLU A N     1 
ATOM   126  C  CA    . GLU A 1 17  ? 20.966 -3.631  17.001 1.00 18.45 ? 17  GLU A CA    1 
ATOM   127  C  C     . GLU A 1 17  ? 22.158 -4.555  17.217 1.00 19.52 ? 17  GLU A C     1 
ATOM   128  O  O     . GLU A 1 17  ? 23.256 -4.281  16.738 1.00 20.78 ? 17  GLU A O     1 
ATOM   129  C  CB    . GLU A 1 17  ? 20.096 -4.138  15.839 1.00 19.41 ? 17  GLU A CB    1 
ATOM   130  C  CG    . GLU A 1 17  ? 20.798 -4.234  14.479 1.00 19.06 ? 17  GLU A CG    1 
ATOM   131  C  CD    . GLU A 1 17  ? 19.939 -4.665  13.300 1.00 19.84 ? 17  GLU A CD    1 
ATOM   132  O  OE1   . GLU A 1 17  ? 20.099 -4.110  12.180 1.00 21.42 ? 17  GLU A OE1   1 
ATOM   133  O  OE2   . GLU A 1 17  ? 19.111 -5.551  13.463 1.00 20.84 ? 17  GLU A OE2   1 
ATOM   134  N  N     . THR A 1 18  ? 21.920 -5.685  17.890 1.00 20.36 ? 18  THR A N     1 
ATOM   135  C  CA    . THR A 1 18  ? 22.930 -6.723  17.931 1.00 21.43 ? 18  THR A CA    1 
ATOM   136  C  C     . THR A 1 18  ? 22.935 -7.365  16.554 1.00 22.61 ? 18  THR A C     1 
ATOM   137  O  O     . THR A 1 18  ? 21.996 -7.164  15.788 1.00 22.39 ? 18  THR A O     1 
ATOM   138  C  CB    . THR A 1 18  ? 22.684 -7.748  19.043 1.00 22.44 ? 18  THR A CB    1 
ATOM   139  O  OG1   . THR A 1 18  ? 21.343 -8.209  19.012 1.00 21.28 ? 18  THR A OG1   1 
ATOM   140  C  CG2   . THR A 1 18  ? 22.967 -7.178  20.416 1.00 23.60 ? 18  THR A CG2   1 
ATOM   141  N  N     . VAL A 1 19  ? 23.933 -8.206  16.304 1.00 23.63 ? 19  VAL A N     1 
ATOM   142  C  CA    . VAL A 1 19  ? 24.082 -8.827  15.005 1.00 24.08 ? 19  VAL A CA    1 
ATOM   143  C  C     . VAL A 1 19  ? 22.809 -9.605  14.667 1.00 23.46 ? 19  VAL A C     1 
ATOM   144  O  O     . VAL A 1 19  ? 22.309 -10.421 15.464 1.00 22.97 ? 19  VAL A O     1 
ATOM   145  C  CB    . VAL A 1 19  ? 25.316 -9.734  14.946 1.00 25.49 ? 19  VAL A CB    1 
ATOM   146  C  CG1   . VAL A 1 19  ? 25.383 -10.479 13.620 1.00 27.31 ? 19  VAL A CG1   1 
ATOM   147  C  CG2   . VAL A 1 19  ? 26.587 -8.942  15.171 1.00 25.51 ? 19  VAL A CG2   1 
ATOM   148  N  N     . PRO A 1 20  ? 22.243 -9.353  13.468 1.00 23.42 ? 20  PRO A N     1 
ATOM   149  C  CA    . PRO A 1 20  ? 21.043 -10.058 13.027 1.00 24.41 ? 20  PRO A CA    1 
ATOM   150  C  C     . PRO A 1 20  ? 21.241 -11.575 13.101 1.00 25.27 ? 20  PRO A C     1 
ATOM   151  O  O     . PRO A 1 20  ? 22.232 -12.105 12.603 1.00 25.31 ? 20  PRO A O     1 
ATOM   152  C  CB    . PRO A 1 20  ? 20.823 -9.521  11.611 1.00 24.98 ? 20  PRO A CB    1 
ATOM   153  C  CG    . PRO A 1 20  ? 21.426 -8.124  11.649 1.00 24.97 ? 20  PRO A CG    1 
ATOM   154  C  CD    . PRO A 1 20  ? 22.641 -8.295  12.535 1.00 24.23 ? 20  PRO A CD    1 
ATOM   155  N  N     . PRO A 1 21  ? 20.311 -12.313 13.750 1.00 26.75 ? 21  PRO A N     1 
ATOM   156  C  CA    . PRO A 1 21  ? 20.339 -13.777 13.780 1.00 28.66 ? 21  PRO A CA    1 
ATOM   157  C  C     . PRO A 1 21  ? 20.656 -14.451 12.446 1.00 30.27 ? 21  PRO A C     1 
ATOM   158  O  O     . PRO A 1 21  ? 21.375 -15.435 12.419 1.00 32.44 ? 21  PRO A O     1 
ATOM   159  C  CB    . PRO A 1 21  ? 18.905 -14.107 14.209 1.00 28.81 ? 21  PRO A CB    1 
ATOM   160  C  CG    . PRO A 1 21  ? 18.579 -13.003 15.165 1.00 27.58 ? 21  PRO A CG    1 
ATOM   161  C  CD    . PRO A 1 21  ? 19.154 -11.775 14.486 1.00 27.03 ? 21  PRO A CD    1 
ATOM   162  N  N     . GLU A 1 22  ? 20.154 -13.887 11.345 1.00 31.53 ? 22  GLU A N     1 
ATOM   163  C  CA    . GLU A 1 22  ? 20.334 -14.458 10.020 1.00 33.65 ? 22  GLU A CA    1 
ATOM   164  C  C     . GLU A 1 22  ? 21.806 -14.576 9.620  1.00 34.89 ? 22  GLU A C     1 
ATOM   165  O  O     . GLU A 1 22  ? 22.123 -15.401 8.779  1.00 36.22 ? 22  GLU A O     1 
ATOM   166  C  CB    . GLU A 1 22  ? 19.745 -13.553 8.936  1.00 33.60 ? 22  GLU A CB    1 
ATOM   167  C  CG    . GLU A 1 22  ? 18.255 -13.364 9.000  1.00 33.19 ? 22  GLU A CG    1 
ATOM   168  C  CD    . GLU A 1 22  ? 17.847 -12.113 9.757  1.00 31.80 ? 22  GLU A CD    1 
ATOM   169  O  OE1   . GLU A 1 22  ? 16.867 -11.467 9.341  1.00 31.89 ? 22  GLU A OE1   1 
ATOM   170  O  OE2   . GLU A 1 22  ? 18.525 -11.780 10.753 1.00 30.41 ? 22  GLU A OE2   1 
ATOM   171  N  N     . ILE A 1 23  ? 22.693 -13.685 10.098 1.00 34.08 ? 23  ILE A N     1 
ATOM   172  C  CA    . ILE A 1 23  ? 24.039 -13.645 9.539  1.00 34.17 ? 23  ILE A CA    1 
ATOM   173  C  C     . ILE A 1 23  ? 25.087 -14.042 10.580 1.00 35.03 ? 23  ILE A C     1 
ATOM   174  O  O     . ILE A 1 23  ? 26.278 -13.824 10.343 1.00 36.33 ? 23  ILE A O     1 
ATOM   175  C  CB    . ILE A 1 23  ? 24.327 -12.264 8.916  1.00 34.09 ? 23  ILE A CB    1 
ATOM   176  C  CG1   . ILE A 1 23  ? 24.270 -11.150 9.958  1.00 32.32 ? 23  ILE A CG1   1 
ATOM   177  C  CG2   . ILE A 1 23  ? 23.391 -11.963 7.760  1.00 33.58 ? 23  ILE A CG2   1 
ATOM   178  C  CD1   . ILE A 1 23  ? 24.790 -9.844  9.476  1.00 31.72 ? 23  ILE A CD1   1 
ATOM   179  N  N     . LEU A 1 24  ? 24.672 -14.647 11.706 1.00 35.00 ? 24  LEU A N     1 
ATOM   180  C  CA    . LEU A 1 24  ? 25.585 -14.941 12.804 1.00 36.24 ? 24  LEU A CA    1 
ATOM   181  C  C     . LEU A 1 24  ? 26.720 -15.851 12.353 1.00 39.79 ? 24  LEU A C     1 
ATOM   182  O  O     . LEU A 1 24  ? 27.791 -15.841 12.954 1.00 42.54 ? 24  LEU A O     1 
ATOM   183  C  CB    . LEU A 1 24  ? 24.843 -15.612 13.960 1.00 35.50 ? 24  LEU A CB    1 
ATOM   184  C  CG    . LEU A 1 24  ? 23.897 -14.728 14.764 1.00 35.49 ? 24  LEU A CG    1 
ATOM   185  C  CD1   . LEU A 1 24  ? 23.247 -15.519 15.882 1.00 35.57 ? 24  LEU A CD1   1 
ATOM   186  C  CD2   . LEU A 1 24  ? 24.621 -13.521 15.355 1.00 35.33 ? 24  LEU A CD2   1 
ATOM   187  N  N     . ASP A 1 25  ? 26.473 -16.657 11.319 1.00 42.49 ? 25  ASP A N     1 
ATOM   188  C  CA    . ASP A 1 25  ? 27.458 -17.624 10.866 1.00 46.56 ? 25  ASP A CA    1 
ATOM   189  C  C     . ASP A 1 25  ? 28.166 -17.101 9.619  1.00 47.51 ? 25  ASP A C     1 
ATOM   190  O  O     . ASP A 1 25  ? 28.921 -17.841 8.995  1.00 49.14 ? 25  ASP A O     1 
ATOM   191  C  CB    . ASP A 1 25  ? 26.792 -18.983 10.627 1.00 52.15 ? 25  ASP A CB    1 
ATOM   192  C  CG    . ASP A 1 25  ? 25.518 -18.867 9.805  1.00 56.74 ? 25  ASP A CG    1 
ATOM   193  O  OD1   . ASP A 1 25  ? 25.227 -17.737 9.320  1.00 59.87 ? 25  ASP A OD1   1 
ATOM   194  O  OD2   . ASP A 1 25  ? 24.793 -19.873 9.698  1.00 59.25 ? 25  ASP A OD2   1 
ATOM   195  N  N     . HIS A 1 26  ? 27.957 -15.830 9.247  1.00 44.15 ? 26  HIS A N     1 
ATOM   196  C  CA    . HIS A 1 26  ? 28.661 -15.294 8.091  1.00 45.51 ? 26  HIS A CA    1 
ATOM   197  C  C     . HIS A 1 26  ? 30.134 -15.133 8.456  1.00 45.20 ? 26  HIS A C     1 
ATOM   198  O  O     . HIS A 1 26  ? 30.460 -14.688 9.552  1.00 44.82 ? 26  HIS A O     1 
ATOM   199  C  CB    . HIS A 1 26  ? 28.003 -14.016 7.567  1.00 45.20 ? 26  HIS A CB    1 
ATOM   200  C  CG    . HIS A 1 26  ? 28.595 -13.562 6.279  1.00 44.36 ? 26  HIS A CG    1 
ATOM   201  N  ND1   . HIS A 1 26  ? 29.832 -12.957 6.200  1.00 43.85 ? 26  HIS A ND1   1 
ATOM   202  C  CD2   . HIS A 1 26  ? 28.119 -13.616 5.032  1.00 44.84 ? 26  HIS A CD2   1 
ATOM   203  C  CE1   . HIS A 1 26  ? 30.094 -12.680 4.930  1.00 43.61 ? 26  HIS A CE1   1 
ATOM   204  N  NE2   . HIS A 1 26  ? 29.066 -13.061 4.208  1.00 44.97 ? 26  HIS A NE2   1 
ATOM   205  N  N     . PRO A 1 27  ? 31.082 -15.544 7.587  1.00 48.38 ? 27  PRO A N     1 
ATOM   206  C  CA    . PRO A 1 27  ? 32.493 -15.560 7.966  1.00 47.62 ? 27  PRO A CA    1 
ATOM   207  C  C     . PRO A 1 27  ? 32.984 -14.243 8.556  1.00 43.94 ? 27  PRO A C     1 
ATOM   208  O  O     . PRO A 1 27  ? 33.753 -14.269 9.509  1.00 43.29 ? 27  PRO A O     1 
ATOM   209  C  CB    . PRO A 1 27  ? 33.202 -15.905 6.644  1.00 50.81 ? 27  PRO A CB    1 
ATOM   210  C  CG    . PRO A 1 27  ? 32.183 -16.776 5.932  1.00 51.54 ? 27  PRO A CG    1 
ATOM   211  C  CD    . PRO A 1 27  ? 30.860 -16.103 6.242  1.00 50.83 ? 27  PRO A CD    1 
ATOM   212  N  N     . ALA A 1 28  ? 32.504 -13.114 8.008  1.00 42.07 ? 28  ALA A N     1 
ATOM   213  C  CA    . ALA A 1 28  ? 32.937 -11.796 8.437  1.00 39.84 ? 28  ALA A CA    1 
ATOM   214  C  C     . ALA A 1 28  ? 32.480 -11.550 9.870  1.00 38.27 ? 28  ALA A C     1 
ATOM   215  O  O     . ALA A 1 28  ? 33.178 -10.882 10.635 1.00 36.94 ? 28  ALA A O     1 
ATOM   216  C  CB    . ALA A 1 28  ? 32.414 -10.728 7.509  1.00 39.14 ? 28  ALA A CB    1 
ATOM   217  N  N     . ILE A 1 29  ? 31.304 -12.102 10.223 1.00 37.32 ? 29  ILE A N     1 
ATOM   218  C  CA    . ILE A 1 29  ? 30.822 -12.058 11.591 1.00 34.53 ? 29  ILE A CA    1 
ATOM   219  C  C     . ILE A 1 29  ? 31.652 -12.985 12.474 1.00 36.52 ? 29  ILE A C     1 
ATOM   220  O  O     . ILE A 1 29  ? 32.027 -12.631 13.582 1.00 37.67 ? 29  ILE A O     1 
ATOM   221  C  CB    . ILE A 1 29  ? 29.328 -12.428 11.659 1.00 32.46 ? 29  ILE A CB    1 
ATOM   222  C  CG1   . ILE A 1 29  ? 28.458 -11.438 10.873 1.00 30.18 ? 29  ILE A CG1   1 
ATOM   223  C  CG2   . ILE A 1 29  ? 28.900 -12.556 13.115 1.00 31.29 ? 29  ILE A CG2   1 
ATOM   224  C  CD1   . ILE A 1 29  ? 28.600 -10.006 11.279 1.00 29.12 ? 29  ILE A CD1   1 
ATOM   225  N  N     . VAL A 1 30  ? 31.875 -14.211 12.022 1.00 41.08 ? 30  VAL A N     1 
ATOM   226  C  CA    . VAL A 1 30  ? 32.536 -15.190 12.869 1.00 44.32 ? 30  VAL A CA    1 
ATOM   227  C  C     . VAL A 1 30  ? 33.974 -14.753 13.149 1.00 44.95 ? 30  VAL A C     1 
ATOM   228  O  O     . VAL A 1 30  ? 34.450 -14.834 14.287 1.00 43.55 ? 30  VAL A O     1 
ATOM   229  C  CB    . VAL A 1 30  ? 32.498 -16.591 12.247 1.00 46.89 ? 30  VAL A CB    1 
ATOM   230  C  CG1   . VAL A 1 30  ? 33.290 -17.564 13.104 1.00 48.73 ? 30  VAL A CG1   1 
ATOM   231  C  CG2   . VAL A 1 30  ? 31.066 -17.082 12.045 1.00 48.20 ? 30  VAL A CG2   1 
ATOM   232  N  N     . ASN A 1 31  ? 34.653 -14.282 12.101 1.00 45.32 ? 31  ASN A N     1 
ATOM   233  C  CA    . ASN A 1 31  ? 36.038 -13.867 12.226 1.00 47.14 ? 31  ASN A CA    1 
ATOM   234  C  C     . ASN A 1 31  ? 36.115 -12.690 13.199 1.00 47.61 ? 31  ASN A C     1 
ATOM   235  O  O     . ASN A 1 31  ? 36.971 -12.652 14.085 1.00 46.43 ? 31  ASN A O     1 
ATOM   236  C  CB    . ASN A 1 31  ? 36.641 -13.497 10.865 1.00 51.12 ? 31  ASN A CB    1 
ATOM   237  C  CG    . ASN A 1 31  ? 36.802 -14.660 9.899  1.00 55.76 ? 31  ASN A CG    1 
ATOM   238  O  OD1   . ASN A 1 31  ? 37.057 -15.796 10.298 1.00 59.95 ? 31  ASN A OD1   1 
ATOM   239  N  ND2   . ASN A 1 31  ? 36.659 -14.384 8.611  1.00 57.04 ? 31  ASN A ND2   1 
ATOM   240  N  N     . TYR A 1 32  ? 35.203 -11.725 13.027 1.00 44.18 ? 32  TYR A N     1 
ATOM   241  C  CA    . TYR A 1 32  ? 35.209 -10.532 13.854 1.00 42.69 ? 32  TYR A CA    1 
ATOM   242  C  C     . TYR A 1 32  ? 35.017 -10.904 15.326 1.00 43.08 ? 32  TYR A C     1 
ATOM   243  O  O     . TYR A 1 32  ? 35.636 -10.316 16.215 1.00 42.51 ? 32  TYR A O     1 
ATOM   244  C  CB    . TYR A 1 32  ? 34.132 -9.576  13.331 1.00 42.86 ? 32  TYR A CB    1 
ATOM   245  C  CG    . TYR A 1 32  ? 33.978 -8.347  14.207 1.00 41.60 ? 32  TYR A CG    1 
ATOM   246  C  CD1   . TYR A 1 32  ? 33.244 -8.396  15.385 1.00 41.04 ? 32  TYR A CD1   1 
ATOM   247  C  CD2   . TYR A 1 32  ? 34.647 -7.172  13.899 1.00 41.19 ? 32  TYR A CD2   1 
ATOM   248  C  CE1   . TYR A 1 32  ? 33.134 -7.287  16.208 1.00 42.08 ? 32  TYR A CE1   1 
ATOM   249  C  CE2   . TYR A 1 32  ? 34.563 -6.064  14.721 1.00 40.70 ? 32  TYR A CE2   1 
ATOM   250  C  CZ    . TYR A 1 32  ? 33.796 -6.116  15.871 1.00 42.82 ? 32  TYR A CZ    1 
ATOM   251  O  OH    . TYR A 1 32  ? 33.702 -4.997  16.647 1.00 43.84 ? 32  TYR A OH    1 
ATOM   252  N  N     . ALA A 1 33  ? 34.110 -11.850 15.585 1.00 45.05 ? 33  ALA A N     1 
ATOM   253  C  CA    . ALA A 1 33  ? 33.741 -12.231 16.945 1.00 44.12 ? 33  ALA A CA    1 
ATOM   254  C  C     . ALA A 1 33  ? 34.848 -13.076 17.582 1.00 45.24 ? 33  ALA A C     1 
ATOM   255  O  O     . ALA A 1 33  ? 35.091 -12.999 18.794 1.00 41.27 ? 33  ALA A O     1 
ATOM   256  C  CB    . ALA A 1 33  ? 32.430 -12.975 16.922 1.00 42.47 ? 33  ALA A CB    1 
ATOM   257  N  N     . LYS A 1 34  ? 35.499 -13.891 16.747 1.00 48.91 ? 34  LYS A N     1 
ATOM   258  C  CA    . LYS A 1 34  ? 36.687 -14.617 17.170 1.00 56.73 ? 34  LYS A CA    1 
ATOM   259  C  C     . LYS A 1 34  ? 37.748 -13.624 17.642 1.00 57.06 ? 34  LYS A C     1 
ATOM   260  O  O     . LYS A 1 34  ? 38.230 -13.710 18.771 1.00 57.03 ? 34  LYS A O     1 
ATOM   261  C  CB    . LYS A 1 34  ? 37.197 -15.504 16.033 1.00 63.60 ? 34  LYS A CB    1 
ATOM   262  C  CG    . LYS A 1 34  ? 38.318 -16.454 16.432 1.00 73.35 ? 34  LYS A CG    1 
ATOM   263  C  CD    . LYS A 1 34  ? 38.459 -17.661 15.524 1.00 80.72 ? 34  LYS A CD    1 
ATOM   264  C  CE    . LYS A 1 34  ? 39.111 -17.333 14.198 1.00 85.97 ? 34  LYS A CE    1 
ATOM   265  N  NZ    . LYS A 1 34  ? 40.559 -17.052 14.356 1.00 91.50 ? 34  LYS A NZ    1 
ATOM   266  N  N     . ARG A 1 35  ? 38.058 -12.634 16.797 1.00 57.90 ? 35  ARG A N     1 
ATOM   267  C  CA    . ARG A 1 35  ? 39.052 -11.635 17.149 1.00 59.94 ? 35  ARG A CA    1 
ATOM   268  C  C     . ARG A 1 35  ? 38.643 -10.928 18.436 1.00 57.79 ? 35  ARG A C     1 
ATOM   269  O  O     . ARG A 1 35  ? 39.488 -10.686 19.281 1.00 62.12 ? 35  ARG A O     1 
ATOM   270  C  CB    . ARG A 1 35  ? 39.288 -10.636 16.012 1.00 62.82 ? 35  ARG A CB    1 
ATOM   271  C  CG    . ARG A 1 35  ? 40.006 -11.229 14.807 1.00 69.27 ? 35  ARG A CG    1 
ATOM   272  C  CD    . ARG A 1 35  ? 40.545 -10.204 13.821 1.00 73.96 ? 35  ARG A CD    1 
ATOM   273  N  NE    . ARG A 1 35  ? 39.639 -9.077  13.593 1.00 81.55 ? 35  ARG A NE    1 
ATOM   274  C  CZ    . ARG A 1 35  ? 38.703 -9.011  12.642 1.00 84.96 ? 35  ARG A CZ    1 
ATOM   275  N  NH1   . ARG A 1 35  ? 38.087 -7.864  12.398 1.00 79.49 ? 35  ARG A NH1   1 
ATOM   276  N  NH2   . ARG A 1 35  ? 38.406 -10.077 11.913 1.00 89.16 ? 35  ARG A NH2   1 
ATOM   277  N  N     . ARG A 1 36  ? 37.352 -10.629 18.621 1.00 56.35 ? 36  ARG A N     1 
ATOM   278  C  CA    . ARG A 1 36  ? 36.942 -9.857  19.782 1.00 52.36 ? 36  ARG A CA    1 
ATOM   279  C  C     . ARG A 1 36  ? 36.701 -10.744 21.003 1.00 51.04 ? 36  ARG A C     1 
ATOM   280  O  O     . ARG A 1 36  ? 36.389 -10.216 22.064 1.00 47.11 ? 36  ARG A O     1 
ATOM   281  C  CB    . ARG A 1 36  ? 35.720 -9.009  19.431 1.00 56.62 ? 36  ARG A CB    1 
ATOM   282  C  CG    . ARG A 1 36  ? 36.074 -7.798  18.579 1.00 61.53 ? 36  ARG A CG    1 
ATOM   283  C  CD    . ARG A 1 36  ? 35.146 -6.624  18.825 1.00 63.02 ? 36  ARG A CD    1 
ATOM   284  N  NE    . ARG A 1 36  ? 34.793 -6.487  20.236 1.00 64.06 ? 36  ARG A NE    1 
ATOM   285  C  CZ    . ARG A 1 36  ? 33.553 -6.351  20.695 1.00 66.17 ? 36  ARG A CZ    1 
ATOM   286  N  NH1   . ARG A 1 36  ? 32.560 -6.015  19.878 1.00 62.01 ? 36  ARG A NH1   1 
ATOM   287  N  NH2   . ARG A 1 36  ? 33.330 -6.496  21.990 1.00 66.92 ? 36  ARG A NH2   1 
ATOM   288  N  N     . LYS A 1 37  ? 36.879 -12.067 20.850 1.00 55.15 ? 37  LYS A N     1 
ATOM   289  C  CA    . LYS A 1 37  ? 36.569 -13.069 21.862 1.00 58.95 ? 37  LYS A CA    1 
ATOM   290  C  C     . LYS A 1 37  ? 35.172 -12.833 22.435 1.00 56.74 ? 37  LYS A C     1 
ATOM   291  O  O     . LYS A 1 37  ? 34.990 -12.762 23.656 1.00 51.50 ? 37  LYS A O     1 
ATOM   292  C  CB    . LYS A 1 37  ? 37.614 -13.073 22.981 1.00 65.82 ? 37  LYS A CB    1 
ATOM   293  C  CG    . LYS A 1 37  ? 39.049 -13.297 22.525 1.00 70.91 ? 37  LYS A CG    1 
ATOM   294  C  CD    . LYS A 1 37  ? 40.044 -13.425 23.669 1.00 77.57 ? 37  LYS A CD    1 
ATOM   295  C  CE    . LYS A 1 37  ? 39.956 -12.303 24.688 1.00 79.30 ? 37  LYS A CE    1 
ATOM   296  N  NZ    . LYS A 1 37  ? 41.098 -12.307 25.638 1.00 82.17 ? 37  LYS A NZ    1 
ATOM   297  N  N     . LYS A 1 38  ? 34.180 -12.736 21.540 1.00 52.17 ? 38  LYS A N     1 
ATOM   298  C  CA    . LYS A 1 38  ? 32.828 -12.410 21.971 1.00 48.58 ? 38  LYS A CA    1 
ATOM   299  C  C     . LYS A 1 38  ? 31.839 -13.272 21.195 1.00 42.85 ? 38  LYS A C     1 
ATOM   300  O  O     . LYS A 1 38  ? 32.081 -13.583 20.029 1.00 41.06 ? 38  LYS A O     1 
ATOM   301  C  CB    . LYS A 1 38  ? 32.557 -10.917 21.739 1.00 49.08 ? 38  LYS A CB    1 
ATOM   302  C  CG    . LYS A 1 38  ? 32.155 -10.145 22.983 1.00 51.75 ? 38  LYS A CG    1 
ATOM   303  C  CD    . LYS A 1 38  ? 30.961 -9.252  22.778 1.00 53.84 ? 38  LYS A CD    1 
ATOM   304  C  CE    . LYS A 1 38  ? 30.573 -8.492  24.026 1.00 54.14 ? 38  LYS A CE    1 
ATOM   305  N  NZ    . LYS A 1 38  ? 29.851 -9.363  24.978 1.00 56.20 ? 38  LYS A NZ    1 
ATOM   306  N  N     . ARG A 1 39  ? 30.722 -13.623 21.839 1.00 38.90 ? 39  ARG A N     1 
ATOM   307  C  CA    . ARG A 1 39  ? 29.648 -14.307 21.136 1.00 39.99 ? 39  ARG A CA    1 
ATOM   308  C  C     . ARG A 1 39  ? 29.006 -13.374 20.099 1.00 36.39 ? 39  ARG A C     1 
ATOM   309  O  O     . ARG A 1 39  ? 28.487 -12.312 20.427 1.00 35.06 ? 39  ARG A O     1 
ATOM   310  C  CB    . ARG A 1 39  ? 28.632 -14.830 22.143 1.00 41.49 ? 39  ARG A CB    1 
ATOM   311  C  CG    . ARG A 1 39  ? 29.078 -16.101 22.853 1.00 47.16 ? 39  ARG A CG    1 
ATOM   312  C  CD    . ARG A 1 39  ? 28.350 -16.318 24.168 1.00 51.99 ? 39  ARG A CD    1 
ATOM   313  N  NE    . ARG A 1 39  ? 27.887 -17.696 24.306 1.00 58.18 ? 39  ARG A NE    1 
ATOM   314  C  CZ    . ARG A 1 39  ? 28.472 -18.645 25.036 1.00 66.59 ? 39  ARG A CZ    1 
ATOM   315  N  NH1   . ARG A 1 39  ? 27.896 -19.832 25.155 1.00 69.69 ? 39  ARG A NH1   1 
ATOM   316  N  NH2   . ARG A 1 39  ? 29.619 -18.413 25.655 1.00 69.13 ? 39  ARG A NH2   1 
ATOM   317  N  N     . PRO A 1 40  ? 28.942 -13.774 18.815 1.00 34.47 ? 40  PRO A N     1 
ATOM   318  C  CA    . PRO A 1 40  ? 28.393 -12.920 17.769 1.00 33.45 ? 40  PRO A CA    1 
ATOM   319  C  C     . PRO A 1 40  ? 27.032 -12.306 18.101 1.00 30.48 ? 40  PRO A C     1 
ATOM   320  O  O     . PRO A 1 40  ? 26.778 -11.156 17.779 1.00 28.35 ? 40  PRO A O     1 
ATOM   321  C  CB    . PRO A 1 40  ? 28.190 -13.875 16.587 1.00 35.69 ? 40  PRO A CB    1 
ATOM   322  C  CG    . PRO A 1 40  ? 29.075 -15.036 16.840 1.00 38.09 ? 40  PRO A CG    1 
ATOM   323  C  CD    . PRO A 1 40  ? 29.287 -15.116 18.334 1.00 38.70 ? 40  PRO A CD    1 
ATOM   324  N  N     . GLU A 1 41  ? 26.148 -13.090 18.727 1.00 29.70 ? 41  GLU A N     1 
ATOM   325  C  CA    . GLU A 1 41  ? 24.805 -12.603 18.986 1.00 30.71 ? 41  GLU A CA    1 
ATOM   326  C  C     . GLU A 1 41  ? 24.816 -11.440 19.985 1.00 30.41 ? 41  GLU A C     1 
ATOM   327  O  O     . GLU A 1 41  ? 23.814 -10.734 20.095 1.00 29.69 ? 41  GLU A O     1 
ATOM   328  C  CB    . GLU A 1 41  ? 23.882 -13.730 19.447 1.00 30.96 ? 41  GLU A CB    1 
ATOM   329  C  CG    . GLU A 1 41  ? 24.332 -14.423 20.724 1.00 32.00 ? 41  GLU A CG    1 
ATOM   330  C  CD    . GLU A 1 41  ? 25.377 -15.507 20.544 1.00 33.77 ? 41  GLU A CD    1 
ATOM   331  O  OE1   . GLU A 1 41  ? 25.510 -16.295 21.462 1.00 35.54 ? 41  GLU A OE1   1 
ATOM   332  O  OE2   . GLU A 1 41  ? 26.029 -15.571 19.476 1.00 34.56 ? 41  GLU A OE2   1 
ATOM   333  N  N     . LYS A 1 42  ? 25.940 -11.241 20.688 1.00 31.27 ? 42  LYS A N     1 
ATOM   334  C  CA    . LYS A 1 42  ? 26.065 -10.231 21.728 1.00 31.42 ? 42  LYS A CA    1 
ATOM   335  C  C     . LYS A 1 42  ? 26.656 -8.933  21.193 1.00 28.80 ? 42  LYS A C     1 
ATOM   336  O  O     . LYS A 1 42  ? 26.666 -7.926  21.899 1.00 28.00 ? 42  LYS A O     1 
ATOM   337  C  CB    . LYS A 1 42  ? 27.060 -10.676 22.798 1.00 34.94 ? 42  LYS A CB    1 
ATOM   338  C  CG    . LYS A 1 42  ? 26.821 -12.046 23.408 1.00 40.59 ? 42  LYS A CG    1 
ATOM   339  C  CD    . LYS A 1 42  ? 25.602 -12.090 24.232 1.00 39.23 ? 42  LYS A CD    1 
ATOM   340  C  CE    . LYS A 1 42  ? 25.633 -13.215 25.239 1.00 41.39 ? 42  LYS A CE    1 
ATOM   341  N  NZ    . LYS A 1 42  ? 24.288 -13.373 25.822 1.00 42.52 ? 42  LYS A NZ    1 
ATOM   342  N  N     . ILE A 1 43  ? 27.162 -8.995  19.961 1.00 27.73 ? 43  ILE A N     1 
ATOM   343  C  CA    . ILE A 1 43  ? 27.911 -7.908  19.356 1.00 27.45 ? 43  ILE A CA    1 
ATOM   344  C  C     . ILE A 1 43  ? 26.952 -6.914  18.707 1.00 24.84 ? 43  ILE A C     1 
ATOM   345  O  O     . ILE A 1 43  ? 25.959 -7.306  18.093 1.00 23.48 ? 43  ILE A O     1 
ATOM   346  C  CB    . ILE A 1 43  ? 28.907 -8.507  18.349 1.00 29.14 ? 43  ILE A CB    1 
ATOM   347  C  CG1   . ILE A 1 43  ? 30.015 -9.253  19.106 1.00 30.44 ? 43  ILE A CG1   1 
ATOM   348  C  CG2   . ILE A 1 43  ? 29.459 -7.453  17.383 1.00 29.30 ? 43  ILE A CG2   1 
ATOM   349  C  CD1   . ILE A 1 43  ? 31.033 -9.886  18.213 1.00 31.78 ? 43  ILE A CD1   1 
ATOM   350  N  N     . ILE A 1 44  ? 27.294 -5.624  18.817 1.00 24.89 ? 44  ILE A N     1 
ATOM   351  C  CA    . ILE A 1 44  ? 26.532 -4.583  18.161 1.00 23.70 ? 44  ILE A CA    1 
ATOM   352  C  C     . ILE A 1 44  ? 26.917 -4.571  16.687 1.00 22.59 ? 44  ILE A C     1 
ATOM   353  O  O     . ILE A 1 44  ? 28.097 -4.593  16.334 1.00 22.05 ? 44  ILE A O     1 
ATOM   354  C  CB    . ILE A 1 44  ? 26.738 -3.218  18.844 1.00 24.43 ? 44  ILE A CB    1 
ATOM   355  C  CG1   . ILE A 1 44  ? 26.145 -3.177  20.251 1.00 26.09 ? 44  ILE A CG1   1 
ATOM   356  C  CG2   . ILE A 1 44  ? 26.129 -2.135  17.982 1.00 24.10 ? 44  ILE A CG2   1 
ATOM   357  C  CD1   . ILE A 1 44  ? 24.622 -3.280  20.288 1.00 26.61 ? 44  ILE A CD1   1 
ATOM   358  N  N     . LEU A 1 45  ? 25.903 -4.550  15.826 1.00 21.12 ? 45  LEU A N     1 
ATOM   359  C  CA    . LEU A 1 45  ? 26.131 -4.533  14.380 1.00 21.26 ? 45  LEU A CA    1 
ATOM   360  C  C     . LEU A 1 45  ? 26.741 -3.185  13.971 1.00 21.52 ? 45  LEU A C     1 
ATOM   361  O  O     . LEU A 1 45  ? 26.254 -2.119  14.344 1.00 20.72 ? 45  LEU A O     1 
ATOM   362  C  CB    . LEU A 1 45  ? 24.809 -4.800  13.654 1.00 20.35 ? 45  LEU A CB    1 
ATOM   363  C  CG    . LEU A 1 45  ? 24.880 -4.785  12.125 1.00 20.89 ? 45  LEU A CG    1 
ATOM   364  C  CD1   . LEU A 1 45  ? 25.643 -5.978  11.603 1.00 23.07 ? 45  LEU A CD1   1 
ATOM   365  C  CD2   . LEU A 1 45  ? 23.514 -4.709  11.494 1.00 20.92 ? 45  LEU A CD2   1 
ATOM   366  N  N     . ASP A 1 46  ? 27.820 -3.264  13.187 1.00 22.41 ? 46  ASP A N     1 
ATOM   367  C  CA    . ASP A 1 46  ? 28.585 -2.111  12.728 1.00 23.26 ? 46  ASP A CA    1 
ATOM   368  C  C     . ASP A 1 46  ? 29.017 -2.321  11.273 1.00 23.93 ? 46  ASP A C     1 
ATOM   369  O  O     . ASP A 1 46  ? 29.933 -3.108  10.986 1.00 24.29 ? 46  ASP A O     1 
ATOM   370  C  CB    . ASP A 1 46  ? 29.770 -1.901  13.651 1.00 23.90 ? 46  ASP A CB    1 
ATOM   371  C  CG    . ASP A 1 46  ? 30.594 -0.672  13.329 1.00 26.84 ? 46  ASP A CG    1 
ATOM   372  O  OD1   . ASP A 1 46  ? 30.444 -0.133  12.208 1.00 26.76 ? 46  ASP A OD1   1 
ATOM   373  O  OD2   . ASP A 1 46  ? 31.396 -0.296  14.207 1.00 29.23 ? 46  ASP A OD2   1 
ATOM   374  N  N     . SER A 1 47  ? 28.367 -1.604  10.350 1.00 24.68 ? 47  SER A N     1 
ATOM   375  C  CA    . SER A 1 47  ? 28.582 -1.852  8.929  1.00 26.70 ? 47  SER A CA    1 
ATOM   376  C  C     . SER A 1 47  ? 30.048 -1.680  8.532  1.00 28.03 ? 47  SER A C     1 
ATOM   377  O  O     . SER A 1 47  ? 30.471 -2.282  7.550  1.00 28.56 ? 47  SER A O     1 
ATOM   378  C  CB    . SER A 1 47  ? 27.682 -1.023  8.043  1.00 28.08 ? 47  SER A CB    1 
ATOM   379  O  OG    . SER A 1 47  ? 27.903 0.367   8.253  1.00 28.05 ? 47  SER A OG    1 
ATOM   380  N  N     . THR A 1 48  ? 30.815 -0.870  9.282  1.00 27.46 ? 48  THR A N     1 
ATOM   381  C  CA    . THR A 1 48  ? 32.233 -0.683  9.025  1.00 28.42 ? 48  THR A CA    1 
ATOM   382  C  C     . THR A 1 48  ? 32.997 -2.014  9.090  1.00 30.81 ? 48  THR A C     1 
ATOM   383  O  O     . THR A 1 48  ? 33.911 -2.253  8.306  1.00 30.17 ? 48  THR A O     1 
ATOM   384  C  CB    . THR A 1 48  ? 32.800 0.405   9.943  1.00 28.35 ? 48  THR A CB    1 
ATOM   385  O  OG1   . THR A 1 48  ? 32.243 1.673   9.589  1.00 28.93 ? 48  THR A OG1   1 
ATOM   386  C  CG2   . THR A 1 48  ? 34.293 0.563   9.840  1.00 30.74 ? 48  THR A CG2   1 
ATOM   387  N  N     . TYR A 1 49  ? 32.622 -2.895  10.005 1.00 31.48 ? 49  TYR A N     1 
ATOM   388  C  CA    . TYR A 1 49  ? 33.284 -4.177  10.134 1.00 33.80 ? 49  TYR A CA    1 
ATOM   389  C  C     . TYR A 1 49  ? 32.485 -5.261  9.421  1.00 32.90 ? 49  TYR A C     1 
ATOM   390  O  O     . TYR A 1 49  ? 33.065 -6.236  8.960  1.00 35.34 ? 49  TYR A O     1 
ATOM   391  C  CB    . TYR A 1 49  ? 33.466 -4.449  11.628 1.00 37.78 ? 49  TYR A CB    1 
ATOM   392  C  CG    . TYR A 1 49  ? 34.534 -3.588  12.286 1.00 45.92 ? 49  TYR A CG    1 
ATOM   393  C  CD1   . TYR A 1 49  ? 35.841 -3.585  11.810 1.00 48.70 ? 49  TYR A CD1   1 
ATOM   394  C  CD2   . TYR A 1 49  ? 34.261 -2.819  13.413 1.00 51.18 ? 49  TYR A CD2   1 
ATOM   395  C  CE1   . TYR A 1 49  ? 36.830 -2.816  12.408 1.00 51.11 ? 49  TYR A CE1   1 
ATOM   396  C  CE2   . TYR A 1 49  ? 35.249 -2.062  14.030 1.00 53.59 ? 49  TYR A CE2   1 
ATOM   397  C  CZ    . TYR A 1 49  ? 36.537 -2.055  13.521 1.00 52.29 ? 49  TYR A CZ    1 
ATOM   398  O  OH    . TYR A 1 49  ? 37.523 -1.311  14.100 1.00 55.67 ? 49  TYR A OH    1 
ATOM   399  N  N     . HIS A 1 50  ? 31.161 -5.093  9.318  1.00 30.51 ? 50  HIS A N     1 
ATOM   400  C  CA    . HIS A 1 50  ? 30.261 -6.205  9.068  1.00 29.74 ? 50  HIS A CA    1 
ATOM   401  C  C     . HIS A 1 50  ? 29.593 -6.133  7.692  1.00 31.66 ? 50  HIS A C     1 
ATOM   402  O  O     . HIS A 1 50  ? 28.700 -6.930  7.394  1.00 29.95 ? 50  HIS A O     1 
ATOM   403  C  CB    . HIS A 1 50  ? 29.220 -6.257  10.194 1.00 28.00 ? 50  HIS A CB    1 
ATOM   404  C  CG    . HIS A 1 50  ? 29.819 -6.466  11.547 1.00 26.95 ? 50  HIS A CG    1 
ATOM   405  N  ND1   . HIS A 1 50  ? 29.281 -5.922  12.696 1.00 24.93 ? 50  HIS A ND1   1 
ATOM   406  C  CD2   . HIS A 1 50  ? 30.908 -7.161  11.932 1.00 27.86 ? 50  HIS A CD2   1 
ATOM   407  C  CE1   . HIS A 1 50  ? 30.019 -6.289  13.737 1.00 26.43 ? 50  HIS A CE1   1 
ATOM   408  N  NE2   . HIS A 1 50  ? 31.037 -7.036  13.294 1.00 27.66 ? 50  HIS A NE2   1 
ATOM   409  N  N     . HIS A 1 51  ? 30.032 -5.187  6.855  1.00 33.72 ? 51  HIS A N     1 
ATOM   410  C  CA    . HIS A 1 51  ? 29.402 -4.882  5.574  1.00 37.45 ? 51  HIS A CA    1 
ATOM   411  C  C     . HIS A 1 51  ? 29.307 -6.109  4.660  1.00 39.52 ? 51  HIS A C     1 
ATOM   412  O  O     . HIS A 1 51  ? 28.290 -6.288  3.995  1.00 41.44 ? 51  HIS A O     1 
ATOM   413  C  CB    . HIS A 1 51  ? 30.149 -3.744  4.854  1.00 41.02 ? 51  HIS A CB    1 
ATOM   414  C  CG    . HIS A 1 51  ? 31.606 -3.999  4.682  1.00 43.12 ? 51  HIS A CG    1 
ATOM   415  N  ND1   . HIS A 1 51  ? 32.126 -4.648  3.577  1.00 47.56 ? 51  HIS A ND1   1 
ATOM   416  C  CD2   . HIS A 1 51  ? 32.651 -3.693  5.466  1.00 44.95 ? 51  HIS A CD2   1 
ATOM   417  C  CE1   . HIS A 1 51  ? 33.442 -4.733  3.707  1.00 46.89 ? 51  HIS A CE1   1 
ATOM   418  N  NE2   . HIS A 1 51  ? 33.787 -4.152  4.840  1.00 46.86 ? 51  HIS A NE2   1 
ATOM   419  N  N     . ALA A 1 52  ? 30.343 -6.958  4.632  1.00 41.03 ? 52  ALA A N     1 
ATOM   420  C  CA    . ALA A 1 52  ? 30.346 -8.124  3.755  1.00 42.01 ? 52  ALA A CA    1 
ATOM   421  C  C     . ALA A 1 52  ? 29.144 -9.013  4.061  1.00 43.19 ? 52  ALA A C     1 
ATOM   422  O  O     . ALA A 1 52  ? 28.498 -9.501  3.138  1.00 46.56 ? 52  ALA A O     1 
ATOM   423  C  CB    . ALA A 1 52  ? 31.639 -8.886  3.892  1.00 42.43 ? 52  ALA A CB    1 
ATOM   424  N  N     . ALA A 1 53  ? 28.819 -9.155  5.353  1.00 38.29 ? 53  ALA A N     1 
ATOM   425  C  CA    . ALA A 1 53  ? 27.703 -9.967  5.808  1.00 38.60 ? 53  ALA A CA    1 
ATOM   426  C  C     . ALA A 1 53  ? 26.359 -9.272  5.556  1.00 39.95 ? 53  ALA A C     1 
ATOM   427  O  O     . ALA A 1 53  ? 25.328 -9.929  5.529  1.00 39.75 ? 53  ALA A O     1 
ATOM   428  C  CB    . ALA A 1 53  ? 27.891 -10.308 7.268  1.00 35.97 ? 53  ALA A CB    1 
ATOM   429  N  N     . LEU A 1 54  ? 26.348 -7.954  5.341  1.00 38.96 ? 54  LEU A N     1 
ATOM   430  C  CA    . LEU A 1 54  ? 25.084 -7.259  5.143  1.00 40.26 ? 54  LEU A CA    1 
ATOM   431  C  C     . LEU A 1 54  ? 24.596 -7.326  3.692  1.00 41.53 ? 54  LEU A C     1 
ATOM   432  O  O     . LEU A 1 54  ? 23.441 -6.993  3.448  1.00 39.02 ? 54  LEU A O     1 
ATOM   433  C  CB    . LEU A 1 54  ? 25.229 -5.806  5.619  1.00 38.01 ? 54  LEU A CB    1 
ATOM   434  C  CG    . LEU A 1 54  ? 25.324 -5.641  7.137  1.00 38.67 ? 54  LEU A CG    1 
ATOM   435  C  CD1   . LEU A 1 54  ? 25.526 -4.172  7.514  1.00 38.66 ? 54  LEU A CD1   1 
ATOM   436  C  CD2   . LEU A 1 54  ? 24.085 -6.187  7.819  1.00 37.79 ? 54  LEU A CD2   1 
ATOM   437  N  N     . ARG A 1 55  ? 25.447 -7.739  2.744  1.00 45.81 ? 55  ARG A N     1 
ATOM   438  C  CA    . ARG A 1 55  ? 25.127 -7.683  1.316  1.00 50.19 ? 55  ARG A CA    1 
ATOM   439  C  C     . ARG A 1 55  ? 23.768 -8.308  1.006  1.00 55.07 ? 55  ARG A C     1 
ATOM   440  O  O     . ARG A 1 55  ? 23.058 -7.857  0.106  1.00 58.19 ? 55  ARG A O     1 
ATOM   441  C  CB    . ARG A 1 55  ? 26.124 -8.484  0.479  1.00 53.66 ? 55  ARG A CB    1 
ATOM   442  C  CG    . ARG A 1 55  ? 27.561 -7.981  0.479  1.00 57.62 ? 55  ARG A CG    1 
ATOM   443  C  CD    . ARG A 1 55  ? 28.458 -9.048  -0.149 1.00 61.59 ? 55  ARG A CD    1 
ATOM   444  N  NE    . ARG A 1 55  ? 29.885 -8.874  0.100  1.00 66.42 ? 55  ARG A NE    1 
ATOM   445  C  CZ    . ARG A 1 55  ? 30.625 -7.860  -0.346 1.00 72.33 ? 55  ARG A CZ    1 
ATOM   446  N  NH1   . ARG A 1 55  ? 30.088 -6.930  -1.119 1.00 72.02 ? 55  ARG A NH1   1 
ATOM   447  N  NH2   . ARG A 1 55  ? 31.907 -7.781  -0.020 1.00 75.02 ? 55  ARG A NH2   1 
ATOM   448  N  N     . GLN A 1 56  ? 23.423 -9.383  1.719  1.00 56.74 ? 56  GLN A N     1 
ATOM   449  C  CA    . GLN A 1 56  ? 22.240 -10.151 1.377  1.00 63.17 ? 56  GLN A CA    1 
ATOM   450  C  C     . GLN A 1 56  ? 21.119 -9.887  2.382  1.00 58.69 ? 56  GLN A C     1 
ATOM   451  O  O     . GLN A 1 56  ? 20.032 -10.419 2.222  1.00 59.03 ? 56  GLN A O     1 
ATOM   452  C  CB    . GLN A 1 56  ? 22.568 -11.643 1.184  1.00 74.76 ? 56  GLN A CB    1 
ATOM   453  C  CG    . GLN A 1 56  ? 23.932 -12.110 1.701  1.00 84.12 ? 56  GLN A CG    1 
ATOM   454  C  CD    . GLN A 1 56  ? 23.957 -12.427 3.178  1.00 88.91 ? 56  GLN A CD    1 
ATOM   455  O  OE1   . GLN A 1 56  ? 23.488 -13.474 3.620  1.00 93.39 ? 56  GLN A OE1   1 
ATOM   456  N  NE2   . GLN A 1 56  ? 24.544 -11.537 3.960  1.00 90.06 ? 56  GLN A NE2   1 
ATOM   457  N  N     . LEU A 1 57  ? 21.339 -9.022  3.377  1.00 51.87 ? 57  LEU A N     1 
ATOM   458  C  CA    . LEU A 1 57  ? 20.324 -8.790  4.387  1.00 51.39 ? 57  LEU A CA    1 
ATOM   459  C  C     . LEU A 1 57  ? 19.356 -7.728  3.896  1.00 50.23 ? 57  LEU A C     1 
ATOM   460  O  O     . LEU A 1 57  ? 19.788 -6.744  3.298  1.00 48.62 ? 57  LEU A O     1 
ATOM   461  C  CB    . LEU A 1 57  ? 20.985 -8.307  5.682  1.00 51.12 ? 57  LEU A CB    1 
ATOM   462  C  CG    . LEU A 1 57  ? 20.981 -9.279  6.852  1.00 54.84 ? 57  LEU A CG    1 
ATOM   463  C  CD1   . LEU A 1 57  ? 21.085 -8.512  8.159  1.00 53.90 ? 57  LEU A CD1   1 
ATOM   464  C  CD2   . LEU A 1 57  ? 19.740 -10.152 6.854  1.00 58.06 ? 57  LEU A CD2   1 
ATOM   465  N  N     . GLU A 1 58  ? 18.074 -7.885  4.252  1.00 47.76 ? 58  GLU A N     1 
ATOM   466  C  CA    . GLU A 1 58  ? 17.085 -6.849  4.005  1.00 47.16 ? 58  GLU A CA    1 
ATOM   467  C  C     . GLU A 1 58  ? 17.533 -5.558  4.691  1.00 43.89 ? 58  GLU A C     1 
ATOM   468  O  O     . GLU A 1 58  ? 17.951 -5.590  5.859  1.00 39.53 ? 58  GLU A O     1 
ATOM   469  C  CB    . GLU A 1 58  ? 15.702 -7.300  4.482  1.00 51.21 ? 58  GLU A CB    1 
ATOM   470  C  CG    . GLU A 1 58  ? 14.635 -6.245  4.270  1.00 54.43 ? 58  GLU A CG    1 
ATOM   471  C  CD    . GLU A 1 58  ? 13.222 -6.681  4.608  1.00 64.71 ? 58  GLU A CD    1 
ATOM   472  O  OE1   . GLU A 1 58  ? 12.332 -5.806  4.665  1.00 70.07 ? 58  GLU A OE1   1 
ATOM   473  O  OE2   . GLU A 1 58  ? 13.011 -7.893  4.807  1.00 67.87 ? 58  GLU A OE2   1 
ATOM   474  N  N     . ASP A 1 59  ? 17.476 -4.446  3.932  1.00 40.84 ? 59  ASP A N     1 
ATOM   475  C  CA    . ASP A 1 59  ? 17.922 -3.124  4.359  1.00 40.87 ? 59  ASP A CA    1 
ATOM   476  C  C     . ASP A 1 59  ? 19.395 -3.145  4.768  1.00 36.77 ? 59  ASP A C     1 
ATOM   477  O  O     . ASP A 1 59  ? 19.848 -2.260  5.498  1.00 36.21 ? 59  ASP A O     1 
ATOM   478  C  CB    . ASP A 1 59  ? 17.132 -2.584  5.559  1.00 45.44 ? 59  ASP A CB    1 
ATOM   479  C  CG    . ASP A 1 59  ? 15.800 -1.949  5.227  1.00 49.23 ? 59  ASP A CG    1 
ATOM   480  O  OD1   . ASP A 1 59  ? 15.407 -2.024  4.043  1.00 48.72 ? 59  ASP A OD1   1 
ATOM   481  O  OD2   . ASP A 1 59  ? 15.189 -1.352  6.160  1.00 43.24 ? 59  ASP A OD2   1 
ATOM   482  N  N     . GLY A 1 60  ? 20.145 -4.128  4.257  1.00 36.09 ? 60  GLY A N     1 
ATOM   483  C  CA    . GLY A 1 60  ? 21.532 -4.329  4.626  1.00 35.77 ? 60  GLY A CA    1 
ATOM   484  C  C     . GLY A 1 60  ? 22.349 -3.049  4.515  1.00 37.25 ? 60  GLY A C     1 
ATOM   485  O  O     . GLY A 1 60  ? 23.252 -2.826  5.318  1.00 37.47 ? 60  GLY A O     1 
ATOM   486  N  N     . GLU A 1 61  ? 21.983 -2.199  3.553  1.00 37.35 ? 61  GLU A N     1 
ATOM   487  C  CA    . GLU A 1 61  ? 22.789 -1.045  3.184  1.00 40.68 ? 61  GLU A CA    1 
ATOM   488  C  C     . GLU A 1 61  ? 22.605 0.107   4.168  1.00 35.43 ? 61  GLU A C     1 
ATOM   489  O  O     . GLU A 1 61  ? 23.389 1.050   4.143  1.00 34.40 ? 61  GLU A O     1 
ATOM   490  C  CB    . GLU A 1 61  ? 22.421 -0.575  1.769  1.00 45.67 ? 61  GLU A CB    1 
ATOM   491  C  CG    . GLU A 1 61  ? 21.187 0.322   1.709  1.00 49.91 ? 61  GLU A CG    1 
ATOM   492  C  CD    . GLU A 1 61  ? 19.817 -0.319  1.902  1.00 55.00 ? 61  GLU A CD    1 
ATOM   493  O  OE1   . GLU A 1 61  ? 18.838 0.455   1.996  1.00 57.88 ? 61  GLU A OE1   1 
ATOM   494  O  OE2   . GLU A 1 61  ? 19.713 -1.586  1.926  1.00 58.61 ? 61  GLU A OE2   1 
ATOM   495  N  N     . ARG A 1 62  ? 21.529 0.102   4.968  1.00 32.67 ? 62  ARG A N     1 
ATOM   496  C  CA    . ARG A 1 62  ? 21.334 1.166   5.950  1.00 32.00 ? 62  ARG A CA    1 
ATOM   497  C  C     . ARG A 1 62  ? 21.521 0.682   7.394  1.00 27.81 ? 62  ARG A C     1 
ATOM   498  O  O     . ARG A 1 62  ? 21.514 1.513   8.316  1.00 26.04 ? 62  ARG A O     1 
ATOM   499  C  CB    . ARG A 1 62  ? 19.958 1.834   5.817  1.00 35.32 ? 62  ARG A CB    1 
ATOM   500  C  CG    . ARG A 1 62  ? 18.775 0.966   6.214  1.00 37.96 ? 62  ARG A CG    1 
ATOM   501  C  CD    . ARG A 1 62  ? 17.430 1.615   5.927  1.00 40.30 ? 62  ARG A CD    1 
ATOM   502  N  NE    . ARG A 1 62  ? 16.863 2.368   7.041  1.00 38.00 ? 62  ARG A NE    1 
ATOM   503  C  CZ    . ARG A 1 62  ? 15.795 3.160   6.933  1.00 41.49 ? 62  ARG A CZ    1 
ATOM   504  N  NH1   . ARG A 1 62  ? 15.434 3.624   5.748  1.00 42.34 ? 62  ARG A NH1   1 
ATOM   505  N  NH2   . ARG A 1 62  ? 15.108 3.522   8.005  1.00 37.67 ? 62  ARG A NH2   1 
ATOM   506  N  N     . ARG A 1 63  ? 21.704 -0.635  7.602  1.00 26.45 ? 63  ARG A N     1 
ATOM   507  C  CA    . ARG A 1 63  ? 21.757 -1.182  8.953  1.00 24.45 ? 63  ARG A CA    1 
ATOM   508  C  C     . ARG A 1 63  ? 23.177 -1.086  9.518  1.00 22.77 ? 63  ARG A C     1 
ATOM   509  O  O     . ARG A 1 63  ? 24.159 -0.895  8.798  1.00 21.93 ? 63  ARG A O     1 
ATOM   510  C  CB    . ARG A 1 63  ? 21.211 -2.615  8.953  1.00 24.47 ? 63  ARG A CB    1 
ATOM   511  C  CG    . ARG A 1 63  ? 19.711 -2.629  8.708  1.00 24.75 ? 63  ARG A CG    1 
ATOM   512  C  CD    . ARG A 1 63  ? 19.134 -3.995  8.450  1.00 26.44 ? 63  ARG A CD    1 
ATOM   513  N  NE    . ARG A 1 63  ? 19.024 -4.757  9.683  1.00 26.86 ? 63  ARG A NE    1 
ATOM   514  C  CZ    . ARG A 1 63  ? 18.429 -5.926  9.753  1.00 26.98 ? 63  ARG A CZ    1 
ATOM   515  N  NH1   . ARG A 1 63  ? 17.981 -6.504  8.643  1.00 28.16 ? 63  ARG A NH1   1 
ATOM   516  N  NH2   . ARG A 1 63  ? 18.282 -6.518  10.921 1.00 26.81 ? 63  ARG A NH2   1 
ATOM   517  N  N     . GLY A 1 64  ? 23.258 -1.190  10.848 1.00 20.77 ? 64  GLY A N     1 
ATOM   518  C  CA    . GLY A 1 64  ? 24.531 -1.222  11.532 1.00 20.16 ? 64  GLY A CA    1 
ATOM   519  C  C     . GLY A 1 64  ? 25.226 0.136   11.530 1.00 18.82 ? 64  GLY A C     1 
ATOM   520  O  O     . GLY A 1 64  ? 26.406 0.222   11.178 1.00 18.85 ? 64  GLY A O     1 
ATOM   521  N  N     . ARG A 1 65  ? 24.503 1.165   11.974 1.00 18.56 ? 65  ARG A N     1 
ATOM   522  C  CA    . ARG A 1 65  ? 25.065 2.520   12.037 1.00 18.76 ? 65  ARG A CA    1 
ATOM   523  C  C     . ARG A 1 65  ? 24.958 3.074   13.447 1.00 18.40 ? 65  ARG A C     1 
ATOM   524  O  O     . ARG A 1 65  ? 24.374 4.143   13.683 1.00 18.55 ? 65  ARG A O     1 
ATOM   525  C  CB    . ARG A 1 65  ? 24.395 3.461   11.030 1.00 19.20 ? 65  ARG A CB    1 
ATOM   526  C  CG    . ARG A 1 65  ? 24.677 3.096   9.574  1.00 21.62 ? 65  ARG A CG    1 
ATOM   527  C  CD    . ARG A 1 65  ? 26.159 3.130   9.264  1.00 23.80 ? 65  ARG A CD    1 
ATOM   528  N  NE    . ARG A 1 65  ? 26.744 4.460   9.500  1.00 25.93 ? 65  ARG A NE    1 
ATOM   529  C  CZ    . ARG A 1 65  ? 26.519 5.515   8.707  1.00 29.72 ? 65  ARG A CZ    1 
ATOM   530  N  NH1   . ARG A 1 65  ? 26.120 5.329   7.452  1.00 31.46 ? 65  ARG A NH1   1 
ATOM   531  N  NH2   . ARG A 1 65  ? 26.790 6.730   9.134  1.00 27.22 ? 65  ARG A NH2   1 
ATOM   532  N  N     . PRO A 1 66  ? 25.548 2.388   14.447 1.00 17.01 ? 66  PRO A N     1 
ATOM   533  C  CA    . PRO A 1 66  ? 25.481 2.909   15.822 1.00 17.22 ? 66  PRO A CA    1 
ATOM   534  C  C     . PRO A 1 66  ? 26.252 4.230   16.009 1.00 17.52 ? 66  PRO A C     1 
ATOM   535  O  O     . PRO A 1 66  ? 25.989 4.945   16.982 1.00 17.13 ? 66  PRO A O     1 
ATOM   536  C  CB    . PRO A 1 66  ? 26.019 1.739   16.633 1.00 17.15 ? 66  PRO A CB    1 
ATOM   537  C  CG    . PRO A 1 66  ? 26.954 1.059   15.674 1.00 17.55 ? 66  PRO A CG    1 
ATOM   538  C  CD    . PRO A 1 66  ? 26.320 1.164   14.309 1.00 17.17 ? 66  PRO A CD    1 
ATOM   539  N  N     . ASP A 1 67  ? 27.148 4.561   15.061 1.00 17.84 ? 67  ASP A N     1 
ATOM   540  C  CA    . ASP A 1 67  ? 27.832 5.858   15.031 1.00 21.38 ? 67  ASP A CA    1 
ATOM   541  C  C     . ASP A 1 67  ? 26.846 7.036   15.017 1.00 21.07 ? 67  ASP A C     1 
ATOM   542  O  O     . ASP A 1 67  ? 27.110 8.082   15.611 1.00 22.16 ? 67  ASP A O     1 
ATOM   543  C  CB    . ASP A 1 67  ? 28.813 5.939   13.860 1.00 22.43 ? 67  ASP A CB    1 
ATOM   544  C  CG    . ASP A 1 67  ? 28.129 5.700   12.517 1.00 26.38 ? 67  ASP A CG    1 
ATOM   545  O  OD1   . ASP A 1 67  ? 27.488 4.663   12.353 1.00 26.97 ? 67  ASP A OD1   1 
ATOM   546  O  OD2   . ASP A 1 67  ? 28.197 6.571   11.666 1.00 31.59 ? 67  ASP A OD2   1 
ATOM   547  N  N     . ILE A 1 68  ? 25.717 6.901   14.306 1.00 20.14 ? 68  ILE A N     1 
ATOM   548  C  CA    . ILE A 1 68  ? 24.750 7.983   14.216 1.00 19.86 ? 68  ILE A CA    1 
ATOM   549  C  C     . ILE A 1 68  ? 24.175 8.281   15.596 1.00 18.67 ? 68  ILE A C     1 
ATOM   550  O  O     . ILE A 1 68  ? 24.043 9.435   15.976 1.00 19.35 ? 68  ILE A O     1 
ATOM   551  C  CB    . ILE A 1 68  ? 23.638 7.677   13.202 1.00 19.78 ? 68  ILE A CB    1 
ATOM   552  C  CG1   . ILE A 1 68  ? 24.191 7.527   11.777 1.00 21.01 ? 68  ILE A CG1   1 
ATOM   553  C  CG2   . ILE A 1 68  ? 22.573 8.760   13.278 1.00 20.45 ? 68  ILE A CG2   1 
ATOM   554  C  CD1   . ILE A 1 68  ? 23.154 7.145   10.697 1.00 22.00 ? 68  ILE A CD1   1 
ATOM   555  N  N     . VAL A 1 69  ? 23.803 7.252   16.340 1.00 17.42 ? 69  VAL A N     1 
ATOM   556  C  CA    . VAL A 1 69  ? 23.309 7.442   17.689 1.00 18.22 ? 69  VAL A CA    1 
ATOM   557  C  C     . VAL A 1 69  ? 24.384 8.060   18.568 1.00 17.00 ? 69  VAL A C     1 
ATOM   558  O  O     . VAL A 1 69  ? 24.094 8.931   19.371 1.00 17.30 ? 69  VAL A O     1 
ATOM   559  C  CB    . VAL A 1 69  ? 22.851 6.106   18.281 1.00 20.13 ? 69  VAL A CB    1 
ATOM   560  C  CG1   . VAL A 1 69  ? 22.446 6.261   19.742 1.00 21.80 ? 69  VAL A CG1   1 
ATOM   561  C  CG2   . VAL A 1 69  ? 21.728 5.524   17.443 1.00 20.80 ? 69  VAL A CG2   1 
ATOM   562  N  N     . HIS A 1 70  ? 25.623 7.576   18.452 1.00 15.83 ? 70  HIS A N     1 
ATOM   563  C  CA    . HIS A 1 70  ? 26.696 8.071   19.316 1.00 16.33 ? 70  HIS A CA    1 
ATOM   564  C  C     . HIS A 1 70  ? 26.853 9.586   19.180 1.00 15.84 ? 70  HIS A C     1 
ATOM   565  O  O     . HIS A 1 70  ? 26.860 10.309  20.179 1.00 15.90 ? 70  HIS A O     1 
ATOM   566  C  CB    . HIS A 1 70  ? 28.011 7.328   19.051 1.00 16.44 ? 70  HIS A CB    1 
ATOM   567  C  CG    . HIS A 1 70  ? 29.152 7.733   19.912 1.00 17.86 ? 70  HIS A CG    1 
ATOM   568  N  ND1   . HIS A 1 70  ? 30.405 7.945   19.377 1.00 18.72 ? 70  HIS A ND1   1 
ATOM   569  C  CD2   . HIS A 1 70  ? 29.278 7.893   21.238 1.00 18.68 ? 70  HIS A CD2   1 
ATOM   570  C  CE1   . HIS A 1 70  ? 31.241 8.241   20.349 1.00 19.67 ? 70  HIS A CE1   1 
ATOM   571  N  NE2   . HIS A 1 70  ? 30.590 8.223   21.496 1.00 19.09 ? 70  HIS A NE2   1 
ATOM   572  N  N     . ILE A 1 71  ? 26.962 10.054  17.936 1.00 15.98 ? 71  ILE A N     1 
ATOM   573  C  CA    . ILE A 1 71  ? 27.212 11.453  17.646 1.00 17.26 ? 71  ILE A CA    1 
ATOM   574  C  C     . ILE A 1 71  ? 25.975 12.282  17.979 1.00 16.08 ? 71  ILE A C     1 
ATOM   575  O  O     . ILE A 1 71  ? 26.098 13.330  18.599 1.00 15.70 ? 71  ILE A O     1 
ATOM   576  C  CB    . ILE A 1 71  ? 27.724 11.663  16.192 1.00 20.96 ? 71  ILE A CB    1 
ATOM   577  C  CG1   . ILE A 1 71  ? 29.011 10.847  15.974 1.00 27.08 ? 71  ILE A CG1   1 
ATOM   578  C  CG2   . ILE A 1 71  ? 27.950 13.170  16.037 1.00 22.70 ? 71  ILE A CG2   1 
ATOM   579  C  CD1   . ILE A 1 71  ? 29.338 10.304  14.550 1.00 30.64 ? 71  ILE A CD1   1 
ATOM   580  N  N     . CYS A 1 72  ? 24.773 11.781  17.681 1.00 14.74 ? 72  CYS A N     1 
ATOM   581  C  CA    . CYS A 1 72  ? 23.568 12.459  18.120 1.00 15.73 ? 72  CYS A CA    1 
ATOM   582  C  C     . CYS A 1 72  ? 23.539 12.648  19.651 1.00 16.42 ? 72  CYS A C     1 
ATOM   583  O  O     . CYS A 1 72  ? 23.133 13.715  20.122 1.00 15.71 ? 72  CYS A O     1 
ATOM   584  C  CB    . CYS A 1 72  ? 22.301 11.753  17.648 1.00 15.91 ? 72  CYS A CB    1 
ATOM   585  S  SG    . CYS A 1 72  ? 22.021 11.943  15.865 1.00 18.32 ? 72  CYS A SG    1 
ATOM   586  N  N     . LEU A 1 73  ? 23.836 11.588  20.400 1.00 15.60 ? 73  LEU A N     1 
ATOM   587  C  CA    . LEU A 1 73  ? 23.727 11.653  21.863 1.00 16.77 ? 73  LEU A CA    1 
ATOM   588  C  C     . LEU A 1 73  ? 24.842 12.490  22.484 1.00 17.43 ? 73  LEU A C     1 
ATOM   589  O  O     . LEU A 1 73  ? 24.629 13.165  23.508 1.00 18.92 ? 73  LEU A O     1 
ATOM   590  C  CB    . LEU A 1 73  ? 23.772 10.238  22.441 1.00 16.49 ? 73  LEU A CB    1 
ATOM   591  C  CG    . LEU A 1 73  ? 22.547 9.374   22.201 1.00 16.75 ? 73  LEU A CG    1 
ATOM   592  C  CD1   . LEU A 1 73  ? 22.696 8.006   22.858 1.00 17.69 ? 73  LEU A CD1   1 
ATOM   593  C  CD2   . LEU A 1 73  ? 21.277 10.056  22.679 1.00 17.25 ? 73  LEU A CD2   1 
ATOM   594  N  N     . LEU A 1 74  ? 26.050 12.431  21.916 1.00 17.96 ? 74  LEU A N     1 
ATOM   595  C  CA    . LEU A 1 74  ? 27.091 13.308  22.426 1.00 19.64 ? 74  LEU A CA    1 
ATOM   596  C  C     . LEU A 1 74  ? 26.633 14.764  22.313 1.00 20.55 ? 74  LEU A C     1 
ATOM   597  O  O     . LEU A 1 74  ? 26.811 15.555  23.255 1.00 20.73 ? 74  LEU A O     1 
ATOM   598  C  CB    . LEU A 1 74  ? 28.409 13.076  21.670 1.00 19.68 ? 74  LEU A CB    1 
ATOM   599  C  CG    . LEU A 1 74  ? 29.170 11.830  22.093 1.00 20.17 ? 74  LEU A CG    1 
ATOM   600  C  CD1   . LEU A 1 74  ? 30.483 11.773  21.368 1.00 21.16 ? 74  LEU A CD1   1 
ATOM   601  C  CD2   . LEU A 1 74  ? 29.428 11.839  23.593 1.00 21.37 ? 74  LEU A CD2   1 
ATOM   602  N  N     . ASN A 1 75  ? 26.113 15.113  21.132 1.00 18.90 ? 75  ASN A N     1 
ATOM   603  C  CA    . ASN A 1 75  ? 25.609 16.437  20.816 1.00 20.09 ? 75  ASN A CA    1 
ATOM   604  C  C     . ASN A 1 75  ? 24.466 16.827  21.763 1.00 20.46 ? 75  ASN A C     1 
ATOM   605  O  O     . ASN A 1 75  ? 24.481 17.916  22.354 1.00 23.99 ? 75  ASN A O     1 
ATOM   606  C  CB    . ASN A 1 75  ? 25.173 16.520  19.356 1.00 19.91 ? 75  ASN A CB    1 
ATOM   607  C  CG    . ASN A 1 75  ? 26.302 16.731  18.363 1.00 22.54 ? 75  ASN A CG    1 
ATOM   608  O  OD1   . ASN A 1 75  ? 27.319 17.333  18.662 1.00 21.89 ? 75  ASN A OD1   1 
ATOM   609  N  ND2   . ASN A 1 75  ? 26.006 16.485  17.103 1.00 28.18 ? 75  ASN A ND2   1 
ATOM   610  N  N     . ALA A 1 76  ? 23.533 15.911  22.005 1.00 17.11 ? 76  ALA A N     1 
ATOM   611  C  CA    . ALA A 1 76  ? 22.384 16.225  22.829 1.00 18.05 ? 76  ALA A CA    1 
ATOM   612  C  C     . ALA A 1 76  ? 22.735 16.358  24.308 1.00 18.13 ? 76  ALA A C     1 
ATOM   613  O  O     . ALA A 1 76  ? 22.309 17.323  24.959 1.00 18.00 ? 76  ALA A O     1 
ATOM   614  C  CB    . ALA A 1 76  ? 21.318 15.166  22.616 1.00 18.44 ? 76  ALA A CB    1 
ATOM   615  N  N     . LEU A 1 77  ? 23.460 15.369  24.848 1.00 18.57 ? 77  LEU A N     1 
ATOM   616  C  CA    . LEU A 1 77  ? 23.708 15.305  26.292 1.00 19.82 ? 77  LEU A CA    1 
ATOM   617  C  C     . LEU A 1 77  ? 24.707 16.359  26.769 1.00 20.57 ? 77  LEU A C     1 
ATOM   618  O  O     . LEU A 1 77  ? 24.673 16.723  27.926 1.00 19.27 ? 77  LEU A O     1 
ATOM   619  C  CB    . LEU A 1 77  ? 24.186 13.898  26.674 1.00 20.41 ? 77  LEU A CB    1 
ATOM   620  C  CG    . LEU A 1 77  ? 23.084 12.835  26.600 1.00 21.46 ? 77  LEU A CG    1 
ATOM   621  C  CD1   . LEU A 1 77  ? 23.666 11.447  26.729 1.00 21.67 ? 77  LEU A CD1   1 
ATOM   622  C  CD2   . LEU A 1 77  ? 22.040 13.052  27.687 1.00 24.35 ? 77  LEU A CD2   1 
ATOM   623  N  N     . ASP A 1 78  ? 25.642 16.779  25.898 1.00 21.12 ? 78  ASP A N     1 
ATOM   624  C  CA    . ASP A 1 78  ? 26.637 17.775  26.244 1.00 22.09 ? 78  ASP A CA    1 
ATOM   625  C  C     . ASP A 1 78  ? 26.104 19.186  25.984 1.00 20.10 ? 78  ASP A C     1 
ATOM   626  O  O     . ASP A 1 78  ? 26.754 20.174  26.302 1.00 19.83 ? 78  ASP A O     1 
ATOM   627  C  CB    . ASP A 1 78  ? 27.950 17.399  25.565 1.00 24.96 ? 78  ASP A CB    1 
ATOM   628  C  CG    . ASP A 1 78  ? 28.554 16.132  26.190 1.00 30.80 ? 78  ASP A CG    1 
ATOM   629  O  OD1   . ASP A 1 78  ? 28.734 16.075  27.478 1.00 31.27 ? 78  ASP A OD1   1 
ATOM   630  O  OD2   . ASP A 1 78  ? 28.843 15.205  25.433 1.00 35.04 ? 78  ASP A OD2   1 
ATOM   631  N  N     . SER A 1 79  ? 24.871 19.299  25.478 1.00 19.82 ? 79  SER A N     1 
ATOM   632  C  CA    . SER A 1 79  ? 24.309 20.597  25.136 1.00 19.58 ? 79  SER A CA    1 
ATOM   633  C  C     . SER A 1 79  ? 24.099 21.472  26.359 1.00 21.37 ? 79  SER A C     1 
ATOM   634  O  O     . SER A 1 79  ? 23.849 20.974  27.451 1.00 21.42 ? 79  SER A O     1 
ATOM   635  C  CB    . SER A 1 79  ? 23.014 20.481  24.328 1.00 19.03 ? 79  SER A CB    1 
ATOM   636  O  OG    . SER A 1 79  ? 21.962 19.861  25.032 1.00 17.67 ? 79  SER A OG    1 
ATOM   637  N  N     . ILE A 1 80  ? 24.102 22.794  26.130 1.00 22.11 ? 80  ILE A N     1 
ATOM   638  C  CA    . ILE A 1 80  ? 23.654 23.701  27.181 1.00 23.16 ? 80  ILE A CA    1 
ATOM   639  C  C     . ILE A 1 80  ? 22.212 23.373  27.545 1.00 23.29 ? 80  ILE A C     1 
ATOM   640  O  O     . ILE A 1 80  ? 21.865 23.382  28.726 1.00 24.75 ? 80  ILE A O     1 
ATOM   641  C  CB    . ILE A 1 80  ? 23.834 25.174  26.760 1.00 23.91 ? 80  ILE A CB    1 
ATOM   642  C  CG1   . ILE A 1 80  ? 25.316 25.516  26.573 1.00 24.83 ? 80  ILE A CG1   1 
ATOM   643  C  CG2   . ILE A 1 80  ? 23.097 26.122  27.701 1.00 25.70 ? 80  ILE A CG2   1 
ATOM   644  C  CD1   . ILE A 1 80  ? 25.573 26.872  25.929 1.00 25.54 ? 80  ILE A CD1   1 
ATOM   645  N  N     . LEU A 1 81  ? 21.354 23.117  26.551 1.00 22.07 ? 81  LEU A N     1 
ATOM   646  C  CA    . LEU A 1 81  ? 19.965 22.757  26.832 1.00 21.99 ? 81  LEU A CA    1 
ATOM   647  C  C     . LEU A 1 81  ? 19.866 21.626  27.854 1.00 22.26 ? 81  LEU A C     1 
ATOM   648  O  O     . LEU A 1 81  ? 19.038 21.703  28.761 1.00 21.94 ? 81  LEU A O     1 
ATOM   649  C  CB    . LEU A 1 81  ? 19.269 22.313  25.554 1.00 21.06 ? 81  LEU A CB    1 
ATOM   650  C  CG    . LEU A 1 81  ? 17.745 22.228  25.592 1.00 20.68 ? 81  LEU A CG    1 
ATOM   651  C  CD1   . LEU A 1 81  ? 17.125 23.594  25.639 1.00 21.14 ? 81  LEU A CD1   1 
ATOM   652  C  CD2   . LEU A 1 81  ? 17.287 21.482  24.338 1.00 20.03 ? 81  LEU A CD2   1 
ATOM   653  N  N     . ASN A 1 82  ? 20.707 20.587  27.715 1.00 21.31 ? 82  ASN A N     1 
ATOM   654  C  CA    . ASN A 1 82  ? 20.692 19.498  28.684 1.00 22.47 ? 82  ASN A CA    1 
ATOM   655  C  C     . ASN A 1 82  ? 21.105 19.969  30.085 1.00 23.19 ? 82  ASN A C     1 
ATOM   656  O  O     . ASN A 1 82  ? 20.465 19.606  31.066 1.00 22.46 ? 82  ASN A O     1 
ATOM   657  C  CB    . ASN A 1 82  ? 21.602 18.339  28.256 1.00 22.88 ? 82  ASN A CB    1 
ATOM   658  C  CG    . ASN A 1 82  ? 21.260 17.092  29.034 1.00 23.34 ? 82  ASN A CG    1 
ATOM   659  O  OD1   . ASN A 1 82  ? 20.088 16.829  29.293 1.00 23.92 ? 82  ASN A OD1   1 
ATOM   660  N  ND2   . ASN A 1 82  ? 22.265 16.349  29.444 1.00 23.47 ? 82  ASN A ND2   1 
ATOM   661  N  N     . LYS A 1 83  ? 22.160 20.793  30.163 1.00 23.85 ? 83  LYS A N     1 
ATOM   662  C  CA    . LYS A 1 83  ? 22.692 21.277  31.434 1.00 26.16 ? 83  LYS A CA    1 
ATOM   663  C  C     . LYS A 1 83  ? 21.690 22.162  32.169 1.00 26.62 ? 83  LYS A C     1 
ATOM   664  O  O     . LYS A 1 83  ? 21.724 22.280  33.404 1.00 25.88 ? 83  LYS A O     1 
ATOM   665  C  CB    . LYS A 1 83  ? 24.017 22.002  31.187 1.00 27.36 ? 83  LYS A CB    1 
ATOM   666  C  CG    . LYS A 1 83  ? 25.095 21.103  30.577 1.00 28.62 ? 83  LYS A CG    1 
ATOM   667  C  CD    . LYS A 1 83  ? 26.481 21.691  30.563 1.00 30.85 ? 83  LYS A CD    1 
ATOM   668  C  CE    . LYS A 1 83  ? 27.474 20.882  29.758 1.00 31.66 ? 83  LYS A CE    1 
ATOM   669  N  NZ    . LYS A 1 83  ? 27.628 19.517  30.271 1.00 33.34 ? 83  LYS A NZ    1 
ATOM   670  N  N     . GLU A 1 84  ? 20.791 22.782  31.402 1.00 26.71 ? 84  GLU A N     1 
ATOM   671  C  CA    . GLU A 1 84  ? 19.768 23.643  31.973 1.00 28.62 ? 84  GLU A CA    1 
ATOM   672  C  C     . GLU A 1 84  ? 18.510 22.841  32.330 1.00 28.00 ? 84  GLU A C     1 
ATOM   673  O  O     . GLU A 1 84  ? 17.469 23.426  32.603 1.00 28.78 ? 84  GLU A O     1 
ATOM   674  C  CB    . GLU A 1 84  ? 19.481 24.755  30.960 1.00 29.23 ? 84  GLU A CB    1 
ATOM   675  C  CG    . GLU A 1 84  ? 20.664 25.688  30.752 1.00 30.59 ? 84  GLU A CG    1 
ATOM   676  C  CD    . GLU A 1 84  ? 20.857 26.702  31.862 1.00 34.74 ? 84  GLU A CD    1 
ATOM   677  O  OE1   . GLU A 1 84  ? 22.014 26.907  32.262 1.00 33.77 ? 84  GLU A OE1   1 
ATOM   678  O  OE2   . GLU A 1 84  ? 19.841 27.261  32.327 1.00 37.68 ? 84  GLU A OE2   1 
ATOM   679  N  N     . ASP A 1 85  ? 18.575 21.506  32.285 1.00 27.49 ? 85  ASP A N     1 
ATOM   680  C  CA    . ASP A 1 85  ? 17.433 20.648  32.587 1.00 26.90 ? 85  ASP A CA    1 
ATOM   681  C  C     . ASP A 1 85  ? 16.237 20.929  31.660 1.00 27.04 ? 85  ASP A C     1 
ATOM   682  O  O     . ASP A 1 85  ? 15.064 20.823  32.055 1.00 26.05 ? 85  ASP A O     1 
ATOM   683  C  CB    . ASP A 1 85  ? 17.085 20.728  34.079 1.00 29.78 ? 85  ASP A CB    1 
ATOM   684  C  CG    . ASP A 1 85  ? 15.990 19.747  34.459 1.00 29.96 ? 85  ASP A CG    1 
ATOM   685  O  OD1   . ASP A 1 85  ? 16.032 18.620  33.916 1.00 29.98 ? 85  ASP A OD1   1 
ATOM   686  O  OD2   . ASP A 1 85  ? 15.073 20.136  35.218 1.00 29.03 ? 85  ASP A OD2   1 
ATOM   687  N  N     . ARG A 1 86  ? 16.516 21.202  30.375 1.00 26.56 ? 86  ARG A N     1 
ATOM   688  C  CA    . ARG A 1 86  ? 15.469 21.487  29.410 1.00 26.43 ? 86  ARG A CA    1 
ATOM   689  C  C     . ARG A 1 86  ? 15.369 20.425  28.323 1.00 23.71 ? 86  ARG A C     1 
ATOM   690  O  O     . ARG A 1 86  ? 14.748 20.693  27.302 1.00 21.67 ? 86  ARG A O     1 
ATOM   691  C  CB    . ARG A 1 86  ? 15.741 22.804  28.690 1.00 27.73 ? 86  ARG A CB    1 
ATOM   692  C  CG    . ARG A 1 86  ? 15.750 24.022  29.596 1.00 30.83 ? 86  ARG A CG    1 
ATOM   693  C  CD    . ARG A 1 86  ? 14.377 24.368  30.054 1.00 34.21 ? 86  ARG A CD    1 
ATOM   694  N  NE    . ARG A 1 86  ? 14.337 25.699  30.658 1.00 37.67 ? 86  ARG A NE    1 
ATOM   695  C  CZ    . ARG A 1 86  ? 13.227 26.277  31.107 1.00 40.27 ? 86  ARG A CZ    1 
ATOM   696  N  NH1   . ARG A 1 86  ? 12.064 25.660  30.987 1.00 41.22 ? 86  ARG A NH1   1 
ATOM   697  N  NH2   . ARG A 1 86  ? 13.285 27.468  31.683 1.00 39.33 ? 86  ARG A NH2   1 
ATOM   698  N  N     . LEU A 1 87  ? 16.017 19.267  28.516 1.00 22.42 ? 87  LEU A N     1 
ATOM   699  C  CA    . LEU A 1 87  ? 16.057 18.231  27.499 1.00 21.44 ? 87  LEU A CA    1 
ATOM   700  C  C     . LEU A 1 87  ? 15.860 16.844  28.123 1.00 21.84 ? 87  LEU A C     1 
ATOM   701  O  O     . LEU A 1 87  ? 16.468 16.498  29.143 1.00 24.26 ? 87  LEU A O     1 
ATOM   702  C  CB    . LEU A 1 87  ? 17.400 18.310  26.760 1.00 21.42 ? 87  LEU A CB    1 
ATOM   703  C  CG    . LEU A 1 87  ? 17.635 17.194  25.738 1.00 21.70 ? 87  LEU A CG    1 
ATOM   704  C  CD1   . LEU A 1 87  ? 16.747 17.407  24.538 1.00 21.68 ? 87  LEU A CD1   1 
ATOM   705  C  CD2   . LEU A 1 87  ? 19.096 17.125  25.298 1.00 21.91 ? 87  LEU A CD2   1 
ATOM   706  N  N     . ARG A 1 88  ? 15.013 16.055  27.481 1.00 20.42 ? 88  ARG A N     1 
ATOM   707  C  CA    . ARG A 1 88  ? 14.934 14.629  27.720 1.00 20.94 ? 88  ARG A CA    1 
ATOM   708  C  C     . ARG A 1 88  ? 15.155 13.906  26.393 1.00 20.43 ? 88  ARG A C     1 
ATOM   709  O  O     . ARG A 1 88  ? 14.572 14.291  25.386 1.00 21.50 ? 88  ARG A O     1 
ATOM   710  C  CB    . ARG A 1 88  ? 13.587 14.309  28.358 1.00 21.84 ? 88  ARG A CB    1 
ATOM   711  C  CG    . ARG A 1 88  ? 13.357 14.897  29.745 1.00 23.24 ? 88  ARG A CG    1 
ATOM   712  C  CD    . ARG A 1 88  ? 14.311 14.380  30.804 1.00 25.06 ? 88  ARG A CD    1 
ATOM   713  N  NE    . ARG A 1 88  ? 14.043 14.936  32.111 1.00 25.10 ? 88  ARG A NE    1 
ATOM   714  C  CZ    . ARG A 1 88  ? 14.633 16.009  32.633 1.00 26.09 ? 88  ARG A CZ    1 
ATOM   715  N  NH1   . ARG A 1 88  ? 15.518 16.717  31.963 1.00 25.02 ? 88  ARG A NH1   1 
ATOM   716  N  NH2   . ARG A 1 88  ? 14.403 16.327  33.893 1.00 28.70 ? 88  ARG A NH2   1 
ATOM   717  N  N     . VAL A 1 89  ? 16.032 12.908  26.367 1.00 20.31 ? 89  VAL A N     1 
ATOM   718  C  CA    . VAL A 1 89  ? 16.435 12.272  25.117 1.00 20.30 ? 89  VAL A CA    1 
ATOM   719  C  C     . VAL A 1 89  ? 16.220 10.766  25.238 1.00 19.60 ? 89  VAL A C     1 
ATOM   720  O  O     . VAL A 1 89  ? 16.328 10.196  26.322 1.00 20.62 ? 89  VAL A O     1 
ATOM   721  C  CB    . VAL A 1 89  ? 17.884 12.629  24.709 1.00 21.66 ? 89  VAL A CB    1 
ATOM   722  C  CG1   . VAL A 1 89  ? 18.895 12.210  25.735 1.00 23.06 ? 89  VAL A CG1   1 
ATOM   723  C  CG2   . VAL A 1 89  ? 18.265 12.044  23.340 1.00 22.86 ? 89  VAL A CG2   1 
ATOM   724  N  N     . TYR A 1 90  ? 15.797 10.163  24.134 1.00 17.50 ? 90  TYR A N     1 
ATOM   725  C  CA    . TYR A 1 90  ? 15.445 8.756   24.038 1.00 17.62 ? 90  TYR A CA    1 
ATOM   726  C  C     . TYR A 1 90  ? 15.972 8.217   22.717 1.00 17.15 ? 90  TYR A C     1 
ATOM   727  O  O     . TYR A 1 90  ? 16.002 8.979   21.736 1.00 17.83 ? 90  TYR A O     1 
ATOM   728  C  CB    . TYR A 1 90  ? 13.921 8.588   23.961 1.00 18.14 ? 90  TYR A CB    1 
ATOM   729  C  CG    . TYR A 1 90  ? 13.105 9.380   24.960 1.00 19.39 ? 90  TYR A CG    1 
ATOM   730  C  CD1   . TYR A 1 90  ? 12.923 10.747  24.804 1.00 20.44 ? 90  TYR A CD1   1 
ATOM   731  C  CD2   . TYR A 1 90  ? 12.573 8.774   26.097 1.00 20.73 ? 90  TYR A CD2   1 
ATOM   732  C  CE1   . TYR A 1 90  ? 12.156 11.470  25.704 1.00 20.83 ? 90  TYR A CE1   1 
ATOM   733  C  CE2   . TYR A 1 90  ? 11.830 9.495   27.025 1.00 21.97 ? 90  TYR A CE2   1 
ATOM   734  C  CZ    . TYR A 1 90  ? 11.639 10.851  26.832 1.00 22.39 ? 90  TYR A CZ    1 
ATOM   735  O  OH    . TYR A 1 90  ? 10.924 11.605  27.714 1.00 23.20 ? 90  TYR A OH    1 
ATOM   736  N  N     . VAL A 1 91  ? 16.269 6.917   22.686 1.00 16.75 ? 91  VAL A N     1 
ATOM   737  C  CA    . VAL A 1 91  ? 16.542 6.202   21.448 1.00 17.29 ? 91  VAL A CA    1 
ATOM   738  C  C     . VAL A 1 91  ? 15.475 5.125   21.267 1.00 18.45 ? 91  VAL A C     1 
ATOM   739  O  O     . VAL A 1 91  ? 15.215 4.334   22.176 1.00 17.89 ? 91  VAL A O     1 
ATOM   740  C  CB    . VAL A 1 91  ? 17.963 5.604   21.459 1.00 16.91 ? 91  VAL A CB    1 
ATOM   741  C  CG1   . VAL A 1 91  ? 18.294 4.844   20.180 1.00 17.36 ? 91  VAL A CG1   1 
ATOM   742  C  CG2   . VAL A 1 91  ? 18.991 6.693   21.706 1.00 17.14 ? 91  VAL A CG2   1 
ATOM   743  N  N     . HIS A 1 92  ? 14.841 5.129   20.092 1.00 18.51 ? 92  HIS A N     1 
ATOM   744  C  CA    . HIS A 1 92  ? 13.980 4.045   19.658 1.00 17.80 ? 92  HIS A CA    1 
ATOM   745  C  C     . HIS A 1 92  ? 14.698 3.378   18.492 1.00 18.89 ? 92  HIS A C     1 
ATOM   746  O  O     . HIS A 1 92  ? 15.069 4.056   17.513 1.00 18.82 ? 92  HIS A O     1 
ATOM   747  C  CB    . HIS A 1 92  ? 12.617 4.621   19.239 1.00 17.27 ? 92  HIS A CB    1 
ATOM   748  C  CG    . HIS A 1 92  ? 11.820 3.677   18.403 1.00 17.70 ? 92  HIS A CG    1 
ATOM   749  N  ND1   . HIS A 1 92  ? 11.783 3.710   17.028 1.00 17.23 ? 92  HIS A ND1   1 
ATOM   750  C  CD2   . HIS A 1 92  ? 11.048 2.650   18.776 1.00 17.34 ? 92  HIS A CD2   1 
ATOM   751  C  CE1   . HIS A 1 92  ? 11.030 2.707   16.596 1.00 17.54 ? 92  HIS A CE1   1 
ATOM   752  N  NE2   . HIS A 1 92  ? 10.580 2.058   17.640 1.00 17.63 ? 92  HIS A NE2   1 
ATOM   753  N  N     . THR A 1 93  ? 14.823 2.048   18.547 1.00 17.71 ? 93  THR A N     1 
ATOM   754  C  CA    . THR A 1 93  ? 15.604 1.341   17.555 1.00 17.57 ? 93  THR A CA    1 
ATOM   755  C  C     . THR A 1 93  ? 14.717 0.749   16.457 1.00 19.15 ? 93  THR A C     1 
ATOM   756  O  O     . THR A 1 93  ? 13.492 0.632   16.594 1.00 18.19 ? 93  THR A O     1 
ATOM   757  C  CB    . THR A 1 93  ? 16.399 0.189   18.183 1.00 17.69 ? 93  THR A CB    1 
ATOM   758  O  OG1   . THR A 1 93  ? 15.502 -0.870  18.523 1.00 17.34 ? 93  THR A OG1   1 
ATOM   759  C  CG2   . THR A 1 93  ? 17.186 0.605   19.393 1.00 17.19 ? 93  THR A CG2   1 
ATOM   760  N  N     . ARG A 1 94  ? 15.374 0.306   15.382 1.00 19.36 ? 94  ARG A N     1 
ATOM   761  C  CA    . ARG A 1 94  ? 14.675 -0.259  14.235 1.00 20.57 ? 94  ARG A CA    1 
ATOM   762  C  C     . ARG A 1 94  ? 13.952 -1.572  14.589 1.00 21.03 ? 94  ARG A C     1 
ATOM   763  O  O     . ARG A 1 94  ? 13.099 -1.996  13.835 1.00 21.36 ? 94  ARG A O     1 
ATOM   764  C  CB    . ARG A 1 94  ? 15.666 -0.497  13.083 1.00 21.46 ? 94  ARG A CB    1 
ATOM   765  C  CG    . ARG A 1 94  ? 16.681 -1.614  13.314 1.00 22.51 ? 94  ARG A CG    1 
ATOM   766  C  CD    . ARG A 1 94  ? 16.703 -2.642  12.175 1.00 24.77 ? 94  ARG A CD    1 
ATOM   767  N  NE    . ARG A 1 94  ? 16.838 -1.920  10.911 1.00 26.81 ? 94  ARG A NE    1 
ATOM   768  C  CZ    . ARG A 1 94  ? 16.264 -2.220  9.744  1.00 29.87 ? 94  ARG A CZ    1 
ATOM   769  N  NH1   . ARG A 1 94  ? 16.439 -1.394  8.723  1.00 29.48 ? 94  ARG A NH1   1 
ATOM   770  N  NH2   . ARG A 1 94  ? 15.536 -3.318  9.603  1.00 31.05 ? 94  ARG A NH2   1 
ATOM   771  N  N     . ASN A 1 95  ? 14.247 -2.191  15.748 1.00 20.58 ? 95  ASN A N     1 
ATOM   772  C  CA    . ASN A 1 95  ? 13.621 -3.432  16.161 1.00 21.48 ? 95  ASN A CA    1 
ATOM   773  C  C     . ASN A 1 95  ? 12.642 -3.214  17.321 1.00 20.89 ? 95  ASN A C     1 
ATOM   774  O  O     . ASN A 1 95  ? 12.250 -4.178  17.970 1.00 21.32 ? 95  ASN A O     1 
ATOM   775  C  CB    . ASN A 1 95  ? 14.668 -4.499  16.499 1.00 22.46 ? 95  ASN A CB    1 
ATOM   776  C  CG    . ASN A 1 95  ? 15.515 -4.868  15.302 1.00 24.89 ? 95  ASN A CG    1 
ATOM   777  O  OD1   . ASN A 1 95  ? 14.990 -4.978  14.195 1.00 25.14 ? 95  ASN A OD1   1 
ATOM   778  N  ND2   . ASN A 1 95  ? 16.815 -5.050  15.502 1.00 25.18 ? 95  ASN A ND2   1 
ATOM   779  N  N     . ASP A 1 96  ? 12.185 -1.981  17.513 1.00 20.19 ? 96  ASP A N     1 
ATOM   780  C  CA    . ASP A 1 96  ? 11.143 -1.644  18.470 1.00 20.35 ? 96  ASP A CA    1 
ATOM   781  C  C     . ASP A 1 96  ? 11.635 -1.940  19.883 1.00 19.71 ? 96  ASP A C     1 
ATOM   782  O  O     . ASP A 1 96  ? 10.938 -2.593  20.663 1.00 20.36 ? 96  ASP A O     1 
ATOM   783  C  CB    . ASP A 1 96  ? 9.798  -2.291  18.125 1.00 21.79 ? 96  ASP A CB    1 
ATOM   784  C  CG    . ASP A 1 96  ? 8.958  -1.522  17.100 1.00 24.61 ? 96  ASP A CG    1 
ATOM   785  O  OD1   . ASP A 1 96  ? 9.160  -0.306  16.960 1.00 24.22 ? 96  ASP A OD1   1 
ATOM   786  O  OD2   . ASP A 1 96  ? 8.057  -2.133  16.475 1.00 24.73 ? 96  ASP A OD2   1 
ATOM   787  N  N     . TYR A 1 97  ? 12.832 -1.421  20.198 1.00 18.98 ? 97  TYR A N     1 
ATOM   788  C  CA    . TYR A 1 97  ? 13.289 -1.264  21.572 1.00 18.64 ? 97  TYR A CA    1 
ATOM   789  C  C     . TYR A 1 97  ? 13.461 0.219   21.846 1.00 18.26 ? 97  TYR A C     1 
ATOM   790  O  O     . TYR A 1 97  ? 13.772 0.962   20.925 1.00 18.25 ? 97  TYR A O     1 
ATOM   791  C  CB    . TYR A 1 97  ? 14.633 -1.936  21.859 1.00 19.97 ? 97  TYR A CB    1 
ATOM   792  C  CG    . TYR A 1 97  ? 14.497 -3.451  21.792 1.00 20.43 ? 97  TYR A CG    1 
ATOM   793  C  CD1   . TYR A 1 97  ? 14.663 -4.132  20.594 1.00 21.17 ? 97  TYR A CD1   1 
ATOM   794  C  CD2   . TYR A 1 97  ? 14.269 -4.199  22.939 1.00 21.23 ? 97  TYR A CD2   1 
ATOM   795  C  CE1   . TYR A 1 97  ? 14.472 -5.512  20.505 1.00 22.02 ? 97  TYR A CE1   1 
ATOM   796  C  CE2   . TYR A 1 97  ? 14.135 -5.581  22.878 1.00 22.70 ? 97  TYR A CE2   1 
ATOM   797  C  CZ    . TYR A 1 97  ? 14.239 -6.245  21.653 1.00 22.92 ? 97  TYR A CZ    1 
ATOM   798  O  OH    . TYR A 1 97  ? 14.084 -7.601  21.575 1.00 24.61 ? 97  TYR A OH    1 
ATOM   799  N  N     . VAL A 1 98  ? 13.244 0.660   23.097 1.00 18.08 ? 98  VAL A N     1 
ATOM   800  C  CA    . VAL A 1 98  ? 13.517 2.033   23.459 1.00 17.94 ? 98  VAL A CA    1 
ATOM   801  C  C     . VAL A 1 98  ? 14.578 2.011   24.553 1.00 19.57 ? 98  VAL A C     1 
ATOM   802  O  O     . VAL A 1 98  ? 14.548 1.133   25.430 1.00 19.86 ? 98  VAL A O     1 
ATOM   803  C  CB    . VAL A 1 98  ? 12.244 2.760   23.914 1.00 19.02 ? 98  VAL A CB    1 
ATOM   804  C  CG1   . VAL A 1 98  ? 12.561 4.114   24.574 1.00 19.74 ? 98  VAL A CG1   1 
ATOM   805  C  CG2   . VAL A 1 98  ? 11.245 2.924   22.778 1.00 18.43 ? 98  VAL A CG2   1 
ATOM   806  N  N     . ILE A 1 99  ? 15.460 3.004   24.482 1.00 18.93 ? 99  ILE A N     1 
ATOM   807  C  CA    . ILE A 1 99  ? 16.456 3.301   25.496 1.00 20.61 ? 99  ILE A CA    1 
ATOM   808  C  C     . ILE A 1 99  ? 16.113 4.641   26.139 1.00 20.86 ? 99  ILE A C     1 
ATOM   809  O  O     . ILE A 1 99  ? 16.069 5.663   25.453 1.00 17.97 ? 99  ILE A O     1 
ATOM   810  C  CB    . ILE A 1 99  ? 17.868 3.330   24.879 1.00 20.26 ? 99  ILE A CB    1 
ATOM   811  C  CG1   . ILE A 1 99  ? 18.178 2.020   24.143 1.00 21.45 ? 99  ILE A CG1   1 
ATOM   812  C  CG2   . ILE A 1 99  ? 18.861 3.666   25.972 1.00 20.64 ? 99  ILE A CG2   1 
ATOM   813  C  CD1   . ILE A 1 99  ? 19.444 2.004   23.313 1.00 21.66 ? 99  ILE A CD1   1 
ATOM   814  N  N     . TYR A 1 100 ? 15.917 4.587   27.469 1.00 21.95 ? 100 TYR A N     1 
ATOM   815  C  CA    . TYR A 1 100 ? 15.725 5.743   28.319 1.00 22.57 ? 100 TYR A CA    1 
ATOM   816  C  C     . TYR A 1 100 ? 17.056 6.149   28.943 1.00 22.37 ? 100 TYR A C     1 
ATOM   817  O  O     . TYR A 1 100 ? 17.805 5.285   29.385 1.00 23.01 ? 100 TYR A O     1 
ATOM   818  C  CB    . TYR A 1 100 ? 14.756 5.327   29.422 1.00 24.60 ? 100 TYR A CB    1 
ATOM   819  C  CG    . TYR A 1 100 ? 13.405 4.844   28.910 1.00 25.50 ? 100 TYR A CG    1 
ATOM   820  C  CD1   . TYR A 1 100 ? 12.365 5.742   28.687 1.00 26.78 ? 100 TYR A CD1   1 
ATOM   821  C  CD2   . TYR A 1 100 ? 13.164 3.494   28.662 1.00 25.89 ? 100 TYR A CD2   1 
ATOM   822  C  CE1   . TYR A 1 100 ? 11.122 5.318   28.243 1.00 26.67 ? 100 TYR A CE1   1 
ATOM   823  C  CE2   . TYR A 1 100 ? 11.923 3.058   28.208 1.00 25.92 ? 100 TYR A CE2   1 
ATOM   824  C  CZ    . TYR A 1 100 ? 10.905 3.974   27.989 1.00 27.41 ? 100 TYR A CZ    1 
ATOM   825  O  OH    . TYR A 1 100 ? 9.673  3.551   27.562 1.00 27.06 ? 100 TYR A OH    1 
ATOM   826  N  N     . ILE A 1 101 ? 17.330 7.459   28.955 1.00 22.56 ? 101 ILE A N     1 
ATOM   827  C  CA    . ILE A 1 101 ? 18.636 8.016   29.289 1.00 22.84 ? 101 ILE A CA    1 
ATOM   828  C  C     . ILE A 1 101 ? 18.433 9.068   30.361 1.00 23.73 ? 101 ILE A C     1 
ATOM   829  O  O     . ILE A 1 101 ? 17.744 10.056  30.149 1.00 23.21 ? 101 ILE A O     1 
ATOM   830  C  CB    . ILE A 1 101 ? 19.275 8.627   28.023 1.00 22.77 ? 101 ILE A CB    1 
ATOM   831  C  CG1   . ILE A 1 101 ? 19.255 7.599   26.896 1.00 22.90 ? 101 ILE A CG1   1 
ATOM   832  C  CG2   . ILE A 1 101 ? 20.661 9.180   28.298 1.00 23.08 ? 101 ILE A CG2   1 
ATOM   833  C  CD1   . ILE A 1 101 ? 19.864 8.067   25.597 1.00 22.10 ? 101 ILE A CD1   1 
ATOM   834  N  N     . LYS A 1 102 ? 19.013 8.846   31.533 1.00 26.53 ? 102 LYS A N     1 
ATOM   835  C  CA    . LYS A 1 102 ? 18.969 9.872   32.549 1.00 27.86 ? 102 LYS A CA    1 
ATOM   836  C  C     . LYS A 1 102 ? 19.774 11.075  32.073 1.00 25.99 ? 102 LYS A C     1 
ATOM   837  O  O     . LYS A 1 102 ? 20.844 10.932  31.476 1.00 24.76 ? 102 LYS A O     1 
ATOM   838  C  CB    . LYS A 1 102 ? 19.426 9.283   33.887 1.00 32.09 ? 102 LYS A CB    1 
ATOM   839  C  CG    . LYS A 1 102 ? 18.380 8.346   34.465 1.00 36.62 ? 102 LYS A CG    1 
ATOM   840  C  CD    . LYS A 1 102 ? 18.734 7.772   35.811 1.00 45.86 ? 102 LYS A CD    1 
ATOM   841  C  CE    . LYS A 1 102 ? 17.678 6.813   36.323 1.00 49.57 ? 102 LYS A CE    1 
ATOM   842  N  NZ    . LYS A 1 102 ? 18.174 6.084   37.514 1.00 55.85 ? 102 LYS A NZ    1 
ATOM   843  N  N     . PRO A 1 103 ? 19.264 12.303  32.297 1.00 27.13 ? 103 PRO A N     1 
ATOM   844  C  CA    . PRO A 1 103 ? 19.897 13.509  31.760 1.00 27.87 ? 103 PRO A CA    1 
ATOM   845  C  C     . PRO A 1 103 ? 21.344 13.697  32.201 1.00 26.92 ? 103 PRO A C     1 
ATOM   846  O  O     . PRO A 1 103 ? 22.146 14.257  31.454 1.00 25.25 ? 103 PRO A O     1 
ATOM   847  C  CB    . PRO A 1 103 ? 19.046 14.668  32.309 1.00 29.68 ? 103 PRO A CB    1 
ATOM   848  C  CG    . PRO A 1 103 ? 17.718 14.030  32.669 1.00 30.52 ? 103 PRO A CG    1 
ATOM   849  C  CD    . PRO A 1 103 ? 18.021 12.592  33.031 1.00 29.88 ? 103 PRO A CD    1 
ATOM   850  N  N     . GLU A 1 104 ? 21.687 13.206  33.400 1.00 27.32 ? 104 GLU A N     1 
ATOM   851  C  CA    . GLU A 1 104 ? 23.056 13.366  33.878 1.00 30.10 ? 104 GLU A CA    1 
ATOM   852  C  C     . GLU A 1 104 ? 24.027 12.349  33.249 1.00 29.03 ? 104 GLU A C     1 
ATOM   853  O  O     . GLU A 1 104 ? 25.201 12.355  33.588 1.00 28.63 ? 104 GLU A O     1 
ATOM   854  C  CB    . GLU A 1 104 ? 23.094 13.258  35.408 1.00 33.32 ? 104 GLU A CB    1 
ATOM   855  C  CG    . GLU A 1 104 ? 22.640 11.912  35.927 1.00 37.02 ? 104 GLU A CG    1 
ATOM   856  C  CD    . GLU A 1 104 ? 21.168 11.749  36.299 1.00 43.11 ? 104 GLU A CD    1 
ATOM   857  O  OE1   . GLU A 1 104 ? 20.941 11.067  37.321 1.00 52.50 ? 104 GLU A OE1   1 
ATOM   858  O  OE2   . GLU A 1 104 ? 20.246 12.293  35.606 1.00 39.38 ? 104 GLU A OE2   1 
ATOM   859  N  N     . THR A 1 105 ? 23.584 11.433  32.373 1.00 28.32 ? 105 THR A N     1 
ATOM   860  C  CA    . THR A 1 105 ? 24.503 10.433  31.823 1.00 28.07 ? 105 THR A CA    1 
ATOM   861  C  C     . THR A 1 105 ? 25.696 11.063  31.080 1.00 27.81 ? 105 THR A C     1 
ATOM   862  O  O     . THR A 1 105 ? 25.527 11.925  30.236 1.00 27.62 ? 105 THR A O     1 
ATOM   863  C  CB    . THR A 1 105 ? 23.777 9.506   30.847 1.00 28.24 ? 105 THR A CB    1 
ATOM   864  O  OG1   . THR A 1 105 ? 22.649 8.919   31.488 1.00 26.73 ? 105 THR A OG1   1 
ATOM   865  C  CG2   . THR A 1 105 ? 24.687 8.431   30.293 1.00 31.13 ? 105 THR A CG2   1 
ATOM   866  N  N     . ARG A 1 106 ? 26.919 10.618  31.376 1.00 30.57 ? 106 ARG A N     1 
ATOM   867  C  CA    . ARG A 1 106 ? 28.107 10.999  30.612 1.00 30.81 ? 106 ARG A CA    1 
ATOM   868  C  C     . ARG A 1 106 ? 28.404 9.870   29.629 1.00 28.72 ? 106 ARG A C     1 
ATOM   869  O  O     . ARG A 1 106 ? 28.916 8.837   30.031 1.00 28.43 ? 106 ARG A O     1 
ATOM   870  C  CB    . ARG A 1 106 ? 29.323 11.188  31.528 1.00 35.75 ? 106 ARG A CB    1 
ATOM   871  C  CG    . ARG A 1 106 ? 30.599 11.612  30.806 1.00 39.21 ? 106 ARG A CG    1 
ATOM   872  C  CD    . ARG A 1 106 ? 31.793 11.631  31.739 1.00 46.73 ? 106 ARG A CD    1 
ATOM   873  N  NE    . ARG A 1 106 ? 33.054 11.871  31.046 1.00 51.95 ? 106 ARG A NE    1 
ATOM   874  C  CZ    . ARG A 1 106 ? 33.717 10.981  30.300 1.00 55.76 ? 106 ARG A CZ    1 
ATOM   875  N  NH1   . ARG A 1 106 ? 33.198 9.790   30.042 1.00 55.57 ? 106 ARG A NH1   1 
ATOM   876  N  NH2   . ARG A 1 106 ? 34.912 11.287  29.809 1.00 54.09 ? 106 ARG A NH2   1 
ATOM   877  N  N     . LEU A 1 107 ? 28.035 10.047  28.364 1.00 27.34 ? 107 LEU A N     1 
ATOM   878  C  CA    . LEU A 1 107 ? 28.241 9.012   27.362 1.00 28.69 ? 107 LEU A CA    1 
ATOM   879  C  C     . LEU A 1 107 ? 29.733 8.936   27.086 1.00 25.14 ? 107 LEU A C     1 
ATOM   880  O  O     . LEU A 1 107 ? 30.362 9.984   26.969 1.00 26.73 ? 107 LEU A O     1 
ATOM   881  C  CB    . LEU A 1 107 ? 27.563 9.398   26.046 1.00 29.18 ? 107 LEU A CB    1 
ATOM   882  C  CG    . LEU A 1 107 ? 26.407 8.572   25.476 1.00 35.81 ? 107 LEU A CG    1 
ATOM   883  C  CD1   . LEU A 1 107 ? 26.531 8.547   23.961 1.00 35.79 ? 107 LEU A CD1   1 
ATOM   884  C  CD2   . LEU A 1 107 ? 26.294 7.165   26.022 1.00 36.89 ? 107 LEU A CD2   1 
ATOM   885  N  N     . PRO A 1 108 ? 30.304 7.736   26.888 1.00 22.80 ? 108 PRO A N     1 
ATOM   886  C  CA    . PRO A 1 108 ? 31.680 7.611   26.423 1.00 23.50 ? 108 PRO A CA    1 
ATOM   887  C  C     . PRO A 1 108 ? 31.902 8.442   25.174 1.00 21.35 ? 108 PRO A C     1 
ATOM   888  O  O     . PRO A 1 108 ? 31.132 8.362   24.228 1.00 20.49 ? 108 PRO A O     1 
ATOM   889  C  CB    . PRO A 1 108 ? 31.798 6.116   26.105 1.00 24.51 ? 108 PRO A CB    1 
ATOM   890  C  CG    . PRO A 1 108 ? 30.842 5.493   27.049 1.00 24.78 ? 108 PRO A CG    1 
ATOM   891  C  CD    . PRO A 1 108 ? 29.671 6.440   27.090 1.00 23.40 ? 108 PRO A CD    1 
ATOM   892  N  N     . ARG A 1 109 ? 32.937 9.265   25.208 1.00 21.69 ? 109 ARG A N     1 
ATOM   893  C  CA    . ARG A 1 109 ? 33.320 10.059  24.061 1.00 22.92 ? 109 ARG A CA    1 
ATOM   894  C  C     . ARG A 1 109 ? 33.927 9.156   22.999 1.00 22.54 ? 109 ARG A C     1 
ATOM   895  O  O     . ARG A 1 109 ? 33.789 9.417   21.813 1.00 23.42 ? 109 ARG A O     1 
ATOM   896  C  CB    . ARG A 1 109 ? 34.314 11.143  24.489 1.00 25.41 ? 109 ARG A CB    1 
ATOM   897  C  CG    . ARG A 1 109 ? 33.685 12.337  25.187 1.00 28.41 ? 109 ARG A CG    1 
ATOM   898  C  CD    . ARG A 1 109 ? 33.607 12.295  26.702 1.00 34.76 ? 109 ARG A CD    1 
ATOM   899  N  NE    . ARG A 1 109 ? 32.258 12.203  27.155 1.00 40.97 ? 109 ARG A NE    1 
ATOM   900  C  CZ    . ARG A 1 109 ? 31.375 13.194  27.188 1.00 38.05 ? 109 ARG A CZ    1 
ATOM   901  N  NH1   . ARG A 1 109 ? 30.198 12.943  26.681 1.00 34.44 ? 109 ARG A NH1   1 
ATOM   902  N  NH2   . ARG A 1 109 ? 31.676 14.424  27.569 1.00 38.45 ? 109 ARG A NH2   1 
ATOM   903  N  N     . ASN A 1 110 ? 34.629 8.109   23.429 1.00 22.28 ? 110 ASN A N     1 
ATOM   904  C  CA    . ASN A 1 110 ? 35.255 7.225   22.471 1.00 22.92 ? 110 ASN A CA    1 
ATOM   905  C  C     . ASN A 1 110 ? 34.193 6.275   21.909 1.00 21.91 ? 110 ASN A C     1 
ATOM   906  O  O     . ASN A 1 110 ? 33.516 5.583   22.659 1.00 21.53 ? 110 ASN A O     1 
ATOM   907  C  CB    . ASN A 1 110 ? 36.432 6.485   23.095 1.00 23.74 ? 110 ASN A CB    1 
ATOM   908  C  CG    . ASN A 1 110 ? 37.092 5.593   22.074 1.00 24.87 ? 110 ASN A CG    1 
ATOM   909  O  OD1   . ASN A 1 110 ? 36.633 4.492   21.828 1.00 24.90 ? 110 ASN A OD1   1 
ATOM   910  N  ND2   . ASN A 1 110 ? 38.162 6.063   21.463 1.00 25.80 ? 110 ASN A ND2   1 
ATOM   911  N  N     . TYR A 1 111 ? 34.099 6.196   20.579 1.00 20.33 ? 111 TYR A N     1 
ATOM   912  C  CA    . TYR A 1 111 ? 33.122 5.344   19.927 1.00 19.39 ? 111 TYR A CA    1 
ATOM   913  C  C     . TYR A 1 111 ? 33.243 3.891   20.363 1.00 20.31 ? 111 TYR A C     1 
ATOM   914  O  O     . TYR A 1 111 ? 32.249 3.208   20.563 1.00 20.45 ? 111 TYR A O     1 
ATOM   915  C  CB    . TYR A 1 111 ? 33.373 5.413   18.418 1.00 19.91 ? 111 TYR A CB    1 
ATOM   916  C  CG    . TYR A 1 111 ? 32.522 4.434   17.620 1.00 19.94 ? 111 TYR A CG    1 
ATOM   917  C  CD1   . TYR A 1 111 ? 31.144 4.599   17.518 1.00 20.49 ? 111 TYR A CD1   1 
ATOM   918  C  CD2   . TYR A 1 111 ? 33.076 3.325   17.011 1.00 20.80 ? 111 TYR A CD2   1 
ATOM   919  C  CE1   . TYR A 1 111 ? 30.359 3.754   16.752 1.00 19.80 ? 111 TYR A CE1   1 
ATOM   920  C  CE2   . TYR A 1 111 ? 32.309 2.469   16.236 1.00 21.44 ? 111 TYR A CE2   1 
ATOM   921  C  CZ    . TYR A 1 111 ? 30.946 2.694   16.111 1.00 21.25 ? 111 TYR A CZ    1 
ATOM   922  O  OH    . TYR A 1 111 ? 30.185 1.852   15.393 1.00 24.22 ? 111 TYR A OH    1 
ATOM   923  N  N     . ASN A 1 112 ? 34.463 3.374   20.449 1.00 20.65 ? 112 ASN A N     1 
ATOM   924  C  CA    . ASN A 1 112 ? 34.607 1.971   20.758 1.00 22.53 ? 112 ASN A CA    1 
ATOM   925  C  C     . ASN A 1 112 ? 34.156 1.702   22.193 1.00 23.17 ? 112 ASN A C     1 
ATOM   926  O  O     . ASN A 1 112 ? 33.643 0.621   22.484 1.00 22.21 ? 112 ASN A O     1 
ATOM   927  C  CB    . ASN A 1 112 ? 36.031 1.491   20.488 1.00 24.50 ? 112 ASN A CB    1 
ATOM   928  C  CG    . ASN A 1 112 ? 36.371 1.559   19.020 1.00 25.12 ? 112 ASN A CG    1 
ATOM   929  O  OD1   . ASN A 1 112 ? 35.628 1.042   18.191 1.00 26.03 ? 112 ASN A OD1   1 
ATOM   930  N  ND2   . ASN A 1 112 ? 37.433 2.264   18.675 1.00 25.05 ? 112 ASN A ND2   1 
ATOM   931  N  N     . ARG A 1 113 ? 34.355 2.670   23.099 1.00 23.88 ? 113 ARG A N     1 
ATOM   932  C  CA    . ARG A 1 113 ? 33.850 2.520   24.457 1.00 25.48 ? 113 ARG A CA    1 
ATOM   933  C  C     . ARG A 1 113 ? 32.328 2.614   24.471 1.00 23.04 ? 113 ARG A C     1 
ATOM   934  O  O     . ARG A 1 113 ? 31.683 1.923   25.230 1.00 22.05 ? 113 ARG A O     1 
ATOM   935  C  CB    . ARG A 1 113 ? 34.437 3.554   25.427 1.00 30.12 ? 113 ARG A CB    1 
ATOM   936  C  CG    . ARG A 1 113 ? 35.601 3.014   26.238 1.00 40.74 ? 113 ARG A CG    1 
ATOM   937  C  CD    . ARG A 1 113 ? 35.879 3.899   27.444 1.00 50.97 ? 113 ARG A CD    1 
ATOM   938  N  NE    . ARG A 1 113 ? 37.228 3.714   27.966 1.00 58.87 ? 113 ARG A NE    1 
ATOM   939  C  CZ    . ARG A 1 113 ? 38.233 4.580   27.817 1.00 62.29 ? 113 ARG A CZ    1 
ATOM   940  N  NH1   . ARG A 1 113 ? 38.112 5.617   27.000 1.00 57.48 ? 113 ARG A NH1   1 
ATOM   941  N  NH2   . ARG A 1 113 ? 39.376 4.371   28.455 1.00 64.04 ? 113 ARG A NH2   1 
ATOM   942  N  N     . PHE A 1 114 ? 31.759 3.462   23.611 1.00 22.24 ? 114 PHE A N     1 
ATOM   943  C  CA    . PHE A 1 114 ? 30.322 3.535   23.442 1.00 21.89 ? 114 PHE A CA    1 
ATOM   944  C  C     . PHE A 1 114 ? 29.765 2.177   23.004 1.00 21.29 ? 114 PHE A C     1 
ATOM   945  O  O     . PHE A 1 114 ? 28.736 1.752   23.511 1.00 21.25 ? 114 PHE A O     1 
ATOM   946  C  CB    . PHE A 1 114 ? 29.976 4.655   22.460 1.00 20.89 ? 114 PHE A CB    1 
ATOM   947  C  CG    . PHE A 1 114 ? 28.540 4.670   22.017 1.00 20.18 ? 114 PHE A CG    1 
ATOM   948  C  CD1   . PHE A 1 114 ? 27.532 5.078   22.877 1.00 20.79 ? 114 PHE A CD1   1 
ATOM   949  C  CD2   . PHE A 1 114 ? 28.198 4.234   20.744 1.00 20.13 ? 114 PHE A CD2   1 
ATOM   950  C  CE1   . PHE A 1 114 ? 26.212 5.056   22.451 1.00 21.66 ? 114 PHE A CE1   1 
ATOM   951  C  CE2   . PHE A 1 114 ? 26.880 4.169   20.351 1.00 19.71 ? 114 PHE A CE2   1 
ATOM   952  C  CZ    . PHE A 1 114 ? 25.895 4.608   21.188 1.00 20.17 ? 114 PHE A CZ    1 
ATOM   953  N  N     . ILE A 1 115 ? 30.417 1.510   22.040 1.00 20.88 ? 115 ILE A N     1 
ATOM   954  C  CA    . ILE A 1 115 ? 29.929 0.236   21.556 1.00 21.40 ? 115 ILE A CA    1 
ATOM   955  C  C     . ILE A 1 115 ? 29.928 -0.779  22.703 1.00 22.39 ? 115 ILE A C     1 
ATOM   956  O  O     . ILE A 1 115 ? 28.981 -1.551  22.845 1.00 22.92 ? 115 ILE A O     1 
ATOM   957  C  CB    . ILE A 1 115 ? 30.751 -0.261  20.358 1.00 22.40 ? 115 ILE A CB    1 
ATOM   958  C  CG1   . ILE A 1 115 ? 30.497 0.576   19.104 1.00 22.54 ? 115 ILE A CG1   1 
ATOM   959  C  CG2   . ILE A 1 115 ? 30.491 -1.729  20.094 1.00 23.54 ? 115 ILE A CG2   1 
ATOM   960  C  CD1   . ILE A 1 115 ? 29.045 0.616   18.643 1.00 22.34 ? 115 ILE A CD1   1 
ATOM   961  N  N     . GLY A 1 116 ? 30.988 -0.767  23.509 1.00 22.61 ? 116 GLY A N     1 
ATOM   962  C  CA    . GLY A 1 116 ? 31.091 -1.637  24.669 1.00 24.64 ? 116 GLY A CA    1 
ATOM   963  C  C     . GLY A 1 116 ? 29.943 -1.423  25.647 1.00 24.13 ? 116 GLY A C     1 
ATOM   964  O  O     . GLY A 1 116 ? 29.417 -2.379  26.199 1.00 25.59 ? 116 GLY A O     1 
ATOM   965  N  N     . LEU A 1 117 ? 29.561 -0.159  25.832 1.00 22.64 ? 117 LEU A N     1 
ATOM   966  C  CA    . LEU A 1 117 ? 28.449 0.208   26.686 1.00 22.72 ? 117 LEU A CA    1 
ATOM   967  C  C     . LEU A 1 117 ? 27.140 -0.311  26.110 1.00 22.64 ? 117 LEU A C     1 
ATOM   968  O  O     . LEU A 1 117 ? 26.299 -0.790  26.858 1.00 23.10 ? 117 LEU A O     1 
ATOM   969  C  CB    . LEU A 1 117 ? 28.432 1.731   26.856 1.00 22.51 ? 117 LEU A CB    1 
ATOM   970  C  CG    . LEU A 1 117 ? 27.282 2.316   27.677 1.00 23.22 ? 117 LEU A CG    1 
ATOM   971  C  CD1   . LEU A 1 117 ? 27.276 1.808   29.108 1.00 25.44 ? 117 LEU A CD1   1 
ATOM   972  C  CD2   . LEU A 1 117 ? 27.342 3.830   27.646 1.00 23.62 ? 117 LEU A CD2   1 
ATOM   973  N  N     . MET A 1 118 ? 26.979 -0.217  24.778 1.00 20.95 ? 118 MET A N     1 
ATOM   974  C  CA    . MET A 1 118 ? 25.775 -0.671  24.116 1.00 20.55 ? 118 MET A CA    1 
ATOM   975  C  C     . MET A 1 118 ? 25.662 -2.189  24.227 1.00 20.63 ? 118 MET A C     1 
ATOM   976  O  O     . MET A 1 118 ? 24.565 -2.683  24.400 1.00 21.12 ? 118 MET A O     1 
ATOM   977  C  CB    . MET A 1 118 ? 25.747 -0.229  22.644 1.00 20.01 ? 118 MET A CB    1 
ATOM   978  C  CG    . MET A 1 118 ? 25.531 1.261   22.453 1.00 19.15 ? 118 MET A CG    1 
ATOM   979  S  SD    . MET A 1 118 ? 23.997 1.953   23.144 1.00 21.71 ? 118 MET A SD    1 
ATOM   980  C  CE    . MET A 1 118 ? 24.580 2.414   24.774 1.00 21.68 ? 118 MET A CE    1 
ATOM   981  N  N     . GLU A 1 119 ? 26.779 -2.899  24.072 1.00 21.58 ? 119 GLU A N     1 
ATOM   982  C  CA    . GLU A 1 119 ? 26.830 -4.337  24.270 1.00 24.36 ? 119 GLU A CA    1 
ATOM   983  C  C     . GLU A 1 119 ? 26.380 -4.678  25.694 1.00 25.26 ? 119 GLU A C     1 
ATOM   984  O  O     . GLU A 1 119 ? 25.560 -5.574  25.867 1.00 24.79 ? 119 GLU A O     1 
ATOM   985  C  CB    . GLU A 1 119 ? 28.235 -4.855  23.918 1.00 26.24 ? 119 GLU A CB    1 
ATOM   986  C  CG    . GLU A 1 119 ? 28.418 -4.783  22.405 1.00 28.08 ? 119 GLU A CG    1 
ATOM   987  C  CD    . GLU A 1 119 ? 29.758 -5.148  21.798 1.00 30.18 ? 119 GLU A CD    1 
ATOM   988  O  OE1   . GLU A 1 119 ? 29.835 -5.154  20.491 1.00 30.76 ? 119 GLU A OE1   1 
ATOM   989  O  OE2   . GLU A 1 119 ? 30.706 -5.421  22.585 1.00 30.16 ? 119 GLU A OE2   1 
ATOM   990  N  N     . ASN A 1 120 ? 26.887 -3.944  26.697 1.00 24.74 ? 120 ASN A N     1 
ATOM   991  C  CA    . ASN A 1 120 ? 26.485 -4.203  28.077 1.00 26.03 ? 120 ASN A CA    1 
ATOM   992  C  C     . ASN A 1 120 ? 24.991 -3.912  28.271 1.00 24.52 ? 120 ASN A C     1 
ATOM   993  O  O     . ASN A 1 120 ? 24.281 -4.678  28.900 1.00 23.64 ? 120 ASN A O     1 
ATOM   994  C  CB    . ASN A 1 120 ? 27.315 -3.380  29.057 1.00 28.73 ? 120 ASN A CB    1 
ATOM   995  C  CG    . ASN A 1 120 ? 28.707 -3.946  29.236 1.00 35.29 ? 120 ASN A CG    1 
ATOM   996  O  OD1   . ASN A 1 120 ? 28.928 -5.129  28.982 1.00 39.35 ? 120 ASN A OD1   1 
ATOM   997  N  ND2   . ASN A 1 120 ? 29.636 -3.132  29.720 1.00 35.99 ? 120 ASN A ND2   1 
ATOM   998  N  N     . LEU A 1 121 ? 24.506 -2.799  27.720 1.00 23.57 ? 121 LEU A N     1 
ATOM   999  C  CA    . LEU A 1 121 ? 23.106 -2.427  27.849 1.00 23.00 ? 121 LEU A CA    1 
ATOM   1000 C  C     . LEU A 1 121 ? 22.190 -3.464  27.217 1.00 23.31 ? 121 LEU A C     1 
ATOM   1001 O  O     . LEU A 1 121 ? 21.186 -3.836  27.796 1.00 22.68 ? 121 LEU A O     1 
ATOM   1002 C  CB    . LEU A 1 121 ? 22.902 -1.053  27.218 1.00 22.94 ? 121 LEU A CB    1 
ATOM   1003 C  CG    . LEU A 1 121 ? 21.445 -0.593  27.148 1.00 22.85 ? 121 LEU A CG    1 
ATOM   1004 C  CD1   . LEU A 1 121 ? 20.845 -0.459  28.559 1.00 24.02 ? 121 LEU A CD1   1 
ATOM   1005 C  CD2   . LEU A 1 121 ? 21.339 0.707   26.417 1.00 21.91 ? 121 LEU A CD2   1 
ATOM   1006 N  N     . PHE A 1 122 ? 22.492 -3.885  25.987 1.00 24.31 ? 122 PHE A N     1 
ATOM   1007 C  CA    . PHE A 1 122 ? 21.685 -4.896  25.326 1.00 24.06 ? 122 PHE A CA    1 
ATOM   1008 C  C     . PHE A 1 122 ? 21.671 -6.214  26.099 1.00 26.30 ? 122 PHE A C     1 
ATOM   1009 O  O     . PHE A 1 122 ? 20.660 -6.926  26.097 1.00 25.44 ? 122 PHE A O     1 
ATOM   1010 C  CB    . PHE A 1 122 ? 22.122 -5.100  23.879 1.00 25.13 ? 122 PHE A CB    1 
ATOM   1011 C  CG    . PHE A 1 122 ? 21.519 -4.114  22.909 1.00 24.70 ? 122 PHE A CG    1 
ATOM   1012 C  CD1   . PHE A 1 122 ? 21.835 -2.767  22.971 1.00 25.89 ? 122 PHE A CD1   1 
ATOM   1013 C  CD2   . PHE A 1 122 ? 20.586 -4.532  21.969 1.00 25.73 ? 122 PHE A CD2   1 
ATOM   1014 C  CE1   . PHE A 1 122 ? 21.292 -1.874  22.059 1.00 25.94 ? 122 PHE A CE1   1 
ATOM   1015 C  CE2   . PHE A 1 122 ? 20.030 -3.640  21.069 1.00 24.70 ? 122 PHE A CE2   1 
ATOM   1016 C  CZ    . PHE A 1 122 ? 20.380 -2.309  21.115 1.00 25.50 ? 122 PHE A CZ    1 
ATOM   1017 N  N     . GLU A 1 123 ? 22.776 -6.537  26.776 1.00 26.33 ? 123 GLU A N     1 
ATOM   1018 C  CA    . GLU A 1 123 ? 22.880 -7.789  27.495 1.00 28.55 ? 123 GLU A CA    1 
ATOM   1019 C  C     . GLU A 1 123 ? 22.103 -7.714  28.809 1.00 29.15 ? 123 GLU A C     1 
ATOM   1020 O  O     . GLU A 1 123 ? 21.359 -8.638  29.114 1.00 28.86 ? 123 GLU A O     1 
ATOM   1021 C  CB    . GLU A 1 123 ? 24.351 -8.135  27.738 1.00 29.37 ? 123 GLU A CB    1 
ATOM   1022 C  CG    . GLU A 1 123 ? 24.569 -9.386  28.571 1.00 33.84 ? 123 GLU A CG    1 
ATOM   1023 C  CD    . GLU A 1 123 ? 24.082 -10.688 27.953 1.00 35.93 ? 123 GLU A CD    1 
ATOM   1024 O  OE1   . GLU A 1 123 ? 23.717 -10.689 26.755 1.00 36.99 ? 123 GLU A OE1   1 
ATOM   1025 O  OE2   . GLU A 1 123 ? 24.050 -11.706 28.678 1.00 40.79 ? 123 GLU A OE2   1 
ATOM   1026 N  N     . LYS A 1 124 ? 22.267 -6.627  29.572 1.00 28.29 ? 124 LYS A N     1 
ATOM   1027 C  CA    . LYS A 1 124 ? 21.779 -6.569  30.942 1.00 30.44 ? 124 LYS A CA    1 
ATOM   1028 C  C     . LYS A 1 124 ? 20.462 -5.812  31.039 1.00 30.34 ? 124 LYS A C     1 
ATOM   1029 O  O     . LYS A 1 124 ? 19.815 -5.880  32.085 1.00 29.62 ? 124 LYS A O     1 
ATOM   1030 C  CB    . LYS A 1 124 ? 22.813 -5.878  31.838 1.00 34.78 ? 124 LYS A CB    1 
ATOM   1031 C  CG    . LYS A 1 124 ? 24.103 -6.655  31.994 1.00 38.66 ? 124 LYS A CG    1 
ATOM   1032 C  CD    . LYS A 1 124 ? 25.324 -5.813  32.143 1.00 45.25 ? 124 LYS A CD    1 
ATOM   1033 C  CE    . LYS A 1 124 ? 26.508 -6.461  31.449 1.00 51.93 ? 124 LYS A CE    1 
ATOM   1034 N  NZ    . LYS A 1 124 ? 27.788 -5.819  31.815 1.00 55.63 ? 124 LYS A NZ    1 
ATOM   1035 N  N     . GLY A 1 125 ? 20.068 -5.063  29.992 1.00 27.54 ? 125 GLY A N     1 
ATOM   1036 C  CA    . GLY A 1 125 ? 18.803 -4.352  30.062 1.00 28.06 ? 125 GLY A CA    1 
ATOM   1037 C  C     . GLY A 1 125 ? 18.882 -2.970  30.717 1.00 28.37 ? 125 GLY A C     1 
ATOM   1038 O  O     . GLY A 1 125 ? 17.988 -2.147  30.492 1.00 26.74 ? 125 GLY A O     1 
ATOM   1039 N  N     . ALA A 1 126 ? 19.903 -2.740  31.552 1.00 29.06 ? 126 ALA A N     1 
ATOM   1040 C  CA    . ALA A 1 126 ? 20.073 -1.475  32.256 1.00 29.73 ? 126 ALA A CA    1 
ATOM   1041 C  C     . ALA A 1 126 ? 21.497 -1.368  32.770 1.00 31.59 ? 126 ALA A C     1 
ATOM   1042 O  O     . ALA A 1 126 ? 22.012 -2.335  33.353 1.00 33.03 ? 126 ALA A O     1 
ATOM   1043 C  CB    . ALA A 1 126 ? 19.108 -1.362  33.404 1.00 30.81 ? 126 ALA A CB    1 
ATOM   1044 N  N     . VAL A 1 127 ? 22.101 -0.183  32.598 1.00 31.26 ? 127 VAL A N     1 
ATOM   1045 C  CA    . VAL A 1 127 ? 23.475 0.013   33.043 1.00 34.08 ? 127 VAL A CA    1 
ATOM   1046 C  C     . VAL A 1 127 ? 23.661 1.416   33.620 1.00 35.81 ? 127 VAL A C     1 
ATOM   1047 O  O     . VAL A 1 127 ? 22.954 2.345   33.225 1.00 31.32 ? 127 VAL A O     1 
ATOM   1048 C  CB    . VAL A 1 127 ? 24.463 -0.240  31.899 1.00 32.88 ? 127 VAL A CB    1 
ATOM   1049 C  CG1   . VAL A 1 127 ? 24.407 -1.688  31.435 1.00 34.31 ? 127 VAL A CG1   1 
ATOM   1050 C  CG2   . VAL A 1 127 ? 24.197 0.711   30.752 1.00 31.81 ? 127 VAL A CG2   1 
ATOM   1051 N  N     . PRO A 1 128 ? 24.540 1.601   34.641 1.00 41.65 ? 128 PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 128 ? 25.057 0.506   35.468 1.00 44.57 ? 128 PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 128 ? 23.989 -0.057  36.398 1.00 47.87 ? 128 PRO A C     1 
ATOM   1054 O  O     . PRO A 1 128 ? 22.853 0.410   36.410 1.00 49.16 ? 128 PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 128 ? 26.226 1.114   36.269 1.00 48.25 ? 128 PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 128 ? 25.997 2.621   36.228 1.00 47.85 ? 128 PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 128 ? 25.088 2.905   35.043 1.00 43.77 ? 128 PRO A CD    1 
ATOM   1058 N  N     . GLU A 1 129 ? 24.377 -1.064  37.189 1.00 58.00 ? 129 GLU A N     1 
ATOM   1059 C  CA    . GLU A 1 129 ? 23.439 -1.981  37.819 1.00 64.83 ? 129 GLU A CA    1 
ATOM   1060 C  C     . GLU A 1 129 ? 22.475 -1.224  38.732 1.00 63.28 ? 129 GLU A C     1 
ATOM   1061 O  O     . GLU A 1 129 ? 21.263 -1.403  38.647 1.00 67.71 ? 129 GLU A O     1 
ATOM   1062 C  CB    . GLU A 1 129 ? 24.199 -3.069  38.583 1.00 72.52 ? 129 GLU A CB    1 
ATOM   1063 C  CG    . GLU A 1 129 ? 25.373 -3.680  37.819 1.00 81.51 ? 129 GLU A CG    1 
ATOM   1064 C  CD    . GLU A 1 129 ? 25.250 -3.739  36.301 1.00 90.94 ? 129 GLU A CD    1 
ATOM   1065 O  OE1   . GLU A 1 129 ? 25.635 -2.744  35.639 1.00 97.55 ? 129 GLU A OE1   1 
ATOM   1066 O  OE2   . GLU A 1 129 ? 24.758 -4.771  35.778 1.00 93.57 ? 129 GLU A OE2   1 
ATOM   1067 N  N     . ASP A 1 130 ? 23.034 -0.370  39.588 1.00 63.46 ? 130 ASP A N     1 
ATOM   1068 C  CA    . ASP A 1 130 ? 22.286 0.425   40.552 1.00 67.84 ? 130 ASP A CA    1 
ATOM   1069 C  C     . ASP A 1 130 ? 21.600 1.608   39.872 1.00 63.54 ? 130 ASP A C     1 
ATOM   1070 O  O     . ASP A 1 130 ? 20.374 1.740   39.929 1.00 58.26 ? 130 ASP A O     1 
ATOM   1071 C  CB    . ASP A 1 130 ? 23.257 0.993   41.579 1.00 74.94 ? 130 ASP A CB    1 
ATOM   1072 C  CG    . ASP A 1 130 ? 24.459 1.561   40.848 1.00 82.31 ? 130 ASP A CG    1 
ATOM   1073 O  OD1   . ASP A 1 130 ? 25.323 0.757   40.431 1.00 88.42 ? 130 ASP A OD1   1 
ATOM   1074 O  OD2   . ASP A 1 130 ? 24.433 2.768   40.554 1.00 83.90 ? 130 ASP A OD2   1 
ATOM   1075 N  N     . LEU A 1 131 ? 22.428 2.447   39.217 1.00 63.57 ? 131 LEU A N     1 
ATOM   1076 C  CA    . LEU A 1 131 ? 22.036 3.759   38.717 1.00 55.23 ? 131 LEU A CA    1 
ATOM   1077 C  C     . LEU A 1 131 ? 20.967 3.618   37.655 1.00 47.83 ? 131 LEU A C     1 
ATOM   1078 O  O     . LEU A 1 131 ? 20.011 4.380   37.652 1.00 49.46 ? 131 LEU A O     1 
ATOM   1079 C  CB    . LEU A 1 131 ? 23.239 4.482   38.101 1.00 56.22 ? 131 LEU A CB    1 
ATOM   1080 C  CG    . LEU A 1 131 ? 24.127 5.295   39.047 1.00 59.19 ? 131 LEU A CG    1 
ATOM   1081 C  CD1   . LEU A 1 131 ? 25.279 5.929   38.282 1.00 57.85 ? 131 LEU A CD1   1 
ATOM   1082 C  CD2   . LEU A 1 131 ? 23.333 6.366   39.781 1.00 59.12 ? 131 LEU A CD2   1 
ATOM   1083 N  N     . GLU A 1 132 ? 21.213 2.711   36.710 1.00 43.29 ? 132 GLU A N     1 
ATOM   1084 C  CA    . GLU A 1 132 ? 20.366 2.549   35.550 1.00 39.86 ? 132 GLU A CA    1 
ATOM   1085 C  C     . GLU A 1 132 ? 20.244 3.873   34.805 1.00 36.88 ? 132 GLU A C     1 
ATOM   1086 O  O     . GLU A 1 132 ? 19.129 4.300   34.481 1.00 38.80 ? 132 GLU A O     1 
ATOM   1087 C  CB    . GLU A 1 132 ? 18.991 2.021   35.943 1.00 43.27 ? 132 GLU A CB    1 
ATOM   1088 C  CG    . GLU A 1 132 ? 19.066 0.698   36.669 1.00 47.93 ? 132 GLU A CG    1 
ATOM   1089 C  CD    . GLU A 1 132 ? 17.734 -0.013  36.731 1.00 50.79 ? 132 GLU A CD    1 
ATOM   1090 O  OE1   . GLU A 1 132 ? 17.716 -1.201  37.130 1.00 57.82 ? 132 GLU A OE1   1 
ATOM   1091 O  OE2   . GLU A 1 132 ? 16.725 0.620   36.365 1.00 52.00 ? 132 GLU A OE2   1 
ATOM   1092 N  N     . LEU A 1 133 ? 21.399 4.477   34.493 1.00 31.77 ? 133 LEU A N     1 
ATOM   1093 C  CA    . LEU A 1 133 ? 21.446 5.699   33.706 1.00 29.12 ? 133 LEU A CA    1 
ATOM   1094 C  C     . LEU A 1 133 ? 20.864 5.445   32.315 1.00 27.91 ? 133 LEU A C     1 
ATOM   1095 O  O     . LEU A 1 133 ? 20.282 6.359   31.721 1.00 27.34 ? 133 LEU A O     1 
ATOM   1096 C  CB    . LEU A 1 133 ? 22.905 6.168   33.611 1.00 29.65 ? 133 LEU A CB    1 
ATOM   1097 C  CG    . LEU A 1 133 ? 23.545 6.584   34.930 1.00 32.56 ? 133 LEU A CG    1 
ATOM   1098 C  CD1   . LEU A 1 133 ? 25.028 6.903   34.747 1.00 32.65 ? 133 LEU A CD1   1 
ATOM   1099 C  CD2   . LEU A 1 133 ? 22.777 7.756   35.533 1.00 34.49 ? 133 LEU A CD2   1 
ATOM   1100 N  N     . LEU A 1 134 ? 21.107 4.228   31.797 1.00 25.20 ? 134 LEU A N     1 
ATOM   1101 C  CA    . LEU A 1 134 ? 20.490 3.719   30.580 1.00 25.68 ? 134 LEU A CA    1 
ATOM   1102 C  C     . LEU A 1 134 ? 19.636 2.497   30.920 1.00 25.23 ? 134 LEU A C     1 
ATOM   1103 O  O     . LEU A 1 134 ? 20.057 1.617   31.673 1.00 25.08 ? 134 LEU A O     1 
ATOM   1104 C  CB    . LEU A 1 134 ? 21.573 3.342   29.558 1.00 25.64 ? 134 LEU A CB    1 
ATOM   1105 C  CG    . LEU A 1 134 ? 22.563 4.436   29.170 1.00 29.44 ? 134 LEU A CG    1 
ATOM   1106 C  CD1   . LEU A 1 134 ? 23.561 3.923   28.153 1.00 32.26 ? 134 LEU A CD1   1 
ATOM   1107 C  CD2   . LEU A 1 134 ? 21.851 5.651   28.611 1.00 29.37 ? 134 LEU A CD2   1 
ATOM   1108 N  N     . ARG A 1 135 ? 18.439 2.463   30.355 1.00 25.60 ? 135 ARG A N     1 
ATOM   1109 C  CA    . ARG A 1 135 ? 17.472 1.397   30.566 1.00 28.70 ? 135 ARG A CA    1 
ATOM   1110 C  C     . ARG A 1 135 ? 16.810 1.100   29.222 1.00 26.20 ? 135 ARG A C     1 
ATOM   1111 O  O     . ARG A 1 135 ? 16.429 2.026   28.513 1.00 22.59 ? 135 ARG A O     1 
ATOM   1112 C  CB    . ARG A 1 135 ? 16.457 1.899   31.601 1.00 34.50 ? 135 ARG A CB    1 
ATOM   1113 C  CG    . ARG A 1 135 ? 15.342 0.947   31.987 1.00 43.85 ? 135 ARG A CG    1 
ATOM   1114 C  CD    . ARG A 1 135 ? 14.514 1.502   33.165 1.00 47.40 ? 135 ARG A CD    1 
ATOM   1115 N  NE    . ARG A 1 135 ? 13.665 2.672   32.844 1.00 53.27 ? 135 ARG A NE    1 
ATOM   1116 C  CZ    . ARG A 1 135 ? 12.477 2.639   32.218 1.00 53.51 ? 135 ARG A CZ    1 
ATOM   1117 N  NH1   . ARG A 1 135 ? 11.984 1.489   31.795 1.00 52.84 ? 135 ARG A NH1   1 
ATOM   1118 N  NH2   . ARG A 1 135 ? 11.776 3.753   32.022 1.00 54.26 ? 135 ARG A NH2   1 
ATOM   1119 N  N     . MET A 1 136 ? 16.605 -0.183  28.907 1.00 25.22 ? 136 MET A N     1 
ATOM   1120 C  CA    . MET A 1 136 ? 16.080 -0.564  27.607 1.00 26.25 ? 136 MET A CA    1 
ATOM   1121 C  C     . MET A 1 136 ? 14.919 -1.544  27.789 1.00 25.28 ? 136 MET A C     1 
ATOM   1122 O  O     . MET A 1 136 ? 14.877 -2.346  28.743 1.00 23.47 ? 136 MET A O     1 
ATOM   1123 C  CB    . MET A 1 136 ? 17.199 -1.202  26.770 1.00 29.00 ? 136 MET A CB    1 
ATOM   1124 C  CG    . MET A 1 136 ? 16.783 -1.696  25.385 1.00 34.73 ? 136 MET A CG    1 
ATOM   1125 S  SD    . MET A 1 136 ? 18.238 -2.372  24.482 1.00 37.72 ? 136 MET A SD    1 
ATOM   1126 C  CE    . MET A 1 136 ? 18.415 -3.902  25.369 1.00 42.94 ? 136 MET A CE    1 
ATOM   1127 N  N     . GLU A 1 137 ? 13.938 -1.435  26.897 1.00 23.10 ? 137 GLU A N     1 
ATOM   1128 C  CA    . GLU A 1 137 ? 12.850 -2.396  26.886 1.00 22.71 ? 137 GLU A CA    1 
ATOM   1129 C  C     . GLU A 1 137 ? 12.127 -2.378  25.547 1.00 20.74 ? 137 GLU A C     1 
ATOM   1130 O  O     . GLU A 1 137 ? 12.299 -1.482  24.712 1.00 19.50 ? 137 GLU A O     1 
ATOM   1131 C  CB    . GLU A 1 137 ? 11.863 -2.169  28.022 1.00 26.84 ? 137 GLU A CB    1 
ATOM   1132 C  CG    . GLU A 1 137 ? 11.094 -0.881  27.945 1.00 28.54 ? 137 GLU A CG    1 
ATOM   1133 C  CD    . GLU A 1 137 ? 10.344 -0.595  29.237 1.00 32.16 ? 137 GLU A CD    1 
ATOM   1134 O  OE1   . GLU A 1 137 ? 10.971 -0.696  30.292 1.00 39.41 ? 137 GLU A OE1   1 
ATOM   1135 O  OE2   . GLU A 1 137 ? 9.129  -0.371  29.186 1.00 31.72 ? 137 GLU A OE2   1 
ATOM   1136 N  N     . LYS A 1 138 ? 11.394 -3.461  25.330 1.00 20.51 ? 138 LYS A N     1 
ATOM   1137 C  CA    . LYS A 1 138 ? 10.664 -3.676  24.100 1.00 21.38 ? 138 LYS A CA    1 
ATOM   1138 C  C     . LYS A 1 138 ? 9.557  -2.631  24.054 1.00 21.97 ? 138 LYS A C     1 
ATOM   1139 O  O     . LYS A 1 138 ? 8.788  -2.492  25.011 1.00 21.80 ? 138 LYS A O     1 
ATOM   1140 C  CB    . LYS A 1 138 ? 10.181 -5.124  24.058 1.00 22.85 ? 138 LYS A CB    1 
ATOM   1141 C  CG    . LYS A 1 138 ? 9.580  -5.557  22.735 1.00 25.16 ? 138 LYS A CG    1 
ATOM   1142 C  CD    . LYS A 1 138 ? 10.618 -5.866  21.671 1.00 25.46 ? 138 LYS A CD    1 
ATOM   1143 C  CE    . LYS A 1 138 ? 9.937  -5.818  20.319 1.00 27.58 ? 138 LYS A CE    1 
ATOM   1144 N  NZ    . LYS A 1 138 ? 10.849 -6.175  19.253 1.00 27.31 ? 138 LYS A NZ    1 
ATOM   1145 N  N     . LYS A 1 139 ? 9.506  -1.870  22.955 1.00 20.74 ? 139 LYS A N     1 
ATOM   1146 C  CA    . LYS A 1 139 ? 8.608  -0.739  22.923 1.00 23.50 ? 139 LYS A CA    1 
ATOM   1147 C  C     . LYS A 1 139 ? 8.557  -0.099  21.539 1.00 23.04 ? 139 LYS A C     1 
ATOM   1148 O  O     . LYS A 1 139 ? 9.597  0.222   20.950 1.00 21.28 ? 139 LYS A O     1 
ATOM   1149 C  CB    . LYS A 1 139 ? 9.079  0.341   23.893 1.00 26.43 ? 139 LYS A CB    1 
ATOM   1150 C  CG    . LYS A 1 139 ? 8.171  1.560   23.879 1.00 31.38 ? 139 LYS A CG    1 
ATOM   1151 C  CD    . LYS A 1 139 ? 7.866  2.058   25.237 1.00 36.43 ? 139 LYS A CD    1 
ATOM   1152 C  CE    . LYS A 1 139 ? 7.080  1.069   26.062 1.00 40.83 ? 139 LYS A CE    1 
ATOM   1153 N  NZ    . LYS A 1 139 ? 7.671  0.975   27.415 1.00 39.00 ? 139 LYS A NZ    1 
ATOM   1154 N  N     . THR A 1 140 ? 7.342  0.188   21.081 1.00 23.15 ? 140 THR A N     1 
ATOM   1155 C  CA    . THR A 1 140 ? 7.142  0.893   19.811 1.00 22.42 ? 140 THR A CA    1 
ATOM   1156 C  C     . THR A 1 140 ? 7.265  2.407   19.990 1.00 22.20 ? 140 THR A C     1 
ATOM   1157 O  O     . THR A 1 140 ? 7.129  2.940   21.112 1.00 21.86 ? 140 THR A O     1 
ATOM   1158 C  CB    . THR A 1 140 ? 5.769  0.574   19.204 1.00 25.31 ? 140 THR A CB    1 
ATOM   1159 O  OG1   . THR A 1 140 ? 4.729  1.078   20.050 1.00 28.42 ? 140 THR A OG1   1 
ATOM   1160 C  CG2   . THR A 1 140 ? 5.568  -0.903  18.974 1.00 25.27 ? 140 THR A CG2   1 
ATOM   1161 N  N     . LEU A 1 141 ? 7.419  3.130   18.860 1.00 20.09 ? 141 LEU A N     1 
ATOM   1162 C  CA    . LEU A 1 141 ? 7.541  4.583   18.937 1.00 21.46 ? 141 LEU A CA    1 
ATOM   1163 C  C     . LEU A 1 141 ? 6.236  5.233   19.425 1.00 22.27 ? 141 LEU A C     1 
ATOM   1164 O  O     . LEU A 1 141 ? 6.264  6.182   20.209 1.00 22.50 ? 141 LEU A O     1 
ATOM   1165 C  CB    . LEU A 1 141 ? 7.963  5.120   17.565 1.00 22.62 ? 141 LEU A CB    1 
ATOM   1166 C  CG    . LEU A 1 141 ? 8.140  6.631   17.461 1.00 21.84 ? 141 LEU A CG    1 
ATOM   1167 C  CD1   . LEU A 1 141 ? 9.166  7.163   18.459 1.00 21.37 ? 141 LEU A CD1   1 
ATOM   1168 C  CD2   . LEU A 1 141 ? 8.537  6.976   16.041 1.00 21.96 ? 141 LEU A CD2   1 
ATOM   1169 N  N     . ASN A 1 142 ? 5.082  4.686   19.023 1.00 25.03 ? 142 ASN A N     1 
ATOM   1170 C  CA    . ASN A 1 142 ? 3.819  5.218   19.495 1.00 27.07 ? 142 ASN A CA    1 
ATOM   1171 C  C     . ASN A 1 142 ? 3.640  5.019   20.989 1.00 29.19 ? 142 ASN A C     1 
ATOM   1172 O  O     . ASN A 1 142 ? 3.102  5.914   21.633 1.00 29.25 ? 142 ASN A O     1 
ATOM   1173 C  CB    . ASN A 1 142 ? 2.610  4.602   18.809 1.00 29.67 ? 142 ASN A CB    1 
ATOM   1174 C  CG    . ASN A 1 142 ? 2.118  5.538   17.727 1.00 33.53 ? 142 ASN A CG    1 
ATOM   1175 O  OD1   . ASN A 1 142 ? 1.902  6.734   17.971 1.00 35.93 ? 142 ASN A OD1   1 
ATOM   1176 N  ND2   . ASN A 1 142 ? 1.944  4.995   16.540 1.00 36.53 ? 142 ASN A ND2   1 
ATOM   1177 N  N     . GLU A 1 143 ? 4.061  3.853   21.498 1.00 28.59 ? 143 GLU A N     1 
ATOM   1178 C  CA    . GLU A 1 143 ? 3.934  3.538   22.917 1.00 31.10 ? 143 GLU A CA    1 
ATOM   1179 C  C     . GLU A 1 143 ? 4.778  4.530   23.704 1.00 29.87 ? 143 GLU A C     1 
ATOM   1180 O  O     . GLU A 1 143 ? 4.316  5.059   24.713 1.00 32.57 ? 143 GLU A O     1 
ATOM   1181 C  CB    . GLU A 1 143 ? 4.301  2.083   23.196 1.00 34.35 ? 143 GLU A CB    1 
ATOM   1182 C  CG    . GLU A 1 143 ? 3.248  1.071   22.775 1.00 42.55 ? 143 GLU A CG    1 
ATOM   1183 C  CD    . GLU A 1 143 ? 3.703  -0.376  22.592 1.00 49.26 ? 143 GLU A CD    1 
ATOM   1184 O  OE1   . GLU A 1 143 ? 2.832  -1.227  22.277 1.00 52.05 ? 143 GLU A OE1   1 
ATOM   1185 O  OE2   . GLU A 1 143 ? 4.934  -0.659  22.704 1.00 44.52 ? 143 GLU A OE2   1 
ATOM   1186 N  N     . LEU A 1 144 ? 5.971  4.861   23.188 1.00 27.81 ? 144 LEU A N     1 
ATOM   1187 C  CA    . LEU A 1 144 ? 6.848  5.820   23.827 1.00 26.12 ? 144 LEU A CA    1 
ATOM   1188 C  C     . LEU A 1 144 ? 6.210  7.210   23.861 1.00 26.71 ? 144 LEU A C     1 
ATOM   1189 O  O     . LEU A 1 144 ? 6.252  7.904   24.886 1.00 23.55 ? 144 LEU A O     1 
ATOM   1190 C  CB    . LEU A 1 144 ? 8.218  5.855   23.130 1.00 23.88 ? 144 LEU A CB    1 
ATOM   1191 C  CG    . LEU A 1 144 ? 9.093  7.039   23.539 1.00 24.62 ? 144 LEU A CG    1 
ATOM   1192 C  CD1   . LEU A 1 144 ? 9.351  7.027   25.033 1.00 25.94 ? 144 LEU A CD1   1 
ATOM   1193 C  CD2   . LEU A 1 144 ? 10.389 7.065   22.744 1.00 24.15 ? 144 LEU A CD2   1 
ATOM   1194 N  N     . ILE A 1 145 ? 5.640  7.618   22.726 1.00 25.65 ? 145 ILE A N     1 
ATOM   1195 C  CA    . ILE A 1 145 ? 4.989  8.912   22.635 1.00 25.86 ? 145 ILE A CA    1 
ATOM   1196 C  C     . ILE A 1 145 ? 3.812  9.007   23.616 1.00 26.35 ? 145 ILE A C     1 
ATOM   1197 O  O     . ILE A 1 145 ? 3.590  10.080  24.150 1.00 26.90 ? 145 ILE A O     1 
ATOM   1198 C  CB    . ILE A 1 145 ? 4.538  9.194   21.192 1.00 26.23 ? 145 ILE A CB    1 
ATOM   1199 C  CG1   . ILE A 1 145 ? 5.757  9.424   20.301 1.00 26.31 ? 145 ILE A CG1   1 
ATOM   1200 C  CG2   . ILE A 1 145 ? 3.581  10.387  21.184 1.00 28.00 ? 145 ILE A CG2   1 
ATOM   1201 C  CD1   . ILE A 1 145 ? 5.490  9.369   18.804 1.00 27.97 ? 145 ILE A CD1   1 
ATOM   1202 N  N     . GLU A 1 146 ? 3.056  7.922   23.774 1.00 26.59 ? 146 GLU A N     1 
ATOM   1203 C  CA    . GLU A 1 146 ? 1.966  7.788   24.724 1.00 30.59 ? 146 GLU A CA    1 
ATOM   1204 C  C     . GLU A 1 146 ? 2.497  8.040   26.139 1.00 30.88 ? 146 GLU A C     1 
ATOM   1205 O  O     . GLU A 1 146 ? 1.871  8.750   26.923 1.00 29.37 ? 146 GLU A O     1 
ATOM   1206 C  CB    . GLU A 1 146 ? 1.335  6.391   24.605 1.00 33.76 ? 146 GLU A CB    1 
ATOM   1207 C  CG    . GLU A 1 146 ? 0.165  6.117   25.551 1.00 39.88 ? 146 GLU A CG    1 
ATOM   1208 C  CD    . GLU A 1 146 ? -0.434 4.714   25.702 1.00 43.21 ? 146 GLU A CD    1 
ATOM   1209 O  OE1   . GLU A 1 146 ? 0.194  3.689   25.317 1.00 47.09 ? 146 GLU A OE1   1 
ATOM   1210 O  OE2   . GLU A 1 146 ? -1.573 4.638   26.211 1.00 48.32 ? 146 GLU A OE2   1 
ATOM   1211 N  N     . GLU A 1 147 ? 3.658  7.458   26.448 1.00 28.71 ? 147 GLU A N     1 
ATOM   1212 C  CA    . GLU A 1 147 ? 4.281  7.643   27.753 1.00 30.55 ? 147 GLU A CA    1 
ATOM   1213 C  C     . GLU A 1 147 ? 4.652  9.099   27.965 1.00 28.21 ? 147 GLU A C     1 
ATOM   1214 O  O     . GLU A 1 147 ? 4.424  9.613   29.051 1.00 27.18 ? 147 GLU A O     1 
ATOM   1215 C  CB    . GLU A 1 147 ? 5.553  6.815   27.915 1.00 30.20 ? 147 GLU A CB    1 
ATOM   1216 C  CG    . GLU A 1 147 ? 5.262  5.339   28.162 1.00 33.90 ? 147 GLU A CG    1 
ATOM   1217 C  CD    . GLU A 1 147 ? 6.508  4.459   28.159 1.00 35.20 ? 147 GLU A CD    1 
ATOM   1218 O  OE1   . GLU A 1 147 ? 7.612  5.030   28.099 1.00 34.20 ? 147 GLU A OE1   1 
ATOM   1219 O  OE2   . GLU A 1 147 ? 6.365  3.208   28.143 1.00 35.13 ? 147 GLU A OE2   1 
ATOM   1220 N  N     . ILE A 1 148 ? 5.198  9.760   26.940 1.00 25.85 ? 148 ILE A N     1 
ATOM   1221 C  CA    . ILE A 1 148 ? 5.599  11.149  27.106 1.00 26.27 ? 148 ILE A CA    1 
ATOM   1222 C  C     . ILE A 1 148 ? 4.356  12.021  27.294 1.00 25.19 ? 148 ILE A C     1 
ATOM   1223 O  O     . ILE A 1 148 ? 4.379  13.004  28.027 1.00 25.36 ? 148 ILE A O     1 
ATOM   1224 C  CB    . ILE A 1 148 ? 6.471  11.597  25.917 1.00 26.67 ? 148 ILE A CB    1 
ATOM   1225 C  CG1   . ILE A 1 148 ? 7.830  10.899  25.945 1.00 28.24 ? 148 ILE A CG1   1 
ATOM   1226 C  CG2   . ILE A 1 148 ? 6.641  13.103  25.877 1.00 27.29 ? 148 ILE A CG2   1 
ATOM   1227 C  CD1   . ILE A 1 148 ? 8.515  10.849  24.602 1.00 26.37 ? 148 ILE A CD1   1 
ATOM   1228 N  N     . ASN A 1 149 ? 3.282  11.693  26.562 1.00 22.77 ? 149 ASN A N     1 
ATOM   1229 C  CA    . ASN A 1 149 ? 2.051  12.454  26.620 1.00 22.05 ? 149 ASN A CA    1 
ATOM   1230 C  C     . ASN A 1 149 ? 2.340  13.915  26.296 1.00 22.09 ? 149 ASN A C     1 
ATOM   1231 O  O     . ASN A 1 149 ? 2.013  14.797  27.067 1.00 21.87 ? 149 ASN A O     1 
ATOM   1232 C  CB    . ASN A 1 149 ? 1.368  12.327  27.984 1.00 22.52 ? 149 ASN A CB    1 
ATOM   1233 C  CG    . ASN A 1 149 ? -0.042 12.864  27.985 1.00 23.05 ? 149 ASN A CG    1 
ATOM   1234 O  OD1   . ASN A 1 149 ? -0.668 13.036  26.931 1.00 21.75 ? 149 ASN A OD1   1 
ATOM   1235 N  ND2   . ASN A 1 149 ? -0.569 13.082  29.180 1.00 23.67 ? 149 ASN A ND2   1 
ATOM   1236 N  N     . PRO A 1 150 ? 2.898  14.212  25.105 1.00 21.56 ? 150 PRO A N     1 
ATOM   1237 C  CA    . PRO A 1 150 ? 3.240  15.585  24.734 1.00 22.09 ? 150 PRO A CA    1 
ATOM   1238 C  C     . PRO A 1 150 ? 2.017  16.377  24.263 1.00 23.07 ? 150 PRO A C     1 
ATOM   1239 O  O     . PRO A 1 150 ? 0.969  15.832  23.938 1.00 24.16 ? 150 PRO A O     1 
ATOM   1240 C  CB    . PRO A 1 150 ? 4.230  15.335  23.571 1.00 20.91 ? 150 PRO A CB    1 
ATOM   1241 C  CG    . PRO A 1 150 ? 3.648  14.119  22.884 1.00 20.95 ? 150 PRO A CG    1 
ATOM   1242 C  CD    . PRO A 1 150 ? 3.254  13.239  24.054 1.00 21.16 ? 150 PRO A CD    1 
ATOM   1243 N  N     . ASP A 1 151 ? 2.174  17.688  24.147 1.00 24.74 ? 151 ASP A N     1 
ATOM   1244 C  CA    . ASP A 1 151 ? 1.119  18.509  23.597 1.00 24.78 ? 151 ASP A CA    1 
ATOM   1245 C  C     . ASP A 1 151 ? 1.302  18.731  22.100 1.00 24.34 ? 151 ASP A C     1 
ATOM   1246 O  O     . ASP A 1 151 ? 0.414  19.332  21.494 1.00 25.94 ? 151 ASP A O     1 
ATOM   1247 C  CB    . ASP A 1 151 ? 0.959  19.830  24.337 1.00 26.39 ? 151 ASP A CB    1 
ATOM   1248 C  CG    . ASP A 1 151 ? 2.216  20.655  24.545 1.00 26.11 ? 151 ASP A CG    1 
ATOM   1249 O  OD1   . ASP A 1 151 ? 3.316  20.078  24.508 1.00 25.30 ? 151 ASP A OD1   1 
ATOM   1250 O  OD2   . ASP A 1 151 ? 2.059  21.879  24.749 1.00 27.95 ? 151 ASP A OD2   1 
ATOM   1251 N  N     . VAL A 1 152 ? 2.409  18.235  21.528 1.00 24.85 ? 152 VAL A N     1 
ATOM   1252 C  CA    . VAL A 1 152 ? 2.694  18.322  20.095 1.00 22.78 ? 152 VAL A CA    1 
ATOM   1253 C  C     . VAL A 1 152 ? 3.823  17.331  19.771 1.00 21.56 ? 152 VAL A C     1 
ATOM   1254 O  O     . VAL A 1 152 ? 4.732  17.141  20.585 1.00 20.23 ? 152 VAL A O     1 
ATOM   1255 C  CB    . VAL A 1 152 ? 3.049  19.769  19.664 1.00 23.27 ? 152 VAL A CB    1 
ATOM   1256 C  CG1   . VAL A 1 152 ? 4.388  20.254  20.192 1.00 23.43 ? 152 VAL A CG1   1 
ATOM   1257 C  CG2   . VAL A 1 152 ? 3.051  19.967  18.152 1.00 23.84 ? 152 VAL A CG2   1 
ATOM   1258 N  N     . VAL A 1 153 ? 3.761  16.729  18.568 1.00 20.39 ? 153 VAL A N     1 
ATOM   1259 C  CA    . VAL A 1 153 ? 4.796  15.865  18.039 1.00 19.39 ? 153 VAL A CA    1 
ATOM   1260 C  C     . VAL A 1 153 ? 5.257  16.457  16.709 1.00 19.10 ? 153 VAL A C     1 
ATOM   1261 O  O     . VAL A 1 153 ? 4.463  16.647  15.801 1.00 18.15 ? 153 VAL A O     1 
ATOM   1262 C  CB    . VAL A 1 153 ? 4.309  14.411  17.835 1.00 20.34 ? 153 VAL A CB    1 
ATOM   1263 C  CG1   . VAL A 1 153 ? 5.379  13.550  17.189 1.00 20.26 ? 153 VAL A CG1   1 
ATOM   1264 C  CG2   . VAL A 1 153 ? 3.820  13.752  19.121 1.00 20.94 ? 153 VAL A CG2   1 
ATOM   1265 N  N     . PHE A 1 154 ? 6.562  16.723  16.597 1.00 18.54 ? 154 PHE A N     1 
ATOM   1266 C  CA    . PHE A 1 154 ? 7.171  17.129  15.355 1.00 18.92 ? 154 PHE A CA    1 
ATOM   1267 C  C     . PHE A 1 154 ? 8.039  15.983  14.866 1.00 19.69 ? 154 PHE A C     1 
ATOM   1268 O  O     . PHE A 1 154 ? 8.767  15.383  15.648 1.00 18.99 ? 154 PHE A O     1 
ATOM   1269 C  CB    . PHE A 1 154 ? 8.037  18.374  15.567 1.00 18.73 ? 154 PHE A CB    1 
ATOM   1270 C  CG    . PHE A 1 154 ? 7.272  19.619  15.908 1.00 19.22 ? 154 PHE A CG    1 
ATOM   1271 C  CD1   . PHE A 1 154 ? 6.517  20.264  14.942 1.00 19.49 ? 154 PHE A CD1   1 
ATOM   1272 C  CD2   . PHE A 1 154 ? 7.240  20.110  17.212 1.00 19.46 ? 154 PHE A CD2   1 
ATOM   1273 C  CE1   . PHE A 1 154 ? 5.783  21.402  15.252 1.00 20.81 ? 154 PHE A CE1   1 
ATOM   1274 C  CE2   . PHE A 1 154 ? 6.516  21.259  17.515 1.00 20.04 ? 154 PHE A CE2   1 
ATOM   1275 C  CZ    . PHE A 1 154 ? 5.795  21.909  16.540 1.00 21.12 ? 154 PHE A CZ    1 
ATOM   1276 N  N     . ILE A 1 155 ? 8.022  15.788  13.555 1.00 20.05 ? 155 ILE A N     1 
ATOM   1277 C  CA    . ILE A 1 155 ? 8.840  14.814  12.876 1.00 19.77 ? 155 ILE A CA    1 
ATOM   1278 C  C     . ILE A 1 155 ? 9.737  15.592  11.924 1.00 19.39 ? 155 ILE A C     1 
ATOM   1279 O  O     . ILE A 1 155 ? 9.249  16.211  10.979 1.00 18.79 ? 155 ILE A O     1 
ATOM   1280 C  CB    . ILE A 1 155 ? 7.949  13.798  12.136 1.00 21.54 ? 155 ILE A CB    1 
ATOM   1281 C  CG1   . ILE A 1 155 ? 6.920  13.171  13.077 1.00 23.51 ? 155 ILE A CG1   1 
ATOM   1282 C  CG2   . ILE A 1 155 ? 8.789  12.724  11.456 1.00 21.91 ? 155 ILE A CG2   1 
ATOM   1283 C  CD1   . ILE A 1 155 ? 5.807  12.465  12.373 1.00 26.32 ? 155 ILE A CD1   1 
ATOM   1284 N  N     . MET A 1 156 ? 11.045 15.548  12.181 1.00 17.90 ? 156 MET A N     1 
ATOM   1285 C  CA    . MET A 1 156 ? 11.988 16.256  11.347 1.00 17.96 ? 156 MET A CA    1 
ATOM   1286 C  C     . MET A 1 156 ? 12.130 15.443  10.083 1.00 18.47 ? 156 MET A C     1 
ATOM   1287 O  O     . MET A 1 156 ? 12.423 14.245  10.138 1.00 18.38 ? 156 MET A O     1 
ATOM   1288 C  CB    . MET A 1 156 ? 13.345 16.434  12.033 1.00 17.89 ? 156 MET A CB    1 
ATOM   1289 C  CG    . MET A 1 156 ? 13.234 17.023  13.428 1.00 17.46 ? 156 MET A CG    1 
ATOM   1290 S  SD    . MET A 1 156 ? 12.219 18.506  13.503 1.00 19.21 ? 156 MET A SD    1 
ATOM   1291 C  CE    . MET A 1 156 ? 13.092 19.531  12.312 1.00 21.42 ? 156 MET A CE    1 
ATOM   1292 N  N     . HIS A 1 157 ? 11.824 16.104  8.960  1.00 19.15 ? 157 HIS A N     1 
ATOM   1293 C  CA    . HIS A 1 157 ? 11.665 15.420  7.696  1.00 21.20 ? 157 HIS A CA    1 
ATOM   1294 C  C     . HIS A 1 157 ? 12.012 16.418  6.603  1.00 21.15 ? 157 HIS A C     1 
ATOM   1295 O  O     . HIS A 1 157 ? 11.469 17.527  6.570  1.00 20.01 ? 157 HIS A O     1 
ATOM   1296 C  CB    . HIS A 1 157 ? 10.232 14.894  7.558  1.00 23.19 ? 157 HIS A CB    1 
ATOM   1297 C  CG    . HIS A 1 157 ? 10.072 13.887  6.482  1.00 27.77 ? 157 HIS A CG    1 
ATOM   1298 N  ND1   . HIS A 1 157 ? 10.244 14.151  5.133  1.00 28.09 ? 157 HIS A ND1   1 
ATOM   1299 C  CD2   . HIS A 1 157 ? 9.721  12.582  6.564  1.00 30.09 ? 157 HIS A CD2   1 
ATOM   1300 C  CE1   . HIS A 1 157 ? 10.042 13.028  4.439  1.00 30.45 ? 157 HIS A CE1   1 
ATOM   1301 N  NE2   . HIS A 1 157 ? 9.699  12.074  5.275  1.00 29.23 ? 157 HIS A NE2   1 
ATOM   1302 N  N     . GLU A 1 158 ? 12.913 16.002  5.725  1.00 21.99 ? 158 GLU A N     1 
ATOM   1303 C  CA    . GLU A 1 158 ? 13.362 16.852  4.645  1.00 23.13 ? 158 GLU A CA    1 
ATOM   1304 C  C     . GLU A 1 158 ? 12.192 17.382  3.815  1.00 23.68 ? 158 GLU A C     1 
ATOM   1305 O  O     . GLU A 1 158 ? 12.350 18.426  3.157  1.00 23.39 ? 158 GLU A O     1 
ATOM   1306 C  CB    . GLU A 1 158 ? 14.347 16.108  3.744  1.00 26.09 ? 158 GLU A CB    1 
ATOM   1307 C  CG    . GLU A 1 158 ? 14.638 16.923  2.506  1.00 31.28 ? 158 GLU A CG    1 
ATOM   1308 C  CD    . GLU A 1 158 ? 15.688 16.400  1.546  1.00 34.41 ? 158 GLU A CD    1 
ATOM   1309 O  OE1   . GLU A 1 158 ? 15.857 17.063  0.505  1.00 30.13 ? 158 GLU A OE1   1 
ATOM   1310 O  OE2   . GLU A 1 158 ? 16.309 15.318  1.861  1.00 38.08 ? 158 GLU A OE2   1 
ATOM   1311 N  N     . GLU A 1 159 ? 11.090 16.611  3.703  1.00 22.67 ? 159 GLU A N     1 
ATOM   1312 C  CA    A GLU A 1 159 ? 9.928  16.917  2.889  0.50 23.98 ? 159 GLU A CA    1 
ATOM   1313 C  CA    B GLU A 1 159 ? 10.020 17.116  2.849  0.50 24.34 ? 159 GLU A CA    1 
ATOM   1314 C  C     . GLU A 1 159 ? 8.858  17.652  3.691  1.00 23.98 ? 159 GLU A C     1 
ATOM   1315 O  O     . GLU A 1 159 ? 7.746  17.824  3.194  1.00 24.27 ? 159 GLU A O     1 
ATOM   1316 C  CB    A GLU A 1 159 ? 9.265  15.620  2.386  0.50 24.05 ? 159 GLU A CB    1 
ATOM   1317 C  CB    B GLU A 1 159 ? 9.620  16.096  1.777  0.50 25.56 ? 159 GLU A CB    1 
ATOM   1318 C  CG    A GLU A 1 159 ? 10.185 14.710  1.587  0.50 24.45 ? 159 GLU A CG    1 
ATOM   1319 C  CG    B GLU A 1 159 ? 10.803 15.486  1.024  0.50 25.72 ? 159 GLU A CG    1 
ATOM   1320 C  CD    A GLU A 1 159 ? 9.488  13.597  0.808  0.50 26.05 ? 159 GLU A CD    1 
ATOM   1321 C  CD    B GLU A 1 159 ? 11.841 16.366  0.318  0.50 27.00 ? 159 GLU A CD    1 
ATOM   1322 O  OE1   A GLU A 1 159 ? 10.168 12.958  -0.023 0.50 26.69 ? 159 GLU A OE1   1 
ATOM   1323 O  OE1   B GLU A 1 159 ? 11.621 17.599  0.044  0.50 27.09 ? 159 GLU A OE1   1 
ATOM   1324 O  OE2   A GLU A 1 159 ? 8.260  13.402  0.983  0.50 25.50 ? 159 GLU A OE2   1 
ATOM   1325 O  OE2   B GLU A 1 159 ? 12.905 15.795  0.010  0.50 27.82 ? 159 GLU A OE2   1 
ATOM   1326 N  N     . GLY A 1 160 ? 9.135  18.022  4.947  1.00 22.92 ? 160 GLY A N     1 
ATOM   1327 C  CA    . GLY A 1 160 ? 8.089  18.618  5.778  1.00 23.69 ? 160 GLY A CA    1 
ATOM   1328 C  C     . GLY A 1 160 ? 7.934  20.116  5.503  1.00 24.44 ? 160 GLY A C     1 
ATOM   1329 O  O     . GLY A 1 160 ? 8.479  20.636  4.530  1.00 22.91 ? 160 GLY A O     1 
ATOM   1330 N  N     . GLU A 1 161 ? 7.138  20.801  6.330  1.00 24.40 ? 161 GLU A N     1 
ATOM   1331 C  CA    . GLU A 1 161 ? 6.955  22.248  6.221  1.00 26.22 ? 161 GLU A CA    1 
ATOM   1332 C  C     . GLU A 1 161 ? 8.289  22.962  6.462  1.00 24.92 ? 161 GLU A C     1 
ATOM   1333 O  O     . GLU A 1 161 ? 8.889  22.800  7.534  1.00 23.94 ? 161 GLU A O     1 
ATOM   1334 C  CB    . GLU A 1 161 ? 5.935  22.668  7.290  1.00 29.10 ? 161 GLU A CB    1 
ATOM   1335 C  CG    . GLU A 1 161 ? 5.597  24.139  7.283  1.00 30.78 ? 161 GLU A CG    1 
ATOM   1336 C  CD    . GLU A 1 161 ? 4.797  24.580  6.076  1.00 32.68 ? 161 GLU A CD    1 
ATOM   1337 O  OE1   . GLU A 1 161 ? 4.080  23.746  5.513  1.00 34.32 ? 161 GLU A OE1   1 
ATOM   1338 O  OE2   . GLU A 1 161 ? 4.916  25.748  5.694  1.00 36.36 ? 161 GLU A OE2   1 
ATOM   1339 N  N     . LEU A 1 162 ? 8.773  23.743  5.486  1.00 24.90 ? 162 LEU A N     1 
ATOM   1340 C  CA    . LEU A 1 162 ? 10.081 24.369  5.622  1.00 25.59 ? 162 LEU A CA    1 
ATOM   1341 C  C     . LEU A 1 162 ? 10.039 25.471  6.679  1.00 25.76 ? 162 LEU A C     1 
ATOM   1342 O  O     . LEU A 1 162 ? 9.228  26.388  6.620  1.00 26.07 ? 162 LEU A O     1 
ATOM   1343 C  CB    . LEU A 1 162 ? 10.585 24.958  4.303  1.00 27.08 ? 162 LEU A CB    1 
ATOM   1344 C  CG    . LEU A 1 162 ? 11.985 25.581  4.364  1.00 28.03 ? 162 LEU A CG    1 
ATOM   1345 C  CD1   . LEU A 1 162 ? 13.043 24.558  4.725  1.00 28.27 ? 162 LEU A CD1   1 
ATOM   1346 C  CD2   . LEU A 1 162 ? 12.348 26.243  3.045  1.00 30.22 ? 162 LEU A CD2   1 
ATOM   1347 N  N     . MET A 1 163 ? 11.009 25.424  7.572  1.00 25.77 ? 163 MET A N     1 
ATOM   1348 C  CA    . MET A 1 163 ? 11.123 26.444  8.587  1.00 28.40 ? 163 MET A CA    1 
ATOM   1349 C  C     . MET A 1 163 ? 12.578 26.866  8.730  1.00 27.74 ? 163 MET A C     1 
ATOM   1350 O  O     . MET A 1 163 ? 13.495 26.059  8.623  1.00 25.70 ? 163 MET A O     1 
ATOM   1351 C  CB    . MET A 1 163 ? 10.529 25.948  9.907  1.00 28.65 ? 163 MET A CB    1 
ATOM   1352 C  CG    . MET A 1 163 ? 9.026  26.186  9.916  1.00 32.56 ? 163 MET A CG    1 
ATOM   1353 S  SD    . MET A 1 163 ? 8.320  25.743  11.477 1.00 40.19 ? 163 MET A SD    1 
ATOM   1354 C  CE    . MET A 1 163 ? 8.715  27.170  12.476 1.00 38.38 ? 163 MET A CE    1 
ATOM   1355 N  N     . ILE A 1 164 ? 12.755 28.168  8.927  1.00 29.36 ? 164 ILE A N     1 
ATOM   1356 C  CA    . ILE A 1 164 ? 14.042 28.706  9.353  1.00 30.71 ? 164 ILE A CA    1 
ATOM   1357 C  C     . ILE A 1 164 ? 14.312 28.156  10.741 1.00 27.72 ? 164 ILE A C     1 
ATOM   1358 O  O     . ILE A 1 164 ? 13.410 28.213  11.576 1.00 25.01 ? 164 ILE A O     1 
ATOM   1359 C  CB    . ILE A 1 164 ? 13.973 30.244  9.345  1.00 33.02 ? 164 ILE A CB    1 
ATOM   1360 C  CG1   . ILE A 1 164 ? 13.700 30.737  7.930  1.00 38.35 ? 164 ILE A CG1   1 
ATOM   1361 C  CG2   . ILE A 1 164 ? 15.226 30.872  9.926  1.00 34.22 ? 164 ILE A CG2   1 
ATOM   1362 C  CD1   . ILE A 1 164 ? 14.629 30.139  6.917  1.00 40.49 ? 164 ILE A CD1   1 
ATOM   1363 N  N     . PRO A 1 165 ? 15.509 27.588  11.029 1.00 27.11 ? 165 PRO A N     1 
ATOM   1364 C  CA    . PRO A 1 165 ? 15.730 26.919  12.303 1.00 26.44 ? 165 PRO A CA    1 
ATOM   1365 C  C     . PRO A 1 165 ? 15.412 27.813  13.491 1.00 26.59 ? 165 PRO A C     1 
ATOM   1366 O  O     . PRO A 1 165 ? 14.825 27.351  14.457 1.00 25.63 ? 165 PRO A O     1 
ATOM   1367 C  CB    . PRO A 1 165 ? 17.208 26.478  12.270 1.00 26.46 ? 165 PRO A CB    1 
ATOM   1368 C  CG    . PRO A 1 165 ? 17.527 26.394  10.802 1.00 26.97 ? 165 PRO A CG    1 
ATOM   1369 C  CD    . PRO A 1 165 ? 16.654 27.431  10.127 1.00 28.30 ? 165 PRO A CD    1 
ATOM   1370 N  N     . LYS A 1 166 ? 15.793 29.090  13.416 1.00 27.35 ? 166 LYS A N     1 
ATOM   1371 C  CA    . LYS A 1 166 ? 15.519 30.033  14.488 1.00 29.49 ? 166 LYS A CA    1 
ATOM   1372 C  C     . LYS A 1 166 ? 14.034 30.054  14.810 1.00 27.72 ? 166 LYS A C     1 
ATOM   1373 O  O     . LYS A 1 166 ? 13.620 30.071  15.973 1.00 27.95 ? 166 LYS A O     1 
ATOM   1374 C  CB    . LYS A 1 166 ? 15.992 31.414  14.014 1.00 34.22 ? 166 LYS A CB    1 
ATOM   1375 C  CG    . LYS A 1 166 ? 15.787 32.573  14.962 1.00 39.39 ? 166 LYS A CG    1 
ATOM   1376 C  CD    . LYS A 1 166 ? 16.399 33.864  14.414 1.00 44.66 ? 166 LYS A CD    1 
ATOM   1377 C  CE    . LYS A 1 166 ? 16.016 35.102  15.200 1.00 51.46 ? 166 LYS A CE    1 
ATOM   1378 N  NZ    . LYS A 1 166 ? 16.905 36.249  14.872 1.00 57.15 ? 166 LYS A NZ    1 
ATOM   1379 N  N     . ASN A 1 167 ? 13.228 30.075  13.746 1.00 26.85 ? 167 ASN A N     1 
ATOM   1380 C  CA    . ASN A 1 167 ? 11.784 30.149  13.873 1.00 27.28 ? 167 ASN A CA    1 
ATOM   1381 C  C     . ASN A 1 167 ? 11.212 28.856  14.432 1.00 25.67 ? 167 ASN A C     1 
ATOM   1382 O  O     . ASN A 1 167 ? 10.221 28.905  15.154 1.00 25.93 ? 167 ASN A O     1 
ATOM   1383 C  CB    . ASN A 1 167 ? 11.101 30.546  12.564 1.00 28.69 ? 167 ASN A CB    1 
ATOM   1384 C  CG    . ASN A 1 167 ? 11.330 32.002  12.233 1.00 31.70 ? 167 ASN A CG    1 
ATOM   1385 O  OD1   . ASN A 1 167 ? 11.727 32.779  13.096 1.00 31.92 ? 167 ASN A OD1   1 
ATOM   1386 N  ND2   . ASN A 1 167 ? 11.112 32.375  10.986 1.00 32.42 ? 167 ASN A ND2   1 
ATOM   1387 N  N     . PHE A 1 168 ? 11.819 27.701  14.119 1.00 23.81 ? 168 PHE A N     1 
ATOM   1388 C  CA    . PHE A 1 168 ? 11.334 26.461  14.703 1.00 22.77 ? 168 PHE A CA    1 
ATOM   1389 C  C     . PHE A 1 168 ? 11.562 26.434  16.224 1.00 22.45 ? 168 PHE A C     1 
ATOM   1390 O  O     . PHE A 1 168 ? 10.757 25.898  16.986 1.00 21.09 ? 168 PHE A O     1 
ATOM   1391 C  CB    . PHE A 1 168 ? 11.987 25.254  14.034 1.00 21.87 ? 168 PHE A CB    1 
ATOM   1392 C  CG    . PHE A 1 168 ? 11.446 23.925  14.492 1.00 21.31 ? 168 PHE A CG    1 
ATOM   1393 C  CD1   . PHE A 1 168 ? 10.084 23.662  14.528 1.00 22.00 ? 168 PHE A CD1   1 
ATOM   1394 C  CD2   . PHE A 1 168 ? 12.305 22.914  14.889 1.00 20.27 ? 168 PHE A CD2   1 
ATOM   1395 C  CE1   . PHE A 1 168 ? 9.603  22.435  14.959 1.00 20.74 ? 168 PHE A CE1   1 
ATOM   1396 C  CE2   . PHE A 1 168 ? 11.827 21.687  15.301 1.00 19.65 ? 168 PHE A CE2   1 
ATOM   1397 C  CZ    . PHE A 1 168 ? 10.471 21.445  15.341 1.00 20.68 ? 168 PHE A CZ    1 
ATOM   1398 N  N     . GLY A 1 169 ? 12.694 26.965  16.667 1.00 22.35 ? 169 GLY A N     1 
ATOM   1399 C  CA    . GLY A 1 169 ? 12.923 27.097  18.098 1.00 23.38 ? 169 GLY A CA    1 
ATOM   1400 C  C     . GLY A 1 169 ? 11.860 27.948  18.790 1.00 25.10 ? 169 GLY A C     1 
ATOM   1401 O  O     . GLY A 1 169 ? 11.421 27.606  19.881 1.00 26.37 ? 169 GLY A O     1 
ATOM   1402 N  N     . LYS A 1 170 ? 11.458 29.055  18.149 1.00 26.64 ? 170 LYS A N     1 
ATOM   1403 C  CA    . LYS A 1 170 ? 10.420 29.918  18.667 1.00 30.03 ? 170 LYS A CA    1 
ATOM   1404 C  C     . LYS A 1 170 ? 9.081  29.185  18.728 1.00 29.61 ? 170 LYS A C     1 
ATOM   1405 O  O     . LYS A 1 170 ? 8.300  29.377  19.659 1.00 30.83 ? 170 LYS A O     1 
ATOM   1406 C  CB    . LYS A 1 170 ? 10.268 31.163  17.792 1.00 34.72 ? 170 LYS A CB    1 
ATOM   1407 C  CG    . LYS A 1 170 ? 11.508 32.038  17.751 1.00 37.05 ? 170 LYS A CG    1 
ATOM   1408 C  CD    . LYS A 1 170 ? 11.285 33.362  17.090 1.00 42.28 ? 170 LYS A CD    1 
ATOM   1409 C  CE    . LYS A 1 170 ? 12.565 34.166  17.044 1.00 44.65 ? 170 LYS A CE    1 
ATOM   1410 N  NZ    . LYS A 1 170 ? 12.239 35.570  16.757 1.00 49.28 ? 170 LYS A NZ    1 
ATOM   1411 N  N     . LEU A 1 171 ? 8.826  28.348  17.727 1.00 28.11 ? 171 LEU A N     1 
ATOM   1412 C  CA    . LEU A 1 171 ? 7.619  27.536  17.696 1.00 28.01 ? 171 LEU A CA    1 
ATOM   1413 C  C     . LEU A 1 171 ? 7.625  26.515  18.832 1.00 25.23 ? 171 LEU A C     1 
ATOM   1414 O  O     . LEU A 1 171 ? 6.617  26.357  19.500 1.00 24.86 ? 171 LEU A O     1 
ATOM   1415 C  CB    . LEU A 1 171 ? 7.523  26.852  16.330 1.00 27.94 ? 171 LEU A CB    1 
ATOM   1416 C  CG    . LEU A 1 171 ? 6.330  25.921  16.120 1.00 28.93 ? 171 LEU A CG    1 
ATOM   1417 C  CD1   . LEU A 1 171 ? 5.000  26.657  16.313 1.00 29.96 ? 171 LEU A CD1   1 
ATOM   1418 C  CD2   . LEU A 1 171 ? 6.394  25.318  14.711 1.00 28.07 ? 171 LEU A CD2   1 
ATOM   1419 N  N     . LEU A 1 172 ? 8.740  25.802  19.011 1.00 23.44 ? 172 LEU A N     1 
ATOM   1420 C  CA    . LEU A 1 172 ? 8.821  24.788  20.053 1.00 23.68 ? 172 LEU A CA    1 
ATOM   1421 C  C     . LEU A 1 172 ? 8.514  25.389  21.430 1.00 24.94 ? 172 LEU A C     1 
ATOM   1422 O  O     . LEU A 1 172 ? 7.917  24.707  22.265 1.00 25.25 ? 172 LEU A O     1 
ATOM   1423 C  CB    . LEU A 1 172 ? 10.227 24.178  20.064 1.00 22.80 ? 172 LEU A CB    1 
ATOM   1424 C  CG    . LEU A 1 172 ? 10.566 23.223  18.922 1.00 22.05 ? 172 LEU A CG    1 
ATOM   1425 C  CD1   . LEU A 1 172 ? 12.057 22.953  18.841 1.00 21.93 ? 172 LEU A CD1   1 
ATOM   1426 C  CD2   . LEU A 1 172 ? 9.797  21.907  19.068 1.00 22.39 ? 172 LEU A CD2   1 
ATOM   1427 N  N     . ASP A 1 173 ? 8.971  26.628  21.674 1.00 25.14 ? 173 ASP A N     1 
ATOM   1428 C  CA    . ASP A 1 173 ? 8.802  27.325  22.952 1.00 27.19 ? 173 ASP A CA    1 
ATOM   1429 C  C     . ASP A 1 173 ? 7.349  27.742  23.231 1.00 28.31 ? 173 ASP A C     1 
ATOM   1430 O  O     . ASP A 1 173 ? 7.027  28.249  24.315 1.00 30.13 ? 173 ASP A O     1 
ATOM   1431 C  CB    . ASP A 1 173 ? 9.713  28.562  23.019 1.00 28.24 ? 173 ASP A CB    1 
ATOM   1432 C  CG    . ASP A 1 173 ? 9.710  29.209  24.393 1.00 31.21 ? 173 ASP A CG    1 
ATOM   1433 O  OD1   . ASP A 1 173 ? 9.974  28.494  25.376 1.00 32.45 ? 173 ASP A OD1   1 
ATOM   1434 O  OD2   . ASP A 1 173 ? 9.377  30.393  24.477 1.00 35.19 ? 173 ASP A OD2   1 
ATOM   1435 N  N     . LYS A 1 174 ? 6.452  27.504  22.278 1.00 28.31 ? 174 LYS A N     1 
ATOM   1436 C  CA    . LYS A 1 174 ? 5.049  27.810  22.463 1.00 29.51 ? 174 LYS A CA    1 
ATOM   1437 C  C     . LYS A 1 174 ? 4.308  26.633  23.091 1.00 28.93 ? 174 LYS A C     1 
ATOM   1438 O  O     . LYS A 1 174 ? 3.119  26.756  23.378 1.00 28.97 ? 174 LYS A O     1 
ATOM   1439 C  CB    . LYS A 1 174 ? 4.391  28.152  21.127 1.00 30.12 ? 174 LYS A CB    1 
ATOM   1440 C  CG    . LYS A 1 174 ? 4.892  29.409  20.427 1.00 32.60 ? 174 LYS A CG    1 
ATOM   1441 C  CD    . LYS A 1 174 ? 4.259  29.552  19.045 1.00 33.99 ? 174 LYS A CD    1 
ATOM   1442 C  CE    . LYS A 1 174 ? 4.849  30.631  18.168 1.00 37.17 ? 174 LYS A CE    1 
ATOM   1443 N  NZ    . LYS A 1 174 ? 4.730  31.952  18.805 1.00 38.28 ? 174 LYS A NZ    1 
ATOM   1444 N  N     . PHE A 1 175 ? 5.002  25.510  23.287 1.00 27.92 ? 175 PHE A N     1 
ATOM   1445 C  CA    . PHE A 1 175 ? 4.396  24.313  23.832 1.00 27.91 ? 175 PHE A CA    1 
ATOM   1446 C  C     . PHE A 1 175 ? 5.019  23.987  25.185 1.00 29.13 ? 175 PHE A C     1 
ATOM   1447 O  O     . PHE A 1 175 ? 6.059  24.532  25.556 1.00 28.74 ? 175 PHE A O     1 
ATOM   1448 C  CB    . PHE A 1 175 ? 4.520  23.176  22.818 1.00 27.22 ? 175 PHE A CB    1 
ATOM   1449 C  CG    . PHE A 1 175 ? 3.835  23.477  21.509 1.00 26.65 ? 175 PHE A CG    1 
ATOM   1450 C  CD1   . PHE A 1 175 ? 2.454  23.405  21.389 1.00 28.65 ? 175 PHE A CD1   1 
ATOM   1451 C  CD2   . PHE A 1 175 ? 4.551  23.945  20.423 1.00 27.59 ? 175 PHE A CD2   1 
ATOM   1452 C  CE1   . PHE A 1 175 ? 1.816  23.710  20.188 1.00 28.16 ? 175 PHE A CE1   1 
ATOM   1453 C  CE2   . PHE A 1 175 ? 3.912  24.242  19.220 1.00 27.27 ? 175 PHE A CE2   1 
ATOM   1454 C  CZ    . PHE A 1 175 ? 2.551  24.152  19.112 1.00 27.49 ? 175 PHE A CZ    1 
ATOM   1455 N  N     . LYS A 1 176 ? 4.345  23.097  25.913 1.00 30.19 ? 176 LYS A N     1 
ATOM   1456 C  CA    . LYS A 1 176 ? 4.749  22.708  27.249 1.00 32.41 ? 176 LYS A CA    1 
ATOM   1457 C  C     . LYS A 1 176 ? 5.736  21.556  27.172 1.00 30.57 ? 176 LYS A C     1 
ATOM   1458 O  O     . LYS A 1 176 ? 6.658  21.510  27.970 1.00 29.34 ? 176 LYS A O     1 
ATOM   1459 C  CB    . LYS A 1 176 ? 3.547  22.242  28.071 1.00 35.14 ? 176 LYS A CB    1 
ATOM   1460 C  CG    . LYS A 1 176 ? 2.428  23.265  28.205 1.00 39.56 ? 176 LYS A CG    1 
ATOM   1461 C  CD    . LYS A 1 176 ? 1.155  22.631  28.748 1.00 43.69 ? 176 LYS A CD    1 
ATOM   1462 C  CE    . LYS A 1 176 ? -0.059 23.519  28.629 1.00 47.83 ? 176 LYS A CE    1 
ATOM   1463 N  NZ    . LYS A 1 176 ? 0.263  24.912  29.017 1.00 53.19 ? 176 LYS A NZ    1 
ATOM   1464 N  N     . LYS A 1 177 ? 5.498  20.613  26.244 1.00 27.72 ? 177 LYS A N     1 
ATOM   1465 C  CA    . LYS A 1 177 ? 6.165  19.325  26.291 1.00 26.27 ? 177 LYS A CA    1 
ATOM   1466 C  C     . LYS A 1 177 ? 6.362  18.803  24.867 1.00 25.01 ? 177 LYS A C     1 
ATOM   1467 O  O     . LYS A 1 177 ? 5.956  17.686  24.510 1.00 24.72 ? 177 LYS A O     1 
ATOM   1468 C  CB    . LYS A 1 177 ? 5.376  18.355  27.180 1.00 26.88 ? 177 LYS A CB    1 
ATOM   1469 C  CG    . LYS A 1 177 ? 6.195  17.166  27.665 1.00 27.95 ? 177 LYS A CG    1 
ATOM   1470 C  CD    . LYS A 1 177 ? 5.430  16.184  28.557 1.00 29.88 ? 177 LYS A CD    1 
ATOM   1471 C  CE    . LYS A 1 177 ? 6.344  15.351  29.432 1.00 31.39 ? 177 LYS A CE    1 
ATOM   1472 N  NZ    . LYS A 1 177 ? 5.685  14.163  30.035 1.00 30.36 ? 177 LYS A NZ    1 
ATOM   1473 N  N     . PRO A 1 178 ? 6.965  19.624  23.996 1.00 24.02 ? 178 PRO A N     1 
ATOM   1474 C  CA    . PRO A 1 178 ? 7.082  19.274  22.589 1.00 22.82 ? 178 PRO A CA    1 
ATOM   1475 C  C     . PRO A 1 178 ? 8.017  18.086  22.419 1.00 22.21 ? 178 PRO A C     1 
ATOM   1476 O  O     . PRO A 1 178 ? 9.076  18.066  23.017 1.00 22.31 ? 178 PRO A O     1 
ATOM   1477 C  CB    . PRO A 1 178 ? 7.691  20.537  21.980 1.00 23.65 ? 178 PRO A CB    1 
ATOM   1478 C  CG    . PRO A 1 178 ? 8.472  21.150  23.092 1.00 24.27 ? 178 PRO A CG    1 
ATOM   1479 C  CD    . PRO A 1 178 ? 7.618  20.910  24.319 1.00 24.59 ? 178 PRO A CD    1 
ATOM   1480 N  N     . THR A 1 179 ? 7.605  17.127  21.587 1.00 21.71 ? 179 THR A N     1 
ATOM   1481 C  CA    . THR A 1 179 ? 8.402  15.981  21.211 1.00 21.11 ? 179 THR A CA    1 
ATOM   1482 C  C     . THR A 1 179 ? 8.880  16.204  19.780 1.00 19.91 ? 179 THR A C     1 
ATOM   1483 O  O     . THR A 1 179 ? 8.085  16.613  18.927 1.00 19.15 ? 179 THR A O     1 
ATOM   1484 C  CB    . THR A 1 179 ? 7.551  14.721  21.410 1.00 21.94 ? 179 THR A CB    1 
ATOM   1485 O  OG1   . THR A 1 179 ? 7.258  14.672  22.806 1.00 25.63 ? 179 THR A OG1   1 
ATOM   1486 C  CG2   . THR A 1 179 ? 8.228  13.446  20.974 1.00 22.22 ? 179 THR A CG2   1 
ATOM   1487 N  N     . VAL A 1 180 ? 10.177 15.953  19.560 1.00 19.90 ? 180 VAL A N     1 
ATOM   1488 C  CA    . VAL A 1 180 ? 10.794 16.027  18.247 1.00 18.45 ? 180 VAL A CA    1 
ATOM   1489 C  C     . VAL A 1 180 ? 11.443 14.678  17.958 1.00 18.75 ? 180 VAL A C     1 
ATOM   1490 O  O     . VAL A 1 180 ? 12.195 14.148  18.792 1.00 16.83 ? 180 VAL A O     1 
ATOM   1491 C  CB    . VAL A 1 180 ? 11.808 17.189  18.145 1.00 18.08 ? 180 VAL A CB    1 
ATOM   1492 C  CG1   . VAL A 1 180 ? 12.574 17.158  16.839 1.00 18.27 ? 180 VAL A CG1   1 
ATOM   1493 C  CG2   . VAL A 1 180 ? 11.135 18.541  18.306 1.00 19.26 ? 180 VAL A CG2   1 
ATOM   1494 N  N     . ILE A 1 181 ? 11.142 14.169  16.754 1.00 18.14 ? 181 ILE A N     1 
ATOM   1495 C  CA    . ILE A 1 181 ? 11.618 12.883  16.289 1.00 18.80 ? 181 ILE A CA    1 
ATOM   1496 C  C     . ILE A 1 181 ? 12.621 13.108  15.169 1.00 18.32 ? 181 ILE A C     1 
ATOM   1497 O  O     . ILE A 1 181 ? 12.318 13.781  14.195 1.00 17.42 ? 181 ILE A O     1 
ATOM   1498 C  CB    . ILE A 1 181 ? 10.460 11.976  15.841 1.00 20.56 ? 181 ILE A CB    1 
ATOM   1499 C  CG1   . ILE A 1 181 ? 9.524  11.650  17.013 1.00 22.31 ? 181 ILE A CG1   1 
ATOM   1500 C  CG2   . ILE A 1 181 ? 11.014 10.722  15.174 1.00 21.78 ? 181 ILE A CG2   1 
ATOM   1501 C  CD1   . ILE A 1 181 ? 8.177  11.094  16.609 1.00 25.22 ? 181 ILE A CD1   1 
ATOM   1502 N  N     . VAL A 1 182 ? 13.815 12.513  15.309 1.00 16.87 ? 182 VAL A N     1 
ATOM   1503 C  CA    . VAL A 1 182 ? 14.807 12.581  14.243 1.00 17.64 ? 182 VAL A CA    1 
ATOM   1504 C  C     . VAL A 1 182 ? 15.184 11.155  13.895 1.00 16.61 ? 182 VAL A C     1 
ATOM   1505 O  O     . VAL A 1 182 ? 15.420 10.393  14.811 1.00 17.20 ? 182 VAL A O     1 
ATOM   1506 C  CB    . VAL A 1 182 ? 16.074 13.321  14.705 1.00 17.94 ? 182 VAL A CB    1 
ATOM   1507 C  CG1   . VAL A 1 182 ? 17.143 13.297  13.633 1.00 18.01 ? 182 VAL A CG1   1 
ATOM   1508 C  CG2   . VAL A 1 182 ? 15.765 14.734  15.140 1.00 18.95 ? 182 VAL A CG2   1 
ATOM   1509 N  N     . GLY A 1 183 ? 15.262 10.813  12.612 1.00 16.61 ? 183 GLY A N     1 
ATOM   1510 C  CA    . GLY A 1 183 ? 15.559 9.442   12.245 1.00 18.24 ? 183 GLY A CA    1 
ATOM   1511 C  C     . GLY A 1 183 ? 17.015 9.106   12.547 1.00 18.38 ? 183 GLY A C     1 
ATOM   1512 O  O     . GLY A 1 183 ? 17.900 9.868   12.142 1.00 18.07 ? 183 GLY A O     1 
ATOM   1513 N  N     . GLY A 1 184 ? 17.253 7.923   13.135 1.00 18.85 ? 184 GLY A N     1 
ATOM   1514 C  CA    . GLY A 1 184 ? 18.616 7.480   13.420 1.00 19.77 ? 184 GLY A CA    1 
ATOM   1515 C  C     . GLY A 1 184 ? 19.209 6.566   12.345 1.00 23.55 ? 184 GLY A C     1 
ATOM   1516 O  O     . GLY A 1 184 ? 19.928 5.607   12.650 1.00 22.55 ? 184 GLY A O     1 
ATOM   1517 N  N     . PHE A 1 185 ? 18.835 6.812   11.093 1.00 26.66 ? 185 PHE A N     1 
ATOM   1518 C  CA    . PHE A 1 185 ? 19.191 5.947   9.984  1.00 26.26 ? 185 PHE A CA    1 
ATOM   1519 C  C     . PHE A 1 185 ? 19.871 6.844   8.958  1.00 27.20 ? 185 PHE A C     1 
ATOM   1520 O  O     . PHE A 1 185 ? 19.594 8.033   8.913  1.00 29.88 ? 185 PHE A O     1 
ATOM   1521 C  CB    . PHE A 1 185 ? 17.967 5.190   9.448  1.00 25.65 ? 185 PHE A CB    1 
ATOM   1522 C  CG    . PHE A 1 185 ? 16.717 6.020   9.278  1.00 25.73 ? 185 PHE A CG    1 
ATOM   1523 C  CD1   . PHE A 1 185 ? 16.475 6.736   8.107  1.00 25.78 ? 185 PHE A CD1   1 
ATOM   1524 C  CD2   . PHE A 1 185 ? 15.790 6.099   10.304 1.00 23.66 ? 185 PHE A CD2   1 
ATOM   1525 C  CE1   . PHE A 1 185 ? 15.349 7.540   7.989  1.00 24.45 ? 185 PHE A CE1   1 
ATOM   1526 C  CE2   . PHE A 1 185 ? 14.654 6.880   10.178 1.00 23.31 ? 185 PHE A CE2   1 
ATOM   1527 C  CZ    . PHE A 1 185 ? 14.441 7.610   9.018  1.00 23.55 ? 185 PHE A CZ    1 
ATOM   1528 N  N     . PRO A 1 186 ? 20.812 6.340   8.131  1.00 28.24 ? 186 PRO A N     1 
ATOM   1529 C  CA    . PRO A 1 186 ? 21.581 7.216   7.251  1.00 29.36 ? 186 PRO A CA    1 
ATOM   1530 C  C     . PRO A 1 186 ? 20.821 7.738   6.025  1.00 32.19 ? 186 PRO A C     1 
ATOM   1531 O  O     . PRO A 1 186 ? 21.098 8.829   5.536  1.00 34.31 ? 186 PRO A O     1 
ATOM   1532 C  CB    . PRO A 1 186 ? 22.735 6.323   6.784  1.00 29.50 ? 186 PRO A CB    1 
ATOM   1533 C  CG    . PRO A 1 186 ? 22.182 4.915   6.872  1.00 29.42 ? 186 PRO A CG    1 
ATOM   1534 C  CD    . PRO A 1 186 ? 21.167 4.924   8.000  1.00 28.15 ? 186 PRO A CD    1 
ATOM   1535 N  N     . HIS A 1 187 ? 19.891 6.951   5.508  1.00 33.06 ? 187 HIS A N     1 
ATOM   1536 C  CA    . HIS A 1 187 ? 19.096 7.397   4.372  1.00 38.24 ? 187 HIS A CA    1 
ATOM   1537 C  C     . HIS A 1 187 ? 17.805 6.589   4.354  1.00 39.97 ? 187 HIS A C     1 
ATOM   1538 O  O     . HIS A 1 187 ? 17.663 5.590   5.075  1.00 38.45 ? 187 HIS A O     1 
ATOM   1539 C  CB    . HIS A 1 187 ? 19.905 7.290   3.069  1.00 37.49 ? 187 HIS A CB    1 
ATOM   1540 C  CG    . HIS A 1 187 ? 20.533 5.946   2.925  1.00 41.34 ? 187 HIS A CG    1 
ATOM   1541 N  ND1   . HIS A 1 187 ? 19.802 4.801   2.670  1.00 47.15 ? 187 HIS A ND1   1 
ATOM   1542 C  CD2   . HIS A 1 187 ? 21.811 5.559   3.052  1.00 44.06 ? 187 HIS A CD2   1 
ATOM   1543 C  CE1   . HIS A 1 187 ? 20.616 3.759   2.650  1.00 46.16 ? 187 HIS A CE1   1 
ATOM   1544 N  NE2   . HIS A 1 187 ? 21.841 4.199   2.905  1.00 48.16 ? 187 HIS A NE2   1 
ATOM   1545 N  N     . GLY A 1 188 ? 16.884 7.046   3.501  1.00 39.98 ? 188 GLY A N     1 
ATOM   1546 C  CA    . GLY A 1 188 ? 15.612 6.383   3.297  1.00 37.98 ? 188 GLY A CA    1 
ATOM   1547 C  C     . GLY A 1 188 ? 14.524 6.960   4.195  1.00 35.61 ? 188 GLY A C     1 
ATOM   1548 O  O     . GLY A 1 188 ? 14.658 8.056   4.733  1.00 33.88 ? 188 GLY A O     1 
ATOM   1549 N  N     . ASP A 1 189 ? 13.428 6.204   4.272  1.00 36.34 ? 189 ASP A N     1 
ATOM   1550 C  CA    . ASP A 1 189 ? 12.211 6.635   4.925  1.00 36.16 ? 189 ASP A CA    1 
ATOM   1551 C  C     . ASP A 1 189 ? 12.242 6.138   6.369  1.00 30.30 ? 189 ASP A C     1 
ATOM   1552 O  O     . ASP A 1 189 ? 12.896 5.152   6.637  1.00 27.53 ? 189 ASP A O     1 
ATOM   1553 C  CB    . ASP A 1 189 ? 10.991 6.006   4.238  1.00 38.91 ? 189 ASP A CB    1 
ATOM   1554 C  CG    . ASP A 1 189 ? 10.831 6.339   2.756  1.00 48.10 ? 189 ASP A CG    1 
ATOM   1555 O  OD1   . ASP A 1 189 ? 11.397 7.353   2.305  1.00 50.03 ? 189 ASP A OD1   1 
ATOM   1556 O  OD2   . ASP A 1 189 ? 10.149 5.555   2.058  1.00 51.17 ? 189 ASP A OD2   1 
ATOM   1557 N  N     . PHE A 1 190 ? 11.424 6.740   7.230  1.00 28.43 ? 190 PHE A N     1 
ATOM   1558 C  CA    . PHE A 1 190 ? 11.099 6.193   8.538  1.00 27.73 ? 190 PHE A CA    1 
ATOM   1559 C  C     . PHE A 1 190 ? 10.455 4.814   8.390  1.00 30.39 ? 190 PHE A C     1 
ATOM   1560 O  O     . PHE A 1 190 ? 9.851  4.521   7.373  1.00 28.91 ? 190 PHE A O     1 
ATOM   1561 C  CB    . PHE A 1 190 ? 10.152 7.137   9.271  1.00 27.29 ? 190 PHE A CB    1 
ATOM   1562 C  CG    . PHE A 1 190 ? 10.806 8.343   9.901  1.00 26.30 ? 190 PHE A CG    1 
ATOM   1563 C  CD1   . PHE A 1 190 ? 11.448 8.235   11.116 1.00 23.72 ? 190 PHE A CD1   1 
ATOM   1564 C  CD2   . PHE A 1 190 ? 10.798 9.574   9.255  1.00 25.96 ? 190 PHE A CD2   1 
ATOM   1565 C  CE1   . PHE A 1 190 ? 12.046 9.339   11.696 1.00 24.81 ? 190 PHE A CE1   1 
ATOM   1566 C  CE2   . PHE A 1 190 ? 11.417 10.677  9.823  1.00 23.76 ? 190 PHE A CE2   1 
ATOM   1567 C  CZ    . PHE A 1 190 ? 12.012 10.562  11.055 1.00 24.95 ? 190 PHE A CZ    1 
ATOM   1568 N  N     . LYS A 1 191 ? 10.571 3.962   9.408  1.00 30.85 ? 191 LYS A N     1 
ATOM   1569 C  CA    . LYS A 1 191 ? 9.840  2.705   9.419  1.00 34.88 ? 191 LYS A CA    1 
ATOM   1570 C  C     . LYS A 1 191 ? 8.584  2.884   10.244 1.00 36.25 ? 191 LYS A C     1 
ATOM   1571 O  O     . LYS A 1 191 ? 7.569  2.283   9.939  1.00 42.19 ? 191 LYS A O     1 
ATOM   1572 C  CB    . LYS A 1 191 ? 10.647 1.555   10.023 1.00 41.25 ? 191 LYS A CB    1 
ATOM   1573 C  CG    . LYS A 1 191 ? 12.103 1.469   9.612  1.00 46.79 ? 191 LYS A CG    1 
ATOM   1574 C  CD    . LYS A 1 191 ? 12.689 0.065   9.781  1.00 53.92 ? 191 LYS A CD    1 
ATOM   1575 C  CE    . LYS A 1 191 ? 12.386 -0.596  11.110 1.00 55.24 ? 191 LYS A CE    1 
ATOM   1576 N  NZ    . LYS A 1 191 ? 12.368 -2.076  10.991 1.00 54.49 ? 191 LYS A NZ    1 
ATOM   1577 N  N     . SER A 1 192 ? 8.669  3.716   11.279 1.00 32.16 ? 192 SER A N     1 
ATOM   1578 C  CA    . SER A 1 192 ? 7.578  3.963   12.199 1.00 35.02 ? 192 SER A CA    1 
ATOM   1579 C  C     . SER A 1 192 ? 6.800  5.220   11.788 1.00 41.26 ? 192 SER A C     1 
ATOM   1580 O  O     . SER A 1 192 ? 7.228  6.351   12.064 1.00 45.70 ? 192 SER A O     1 
ATOM   1581 C  CB    . SER A 1 192 ? 8.106  4.090   13.633 1.00 30.88 ? 192 SER A CB    1 
ATOM   1582 O  OG    . SER A 1 192 ? 8.807  2.913   14.046 1.00 26.70 ? 192 SER A OG    1 
ATOM   1583 N  N     . LYS A 1 193 ? 5.604  5.016   11.231 1.00 40.83 ? 193 LYS A N     1 
ATOM   1584 C  CA    . LYS A 1 193 ? 4.708  6.123   10.937 1.00 41.60 ? 193 LYS A CA    1 
ATOM   1585 C  C     . LYS A 1 193 ? 3.841  6.378   12.163 1.00 41.44 ? 193 LYS A C     1 
ATOM   1586 O  O     . LYS A 1 193 ? 3.064  5.516   12.570 1.00 49.38 ? 193 LYS A O     1 
ATOM   1587 C  CB    . LYS A 1 193 ? 3.842  5.819   9.715  1.00 48.89 ? 193 LYS A CB    1 
ATOM   1588 C  CG    . LYS A 1 193 ? 4.622  5.436   8.465  1.00 52.13 ? 193 LYS A CG    1 
ATOM   1589 C  CD    . LYS A 1 193 ? 5.868  6.272   8.252  1.00 52.62 ? 193 LYS A CD    1 
ATOM   1590 C  CE    . LYS A 1 193 ? 6.195  6.473   6.789  1.00 56.04 ? 193 LYS A CE    1 
ATOM   1591 N  NZ    . LYS A 1 193 ? 6.675  5.244   6.126  1.00 55.64 ? 193 LYS A NZ    1 
ATOM   1592 N  N     . VAL A 1 194 ? 4.059  7.537   12.780 1.00 34.98 ? 194 VAL A N     1 
ATOM   1593 C  CA    . VAL A 1 194 ? 3.305  7.976   13.936 1.00 32.38 ? 194 VAL A CA    1 
ATOM   1594 C  C     . VAL A 1 194 ? 2.681  9.309   13.541 1.00 29.97 ? 194 VAL A C     1 
ATOM   1595 O  O     . VAL A 1 194 ? 3.181  9.947   12.613 1.00 26.48 ? 194 VAL A O     1 
ATOM   1596 C  CB    . VAL A 1 194 ? 4.199  8.115   15.184 1.00 30.54 ? 194 VAL A CB    1 
ATOM   1597 C  CG1   . VAL A 1 194 ? 4.809  6.780   15.625 1.00 30.36 ? 194 VAL A CG1   1 
ATOM   1598 C  CG2   . VAL A 1 194 ? 5.301  9.140   14.960 1.00 31.09 ? 194 VAL A CG2   1 
ATOM   1599 N  N     . ASP A 1 195 ? 1.638  9.743   14.264 1.00 28.85 ? 195 ASP A N     1 
ATOM   1600 C  CA    . ASP A 1 195 ? 1.076  11.064  14.005 1.00 31.59 ? 195 ASP A CA    1 
ATOM   1601 C  C     . ASP A 1 195 ? 2.090  12.126  14.436 1.00 29.36 ? 195 ASP A C     1 
ATOM   1602 O  O     . ASP A 1 195 ? 2.649  12.050  15.535 1.00 30.94 ? 195 ASP A O     1 
ATOM   1603 C  CB    . ASP A 1 195 ? -0.229 11.334  14.760 1.00 32.87 ? 195 ASP A CB    1 
ATOM   1604 C  CG    . ASP A 1 195 ? -1.437 10.589  14.229 1.00 39.12 ? 195 ASP A CG    1 
ATOM   1605 O  OD1   . ASP A 1 195 ? -1.292 9.851   13.193 1.00 38.81 ? 195 ASP A OD1   1 
ATOM   1606 O  OD2   . ASP A 1 195 ? -2.525 10.766  14.839 1.00 40.88 ? 195 ASP A OD2   1 
ATOM   1607 N  N     . GLY A 1 196 ? 2.326  13.095  13.556 1.00 26.70 ? 196 GLY A N     1 
ATOM   1608 C  CA    . GLY A 1 196 ? 3.137  14.242  13.918 1.00 24.96 ? 196 GLY A CA    1 
ATOM   1609 C  C     . GLY A 1 196 ? 3.229  15.257  12.791 1.00 23.58 ? 196 GLY A C     1 
ATOM   1610 O  O     . GLY A 1 196 ? 2.885  14.978  11.647 1.00 22.77 ? 196 GLY A O     1 
ATOM   1611 N  N     . VAL A 1 197 ? 3.716  16.441  13.143 1.00 22.22 ? 197 VAL A N     1 
ATOM   1612 C  CA    . VAL A 1 197 ? 3.878  17.523  12.194 1.00 22.19 ? 197 VAL A CA    1 
ATOM   1613 C  C     . VAL A 1 197 ? 5.249  17.409  11.537 1.00 20.60 ? 197 VAL A C     1 
ATOM   1614 O  O     . VAL A 1 197 ? 6.246  17.582  12.209 1.00 18.43 ? 197 VAL A O     1 
ATOM   1615 C  CB    . VAL A 1 197 ? 3.746  18.863  12.930 1.00 23.05 ? 197 VAL A CB    1 
ATOM   1616 C  CG1   . VAL A 1 197 ? 3.897  20.023  11.956 1.00 23.90 ? 197 VAL A CG1   1 
ATOM   1617 C  CG2   . VAL A 1 197 ? 2.443  18.921  13.725 1.00 25.22 ? 197 VAL A CG2   1 
ATOM   1618 N  N     . LYS A 1 198 ? 5.317  17.258  10.211 1.00 21.15 ? 198 LYS A N     1 
ATOM   1619 C  CA    . LYS A 1 198 ? 6.624  17.166  9.573  1.00 22.18 ? 198 LYS A CA    1 
ATOM   1620 C  C     . LYS A 1 198 ? 7.227  18.551  9.318  1.00 21.03 ? 198 LYS A C     1 
ATOM   1621 O  O     . LYS A 1 198 ? 6.567  19.411  8.739  1.00 19.72 ? 198 LYS A O     1 
ATOM   1622 C  CB    . LYS A 1 198 ? 6.509  16.393  8.261  1.00 26.80 ? 198 LYS A CB    1 
ATOM   1623 C  CG    . LYS A 1 198 ? 6.155  14.924  8.454  1.00 30.15 ? 198 LYS A CG    1 
ATOM   1624 C  CD    . LYS A 1 198 ? 5.940  14.218  7.148  1.00 36.24 ? 198 LYS A CD    1 
ATOM   1625 C  CE    . LYS A 1 198 ? 5.586  12.759  7.342  1.00 43.96 ? 198 LYS A CE    1 
ATOM   1626 N  NZ    . LYS A 1 198 ? 5.365  12.084  6.042  1.00 49.68 ? 198 LYS A NZ    1 
ATOM   1627 N  N     . ILE A 1 199 ? 8.504  18.712  9.703  1.00 19.53 ? 199 ILE A N     1 
ATOM   1628 C  CA    . ILE A 1 199 ? 9.235  19.963  9.650  1.00 19.87 ? 199 ILE A CA    1 
ATOM   1629 C  C     . ILE A 1 199 ? 10.557 19.742  8.925  1.00 19.70 ? 199 ILE A C     1 
ATOM   1630 O  O     . ILE A 1 199 ? 11.365 18.890  9.331  1.00 19.04 ? 199 ILE A O     1 
ATOM   1631 C  CB    . ILE A 1 199 ? 9.505  20.491  11.066 1.00 20.12 ? 199 ILE A CB    1 
ATOM   1632 C  CG1   . ILE A 1 199 ? 8.196  20.710  11.834 1.00 20.66 ? 199 ILE A CG1   1 
ATOM   1633 C  CG2   . ILE A 1 199 ? 10.367 21.766  10.995 1.00 20.82 ? 199 ILE A CG2   1 
ATOM   1634 C  CD1   . ILE A 1 199 ? 7.348  21.871  11.290 1.00 22.25 ? 199 ILE A CD1   1 
ATOM   1635 N  N     . SER A 1 200 ? 10.771 20.495  7.842  1.00 20.20 ? 200 SER A N     1 
ATOM   1636 C  CA    . SER A 1 200 ? 12.084 20.573  7.221  1.00 20.81 ? 200 SER A CA    1 
ATOM   1637 C  C     . SER A 1 200 ? 12.847 21.796  7.731  1.00 20.54 ? 200 SER A C     1 
ATOM   1638 O  O     . SER A 1 200 ? 12.285 22.878  7.822  1.00 21.08 ? 200 SER A O     1 
ATOM   1639 C  CB    . SER A 1 200 ? 11.974 20.648  5.728  1.00 22.03 ? 200 SER A CB    1 
ATOM   1640 O  OG    . SER A 1 200 ? 13.263 20.905  5.156  1.00 22.96 ? 200 SER A OG    1 
ATOM   1641 N  N     . LEU A 1 201 ? 14.156 21.673  7.914  1.00 20.59 ? 201 LEU A N     1 
ATOM   1642 C  CA    . LEU A 1 201 ? 14.978 22.833  8.253  1.00 22.55 ? 201 LEU A CA    1 
ATOM   1643 C  C     . LEU A 1 201 ? 15.887 23.250  7.101  1.00 23.09 ? 201 LEU A C     1 
ATOM   1644 O  O     . LEU A 1 201 ? 16.665 24.186  7.268  1.00 25.68 ? 201 LEU A O     1 
ATOM   1645 C  CB    . LEU A 1 201 ? 15.828 22.531  9.487  1.00 21.70 ? 201 LEU A CB    1 
ATOM   1646 C  CG    . LEU A 1 201 ? 15.036 22.230  10.757 1.00 21.81 ? 201 LEU A CG    1 
ATOM   1647 C  CD1   . LEU A 1 201 ? 16.003 22.034  11.927 1.00 21.87 ? 201 LEU A CD1   1 
ATOM   1648 C  CD2   . LEU A 1 201 ? 14.024 23.322  11.056 1.00 22.47 ? 201 LEU A CD2   1 
ATOM   1649 N  N     . TYR A 1 202 ? 15.813 22.552  5.977  1.00 23.13 ? 202 TYR A N     1 
ATOM   1650 C  CA    . TYR A 1 202 ? 16.684 22.820  4.846  1.00 25.67 ? 202 TYR A CA    1 
ATOM   1651 C  C     . TYR A 1 202 ? 16.166 22.025  3.661  1.00 28.17 ? 202 TYR A C     1 
ATOM   1652 O  O     . TYR A 1 202 ? 15.633 20.946  3.850  1.00 26.79 ? 202 TYR A O     1 
ATOM   1653 C  CB    . TYR A 1 202 ? 18.105 22.369  5.191  1.00 24.72 ? 202 TYR A CB    1 
ATOM   1654 C  CG    . TYR A 1 202 ? 19.234 22.983  4.383  1.00 25.15 ? 202 TYR A CG    1 
ATOM   1655 C  CD1   . TYR A 1 202 ? 19.421 24.360  4.330  1.00 25.78 ? 202 TYR A CD1   1 
ATOM   1656 C  CD2   . TYR A 1 202 ? 20.160 22.179  3.723  1.00 25.34 ? 202 TYR A CD2   1 
ATOM   1657 C  CE1   . TYR A 1 202 ? 20.465 24.920  3.613  1.00 25.92 ? 202 TYR A CE1   1 
ATOM   1658 C  CE2   . TYR A 1 202 ? 21.205 22.735  2.992  1.00 25.27 ? 202 TYR A CE2   1 
ATOM   1659 C  CZ    . TYR A 1 202 ? 21.374 24.098  2.967  1.00 25.44 ? 202 TYR A CZ    1 
ATOM   1660 O  OH    . TYR A 1 202 ? 22.438 24.636  2.296  1.00 27.91 ? 202 TYR A OH    1 
ATOM   1661 N  N     . ARG A 1 203 ? 16.360 22.509  2.429  1.00 34.77 ? 203 ARG A N     1 
ATOM   1662 C  CA    . ARG A 1 203 ? 15.804 21.741  1.327  1.00 39.64 ? 203 ARG A CA    1 
ATOM   1663 C  C     . ARG A 1 203 ? 16.866 20.876  0.673  1.00 36.54 ? 203 ARG A C     1 
ATOM   1664 O  O     . ARG A 1 203 ? 16.781 20.579  -0.520 1.00 33.94 ? 203 ARG A O     1 
ATOM   1665 C  CB    . ARG A 1 203 ? 15.117 22.612  0.277  1.00 52.66 ? 203 ARG A CB    1 
ATOM   1666 C  CG    . ARG A 1 203 ? 14.238 21.829  -0.695 1.00 61.68 ? 203 ARG A CG    1 
ATOM   1667 C  CD    . ARG A 1 203 ? 13.550 20.602  -0.107 1.00 69.18 ? 203 ARG A CD    1 
ATOM   1668 N  NE    . ARG A 1 203 ? 14.176 19.438  -0.692 1.00 73.22 ? 203 ARG A NE    1 
ATOM   1669 C  CZ    . ARG A 1 203 ? 14.026 19.109  -1.965 1.00 60.16 ? 203 ARG A CZ    1 
ATOM   1670 N  NH1   . ARG A 1 203 ? 15.045 18.547  -2.592 1.00 63.66 ? 203 ARG A NH1   1 
ATOM   1671 N  NH2   . ARG A 1 203 ? 12.930 19.465  -2.623 1.00 49.58 ? 203 ARG A NH2   1 
ATOM   1672 N  N     . GLU A 1 204 ? 17.845 20.464  1.481  1.00 31.49 ? 204 GLU A N     1 
ATOM   1673 C  CA    . GLU A 1 204 ? 18.702 19.347  1.124  1.00 31.40 ? 204 GLU A CA    1 
ATOM   1674 C  C     . GLU A 1 204 ? 18.710 18.399  2.315  1.00 29.31 ? 204 GLU A C     1 
ATOM   1675 O  O     . GLU A 1 204 ? 18.457 18.810  3.446  1.00 27.20 ? 204 GLU A O     1 
ATOM   1676 C  CB    . GLU A 1 204 ? 20.117 19.812  0.772  1.00 30.86 ? 204 GLU A CB    1 
ATOM   1677 C  CG    . GLU A 1 204 ? 20.194 20.821  -0.361 1.00 34.93 ? 204 GLU A CG    1 
ATOM   1678 C  CD    . GLU A 1 204 ? 19.744 20.282  -1.713 1.00 36.94 ? 204 GLU A CD    1 
ATOM   1679 O  OE1   . GLU A 1 204 ? 19.455 19.072  -1.776 1.00 37.85 ? 204 GLU A OE1   1 
ATOM   1680 O  OE2   . GLU A 1 204 ? 19.668 21.068  -2.699 1.00 38.39 ? 204 GLU A OE2   1 
ATOM   1681 N  N     . PRO A 1 205 ? 18.972 17.104  2.100  1.00 29.35 ? 205 PRO A N     1 
ATOM   1682 C  CA    . PRO A 1 205 ? 19.132 16.171  3.202  1.00 27.88 ? 205 PRO A CA    1 
ATOM   1683 C  C     . PRO A 1 205 ? 20.302 16.577  4.102  1.00 26.36 ? 205 PRO A C     1 
ATOM   1684 O  O     . PRO A 1 205 ? 21.306 17.078  3.614  1.00 25.39 ? 205 PRO A O     1 
ATOM   1685 C  CB    . PRO A 1 205 ? 19.399 14.825  2.539  1.00 29.35 ? 205 PRO A CB    1 
ATOM   1686 C  CG    . PRO A 1 205 ? 19.800 15.174  1.128  1.00 32.78 ? 205 PRO A CG    1 
ATOM   1687 C  CD    . PRO A 1 205 ? 19.090 16.465  0.781  1.00 32.34 ? 205 PRO A CD    1 
ATOM   1688 N  N     . LEU A 1 206 ? 20.084 16.463  5.416  1.00 24.84 ? 206 LEU A N     1 
ATOM   1689 C  CA    . LEU A 1 206 ? 21.131 16.666  6.412  1.00 23.92 ? 206 LEU A CA    1 
ATOM   1690 C  C     . LEU A 1 206 ? 21.231 15.415  7.287  1.00 22.02 ? 206 LEU A C     1 
ATOM   1691 O  O     . LEU A 1 206 ? 20.301 14.609  7.392  1.00 20.61 ? 206 LEU A O     1 
ATOM   1692 C  CB    . LEU A 1 206 ? 20.756 17.884  7.258  1.00 24.69 ? 206 LEU A CB    1 
ATOM   1693 C  CG    . LEU A 1 206 ? 20.666 19.206  6.495  1.00 25.48 ? 206 LEU A CG    1 
ATOM   1694 C  CD1   . LEU A 1 206 ? 20.115 20.284  7.398  1.00 26.00 ? 206 LEU A CD1   1 
ATOM   1695 C  CD2   . LEU A 1 206 ? 22.009 19.595  5.919  1.00 25.94 ? 206 LEU A CD2   1 
ATOM   1696 N  N     . MET A 1 207 ? 22.382 15.268  7.940  1.00 21.13 ? 207 MET A N     1 
ATOM   1697 C  CA    . MET A 1 207 ? 22.609 14.170  8.859  1.00 19.87 ? 207 MET A CA    1 
ATOM   1698 C  C     . MET A 1 207 ? 21.840 14.446  10.135 1.00 18.47 ? 207 MET A C     1 
ATOM   1699 O  O     . MET A 1 207 ? 21.551 15.598  10.440 1.00 16.69 ? 207 MET A O     1 
ATOM   1700 C  CB    . MET A 1 207 ? 24.107 14.063  9.138  1.00 22.53 ? 207 MET A CB    1 
ATOM   1701 C  CG    . MET A 1 207 ? 24.877 13.892  7.818  1.00 25.98 ? 207 MET A CG    1 
ATOM   1702 S  SD    . MET A 1 207 ? 24.825 12.190  7.202  1.00 34.42 ? 207 MET A SD    1 
ATOM   1703 C  CE    . MET A 1 207 ? 23.114 11.738  6.979  1.00 33.21 ? 207 MET A CE    1 
ATOM   1704 N  N     . ALA A 1 208 ? 21.545 13.373  10.861 1.00 17.07 ? 208 ALA A N     1 
ATOM   1705 C  CA    . ALA A 1 208 ? 20.741 13.415  12.071 1.00 16.87 ? 208 ALA A CA    1 
ATOM   1706 C  C     . ALA A 1 208 ? 21.348 14.358  13.113 1.00 16.81 ? 208 ALA A C     1 
ATOM   1707 O  O     . ALA A 1 208 ? 20.620 15.090  13.785 1.00 17.15 ? 208 ALA A O     1 
ATOM   1708 C  CB    . ALA A 1 208 ? 20.576 12.013  12.594 1.00 16.78 ? 208 ALA A CB    1 
ATOM   1709 N  N     . TRP A 1 209 ? 22.677 14.378  13.227 1.00 16.84 ? 209 TRP A N     1 
ATOM   1710 C  CA    . TRP A 1 209 ? 23.326 15.141  14.281 1.00 16.56 ? 209 TRP A CA    1 
ATOM   1711 C  C     . TRP A 1 209 ? 23.216 16.629  13.970 1.00 16.54 ? 209 TRP A C     1 
ATOM   1712 O  O     . TRP A 1 209 ? 23.082 17.421  14.890 1.00 15.76 ? 209 TRP A O     1 
ATOM   1713 C  CB    . TRP A 1 209 ? 24.776 14.703  14.519 1.00 17.97 ? 209 TRP A CB    1 
ATOM   1714 C  CG    . TRP A 1 209 ? 25.690 14.720  13.322 1.00 18.64 ? 209 TRP A CG    1 
ATOM   1715 C  CD1   . TRP A 1 209 ? 26.431 15.728  12.779 1.00 20.23 ? 209 TRP A CD1   1 
ATOM   1716 C  CD2   . TRP A 1 209 ? 25.972 13.564  12.539 1.00 20.92 ? 209 TRP A CD2   1 
ATOM   1717 N  NE1   . TRP A 1 209 ? 27.118 15.279  11.682 1.00 19.97 ? 209 TRP A NE1   1 
ATOM   1718 C  CE2   . TRP A 1 209 ? 26.851 13.950  11.516 1.00 21.77 ? 209 TRP A CE2   1 
ATOM   1719 C  CE3   . TRP A 1 209 ? 25.534 12.245  12.611 1.00 24.80 ? 209 TRP A CE3   1 
ATOM   1720 C  CZ2   . TRP A 1 209 ? 27.320 13.047  10.571 1.00 25.16 ? 209 TRP A CZ2   1 
ATOM   1721 C  CZ3   . TRP A 1 209 ? 25.969 11.367  11.653 1.00 27.87 ? 209 TRP A CZ3   1 
ATOM   1722 C  CH2   . TRP A 1 209 ? 26.852 11.765  10.651 1.00 26.87 ? 209 TRP A CH2   1 
ATOM   1723 N  N     . THR A 1 210 ? 23.228 16.982  12.674 1.00 15.67 ? 210 THR A N     1 
ATOM   1724 C  CA    . THR A 1 210 ? 23.080 18.361  12.243 1.00 16.88 ? 210 THR A CA    1 
ATOM   1725 C  C     . THR A 1 210 ? 21.681 18.828  12.608 1.00 17.07 ? 210 THR A C     1 
ATOM   1726 O  O     . THR A 1 210 ? 21.492 19.913  13.151 1.00 18.72 ? 210 THR A O     1 
ATOM   1727 C  CB    . THR A 1 210 ? 23.298 18.484  10.731 1.00 17.27 ? 210 THR A CB    1 
ATOM   1728 O  OG1   . THR A 1 210 ? 24.545 17.909  10.384 1.00 17.63 ? 210 THR A OG1   1 
ATOM   1729 C  CG2   . THR A 1 210 ? 23.250 19.902  10.219 1.00 18.60 ? 210 THR A CG2   1 
ATOM   1730 N  N     . ILE A 1 211 ? 20.675 17.986  12.322 1.00 16.75 ? 211 ILE A N     1 
ATOM   1731 C  CA    . ILE A 1 211 ? 19.311 18.334  12.702 1.00 16.94 ? 211 ILE A CA    1 
ATOM   1732 C  C     . ILE A 1 211 ? 19.182 18.461  14.214 1.00 16.77 ? 211 ILE A C     1 
ATOM   1733 O  O     . ILE A 1 211 ? 18.551 19.410  14.733 1.00 16.64 ? 211 ILE A O     1 
ATOM   1734 C  CB    . ILE A 1 211 ? 18.320 17.309  12.129 1.00 17.31 ? 211 ILE A CB    1 
ATOM   1735 C  CG1   . ILE A 1 211 ? 18.318 17.370  10.601 1.00 18.14 ? 211 ILE A CG1   1 
ATOM   1736 C  CG2   . ILE A 1 211 ? 16.942 17.519  12.752 1.00 18.48 ? 211 ILE A CG2   1 
ATOM   1737 C  CD1   . ILE A 1 211 ? 18.019 18.726  10.056 1.00 18.80 ? 211 ILE A CD1   1 
ATOM   1738 N  N     . VAL A 1 212 ? 19.791 17.528  14.939 1.00 16.63 ? 212 VAL A N     1 
ATOM   1739 C  CA    . VAL A 1 212 ? 19.809 17.616  16.399 1.00 16.51 ? 212 VAL A CA    1 
ATOM   1740 C  C     . VAL A 1 212 ? 20.353 18.977  16.844 1.00 17.81 ? 212 VAL A C     1 
ATOM   1741 O  O     . VAL A 1 212 ? 19.723 19.655  17.649 1.00 18.21 ? 212 VAL A O     1 
ATOM   1742 C  CB    . VAL A 1 212 ? 20.580 16.433  17.005 1.00 16.95 ? 212 VAL A CB    1 
ATOM   1743 C  CG1   . VAL A 1 212 ? 20.910 16.628  18.468 1.00 16.69 ? 212 VAL A CG1   1 
ATOM   1744 C  CG2   . VAL A 1 212 ? 19.834 15.124  16.821 1.00 16.76 ? 212 VAL A CG2   1 
ATOM   1745 N  N     . ASN A 1 213 ? 21.510 19.401  16.310 1.00 18.58 ? 213 ASN A N     1 
ATOM   1746 C  CA    . ASN A 1 213 ? 22.108 20.675  16.694 1.00 20.35 ? 213 ASN A CA    1 
ATOM   1747 C  C     . ASN A 1 213 ? 21.213 21.875  16.387 1.00 19.93 ? 213 ASN A C     1 
ATOM   1748 O  O     . ASN A 1 213 ? 21.117 22.808  17.195 1.00 21.30 ? 213 ASN A O     1 
ATOM   1749 C  CB    . ASN A 1 213 ? 23.456 20.899  15.999 1.00 20.73 ? 213 ASN A CB    1 
ATOM   1750 C  CG    . ASN A 1 213 ? 24.478 19.836  16.351 1.00 22.27 ? 213 ASN A CG    1 
ATOM   1751 O  OD1   . ASN A 1 213 ? 24.420 19.209  17.423 1.00 23.42 ? 213 ASN A OD1   1 
ATOM   1752 N  ND2   . ASN A 1 213 ? 25.418 19.647  15.439 1.00 22.24 ? 213 ASN A ND2   1 
ATOM   1753 N  N     . GLU A 1 214 ? 20.647 21.920  15.177 1.00 19.41 ? 214 GLU A N     1 
ATOM   1754 C  CA    . GLU A 1 214 ? 19.758 23.001  14.794 1.00 19.88 ? 214 GLU A CA    1 
ATOM   1755 C  C     . GLU A 1 214 ? 18.556 23.111  15.744 1.00 19.77 ? 214 GLU A C     1 
ATOM   1756 O  O     . GLU A 1 214 ? 18.164 24.216  16.125 1.00 19.06 ? 214 GLU A O     1 
ATOM   1757 C  CB    . GLU A 1 214 ? 19.289 22.851  13.345 1.00 21.16 ? 214 GLU A CB    1 
ATOM   1758 C  CG    . GLU A 1 214 ? 20.387 22.972  12.307 1.00 20.88 ? 214 GLU A CG    1 
ATOM   1759 C  CD    . GLU A 1 214 ? 20.938 24.365  12.035 1.00 23.63 ? 214 GLU A CD    1 
ATOM   1760 O  OE1   . GLU A 1 214 ? 21.973 24.483  11.363 1.00 23.99 ? 214 GLU A OE1   1 
ATOM   1761 O  OE2   . GLU A 1 214 ? 20.323 25.321  12.471 1.00 24.64 ? 214 GLU A OE2   1 
ATOM   1762 N  N     . VAL A 1 215 ? 17.929 21.984  16.092 1.00 18.77 ? 215 VAL A N     1 
ATOM   1763 C  CA    . VAL A 1 215 ? 16.762 21.979  16.951 1.00 19.04 ? 215 VAL A CA    1 
ATOM   1764 C  C     . VAL A 1 215 ? 17.150 22.422  18.373 1.00 19.82 ? 215 VAL A C     1 
ATOM   1765 O  O     . VAL A 1 215 ? 16.506 23.283  18.968 1.00 19.53 ? 215 VAL A O     1 
ATOM   1766 C  CB    . VAL A 1 215 ? 16.114 20.578  16.988 1.00 19.01 ? 215 VAL A CB    1 
ATOM   1767 C  CG1   . VAL A 1 215 ? 15.043 20.482  18.051 1.00 19.88 ? 215 VAL A CG1   1 
ATOM   1768 C  CG2   . VAL A 1 215 ? 15.530 20.169  15.650 1.00 18.89 ? 215 VAL A CG2   1 
ATOM   1769 N  N     . ILE A 1 216 ? 18.207 21.816  18.923 1.00 19.41 ? 216 ILE A N     1 
ATOM   1770 C  CA    . ILE A 1 216 ? 18.568 22.055  20.314 1.00 21.55 ? 216 ILE A CA    1 
ATOM   1771 C  C     . ILE A 1 216 ? 19.005 23.499  20.492 1.00 22.61 ? 216 ILE A C     1 
ATOM   1772 O  O     . ILE A 1 216 ? 18.547 24.157  21.419 1.00 23.63 ? 216 ILE A O     1 
ATOM   1773 C  CB    . ILE A 1 216 ? 19.641 21.050  20.771 1.00 21.85 ? 216 ILE A CB    1 
ATOM   1774 C  CG1   . ILE A 1 216 ? 19.006 19.680  20.978 1.00 20.88 ? 216 ILE A CG1   1 
ATOM   1775 C  CG2   . ILE A 1 216 ? 20.383 21.524  22.011 1.00 22.68 ? 216 ILE A CG2   1 
ATOM   1776 C  CD1   . ILE A 1 216 ? 19.990 18.592  21.353 1.00 20.38 ? 216 ILE A CD1   1 
ATOM   1777 N  N     . VAL A 1 217 ? 19.849 23.998  19.580 1.00 22.91 ? 217 VAL A N     1 
ATOM   1778 C  CA    . VAL A 1 217 ? 20.407 25.337  19.706 1.00 23.23 ? 217 VAL A CA    1 
ATOM   1779 C  C     . VAL A 1 217 ? 19.321 26.392  19.520 1.00 25.14 ? 217 VAL A C     1 
ATOM   1780 O  O     . VAL A 1 217 ? 19.342 27.389  20.248 1.00 26.40 ? 217 VAL A O     1 
ATOM   1781 C  CB    . VAL A 1 217 ? 21.611 25.606  18.776 1.00 24.15 ? 217 VAL A CB    1 
ATOM   1782 C  CG1   . VAL A 1 217 ? 21.966 27.081  18.737 1.00 26.11 ? 217 VAL A CG1   1 
ATOM   1783 C  CG2   . VAL A 1 217 ? 22.820 24.786  19.163 1.00 24.01 ? 217 VAL A CG2   1 
ATOM   1784 N  N     . SER A 1 218 ? 18.434 26.195  18.526 1.00 26.16 ? 218 SER A N     1 
ATOM   1785 C  CA    . SER A 1 218 ? 17.340 27.121  18.251 1.00 28.26 ? 218 SER A CA    1 
ATOM   1786 C  C     . SER A 1 218 ? 16.376 27.235  19.435 1.00 27.15 ? 218 SER A C     1 
ATOM   1787 O  O     . SER A 1 218 ? 15.891 28.341  19.747 1.00 27.26 ? 218 SER A O     1 
ATOM   1788 C  CB    . SER A 1 218 ? 16.605 26.765  16.957 1.00 29.37 ? 218 SER A CB    1 
ATOM   1789 O  OG    . SER A 1 218 ? 15.694 25.690  17.168 1.00 35.89 ? 218 SER A OG    1 
ATOM   1790 N  N     . TYR A 1 219 ? 16.092 26.092  20.063 1.00 24.94 ? 219 TYR A N     1 
ATOM   1791 C  CA    . TYR A 1 219 ? 15.237 26.024  21.229 1.00 24.98 ? 219 TYR A CA    1 
ATOM   1792 C  C     . TYR A 1 219 ? 15.909 26.704  22.420 1.00 25.48 ? 219 TYR A C     1 
ATOM   1793 O  O     . TYR A 1 219 ? 15.279 27.485  23.135 1.00 25.52 ? 219 TYR A O     1 
ATOM   1794 C  CB    . TYR A 1 219 ? 14.904 24.573  21.554 1.00 24.12 ? 219 TYR A CB    1 
ATOM   1795 C  CG    . TYR A 1 219 ? 13.896 24.341  22.672 1.00 24.04 ? 219 TYR A CG    1 
ATOM   1796 C  CD1   . TYR A 1 219 ? 12.609 24.884  22.609 1.00 24.87 ? 219 TYR A CD1   1 
ATOM   1797 C  CD2   . TYR A 1 219 ? 14.190 23.519  23.749 1.00 23.49 ? 219 TYR A CD2   1 
ATOM   1798 C  CE1   . TYR A 1 219 ? 11.658 24.629  23.589 1.00 25.20 ? 219 TYR A CE1   1 
ATOM   1799 C  CE2   . TYR A 1 219 ? 13.252 23.258  24.741 1.00 24.40 ? 219 TYR A CE2   1 
ATOM   1800 C  CZ    . TYR A 1 219 ? 11.973 23.785  24.645 1.00 25.40 ? 219 TYR A CZ    1 
ATOM   1801 O  OH    . TYR A 1 219 ? 11.076 23.559  25.642 1.00 25.58 ? 219 TYR A OH    1 
ATOM   1802 N  N     . GLU A 1 220 ? 17.184 26.406  22.620 1.00 25.08 ? 220 GLU A N     1 
ATOM   1803 C  CA    . GLU A 1 220 ? 17.954 26.984  23.710 1.00 27.19 ? 220 GLU A CA    1 
ATOM   1804 C  C     . GLU A 1 220 ? 17.749 28.489  23.772 1.00 29.54 ? 220 GLU A C     1 
ATOM   1805 O  O     . GLU A 1 220 ? 17.569 29.078  24.828 1.00 33.14 ? 220 GLU A O     1 
ATOM   1806 C  CB    . GLU A 1 220 ? 19.454 26.790  23.480 1.00 26.16 ? 220 GLU A CB    1 
ATOM   1807 C  CG    . GLU A 1 220 ? 19.975 25.464  23.942 1.00 24.85 ? 220 GLU A CG    1 
ATOM   1808 C  CD    . GLU A 1 220 ? 21.466 25.262  23.682 1.00 24.15 ? 220 GLU A CD    1 
ATOM   1809 O  OE1   . GLU A 1 220 ? 21.935 24.137  23.890 1.00 21.63 ? 220 GLU A OE1   1 
ATOM   1810 O  OE2   . GLU A 1 220 ? 22.142 26.234  23.228 1.00 24.11 ? 220 GLU A OE2   1 
ATOM   1811 N  N     . TRP A 1 221 ? 17.811 29.128  22.623 1.00 31.54 ? 221 TRP A N     1 
ATOM   1812 C  CA    . TRP A 1 221 ? 17.880 30.569  22.628 1.00 37.26 ? 221 TRP A CA    1 
ATOM   1813 C  C     . TRP A 1 221 ? 16.513 31.195  22.862 1.00 38.17 ? 221 TRP A C     1 
ATOM   1814 O  O     . TRP A 1 221 ? 16.425 32.400  23.121 1.00 39.42 ? 221 TRP A O     1 
ATOM   1815 C  CB    . TRP A 1 221 ? 18.560 31.010  21.336 1.00 40.38 ? 221 TRP A CB    1 
ATOM   1816 C  CG    . TRP A 1 221 ? 19.947 30.418  21.251 1.00 45.38 ? 221 TRP A CG    1 
ATOM   1817 C  CD1   . TRP A 1 221 ? 20.671 29.734  22.201 1.00 48.40 ? 221 TRP A CD1   1 
ATOM   1818 C  CD2   . TRP A 1 221 ? 20.776 30.459  20.078 1.00 45.94 ? 221 TRP A CD2   1 
ATOM   1819 N  NE1   . TRP A 1 221 ? 21.901 29.349  21.716 1.00 43.95 ? 221 TRP A NE1   1 
ATOM   1820 C  CE2   . TRP A 1 221 ? 21.979 29.787  20.408 1.00 52.26 ? 221 TRP A CE2   1 
ATOM   1821 C  CE3   . TRP A 1 221 ? 20.591 30.999  18.801 1.00 49.27 ? 221 TRP A CE3   1 
ATOM   1822 C  CZ2   . TRP A 1 221 ? 23.000 29.662  19.468 1.00 57.71 ? 221 TRP A CZ2   1 
ATOM   1823 C  CZ3   . TRP A 1 221 ? 21.594 30.857  17.879 1.00 52.24 ? 221 TRP A CZ3   1 
ATOM   1824 C  CH2   . TRP A 1 221 ? 22.777 30.197  18.217 1.00 58.18 ? 221 TRP A CH2   1 
ATOM   1825 N  N     . GLU A 1 222 ? 15.475 30.349  22.887 1.00 35.83 ? 222 GLU A N     1 
ATOM   1826 C  CA    . GLU A 1 222 ? 14.144 30.793  23.252 1.00 38.43 ? 222 GLU A CA    1 
ATOM   1827 C  C     . GLU A 1 222 ? 13.806 30.397  24.681 1.00 38.68 ? 222 GLU A C     1 
ATOM   1828 O  O     . GLU A 1 222 ? 13.176 31.166  25.393 1.00 38.47 ? 222 GLU A O     1 
ATOM   1829 C  CB    . GLU A 1 222 ? 13.104 30.218  22.297 1.00 38.32 ? 222 GLU A CB    1 
ATOM   1830 C  CG    . GLU A 1 222 ? 13.247 30.784  20.908 1.00 40.18 ? 222 GLU A CG    1 
ATOM   1831 C  CD    . GLU A 1 222 ? 13.099 32.296  20.840 1.00 44.12 ? 222 GLU A CD    1 
ATOM   1832 O  OE1   . GLU A 1 222 ? 12.196 32.826  21.508 1.00 41.68 ? 222 GLU A OE1   1 
ATOM   1833 O  OE2   . GLU A 1 222 ? 13.886 32.932  20.078 1.00 51.29 ? 222 GLU A OE2   1 
ATOM   1834 N  N     . VAL A 1 223 ? 14.154 29.183  25.086 1.00 36.11 ? 223 VAL A N     1 
ATOM   1835 C  CA    . VAL A 1 223 ? 13.530 28.623  26.269 1.00 38.06 ? 223 VAL A CA    1 
ATOM   1836 C  C     . VAL A 1 223 ? 14.310 28.996  27.530 1.00 39.30 ? 223 VAL A C     1 
ATOM   1837 O  O     . VAL A 1 223 ? 13.754 29.002  28.621 1.00 42.55 ? 223 VAL A O     1 
ATOM   1838 C  CB    . VAL A 1 223 ? 13.375 27.096  26.137 1.00 36.20 ? 223 VAL A CB    1 
ATOM   1839 C  CG1   . VAL A 1 223 ? 14.712 26.380  26.264 1.00 32.74 ? 223 VAL A CG1   1 
ATOM   1840 C  CG2   . VAL A 1 223 ? 12.364 26.571  27.158 1.00 38.22 ? 223 VAL A CG2   1 
ATOM   1841 N  N     . ILE A 1 224 ? 15.611 29.233  27.379 1.00 42.04 ? 224 ILE A N     1 
ATOM   1842 C  CA    . ILE A 1 224 ? 16.488 29.598  28.474 1.00 45.27 ? 224 ILE A CA    1 
ATOM   1843 C  C     . ILE A 1 224 ? 16.427 31.120  28.609 1.00 50.92 ? 224 ILE A C     1 
ATOM   1844 O  O     . ILE A 1 224 ? 16.999 31.853  27.801 1.00 49.23 ? 224 ILE A O     1 
ATOM   1845 C  CB    . ILE A 1 224 ? 17.926 29.087  28.213 1.00 43.61 ? 224 ILE A CB    1 
ATOM   1846 C  CG1   . ILE A 1 224 ? 17.978 27.579  27.949 1.00 39.75 ? 224 ILE A CG1   1 
ATOM   1847 C  CG2   . ILE A 1 224 ? 18.852 29.489  29.357 1.00 45.80 ? 224 ILE A CG2   1 
ATOM   1848 C  CD1   . ILE A 1 224 ? 19.364 27.070  27.607 1.00 40.97 ? 224 ILE A CD1   1 
ATOM   1849 N  N     . LYS A 1 225 ? 15.723 31.595  29.640 1.00 62.40 ? 225 LYS A N     1 
ATOM   1850 C  CA    . LYS A 1 225 ? 15.387 33.010  29.750 1.00 68.09 ? 225 LYS A CA    1 
ATOM   1851 C  C     . LYS A 1 225 ? 16.645 33.867  29.869 1.00 67.97 ? 225 LYS A C     1 
ATOM   1852 O  O     . LYS A 1 225 ? 16.641 35.017  29.428 1.00 73.03 ? 225 LYS A O     1 
ATOM   1853 C  CB    . LYS A 1 225 ? 14.438 33.267  30.927 1.00 78.47 ? 225 LYS A CB    1 
ATOM   1854 C  CG    . LYS A 1 225 ? 12.973 33.480  30.553 1.00 85.16 ? 225 LYS A CG    1 
ATOM   1855 C  CD    . LYS A 1 225 ? 12.364 32.379  29.699 1.00 87.14 ? 225 LYS A CD    1 
ATOM   1856 C  CE    . LYS A 1 225 ? 10.849 32.350  29.766 1.00 91.06 ? 225 LYS A CE    1 
ATOM   1857 N  NZ    . LYS A 1 225 ? 10.226 33.500  29.068 1.00 95.64 ? 225 LYS A NZ    1 
ATOM   1858 N  N     . LYS A 1 226 ? 17.723 33.308  30.437 1.00 64.77 ? 226 LYS A N     1 
ATOM   1859 C  CA    . LYS A 1 226 ? 18.972 34.045  30.562 1.00 64.84 ? 226 LYS A CA    1 
ATOM   1860 C  C     . LYS A 1 226 ? 19.687 34.184  29.212 1.00 63.18 ? 226 LYS A C     1 
ATOM   1861 O  O     . LYS A 1 226 ? 20.736 34.831  29.167 1.00 58.91 ? 226 LYS A O     1 
ATOM   1862 C  CB    . LYS A 1 226 ? 19.886 33.392  31.605 1.00 64.97 ? 226 LYS A CB    1 
ATOM   1863 C  CG    . LYS A 1 226 ? 20.499 32.061  31.198 1.00 63.52 ? 226 LYS A CG    1 
ATOM   1864 C  CD    . LYS A 1 226 ? 21.431 31.500  32.233 1.00 63.93 ? 226 LYS A CD    1 
ATOM   1865 C  CE    . LYS A 1 226 ? 22.211 30.296  31.751 1.00 62.54 ? 226 LYS A CE    1 
ATOM   1866 N  NZ    . LYS A 1 226 ? 23.354 30.003  32.659 1.00 61.60 ? 226 LYS A NZ    1 
ATOM   1867 N  N     . PHE A 1 227 ? 19.140 33.571  28.138 1.00 58.73 ? 227 PHE A N     1 
ATOM   1868 C  CA    . PHE A 1 227 ? 19.569 33.845  26.769 1.00 55.67 ? 227 PHE A CA    1 
ATOM   1869 C  C     . PHE A 1 227 ? 18.568 34.788  26.089 1.00 57.42 ? 227 PHE A C     1 
ATOM   1870 O  O     . PHE A 1 227 ? 17.609 35.188  26.783 1.00 65.11 ? 227 PHE A O     1 
ATOM   1871 C  CB    . PHE A 1 227 ? 19.729 32.553  25.962 1.00 51.44 ? 227 PHE A CB    1 
ATOM   1872 C  CG    . PHE A 1 227 ? 20.913 31.678  26.319 1.00 47.97 ? 227 PHE A CG    1 
ATOM   1873 C  CD1   . PHE A 1 227 ? 21.819 32.018  27.322 1.00 50.39 ? 227 PHE A CD1   1 
ATOM   1874 C  CD2   . PHE A 1 227 ? 21.140 30.504  25.618 1.00 44.88 ? 227 PHE A CD2   1 
ATOM   1875 C  CE1   . PHE A 1 227 ? 22.910 31.206  27.618 1.00 47.55 ? 227 PHE A CE1   1 
ATOM   1876 C  CE2   . PHE A 1 227 ? 22.228 29.691  25.909 1.00 43.29 ? 227 PHE A CE2   1 
ATOM   1877 C  CZ    . PHE A 1 227 ? 23.109 30.039  26.912 1.00 44.95 ? 227 PHE A CZ    1 
HETATM 1878 CL CL    . CL  B 2 .   ? 18.171 -5.779  18.439 1.00 25.31 ? 301 CL  A CL    1 
HETATM 1879 O  "O5'" . ADN C 3 .   ? 18.918 12.179  8.043  1.00 25.36 ? 302 ADN A "O5'" 1 
HETATM 1880 C  "C5'" . ADN C 3 .   ? 18.519 11.555  9.250  1.00 23.34 ? 302 ADN A "C5'" 1 
HETATM 1881 C  "C4'" . ADN C 3 .   ? 17.278 12.194  9.789  1.00 21.71 ? 302 ADN A "C4'" 1 
HETATM 1882 O  "O4'" . ADN C 3 .   ? 17.495 13.613  9.867  1.00 21.16 ? 302 ADN A "O4'" 1 
HETATM 1883 C  "C3'" . ADN C 3 .   ? 16.015 12.096  8.925  1.00 21.10 ? 302 ADN A "C3'" 1 
HETATM 1884 O  "O3'" . ADN C 3 .   ? 15.399 10.847  9.137  1.00 24.13 ? 302 ADN A "O3'" 1 
HETATM 1885 C  "C2'" . ADN C 3 .   ? 15.191 13.248  9.483  1.00 20.22 ? 302 ADN A "C2'" 1 
HETATM 1886 O  "O2'" . ADN C 3 .   ? 14.598 12.986  10.754 1.00 20.34 ? 302 ADN A "O2'" 1 
HETATM 1887 C  "C1'" . ADN C 3 .   ? 16.290 14.300  9.590  1.00 21.37 ? 302 ADN A "C1'" 1 
HETATM 1888 N  N9    . ADN C 3 .   ? 16.505 15.153  8.429  1.00 19.11 ? 302 ADN A N9    1 
HETATM 1889 C  C8    . ADN C 3 .   ? 17.330 14.946  7.340  1.00 18.61 ? 302 ADN A C8    1 
HETATM 1890 N  N7    . ADN C 3 .   ? 17.377 15.973  6.525  1.00 17.91 ? 302 ADN A N7    1 
HETATM 1891 C  C5    . ADN C 3 .   ? 16.457 16.875  7.060  1.00 17.48 ? 302 ADN A C5    1 
HETATM 1892 C  C6    . ADN C 3 .   ? 16.040 18.156  6.660  1.00 20.00 ? 302 ADN A C6    1 
HETATM 1893 N  N6    . ADN C 3 .   ? 16.488 18.788  5.576  1.00 20.52 ? 302 ADN A N6    1 
HETATM 1894 N  N1    . ADN C 3 .   ? 15.155 18.806  7.459  1.00 20.40 ? 302 ADN A N1    1 
HETATM 1895 C  C2    . ADN C 3 .   ? 14.709 18.184  8.564  1.00 20.99 ? 302 ADN A C2    1 
HETATM 1896 N  N3    . ADN C 3 .   ? 15.025 16.982  9.038  1.00 18.79 ? 302 ADN A N3    1 
HETATM 1897 C  C4    . ADN C 3 .   ? 15.927 16.386  8.239  1.00 17.32 ? 302 ADN A C4    1 
HETATM 1898 S  S     . SO4 D 4 .   ? 9.331  27.601  31.985 1.00 58.22 ? 303 SO4 A S     1 
HETATM 1899 O  O1    . SO4 D 4 .   ? 10.321 27.819  32.998 1.00 61.72 ? 303 SO4 A O1    1 
HETATM 1900 O  O2    . SO4 D 4 .   ? 8.195  28.436  32.228 1.00 61.28 ? 303 SO4 A O2    1 
HETATM 1901 O  O3    . SO4 D 4 .   ? 9.874  27.913  30.691 1.00 67.05 ? 303 SO4 A O3    1 
HETATM 1902 O  O4    . SO4 D 4 .   ? 8.924  26.226  32.014 1.00 54.70 ? 303 SO4 A O4    1 
HETATM 1903 S  S     . SO3 E 5 .   ? 30.177 -13.490 25.294 1.00 73.16 ? 304 SO3 A S     1 
HETATM 1904 O  O1    . SO3 E 5 .   ? 30.266 -12.105 24.765 1.00 54.83 ? 304 SO3 A O1    1 
HETATM 1905 O  O2    . SO3 E 5 .   ? 29.248 -13.404 26.477 1.00 68.89 ? 304 SO3 A O2    1 
HETATM 1906 O  O3    . SO3 E 5 .   ? 31.530 -13.746 25.897 1.00 74.40 ? 304 SO3 A O3    1 
HETATM 1907 S  S     . SO3 F 5 .   ? 35.717 7.982   27.337 1.00 48.57 ? 305 SO3 A S     1 
HETATM 1908 O  O1    . SO3 F 5 .   ? 36.930 8.681   26.811 1.00 69.60 ? 305 SO3 A O1    1 
HETATM 1909 O  O2    . SO3 F 5 .   ? 34.762 9.112   27.587 1.00 36.53 ? 305 SO3 A O2    1 
HETATM 1910 O  O3    . SO3 F 5 .   ? 35.228 7.222   26.164 1.00 40.52 ? 305 SO3 A O3    1 
HETATM 1911 C  C1    . EDO G 6 .   ? 2.071  0.026   18.235 1.00 45.39 ? 306 EDO A C1    1 
HETATM 1912 O  O1    . EDO G 6 .   ? 2.404  0.885   19.315 1.00 32.77 ? 306 EDO A O1    1 
HETATM 1913 C  C2    . EDO G 6 .   ? 2.721  0.437   16.963 1.00 50.69 ? 306 EDO A C2    1 
HETATM 1914 O  O2    . EDO G 6 .   ? 2.128  1.565   16.359 1.00 59.84 ? 306 EDO A O2    1 
HETATM 1915 C  C1    . EDO H 6 .   ? 13.960 10.016  30.388 1.00 40.79 ? 307 EDO A C1    1 
HETATM 1916 O  O1    . EDO H 6 .   ? 14.885 9.838   31.454 1.00 49.59 ? 307 EDO A O1    1 
HETATM 1917 C  C2    . EDO H 6 .   ? 14.642 10.183  29.056 1.00 32.62 ? 307 EDO A C2    1 
HETATM 1918 O  O2    . EDO H 6 .   ? 15.103 9.008   28.457 1.00 28.08 ? 307 EDO A O2    1 
HETATM 1919 C  C1    . EDO I 6 .   ? 18.959 -8.203  15.836 1.00 35.79 ? 308 EDO A C1    1 
HETATM 1920 O  O1    . EDO I 6 .   ? 18.794 -8.964  16.998 1.00 39.38 ? 308 EDO A O1    1 
HETATM 1921 C  C2    . EDO I 6 .   ? 17.721 -8.535  15.080 1.00 41.14 ? 308 EDO A C2    1 
HETATM 1922 O  O2    . EDO I 6 .   ? 17.693 -7.975  13.795 1.00 44.51 ? 308 EDO A O2    1 
HETATM 1923 C  C1    . EDO J 6 .   ? 19.350 -8.062  22.407 1.00 32.58 ? 309 EDO A C1    1 
HETATM 1924 O  O1    . EDO J 6 .   ? 20.243 -8.949  21.787 1.00 43.91 ? 309 EDO A O1    1 
HETATM 1925 C  C2    . EDO J 6 .   ? 18.637 -7.338  21.356 1.00 29.13 ? 309 EDO A C2    1 
HETATM 1926 O  O2    . EDO J 6 .   ? 17.750 -6.439  21.992 1.00 36.84 ? 309 EDO A O2    1 
HETATM 1927 C  C1    . EDO K 6 .   ? 21.258 17.902  33.780 1.00 62.76 ? 310 EDO A C1    1 
HETATM 1928 O  O1    . EDO K 6 .   ? 22.570 17.341  33.818 1.00 60.73 ? 310 EDO A O1    1 
HETATM 1929 C  C2    . EDO K 6 .   ? 20.417 17.577  34.970 1.00 62.12 ? 310 EDO A C2    1 
HETATM 1930 O  O2    . EDO K 6 .   ? 19.013 17.585  34.707 1.00 56.44 ? 310 EDO A O2    1 
HETATM 1931 C  C1    . EDO L 6 .   ? 9.539  8.939   5.937  1.00 38.03 ? 311 EDO A C1    1 
HETATM 1932 O  O1    . EDO L 6 .   ? 10.002 8.223   4.858  1.00 44.04 ? 311 EDO A O1    1 
HETATM 1933 C  C2    . EDO L 6 .   ? 8.100  8.985   5.933  1.00 41.43 ? 311 EDO A C2    1 
HETATM 1934 O  O2    . EDO L 6 .   ? 7.576  9.550   7.123  1.00 39.06 ? 311 EDO A O2    1 
HETATM 1935 C  C1    . PEG M 7 .   ? 34.102 15.094  30.347 1.00 65.65 ? 312 PEG A C1    1 
HETATM 1936 O  O1    . PEG M 7 .   ? 34.014 15.214  31.754 1.00 67.10 ? 312 PEG A O1    1 
HETATM 1937 C  C2    . PEG M 7 .   ? 35.093 14.051  29.939 1.00 69.22 ? 312 PEG A C2    1 
HETATM 1938 O  O2    . PEG M 7 .   ? 36.316 14.651  29.526 1.00 75.07 ? 312 PEG A O2    1 
HETATM 1939 C  C3    . PEG M 7 .   ? 36.835 14.115  28.315 1.00 67.28 ? 312 PEG A C3    1 
HETATM 1940 C  C4    . PEG M 7 .   ? 35.892 14.376  27.167 1.00 62.54 ? 312 PEG A C4    1 
HETATM 1941 O  O4    . PEG M 7 .   ? 36.377 15.299  26.201 1.00 60.84 ? 312 PEG A O4    1 
HETATM 1942 O  O     . HOH N 8 .   ? 11.772 14.025  33.871 1.00 57.20 ? 401 HOH A O     1 
HETATM 1943 O  O     . HOH N 8 .   ? 21.486 -10.855 21.878 1.00 37.15 ? 402 HOH A O     1 
HETATM 1944 O  O     . HOH N 8 .   ? 29.451 18.126  28.257 1.00 40.70 ? 403 HOH A O     1 
HETATM 1945 O  O     . HOH N 8 .   ? 0.186  23.326  25.099 1.00 45.72 ? 404 HOH A O     1 
HETATM 1946 O  O     . HOH N 8 .   ? 7.938  31.351  21.084 1.00 40.81 ? 405 HOH A O     1 
HETATM 1947 O  O     . HOH N 8 .   ? 17.446 18.154  -3.012 1.00 30.46 ? 406 HOH A O     1 
HETATM 1948 O  O     . HOH N 8 .   ? 26.056 17.607  30.213 1.00 37.35 ? 407 HOH A O     1 
HETATM 1949 O  O     . HOH N 8 .   ? 6.720  -1.244  14.590 1.00 40.59 ? 408 HOH A O     1 
HETATM 1950 O  O     . HOH N 8 .   ? 2.605  3.986   26.161 1.00 37.31 ? 409 HOH A O     1 
HETATM 1951 O  O     . HOH N 8 .   ? 14.897 -5.510  11.768 1.00 35.40 ? 410 HOH A O     1 
HETATM 1952 O  O     . HOH N 8 .   ? 16.182 24.850  1.554  1.00 42.97 ? 411 HOH A O     1 
HETATM 1953 O  O     . HOH N 8 .   ? 11.378 29.438  29.381 1.00 37.42 ? 412 HOH A O     1 
HETATM 1954 O  O     . HOH N 8 .   ? 8.762  24.363  24.980 1.00 31.16 ? 413 HOH A O     1 
HETATM 1955 O  O     . HOH N 8 .   ? 1.753  10.949  17.643 1.00 25.73 ? 414 HOH A O     1 
HETATM 1956 O  O     . HOH N 8 .   ? 24.221 23.401  10.812 1.00 19.48 ? 415 HOH A O     1 
HETATM 1957 O  O     . HOH N 8 .   ? 2.193  29.128  23.731 1.00 45.91 ? 416 HOH A O     1 
HETATM 1958 O  O     . HOH N 8 .   ? 31.844 -1.574  16.395 1.00 28.91 ? 417 HOH A O     1 
HETATM 1959 O  O     . HOH N 8 .   ? 33.540 -16.284 16.217 1.00 44.47 ? 418 HOH A O     1 
HETATM 1960 O  O     . HOH N 8 .   ? 17.211 -9.158  11.530 1.00 29.24 ? 419 HOH A O     1 
HETATM 1961 O  O     . HOH N 8 .   ? 14.383 -4.833  29.339 1.00 34.06 ? 420 HOH A O     1 
HETATM 1962 O  O     . HOH N 8 .   ? 4.116  10.044  10.181 1.00 33.53 ? 421 HOH A O     1 
HETATM 1963 O  O     . HOH N 8 .   ? 21.730 -10.680 17.996 1.00 28.43 ? 422 HOH A O     1 
HETATM 1964 O  O     . HOH N 8 .   ? 18.434 -10.188 19.276 1.00 37.66 ? 423 HOH A O     1 
HETATM 1965 O  O     . HOH N 8 .   ? 24.789 0.307   6.567  1.00 32.79 ? 424 HOH A O     1 
HETATM 1966 O  O     . HOH N 8 .   ? 15.618 2.191   10.480 1.00 20.50 ? 425 HOH A O     1 
HETATM 1967 O  O     . HOH N 8 .   ? 18.574 14.774  28.737 1.00 24.10 ? 426 HOH A O     1 
HETATM 1968 O  O     . HOH N 8 .   ? 7.076  27.021  4.958  1.00 36.94 ? 427 HOH A O     1 
HETATM 1969 O  O     . HOH N 8 .   ? 34.082 -1.074  18.304 1.00 29.11 ? 428 HOH A O     1 
HETATM 1970 O  O     . HOH N 8 .   ? 16.840 -9.084  8.239  1.00 38.21 ? 429 HOH A O     1 
HETATM 1971 O  O     . HOH N 8 .   ? 12.441 6.278   32.299 1.00 50.06 ? 430 HOH A O     1 
HETATM 1972 O  O     . HOH N 8 .   ? 13.109 -0.008  7.041  1.00 55.26 ? 431 HOH A O     1 
HETATM 1973 O  O     . HOH N 8 .   ? 21.698 4.680   14.361 1.00 30.57 ? 432 HOH A O     1 
HETATM 1974 O  O     . HOH N 8 .   ? 3.717  21.141  5.314  1.00 38.99 ? 433 HOH A O     1 
HETATM 1975 O  O     . HOH N 8 .   ? 29.279 2.724   12.311 1.00 38.85 ? 434 HOH A O     1 
HETATM 1976 O  O     . HOH N 8 .   ? 25.332 -7.622  24.160 1.00 36.43 ? 435 HOH A O     1 
HETATM 1977 O  O     . HOH N 8 .   ? 6.848  9.724   9.658  1.00 43.96 ? 436 HOH A O     1 
HETATM 1978 O  O     . HOH N 8 .   ? 26.943 -18.462 20.956 1.00 40.48 ? 437 HOH A O     1 
HETATM 1979 O  O     . HOH N 8 .   ? 20.892 -1.587  12.309 1.00 17.68 ? 438 HOH A O     1 
HETATM 1980 O  O     . HOH N 8 .   ? 7.484  19.938  30.077 1.00 31.55 ? 439 HOH A O     1 
HETATM 1981 O  O     . HOH N 8 .   ? 7.144  -4.631  16.598 1.00 26.21 ? 440 HOH A O     1 
HETATM 1982 O  O     . HOH N 8 .   ? 23.792 -1.420  15.078 1.00 17.72 ? 441 HOH A O     1 
HETATM 1983 O  O     . HOH N 8 .   ? 15.112 30.360  18.192 1.00 32.08 ? 442 HOH A O     1 
HETATM 1984 O  O     . HOH N 8 .   ? 32.402 -7.023  6.326  1.00 41.65 ? 443 HOH A O     1 
HETATM 1985 O  O     . HOH N 8 .   ? 16.310 16.126  -1.958 1.00 34.58 ? 444 HOH A O     1 
HETATM 1986 O  O     . HOH N 8 .   ? 15.511 38.145  16.144 1.00 55.99 ? 445 HOH A O     1 
HETATM 1987 O  O     . HOH N 8 .   ? 17.133 12.423  29.059 1.00 17.02 ? 446 HOH A O     1 
HETATM 1988 O  O     . HOH N 8 .   ? 4.028  19.506  7.863  1.00 34.42 ? 447 HOH A O     1 
HETATM 1989 O  O     . HOH N 8 .   ? 7.583  1.926   16.229 1.00 25.01 ? 448 HOH A O     1 
HETATM 1990 O  O     . HOH N 8 .   ? 13.875 10.873  6.917  1.00 33.55 ? 449 HOH A O     1 
HETATM 1991 O  O     . HOH N 8 .   ? 8.450  -4.002  27.219 1.00 17.89 ? 450 HOH A O     1 
HETATM 1992 O  O     . HOH N 8 .   ? 26.663 19.514  22.345 1.00 24.35 ? 451 HOH A O     1 
HETATM 1993 O  O     . HOH N 8 .   ? 34.095 -1.788  21.332 1.00 46.29 ? 452 HOH A O     1 
HETATM 1994 O  O     . HOH N 8 .   ? 8.092  30.562  14.858 1.00 37.61 ? 453 HOH A O     1 
HETATM 1995 O  O     . HOH N 8 .   ? 17.512 -2.810  18.340 1.00 21.59 ? 454 HOH A O     1 
HETATM 1996 O  O     . HOH N 8 .   ? 15.434 26.540  6.651  1.00 38.79 ? 455 HOH A O     1 
HETATM 1997 O  O     . HOH N 8 .   ? 23.323 -9.279  24.446 1.00 26.74 ? 456 HOH A O     1 
HETATM 1998 O  O     . HOH N 8 .   ? 30.672 -3.943  17.000 1.00 23.82 ? 457 HOH A O     1 
HETATM 1999 O  O     . HOH N 8 .   ? 2.055  32.404  18.412 1.00 41.97 ? 458 HOH A O     1 
HETATM 2000 O  O     . HOH N 8 .   ? 24.911 14.547  30.751 1.00 42.69 ? 459 HOH A O     1 
HETATM 2001 O  O     . HOH N 8 .   ? -4.192 8.822   13.850 1.00 46.12 ? 460 HOH A O     1 
HETATM 2002 O  O     . HOH N 8 .   ? 6.231  30.869  24.582 1.00 58.64 ? 461 HOH A O     1 
HETATM 2003 O  O     . HOH N 8 .   ? 30.628 -0.565  29.637 1.00 47.14 ? 462 HOH A O     1 
HETATM 2004 O  O     . HOH N 8 .   ? 27.207 12.585  27.681 1.00 34.81 ? 463 HOH A O     1 
HETATM 2005 O  O     . HOH N 8 .   ? 32.423 0.657   27.572 1.00 44.60 ? 464 HOH A O     1 
HETATM 2006 O  O     . HOH N 8 .   ? 10.246 30.632  27.113 1.00 41.45 ? 465 HOH A O     1 
HETATM 2007 O  O     . HOH N 8 .   ? 18.354 -5.823  27.165 1.00 42.69 ? 466 HOH A O     1 
HETATM 2008 O  O     . HOH N 8 .   ? 3.947  3.171   13.763 1.00 41.96 ? 467 HOH A O     1 
HETATM 2009 O  O     . HOH N 8 .   ? 7.881  9.052   12.049 1.00 41.64 ? 468 HOH A O     1 
HETATM 2010 O  O     . HOH N 8 .   ? 0.928  17.357  27.099 1.00 49.19 ? 469 HOH A O     1 
HETATM 2011 O  O     . HOH N 8 .   ? 2.934  16.853  8.803  1.00 33.09 ? 470 HOH A O     1 
HETATM 2012 O  O     . HOH N 8 .   ? -2.225 15.283  26.318 1.00 36.07 ? 471 HOH A O     1 
HETATM 2013 O  O     . HOH N 8 .   ? 17.994 18.317  30.636 1.00 23.75 ? 472 HOH A O     1 
HETATM 2014 O  O     . HOH N 8 .   ? 23.793 21.093  34.903 1.00 48.51 ? 473 HOH A O     1 
HETATM 2015 O  O     . HOH N 8 .   ? 31.389 8.196   16.749 1.00 24.15 ? 474 HOH A O     1 
HETATM 2016 O  O     . HOH N 8 .   ? 24.367 17.188  7.373  1.00 30.19 ? 475 HOH A O     1 
HETATM 2017 O  O     . HOH N 8 .   ? 2.450  15.418  29.802 1.00 40.94 ? 476 HOH A O     1 
HETATM 2018 O  O     . HOH N 8 .   ? 35.130 8.387   19.096 1.00 22.44 ? 477 HOH A O     1 
HETATM 2019 O  O     . HOH N 8 .   ? 15.702 2.466   3.157  1.00 54.85 ? 478 HOH A O     1 
HETATM 2020 O  O     . HOH N 8 .   ? 9.315  2.585   31.145 1.00 52.87 ? 479 HOH A O     1 
HETATM 2021 O  O     . HOH N 8 .   ? 25.243 3.089   5.837  1.00 32.50 ? 480 HOH A O     1 
HETATM 2022 O  O     . HOH N 8 .   ? 29.484 2.270   10.270 1.00 33.10 ? 481 HOH A O     1 
HETATM 2023 O  O     . HOH N 8 .   ? 17.140 -4.753  1.063  1.00 57.04 ? 482 HOH A O     1 
HETATM 2024 O  O     . HOH N 8 .   ? 14.237 13.408  5.938  1.00 23.21 ? 483 HOH A O     1 
HETATM 2025 O  O     . HOH N 8 .   ? 9.120  17.529  30.776 1.00 23.57 ? 484 HOH A O     1 
HETATM 2026 O  O     . HOH N 8 .   ? 17.414 5.338   32.282 1.00 32.12 ? 485 HOH A O     1 
HETATM 2027 O  O     . HOH N 8 .   ? 23.316 19.974  20.024 1.00 26.47 ? 486 HOH A O     1 
HETATM 2028 O  O     . HOH N 8 .   ? 33.270 -15.951 18.753 1.00 46.70 ? 487 HOH A O     1 
HETATM 2029 O  O     . HOH N 8 .   ? 27.488 9.403   34.000 1.00 36.26 ? 488 HOH A O     1 
HETATM 2030 O  O     . HOH N 8 .   ? 21.978 10.729  9.621  1.00 19.12 ? 489 HOH A O     1 
HETATM 2031 O  O     . HOH N 8 .   ? 20.439 -4.367  34.861 1.00 46.44 ? 490 HOH A O     1 
HETATM 2032 O  O     . HOH N 8 .   ? 31.209 -4.753  26.432 1.00 36.73 ? 491 HOH A O     1 
HETATM 2033 O  O     . HOH N 8 .   ? 16.356 13.522  4.243  1.00 33.83 ? 492 HOH A O     1 
HETATM 2034 O  O     . HOH N 8 .   ? 16.551 27.536  31.531 1.00 39.44 ? 493 HOH A O     1 
HETATM 2035 O  O     . HOH N 8 .   ? 17.836 10.801  36.625 1.00 56.76 ? 494 HOH A O     1 
HETATM 2036 O  O     . HOH N 8 .   ? 4.528  15.789  32.295 1.00 53.46 ? 495 HOH A O     1 
HETATM 2037 O  O     . HOH N 8 .   ? 25.446 31.439  31.028 1.00 35.98 ? 496 HOH A O     1 
HETATM 2038 O  O     . HOH N 8 .   ? 15.032 -2.264  31.776 1.00 45.77 ? 497 HOH A O     1 
HETATM 2039 O  O     . HOH N 8 .   ? 0.986  16.630  17.297 1.00 24.92 ? 498 HOH A O     1 
HETATM 2040 O  O     . HOH N 8 .   ? 4.966  2.897   16.546 1.00 24.16 ? 499 HOH A O     1 
HETATM 2041 O  O     . HOH N 8 .   ? 0.429  25.257  23.350 1.00 43.99 ? 500 HOH A O     1 
HETATM 2042 O  O     . HOH N 8 .   ? -0.000 -0.000  14.759 0.33 44.04 ? 501 HOH A O     1 
HETATM 2043 O  O     . HOH N 8 .   ? 10.137 30.060  9.181  1.00 18.68 ? 502 HOH A O     1 
HETATM 2044 O  O     . HOH N 8 .   ? 0.111  5.370   14.075 1.00 46.06 ? 503 HOH A O     1 
HETATM 2045 O  O     . HOH N 8 .   ? 8.052  12.548  31.205 1.00 39.29 ? 504 HOH A O     1 
HETATM 2046 O  O     . HOH N 8 .   ? 34.100 6.633   29.326 1.00 54.82 ? 505 HOH A O     1 
HETATM 2047 O  O     . HOH N 8 .   ? 16.372 -8.242  18.819 1.00 28.61 ? 506 HOH A O     1 
HETATM 2048 O  O     . HOH N 8 .   ? 15.401 29.665  32.347 1.00 35.08 ? 507 HOH A O     1 
HETATM 2049 O  O     . HOH N 8 .   ? 0.269  12.873  11.186 1.00 40.23 ? 508 HOH A O     1 
HETATM 2050 O  O     . HOH N 8 .   ? 0.159  6.971   22.010 1.00 44.07 ? 509 HOH A O     1 
HETATM 2051 O  O     . HOH N 8 .   ? 1.538  12.823  31.551 1.00 35.07 ? 510 HOH A O     1 
HETATM 2052 O  O     . HOH N 8 .   ? 9.966  14.040  31.813 1.00 45.00 ? 511 HOH A O     1 
HETATM 2053 O  O     . HOH N 8 .   ? -0.000 -0.000  23.103 0.33 39.72 ? 512 HOH A O     1 
HETATM 2054 O  O     . HOH N 8 .   ? 29.988 -4.527  1.137  1.00 57.52 ? 513 HOH A O     1 
HETATM 2055 O  O     . HOH N 8 .   ? 27.644 5.942   30.769 1.00 53.19 ? 514 HOH A O     1 
HETATM 2056 O  O     . HOH N 8 .   ? 39.335 13.588  30.189 1.00 53.63 ? 515 HOH A O     1 
HETATM 2057 O  O     . HOH N 8 .   ? 13.678 3.458   2.490  1.00 61.93 ? 516 HOH A O     1 
HETATM 2058 O  O     . HOH N 8 .   ? 25.447 21.850  12.925 1.00 28.47 ? 517 HOH A O     1 
HETATM 2059 O  O     . HOH N 8 .   ? -0.044 8.735   19.825 1.00 31.11 ? 518 HOH A O     1 
HETATM 2060 O  O     . HOH N 8 .   ? 14.280 34.834  24.191 1.00 53.44 ? 519 HOH A O     1 
HETATM 2061 O  O     . HOH N 8 .   ? 17.404 22.892  36.916 1.00 50.44 ? 520 HOH A O     1 
HETATM 2062 O  O     . HOH N 8 .   ? 4.235  1.948   11.980 1.00 49.85 ? 521 HOH A O     1 
HETATM 2063 O  O     . HOH N 8 .   ? 14.837 -8.442  11.818 1.00 38.84 ? 522 HOH A O     1 
HETATM 2064 O  O     . HOH N 8 .   ? 13.687 -8.214  14.697 1.00 35.74 ? 523 HOH A O     1 
HETATM 2065 O  O     . HOH N 8 .   ? 22.509 13.914  4.608  1.00 47.13 ? 524 HOH A O     1 
HETATM 2066 O  O     . HOH N 8 .   ? 22.586 -15.850 27.712 1.00 61.13 ? 525 HOH A O     1 
HETATM 2067 O  O     . HOH N 8 .   ? 18.075 -7.736  0.347  1.00 57.67 ? 526 HOH A O     1 
HETATM 2068 O  O     . HOH N 8 .   ? 4.666  8.891   4.631  1.00 57.20 ? 527 HOH A O     1 
HETATM 2069 O  O     . HOH N 8 .   ? 27.091 15.283  30.609 1.00 46.79 ? 528 HOH A O     1 
HETATM 2070 O  O     . HOH N 8 .   ? -0.000 -0.000  25.315 0.33 39.54 ? 529 HOH A O     1 
HETATM 2071 O  O     . HOH N 8 .   ? 1.559  5.343   28.644 1.00 51.40 ? 530 HOH A O     1 
HETATM 2072 O  O     . HOH N 8 .   ? 8.182  15.795  32.311 1.00 48.58 ? 531 HOH A O     1 
HETATM 2073 O  O     . HOH N 8 .   ? 37.031 0.152   24.198 1.00 44.79 ? 532 HOH A O     1 
HETATM 2074 O  O     . HOH N 8 .   ? 31.542 -17.461 20.044 1.00 56.56 ? 533 HOH A O     1 
HETATM 2075 O  O     . HOH N 8 .   ? 26.322 10.149  36.786 1.00 43.96 ? 534 HOH A O     1 
HETATM 2076 O  O     . HOH N 8 .   ? 5.394  30.195  15.147 1.00 51.10 ? 535 HOH A O     1 
HETATM 2077 O  O     . HOH N 8 .   ? 8.699  8.744   29.684 1.00 55.11 ? 536 HOH A O     1 
HETATM 2078 O  O     . HOH N 8 .   ? 25.133 -0.737  0.749  1.00 52.24 ? 537 HOH A O     1 
HETATM 2079 O  O     . HOH N 8 .   ? 33.953 -1.246  26.863 1.00 65.76 ? 538 HOH A O     1 
HETATM 2080 O  O     . HOH N 8 .   ? 4.632  26.101  29.917 1.00 49.09 ? 539 HOH A O     1 
HETATM 2081 O  O     . HOH N 8 .   ? 18.018 11.166  2.234  1.00 52.30 ? 540 HOH A O     1 
HETATM 2082 O  O     . HOH N 8 .   ? 23.245 20.351  0.218  1.00 50.24 ? 541 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   . GLU A 2   ? 0.9020 1.0681 0.7613 -0.0038 0.0537  -0.1081 2   GLU A N   
2    C CA  . GLU A 2   ? 0.9143 1.0763 0.7917 -0.0018 0.0527  -0.0933 2   GLU A CA  
3    C C   . GLU A 2   ? 0.9089 1.0691 0.8091 0.0024  0.0621  -0.0977 2   GLU A C   
4    O O   . GLU A 2   ? 0.9352 1.0974 0.8466 0.0036  0.0651  -0.0871 2   GLU A O   
5    C CB  . GLU A 2   ? 0.9877 1.1586 0.8531 -0.0040 0.0530  -0.0783 2   GLU A CB  
6    C CG  . GLU A 2   ? 1.0406 1.2083 0.8985 -0.0067 0.0410  -0.0666 2   GLU A CG  
7    C CD  . GLU A 2   ? 1.0958 1.2664 0.9569 -0.0076 0.0402  -0.0493 2   GLU A CD  
8    O OE1 . GLU A 2   ? 1.0517 1.2283 0.9183 -0.0066 0.0490  -0.0456 2   GLU A OE1 
9    O OE2 . GLU A 2   ? 1.1476 1.3141 1.0077 -0.0093 0.0311  -0.0399 2   GLU A OE2 
10   N N   . GLU A 3   ? 0.8657 1.0217 0.7749 0.0044  0.0664  -0.1133 3   GLU A N   
11   C CA  . GLU A 3   ? 0.7347 0.8875 0.6700 0.0088  0.0741  -0.1173 3   GLU A CA  
12   C C   . GLU A 3   ? 0.6052 0.7453 0.5593 0.0108  0.0684  -0.1231 3   GLU A C   
13   O O   . GLU A 3   ? 0.5755 0.7107 0.5543 0.0144  0.0707  -0.1210 3   GLU A O   
14   C CB  . GLU A 3   ? 0.7855 0.9476 0.7170 0.0099  0.0882  -0.1298 3   GLU A CB  
15   C CG  . GLU A 3   ? 0.7908 0.9481 0.7482 0.0143  0.0963  -0.1423 3   GLU A CG  
16   C CD  . GLU A 3   ? 0.9040 1.0701 0.8724 0.0170  0.1108  -0.1444 3   GLU A CD  
17   O OE1 . GLU A 3   ? 0.8952 1.0594 0.8814 0.0204  0.1198  -0.1581 3   GLU A OE1 
18   O OE2 . GLU A 3   ? 0.9815 1.1560 0.9436 0.0160  0.1133  -0.1320 3   GLU A OE2 
19   N N   . LYS A 4   ? 0.5179 0.6527 0.4619 0.0084  0.0607  -0.1291 4   LYS A N   
20   C CA  . LYS A 4   ? 0.4602 0.5828 0.4226 0.0098  0.0553  -0.1328 4   LYS A CA  
21   C C   . LYS A 4   ? 0.4022 0.5185 0.3771 0.0107  0.0481  -0.1161 4   LYS A C   
22   O O   . LYS A 4   ? 0.3743 0.4945 0.3390 0.0091  0.0447  -0.1035 4   LYS A O   
23   C CB  . LYS A 4   ? 0.4686 0.5878 0.4180 0.0065  0.0481  -0.1416 4   LYS A CB  
24   C CG  . LYS A 4   ? 0.4652 0.5843 0.3995 0.0031  0.0372  -0.1296 4   LYS A CG  
25   C CD  . LYS A 4   ? 0.4780 0.5955 0.4008 -0.0004 0.0299  -0.1382 4   LYS A CD  
26   C CE  . LYS A 4   ? 0.5161 0.6436 0.4177 -0.0029 0.0336  -0.1509 4   LYS A CE  
27   N NZ  . LYS A 4   ? 0.5227 0.6539 0.4045 -0.0074 0.0238  -0.1505 4   LYS A NZ  
28   N N   . LYS A 5   ? 0.3695 0.4759 0.3663 0.0132  0.0460  -0.1161 5   LYS A N   
29   C CA  . LYS A 5   ? 0.3515 0.4512 0.3576 0.0134  0.0384  -0.1017 5   LYS A CA  
30   C C   . LYS A 5   ? 0.3334 0.4309 0.3221 0.0096  0.0293  -0.0963 5   LYS A C   
31   O O   . LYS A 5   ? 0.3337 0.4293 0.3147 0.0077  0.0267  -0.1051 5   LYS A O   
32   C CB  . LYS A 5   ? 0.3659 0.4554 0.3964 0.0162  0.0373  -0.1035 5   LYS A CB  
33   C CG  . LYS A 5   ? 0.3998 0.4901 0.4535 0.0206  0.0454  -0.1077 5   LYS A CG  
34   C CD  . LYS A 5   ? 0.4304 0.5103 0.5087 0.0231  0.0438  -0.1092 5   LYS A CD  
35   C CE  . LYS A 5   ? 0.4812 0.5616 0.5864 0.0277  0.0492  -0.1065 5   LYS A CE  
36   N NZ  . LYS A 5   ? 0.5357 0.6067 0.6661 0.0304  0.0500  -0.1118 5   LYS A NZ  
37   N N   . ARG A 6   ? 0.3071 0.4049 0.2918 0.0085  0.0246  -0.0823 6   ARG A N   
38   C CA  . ARG A 6   ? 0.2858 0.3805 0.2591 0.0055  0.0164  -0.0753 6   ARG A CA  
39   C C   . ARG A 6   ? 0.2720 0.3620 0.2534 0.0058  0.0123  -0.0623 6   ARG A C   
40   O O   . ARG A 6   ? 0.2714 0.3641 0.2612 0.0074  0.0149  -0.0568 6   ARG A O   
41   C CB  . ARG A 6   ? 0.2862 0.3893 0.2387 0.0025  0.0153  -0.0728 6   ARG A CB  
42   C CG  . ARG A 6   ? 0.3000 0.4095 0.2395 0.0014  0.0186  -0.0849 6   ARG A CG  
43   C CD  . ARG A 6   ? 0.3084 0.4252 0.2274 -0.0019 0.0149  -0.0796 6   ARG A CD  
44   N NE  . ARG A 6   ? 0.3236 0.4479 0.2277 -0.0034 0.0176  -0.0908 6   ARG A NE  
45   C CZ  . ARG A 6   ? 0.3483 0.4825 0.2420 -0.0034 0.0249  -0.0927 6   ARG A CZ  
46   N NH1 . ARG A 6   ? 0.3474 0.4847 0.2477 -0.0017 0.0306  -0.0847 6   ARG A NH1 
47   N NH2 . ARG A 6   ? 0.3807 0.5220 0.2579 -0.0053 0.0266  -0.1030 6   ARG A NH2 
48   N N   . LEU A 7   ? 0.2687 0.3518 0.2482 0.0040  0.0059  -0.0581 7   LEU A N   
49   C CA  . LEU A 7   ? 0.2599 0.3393 0.2406 0.0032  0.0015  -0.0465 7   LEU A CA  
50   C C   . LEU A 7   ? 0.2612 0.3456 0.2277 0.0005  -0.0007 -0.0403 7   LEU A C   
51   O O   . LEU A 7   ? 0.2659 0.3522 0.2213 -0.0014 -0.0026 -0.0428 7   LEU A O   
52   C CB  . LEU A 7   ? 0.2699 0.3400 0.2545 0.0023  -0.0029 -0.0456 7   LEU A CB  
53   C CG  . LEU A 7   ? 0.2617 0.3274 0.2440 0.0006  -0.0073 -0.0352 7   LEU A CG  
54   C CD1 . LEU A 7   ? 0.2649 0.3303 0.2561 0.0021  -0.0073 -0.0283 7   LEU A CD1 
55   C CD2 . LEU A 7   ? 0.2778 0.3353 0.2629 -0.0004 -0.0100 -0.0354 7   LEU A CD2 
56   N N   . HIS A 8   ? 0.2560 0.3421 0.2245 0.0003  -0.0012 -0.0319 8   HIS A N   
57   C CA  . HIS A 8   ? 0.2484 0.3376 0.2076 -0.0023 -0.0035 -0.0248 8   HIS A CA  
58   C C   . HIS A 8   ? 0.2419 0.3237 0.2029 -0.0037 -0.0085 -0.0185 8   HIS A C   
59   O O   . HIS A 8   ? 0.2345 0.3144 0.2030 -0.0033 -0.0095 -0.0141 8   HIS A O   
60   C CB  . HIS A 8   ? 0.2525 0.3499 0.2134 -0.0019 0.0004  -0.0211 8   HIS A CB  
61   C CG  . HIS A 8   ? 0.2750 0.3802 0.2305 -0.0010 0.0062  -0.0277 8   HIS A CG  
62   N ND1 . HIS A 8   ? 0.2700 0.3826 0.2137 -0.0028 0.0077  -0.0252 8   HIS A ND1 
63   C CD2 . HIS A 8   ? 0.2849 0.3913 0.2441 0.0012  0.0109  -0.0371 8   HIS A CD2 
64   C CE1 . HIS A 8   ? 0.2855 0.4044 0.2237 -0.0019 0.0133  -0.0328 8   HIS A CE1 
65   N NE2 . HIS A 8   ? 0.2877 0.4028 0.2354 0.0005  0.0156  -0.0411 8   HIS A NE2 
66   N N   . LEU A 9   ? 0.2310 0.3091 0.1852 -0.0056 -0.0116 -0.0182 9   LEU A N   
67   C CA  . LEU A 9   ? 0.2303 0.3009 0.1854 -0.0070 -0.0150 -0.0140 9   LEU A CA  
68   C C   . LEU A 9   ? 0.2314 0.3031 0.1812 -0.0094 -0.0168 -0.0084 9   LEU A C   
69   O O   . LEU A 9   ? 0.2344 0.3093 0.1790 -0.0104 -0.0172 -0.0083 9   LEU A O   
70   C CB  . LEU A 9   ? 0.2473 0.3125 0.2022 -0.0073 -0.0162 -0.0182 9   LEU A CB  
71   C CG  . LEU A 9   ? 0.2560 0.3141 0.2104 -0.0090 -0.0184 -0.0145 9   LEU A CG  
72   C CD1 . LEU A 9   ? 0.2544 0.3077 0.2135 -0.0086 -0.0186 -0.0111 9   LEU A CD1 
73   C CD2 . LEU A 9   ? 0.2815 0.3362 0.2371 -0.0095 -0.0191 -0.0186 9   LEU A CD2 
74   N N   . ILE A 10  ? 0.2268 0.2958 0.1789 -0.0106 -0.0183 -0.0037 10  ILE A N   
75   C CA  . ILE A 10  ? 0.2124 0.2814 0.1620 -0.0130 -0.0197 0.0006  10  ILE A CA  
76   C C   . ILE A 10  ? 0.2202 0.2812 0.1682 -0.0147 -0.0216 0.0012  10  ILE A C   
77   O O   . ILE A 10  ? 0.2150 0.2723 0.1640 -0.0149 -0.0226 0.0018  10  ILE A O   
78   C CB  . ILE A 10  ? 0.2189 0.2925 0.1726 -0.0136 -0.0196 0.0046  10  ILE A CB  
79   C CG1 . ILE A 10  ? 0.2365 0.3184 0.1930 -0.0118 -0.0162 0.0039  10  ILE A CG1 
80   C CG2 . ILE A 10  ? 0.2250 0.2982 0.1781 -0.0164 -0.0209 0.0085  10  ILE A CG2 
81   C CD1 . ILE A 10  ? 0.2311 0.3173 0.1958 -0.0120 -0.0160 0.0076  10  ILE A CD1 
82   N N   . ILE A 11  ? 0.2217 0.2805 0.1675 -0.0160 -0.0218 0.0012  11  ILE A N   
83   C CA  . ILE A 11  ? 0.2217 0.2737 0.1665 -0.0180 -0.0222 0.0016  11  ILE A CA  
84   C C   . ILE A 11  ? 0.2205 0.2731 0.1663 -0.0202 -0.0230 0.0044  11  ILE A C   
85   O O   . ILE A 11  ? 0.2145 0.2698 0.1628 -0.0208 -0.0228 0.0065  11  ILE A O   
86   C CB  . ILE A 11  ? 0.2380 0.2876 0.1835 -0.0182 -0.0217 0.0001  11  ILE A CB  
87   C CG1 . ILE A 11  ? 0.2643 0.3146 0.2106 -0.0164 -0.0215 -0.0033 11  ILE A CG1 
88   C CG2 . ILE A 11  ? 0.2450 0.2874 0.1904 -0.0201 -0.0204 -0.0004 11  ILE A CG2 
89   C CD1 . ILE A 11  ? 0.2684 0.3142 0.2153 -0.0156 -0.0207 -0.0049 11  ILE A CD1 
90   N N   . ALA A 12  ? 0.2163 0.2663 0.1608 -0.0218 -0.0243 0.0048  12  ALA A N   
91   C CA  . ALA A 12  ? 0.2172 0.2693 0.1644 -0.0239 -0.0258 0.0068  12  ALA A CA  
92   C C   . ALA A 12  ? 0.2129 0.2588 0.1579 -0.0270 -0.0262 0.0049  12  ALA A C   
93   O O   . ALA A 12  ? 0.2119 0.2522 0.1511 -0.0277 -0.0254 0.0024  12  ALA A O   
94   C CB  . ALA A 12  ? 0.2299 0.2859 0.1790 -0.0233 -0.0279 0.0084  12  ALA A CB  
95   N N   . ASP A 13  ? 0.2141 0.2609 0.1640 -0.0293 -0.0270 0.0058  13  ASP A N   
96   C CA  . ASP A 13  ? 0.2268 0.2678 0.1760 -0.0327 -0.0270 0.0024  13  ASP A CA  
97   C C   . ASP A 13  ? 0.2333 0.2685 0.1809 -0.0323 -0.0234 -0.0004 13  ASP A C   
98   O O   . ASP A 13  ? 0.2434 0.2726 0.1863 -0.0343 -0.0218 -0.0047 13  ASP A O   
99   C CB  . ASP A 13  ? 0.2377 0.2770 0.1795 -0.0350 -0.0302 0.0003  13  ASP A CB  
100  C CG  . ASP A 13  ? 0.2498 0.2946 0.1962 -0.0363 -0.0346 0.0026  13  ASP A CG  
101  O OD1 . ASP A 13  ? 0.2564 0.3054 0.2125 -0.0362 -0.0344 0.0053  13  ASP A OD1 
102  O OD2 . ASP A 13  ? 0.2616 0.3069 0.2024 -0.0374 -0.0385 0.0027  13  ASP A OD2 
103  N N   . ALA A 14  ? 0.2149 0.2525 0.1674 -0.0298 -0.0219 0.0021  14  ALA A N   
104  C CA  . ALA A 14  ? 0.2335 0.2669 0.1870 -0.0290 -0.0190 0.0002  14  ALA A CA  
105  C C   . ALA A 14  ? 0.2476 0.2760 0.2081 -0.0311 -0.0167 -0.0021 14  ALA A C   
106  O O   . ALA A 14  ? 0.2493 0.2792 0.2177 -0.0322 -0.0176 0.0001  14  ALA A O   
107  C CB  . ALA A 14  ? 0.2462 0.2848 0.2034 -0.0263 -0.0196 0.0036  14  ALA A CB  
108  N N   . GLU A 15  ? 0.2385 0.2610 0.1978 -0.0316 -0.0130 -0.0063 15  GLU A N   
109  C CA  . GLU A 15  ? 0.2445 0.2616 0.2120 -0.0332 -0.0093 -0.0098 15  GLU A CA  
110  C C   . GLU A 15  ? 0.2336 0.2524 0.2152 -0.0311 -0.0087 -0.0059 15  GLU A C   
111  O O   . GLU A 15  ? 0.2497 0.2650 0.2374 -0.0305 -0.0051 -0.0079 15  GLU A O   
112  C CB  . GLU A 15  ? 0.2660 0.2769 0.2251 -0.0348 -0.0048 -0.0161 15  GLU A CB  
113  C CG  . GLU A 15  ? 0.2805 0.2905 0.2257 -0.0375 -0.0068 -0.0190 15  GLU A CG  
114  C CD  . GLU A 15  ? 0.3048 0.3138 0.2517 -0.0408 -0.0089 -0.0220 15  GLU A CD  
115  O OE1 . GLU A 15  ? 0.3358 0.3450 0.2713 -0.0434 -0.0118 -0.0243 15  GLU A OE1 
116  O OE2 . GLU A 15  ? 0.3095 0.3175 0.2695 -0.0411 -0.0080 -0.0222 15  GLU A OE2 
117  N N   . LEU A 16  ? 0.2137 0.2385 0.2003 -0.0301 -0.0125 0.0005  16  LEU A N   
118  C CA  . LEU A 16  ? 0.2055 0.2338 0.2039 -0.0284 -0.0138 0.0065  16  LEU A CA  
119  C C   . LEU A 16  ? 0.2048 0.2340 0.2140 -0.0296 -0.0148 0.0109  16  LEU A C   
120  O O   . LEU A 16  ? 0.2200 0.2540 0.2257 -0.0302 -0.0172 0.0145  16  LEU A O   
121  C CB  . LEU A 16  ? 0.2010 0.2370 0.1922 -0.0263 -0.0175 0.0109  16  LEU A CB  
122  C CG  . LEU A 16  ? 0.2063 0.2482 0.2059 -0.0248 -0.0204 0.0178  16  LEU A CG  
123  C CD1 . LEU A 16  ? 0.2145 0.2532 0.2236 -0.0239 -0.0192 0.0165  16  LEU A CD1 
124  C CD2 . LEU A 16  ? 0.2046 0.2546 0.1938 -0.0233 -0.0237 0.0204  16  LEU A CD2 
125  N N   . GLU A 17  ? 0.2038 0.2282 0.2282 -0.0302 -0.0123 0.0104  17  GLU A N   
126  C CA  . GLU A 17  ? 0.2131 0.2365 0.2515 -0.0316 -0.0124 0.0140  17  GLU A CA  
127  C C   . GLU A 17  ? 0.2211 0.2413 0.2792 -0.0306 -0.0105 0.0165  17  GLU A C   
128  O O   . GLU A 17  ? 0.2373 0.2539 0.2982 -0.0296 -0.0075 0.0119  17  GLU A O   
129  C CB  . GLU A 17  ? 0.2278 0.2453 0.2642 -0.0350 -0.0104 0.0062  17  GLU A CB  
130  C CG  . GLU A 17  ? 0.2267 0.2355 0.2618 -0.0364 -0.0053 -0.0047 17  GLU A CG  
131  C CD  . GLU A 17  ? 0.2401 0.2438 0.2698 -0.0404 -0.0042 -0.0135 17  GLU A CD  
132  O OE1 . GLU A 17  ? 0.2660 0.2658 0.2821 -0.0418 -0.0017 -0.0218 17  GLU A OE1 
133  O OE2 . GLU A 17  ? 0.2498 0.2535 0.2886 -0.0423 -0.0060 -0.0121 17  GLU A OE2 
134  N N   . THR A 18  ? 0.2259 0.2475 0.3001 -0.0309 -0.0119 0.0241  18  THR A N   
135  C CA  . THR A 18  ? 0.2333 0.2506 0.3303 -0.0302 -0.0097 0.0262  18  THR A CA  
136  C C   . THR A 18  ? 0.2497 0.2567 0.3528 -0.0326 -0.0037 0.0142  18  THR A C   
137  O O   . THR A 18  ? 0.2519 0.2566 0.3421 -0.0351 -0.0030 0.0069  18  THR A O   
138  C CB  . THR A 18  ? 0.2391 0.2607 0.3528 -0.0299 -0.0130 0.0391  18  THR A CB  
139  O OG1 . THR A 18  ? 0.2249 0.2468 0.3369 -0.0324 -0.0134 0.0401  18  THR A OG1 
140  C CG2 . THR A 18  ? 0.2523 0.2844 0.3600 -0.0276 -0.0187 0.0508  18  THR A CG2 
141  N N   . VAL A 19  ? 0.2575 0.2588 0.3817 -0.0319 0.0003  0.0125  19  VAL A N   
142  C CA  . VAL A 19  ? 0.2645 0.2557 0.3948 -0.0341 0.0072  -0.0006 19  VAL A CA  
143  C C   . VAL A 19  ? 0.2571 0.2454 0.3888 -0.0377 0.0065  -0.0037 19  VAL A C   
144  O O   . VAL A 19  ? 0.2452 0.2357 0.3919 -0.0379 0.0034  0.0056  19  VAL A O   
145  C CB  . VAL A 19  ? 0.2749 0.2609 0.4328 -0.0324 0.0121  -0.0010 19  VAL A CB  
146  C CG1 . VAL A 19  ? 0.2992 0.2745 0.4640 -0.0351 0.0202  -0.0160 19  VAL A CG1 
147  C CG2 . VAL A 19  ? 0.2741 0.2632 0.4321 -0.0293 0.0128  0.0011  19  VAL A CG2 
148  N N   . PRO A 20  ? 0.2634 0.2471 0.3793 -0.0409 0.0090  -0.0163 20  PRO A N   
149  C CA  . PRO A 20  ? 0.2765 0.2574 0.3936 -0.0449 0.0077  -0.0210 20  PRO A CA  
150  C C   . PRO A 20  ? 0.2795 0.2539 0.4266 -0.0459 0.0107  -0.0214 20  PRO A C   
151  O O   . PRO A 20  ? 0.2777 0.2451 0.4388 -0.0453 0.0170  -0.0283 20  PRO A O   
152  C CB  . PRO A 20  ? 0.2922 0.2687 0.3881 -0.0480 0.0105  -0.0355 20  PRO A CB  
153  C CG  . PRO A 20  ? 0.2970 0.2780 0.3737 -0.0452 0.0105  -0.0333 20  PRO A CG  
154  C CD  . PRO A 20  ? 0.2813 0.2635 0.3759 -0.0411 0.0121  -0.0254 20  PRO A CD  
155  N N   . PRO A 21  ? 0.2933 0.2699 0.4532 -0.0473 0.0068  -0.0137 21  PRO A N   
156  C CA  . PRO A 21  ? 0.3096 0.2795 0.4998 -0.0488 0.0094  -0.0139 21  PRO A CA  
157  C C   . PRO A 21  ? 0.3315 0.2900 0.5287 -0.0519 0.0161  -0.0322 21  PRO A C   
158  O O   . PRO A 21  ? 0.3523 0.3041 0.5762 -0.0511 0.0209  -0.0340 21  PRO A O   
159  C CB  . PRO A 21  ? 0.3096 0.2836 0.5012 -0.0517 0.0042  -0.0078 21  PRO A CB  
160  C CG  . PRO A 21  ? 0.2966 0.2821 0.4691 -0.0490 -0.0009 0.0045  21  PRO A CG  
161  C CD  . PRO A 21  ? 0.2980 0.2837 0.4453 -0.0477 0.0004  -0.0041 21  PRO A CD  
162  N N   . GLU A 22  ? 0.3561 0.3129 0.5291 -0.0552 0.0165  -0.0456 22  GLU A N   
163  C CA  . GLU A 22  ? 0.3858 0.3328 0.5599 -0.0590 0.0227  -0.0644 22  GLU A CA  
164  C C   . GLU A 22  ? 0.4006 0.3416 0.5836 -0.0563 0.0316  -0.0710 22  GLU A C   
165  O O   . GLU A 22  ? 0.4164 0.3483 0.6114 -0.0587 0.0385  -0.0851 22  GLU A O   
166  C CB  . GLU A 22  ? 0.3959 0.3441 0.5365 -0.0625 0.0211  -0.0756 22  GLU A CB  
167  C CG  . GLU A 22  ? 0.3925 0.3461 0.5222 -0.0658 0.0127  -0.0729 22  GLU A CG  
168  C CD  . GLU A 22  ? 0.3776 0.3419 0.4889 -0.0628 0.0066  -0.0596 22  GLU A CD  
169  O OE1 . GLU A 22  ? 0.3837 0.3524 0.4754 -0.0653 0.0012  -0.0616 22  GLU A OE1 
170  O OE2 . GLU A 22  ? 0.3566 0.3250 0.4737 -0.0580 0.0070  -0.0476 22  GLU A OE2 
171  N N   . ILE A 23  ? 0.3909 0.3371 0.5668 -0.0518 0.0322  -0.0628 23  ILE A N   
172  C CA  . ILE A 23  ? 0.3919 0.3331 0.5734 -0.0498 0.0412  -0.0707 23  ILE A CA  
173  C C   . ILE A 23  ? 0.3925 0.3352 0.6030 -0.0448 0.0420  -0.0581 23  ILE A C   
174  O O   . ILE A 23  ? 0.4076 0.3486 0.6241 -0.0421 0.0483  -0.0610 23  ILE A O   
175  C CB  . ILE A 23  ? 0.4004 0.3451 0.5498 -0.0496 0.0426  -0.0749 23  ILE A CB  
176  C CG1 . ILE A 23  ? 0.3785 0.3334 0.5161 -0.0461 0.0350  -0.0593 23  ILE A CG1 
177  C CG2 . ILE A 23  ? 0.4037 0.3464 0.5259 -0.0548 0.0420  -0.0876 23  ILE A CG2 
178  C CD1 . ILE A 23  ? 0.3779 0.3356 0.4917 -0.0451 0.0371  -0.0618 23  ILE A CD1 
179  N N   . LEU A 24  ? 0.3847 0.3309 0.6142 -0.0435 0.0357  -0.0437 24  LEU A N   
180  C CA  . LEU A 24  ? 0.3909 0.3406 0.6453 -0.0389 0.0341  -0.0289 24  LEU A CA  
181  C C   . LEU A 24  ? 0.4285 0.3696 0.7137 -0.0374 0.0431  -0.0361 24  LEU A C   
182  O O   . LEU A 24  ? 0.4566 0.4004 0.7596 -0.0332 0.0434  -0.0272 24  LEU A O   
183  C CB  . LEU A 24  ? 0.3749 0.3290 0.6449 -0.0388 0.0268  -0.0129 24  LEU A CB  
184  C CG  . LEU A 24  ? 0.3795 0.3442 0.6246 -0.0389 0.0181  -0.0017 24  LEU A CG  
185  C CD1 . LEU A 24  ? 0.3732 0.3420 0.6364 -0.0390 0.0127  0.0143  24  LEU A CD1 
186  C CD2 . LEU A 24  ? 0.3802 0.3534 0.6089 -0.0353 0.0149  0.0058  24  LEU A CD2 
187  N N   . ASP A 25  ? 0.4635 0.3944 0.7565 -0.0409 0.0502  -0.0524 25  ASP A N   
188  C CA  . ASP A 25  ? 0.5073 0.4291 0.8325 -0.0396 0.0599  -0.0609 25  ASP A CA  
189  C C   . ASP A 25  ? 0.5263 0.4435 0.8354 -0.0405 0.0703  -0.0790 25  ASP A C   
190  O O   . ASP A 25  ? 0.5422 0.4511 0.8739 -0.0402 0.0806  -0.0906 25  ASP A O   
191  C CB  . ASP A 25  ? 0.5730 0.4859 0.9225 -0.0429 0.0618  -0.0673 25  ASP A CB  
192  C CG  . ASP A 25  ? 0.6407 0.5513 0.9637 -0.0489 0.0601  -0.0804 25  ASP A CG  
193  O OD1 . ASP A 25  ? 0.6912 0.6066 0.9770 -0.0504 0.0584  -0.0851 25  ASP A OD1 
194  O OD2 . ASP A 25  ? 0.6687 0.5735 1.0090 -0.0523 0.0596  -0.0845 25  ASP A OD2 
195  N N   . HIS A 26  ? 0.4943 0.4171 0.7661 -0.0415 0.0683  -0.0813 26  HIS A N   
196  C CA  . HIS A 26  ? 0.5180 0.4373 0.7739 -0.0423 0.0785  -0.0965 26  HIS A CA  
197  C C   . HIS A 26  ? 0.5064 0.4274 0.7837 -0.0372 0.0838  -0.0908 26  HIS A C   
198  O O   . HIS A 26  ? 0.4968 0.4258 0.7804 -0.0335 0.0762  -0.0738 26  HIS A O   
199  C CB  . HIS A 26  ? 0.5269 0.4513 0.7392 -0.0450 0.0748  -0.0994 26  HIS A CB  
200  C CG  . HIS A 26  ? 0.5236 0.4440 0.7179 -0.0468 0.0858  -0.1152 26  HIS A CG  
201  N ND1 . HIS A 26  ? 0.5154 0.4376 0.7130 -0.0435 0.0927  -0.1139 26  HIS A ND1 
202  C CD2 . HIS A 26  ? 0.5385 0.4540 0.7110 -0.0519 0.0909  -0.1321 26  HIS A CD2 
203  C CE1 . HIS A 26  ? 0.5201 0.4382 0.6986 -0.0464 0.1028  -0.1294 26  HIS A CE1 
204  N NE2 . HIS A 26  ? 0.5443 0.4585 0.7060 -0.0515 0.1017  -0.1405 26  HIS A NE2 
205  N N   . PRO A 27  ? 0.5443 0.4581 0.8358 -0.0369 0.0971  -0.1046 27  PRO A N   
206  C CA  . PRO A 27  ? 0.5249 0.4402 0.8443 -0.0319 0.1023  -0.0988 27  PRO A CA  
207  C C   . PRO A 27  ? 0.4800 0.4057 0.7837 -0.0291 0.0964  -0.0861 27  PRO A C   
208  O O   . PRO A 27  ? 0.4620 0.3928 0.7898 -0.0248 0.0922  -0.0724 27  PRO A O   
209  C CB  . PRO A 27  ? 0.5666 0.4733 0.8905 -0.0334 0.1191  -0.1195 27  PRO A CB  
210  C CG  . PRO A 27  ? 0.5807 0.4788 0.8990 -0.0385 0.1212  -0.1342 27  PRO A CG  
211  C CD  . PRO A 27  ? 0.5809 0.4850 0.8653 -0.0415 0.1079  -0.1267 27  PRO A CD  
212  N N   . ALA A 28  ? 0.4684 0.3973 0.7327 -0.0317 0.0953  -0.0904 28  ALA A N   
213  C CA  . ALA A 28  ? 0.4426 0.3802 0.6910 -0.0296 0.0906  -0.0807 28  ALA A CA  
214  C C   . ALA A 28  ? 0.4192 0.3653 0.6695 -0.0274 0.0758  -0.0620 28  ALA A C   
215  O O   . ALA A 28  ? 0.3983 0.3517 0.6538 -0.0243 0.0710  -0.0510 28  ALA A O   
216  C CB  . ALA A 28  ? 0.4471 0.3853 0.6548 -0.0330 0.0927  -0.0889 28  ALA A CB  
217  N N   . ILE A 29  ? 0.4087 0.3541 0.6550 -0.0294 0.0687  -0.0589 29  ILE A N   
218  C CA  . ILE A 29  ? 0.3695 0.3228 0.6196 -0.0277 0.0560  -0.0415 29  ILE A CA  
219  C C   . ILE A 29  ? 0.3813 0.3354 0.6710 -0.0240 0.0546  -0.0306 29  ILE A C   
220  O O   . ILE A 29  ? 0.3910 0.3536 0.6868 -0.0212 0.0462  -0.0156 29  ILE A O   
221  C CB  . ILE A 29  ? 0.3480 0.3004 0.5848 -0.0311 0.0503  -0.0414 29  ILE A CB  
222  C CG1 . ILE A 29  ? 0.3317 0.2849 0.5299 -0.0345 0.0497  -0.0498 29  ILE A CG1 
223  C CG2 . ILE A 29  ? 0.3279 0.2884 0.5726 -0.0292 0.0390  -0.0228 29  ILE A CG2 
224  C CD1 . ILE A 29  ? 0.3229 0.2845 0.4988 -0.0328 0.0446  -0.0427 29  ILE A CD1 
225  N N   . VAL A 30  ? 0.4327 0.3781 0.7501 -0.0243 0.0620  -0.0378 30  VAL A N   
226  C CA  . VAL A 30  ? 0.4601 0.4058 0.8179 -0.0209 0.0600  -0.0261 30  VAL A CA  
227  C C   . VAL A 30  ? 0.4609 0.4113 0.8355 -0.0168 0.0616  -0.0208 30  VAL A C   
228  O O   . VAL A 30  ? 0.4347 0.3925 0.8275 -0.0137 0.0530  -0.0040 30  VAL A O   
229  C CB  . VAL A 30  ? 0.4868 0.4211 0.8737 -0.0220 0.0687  -0.0363 30  VAL A CB  
230  C CG1 . VAL A 30  ? 0.4948 0.4295 0.9271 -0.0180 0.0668  -0.0230 30  VAL A CG1 
231  C CG2 . VAL A 30  ? 0.5091 0.4392 0.8830 -0.0264 0.0658  -0.0407 30  VAL A CG2 
232  N N   . ASN A 31  ? 0.4691 0.4156 0.8371 -0.0171 0.0726  -0.0351 31  ASN A N   
233  C CA  . ASN A 31  ? 0.4849 0.4354 0.8708 -0.0136 0.0758  -0.0320 31  ASN A CA  
234  C C   . ASN A 31  ? 0.4929 0.4553 0.8607 -0.0124 0.0635  -0.0179 31  ASN A C   
235  O O   . ASN A 31  ? 0.4683 0.4378 0.8582 -0.0091 0.0574  -0.0052 31  ASN A O   
236  C CB  . ASN A 31  ? 0.5399 0.4844 0.9180 -0.0148 0.0910  -0.0502 31  ASN A CB  
237  C CG  . ASN A 31  ? 0.5954 0.5283 0.9949 -0.0158 0.1048  -0.0659 31  ASN A CG  
238  O OD1 . ASN A 31  ? 0.6373 0.5667 1.0737 -0.0137 0.1052  -0.0618 31  ASN A OD1 
239  N ND2 . ASN A 31  ? 0.6213 0.5482 0.9979 -0.0191 0.1164  -0.0840 31  ASN A ND2 
240  N N   . TYR A 32  ? 0.4619 0.4268 0.7900 -0.0152 0.0597  -0.0207 32  TYR A N   
241  C CA  . TYR A 32  ? 0.4460 0.4212 0.7547 -0.0144 0.0493  -0.0101 32  TYR A CA  
242  C C   . TYR A 32  ? 0.4442 0.4274 0.7651 -0.0126 0.0359  0.0080  32  TYR A C   
243  O O   . TYR A 32  ? 0.4328 0.4251 0.7572 -0.0106 0.0278  0.0188  32  TYR A O   
244  C CB  . TYR A 32  ? 0.4621 0.4371 0.7292 -0.0178 0.0486  -0.0171 32  TYR A CB  
245  C CG  . TYR A 32  ? 0.4497 0.4347 0.6963 -0.0172 0.0380  -0.0073 32  TYR A CG  
246  C CD1 . TYR A 32  ? 0.4422 0.4340 0.6833 -0.0169 0.0262  0.0052  32  TYR A CD1 
247  C CD2 . TYR A 32  ? 0.4472 0.4349 0.6829 -0.0168 0.0403  -0.0104 32  TYR A CD2 
248  C CE1 . TYR A 32  ? 0.4583 0.4592 0.6814 -0.0164 0.0172  0.0126  32  TYR A CE1 
249  C CE2 . TYR A 32  ? 0.4433 0.4396 0.6634 -0.0164 0.0307  -0.0026 32  TYR A CE2 
250  C CZ  . TYR A 32  ? 0.4704 0.4732 0.6834 -0.0162 0.0193  0.0081  32  TYR A CZ  
251  O OH  . TYR A 32  ? 0.4861 0.4971 0.6826 -0.0160 0.0108  0.0138  32  TYR A OH  
252  N N   . ALA A 33  ? 0.4686 0.4489 0.7944 -0.0138 0.0334  0.0115  33  ALA A N   
253  C CA  . ALA A 33  ? 0.4517 0.4396 0.7849 -0.0127 0.0214  0.0293  33  ALA A CA  
254  C C   . ALA A 33  ? 0.4515 0.4415 0.8258 -0.0092 0.0193  0.0406  33  ALA A C   
255  O O   . ALA A 33  ? 0.3959 0.3958 0.7762 -0.0076 0.0081  0.0571  33  ALA A O   
256  C CB  . ALA A 33  ? 0.4342 0.4179 0.7614 -0.0153 0.0207  0.0292  33  ALA A CB  
257  N N   . LYS A 34  ? 0.4916 0.4724 0.8942 -0.0083 0.0301  0.0313  34  LYS A N   
258  C CA  . LYS A 34  ? 0.5760 0.5582 1.0213 -0.0046 0.0298  0.0401  34  LYS A CA  
259  C C   . LYS A 34  ? 0.5770 0.5690 1.0220 -0.0024 0.0245  0.0461  34  LYS A C   
260  O O   . LYS A 34  ? 0.5684 0.5698 1.0288 -0.0003 0.0132  0.0629  34  LYS A O   
261  C CB  . LYS A 34  ? 0.6578 0.6278 1.1308 -0.0040 0.0448  0.0253  34  LYS A CB  
262  C CG  . LYS A 34  ? 0.7645 0.7346 1.2880 0.0001  0.0455  0.0344  34  LYS A CG  
263  C CD  . LYS A 34  ? 0.8518 0.8088 1.4063 0.0003  0.0591  0.0217  34  LYS A CD  
264  C CE  . LYS A 34  ? 0.9214 0.8713 1.4739 0.0000  0.0751  0.0007  34  LYS A CE  
265  N NZ  . LYS A 34  ? 0.9804 0.9358 1.5603 0.0039  0.0770  0.0052  34  LYS A NZ  
266  N N   . ARG A 35  ? 0.5946 0.5850 1.0202 -0.0034 0.0317  0.0327  35  ARG A N   
267  C CA  . ARG A 35  ? 0.6175 0.6166 1.0435 -0.0019 0.0275  0.0368  35  ARG A CA  
268  C C   . ARG A 35  ? 0.5932 0.6041 0.9985 -0.0024 0.0113  0.0511  35  ARG A C   
269  O O   . ARG A 35  ? 0.6400 0.6602 1.0601 -0.0005 0.0024  0.0623  35  ARG A O   
270  C CB  . ARG A 35  ? 0.6622 0.6574 1.0674 -0.0034 0.0382  0.0207  35  ARG A CB  
271  C CG  . ARG A 35  ? 0.7394 0.7249 1.1675 -0.0027 0.0549  0.0069  35  ARG A CG  
272  C CD  . ARG A 35  ? 0.8043 0.7884 1.2173 -0.0038 0.0653  -0.0055 35  ARG A CD  
273  N NE  . ARG A 35  ? 0.9150 0.9003 1.2833 -0.0069 0.0624  -0.0095 35  ARG A NE  
274  C CZ  . ARG A 35  ? 0.9699 0.9479 1.3103 -0.0101 0.0695  -0.0215 35  ARG A CZ  
275  N NH1 . ARG A 35  ? 0.9120 0.8920 1.2162 -0.0124 0.0672  -0.0242 35  ARG A NH1 
276  N NH2 . ARG A 35  ? 1.0231 0.9918 1.3728 -0.0110 0.0787  -0.0311 35  ARG A NH2 
277  N N   . ARG A 36  ? 0.5858 0.5970 0.9580 -0.0049 0.0074  0.0509  36  ARG A N   
278  C CA  . ARG A 36  ? 0.5392 0.5615 0.8888 -0.0056 -0.0061 0.0621  36  ARG A CA  
279  C C   . ARG A 36  ? 0.5156 0.5442 0.8796 -0.0047 -0.0168 0.0801  36  ARG A C   
280  O O   . ARG A 36  ? 0.4684 0.5072 0.8146 -0.0053 -0.0281 0.0903  36  ARG A O   
281  C CB  . ARG A 36  ? 0.6074 0.6280 0.9159 -0.0085 -0.0049 0.0537  36  ARG A CB  
282  C CG  . ARG A 36  ? 0.6761 0.6948 0.9670 -0.0094 0.0013  0.0411  36  ARG A CG  
283  C CD  . ARG A 36  ? 0.7062 0.7290 0.9595 -0.0114 -0.0037 0.0394  36  ARG A CD  
284  N NE  . ARG A 36  ? 0.7183 0.7515 0.9642 -0.0112 -0.0167 0.0528  36  ARG A NE  
285  C CZ  . ARG A 36  ? 0.7520 0.7876 0.9745 -0.0127 -0.0209 0.0556  36  ARG A CZ  
286  N NH1 . ARG A 36  ? 0.7087 0.7382 0.9093 -0.0146 -0.0149 0.0457  36  ARG A NH1 
287  N NH2 . ARG A 36  ? 0.7590 0.8040 0.9795 -0.0125 -0.0313 0.0688  36  ARG A NH2 
288  N N   . LYS A 37  ? 0.5586 0.5814 0.9552 -0.0033 -0.0128 0.0837  37  LYS A N   
289  C CA  . LYS A 37  ? 0.5999 0.6268 1.0131 -0.0026 -0.0211 0.1012  37  LYS A CA  
290  C C   . LYS A 37  ? 0.5818 0.6123 0.9619 -0.0053 -0.0266 0.1058  37  LYS A C   
291  O O   . LYS A 37  ? 0.5141 0.5554 0.8872 -0.0054 -0.0380 0.1216  37  LYS A O   
292  C CB  . LYS A 37  ? 0.6761 0.7148 1.1098 -0.0002 -0.0331 0.1182  37  LYS A CB  
293  C CG  . LYS A 37  ? 0.7290 0.7658 1.1996 0.0027  -0.0286 0.1155  37  LYS A CG  
294  C CD  . LYS A 37  ? 0.8011 0.8504 1.2957 0.0050  -0.0421 0.1341  37  LYS A CD  
295  C CE  . LYS A 37  ? 0.8290 0.8918 1.2922 0.0032  -0.0558 0.1414  37  LYS A CE  
296  N NZ  . LYS A 37  ? 0.8534 0.9285 1.3402 0.0050  -0.0688 0.1566  37  LYS A NZ  
297  N N   . LYS A 38  ? 0.5334 0.5553 0.8935 -0.0077 -0.0182 0.0920  38  LYS A N   
298  C CA  . LYS A 38  ? 0.4972 0.5226 0.8262 -0.0103 -0.0222 0.0946  38  LYS A CA  
299  C C   . LYS A 38  ? 0.4269 0.4417 0.7594 -0.0123 -0.0142 0.0869  38  LYS A C   
300  O O   . LYS A 38  ? 0.4044 0.4086 0.7472 -0.0126 -0.0041 0.0725  38  LYS A O   
301  C CB  . LYS A 38  ? 0.5146 0.5433 0.8069 -0.0116 -0.0226 0.0848  38  LYS A CB  
302  C CG  . LYS A 38  ? 0.5522 0.5934 0.8206 -0.0121 -0.0336 0.0957  38  LYS A CG  
303  C CD  . LYS A 38  ? 0.5905 0.6320 0.8232 -0.0144 -0.0322 0.0877  38  LYS A CD  
304  C CE  . LYS A 38  ? 0.5978 0.6516 0.8077 -0.0149 -0.0419 0.0971  38  LYS A CE  
305  N NZ  . LYS A 38  ? 0.6210 0.6799 0.8344 -0.0155 -0.0465 0.1119  38  LYS A NZ  
306  N N   . ARG A 39  ? 0.3791 0.3970 0.7020 -0.0141 -0.0185 0.0960  39  ARG A N   
307  C CA  . ARG A 39  ? 0.3958 0.4047 0.7189 -0.0167 -0.0121 0.0881  39  ARG A CA  
308  C C   . ARG A 39  ? 0.3620 0.3665 0.6539 -0.0190 -0.0067 0.0700  39  ARG A C   
309  O O   . ARG A 39  ? 0.3530 0.3643 0.6148 -0.0198 -0.0108 0.0703  39  ARG A O   
310  C CB  . ARG A 39  ? 0.4136 0.4283 0.7347 -0.0180 -0.0182 0.1035  39  ARG A CB  
311  C CG  . ARG A 39  ? 0.4729 0.4881 0.8309 -0.0164 -0.0212 0.1201  39  ARG A CG  
312  C CD  . ARG A 39  ? 0.5329 0.5585 0.8842 -0.0173 -0.0293 0.1400  39  ARG A CD  
313  N NE  . ARG A 39  ? 0.6032 0.6237 0.9838 -0.0181 -0.0275 0.1493  39  ARG A NE  
314  C CZ  . ARG A 39  ? 0.6984 0.7210 1.1107 -0.0163 -0.0316 0.1671  39  ARG A CZ  
315  N NH1 . ARG A 39  ? 0.7309 0.7487 1.1683 -0.0175 -0.0296 0.1756  39  ARG A NH1 
316  N NH2 . ARG A 39  ? 0.7253 0.7554 1.1460 -0.0133 -0.0382 0.1772  39  ARG A NH2 
317  N N   . PRO A 40  ? 0.3396 0.3327 0.6376 -0.0205 0.0028  0.0539  40  PRO A N   
318  C CA  . PRO A 40  ? 0.3376 0.3269 0.6065 -0.0230 0.0075  0.0377  40  PRO A CA  
319  C C   . PRO A 40  ? 0.3079 0.3027 0.5477 -0.0253 0.0024  0.0400  40  PRO A C   
320  O O   . PRO A 40  ? 0.2893 0.2865 0.5014 -0.0259 0.0021  0.0336  40  PRO A O   
321  C CB  . PRO A 40  ? 0.3652 0.3421 0.6485 -0.0252 0.0167  0.0234  40  PRO A CB  
322  C CG  . PRO A 40  ? 0.3837 0.3567 0.7069 -0.0229 0.0191  0.0291  40  PRO A CG  
323  C CD  . PRO A 40  ? 0.3847 0.3681 0.7177 -0.0204 0.0091  0.0508  40  PRO A CD  
324  N N   . GLU A 41  ? 0.2948 0.2911 0.5426 -0.0266 -0.0009 0.0495  41  GLU A N   
325  C CA  . GLU A 41  ? 0.3140 0.3153 0.5377 -0.0288 -0.0045 0.0511  41  GLU A CA  
326  C C   . GLU A 41  ? 0.3138 0.3268 0.5150 -0.0271 -0.0111 0.0601  41  GLU A C   
327  O O   . GLU A 41  ? 0.3109 0.3283 0.4888 -0.0285 -0.0130 0.0590  41  GLU A O   
328  C CB  . GLU A 41  ? 0.3118 0.3126 0.5518 -0.0308 -0.0058 0.0599  41  GLU A CB  
329  C CG  . GLU A 41  ? 0.3159 0.3227 0.5772 -0.0286 -0.0106 0.0793  41  GLU A CG  
330  C CD  . GLU A 41  ? 0.3286 0.3284 0.6260 -0.0269 -0.0075 0.0811  41  GLU A CD  
331  O OE1 . GLU A 41  ? 0.3428 0.3461 0.6613 -0.0258 -0.0112 0.0974  41  GLU A OE1 
332  O OE2 . GLU A 41  ? 0.3392 0.3301 0.6439 -0.0267 -0.0010 0.0664  41  GLU A OE2 
333  N N   . LYS A 42  ? 0.3203 0.3384 0.5295 -0.0243 -0.0146 0.0683  42  LYS A N   
334  C CA  . LYS A 42  ? 0.3247 0.3542 0.5151 -0.0229 -0.0216 0.0767  42  LYS A CA  
335  C C   . LYS A 42  ? 0.2974 0.3269 0.4699 -0.0221 -0.0204 0.0658  42  LYS A C   
336  O O   . LYS A 42  ? 0.2906 0.3284 0.4447 -0.0214 -0.0254 0.0692  42  LYS A O   
337  C CB  . LYS A 42  ? 0.3608 0.3968 0.5699 -0.0206 -0.0275 0.0916  42  LYS A CB  
338  C CG  . LYS A 42  ? 0.4241 0.4604 0.6578 -0.0208 -0.0291 0.1056  42  LYS A CG  
339  C CD  . LYS A 42  ? 0.4094 0.4527 0.6287 -0.0225 -0.0323 0.1152  42  LYS A CD  
340  C CE  . LYS A 42  ? 0.4279 0.4757 0.6690 -0.0222 -0.0364 0.1345  42  LYS A CE  
341  N NZ  . LYS A 42  ? 0.4446 0.4975 0.6734 -0.0245 -0.0368 0.1420  42  LYS A NZ  
342  N N   . ILE A 43  ? 0.2849 0.3050 0.4639 -0.0223 -0.0133 0.0530  43  ILE A N   
343  C CA  . ILE A 43  ? 0.2854 0.3045 0.4532 -0.0215 -0.0108 0.0436  43  ILE A CA  
344  C C   . ILE A 43  ? 0.2623 0.2803 0.4013 -0.0234 -0.0091 0.0341  43  ILE A C   
345  O O   . ILE A 43  ? 0.2484 0.2618 0.3820 -0.0257 -0.0063 0.0289  43  ILE A O   
346  C CB  . ILE A 43  ? 0.3027 0.3127 0.4918 -0.0209 -0.0029 0.0351  43  ILE A CB  
347  C CG1 . ILE A 43  ? 0.3081 0.3210 0.5274 -0.0183 -0.0058 0.0459  43  ILE A CG1 
348  C CG2 . ILE A 43  ? 0.3103 0.3172 0.4857 -0.0210 0.0026  0.0230  43  ILE A CG2 
349  C CD1 . ILE A 43  ? 0.3196 0.3241 0.5639 -0.0173 0.0026  0.0380  43  ILE A CD1 
350  N N   . ILE A 44  ? 0.2670 0.2892 0.3895 -0.0225 -0.0110 0.0320  44  ILE A N   
351  C CA  . ILE A 44  ? 0.2604 0.2816 0.3583 -0.0239 -0.0093 0.0237  44  ILE A CA  
352  C C   . ILE A 44  ? 0.2495 0.2614 0.3475 -0.0251 -0.0011 0.0114  44  ILE A C   
353  O O   . ILE A 44  ? 0.2395 0.2486 0.3498 -0.0239 0.0029  0.0085  44  ILE A O   
354  C CB  . ILE A 44  ? 0.2724 0.3009 0.3549 -0.0226 -0.0141 0.0259  44  ILE A CB  
355  C CG1 . ILE A 44  ? 0.2921 0.3303 0.3690 -0.0221 -0.0215 0.0364  44  ILE A CG1 
356  C CG2 . ILE A 44  ? 0.2761 0.3020 0.3376 -0.0238 -0.0114 0.0171  44  ILE A CG2 
357  C CD1 . ILE A 44  ? 0.3025 0.3417 0.3667 -0.0237 -0.0216 0.0369  44  ILE A CD1 
358  N N   . LEU A 45  ? 0.2368 0.2445 0.3211 -0.0275 0.0015  0.0042  45  LEU A N   
359  C CA  . LEU A 45  ? 0.2429 0.2423 0.3225 -0.0294 0.0091  -0.0078 45  LEU A CA  
360  C C   . LEU A 45  ? 0.2505 0.2509 0.3164 -0.0286 0.0110  -0.0112 45  LEU A C   
361  O O   . LEU A 45  ? 0.2439 0.2493 0.2939 -0.0281 0.0065  -0.0084 45  LEU A O   
362  C CB  . LEU A 45  ? 0.2366 0.2330 0.3035 -0.0326 0.0093  -0.0136 45  LEU A CB  
363  C CG  . LEU A 45  ? 0.2493 0.2380 0.3066 -0.0353 0.0164  -0.0263 45  LEU A CG  
364  C CD1 . LEU A 45  ? 0.2726 0.2539 0.3501 -0.0359 0.0235  -0.0328 45  LEU A CD1 
365  C CD2 . LEU A 45  ? 0.2555 0.2436 0.2957 -0.0387 0.0138  -0.0307 45  LEU A CD2 
366  N N   . ASP A 46  ? 0.2607 0.2560 0.3347 -0.0284 0.0185  -0.0175 46  ASP A N   
367  C CA  . ASP A 46  ? 0.2741 0.2696 0.3399 -0.0278 0.0219  -0.0203 46  ASP A CA  
368  C C   . ASP A 46  ? 0.2860 0.2738 0.3493 -0.0298 0.0324  -0.0312 46  ASP A C   
369  O O   . ASP A 46  ? 0.2856 0.2694 0.3679 -0.0293 0.0390  -0.0348 46  ASP A O   
370  C CB  . ASP A 46  ? 0.2748 0.2750 0.3582 -0.0249 0.0194  -0.0138 46  ASP A CB  
371  C CG  . ASP A 46  ? 0.3134 0.3146 0.3917 -0.0244 0.0222  -0.0157 46  ASP A CG  
372  O OD1 . ASP A 46  ? 0.3187 0.3155 0.3824 -0.0261 0.0284  -0.0225 46  ASP A OD1 
373  O OD2 . ASP A 46  ? 0.3381 0.3446 0.4279 -0.0224 0.0179  -0.0100 46  ASP A OD2 
374  N N   . SER A 47  ? 0.3039 0.2899 0.3438 -0.0321 0.0341  -0.0362 47  SER A N   
375  C CA  . SER A 47  ? 0.3343 0.3136 0.3668 -0.0348 0.0438  -0.0468 47  SER A CA  
376  C C   . SER A 47  ? 0.3478 0.3249 0.3924 -0.0336 0.0531  -0.0497 47  SER A C   
377  O O   . SER A 47  ? 0.3556 0.3270 0.4026 -0.0353 0.0628  -0.0588 47  SER A O   
378  C CB  . SER A 47  ? 0.3612 0.3401 0.3657 -0.0376 0.0429  -0.0497 47  SER A CB  
379  O OG  . SER A 47  ? 0.3624 0.3453 0.3579 -0.0362 0.0407  -0.0440 47  SER A OG  
380  N N   . THR A 48  ? 0.3360 0.3180 0.3891 -0.0309 0.0504  -0.0426 48  THR A N   
381  C CA  . THR A 48  ? 0.3434 0.3245 0.4121 -0.0296 0.0585  -0.0441 48  THR A CA  
382  C C   . THR A 48  ? 0.3655 0.3434 0.4615 -0.0285 0.0640  -0.0472 48  THR A C   
383  O O   . THR A 48  ? 0.3556 0.3296 0.4613 -0.0287 0.0752  -0.0538 48  THR A O   
384  C CB  . THR A 48  ? 0.3384 0.3260 0.4125 -0.0273 0.0524  -0.0358 48  THR A CB  
385  O OG1 . THR A 48  ? 0.3532 0.3419 0.4042 -0.0285 0.0506  -0.0349 48  THR A OG1 
386  C CG2 . THR A 48  ? 0.3616 0.3495 0.4567 -0.0259 0.0594  -0.0362 48  THR A CG2 
387  N N   . TYR A 49  ? 0.3690 0.3485 0.4786 -0.0272 0.0569  -0.0423 49  TYR A N   
388  C CA  . TYR A 49  ? 0.3899 0.3662 0.5282 -0.0259 0.0612  -0.0438 49  TYR A CA  
389  C C   . TYR A 49  ? 0.3819 0.3513 0.5168 -0.0285 0.0653  -0.0525 49  TYR A C   
390  O O   . TYR A 49  ? 0.4081 0.3719 0.5626 -0.0284 0.0739  -0.0593 49  TYR A O   
391  C CB  . TYR A 49  ? 0.4317 0.4148 0.5890 -0.0230 0.0504  -0.0312 49  TYR A CB  
392  C CG  . TYR A 49  ? 0.5292 0.5188 0.6968 -0.0206 0.0472  -0.0244 49  TYR A CG  
393  C CD1 . TYR A 49  ? 0.5584 0.5465 0.7456 -0.0194 0.0560  -0.0280 49  TYR A CD1 
394  C CD2 . TYR A 49  ? 0.5957 0.5934 0.7554 -0.0196 0.0354  -0.0150 49  TYR A CD2 
395  C CE1 . TYR A 49  ? 0.5827 0.5772 0.7819 -0.0176 0.0525  -0.0219 49  TYR A CE1 
396  C CE2 . TYR A 49  ? 0.6208 0.6246 0.7909 -0.0180 0.0317  -0.0098 49  TYR A CE2 
397  C CZ  . TYR A 49  ? 0.5980 0.6002 0.7884 -0.0170 0.0398  -0.0131 49  TYR A CZ  
398  O OH  . TYR A 49  ? 0.6347 0.6432 0.8375 -0.0157 0.0357  -0.0083 49  TYR A OH  
399  N N   . HIS A 50  ? 0.3593 0.3289 0.4709 -0.0309 0.0595  -0.0530 50  HIS A N   
400  C CA  . HIS A 50  ? 0.3507 0.3155 0.4638 -0.0333 0.0591  -0.0581 50  HIS A CA  
401  C C   . HIS A 50  ? 0.3849 0.3445 0.4736 -0.0376 0.0647  -0.0707 50  HIS A C   
402  O O   . HIS A 50  ? 0.3652 0.3212 0.4514 -0.0404 0.0633  -0.0761 50  HIS A O   
403  C CB  . HIS A 50  ? 0.3276 0.2981 0.4383 -0.0327 0.0468  -0.0473 50  HIS A CB  
404  C CG  . HIS A 50  ? 0.3049 0.2810 0.4380 -0.0291 0.0408  -0.0348 50  HIS A CG  
405  N ND1 . HIS A 50  ? 0.2791 0.2631 0.4049 -0.0278 0.0303  -0.0234 50  HIS A ND1 
406  C CD2 . HIS A 50  ? 0.3070 0.2823 0.4694 -0.0265 0.0436  -0.0318 50  HIS A CD2 
407  C CE1 . HIS A 50  ? 0.2893 0.2776 0.4372 -0.0249 0.0264  -0.0137 50  HIS A CE1 
408  N NE2 . HIS A 50  ? 0.2987 0.2819 0.4703 -0.0240 0.0339  -0.0180 50  HIS A NE2 
409  N N   . HIS A 51  ? 0.4169 0.3763 0.4880 -0.0385 0.0708  -0.0751 51  HIS A N   
410  C CA  . HIS A 51  ? 0.4746 0.4309 0.5176 -0.0429 0.0747  -0.0848 51  HIS A CA  
411  C C   . HIS A 51  ? 0.5020 0.4505 0.5492 -0.0461 0.0827  -0.0990 51  HIS A C   
412  O O   . HIS A 51  ? 0.5333 0.4800 0.5611 -0.0502 0.0802  -0.1056 51  HIS A O   
413  C CB  . HIS A 51  ? 0.5244 0.4816 0.5526 -0.0430 0.0818  -0.0858 51  HIS A CB  
414  C CG  . HIS A 51  ? 0.5447 0.4995 0.5943 -0.0410 0.0933  -0.0892 51  HIS A CG  
415  N ND1 . HIS A 51  ? 0.6026 0.5512 0.6533 -0.0432 0.1067  -0.1024 51  HIS A ND1 
416  C CD2 . HIS A 51  ? 0.5593 0.5176 0.6308 -0.0371 0.0936  -0.0816 51  HIS A CD2 
417  C CE1 . HIS A 51  ? 0.5863 0.5347 0.6608 -0.0404 0.1153  -0.1022 51  HIS A CE1 
418  N NE2 . HIS A 51  ? 0.5794 0.5338 0.6671 -0.0367 0.1070  -0.0894 51  HIS A NE2 
419  N N   . ALA A 52  ? 0.5137 0.4578 0.5874 -0.0445 0.0920  -0.1041 52  ALA A N   
420  C CA  . ALA A 52  ? 0.5267 0.4627 0.6069 -0.0475 0.1010  -0.1193 52  ALA A CA  
421  C C   . ALA A 52  ? 0.5412 0.4752 0.6244 -0.0497 0.0925  -0.1204 52  ALA A C   
422  O O   . ALA A 52  ? 0.5900 0.5193 0.6597 -0.0544 0.0949  -0.1330 52  ALA A O   
423  C CB  . ALA A 52  ? 0.5220 0.4541 0.6362 -0.0443 0.1114  -0.1226 52  ALA A CB  
424  N N   . ALA A 53  ? 0.4724 0.4108 0.5718 -0.0467 0.0821  -0.1067 53  ALA A N   
425  C CA  . ALA A 53  ? 0.4744 0.4120 0.5802 -0.0484 0.0739  -0.1049 53  ALA A CA  
426  C C   . ALA A 53  ? 0.5004 0.4421 0.5752 -0.0518 0.0649  -0.1037 53  ALA A C   
427  O O   . ALA A 53  ? 0.4984 0.4386 0.5735 -0.0548 0.0598  -0.1065 53  ALA A O   
428  C CB  . ALA A 53  ? 0.4308 0.3726 0.5632 -0.0441 0.0670  -0.0896 53  ALA A CB  
429  N N   . LEU A 54  ? 0.4945 0.4413 0.5443 -0.0515 0.0630  -0.0997 54  LEU A N   
430  C CA  . LEU A 54  ? 0.5183 0.4695 0.5420 -0.0542 0.0541  -0.0973 54  LEU A CA  
431  C C   . LEU A 54  ? 0.5435 0.4909 0.5434 -0.0598 0.0576  -0.1113 54  LEU A C   
432  O O   . LEU A 54  ? 0.5169 0.4675 0.4984 -0.0627 0.0495  -0.1105 54  LEU A O   
433  C CB  . LEU A 54  ? 0.4920 0.4503 0.5019 -0.0512 0.0498  -0.0859 54  LEU A CB  
434  C CG  . LEU A 54  ? 0.4927 0.4568 0.5196 -0.0467 0.0429  -0.0717 54  LEU A CG  
435  C CD1 . LEU A 54  ? 0.4951 0.4654 0.5084 -0.0442 0.0395  -0.0631 54  LEU A CD1 
436  C CD2 . LEU A 54  ? 0.4792 0.4460 0.5104 -0.0476 0.0339  -0.0667 54  LEU A CD2 
437  N N   . ARG A 55  ? 0.5998 0.5410 0.5999 -0.0614 0.0694  -0.1240 55  ARG A N   
438  C CA  . ARG A 55  ? 0.6651 0.6034 0.6384 -0.0670 0.0737  -0.1375 55  ARG A CA  
439  C C   . ARG A 55  ? 0.7297 0.6674 0.6952 -0.0720 0.0652  -0.1436 55  ARG A C   
440  O O   . ARG A 55  ? 0.7781 0.7177 0.7152 -0.0764 0.0616  -0.1484 55  ARG A O   
441  C CB  . ARG A 55  ? 0.7088 0.6394 0.6905 -0.0684 0.0884  -0.1530 55  ARG A CB  
442  C CG  . ARG A 55  ? 0.7564 0.6869 0.7460 -0.0645 0.0995  -0.1507 55  ARG A CG  
443  C CD  . ARG A 55  ? 0.8036 0.7260 0.8105 -0.0654 0.1142  -0.1663 55  ARG A CD  
444  N NE  . ARG A 55  ? 0.8581 0.7801 0.8853 -0.0609 0.1248  -0.1633 55  ARG A NE  
445  C CZ  . ARG A 55  ? 0.9368 0.8618 0.9497 -0.0601 0.1317  -0.1608 55  ARG A CZ  
446  N NH1 . ARG A 55  ? 0.9439 0.8721 0.9206 -0.0636 0.1296  -0.1608 55  ARG A NH1 
447  N NH2 . ARG A 55  ? 0.9630 0.8880 0.9995 -0.0558 0.1405  -0.1576 55  ARG A NH2 
448  N N   . GLN A 56  ? 0.7430 0.6780 0.7348 -0.0715 0.0620  -0.1434 56  GLN A N   
449  C CA  . GLN A 56  ? 0.8258 0.7591 0.8155 -0.0767 0.0554  -0.1511 56  GLN A CA  
450  C C   . GLN A 56  ? 0.7653 0.7055 0.7592 -0.0754 0.0421  -0.1368 56  GLN A C   
451  O O   . GLN A 56  ? 0.7696 0.7099 0.7633 -0.0795 0.0352  -0.1407 56  GLN A O   
452  C CB  . GLN A 56  ? 0.9670 0.8910 0.9825 -0.0785 0.0627  -0.1645 56  GLN A CB  
453  C CG  . GLN A 56  ? 1.0773 0.9969 1.1220 -0.0734 0.0733  -0.1631 56  GLN A CG  
454  C CD  . GLN A 56  ? 1.1270 1.0493 1.2018 -0.0684 0.0675  -0.1468 56  GLN A CD  
455  O OE1 . GLN A 56  ? 1.1771 1.0960 1.2753 -0.0693 0.0646  -0.1471 56  GLN A OE1 
456  N NE2 . GLN A 56  ? 1.1396 1.0678 1.2145 -0.0632 0.0660  -0.1325 56  GLN A NE2 
457  N N   . LEU A 57  ? 0.6760 0.6225 0.6724 -0.0702 0.0386  -0.1210 57  LEU A N   
458  C CA  . LEU A 57  ? 0.6661 0.6193 0.6672 -0.0688 0.0276  -0.1079 57  LEU A CA  
459  C C   . LEU A 57  ? 0.6587 0.6182 0.6316 -0.0710 0.0198  -0.1054 57  LEU A C   
460  O O   . LEU A 57  ? 0.6448 0.6057 0.5969 -0.0707 0.0224  -0.1057 57  LEU A O   
461  C CB  . LEU A 57  ? 0.6566 0.6141 0.6715 -0.0624 0.0273  -0.0931 57  LEU A CB  
462  C CG  . LEU A 57  ? 0.6938 0.6510 0.7389 -0.0601 0.0256  -0.0855 57  LEU A CG  
463  C CD1 . LEU A 57  ? 0.6782 0.6434 0.7264 -0.0551 0.0206  -0.0691 57  LEU A CD1 
464  C CD2 . LEU A 57  ? 0.7322 0.6888 0.7850 -0.0641 0.0199  -0.0878 57  LEU A CD2 
465  N N   . GLU A 58  ? 0.6253 0.5891 0.6003 -0.0729 0.0102  -0.1011 58  GLU A N   
466  C CA  . GLU A 58  ? 0.6223 0.5934 0.5760 -0.0741 0.0016  -0.0958 58  GLU A CA  
467  C C   . GLU A 58  ? 0.5812 0.5576 0.5287 -0.0686 0.0015  -0.0833 58  GLU A C   
468  O O   . GLU A 58  ? 0.5199 0.4979 0.4842 -0.0641 0.0025  -0.0744 58  GLU A O   
469  C CB  . GLU A 58  ? 0.6688 0.6442 0.6327 -0.0762 -0.0077 -0.0918 58  GLU A CB  
470  C CG  . GLU A 58  ? 0.7130 0.6964 0.6587 -0.0771 -0.0169 -0.0857 58  GLU A CG  
471  C CD  . GLU A 58  ? 0.8380 0.8263 0.7943 -0.0797 -0.0259 -0.0827 58  GLU A CD  
472  O OE1 . GLU A 58  ? 0.9065 0.9024 0.8536 -0.0793 -0.0334 -0.0755 58  GLU A OE1 
473  O OE2 . GLU A 58  ? 0.8728 0.8574 0.8485 -0.0820 -0.0253 -0.0874 58  GLU A OE2 
474  N N   . ASP A 59  ? 0.5498 0.5288 0.4731 -0.0694 0.0002  -0.0828 59  ASP A N   
475  C CA  . ASP A 59  ? 0.5513 0.5345 0.4671 -0.0649 0.0005  -0.0728 59  ASP A CA  
476  C C   . ASP A 59  ? 0.4971 0.4765 0.4237 -0.0611 0.0098  -0.0724 59  ASP A C   
477  O O   . ASP A 59  ? 0.4881 0.4709 0.4167 -0.0568 0.0097  -0.0634 59  ASP A O   
478  C CB  . ASP A 59  ? 0.6040 0.5944 0.5280 -0.0615 -0.0069 -0.0604 59  ASP A CB  
479  C CG  . ASP A 59  ? 0.6541 0.6505 0.5659 -0.0635 -0.0160 -0.0570 59  ASP A CG  
480  O OD1 . ASP A 59  ? 0.6532 0.6484 0.5497 -0.0681 -0.0182 -0.0640 59  ASP A OD1 
481  O OD2 . ASP A 59  ? 0.5743 0.5769 0.4919 -0.0603 -0.0208 -0.0473 59  ASP A OD2 
482  N N   . GLY A 60  ? 0.4882 0.4607 0.4222 -0.0629 0.0177  -0.0827 60  GLY A N   
483  C CA  . GLY A 60  ? 0.4804 0.4493 0.4294 -0.0595 0.0265  -0.0828 60  GLY A CA  
484  C C   . GLY A 60  ? 0.5022 0.4733 0.4400 -0.0568 0.0300  -0.0777 60  GLY A C   
485  O O   . GLY A 60  ? 0.4999 0.4718 0.4521 -0.0527 0.0328  -0.0719 60  GLY A O   
486  N N   . GLU A 61  ? 0.5112 0.4836 0.4243 -0.0593 0.0290  -0.0791 61  GLU A N   
487  C CA  . GLU A 61  ? 0.5569 0.5302 0.4586 -0.0578 0.0339  -0.0756 61  GLU A CA  
488  C C   . GLU A 61  ? 0.4876 0.4669 0.3918 -0.0537 0.0275  -0.0628 61  GLU A C   
489  O O   . GLU A 61  ? 0.4752 0.4551 0.3768 -0.0516 0.0314  -0.0587 61  GLU A O   
490  C CB  . GLU A 61  ? 0.6295 0.6025 0.5034 -0.0624 0.0349  -0.0805 61  GLU A CB  
491  C CG  . GLU A 61  ? 0.6863 0.6652 0.5449 -0.0632 0.0239  -0.0726 61  GLU A CG  
492  C CD  . GLU A 61  ? 0.7493 0.7306 0.6097 -0.0655 0.0139  -0.0737 61  GLU A CD  
493  O OE1 . GLU A 61  ? 0.7866 0.7735 0.6390 -0.0654 0.0049  -0.0660 61  GLU A OE1 
494  O OE2 . GLU A 61  ? 0.7927 0.7704 0.6640 -0.0676 0.0152  -0.0822 61  GLU A OE2 
495  N N   . ARG A 62  ? 0.4497 0.4335 0.3582 -0.0528 0.0181  -0.0570 62  ARG A N   
496  C CA  . ARG A 62  ? 0.4384 0.4278 0.3497 -0.0489 0.0128  -0.0464 62  ARG A CA  
497  C C   . ARG A 62  ? 0.3775 0.3692 0.3098 -0.0454 0.0107  -0.0415 62  ARG A C   
498  O O   . ARG A 62  ? 0.3525 0.3488 0.2880 -0.0422 0.0072  -0.0339 62  ARG A O   
499  C CB  . ARG A 62  ? 0.4829 0.4772 0.3819 -0.0500 0.0040  -0.0418 62  ARG A CB  
500  C CG  . ARG A 62  ? 0.5134 0.5101 0.4190 -0.0515 -0.0026 -0.0422 62  ARG A CG  
501  C CD  . ARG A 62  ? 0.5449 0.5467 0.4396 -0.0529 -0.0110 -0.0382 62  ARG A CD  
502  N NE  . ARG A 62  ? 0.5114 0.5192 0.4133 -0.0491 -0.0158 -0.0292 62  ARG A NE  
503  C CZ  . ARG A 62  ? 0.5558 0.5687 0.4518 -0.0490 -0.0223 -0.0243 62  ARG A CZ  
504  N NH1 . ARG A 62  ? 0.5719 0.5846 0.4522 -0.0519 -0.0248 -0.0252 62  ARG A NH1 
505  N NH2 . ARG A 62  ? 0.5024 0.5209 0.4079 -0.0461 -0.0261 -0.0180 62  ARG A NH2 
506  N N   . ARG A 63  ? 0.3565 0.3451 0.3033 -0.0462 0.0129  -0.0456 63  ARG A N   
507  C CA  . ARG A 63  ? 0.3240 0.3155 0.2898 -0.0434 0.0100  -0.0394 63  ARG A CA  
508  C C   . ARG A 63  ? 0.2983 0.2892 0.2775 -0.0402 0.0147  -0.0370 63  ARG A C   
509  O O   . ARG A 63  ? 0.2895 0.2764 0.2674 -0.0404 0.0216  -0.0418 63  ARG A O   
510  C CB  . ARG A 63  ? 0.3212 0.3100 0.2987 -0.0458 0.0093  -0.0432 63  ARG A CB  
511  C CG  . ARG A 63  ? 0.3269 0.3186 0.2948 -0.0486 0.0026  -0.0432 63  ARG A CG  
512  C CD  . ARG A 63  ? 0.3460 0.3341 0.3243 -0.0521 0.0022  -0.0489 63  ARG A CD  
513  N NE  . ARG A 63  ? 0.3436 0.3340 0.3428 -0.0501 0.0003  -0.0415 63  ARG A NE  
514  C CZ  . ARG A 63  ? 0.3414 0.3297 0.3542 -0.0526 -0.0009 -0.0434 63  ARG A CZ  
515  N NH1 . ARG A 63  ? 0.3594 0.3428 0.3678 -0.0572 -0.0003 -0.0543 63  ARG A NH1 
516  N NH2 . ARG A 63  ? 0.3322 0.3235 0.3630 -0.0507 -0.0028 -0.0345 63  ARG A NH2 
517  N N   . GLY A 64  ? 0.2672 0.2628 0.2593 -0.0373 0.0104  -0.0291 64  GLY A N   
518  C CA  . GLY A 64  ? 0.2542 0.2505 0.2615 -0.0344 0.0127  -0.0257 64  GLY A CA  
519  C C   . GLY A 64  ? 0.2390 0.2373 0.2388 -0.0327 0.0136  -0.0241 64  GLY A C   
520  O O   . GLY A 64  ? 0.2378 0.2335 0.2450 -0.0320 0.0194  -0.0267 64  GLY A O   
521  N N   . ARG A 65  ? 0.2380 0.2413 0.2260 -0.0319 0.0081  -0.0198 65  ARG A N   
522  C CA  . ARG A 65  ? 0.2417 0.2468 0.2242 -0.0304 0.0083  -0.0182 65  ARG A CA  
523  C C   . ARG A 65  ? 0.2337 0.2457 0.2198 -0.0278 0.0018  -0.0118 65  ARG A C   
524  O O   . ARG A 65  ? 0.2378 0.2530 0.2140 -0.0271 -0.0015 -0.0101 65  ARG A O   
525  C CB  . ARG A 65  ? 0.2540 0.2575 0.2180 -0.0320 0.0089  -0.0204 65  ARG A CB  
526  C CG  . ARG A 65  ? 0.2892 0.2864 0.2459 -0.0349 0.0159  -0.0271 65  ARG A CG  
527  C CD  . ARG A 65  ? 0.3147 0.3088 0.2809 -0.0342 0.0237  -0.0296 65  ARG A CD  
528  N NE  . ARG A 65  ? 0.3412 0.3374 0.3067 -0.0325 0.0236  -0.0257 65  ARG A NE  
529  C CZ  . ARG A 65  ? 0.3942 0.3894 0.3455 -0.0335 0.0251  -0.0250 65  ARG A CZ  
530  N NH1 . ARG A 65  ? 0.4223 0.4141 0.3587 -0.0366 0.0289  -0.0289 65  ARG A NH1 
531  N NH2 . ARG A 65  ? 0.3613 0.3589 0.3141 -0.0318 0.0231  -0.0207 65  ARG A NH2 
532  N N   . PRO A 66  ? 0.2102 0.2252 0.2110 -0.0264 -0.0003 -0.0080 66  PRO A N   
533  C CA  . PRO A 66  ? 0.2099 0.2324 0.2117 -0.0245 -0.0067 -0.0022 66  PRO A CA  
534  C C   . PRO A 66  ? 0.2138 0.2379 0.2141 -0.0233 -0.0072 -0.0031 66  PRO A C   
535  O O   . PRO A 66  ? 0.2082 0.2381 0.2045 -0.0221 -0.0122 -0.0006 66  PRO A O   
536  C CB  . PRO A 66  ? 0.2029 0.2277 0.2209 -0.0238 -0.0085 0.0025  66  PRO A CB  
537  C CG  . PRO A 66  ? 0.2064 0.2244 0.2362 -0.0244 -0.0019 -0.0018 66  PRO A CG  
538  C CD  . PRO A 66  ? 0.2079 0.2196 0.2249 -0.0266 0.0033  -0.0088 66  PRO A CD  
539  N N   . ASP A 67  ? 0.2185 0.2376 0.2219 -0.0238 -0.0015 -0.0069 67  ASP A N   
540  C CA  . ASP A 67  ? 0.2633 0.2827 0.2662 -0.0231 -0.0009 -0.0079 67  ASP A CA  
541  C C   . ASP A 67  ? 0.2637 0.2844 0.2523 -0.0230 -0.0034 -0.0081 67  ASP A C   
542  O O   . ASP A 67  ? 0.2763 0.2998 0.2659 -0.0220 -0.0062 -0.0079 67  ASP A O   
543  C CB  . ASP A 67  ? 0.2769 0.2905 0.2848 -0.0241 0.0072  -0.0115 67  ASP A CB  
544  C CG  . ASP A 67  ? 0.3332 0.3412 0.3279 -0.0261 0.0127  -0.0151 67  ASP A CG  
545  O OD1 . ASP A 67  ? 0.3418 0.3485 0.3344 -0.0271 0.0125  -0.0162 67  ASP A OD1 
546  O OD2 . ASP A 67  ? 0.4029 0.4081 0.3892 -0.0270 0.0165  -0.0164 67  ASP A OD2 
547  N N   . ILE A 68  ? 0.2567 0.2751 0.2333 -0.0241 -0.0025 -0.0089 68  ILE A N   
548  C CA  . ILE A 68  ? 0.2565 0.2760 0.2221 -0.0238 -0.0048 -0.0083 68  ILE A CA  
549  C C   . ILE A 68  ? 0.2390 0.2652 0.2050 -0.0221 -0.0107 -0.0063 68  ILE A C   
550  O O   . ILE A 68  ? 0.2476 0.2756 0.2119 -0.0210 -0.0124 -0.0068 68  ILE A O   
551  C CB  . ILE A 68  ? 0.2602 0.2771 0.2144 -0.0255 -0.0039 -0.0089 68  ILE A CB  
552  C CG1 . ILE A 68  ? 0.2792 0.2899 0.2292 -0.0277 0.0023  -0.0117 68  ILE A CG1 
553  C CG2 . ILE A 68  ? 0.2704 0.2896 0.2169 -0.0247 -0.0073 -0.0071 68  ILE A CG2 
554  C CD1 . ILE A 68  ? 0.2967 0.3052 0.2338 -0.0302 0.0024  -0.0130 68  ILE A CD1 
555  N N   . VAL A 69  ? 0.2211 0.2511 0.1896 -0.0220 -0.0133 -0.0041 69  VAL A N   
556  C CA  . VAL A 69  ? 0.2293 0.2664 0.1967 -0.0207 -0.0179 -0.0018 69  VAL A CA  
557  C C   . VAL A 69  ? 0.2107 0.2511 0.1840 -0.0197 -0.0203 -0.0025 69  VAL A C   
558  O O   . VAL A 69  ? 0.2144 0.2590 0.1839 -0.0188 -0.0231 -0.0037 69  VAL A O   
559  C CB  . VAL A 69  ? 0.2514 0.2919 0.2216 -0.0212 -0.0197 0.0022  69  VAL A CB  
560  C CG1 . VAL A 69  ? 0.2705 0.3194 0.2383 -0.0201 -0.0238 0.0052  69  VAL A CG1 
561  C CG2 . VAL A 69  ? 0.2623 0.3001 0.2281 -0.0226 -0.0180 0.0020  69  VAL A CG2 
562  N N   . HIS A 70  ? 0.1930 0.2317 0.1768 -0.0201 -0.0195 -0.0021 70  HIS A N   
563  C CA  . HIS A 70  ? 0.1955 0.2381 0.1869 -0.0195 -0.0230 -0.0024 70  HIS A CA  
564  C C   . HIS A 70  ? 0.1904 0.2317 0.1795 -0.0192 -0.0226 -0.0068 70  HIS A C   
565  O O   . HIS A 70  ? 0.1901 0.2364 0.1776 -0.0188 -0.0270 -0.0086 70  HIS A O   
566  C CB  . HIS A 70  ? 0.1925 0.2333 0.1987 -0.0198 -0.0216 -0.0010 70  HIS A CB  
567  C CG  . HIS A 70  ? 0.2055 0.2511 0.2219 -0.0196 -0.0263 -0.0007 70  HIS A CG  
568  N ND1 . HIS A 70  ? 0.2128 0.2554 0.2429 -0.0198 -0.0235 -0.0022 70  HIS A ND1 
569  C CD2 . HIS A 70  ? 0.2136 0.2671 0.2292 -0.0194 -0.0337 0.0011  70  HIS A CD2 
570  C CE1 . HIS A 70  ? 0.2201 0.2687 0.2588 -0.0198 -0.0298 -0.0014 70  HIS A CE1 
571  N NE2 . HIS A 70  ? 0.2137 0.2691 0.2427 -0.0197 -0.0364 0.0004  70  HIS A NE2 
572  N N   . ILE A 71  ? 0.1946 0.2291 0.1835 -0.0197 -0.0173 -0.0085 71  ILE A N   
573  C CA  . ILE A 71  ? 0.2113 0.2433 0.2012 -0.0196 -0.0160 -0.0114 71  ILE A CA  
574  C C   . ILE A 71  ? 0.1989 0.2326 0.1795 -0.0186 -0.0179 -0.0127 71  ILE A C   
575  O O   . ILE A 71  ? 0.1926 0.2281 0.1757 -0.0181 -0.0201 -0.0159 71  ILE A O   
576  C CB  . ILE A 71  ? 0.2598 0.2846 0.2520 -0.0206 -0.0092 -0.0114 71  ILE A CB  
577  C CG1 . ILE A 71  ? 0.3335 0.3574 0.3379 -0.0213 -0.0064 -0.0110 71  ILE A CG1 
578  C CG2 . ILE A 71  ? 0.2815 0.3043 0.2768 -0.0205 -0.0084 -0.0130 71  ILE A CG2 
579  C CD1 . ILE A 71  ? 0.3810 0.3985 0.3847 -0.0226 0.0018  -0.0111 71  ILE A CD1 
580  N N   . CYS A 72  ? 0.1849 0.2187 0.1564 -0.0185 -0.0174 -0.0108 72  CYS A N   
581  C CA  . CYS A 72  ? 0.1986 0.2352 0.1638 -0.0173 -0.0191 -0.0117 72  CYS A CA  
582  C C   . CYS A 72  ? 0.2050 0.2488 0.1701 -0.0165 -0.0232 -0.0140 72  CYS A C   
583  O O   . CYS A 72  ? 0.1957 0.2409 0.1603 -0.0154 -0.0238 -0.0177 72  CYS A O   
584  C CB  . CYS A 72  ? 0.2033 0.2401 0.1610 -0.0175 -0.0185 -0.0088 72  CYS A CB  
585  S SG  . CYS A 72  ? 0.2377 0.2672 0.1913 -0.0188 -0.0149 -0.0071 72  CYS A SG  
586  N N   . LEU A 73  ? 0.1931 0.2416 0.1581 -0.0170 -0.0258 -0.0116 73  LEU A N   
587  C CA  . LEU A 73  ? 0.2063 0.2628 0.1679 -0.0166 -0.0298 -0.0129 73  LEU A CA  
588  C C   . LEU A 73  ? 0.2124 0.2705 0.1794 -0.0170 -0.0330 -0.0175 73  LEU A C   
589  O O   . LEU A 73  ? 0.2309 0.2942 0.1936 -0.0168 -0.0356 -0.0220 73  LEU A O   
590  C CB  . LEU A 73  ? 0.2015 0.2628 0.1622 -0.0172 -0.0321 -0.0070 73  LEU A CB  
591  C CG  . LEU A 73  ? 0.2062 0.2680 0.1620 -0.0172 -0.0299 -0.0028 73  LEU A CG  
592  C CD1 . LEU A 73  ? 0.2161 0.2825 0.1737 -0.0179 -0.0322 0.0037  73  LEU A CD1 
593  C CD2 . LEU A 73  ? 0.2140 0.2796 0.1619 -0.0162 -0.0289 -0.0051 73  LEU A CD2 
594  N N   . LEU A 74  ? 0.2169 0.2712 0.1941 -0.0178 -0.0328 -0.0170 74  LEU A N   
595  C CA  . LEU A 74  ? 0.2353 0.2909 0.2201 -0.0184 -0.0361 -0.0217 74  LEU A CA  
596  C C   . LEU A 74  ? 0.2479 0.3005 0.2323 -0.0179 -0.0343 -0.0280 74  LEU A C   
597  O O   . LEU A 74  ? 0.2489 0.3053 0.2335 -0.0182 -0.0378 -0.0341 74  LEU A O   
598  C CB  . LEU A 74  ? 0.2326 0.2841 0.2312 -0.0193 -0.0347 -0.0199 74  LEU A CB  
599  C CG  . LEU A 74  ? 0.2354 0.2911 0.2400 -0.0198 -0.0381 -0.0149 74  LEU A CG  
600  C CD1 . LEU A 74  ? 0.2438 0.2956 0.2645 -0.0204 -0.0358 -0.0143 74  LEU A CD1 
601  C CD2 . LEU A 74  ? 0.2482 0.3133 0.2503 -0.0204 -0.0464 -0.0156 74  LEU A CD2 
602  N N   . ASN A 75  ? 0.2292 0.2749 0.2139 -0.0172 -0.0289 -0.0264 75  ASN A N   
603  C CA  . ASN A 75  ? 0.2449 0.2866 0.2318 -0.0163 -0.0266 -0.0302 75  ASN A CA  
604  C C   . ASN A 75  ? 0.2505 0.2971 0.2298 -0.0150 -0.0278 -0.0343 75  ASN A C   
605  O O   . ASN A 75  ? 0.2937 0.3409 0.2770 -0.0147 -0.0287 -0.0412 75  ASN A O   
606  C CB  . ASN A 75  ? 0.2450 0.2797 0.2317 -0.0160 -0.0215 -0.0254 75  ASN A CB  
607  C CG  . ASN A 75  ? 0.2772 0.3062 0.2730 -0.0172 -0.0184 -0.0234 75  ASN A CG  
608  O OD1 . ASN A 75  ? 0.2656 0.2941 0.2720 -0.0180 -0.0194 -0.0265 75  ASN A OD1 
609  N ND2 . ASN A 75  ? 0.3516 0.3757 0.3435 -0.0175 -0.0140 -0.0186 75  ASN A ND2 
610  N N   . ALA A 76  ? 0.2100 0.2607 0.1796 -0.0144 -0.0277 -0.0307 76  ALA A N   
611  C CA  . ALA A 76  ? 0.2224 0.2780 0.1854 -0.0132 -0.0273 -0.0340 76  ALA A CA  
612  C C   . ALA A 76  ? 0.2224 0.2856 0.1808 -0.0139 -0.0310 -0.0399 76  ALA A C   
613  O O   . ALA A 76  ? 0.2204 0.2853 0.1783 -0.0132 -0.0302 -0.0474 76  ALA A O   
614  C CB  . ALA A 76  ? 0.2290 0.2870 0.1847 -0.0127 -0.0258 -0.0278 76  ALA A CB  
615  N N   . LEU A 77  ? 0.2275 0.2954 0.1825 -0.0154 -0.0350 -0.0364 77  LEU A N   
616  C CA  . LEU A 77  ? 0.2430 0.3198 0.1902 -0.0165 -0.0395 -0.0400 77  LEU A CA  
617  C C   . LEU A 77  ? 0.2505 0.3274 0.2037 -0.0177 -0.0432 -0.0488 77  LEU A C   
618  O O   . LEU A 77  ? 0.2343 0.3179 0.1799 -0.0187 -0.0461 -0.0552 77  LEU A O   
619  C CB  . LEU A 77  ? 0.2499 0.3320 0.1936 -0.0176 -0.0434 -0.0317 77  LEU A CB  
620  C CG  . LEU A 77  ? 0.2648 0.3492 0.2016 -0.0168 -0.0403 -0.0242 77  LEU A CG  
621  C CD1 . LEU A 77  ? 0.2659 0.3531 0.2043 -0.0179 -0.0437 -0.0151 77  LEU A CD1 
622  C CD2 . LEU A 77  ? 0.3028 0.3949 0.2273 -0.0165 -0.0388 -0.0271 77  LEU A CD2 
623  N N   . ASP A 78  ? 0.2552 0.3252 0.2220 -0.0182 -0.0433 -0.0488 78  ASP A N   
624  C CA  . ASP A 78  ? 0.2646 0.3340 0.2407 -0.0197 -0.0469 -0.0567 78  ASP A CA  
625  C C   . ASP A 78  ? 0.2394 0.3030 0.2214 -0.0187 -0.0427 -0.0647 78  ASP A C   
626  O O   . ASP A 78  ? 0.2334 0.2957 0.2243 -0.0200 -0.0450 -0.0729 78  ASP A O   
627  C CB  . ASP A 78  ? 0.2977 0.3638 0.2868 -0.0210 -0.0489 -0.0518 78  ASP A CB  
628  C CG  . ASP A 78  ? 0.3704 0.4440 0.3559 -0.0221 -0.0546 -0.0456 78  ASP A CG  
629  O OD1 . ASP A 78  ? 0.3759 0.4585 0.3535 -0.0235 -0.0613 -0.0488 78  ASP A OD1 
630  O OD2 . ASP A 78  ? 0.4234 0.4943 0.4137 -0.0216 -0.0526 -0.0376 78  ASP A OD2 
631  N N   . SER A 79  ? 0.2379 0.2985 0.2164 -0.0164 -0.0370 -0.0627 79  SER A N   
632  C CA  . SER A 79  ? 0.2340 0.2887 0.2211 -0.0149 -0.0328 -0.0685 79  SER A CA  
633  C C   . SER A 79  ? 0.2560 0.3149 0.2411 -0.0153 -0.0340 -0.0810 79  SER A C   
634  O O   . SER A 79  ? 0.2583 0.3258 0.2297 -0.0160 -0.0362 -0.0840 79  SER A O   
635  C CB  . SER A 79  ? 0.2288 0.2804 0.2139 -0.0123 -0.0274 -0.0625 79  SER A CB  
636  O OG  . SER A 79  ? 0.2134 0.2718 0.1860 -0.0114 -0.0264 -0.0622 79  SER A OG  
637  N N   . ILE A 80  ? 0.2627 0.3155 0.2617 -0.0147 -0.0316 -0.0882 80  ILE A N   
638  C CA  . ILE A 80  ? 0.2754 0.3309 0.2737 -0.0146 -0.0308 -0.1015 80  ILE A CA  
639  C C   . ILE A 80  ? 0.2793 0.3393 0.2662 -0.0122 -0.0259 -0.1011 80  ILE A C   
640  O O   . ILE A 80  ? 0.2991 0.3665 0.2746 -0.0128 -0.0259 -0.1095 80  ILE A O   
641  C CB  . ILE A 80  ? 0.2809 0.3277 0.2999 -0.0141 -0.0283 -0.1085 80  ILE A CB  
642  C CG1 . ILE A 80  ? 0.2896 0.3331 0.3208 -0.0171 -0.0331 -0.1101 80  ILE A CG1 
643  C CG2 . ILE A 80  ? 0.3027 0.3510 0.3229 -0.0132 -0.0252 -0.1227 80  ILE A CG2 
644  C CD1 . ILE A 80  ? 0.2940 0.3277 0.3486 -0.0168 -0.0303 -0.1136 80  ILE A CD1 
645  N N   . LEU A 81  ? 0.2641 0.3202 0.2542 -0.0096 -0.0217 -0.0915 81  LEU A N   
646  C CA  . LEU A 81  ? 0.2642 0.3250 0.2463 -0.0074 -0.0171 -0.0901 81  LEU A CA  
647  C C   . LEU A 81  ? 0.2707 0.3419 0.2333 -0.0088 -0.0191 -0.0890 81  LEU A C   
648  O O   . LEU A 81  ? 0.2672 0.3447 0.2218 -0.0081 -0.0155 -0.0949 81  LEU A O   
649  C CB  . LEU A 81  ? 0.2524 0.3089 0.2387 -0.0055 -0.0149 -0.0777 81  LEU A CB  
650  C CG  . LEU A 81  ? 0.2468 0.3065 0.2323 -0.0028 -0.0099 -0.0759 81  LEU A CG  
651  C CD1 . LEU A 81  ? 0.2487 0.3047 0.2496 -0.0003 -0.0055 -0.0837 81  LEU A CD1 
652  C CD2 . LEU A 81  ? 0.2393 0.2963 0.2256 -0.0022 -0.0103 -0.0628 81  LEU A CD2 
653  N N   . ASN A 82  ? 0.2601 0.3332 0.2161 -0.0109 -0.0242 -0.0812 82  ASN A N   
654  C CA  . ASN A 82  ? 0.2773 0.3602 0.2164 -0.0124 -0.0267 -0.0784 82  ASN A CA  
655  C C   . ASN A 82  ? 0.2871 0.3771 0.2169 -0.0145 -0.0295 -0.0900 82  ASN A C   
656  O O   . ASN A 82  ? 0.2797 0.3784 0.1951 -0.0147 -0.0277 -0.0918 82  ASN A O   
657  C CB  . ASN A 82  ? 0.2829 0.3659 0.2205 -0.0140 -0.0319 -0.0679 82  ASN A CB  
658  C CG  . ASN A 82  ? 0.2906 0.3827 0.2134 -0.0149 -0.0332 -0.0613 82  ASN A CG  
659  O OD1 . ASN A 82  ? 0.2988 0.3947 0.2152 -0.0136 -0.0284 -0.0598 82  ASN A OD1 
660  N ND2 . ASN A 82  ? 0.2922 0.3884 0.2112 -0.0170 -0.0395 -0.0571 82  ASN A ND2 
661  N N   . LYS A 83  ? 0.2937 0.3804 0.2319 -0.0162 -0.0337 -0.0978 83  LYS A N   
662  C CA  . LYS A 83  ? 0.3236 0.4169 0.2534 -0.0189 -0.0380 -0.1099 83  LYS A CA  
663  C C   . LYS A 83  ? 0.3301 0.4256 0.2558 -0.0177 -0.0314 -0.1228 83  LYS A C   
664  O O   . LYS A 83  ? 0.3228 0.4267 0.2338 -0.0199 -0.0330 -0.1322 83  LYS A O   
665  C CB  . LYS A 83  ? 0.3358 0.4240 0.2799 -0.0210 -0.0438 -0.1153 83  LYS A CB  
666  C CG  . LYS A 83  ? 0.3504 0.4377 0.2993 -0.0223 -0.0498 -0.1035 83  LYS A CG  
667  C CD  . LYS A 83  ? 0.3749 0.4600 0.3371 -0.0250 -0.0564 -0.1087 83  LYS A CD  
668  C CE  . LYS A 83  ? 0.3828 0.4657 0.3544 -0.0256 -0.0599 -0.0969 83  LYS A CE  
669  N NZ  . LYS A 83  ? 0.4056 0.4971 0.3639 -0.0263 -0.0646 -0.0876 83  LYS A NZ  
670  N N   . GLU A 84  ? 0.3293 0.4174 0.2681 -0.0144 -0.0241 -0.1231 84  GLU A N   
671  C CA  . GLU A 84  ? 0.3528 0.4421 0.2925 -0.0126 -0.0165 -0.1349 84  GLU A CA  
672  C C   . GLU A 84  ? 0.3468 0.4435 0.2735 -0.0108 -0.0104 -0.1291 84  GLU A C   
673  O O   . GLU A 84  ? 0.3553 0.4527 0.2854 -0.0085 -0.0025 -0.1362 84  GLU A O   
674  C CB  . GLU A 84  ? 0.3562 0.4340 0.3203 -0.0098 -0.0123 -0.1370 84  GLU A CB  
675  C CG  . GLU A 84  ? 0.3709 0.4417 0.3495 -0.0118 -0.0170 -0.1443 84  GLU A CG  
676  C CD  . GLU A 84  ? 0.4229 0.4957 0.4015 -0.0136 -0.0166 -0.1636 84  GLU A CD  
677  O OE1 . GLU A 84  ? 0.4105 0.4841 0.3887 -0.0172 -0.0238 -0.1698 84  GLU A OE1 
678  O OE2 . GLU A 84  ? 0.4594 0.5333 0.4390 -0.0115 -0.0091 -0.1728 84  GLU A OE2 
679  N N   . ASP A 85  ? 0.3427 0.4446 0.2572 -0.0118 -0.0136 -0.1160 85  ASP A N   
680  C CA  . ASP A 85  ? 0.3364 0.4455 0.2404 -0.0105 -0.0081 -0.1089 85  ASP A CA  
681  C C   . ASP A 85  ? 0.3348 0.4384 0.2542 -0.0067 -0.0010 -0.1051 85  ASP A C   
682  O O   . ASP A 85  ? 0.3214 0.4303 0.2380 -0.0050 0.0063  -0.1057 85  ASP A O   
683  C CB  . ASP A 85  ? 0.3754 0.4954 0.2607 -0.0121 -0.0049 -0.1187 85  ASP A CB  
684  C CG  . ASP A 85  ? 0.3786 0.5071 0.2527 -0.0113 0.0010  -0.1100 85  ASP A CG  
685  O OD1 . ASP A 85  ? 0.3789 0.5075 0.2525 -0.0114 -0.0022 -0.0951 85  ASP A OD1 
686  O OD2 . ASP A 85  ? 0.3668 0.5010 0.2352 -0.0104 0.0094  -0.1182 85  ASP A OD2 
687  N N   . ARG A 86  ? 0.3267 0.4203 0.2624 -0.0054 -0.0032 -0.0995 86  ARG A N   
688  C CA  . ARG A 86  ? 0.3216 0.4102 0.2723 -0.0021 0.0016  -0.0945 86  ARG A CA  
689  C C   . ARG A 86  ? 0.2877 0.3740 0.2392 -0.0021 -0.0013 -0.0793 86  ARG A C   
690  O O   . ARG A 86  ? 0.2594 0.3403 0.2237 0.0000  0.0003  -0.0742 86  ARG A O   
691  C CB  . ARG A 86  ? 0.3349 0.4135 0.3052 -0.0006 0.0019  -0.1000 86  ARG A CB  
692  C CG  . ARG A 86  ? 0.3725 0.4513 0.3476 -0.0002 0.0056  -0.1165 86  ARG A CG  
693  C CD  . ARG A 86  ? 0.4126 0.4954 0.3917 0.0027  0.0143  -0.1217 86  ARG A CD  
694  N NE  . ARG A 86  ? 0.4538 0.5341 0.4435 0.0036  0.0189  -0.1381 86  ARG A NE  
695  C CZ  . ARG A 86  ? 0.4832 0.5660 0.4809 0.0064  0.0277  -0.1460 86  ARG A CZ  
696  N NH1 . ARG A 86  ? 0.4936 0.5817 0.4909 0.0086  0.0326  -0.1380 86  ARG A NH1 
697  N NH2 . ARG A 86  ? 0.4689 0.5488 0.4766 0.0070  0.0319  -0.1625 86  ARG A NH2 
698  N N   . LEU A 87  ? 0.2744 0.3643 0.2131 -0.0046 -0.0060 -0.0724 87  LEU A N   
699  C CA  . LEU A 87  ? 0.2625 0.3496 0.2024 -0.0051 -0.0088 -0.0597 87  LEU A CA  
700  C C   . LEU A 87  ? 0.2693 0.3646 0.1959 -0.0067 -0.0095 -0.0525 87  LEU A C   
701  O O   . LEU A 87  ? 0.3018 0.4032 0.2167 -0.0086 -0.0120 -0.0545 87  LEU A O   
702  C CB  . LEU A 87  ? 0.2631 0.3429 0.2076 -0.0066 -0.0143 -0.0579 87  LEU A CB  
703  C CG  . LEU A 87  ? 0.2678 0.3444 0.2122 -0.0075 -0.0168 -0.0465 87  LEU A CG  
704  C CD1 . LEU A 87  ? 0.2664 0.3377 0.2197 -0.0058 -0.0143 -0.0417 87  LEU A CD1 
705  C CD2 . LEU A 87  ? 0.2711 0.3428 0.2184 -0.0093 -0.0213 -0.0455 87  LEU A CD2 
706  N N   . ARG A 88  ? 0.2504 0.3457 0.1798 -0.0061 -0.0079 -0.0436 88  ARG A N   
707  C CA  . ARG A 88  ? 0.2579 0.3583 0.1795 -0.0077 -0.0093 -0.0344 88  ARG A CA  
708  C C   . ARG A 88  ? 0.2515 0.3449 0.1798 -0.0084 -0.0125 -0.0261 88  ARG A C   
709  O O   . ARG A 88  ? 0.2639 0.3521 0.2010 -0.0071 -0.0113 -0.0251 88  ARG A O   
710  C CB  . ARG A 88  ? 0.2674 0.3759 0.1864 -0.0069 -0.0034 -0.0327 88  ARG A CB  
711  C CG  . ARG A 88  ? 0.2856 0.4022 0.1951 -0.0067 0.0009  -0.0413 88  ARG A CG  
712  C CD  . ARG A 88  ? 0.3118 0.4345 0.2058 -0.0093 -0.0030 -0.0410 88  ARG A CD  
713  N NE  . ARG A 88  ? 0.3135 0.4446 0.1957 -0.0096 0.0012  -0.0498 88  ARG A NE  
714  C CZ  . ARG A 88  ? 0.3274 0.4578 0.2061 -0.0099 0.0004  -0.0623 88  ARG A CZ  
715  N NH1 . ARG A 88  ? 0.3137 0.4354 0.2017 -0.0097 -0.0044 -0.0670 88  ARG A NH1 
716  N NH2 . ARG A 88  ? 0.3621 0.5014 0.2269 -0.0108 0.0042  -0.0702 88  ARG A NH2 
717  N N   . VAL A 89  ? 0.2514 0.3445 0.1759 -0.0103 -0.0165 -0.0205 89  VAL A N   
718  C CA  . VAL A 89  ? 0.2517 0.3375 0.1822 -0.0112 -0.0189 -0.0149 89  VAL A CA  
719  C C   . VAL A 89  ? 0.2423 0.3315 0.1709 -0.0127 -0.0197 -0.0063 89  VAL A C   
720  O O   . VAL A 89  ? 0.2549 0.3513 0.1771 -0.0135 -0.0202 -0.0036 89  VAL A O   
721  C CB  . VAL A 89  ? 0.2700 0.3498 0.2032 -0.0119 -0.0224 -0.0174 89  VAL A CB  
722  C CG1 . VAL A 89  ? 0.2878 0.3726 0.2157 -0.0133 -0.0261 -0.0172 89  VAL A CG1 
723  C CG2 . VAL A 89  ? 0.2858 0.3580 0.2246 -0.0128 -0.0232 -0.0126 89  VAL A CG2 
724  N N   . TYR A 90  ? 0.2155 0.2998 0.1497 -0.0132 -0.0195 -0.0019 90  TYR A N   
725  C CA  . TYR A 90  ? 0.2159 0.3018 0.1519 -0.0148 -0.0198 0.0055  90  TYR A CA  
726  C C   . TYR A 90  ? 0.2111 0.2884 0.1522 -0.0161 -0.0216 0.0069  90  TYR A C   
727  O O   . TYR A 90  ? 0.2210 0.2926 0.1638 -0.0156 -0.0214 0.0034  90  TYR A O   
728  C CB  . TYR A 90  ? 0.2202 0.3098 0.1591 -0.0145 -0.0168 0.0078  90  TYR A CB  
729  C CG  . TYR A 90  ? 0.2345 0.3316 0.1704 -0.0128 -0.0130 0.0046  90  TYR A CG  
730  C CD1 . TYR A 90  ? 0.2480 0.3433 0.1854 -0.0107 -0.0115 -0.0025 90  TYR A CD1 
731  C CD2 . TYR A 90  ? 0.2500 0.3560 0.1818 -0.0133 -0.0102 0.0085  90  TYR A CD2 
732  C CE1 . TYR A 90  ? 0.2511 0.3529 0.1873 -0.0090 -0.0069 -0.0068 90  TYR A CE1 
733  C CE2 . TYR A 90  ? 0.2644 0.3777 0.1925 -0.0118 -0.0053 0.0046  90  TYR A CE2 
734  C CZ  . TYR A 90  ? 0.2698 0.3807 0.2004 -0.0096 -0.0036 -0.0039 90  TYR A CZ  
735  O OH  . TYR A 90  ? 0.2785 0.3959 0.2072 -0.0080 0.0021  -0.0093 90  TYR A OH  
736  N N   . VAL A 91  ? 0.2050 0.2820 0.1493 -0.0177 -0.0226 0.0123  91  VAL A N   
737  C CA  . VAL A 91  ? 0.2127 0.2821 0.1622 -0.0193 -0.0231 0.0129  91  VAL A CA  
738  C C   . VAL A 91  ? 0.2253 0.2963 0.1793 -0.0209 -0.0225 0.0174  91  VAL A C   
739  O O   . VAL A 91  ? 0.2156 0.2922 0.1717 -0.0213 -0.0222 0.0229  91  VAL A O   
740  C CB  . VAL A 91  ? 0.2077 0.2739 0.1608 -0.0199 -0.0245 0.0140  91  VAL A CB  
741  C CG1 . VAL A 91  ? 0.2143 0.2724 0.1729 -0.0216 -0.0236 0.0132  91  VAL A CG1 
742  C CG2 . VAL A 91  ? 0.2117 0.2772 0.1622 -0.0187 -0.0255 0.0096  91  VAL A CG2 
743  N N   . HIS A 92  ? 0.2270 0.2936 0.1827 -0.0219 -0.0226 0.0154  92  HIS A N   
744  C CA  . HIS A 92  ? 0.2160 0.2824 0.1778 -0.0242 -0.0229 0.0183  92  HIS A CA  
745  C C   . HIS A 92  ? 0.2320 0.2899 0.1958 -0.0263 -0.0235 0.0155  92  HIS A C   
746  O O   . HIS A 92  ? 0.2345 0.2872 0.1932 -0.0263 -0.0236 0.0110  92  HIS A O   
747  C CB  . HIS A 92  ? 0.2084 0.2774 0.1705 -0.0241 -0.0233 0.0175  92  HIS A CB  
748  C CG  . HIS A 92  ? 0.2123 0.2796 0.1806 -0.0271 -0.0250 0.0184  92  HIS A CG  
749  N ND1 . HIS A 92  ? 0.2091 0.2704 0.1751 -0.0290 -0.0274 0.0146  92  HIS A ND1 
750  C CD2 . HIS A 92  ? 0.2036 0.2746 0.1805 -0.0288 -0.0248 0.0226  92  HIS A CD2 
751  C CE1 . HIS A 92  ? 0.2108 0.2721 0.1836 -0.0320 -0.0290 0.0154  92  HIS A CE1 
752  N NE2 . HIS A 92  ? 0.2074 0.2743 0.1881 -0.0319 -0.0274 0.0204  92  HIS A NE2 
753  N N   . THR A 93  ? 0.2149 0.2713 0.1868 -0.0282 -0.0233 0.0182  93  THR A N   
754  C CA  . THR A 93  ? 0.2147 0.2631 0.1900 -0.0300 -0.0226 0.0144  93  THR A CA  
755  C C   . THR A 93  ? 0.2352 0.2802 0.2124 -0.0332 -0.0236 0.0112  93  THR A C   
756  O O   . THR A 93  ? 0.2207 0.2701 0.2004 -0.0341 -0.0252 0.0135  93  THR A O   
757  C CB  . THR A 93  ? 0.2129 0.2605 0.1989 -0.0302 -0.0217 0.0185  93  THR A CB  
758  O OG1 . THR A 93  ? 0.2045 0.2547 0.1998 -0.0320 -0.0221 0.0232  93  THR A OG1 
759  C CG2 . THR A 93  ? 0.2052 0.2580 0.1900 -0.0277 -0.0223 0.0229  93  THR A CG2 
760  N N   . ARG A 94  ? 0.2405 0.2778 0.2174 -0.0351 -0.0224 0.0055  94  ARG A N   
761  C CA  . ARG A 94  ? 0.2572 0.2907 0.2336 -0.0388 -0.0237 0.0006  94  ARG A CA  
762  C C   . ARG A 94  ? 0.2579 0.2927 0.2483 -0.0411 -0.0245 0.0032  94  ARG A C   
763  O O   . ARG A 94  ? 0.2621 0.2957 0.2536 -0.0444 -0.0268 -0.0003 94  ARG A O   
764  C CB  . ARG A 94  ? 0.2727 0.2977 0.2449 -0.0405 -0.0208 -0.0069 94  ARG A CB  
765  C CG  . ARG A 94  ? 0.2833 0.3037 0.2682 -0.0406 -0.0170 -0.0079 94  ARG A CG  
766  C CD  . ARG A 94  ? 0.3133 0.3264 0.3015 -0.0445 -0.0151 -0.0163 94  ARG A CD  
767  N NE  . ARG A 94  ? 0.3458 0.3555 0.3174 -0.0461 -0.0143 -0.0233 94  ARG A NE  
768  C CZ  . ARG A 94  ? 0.3881 0.3947 0.3520 -0.0503 -0.0155 -0.0305 94  ARG A CZ  
769  N NH1 . ARG A 94  ? 0.3894 0.3944 0.3362 -0.0513 -0.0150 -0.0345 94  ARG A NH1 
770  N NH2 . ARG A 94  ? 0.4004 0.4058 0.3737 -0.0535 -0.0175 -0.0335 94  ARG A NH2 
771  N N   . ASN A 95  ? 0.2478 0.2853 0.2489 -0.0396 -0.0231 0.0098  95  ASN A N   
772  C CA  . ASN A 95  ? 0.2537 0.2925 0.2701 -0.0417 -0.0234 0.0140  95  ASN A CA  
773  C C   . ASN A 95  ? 0.2422 0.2906 0.2609 -0.0404 -0.0242 0.0227  95  ASN A C   
774  O O   . ASN A 95  ? 0.2425 0.2933 0.2744 -0.0415 -0.0236 0.0290  95  ASN A O   
775  C CB  . ASN A 95  ? 0.2631 0.2974 0.2929 -0.0415 -0.0208 0.0160  95  ASN A CB  
776  C CG  . ASN A 95  ? 0.2969 0.3215 0.3271 -0.0431 -0.0185 0.0062  95  ASN A CG  
777  O OD1 . ASN A 95  ? 0.3029 0.3236 0.3287 -0.0463 -0.0192 -0.0018 95  ASN A OD1 
778  N ND2 . ASN A 95  ? 0.3000 0.3212 0.3354 -0.0412 -0.0156 0.0066  95  ASN A ND2 
779  N N   . ASP A 96  ? 0.2354 0.2890 0.2426 -0.0384 -0.0251 0.0229  96  ASP A N   
780  C CA  . ASP A 96  ? 0.2338 0.2968 0.2425 -0.0373 -0.0249 0.0293  96  ASP A CA  
781  C C   . ASP A 96  ? 0.2232 0.2913 0.2344 -0.0353 -0.0225 0.0375  96  ASP A C   
782  O O   . ASP A 96  ? 0.2266 0.3003 0.2465 -0.0361 -0.0212 0.0448  96  ASP A O   
783  C CB  . ASP A 96  ? 0.2478 0.3131 0.2672 -0.0404 -0.0265 0.0302  96  ASP A CB  
784  C CG  . ASP A 96  ? 0.2852 0.3507 0.2991 -0.0415 -0.0300 0.0246  96  ASP A CG  
785  O OD1 . ASP A 96  ? 0.2840 0.3502 0.2862 -0.0389 -0.0303 0.0224  96  ASP A OD1 
786  O OD2 . ASP A 96  ? 0.2839 0.3492 0.3064 -0.0449 -0.0328 0.0231  96  ASP A OD2 
787  N N   . TYR A 97  ? 0.2170 0.2837 0.2205 -0.0330 -0.0222 0.0366  97  TYR A N   
788  C CA  . TYR A 97  ? 0.2115 0.2848 0.2118 -0.0308 -0.0213 0.0434  97  TYR A CA  
789  C C   . TYR A 97  ? 0.2103 0.2868 0.1966 -0.0281 -0.0212 0.0392  97  TYR A C   
790  O O   . TYR A 97  ? 0.2137 0.2849 0.1947 -0.0277 -0.0221 0.0321  97  TYR A O   
791  C CB  . TYR A 97  ? 0.2277 0.2978 0.2334 -0.0305 -0.0220 0.0464  97  TYR A CB  
792  C CG  . TYR A 97  ? 0.2288 0.2960 0.2514 -0.0328 -0.0215 0.0518  97  TYR A CG  
793  C CD1 . TYR A 97  ? 0.2382 0.2962 0.2700 -0.0349 -0.0213 0.0456  97  TYR A CD1 
794  C CD2 . TYR A 97  ? 0.2344 0.3082 0.2643 -0.0330 -0.0211 0.0632  97  TYR A CD2 
795  C CE1 . TYR A 97  ? 0.2441 0.2989 0.2938 -0.0372 -0.0207 0.0493  97  TYR A CE1 
796  C CE2 . TYR A 97  ? 0.2479 0.3186 0.2961 -0.0351 -0.0205 0.0688  97  TYR A CE2 
797  C CZ  . TYR A 97  ? 0.2503 0.3111 0.3096 -0.0372 -0.0203 0.0613  97  TYR A CZ  
798  O OH  . TYR A 97  ? 0.2662 0.3232 0.3457 -0.0395 -0.0196 0.0657  97  TYR A OH  
799  N N   . VAL A 98  ? 0.2072 0.2924 0.1875 -0.0266 -0.0200 0.0435  98  VAL A N   
800  C CA  . VAL A 98  ? 0.2085 0.2963 0.1769 -0.0242 -0.0198 0.0385  98  VAL A CA  
801  C C   . VAL A 98  ? 0.2295 0.3213 0.1928 -0.0233 -0.0210 0.0420  98  VAL A C   
802  O O   . VAL A 98  ? 0.2305 0.3275 0.1966 -0.0241 -0.0209 0.0505  98  VAL A O   
803  C CB  . VAL A 98  ? 0.2210 0.3159 0.1860 -0.0232 -0.0169 0.0379  98  VAL A CB  
804  C CG1 . VAL A 98  ? 0.2326 0.3310 0.1865 -0.0207 -0.0160 0.0327  98  VAL A CG1 
805  C CG2 . VAL A 98  ? 0.2127 0.3042 0.1835 -0.0239 -0.0172 0.0345  98  VAL A CG2 
806  N N   . ILE A 99  ? 0.2244 0.3140 0.1808 -0.0218 -0.0226 0.0359  99  ILE A N   
807  C CA  . ILE A 99  ? 0.2463 0.3403 0.1964 -0.0210 -0.0248 0.0371  99  ILE A CA  
808  C C   . ILE A 99  ? 0.2515 0.3507 0.1902 -0.0195 -0.0235 0.0311  99  ILE A C   
809  O O   . ILE A 99  ? 0.2169 0.3115 0.1545 -0.0184 -0.0228 0.0234  99  ILE A O   
810  C CB  . ILE A 99  ? 0.2427 0.3297 0.1973 -0.0209 -0.0278 0.0341  99  ILE A CB  
811  C CG1 . ILE A 99  ? 0.2556 0.3364 0.2231 -0.0223 -0.0279 0.0383  99  ILE A CG1 
812  C CG2 . ILE A 99  ? 0.2474 0.3402 0.1967 -0.0204 -0.0314 0.0355  99  ILE A CG2 
813  C CD1 . ILE A 99  ? 0.2586 0.3317 0.2326 -0.0222 -0.0289 0.0343  99  ILE A CD1 
814  N N   . TYR A 100 ? 0.2648 0.3736 0.1955 -0.0196 -0.0230 0.0350  100 TYR A N   
815  C CA  . TYR A 100 ? 0.2745 0.3894 0.1935 -0.0185 -0.0214 0.0288  100 TYR A CA  
816  C C   . TYR A 100 ? 0.2736 0.3901 0.1862 -0.0187 -0.0264 0.0263  100 TYR A C   
817  O O   . TYR A 100 ? 0.2805 0.3995 0.1943 -0.0198 -0.0304 0.0339  100 TYR A O   
818  C CB  . TYR A 100 ? 0.2989 0.4241 0.2116 -0.0190 -0.0174 0.0347  100 TYR A CB  
819  C CG  . TYR A 100 ? 0.3075 0.4325 0.2289 -0.0192 -0.0127 0.0380  100 TYR A CG  
820  C CD1 . TYR A 100 ? 0.3232 0.4490 0.2452 -0.0177 -0.0080 0.0315  100 TYR A CD1 
821  C CD2 . TYR A 100 ? 0.3095 0.4335 0.2408 -0.0209 -0.0131 0.0477  100 TYR A CD2 
822  C CE1 . TYR A 100 ? 0.3183 0.4449 0.2501 -0.0180 -0.0044 0.0348  100 TYR A CE1 
823  C CE2 . TYR A 100 ? 0.3066 0.4308 0.2473 -0.0215 -0.0093 0.0503  100 TYR A CE2 
824  C CZ  . TYR A 100 ? 0.3249 0.4507 0.2657 -0.0201 -0.0053 0.0440  100 TYR A CZ  
825  O OH  . TYR A 100 ? 0.3164 0.4435 0.2683 -0.0208 -0.0024 0.0469  100 TYR A OH  
826  N N   . ILE A 101 ? 0.2781 0.3932 0.1860 -0.0176 -0.0265 0.0160  101 ILE A N   
827  C CA  . ILE A 101 ? 0.2826 0.3975 0.1877 -0.0180 -0.0318 0.0116  101 ILE A CA  
828  C C   . ILE A 101 ? 0.2957 0.4177 0.1881 -0.0178 -0.0308 0.0035  101 ILE A C   
829  O O   . ILE A 101 ? 0.2899 0.4099 0.1821 -0.0164 -0.0263 -0.0047 101 ILE A O   
830  C CB  . ILE A 101 ? 0.2819 0.3862 0.1971 -0.0172 -0.0326 0.0058  101 ILE A CB  
831  C CG1 . ILE A 101 ? 0.2823 0.3796 0.2082 -0.0175 -0.0319 0.0120  101 ILE A CG1 
832  C CG2 . ILE A 101 ? 0.2857 0.3895 0.2016 -0.0177 -0.0379 0.0014  101 ILE A CG2 
833  C CD1 . ILE A 101 ? 0.2728 0.3601 0.2068 -0.0171 -0.0317 0.0074  101 ILE A CD1 
834  N N   . LYS A 102 ? 0.3318 0.4624 0.2139 -0.0194 -0.0350 0.0059  102 LYS A N   
835  C CA  . LYS A 102 ? 0.3509 0.4880 0.2196 -0.0198 -0.0346 -0.0037 102 LYS A CA  
836  C C   . LYS A 102 ? 0.3275 0.4578 0.2022 -0.0193 -0.0373 -0.0152 102 LYS A C   
837  O O   . LYS A 102 ? 0.3105 0.4354 0.1949 -0.0197 -0.0425 -0.0135 102 LYS A O   
838  C CB  . LYS A 102 ? 0.4054 0.5541 0.2600 -0.0222 -0.0395 0.0024  102 LYS A CB  
839  C CG  . LYS A 102 ? 0.4625 0.6187 0.3100 -0.0226 -0.0345 0.0127  102 LYS A CG  
840  C CD  . LYS A 102 ? 0.5808 0.7494 0.4124 -0.0251 -0.0389 0.0203  102 LYS A CD  
841  C CE  . LYS A 102 ? 0.6270 0.8028 0.4535 -0.0256 -0.0329 0.0320  102 LYS A CE  
842  N NZ  . LYS A 102 ? 0.7074 0.8947 0.5201 -0.0282 -0.0385 0.0430  102 LYS A NZ  
843  N N   . PRO A 103 ? 0.3432 0.4733 0.2143 -0.0184 -0.0330 -0.0272 103 PRO A N   
844  C CA  . PRO A 103 ? 0.3521 0.4746 0.2320 -0.0178 -0.0345 -0.0379 103 PRO A CA  
845  C C   . PRO A 103 ? 0.3399 0.4641 0.2190 -0.0200 -0.0431 -0.0407 103 PRO A C   
846  O O   . PRO A 103 ? 0.3171 0.4336 0.2087 -0.0199 -0.0455 -0.0445 103 PRO A O   
847  C CB  . PRO A 103 ? 0.3762 0.5009 0.2508 -0.0168 -0.0284 -0.0501 103 PRO A CB  
848  C CG  . PRO A 103 ? 0.3870 0.5179 0.2548 -0.0159 -0.0216 -0.0445 103 PRO A CG  
849  C CD  . PRO A 103 ? 0.3792 0.5159 0.2403 -0.0177 -0.0257 -0.0310 103 PRO A CD  
850  N N   . GLU A 104 ? 0.3460 0.4807 0.2112 -0.0223 -0.0480 -0.0380 104 GLU A N   
851  C CA  . GLU A 104 ? 0.3802 0.5180 0.2454 -0.0247 -0.0576 -0.0403 104 GLU A CA  
852  C C   . GLU A 104 ? 0.3635 0.4982 0.2414 -0.0250 -0.0633 -0.0284 104 GLU A C   
853  O O   . GLU A 104 ? 0.3563 0.4940 0.2375 -0.0269 -0.0718 -0.0283 104 GLU A O   
854  C CB  . GLU A 104 ? 0.4235 0.5746 0.2679 -0.0274 -0.0617 -0.0417 104 GLU A CB  
855  C CG  . GLU A 104 ? 0.4710 0.6301 0.3055 -0.0279 -0.0616 -0.0268 104 GLU A CG  
856  C CD  . GLU A 104 ? 0.5505 0.7139 0.3736 -0.0268 -0.0517 -0.0258 104 GLU A CD  
857  O OE1 . GLU A 104 ? 0.6711 0.8455 0.4782 -0.0286 -0.0528 -0.0184 104 GLU A OE1 
858  O OE2 . GLU A 104 ? 0.5032 0.6596 0.3335 -0.0243 -0.0431 -0.0316 104 GLU A OE2 
859  N N   . THR A 105 ? 0.3534 0.4830 0.2397 -0.0233 -0.0592 -0.0185 105 THR A N   
860  C CA  . THR A 105 ? 0.3468 0.4736 0.2462 -0.0235 -0.0638 -0.0083 105 THR A CA  
861  C C   . THR A 105 ? 0.3408 0.4604 0.2555 -0.0236 -0.0670 -0.0137 105 THR A C   
862  O O   . THR A 105 ? 0.3389 0.4503 0.2602 -0.0225 -0.0623 -0.0211 105 THR A O   
863  C CB  . THR A 105 ? 0.3485 0.4690 0.2554 -0.0219 -0.0577 -0.0001 105 THR A CB  
864  O OG1 . THR A 105 ? 0.3311 0.4581 0.2266 -0.0219 -0.0542 0.0054  105 THR A OG1 
865  C CG2 . THR A 105 ? 0.3813 0.4987 0.3028 -0.0220 -0.0612 0.0093  105 THR A CG2 
866  N N   . ARG A 106 ? 0.3721 0.4953 0.2942 -0.0251 -0.0750 -0.0090 106 ARG A N   
867  C CA  . ARG A 106 ? 0.3712 0.4880 0.3113 -0.0252 -0.0774 -0.0119 106 ARG A CA  
868  C C   . ARG A 106 ? 0.3419 0.4528 0.2966 -0.0239 -0.0748 -0.0020 106 ARG A C   
869  O O   . ARG A 106 ? 0.3349 0.4508 0.2944 -0.0244 -0.0797 0.0076  106 ARG A O   
870  C CB  . ARG A 106 ? 0.4304 0.5553 0.3728 -0.0277 -0.0882 -0.0130 106 ARG A CB  
871  C CG  . ARG A 106 ? 0.4690 0.5884 0.4325 -0.0280 -0.0906 -0.0159 106 ARG A CG  
872  C CD  . ARG A 106 ? 0.5595 0.6883 0.5275 -0.0306 -0.1026 -0.0153 106 ARG A CD  
873  N NE  . ARG A 106 ? 0.6193 0.7436 0.6109 -0.0310 -0.1046 -0.0163 106 ARG A NE  
874  C CZ  . ARG A 106 ? 0.6625 0.7833 0.6727 -0.0297 -0.1033 -0.0074 106 ARG A CZ  
875  N NH1 . ARG A 106 ? 0.6611 0.7807 0.6698 -0.0279 -0.0995 0.0027  106 ARG A NH1 
876  N NH2 . ARG A 106 ? 0.6349 0.7532 0.6668 -0.0303 -0.1052 -0.0090 106 ARG A NH2 
877  N N   . LEU A 107 ? 0.3256 0.4262 0.2871 -0.0224 -0.0669 -0.0043 107 LEU A N   
878  C CA  . LEU A 107 ? 0.3406 0.4349 0.3145 -0.0214 -0.0632 0.0029  107 LEU A CA  
879  C C   . LEU A 107 ? 0.2901 0.3832 0.2819 -0.0220 -0.0670 0.0038  107 LEU A C   
880  O O   . LEU A 107 ? 0.3091 0.4006 0.3058 -0.0226 -0.0682 -0.0035 107 LEU A O   
881  C CB  . LEU A 107 ? 0.3499 0.4340 0.3247 -0.0202 -0.0546 -0.0012 107 LEU A CB  
882  C CG  . LEU A 107 ? 0.4365 0.5174 0.4068 -0.0194 -0.0490 0.0033  107 LEU A CG  
883  C CD1 . LEU A 107 ? 0.4369 0.5075 0.4155 -0.0189 -0.0429 0.0017  107 LEU A CD1 
884  C CD2 . LEU A 107 ? 0.4481 0.5339 0.4196 -0.0197 -0.0514 0.0130  107 LEU A CD2 
885  N N   . PRO A 108 ? 0.2562 0.3494 0.2607 -0.0216 -0.0680 0.0124  108 PRO A N   
886  C CA  . PRO A 108 ? 0.2589 0.3498 0.2841 -0.0217 -0.0695 0.0133  108 PRO A CA  
887  C C   . PRO A 108 ? 0.2328 0.3141 0.2643 -0.0214 -0.0619 0.0057  108 PRO A C   
888  O O   . PRO A 108 ? 0.2261 0.3000 0.2526 -0.0206 -0.0541 0.0043  108 PRO A O   
889  C CB  . PRO A 108 ? 0.2683 0.3578 0.3051 -0.0208 -0.0678 0.0227  108 PRO A CB  
890  C CG  . PRO A 108 ? 0.2743 0.3704 0.2968 -0.0210 -0.0710 0.0292  108 PRO A CG  
891  C CD  . PRO A 108 ? 0.2639 0.3590 0.2662 -0.0211 -0.0673 0.0217  108 PRO A CD  
892  N N   . ARG A 109 ? 0.2333 0.3152 0.2756 -0.0223 -0.0648 0.0012  109 ARG A N   
893  C CA  . ARG A 109 ? 0.2488 0.3223 0.2997 -0.0222 -0.0577 -0.0044 109 ARG A CA  
894  C C   . ARG A 109 ? 0.2408 0.3085 0.3072 -0.0214 -0.0511 -0.0003 109 ARG A C   
895  O O   . ARG A 109 ? 0.2546 0.3140 0.3215 -0.0211 -0.0423 -0.0032 109 ARG A O   
896  C CB  . ARG A 109 ? 0.2760 0.3525 0.3368 -0.0238 -0.0630 -0.0098 109 ARG A CB  
897  C CG  . ARG A 109 ? 0.3180 0.3969 0.3646 -0.0247 -0.0663 -0.0176 109 ARG A CG  
898  C CD  . ARG A 109 ? 0.3982 0.4880 0.4344 -0.0261 -0.0767 -0.0180 109 ARG A CD  
899  N NE  . ARG A 109 ? 0.4834 0.5749 0.4983 -0.0253 -0.0751 -0.0184 109 ARG A NE  
900  C CZ  . ARG A 109 ? 0.4511 0.5401 0.4545 -0.0251 -0.0717 -0.0262 109 ARG A CZ  
901  N NH1 . ARG A 109 ? 0.4102 0.4950 0.4035 -0.0234 -0.0647 -0.0244 109 ARG A NH1 
902  N NH2 . ARG A 109 ? 0.4555 0.5451 0.4605 -0.0265 -0.0744 -0.0357 109 ARG A NH2 
903  N N   . ASN A 110 ? 0.2315 0.3038 0.3112 -0.0211 -0.0554 0.0063  110 ASN A N   
904  C CA  . ASN A 110 ? 0.2357 0.3025 0.3326 -0.0202 -0.0485 0.0091  110 ASN A CA  
905  C C   . ASN A 110 ? 0.2279 0.2896 0.3148 -0.0193 -0.0424 0.0113  110 ASN A C   
906  O O   . ASN A 110 ? 0.2243 0.2904 0.3034 -0.0191 -0.0470 0.0165  110 ASN A O   
907  C CB  . ASN A 110 ? 0.2366 0.3100 0.3556 -0.0200 -0.0552 0.0155  110 ASN A CB  
908  C CG  . ASN A 110 ? 0.2462 0.3135 0.3854 -0.0188 -0.0467 0.0172  110 ASN A CG  
909  O OD1 . ASN A 110 ? 0.2473 0.3118 0.3870 -0.0178 -0.0433 0.0210  110 ASN A OD1 
910  N ND2 . ASN A 110 ? 0.2527 0.3178 0.4097 -0.0190 -0.0424 0.0140  110 ASN A ND2 
911  N N   . TYR A 111 ? 0.2106 0.2633 0.2986 -0.0191 -0.0321 0.0077  111 TYR A N   
912  C CA  . TYR A 111 ? 0.2034 0.2508 0.2826 -0.0189 -0.0264 0.0082  111 TYR A CA  
913  C C   . TYR A 111 ? 0.2104 0.2600 0.3014 -0.0181 -0.0287 0.0150  111 TYR A C   
914  O O   . TYR A 111 ? 0.2152 0.2648 0.2971 -0.0181 -0.0293 0.0178  111 TYR A O   
915  C CB  . TYR A 111 ? 0.2121 0.2504 0.2942 -0.0192 -0.0153 0.0030  111 TYR A CB  
916  C CG  . TYR A 111 ? 0.2167 0.2491 0.2919 -0.0195 -0.0093 0.0021  111 TYR A CG  
917  C CD1 . TYR A 111 ? 0.2307 0.2620 0.2858 -0.0201 -0.0099 0.0012  111 TYR A CD1 
918  C CD2 . TYR A 111 ? 0.2239 0.2522 0.3142 -0.0193 -0.0034 0.0019  111 TYR A CD2 
919  C CE1 . TYR A 111 ? 0.2256 0.2518 0.2750 -0.0208 -0.0052 -0.0004 111 TYR A CE1 
920  C CE2 . TYR A 111 ? 0.2360 0.2584 0.3202 -0.0200 0.0021  -0.0006 111 TYR A CE2 
921  C CZ  . TYR A 111 ? 0.2409 0.2625 0.3041 -0.0210 0.0007  -0.0017 111 TYR A CZ  
922  O OH  . TYR A 111 ? 0.2819 0.2984 0.3399 -0.0221 0.0048  -0.0043 111 TYR A OH  
923  N N   . ASN A 112 ? 0.2065 0.2577 0.3205 -0.0174 -0.0294 0.0179  112 ASN A N   
924  C CA  . ASN A 112 ? 0.2250 0.2773 0.3538 -0.0165 -0.0308 0.0249  112 ASN A CA  
925  C C   . ASN A 112 ? 0.2322 0.2939 0.3543 -0.0165 -0.0419 0.0334  112 ASN A C   
926  O O   . ASN A 112 ? 0.2190 0.2812 0.3437 -0.0161 -0.0428 0.0398  112 ASN A O   
927  C CB  . ASN A 112 ? 0.2403 0.2923 0.3983 -0.0155 -0.0286 0.0264  112 ASN A CB  
928  C CG  . ASN A 112 ? 0.2496 0.2921 0.4128 -0.0156 -0.0156 0.0181  112 ASN A CG  
929  O OD1 . ASN A 112 ? 0.2663 0.3016 0.4209 -0.0160 -0.0081 0.0142  112 ASN A OD1 
930  N ND2 . ASN A 112 ? 0.2445 0.2872 0.4200 -0.0157 -0.0128 0.0150  112 ASN A ND2 
931  N N   . ARG A 113 ? 0.2414 0.3108 0.3552 -0.0172 -0.0501 0.0335  113 ARG A N   
932  C CA  . ARG A 113 ? 0.2623 0.3412 0.3648 -0.0177 -0.0598 0.0406  113 ARG A CA  
933  C C   . ARG A 113 ? 0.2398 0.3170 0.3185 -0.0181 -0.0569 0.0389  113 ARG A C   
934  O O   . ARG A 113 ? 0.2276 0.3097 0.3005 -0.0182 -0.0606 0.0463  113 ARG A O   
935  C CB  . ARG A 113 ? 0.3196 0.4074 0.4176 -0.0188 -0.0693 0.0394  113 ARG A CB  
936  C CG  . ARG A 113 ? 0.4446 0.5407 0.5624 -0.0187 -0.0788 0.0480  113 ARG A CG  
937  C CD  . ARG A 113 ? 0.5743 0.6811 0.6814 -0.0206 -0.0903 0.0475  113 ARG A CD  
938  N NE  . ARG A 113 ? 0.6645 0.7787 0.7936 -0.0209 -0.0996 0.0530  113 ARG A NE  
939  C CZ  . ARG A 113 ? 0.7033 0.8186 0.8447 -0.0219 -0.1021 0.0469  113 ARG A CZ  
940  N NH1 . ARG A 113 ? 0.6466 0.7543 0.7830 -0.0222 -0.0942 0.0357  113 ARG A NH1 
941  N NH2 . ARG A 113 ? 0.7162 0.8401 0.8771 -0.0225 -0.1124 0.0531  113 ARG A NH2 
942  N N   . PHE A 114 ? 0.2359 0.3066 0.3026 -0.0184 -0.0502 0.0298  114 PHE A N   
943  C CA  . PHE A 114 ? 0.2385 0.3070 0.2863 -0.0187 -0.0467 0.0279  114 PHE A CA  
944  C C   . PHE A 114 ? 0.2302 0.2945 0.2840 -0.0185 -0.0426 0.0325  114 PHE A C   
945  O O   . PHE A 114 ? 0.2320 0.2994 0.2761 -0.0188 -0.0439 0.0367  114 PHE A O   
946  C CB  . PHE A 114 ? 0.2313 0.2931 0.2694 -0.0189 -0.0406 0.0184  114 PHE A CB  
947  C CG  . PHE A 114 ? 0.2286 0.2871 0.2513 -0.0191 -0.0364 0.0164  114 PHE A CG  
948  C CD1 . PHE A 114 ? 0.2394 0.3037 0.2469 -0.0192 -0.0397 0.0171  114 PHE A CD1 
949  C CD2 . PHE A 114 ? 0.2303 0.2804 0.2542 -0.0194 -0.0292 0.0136  114 PHE A CD2 
950  C CE1 . PHE A 114 ? 0.2548 0.3166 0.2514 -0.0193 -0.0359 0.0158  114 PHE A CE1 
951  C CE2 . PHE A 114 ? 0.2299 0.2778 0.2414 -0.0199 -0.0266 0.0123  114 PHE A CE2 
952  C CZ  . PHE A 114 ? 0.2379 0.2916 0.2369 -0.0197 -0.0300 0.0137  114 PHE A CZ  
953  N N   . ILE A 115 ? 0.2219 0.2792 0.2924 -0.0181 -0.0370 0.0311  115 ILE A N   
954  C CA  . ILE A 115 ? 0.2276 0.2799 0.3055 -0.0182 -0.0327 0.0336  115 ILE A CA  
955  C C   . ILE A 115 ? 0.2348 0.2939 0.3220 -0.0178 -0.0392 0.0453  115 ILE A C   
956  O O   . ILE A 115 ? 0.2425 0.3013 0.3269 -0.0183 -0.0385 0.0495  115 ILE A O   
957  C CB  . ILE A 115 ? 0.2375 0.2812 0.3325 -0.0180 -0.0249 0.0286  115 ILE A CB  
958  C CG1 . ILE A 115 ? 0.2458 0.2824 0.3283 -0.0189 -0.0174 0.0182  115 ILE A CG1 
959  C CG2 . ILE A 115 ? 0.2487 0.2882 0.3575 -0.0180 -0.0218 0.0318  115 ILE A CG2 
960  C CD1 . ILE A 115 ? 0.2505 0.2840 0.3142 -0.0202 -0.0152 0.0151  115 ILE A CD1 
961  N N   . GLY A 116 ? 0.2314 0.2972 0.3303 -0.0171 -0.0459 0.0512  116 GLY A N   
962  C CA  . GLY A 116 ? 0.2518 0.3256 0.3589 -0.0168 -0.0535 0.0641  116 GLY A CA  
963  C C   . GLY A 116 ? 0.2503 0.3314 0.3352 -0.0178 -0.0577 0.0686  116 GLY A C   
964  O O   . GLY A 116 ? 0.2668 0.3508 0.3547 -0.0180 -0.0594 0.0784  116 GLY A O   
965  N N   . LEU A 117 ? 0.2374 0.3211 0.3016 -0.0185 -0.0585 0.0614  117 LEU A N   
966  C CA  . LEU A 117 ? 0.2436 0.3340 0.2859 -0.0193 -0.0607 0.0632  117 LEU A CA  
967  C C   . LEU A 117 ? 0.2461 0.3311 0.2831 -0.0197 -0.0539 0.0625  117 LEU A C   
968  O O   . LEU A 117 ? 0.2524 0.3429 0.2824 -0.0203 -0.0551 0.0699  117 LEU A O   
969  C CB  . LEU A 117 ? 0.2456 0.3383 0.2711 -0.0197 -0.0620 0.0535  117 LEU A CB  
970  C CG  . LEU A 117 ? 0.2602 0.3594 0.2628 -0.0204 -0.0627 0.0526  117 LEU A CG  
971  C CD1 . LEU A 117 ? 0.2863 0.3972 0.2831 -0.0213 -0.0699 0.0634  117 LEU A CD1 
972  C CD2 . LEU A 117 ? 0.2691 0.3683 0.2600 -0.0206 -0.0627 0.0412  117 LEU A CD2 
973  N N   . MET A 118 ? 0.2269 0.3016 0.2674 -0.0196 -0.0467 0.0538  118 MET A N   
974  C CA  . MET A 118 ? 0.2249 0.2944 0.2613 -0.0203 -0.0411 0.0519  118 MET A CA  
975  C C   . MET A 118 ? 0.2209 0.2892 0.2738 -0.0206 -0.0407 0.0609  118 MET A C   
976  O O   . MET A 118 ? 0.2281 0.2975 0.2769 -0.0216 -0.0393 0.0645  118 MET A O   
977  C CB  . MET A 118 ? 0.2217 0.2812 0.2573 -0.0205 -0.0345 0.0408  118 MET A CB  
978  C CG  . MET A 118 ? 0.2160 0.2760 0.2354 -0.0203 -0.0341 0.0329  118 MET A CG  
979  S SD  . MET A 118 ? 0.2532 0.3194 0.2524 -0.0206 -0.0351 0.0329  118 MET A SD  
980  C CE  . MET A 118 ? 0.2508 0.3283 0.2447 -0.0201 -0.0423 0.0379  118 MET A CE  
981  N N   . GLU A 119 ? 0.2269 0.2927 0.3005 -0.0199 -0.0414 0.0641  119 GLU A N   
982  C CA  . GLU A 119 ? 0.2559 0.3206 0.3493 -0.0199 -0.0416 0.0736  119 GLU A CA  
983  C C   . GLU A 119 ? 0.2654 0.3408 0.3536 -0.0202 -0.0479 0.0872  119 GLU A C   
984  O O   . GLU A 119 ? 0.2579 0.3332 0.3508 -0.0211 -0.0464 0.0939  119 GLU A O   
985  C CB  . GLU A 119 ? 0.2727 0.3336 0.3906 -0.0185 -0.0414 0.0743  119 GLU A CB  
986  C CG  . GLU A 119 ? 0.2983 0.3478 0.4208 -0.0187 -0.0327 0.0610  119 GLU A CG  
987  C CD  . GLU A 119 ? 0.3188 0.3632 0.4646 -0.0174 -0.0294 0.0581  119 GLU A CD  
988  O OE1 . GLU A 119 ? 0.3287 0.3635 0.4763 -0.0180 -0.0208 0.0465  119 GLU A OE1 
989  O OE2 . GLU A 119 ? 0.3113 0.3615 0.4732 -0.0160 -0.0352 0.0671  119 GLU A OE2 
990  N N   . ASN A 120 ? 0.2592 0.3441 0.3369 -0.0198 -0.0548 0.0909  120 ASN A N   
991  C CA  . ASN A 120 ? 0.2745 0.3708 0.3436 -0.0205 -0.0607 0.1037  120 ASN A CA  
992  C C   . ASN A 120 ? 0.2613 0.3599 0.3105 -0.0218 -0.0567 0.1019  120 ASN A C   
993  O O   . ASN A 120 ? 0.2484 0.3514 0.2982 -0.0226 -0.0567 0.1126  120 ASN A O   
994  C CB  . ASN A 120 ? 0.3087 0.4150 0.3678 -0.0204 -0.0690 0.1056  120 ASN A CB  
995  C CG  . ASN A 120 ? 0.3837 0.4914 0.4656 -0.0194 -0.0751 0.1130  120 ASN A CG  
996  O OD1 . ASN A 120 ? 0.4289 0.5326 0.5336 -0.0188 -0.0738 0.1209  120 ASN A OD1 
997  N ND2 . ASN A 120 ? 0.3919 0.5059 0.4698 -0.0195 -0.0821 0.1110  120 ASN A ND2 
998  N N   . LEU A 121 ? 0.2555 0.3511 0.2889 -0.0218 -0.0531 0.0891  121 LEU A N   
999  C CA  . LEU A 121 ? 0.2530 0.3509 0.2700 -0.0226 -0.0491 0.0867  121 LEU A CA  
1000 C C   . LEU A 121 ? 0.2552 0.3472 0.2833 -0.0235 -0.0439 0.0892  121 LEU A C   
1001 O O   . LEU A 121 ? 0.2471 0.3441 0.2705 -0.0245 -0.0425 0.0960  121 LEU A O   
1002 C CB  . LEU A 121 ? 0.2580 0.3525 0.2610 -0.0221 -0.0465 0.0726  121 LEU A CB  
1003 C CG  . LEU A 121 ? 0.2611 0.3567 0.2505 -0.0226 -0.0418 0.0686  121 LEU A CG  
1004 C CD1 . LEU A 121 ? 0.2765 0.3840 0.2520 -0.0231 -0.0435 0.0757  121 LEU A CD1 
1005 C CD2 . LEU A 121 ? 0.2537 0.3449 0.2338 -0.0219 -0.0396 0.0559  121 LEU A CD2 
1006 N N   . PHE A 122 ? 0.2667 0.3479 0.3091 -0.0235 -0.0405 0.0828  122 PHE A N   
1007 C CA  . PHE A 122 ? 0.2617 0.3366 0.3159 -0.0249 -0.0362 0.0836  122 PHE A CA  
1008 C C   . PHE A 122 ? 0.2834 0.3618 0.3540 -0.0254 -0.0380 0.0983  122 PHE A C   
1009 O O   . PHE A 122 ? 0.2710 0.3488 0.3467 -0.0270 -0.0353 0.1026  122 PHE A O   
1010 C CB  . PHE A 122 ? 0.2755 0.3386 0.3406 -0.0250 -0.0322 0.0728  122 PHE A CB  
1011 C CG  . PHE A 122 ? 0.2766 0.3354 0.3265 -0.0256 -0.0289 0.0602  122 PHE A CG  
1012 C CD1 . PHE A 122 ? 0.2960 0.3573 0.3303 -0.0244 -0.0301 0.0544  122 PHE A CD1 
1013 C CD2 . PHE A 122 ? 0.2910 0.3437 0.3430 -0.0275 -0.0252 0.0547  122 PHE A CD2 
1014 C CE1 . PHE A 122 ? 0.3019 0.3593 0.3243 -0.0248 -0.0273 0.0443  122 PHE A CE1 
1015 C CE2 . PHE A 122 ? 0.2836 0.3331 0.3219 -0.0281 -0.0232 0.0445  122 PHE A CE2 
1016 C CZ  . PHE A 122 ? 0.2977 0.3496 0.3215 -0.0265 -0.0242 0.0400  122 PHE A CZ  
1017 N N   . GLU A 123 ? 0.2794 0.3615 0.3594 -0.0243 -0.0429 0.1070  123 GLU A N   
1018 C CA  . GLU A 123 ? 0.3005 0.3858 0.3983 -0.0246 -0.0452 0.1226  123 GLU A CA  
1019 C C   . GLU A 123 ? 0.3092 0.4067 0.3916 -0.0256 -0.0476 0.1345  123 GLU A C   
1020 O O   . GLU A 123 ? 0.3021 0.4007 0.3937 -0.0269 -0.0457 0.1445  123 GLU A O   
1021 C CB  . GLU A 123 ? 0.3052 0.3909 0.4199 -0.0229 -0.0504 0.1285  123 GLU A CB  
1022 C CG  . GLU A 123 ? 0.3537 0.4436 0.4883 -0.0230 -0.0541 0.1469  123 GLU A CG  
1023 C CD  . GLU A 123 ? 0.3749 0.4558 0.5344 -0.0238 -0.0488 0.1495  123 GLU A CD  
1024 O OE1 . GLU A 123 ? 0.3907 0.4612 0.5534 -0.0245 -0.0424 0.1355  123 GLU A OE1 
1025 O OE2 . GLU A 123 ? 0.4300 0.5144 0.6056 -0.0241 -0.0512 0.1659  123 GLU A OE2 
1026 N N   . LYS A 124 ? 0.3029 0.4094 0.3627 -0.0252 -0.0513 0.1331  124 LYS A N   
1027 C CA  . LYS A 124 ? 0.3310 0.4504 0.3753 -0.0261 -0.0539 0.1448  124 LYS A CA  
1028 C C   . LYS A 124 ? 0.3355 0.4582 0.3589 -0.0270 -0.0485 0.1381  124 LYS A C   
1029 O O   . LYS A 124 ? 0.3271 0.4600 0.3385 -0.0281 -0.0481 0.1474  124 LYS A O   
1030 C CB  . LYS A 124 ? 0.3870 0.5154 0.4190 -0.0255 -0.0619 0.1471  124 LYS A CB  
1031 C CG  . LYS A 124 ? 0.4291 0.5573 0.4826 -0.0247 -0.0687 0.1571  124 LYS A CG  
1032 C CD  . LYS A 124 ? 0.5131 0.6441 0.5622 -0.0238 -0.0755 0.1514  124 LYS A CD  
1033 C CE  . LYS A 124 ? 0.5904 0.7138 0.6688 -0.0221 -0.0775 0.1525  124 LYS A CE  
1034 N NZ  . LYS A 124 ? 0.6355 0.7642 0.7139 -0.0215 -0.0858 0.1512  124 LYS A NZ  
1035 N N   . GLY A 125 ? 0.3042 0.4192 0.3232 -0.0266 -0.0442 0.1225  125 GLY A N   
1036 C CA  . GLY A 125 ? 0.3150 0.4333 0.3179 -0.0271 -0.0391 0.1167  125 GLY A CA  
1037 C C   . GLY A 125 ? 0.3245 0.4501 0.3035 -0.0264 -0.0405 0.1096  125 GLY A C   
1038 O O   . GLY A 125 ? 0.3074 0.4333 0.2755 -0.0261 -0.0360 0.1007  125 GLY A O   
1039 N N   . ALA A 126 ? 0.3332 0.4653 0.3057 -0.0261 -0.0469 0.1136  126 ALA A N   
1040 C CA  . ALA A 126 ? 0.3466 0.4858 0.2972 -0.0259 -0.0489 0.1063  126 ALA A CA  
1041 C C   . ALA A 126 ? 0.3688 0.5117 0.3198 -0.0258 -0.0577 0.1091  126 ALA A C   
1042 O O   . ALA A 126 ? 0.3827 0.5301 0.3423 -0.0264 -0.0626 0.1231  126 ALA A O   
1043 C CB  . ALA A 126 ? 0.3623 0.5130 0.2953 -0.0271 -0.0459 0.1118  126 ALA A CB  
1044 N N   . VAL A 127 ? 0.3677 0.5093 0.3106 -0.0252 -0.0601 0.0966  127 VAL A N   
1045 C CA  . VAL A 127 ? 0.4016 0.5468 0.3464 -0.0253 -0.0690 0.0980  127 VAL A CA  
1046 C C   . VAL A 127 ? 0.4283 0.5790 0.3533 -0.0259 -0.0715 0.0866  127 VAL A C   
1047 O O   . VAL A 127 ? 0.3755 0.5226 0.2917 -0.0252 -0.0656 0.0746  127 VAL A O   
1048 C CB  . VAL A 127 ? 0.3825 0.5169 0.3498 -0.0240 -0.0700 0.0947  127 VAL A CB  
1049 C CG1 . VAL A 127 ? 0.3953 0.5245 0.3838 -0.0237 -0.0681 0.1055  127 VAL A CG1 
1050 C CG2 . VAL A 127 ? 0.3726 0.4972 0.3388 -0.0230 -0.0640 0.0792  127 VAL A CG2 
1051 N N   . PRO A 128 ? 0.5017 0.6621 0.4189 -0.0272 -0.0806 0.0902  128 PRO A N   
1052 C CA  . PRO A 128 ? 0.5342 0.7029 0.4563 -0.0283 -0.0878 0.1074  128 PRO A CA  
1053 C C   . PRO A 128 ? 0.5780 0.7558 0.4851 -0.0297 -0.0846 0.1182  128 PRO A C   
1054 O O   . PRO A 128 ? 0.5986 0.7766 0.4924 -0.0297 -0.0763 0.1116  128 PRO A O   
1055 C CB  . PRO A 128 ? 0.5804 0.7577 0.4953 -0.0298 -0.0991 0.1057  128 PRO A CB  
1056 C CG  . PRO A 128 ? 0.5811 0.7573 0.4796 -0.0301 -0.0964 0.0870  128 PRO A CG  
1057 C CD  . PRO A 128 ? 0.5316 0.6956 0.4359 -0.0280 -0.0850 0.0778  128 PRO A CD  
1058 N N   . GLU A 129 ? 0.7024 0.8884 0.6131 -0.0308 -0.0910 0.1358  129 GLU A N   
1059 C CA  . GLU A 129 ? 0.7883 0.9805 0.6942 -0.0319 -0.0869 0.1505  129 GLU A CA  
1060 C C   . GLU A 129 ? 0.7756 0.9777 0.6511 -0.0335 -0.0821 0.1454  129 GLU A C   
1061 O O   . GLU A 129 ? 0.8331 1.0345 0.7050 -0.0334 -0.0724 0.1461  129 GLU A O   
1062 C CB  . GLU A 129 ? 0.8801 1.0804 0.7951 -0.0329 -0.0963 0.1710  129 GLU A CB  
1063 C CG  . GLU A 129 ? 0.9864 1.1785 0.9322 -0.0311 -0.1022 0.1747  129 GLU A CG  
1064 C CD  . GLU A 129 ? 1.1041 1.2798 1.0713 -0.0288 -0.0944 0.1635  129 GLU A CD  
1065 O OE1 . GLU A 129 ? 1.1905 1.3602 1.1559 -0.0279 -0.0936 0.1471  129 GLU A OE1 
1066 O OE2 . GLU A 129 ? 1.1336 1.3026 1.1190 -0.0281 -0.0889 0.1710  129 GLU A OE2 
1067 N N   . ASP A 130 ? 0.7816 0.9930 0.6365 -0.0351 -0.0889 0.1396  130 ASP A N   
1068 C CA  . ASP A 130 ? 0.8439 1.0655 0.6683 -0.0370 -0.0848 0.1330  130 ASP A CA  
1069 C C   . ASP A 130 ? 0.7935 1.0072 0.6135 -0.0354 -0.0758 0.1122  130 ASP A C   
1070 O O   . ASP A 130 ? 0.7291 0.9436 0.5410 -0.0351 -0.0652 0.1095  130 ASP A O   
1071 C CB  . ASP A 130 ? 0.9362 1.1692 0.7421 -0.0395 -0.0963 0.1311  130 ASP A CB  
1072 C CG  . ASP A 130 ? 1.0268 1.2517 0.8488 -0.0384 -0.1041 0.1207  130 ASP A CG  
1073 O OD1 . ASP A 130 ? 1.0977 1.3190 0.9428 -0.0375 -0.1108 0.1313  130 ASP A OD1 
1074 O OD2 . ASP A 130 ? 1.0507 1.2713 0.8658 -0.0381 -0.1015 0.1018  130 ASP A OD2 
1075 N N   . LEU A 131 ? 0.7939 1.0000 0.6216 -0.0344 -0.0801 0.0985  131 LEU A N   
1076 C CA  . LEU A 131 ? 0.6921 0.8918 0.5146 -0.0332 -0.0741 0.0786  131 LEU A CA  
1077 C C   . LEU A 131 ? 0.5976 0.7870 0.4328 -0.0308 -0.0632 0.0759  131 LEU A C   
1078 O O   . LEU A 131 ? 0.6214 0.8106 0.4473 -0.0302 -0.0550 0.0657  131 LEU A O   
1079 C CB  . LEU A 131 ? 0.7031 0.8959 0.5371 -0.0327 -0.0812 0.0681  131 LEU A CB  
1080 C CG  . LEU A 131 ? 0.7430 0.9446 0.5615 -0.0352 -0.0907 0.0609  131 LEU A CG  
1081 C CD1 . LEU A 131 ? 0.7230 0.9164 0.5584 -0.0345 -0.0967 0.0516  131 LEU A CD1 
1082 C CD2 . LEU A 131 ? 0.7482 0.9557 0.5422 -0.0363 -0.0851 0.0473  131 LEU A CD2 
1083 N N   . GLU A 132 ? 0.5354 0.7160 0.3934 -0.0296 -0.0637 0.0838  132 GLU A N   
1084 C CA  . GLU A 132 ? 0.4909 0.6609 0.3628 -0.0277 -0.0553 0.0806  132 GLU A CA  
1085 C C   . GLU A 132 ? 0.4561 0.6185 0.3269 -0.0262 -0.0519 0.0629  132 GLU A C   
1086 O O   . GLU A 132 ? 0.4819 0.6421 0.3503 -0.0252 -0.0438 0.0568  132 GLU A O   
1087 C CB  . GLU A 132 ? 0.5343 0.7094 0.4005 -0.0282 -0.0471 0.0877  132 GLU A CB  
1088 C CG  . GLU A 132 ? 0.5901 0.7724 0.4587 -0.0298 -0.0499 0.1068  132 GLU A CG  
1089 C CD  . GLU A 132 ? 0.6247 0.8091 0.4962 -0.0302 -0.0410 0.1150  132 GLU A CD  
1090 O OE1 . GLU A 132 ? 0.7100 0.8982 0.5888 -0.0314 -0.0423 0.1316  132 GLU A OE1 
1091 O OE2 . GLU A 132 ? 0.6417 0.8238 0.5102 -0.0293 -0.0330 0.1052  132 GLU A OE2 
1092 N N   . LEU A 133 ? 0.3910 0.5494 0.2666 -0.0260 -0.0582 0.0557  133 LEU A N   
1093 C CA  . LEU A 133 ? 0.3594 0.5097 0.2374 -0.0247 -0.0556 0.0405  133 LEU A CA  
1094 C C   . LEU A 133 ? 0.3429 0.4817 0.2360 -0.0229 -0.0494 0.0395  133 LEU A C   
1095 O O   . LEU A 133 ? 0.3375 0.4711 0.2300 -0.0217 -0.0444 0.0294  133 LEU A O   
1096 C CB  . LEU A 133 ? 0.3647 0.5130 0.2488 -0.0251 -0.0638 0.0360  133 LEU A CB  
1097 C CG  . LEU A 133 ? 0.4029 0.5625 0.2717 -0.0274 -0.0715 0.0346  133 LEU A CG  
1098 C CD1 . LEU A 133 ? 0.4010 0.5587 0.2808 -0.0280 -0.0804 0.0316  133 LEU A CD1 
1099 C CD2 . LEU A 133 ? 0.4321 0.5958 0.2827 -0.0277 -0.0668 0.0217  133 LEU A CD2 
1100 N N   . LEU A 134 ? 0.3051 0.4400 0.2123 -0.0229 -0.0504 0.0498  134 LEU A N   
1101 C CA  . LEU A 134 ? 0.3101 0.4356 0.2303 -0.0221 -0.0451 0.0504  134 LEU A CA  
1102 C C   . LEU A 134 ? 0.3021 0.4315 0.2251 -0.0229 -0.0424 0.0623  134 LEU A C   
1103 O O   . LEU A 134 ? 0.2976 0.4329 0.2222 -0.0239 -0.0463 0.0737  134 LEU A O   
1104 C CB  . LEU A 134 ? 0.3070 0.4232 0.2439 -0.0216 -0.0478 0.0502  134 LEU A CB  
1105 C CG  . LEU A 134 ? 0.3562 0.4684 0.2941 -0.0211 -0.0504 0.0401  134 LEU A CG  
1106 C CD1 . LEU A 134 ? 0.3889 0.4926 0.3443 -0.0207 -0.0514 0.0409  134 LEU A CD1 
1107 C CD2 . LEU A 134 ? 0.3589 0.4668 0.2902 -0.0202 -0.0455 0.0288  134 LEU A CD2 
1108 N N   . ARG A 135 ? 0.3071 0.4334 0.2320 -0.0226 -0.0360 0.0603  135 ARG A N   
1109 C CA  . ARG A 135 ? 0.3437 0.4731 0.2735 -0.0235 -0.0324 0.0704  135 ARG A CA  
1110 C C   . ARG A 135 ? 0.3110 0.4307 0.2539 -0.0234 -0.0287 0.0669  135 ARG A C   
1111 O O   . ARG A 135 ? 0.2676 0.3828 0.2079 -0.0224 -0.0264 0.0568  135 ARG A O   
1112 C CB  . ARG A 135 ? 0.4190 0.5587 0.3332 -0.0238 -0.0279 0.0704  135 ARG A CB  
1113 C CG  . ARG A 135 ? 0.5343 0.6793 0.4523 -0.0250 -0.0229 0.0810  135 ARG A CG  
1114 C CD  . ARG A 135 ? 0.5812 0.7378 0.4818 -0.0252 -0.0177 0.0808  135 ARG A CD  
1115 N NE  . ARG A 135 ? 0.6574 0.8130 0.5535 -0.0237 -0.0121 0.0682  135 ARG A NE  
1116 C CZ  . ARG A 135 ? 0.6580 0.8113 0.5638 -0.0232 -0.0063 0.0667  135 ARG A CZ  
1117 N NH1 . ARG A 135 ? 0.6454 0.7966 0.5656 -0.0245 -0.0053 0.0760  135 ARG A NH1 
1118 N NH2 . ARG A 135 ? 0.6685 0.8217 0.5713 -0.0215 -0.0017 0.0560  135 ARG A NH2 
1119 N N   . MET A 136 ? 0.2948 0.4117 0.2518 -0.0246 -0.0282 0.0754  136 MET A N   
1120 C CA  . MET A 136 ? 0.3069 0.4145 0.2762 -0.0251 -0.0257 0.0714  136 MET A CA  
1121 C C   . MET A 136 ? 0.2906 0.4013 0.2684 -0.0267 -0.0223 0.0797  136 MET A C   
1122 O O   . MET A 136 ? 0.2648 0.3820 0.2449 -0.0276 -0.0223 0.0914  136 MET A O   
1123 C CB  . MET A 136 ? 0.3403 0.4387 0.3228 -0.0252 -0.0287 0.0707  136 MET A CB  
1124 C CG  . MET A 136 ? 0.4122 0.5008 0.4064 -0.0263 -0.0264 0.0656  136 MET A CG  
1125 S SD  . MET A 136 ? 0.4488 0.5270 0.4576 -0.0263 -0.0283 0.0632  136 MET A SD  
1126 C CE  . MET A 136 ? 0.5082 0.5901 0.5330 -0.0272 -0.0297 0.0780  136 MET A CE  
1127 N N   . GLU A 137 ? 0.2629 0.3694 0.2454 -0.0273 -0.0194 0.0741  137 GLU A N   
1128 C CA  . GLU A 137 ? 0.2535 0.3617 0.2478 -0.0292 -0.0165 0.0809  137 GLU A CA  
1129 C C   . GLU A 137 ? 0.2282 0.3291 0.2306 -0.0303 -0.0159 0.0729  137 GLU A C   
1130 O O   . GLU A 137 ? 0.2162 0.3121 0.2124 -0.0293 -0.0171 0.0629  137 GLU A O   
1131 C CB  . GLU A 137 ? 0.3044 0.4242 0.2913 -0.0292 -0.0122 0.0868  137 GLU A CB  
1132 C CG  . GLU A 137 ? 0.3284 0.4513 0.3048 -0.0277 -0.0092 0.0778  137 GLU A CG  
1133 C CD  . GLU A 137 ? 0.3733 0.5084 0.3404 -0.0274 -0.0039 0.0828  137 GLU A CD  
1134 O OE1 . GLU A 137 ? 0.4665 0.6077 0.4234 -0.0274 -0.0046 0.0887  137 GLU A OE1 
1135 O OE2 . GLU A 137 ? 0.3651 0.5040 0.3361 -0.0275 0.0009  0.0818  137 GLU A OE2 
1136 N N   . LYS A 138 ? 0.2206 0.3206 0.2380 -0.0327 -0.0147 0.0782  138 LYS A N   
1137 C CA  . LYS A 138 ? 0.2305 0.3243 0.2573 -0.0346 -0.0153 0.0717  138 LYS A CA  
1138 C C   . LYS A 138 ? 0.2386 0.3379 0.2581 -0.0338 -0.0135 0.0673  138 LYS A C   
1139 O O   . LYS A 138 ? 0.2338 0.3424 0.2520 -0.0333 -0.0097 0.0732  138 LYS A O   
1140 C CB  . LYS A 138 ? 0.2432 0.3355 0.2895 -0.0377 -0.0146 0.0788  138 LYS A CB  
1141 C CG  . LYS A 138 ? 0.2711 0.3561 0.3287 -0.0406 -0.0163 0.0713  138 LYS A CG  
1142 C CD  . LYS A 138 ? 0.2781 0.3518 0.3376 -0.0412 -0.0188 0.0631  138 LYS A CD  
1143 C CE  . LYS A 138 ? 0.3060 0.3743 0.3676 -0.0438 -0.0210 0.0529  138 LYS A CE  
1144 N NZ  . LYS A 138 ? 0.3058 0.3635 0.3684 -0.0449 -0.0222 0.0443  138 LYS A NZ  
1145 N N   . LYS A 139 ? 0.2263 0.3201 0.2414 -0.0334 -0.0158 0.0575  139 LYS A N   
1146 C CA  . LYS A 139 ? 0.2616 0.3603 0.2708 -0.0319 -0.0146 0.0536  139 LYS A CA  
1147 C C   . LYS A 139 ? 0.2589 0.3508 0.2657 -0.0321 -0.0182 0.0445  139 LYS A C   
1148 O O   . LYS A 139 ? 0.2414 0.3263 0.2408 -0.0315 -0.0203 0.0394  139 LYS A O   
1149 C CB  . LYS A 139 ? 0.3018 0.4058 0.2967 -0.0286 -0.0123 0.0528  139 LYS A CB  
1150 C CG  . LYS A 139 ? 0.3641 0.4726 0.3554 -0.0266 -0.0103 0.0481  139 LYS A CG  
1151 C CD  . LYS A 139 ? 0.4272 0.5455 0.4117 -0.0248 -0.0051 0.0509  139 LYS A CD  
1152 C CE  . LYS A 139 ? 0.4776 0.6036 0.4700 -0.0265 -0.0010 0.0604  139 LYS A CE  
1153 N NZ  . LYS A 139 ? 0.4561 0.5886 0.4372 -0.0259 0.0018  0.0657  139 LYS A NZ  
1154 N N   . THR A 140 ? 0.2574 0.3523 0.2699 -0.0329 -0.0189 0.0433  140 THR A N   
1155 C CA  . THR A 140 ? 0.2507 0.3410 0.2602 -0.0332 -0.0231 0.0363  140 THR A CA  
1156 C C   . THR A 140 ? 0.2506 0.3428 0.2499 -0.0295 -0.0220 0.0330  140 THR A C   
1157 O O   . THR A 140 ? 0.2450 0.3438 0.2417 -0.0269 -0.0178 0.0351  140 THR A O   
1158 C CB  . THR A 140 ? 0.2823 0.3756 0.3040 -0.0357 -0.0256 0.0369  140 THR A CB  
1159 O OG1 . THR A 140 ? 0.3164 0.4194 0.3440 -0.0338 -0.0220 0.0410  140 THR A OG1 
1160 C CG2 . THR A 140 ? 0.2784 0.3693 0.3126 -0.0399 -0.0269 0.0391  140 THR A CG2 
1161 N N   . LEU A 141 ? 0.2274 0.3143 0.2217 -0.0294 -0.0258 0.0277  141 LEU A N   
1162 C CA  . LEU A 141 ? 0.2468 0.3344 0.2342 -0.0259 -0.0250 0.0249  141 LEU A CA  
1163 C C   . LEU A 141 ? 0.2514 0.3475 0.2471 -0.0241 -0.0230 0.0268  141 LEU A C   
1164 O O   . LEU A 141 ? 0.2541 0.3538 0.2470 -0.0208 -0.0192 0.0255  141 LEU A O   
1165 C CB  . LEU A 141 ? 0.2659 0.3462 0.2472 -0.0267 -0.0294 0.0207  141 LEU A CB  
1166 C CG  . LEU A 141 ? 0.2578 0.3375 0.2344 -0.0234 -0.0291 0.0184  141 LEU A CG  
1167 C CD1 . LEU A 141 ? 0.2541 0.3335 0.2243 -0.0208 -0.0251 0.0166  141 LEU A CD1 
1168 C CD2 . LEU A 141 ? 0.2638 0.3365 0.2340 -0.0249 -0.0334 0.0161  141 LEU A CD2 
1169 N N   . ASN A 142 ? 0.2812 0.3810 0.2886 -0.0262 -0.0252 0.0295  142 ASN A N   
1170 C CA  . ASN A 142 ? 0.3005 0.4090 0.3190 -0.0245 -0.0227 0.0318  142 ASN A CA  
1171 C C   . ASN A 142 ? 0.3244 0.4403 0.3442 -0.0230 -0.0150 0.0348  142 ASN A C   
1172 O O   . ASN A 142 ? 0.3223 0.4442 0.3449 -0.0199 -0.0103 0.0339  142 ASN A O   
1173 C CB  . ASN A 142 ? 0.3275 0.4393 0.3605 -0.0275 -0.0270 0.0345  142 ASN A CB  
1174 C CG  . ASN A 142 ? 0.3759 0.4868 0.4114 -0.0268 -0.0330 0.0328  142 ASN A CG  
1175 O OD1 . ASN A 142 ? 0.4049 0.5183 0.4419 -0.0230 -0.0309 0.0321  142 ASN A OD1 
1176 N ND2 . ASN A 142 ? 0.4148 0.5221 0.4511 -0.0307 -0.0406 0.0322  142 ASN A ND2 
1177 N N   . GLU A 143 ? 0.3173 0.4331 0.3360 -0.0252 -0.0134 0.0386  143 GLU A N   
1178 C CA  . GLU A 143 ? 0.3467 0.4701 0.3647 -0.0244 -0.0064 0.0431  143 GLU A CA  
1179 C C   . GLU A 143 ? 0.3359 0.4596 0.3393 -0.0211 -0.0031 0.0391  143 GLU A C   
1180 O O   . GLU A 143 ? 0.3680 0.4995 0.3701 -0.0190 0.0032  0.0391  143 GLU A O   
1181 C CB  . GLU A 143 ? 0.3874 0.5096 0.4081 -0.0275 -0.0065 0.0492  143 GLU A CB  
1182 C CG  . GLU A 143 ? 0.4846 0.6089 0.5230 -0.0310 -0.0078 0.0537  143 GLU A CG  
1183 C CD  . GLU A 143 ? 0.5693 0.6887 0.6137 -0.0346 -0.0100 0.0578  143 GLU A CD  
1184 O OE1 . GLU A 143 ? 0.5987 0.7197 0.6593 -0.0378 -0.0111 0.0610  143 GLU A OE1 
1185 O OE2 . GLU A 143 ? 0.5143 0.6279 0.5493 -0.0344 -0.0110 0.0574  143 GLU A OE2 
1186 N N   . LEU A 144 ? 0.3160 0.4315 0.3092 -0.0207 -0.0072 0.0347  144 LEU A N   
1187 C CA  . LEU A 144 ? 0.2988 0.4139 0.2797 -0.0181 -0.0053 0.0301  144 LEU A CA  
1188 C C   . LEU A 144 ? 0.3046 0.4223 0.2878 -0.0149 -0.0027 0.0247  144 LEU A C   
1189 O O   . LEU A 144 ? 0.2648 0.3875 0.2423 -0.0128 0.0024  0.0216  144 LEU A O   
1190 C CB  . LEU A 144 ? 0.2761 0.3818 0.2493 -0.0186 -0.0102 0.0269  144 LEU A CB  
1191 C CG  . LEU A 144 ? 0.2893 0.3934 0.2526 -0.0160 -0.0095 0.0209  144 LEU A CG  
1192 C CD1 . LEU A 144 ? 0.3062 0.4178 0.2616 -0.0153 -0.0055 0.0217  144 LEU A CD1 
1193 C CD2 . LEU A 144 ? 0.2879 0.3830 0.2466 -0.0167 -0.0138 0.0183  144 LEU A CD2 
1194 N N   . ILE A 145 ? 0.2895 0.4038 0.2812 -0.0148 -0.0064 0.0236  145 ILE A N   
1195 C CA  . ILE A 145 ? 0.2895 0.4057 0.2875 -0.0117 -0.0046 0.0197  145 ILE A CA  
1196 C C   . ILE A 145 ? 0.2891 0.4158 0.2961 -0.0102 0.0027  0.0210  145 ILE A C   
1197 O O   . ILE A 145 ? 0.2947 0.4241 0.3031 -0.0071 0.0074  0.0160  145 ILE A O   
1198 C CB  . ILE A 145 ? 0.2929 0.4046 0.2991 -0.0122 -0.0111 0.0205  145 ILE A CB  
1199 C CG1 . ILE A 145 ? 0.3007 0.4025 0.2964 -0.0130 -0.0161 0.0180  145 ILE A CG1 
1200 C CG2 . ILE A 145 ? 0.3099 0.4256 0.3283 -0.0089 -0.0090 0.0189  145 ILE A CG2 
1201 C CD1 . ILE A 145 ? 0.3222 0.4193 0.3211 -0.0150 -0.0232 0.0198  145 ILE A CD1 
1202 N N   . GLU A 146 ? 0.2879 0.4198 0.3026 -0.0125 0.0038  0.0272  146 GLU A N   
1203 C CA  . GLU A 146 ? 0.3321 0.4745 0.3557 -0.0118 0.0116  0.0298  146 GLU A CA  
1204 C C   . GLU A 146 ? 0.3389 0.4860 0.3484 -0.0105 0.0192  0.0272  146 GLU A C   
1205 O O   . GLU A 146 ? 0.3166 0.4706 0.3288 -0.0080 0.0269  0.0238  146 GLU A O   
1206 C CB  . GLU A 146 ? 0.3679 0.5137 0.4012 -0.0155 0.0107  0.0379  146 GLU A CB  
1207 C CG  . GLU A 146 ? 0.4378 0.5950 0.4823 -0.0153 0.0195  0.0422  146 GLU A CG  
1208 C CD  . GLU A 146 ? 0.4749 0.6366 0.5301 -0.0191 0.0204  0.0511  146 GLU A CD  
1209 O OE1 . GLU A 146 ? 0.5271 0.6831 0.5791 -0.0222 0.0150  0.0546  146 GLU A OE1 
1210 O OE2 . GLU A 146 ? 0.5319 0.7030 0.6010 -0.0188 0.0271  0.0546  146 GLU A OE2 
1211 N N   . GLU A 147 ? 0.3176 0.4611 0.3123 -0.0122 0.0166  0.0285  147 GLU A N   
1212 C CA  . GLU A 147 ? 0.3445 0.4927 0.3236 -0.0115 0.0217  0.0265  147 GLU A CA  
1213 C C   . GLU A 147 ? 0.3175 0.4638 0.2906 -0.0084 0.0234  0.0161  147 GLU A C   
1214 O O   . GLU A 147 ? 0.3041 0.4575 0.2710 -0.0071 0.0308  0.0119  147 GLU A O   
1215 C CB  . GLU A 147 ? 0.3454 0.4896 0.3122 -0.0138 0.0168  0.0303  147 GLU A CB  
1216 C CG  . GLU A 147 ? 0.3895 0.5373 0.3611 -0.0169 0.0172  0.0411  147 GLU A CG  
1217 C CD  . GLU A 147 ? 0.4102 0.5529 0.3743 -0.0189 0.0116  0.0456  147 GLU A CD  
1218 O OE1 . GLU A 147 ? 0.4025 0.5404 0.3564 -0.0179 0.0079  0.0402  147 GLU A OE1 
1219 O OE2 . GLU A 147 ? 0.4067 0.5500 0.3780 -0.0214 0.0108  0.0544  147 GLU A OE2 
1220 N N   . ILE A 148 ? 0.2899 0.4270 0.2652 -0.0074 0.0173  0.0117  148 ILE A N   
1221 C CA  . ILE A 148 ? 0.2972 0.4316 0.2693 -0.0046 0.0187  0.0021  148 ILE A CA  
1222 C C   . ILE A 148 ? 0.2773 0.4169 0.2629 -0.0017 0.0254  -0.0018 148 ILE A C   
1223 O O   . ILE A 148 ? 0.2796 0.4214 0.2626 0.0006  0.0310  -0.0102 148 ILE A O   
1224 C CB  . ILE A 148 ? 0.3058 0.4292 0.2785 -0.0046 0.0109  0.0001  148 ILE A CB  
1225 C CG1 . ILE A 148 ? 0.3314 0.4505 0.2912 -0.0070 0.0060  0.0020  148 ILE A CG1 
1226 C CG2 . ILE A 148 ? 0.3137 0.4337 0.2896 -0.0016 0.0123  -0.0087 148 ILE A CG2 
1227 C CD1 . ILE A 148 ? 0.3104 0.4195 0.2722 -0.0079 -0.0010 0.0031  148 ILE A CD1 
1228 N N   . ASN A 149 ? 0.2406 0.3818 0.2426 -0.0017 0.0245  0.0038  149 ASN A N   
1229 C CA  . ASN A 149 ? 0.2240 0.3704 0.2433 0.0012  0.0302  0.0015  149 ASN A CA  
1230 C C   . ASN A 149 ? 0.2250 0.3655 0.2489 0.0045  0.0297  -0.0067 149 ASN A C   
1231 O O   . ASN A 149 ? 0.2198 0.3640 0.2474 0.0073  0.0374  -0.0142 149 ASN A O   
1232 C CB  . ASN A 149 ? 0.2268 0.3842 0.2447 0.0018  0.0415  0.0001  149 ASN A CB  
1233 C CG  . ASN A 149 ? 0.2240 0.3879 0.2639 0.0045  0.0481  -0.0007 149 ASN A CG  
1234 O OD1 . ASN A 149 ? 0.2022 0.3638 0.2602 0.0053  0.0428  0.0029  149 ASN A OD1 
1235 N ND2 . ASN A 149 ? 0.2292 0.4021 0.2679 0.0058  0.0597  -0.0048 149 ASN A ND2 
1236 N N   . PRO A 150 ? 0.2207 0.3520 0.2464 0.0043  0.0209  -0.0053 150 PRO A N   
1237 C CA  . PRO A 150 ? 0.2276 0.3526 0.2590 0.0072  0.0200  -0.0115 150 PRO A CA  
1238 C C   . PRO A 150 ? 0.2314 0.3587 0.2865 0.0104  0.0215  -0.0105 150 PRO A C   
1239 O O   . PRO A 150 ? 0.2392 0.3720 0.3066 0.0099  0.0209  -0.0040 150 PRO A O   
1240 C CB  . PRO A 150 ? 0.2185 0.3339 0.2422 0.0049  0.0102  -0.0075 150 PRO A CB  
1241 C CG  . PRO A 150 ? 0.2173 0.3350 0.2437 0.0021  0.0056  0.0014  150 PRO A CG  
1242 C CD  . PRO A 150 ? 0.2185 0.3449 0.2405 0.0010  0.0120  0.0022  150 PRO A CD  
1243 N N   . ASP A 151 ? 0.2511 0.3739 0.3151 0.0136  0.0228  -0.0163 151 ASP A N   
1244 C CA  . ASP A 151 ? 0.2429 0.3670 0.3318 0.0169  0.0230  -0.0142 151 ASP A CA  
1245 C C   . ASP A 151 ? 0.2378 0.3547 0.3322 0.0163  0.0122  -0.0064 151 ASP A C   
1246 O O   . ASP A 151 ? 0.2506 0.3688 0.3661 0.0187  0.0102  -0.0021 151 ASP A O   
1247 C CB  . ASP A 151 ? 0.2593 0.3833 0.3600 0.0211  0.0315  -0.0245 151 ASP A CB  
1248 C CG  . ASP A 151 ? 0.2621 0.3776 0.3524 0.0214  0.0313  -0.0330 151 ASP A CG  
1249 O OD1 . ASP A 151 ? 0.2600 0.3716 0.3296 0.0182  0.0267  -0.0325 151 ASP A OD1 
1250 O OD2 . ASP A 151 ? 0.2811 0.3941 0.3866 0.0249  0.0358  -0.0401 151 ASP A OD2 
1251 N N   . VAL A 152 ? 0.2528 0.3628 0.3288 0.0130  0.0056  -0.0041 152 VAL A N   
1252 C CA  . VAL A 152 ? 0.2286 0.3321 0.3049 0.0116  -0.0041 0.0033  152 VAL A CA  
1253 C C   . VAL A 152 ? 0.2223 0.3210 0.2761 0.0074  -0.0085 0.0045  152 VAL A C   
1254 O O   . VAL A 152 ? 0.2104 0.3077 0.2507 0.0067  -0.0048 -0.0014 152 VAL A O   
1255 C CB  . VAL A 152 ? 0.2336 0.3302 0.3203 0.0147  -0.0049 0.0017  152 VAL A CB  
1256 C CG1 . VAL A 152 ? 0.2420 0.3319 0.3162 0.0146  -0.0018 -0.0065 152 VAL A CG1 
1257 C CG2 . VAL A 152 ? 0.2413 0.3332 0.3313 0.0135  -0.0145 0.0114  152 VAL A CG2 
1258 N N   . VAL A 153 ? 0.2093 0.3058 0.2598 0.0045  -0.0166 0.0119  153 VAL A N   
1259 C CA  . VAL A 153 ? 0.2045 0.2956 0.2367 0.0007  -0.0208 0.0131  153 VAL A CA  
1260 C C   . VAL A 153 ? 0.2039 0.2878 0.2342 0.0000  -0.0271 0.0173  153 VAL A C   
1261 O O   . VAL A 153 ? 0.1885 0.2739 0.2275 -0.0002 -0.0327 0.0236  153 VAL A O   
1262 C CB  . VAL A 153 ? 0.2165 0.3117 0.2446 -0.0030 -0.0237 0.0170  153 VAL A CB  
1263 C CG1 . VAL A 153 ? 0.2232 0.3120 0.2346 -0.0068 -0.0276 0.0174  153 VAL A CG1 
1264 C CG2 . VAL A 153 ? 0.2209 0.3237 0.2511 -0.0027 -0.0171 0.0148  153 VAL A CG2 
1265 N N   . PHE A 154 ? 0.2030 0.2796 0.2218 -0.0006 -0.0265 0.0144  154 PHE A N   
1266 C CA  . PHE A 154 ? 0.2117 0.2815 0.2255 -0.0019 -0.0313 0.0187  154 PHE A CA  
1267 C C   . PHE A 154 ? 0.2285 0.2947 0.2248 -0.0061 -0.0333 0.0186  154 PHE A C   
1268 O O   . PHE A 154 ? 0.2223 0.2882 0.2110 -0.0068 -0.0297 0.0138  154 PHE A O   
1269 C CB  . PHE A 154 ? 0.2101 0.2740 0.2273 0.0005  -0.0281 0.0154  154 PHE A CB  
1270 C CG  . PHE A 154 ? 0.2094 0.2750 0.2461 0.0047  -0.0259 0.0150  154 PHE A CG  
1271 C CD1 . PHE A 154 ? 0.2087 0.2743 0.2576 0.0058  -0.0306 0.0233  154 PHE A CD1 
1272 C CD2 . PHE A 154 ? 0.2093 0.2772 0.2531 0.0075  -0.0190 0.0065  154 PHE A CD2 
1273 C CE1 . PHE A 154 ? 0.2177 0.2848 0.2882 0.0100  -0.0284 0.0233  154 PHE A CE1 
1274 C CE2 . PHE A 154 ? 0.2095 0.2786 0.2734 0.0115  -0.0161 0.0050  154 PHE A CE2 
1275 C CZ  . PHE A 154 ? 0.2185 0.2869 0.2972 0.0130  -0.0206 0.0136  154 PHE A CZ  
1276 N N   . ILE A 155 ? 0.2359 0.2995 0.2263 -0.0087 -0.0390 0.0240  155 ILE A N   
1277 C CA  . ILE A 155 ? 0.2391 0.2985 0.2137 -0.0127 -0.0405 0.0234  155 ILE A CA  
1278 C C   . ILE A 155 ? 0.2387 0.2912 0.2069 -0.0132 -0.0411 0.0259  155 ILE A C   
1279 O O   . ILE A 155 ? 0.2304 0.2828 0.2008 -0.0134 -0.0455 0.0323  155 ILE A O   
1280 C CB  . ILE A 155 ? 0.2611 0.3241 0.2332 -0.0162 -0.0462 0.0265  155 ILE A CB  
1281 C CG1 . ILE A 155 ? 0.2801 0.3507 0.2626 -0.0154 -0.0452 0.0255  155 ILE A CG1 
1282 C CG2 . ILE A 155 ? 0.2726 0.3308 0.2291 -0.0204 -0.0468 0.0241  155 ILE A CG2 
1283 C CD1 . ILE A 155 ? 0.3129 0.3881 0.2990 -0.0184 -0.0517 0.0291  155 ILE A CD1 
1284 N N   . MET A 156 ? 0.2239 0.2713 0.1851 -0.0136 -0.0367 0.0217  156 MET A N   
1285 C CA  . MET A 156 ? 0.2285 0.2694 0.1846 -0.0142 -0.0359 0.0241  156 MET A CA  
1286 C C   . MET A 156 ? 0.2403 0.2793 0.1821 -0.0184 -0.0389 0.0267  156 MET A C   
1287 O O   . MET A 156 ? 0.2419 0.2807 0.1758 -0.0209 -0.0380 0.0225  156 MET A O   
1288 C CB  . MET A 156 ? 0.2292 0.2660 0.1845 -0.0135 -0.0305 0.0185  156 MET A CB  
1289 C CG  . MET A 156 ? 0.2191 0.2586 0.1856 -0.0100 -0.0277 0.0136  156 MET A CG  
1290 S SD  . MET A 156 ? 0.2353 0.2763 0.2186 -0.0062 -0.0286 0.0167  156 MET A SD  
1291 C CE  . MET A 156 ? 0.2658 0.2990 0.2491 -0.0069 -0.0287 0.0226  156 MET A CE  
1292 N N   . HIS A 157 ? 0.2501 0.2881 0.1892 -0.0193 -0.0426 0.0337  157 HIS A N   
1293 C CA  . HIS A 157 ? 0.2811 0.3188 0.2055 -0.0237 -0.0466 0.0364  157 HIS A CA  
1294 C C   . HIS A 157 ? 0.2834 0.3178 0.2025 -0.0243 -0.0476 0.0441  157 HIS A C   
1295 O O   . HIS A 157 ? 0.2646 0.3004 0.1952 -0.0217 -0.0502 0.0509  157 HIS A O   
1296 C CB  . HIS A 157 ? 0.3029 0.3474 0.2308 -0.0247 -0.0538 0.0385  157 HIS A CB  
1297 C CG  . HIS A 157 ? 0.3660 0.4108 0.2784 -0.0299 -0.0581 0.0379  157 HIS A CG  
1298 N ND1 . HIS A 157 ? 0.3754 0.4184 0.2734 -0.0331 -0.0613 0.0428  157 HIS A ND1 
1299 C CD2 . HIS A 157 ? 0.3958 0.4426 0.3048 -0.0328 -0.0596 0.0324  157 HIS A CD2 
1300 C CE1 . HIS A 157 ? 0.4093 0.4532 0.2943 -0.0379 -0.0645 0.0388  157 HIS A CE1 
1301 N NE2 . HIS A 157 ? 0.3906 0.4365 0.2834 -0.0378 -0.0638 0.0325  157 HIS A NE2 
1302 N N   . GLU A 158 ? 0.3008 0.3311 0.2037 -0.0278 -0.0449 0.0432  158 GLU A N   
1303 C CA  . GLU A 158 ? 0.3188 0.3460 0.2140 -0.0291 -0.0446 0.0510  158 GLU A CA  
1304 C C   . GLU A 158 ? 0.3243 0.3562 0.2191 -0.0298 -0.0534 0.0612  158 GLU A C   
1305 O O   . GLU A 158 ? 0.3211 0.3515 0.2163 -0.0294 -0.0540 0.0706  158 GLU A O   
1306 C CB  . GLU A 158 ? 0.3641 0.3875 0.2396 -0.0335 -0.0401 0.0476  158 GLU A CB  
1307 C CG  . GLU A 158 ? 0.4340 0.4557 0.2986 -0.0355 -0.0401 0.0571  158 GLU A CG  
1308 C CD  . GLU A 158 ? 0.4816 0.4994 0.3264 -0.0397 -0.0338 0.0545  158 GLU A CD  
1309 O OE1 . GLU A 158 ? 0.4311 0.4484 0.2654 -0.0416 -0.0337 0.0633  158 GLU A OE1 
1310 O OE2 . GLU A 158 ? 0.5301 0.5457 0.3711 -0.0409 -0.0287 0.0439  158 GLU A OE2 
1311 N N   . GLU A 159 ? 0.3102 0.3478 0.2032 -0.0315 -0.0606 0.0601  159 GLU A N   
1312 C CA  A GLU A 159 ? 0.3252 0.3685 0.2175 -0.0329 -0.0706 0.0693  159 GLU A CA  
1313 C CA  B GLU A 159 ? 0.3298 0.3725 0.2227 -0.0325 -0.0701 0.0705  159 GLU A CA  
1314 C C   . GLU A 159 ? 0.3153 0.3634 0.2323 -0.0281 -0.0744 0.0736  159 GLU A C   
1315 O O   . GLU A 159 ? 0.3154 0.3695 0.2370 -0.0287 -0.0835 0.0809  159 GLU A O   
1316 C CB  A GLU A 159 ? 0.3288 0.3764 0.2086 -0.0377 -0.0768 0.0645  159 GLU A CB  
1317 C CB  B GLU A 159 ? 0.3510 0.3968 0.2235 -0.0385 -0.0765 0.0693  159 GLU A CB  
1318 C CG  A GLU A 159 ? 0.3433 0.3866 0.1992 -0.0428 -0.0728 0.0579  159 GLU A CG  
1319 C CG  B GLU A 159 ? 0.3626 0.4029 0.2118 -0.0427 -0.0702 0.0639  159 GLU A CG  
1320 C CD  A GLU A 159 ? 0.3669 0.4141 0.2088 -0.0484 -0.0802 0.0539  159 GLU A CD  
1321 C CD  B GLU A 159 ? 0.3836 0.4191 0.2232 -0.0431 -0.0645 0.0704  159 GLU A CD  
1322 O OE1 A GLU A 159 ? 0.3830 0.4270 0.2041 -0.0530 -0.0773 0.0487  159 GLU A OE1 
1323 O OE1 B GLU A 159 ? 0.3820 0.4183 0.2291 -0.0409 -0.0673 0.0824  159 GLU A OE1 
1324 O OE2 A GLU A 159 ? 0.3543 0.4081 0.2066 -0.0485 -0.0888 0.0559  159 GLU A OE2 
1325 O OE2 B GLU A 159 ? 0.4003 0.4311 0.2258 -0.0456 -0.0567 0.0637  159 GLU A OE2 
1326 N N   . GLY A 160 ? 0.2972 0.3433 0.2304 -0.0236 -0.0678 0.0685  160 GLY A N   
1327 C CA  . GLY A 160 ? 0.2976 0.3484 0.2542 -0.0191 -0.0700 0.0705  160 GLY A CA  
1328 C C   . GLY A 160 ? 0.3026 0.3523 0.2738 -0.0158 -0.0713 0.0806  160 GLY A C   
1329 O O   . GLY A 160 ? 0.2875 0.3337 0.2492 -0.0176 -0.0723 0.0882  160 GLY A O   
1330 N N   . GLU A 161 ? 0.2931 0.3459 0.2883 -0.0111 -0.0712 0.0812  161 GLU A N   
1331 C CA  . GLU A 161 ? 0.3103 0.3614 0.3247 -0.0073 -0.0716 0.0898  161 GLU A CA  
1332 C C   . GLU A 161 ? 0.2969 0.3393 0.3106 -0.0062 -0.0634 0.0871  161 GLU A C   
1333 O O   . GLU A 161 ? 0.2846 0.3244 0.3006 -0.0047 -0.0561 0.0759  161 GLU A O   
1334 C CB  . GLU A 161 ? 0.3364 0.3921 0.3773 -0.0023 -0.0704 0.0868  161 GLU A CB  
1335 C CG  . GLU A 161 ? 0.3498 0.4039 0.4158 0.0022  -0.0706 0.0947  161 GLU A CG  
1336 C CD  . GLU A 161 ? 0.3708 0.4290 0.4420 0.0014  -0.0810 0.1105  161 GLU A CD  
1337 O OE1 . GLU A 161 ? 0.3925 0.4574 0.4540 -0.0018 -0.0890 0.1137  161 GLU A OE1 
1338 O OE2 . GLU A 161 ? 0.4140 0.4687 0.4989 0.0037  -0.0816 0.1198  161 GLU A OE2 
1339 N N   . LEU A 162 ? 0.2990 0.3374 0.3097 -0.0071 -0.0648 0.0975  162 LEU A N   
1340 C CA  . LEU A 162 ? 0.3105 0.3408 0.3210 -0.0068 -0.0571 0.0955  162 LEU A CA  
1341 C C   . LEU A 162 ? 0.3045 0.3319 0.3425 -0.0015 -0.0523 0.0916  162 LEU A C   
1342 O O   . LEU A 162 ? 0.3009 0.3297 0.3600 0.0017  -0.0554 0.0991  162 LEU A O   
1343 C CB  . LEU A 162 ? 0.3334 0.3605 0.3349 -0.0093 -0.0590 0.1088  162 LEU A CB  
1344 C CG  . LEU A 162 ? 0.3479 0.3669 0.3504 -0.0094 -0.0505 0.1074  162 LEU A CG  
1345 C CD1 . LEU A 162 ? 0.3577 0.3742 0.3423 -0.0121 -0.0442 0.0951  162 LEU A CD1 
1346 C CD2 . LEU A 162 ? 0.3788 0.3954 0.3742 -0.0118 -0.0521 0.1227  162 LEU A CD2 
1347 N N   . MET A 163 ? 0.3061 0.3291 0.3440 -0.0010 -0.0447 0.0802  163 MET A N   
1348 C CA  . MET A 163 ? 0.3327 0.3524 0.3941 0.0032  -0.0397 0.0742  163 MET A CA  
1349 C C   . MET A 163 ? 0.3272 0.3394 0.3872 0.0021  -0.0334 0.0701  163 MET A C   
1350 O O   . MET A 163 ? 0.3082 0.3191 0.3493 -0.0011 -0.0311 0.0657  163 MET A O   
1351 C CB  . MET A 163 ? 0.3323 0.3569 0.3993 0.0055  -0.0374 0.0617  163 MET A CB  
1352 C CG  . MET A 163 ? 0.3743 0.4051 0.4575 0.0084  -0.0419 0.0667  163 MET A CG  
1353 S SD  . MET A 163 ? 0.4663 0.5029 0.5578 0.0112  -0.0373 0.0527  163 MET A SD  
1354 C CE  . MET A 163 ? 0.4372 0.4680 0.5530 0.0156  -0.0298 0.0442  163 MET A CE  
1355 N N   . ILE A 164 ? 0.3419 0.3491 0.4245 0.0049  -0.0308 0.0720  164 ILE A N   
1356 C CA  . ILE A 164 ? 0.3595 0.3599 0.4475 0.0044  -0.0247 0.0656  164 ILE A CA  
1357 C C   . ILE A 164 ? 0.3218 0.3241 0.4072 0.0050  -0.0212 0.0487  164 ILE A C   
1358 O O   . ILE A 164 ? 0.2829 0.2891 0.3781 0.0079  -0.0213 0.0424  164 ILE A O   
1359 C CB  . ILE A 164 ? 0.3810 0.3758 0.4979 0.0074  -0.0232 0.0706  164 ILE A CB  
1360 C CG1 . ILE A 164 ? 0.4484 0.4422 0.5664 0.0065  -0.0273 0.0897  164 ILE A CG1 
1361 C CG2 . ILE A 164 ? 0.3951 0.3831 0.5219 0.0069  -0.0171 0.0622  164 ILE A CG2 
1362 C CD1 . ILE A 164 ? 0.4841 0.4767 0.5774 0.0017  -0.0268 0.0964  164 ILE A CD1 
1363 N N   . PRO A 165 ? 0.3191 0.3195 0.3916 0.0023  -0.0180 0.0415  165 PRO A N   
1364 C CA  . PRO A 165 ? 0.3113 0.3150 0.3783 0.0024  -0.0160 0.0272  165 PRO A CA  
1365 C C   . PRO A 165 ? 0.3067 0.3100 0.3937 0.0058  -0.0135 0.0171  165 PRO A C   
1366 O O   . PRO A 165 ? 0.2936 0.3023 0.3780 0.0071  -0.0130 0.0085  165 PRO A O   
1367 C CB  . PRO A 165 ? 0.3162 0.3168 0.3724 -0.0008 -0.0133 0.0236  165 PRO A CB  
1368 C CG  . PRO A 165 ? 0.3266 0.3245 0.3737 -0.0034 -0.0139 0.0363  165 PRO A CG  
1369 C CD  . PRO A 165 ? 0.3392 0.3355 0.4006 -0.0013 -0.0162 0.0473  165 PRO A CD  
1370 N N   . LYS A 166 ? 0.3117 0.3086 0.4189 0.0070  -0.0114 0.0180  166 LYS A N   
1371 C CA  . LYS A 166 ? 0.3323 0.3279 0.4604 0.0100  -0.0084 0.0072  166 LYS A CA  
1372 C C   . LYS A 166 ? 0.3055 0.3065 0.4414 0.0136  -0.0092 0.0070  166 LYS A C   
1373 O O   . LYS A 166 ? 0.3059 0.3104 0.4458 0.0154  -0.0063 -0.0054 166 LYS A O   
1374 C CB  . LYS A 166 ? 0.3871 0.3744 0.5387 0.0107  -0.0067 0.0121  166 LYS A CB  
1375 C CG  . LYS A 166 ? 0.4451 0.4290 0.6226 0.0137  -0.0032 0.0010  166 LYS A CG  
1376 C CD  . LYS A 166 ? 0.5068 0.4816 0.7085 0.0137  -0.0016 0.0069  166 LYS A CD  
1377 C CE  . LYS A 166 ? 0.5843 0.5548 0.8161 0.0171  0.0019  -0.0030 166 LYS A CE  
1378 N NZ  . LYS A 166 ? 0.6518 0.6129 0.9066 0.0161  0.0039  -0.0006 166 LYS A NZ  
1379 N N   . ASN A 167 ? 0.2933 0.2954 0.4314 0.0144  -0.0130 0.0213  167 ASN A N   
1380 C CA  . ASN A 167 ? 0.2932 0.3007 0.4425 0.0177  -0.0144 0.0236  167 ASN A CA  
1381 C C   . ASN A 167 ? 0.2762 0.2921 0.4069 0.0169  -0.0151 0.0181  167 ASN A C   
1382 O O   . ASN A 167 ? 0.2744 0.2954 0.4153 0.0198  -0.0132 0.0127  167 ASN A O   
1383 C CB  . ASN A 167 ? 0.3084 0.3155 0.4662 0.0185  -0.0197 0.0414  167 ASN A CB  
1384 C CG  . ASN A 167 ? 0.3402 0.3397 0.5246 0.0206  -0.0182 0.0470  167 ASN A CG  
1385 O OD1 . ASN A 167 ? 0.3391 0.3340 0.5399 0.0223  -0.0129 0.0358  167 ASN A OD1 
1386 N ND2 . ASN A 167 ? 0.3484 0.3465 0.5369 0.0202  -0.0230 0.0644  167 ASN A ND2 
1387 N N   . PHE A 168 ? 0.2605 0.2781 0.3660 0.0131  -0.0173 0.0193  168 PHE A N   
1388 C CA  . PHE A 168 ? 0.2500 0.2751 0.3400 0.0122  -0.0176 0.0142  168 PHE A CA  
1389 C C   . PHE A 168 ? 0.2451 0.2724 0.3355 0.0132  -0.0123 -0.0011 168 PHE A C   
1390 O O   . PHE A 168 ? 0.2262 0.2604 0.3146 0.0143  -0.0107 -0.0060 168 PHE A O   
1391 C CB  . PHE A 168 ? 0.2467 0.2722 0.3122 0.0079  -0.0206 0.0184  168 PHE A CB  
1392 C CG  . PHE A 168 ? 0.2418 0.2746 0.2933 0.0067  -0.0216 0.0151  168 PHE A CG  
1393 C CD1 . PHE A 168 ? 0.2463 0.2856 0.3040 0.0083  -0.0236 0.0181  168 PHE A CD1 
1394 C CD2 . PHE A 168 ? 0.2342 0.2675 0.2683 0.0039  -0.0205 0.0097  168 PHE A CD2 
1395 C CE1 . PHE A 168 ? 0.2319 0.2777 0.2784 0.0069  -0.0241 0.0156  168 PHE A CE1 
1396 C CE2 . PHE A 168 ? 0.2280 0.2674 0.2510 0.0027  -0.0213 0.0077  168 PHE A CE2 
1397 C CZ  . PHE A 168 ? 0.2370 0.2826 0.2661 0.0041  -0.0229 0.0106  168 PHE A CZ  
1398 N N   . GLY A 169 ? 0.2450 0.2671 0.3370 0.0124  -0.0097 -0.0085 169 GLY A N   
1399 C CA  . GLY A 169 ? 0.2571 0.2815 0.3498 0.0131  -0.0053 -0.0234 169 GLY A CA  
1400 C C   . GLY A 169 ? 0.2717 0.2980 0.3841 0.0171  -0.0012 -0.0297 169 GLY A C   
1401 O O   . GLY A 169 ? 0.2873 0.3198 0.3950 0.0179  0.0023  -0.0393 169 GLY A O   
1402 N N   . LYS A 170 ? 0.2852 0.3067 0.4203 0.0197  -0.0012 -0.0239 170 LYS A N   
1403 C CA  . LYS A 170 ? 0.3201 0.3427 0.4783 0.0240  0.0031  -0.0288 170 LYS A CA  
1404 C C   . LYS A 170 ? 0.3123 0.3439 0.4686 0.0256  0.0028  -0.0248 170 LYS A C   
1405 O O   . LYS A 170 ? 0.3232 0.3595 0.4888 0.0282  0.0084  -0.0339 170 LYS A O   
1406 C CB  . LYS A 170 ? 0.3731 0.3886 0.5576 0.0264  0.0020  -0.0200 170 LYS A CB  
1407 C CG  . LYS A 170 ? 0.4031 0.4093 0.5953 0.0250  0.0031  -0.0239 170 LYS A CG  
1408 C CD  . LYS A 170 ? 0.4617 0.4607 0.6840 0.0277  0.0033  -0.0163 170 LYS A CD  
1409 C CE  . LYS A 170 ? 0.4921 0.4820 0.7226 0.0258  0.0045  -0.0198 170 LYS A CE  
1410 N NZ  . LYS A 170 ? 0.5414 0.5242 0.8066 0.0291  0.0065  -0.0163 170 LYS A NZ  
1411 N N   . LEU A 171 ? 0.2964 0.3305 0.4411 0.0238  -0.0033 -0.0116 171 LEU A N   
1412 C CA  . LEU A 171 ? 0.2930 0.3358 0.4355 0.0245  -0.0047 -0.0071 171 LEU A CA  
1413 C C   . LEU A 171 ? 0.2615 0.3110 0.3860 0.0230  -0.0008 -0.0172 171 LEU A C   
1414 O O   . LEU A 171 ? 0.2522 0.3086 0.3837 0.0251  0.0032  -0.0209 171 LEU A O   
1415 C CB  . LEU A 171 ? 0.2956 0.3387 0.4272 0.0218  -0.0130 0.0080  171 LEU A CB  
1416 C CG  . LEU A 171 ? 0.3061 0.3580 0.4352 0.0216  -0.0163 0.0138  171 LEU A CG  
1417 C CD1 . LEU A 171 ? 0.3084 0.3647 0.4653 0.0261  -0.0145 0.0154  171 LEU A CD1 
1418 C CD2 . LEU A 171 ? 0.2996 0.3509 0.4160 0.0183  -0.0250 0.0272  171 LEU A CD2 
1419 N N   . LEU A 172 ? 0.2468 0.2947 0.3492 0.0194  -0.0020 -0.0203 172 LEU A N   
1420 C CA  . LEU A 172 ? 0.2534 0.3078 0.3384 0.0177  0.0008  -0.0277 172 LEU A CA  
1421 C C   . LEU A 172 ? 0.2658 0.3235 0.3583 0.0201  0.0085  -0.0414 172 LEU A C   
1422 O O   . LEU A 172 ? 0.2695 0.3352 0.3548 0.0201  0.0122  -0.0453 172 LEU A O   
1423 C CB  . LEU A 172 ? 0.2501 0.3011 0.3150 0.0139  -0.0018 -0.0294 172 LEU A CB  
1424 C CG  . LEU A 172 ? 0.2456 0.2951 0.2973 0.0108  -0.0078 -0.0184 172 LEU A CG  
1425 C CD1 . LEU A 172 ? 0.2499 0.2945 0.2887 0.0078  -0.0092 -0.0204 172 LEU A CD1 
1426 C CD2 . LEU A 172 ? 0.2508 0.3079 0.2921 0.0096  -0.0088 -0.0151 172 LEU A CD2 
1427 N N   . ASP A 173 ? 0.2658 0.3174 0.3721 0.0217  0.0113  -0.0491 173 ASP A N   
1428 C CA  . ASP A 173 ? 0.2886 0.3422 0.4022 0.0236  0.0189  -0.0644 173 ASP A CA  
1429 C C   . ASP A 173 ? 0.2946 0.3532 0.4280 0.0278  0.0249  -0.0658 173 ASP A C   
1430 O O   . ASP A 173 ? 0.3147 0.3761 0.4541 0.0296  0.0328  -0.0792 173 ASP A O   
1431 C CB  . ASP A 173 ? 0.3009 0.3455 0.4266 0.0239  0.0197  -0.0723 173 ASP A CB  
1432 C CG  . ASP A 173 ? 0.3368 0.3832 0.4661 0.0249  0.0271  -0.0906 173 ASP A CG  
1433 O OD1 . ASP A 173 ? 0.3574 0.4103 0.4655 0.0226  0.0288  -0.0983 173 ASP A OD1 
1434 O OD2 . ASP A 173 ? 0.3806 0.4225 0.5339 0.0279  0.0314  -0.0969 173 ASP A OD2 
1435 N N   . LYS A 174 ? 0.2905 0.3509 0.4342 0.0292  0.0213  -0.0526 174 LYS A N   
1436 C CA  . LYS A 174 ? 0.2968 0.3628 0.4615 0.0331  0.0262  -0.0522 174 LYS A CA  
1437 C C   . LYS A 174 ? 0.2903 0.3672 0.4418 0.0321  0.0292  -0.0523 174 LYS A C   
1438 O O   . LYS A 174 ? 0.2832 0.3664 0.4513 0.0351  0.0344  -0.0527 174 LYS A O   
1439 C CB  . LYS A 174 ? 0.2988 0.3626 0.4831 0.0350  0.0197  -0.0369 174 LYS A CB  
1440 C CG  . LYS A 174 ? 0.3273 0.3811 0.5304 0.0366  0.0172  -0.0339 174 LYS A CG  
1441 C CD  . LYS A 174 ? 0.3404 0.3935 0.5577 0.0377  0.0092  -0.0160 174 LYS A CD  
1442 C CE  . LYS A 174 ? 0.3790 0.4224 0.6110 0.0384  0.0054  -0.0089 174 LYS A CE  
1443 N NZ  . LYS A 174 ? 0.3853 0.4239 0.6453 0.0425  0.0127  -0.0188 174 LYS A NZ  
1444 N N   . PHE A 175 ? 0.2859 0.3649 0.4100 0.0280  0.0261  -0.0513 175 PHE A N   
1445 C CA  . PHE A 175 ? 0.2868 0.3755 0.3981 0.0264  0.0284  -0.0496 175 PHE A CA  
1446 C C   . PHE A 175 ? 0.3078 0.4002 0.3990 0.0246  0.0342  -0.0615 175 PHE A C   
1447 O O   . PHE A 175 ? 0.3069 0.3940 0.3911 0.0236  0.0341  -0.0701 175 PHE A O   
1448 C CB  . PHE A 175 ? 0.2821 0.3708 0.3814 0.0232  0.0194  -0.0363 175 PHE A CB  
1449 C CG  . PHE A 175 ? 0.2696 0.3563 0.3866 0.0245  0.0130  -0.0245 175 PHE A CG  
1450 C CD1 . PHE A 175 ? 0.2866 0.3803 0.4217 0.0267  0.0143  -0.0196 175 PHE A CD1 
1451 C CD2 . PHE A 175 ? 0.2842 0.3623 0.4018 0.0238  0.0061  -0.0183 175 PHE A CD2 
1452 C CE1 . PHE A 175 ? 0.2751 0.3679 0.4270 0.0278  0.0072  -0.0081 175 PHE A CE1 
1453 C CE2 . PHE A 175 ? 0.2756 0.3527 0.4079 0.0247  -0.0004 -0.0066 175 PHE A CE2 
1454 C CZ  . PHE A 175 ? 0.2702 0.3546 0.4197 0.0268  -0.0004 -0.0016 175 PHE A CZ  
1455 N N   . LYS A 176 ? 0.3207 0.4228 0.4035 0.0238  0.0389  -0.0614 176 LYS A N   
1456 C CA  . LYS A 176 ? 0.3537 0.4614 0.4164 0.0219  0.0446  -0.0709 176 LYS A CA  
1457 C C   . LYS A 176 ? 0.3386 0.4459 0.3770 0.0176  0.0376  -0.0649 176 LYS A C   
1458 O O   . LYS A 176 ? 0.3286 0.4362 0.3500 0.0155  0.0379  -0.0723 176 LYS A O   
1459 C CB  . LYS A 176 ? 0.3837 0.5026 0.4488 0.0230  0.0538  -0.0719 176 LYS A CB  
1460 C CG  . LYS A 176 ? 0.4301 0.5510 0.5221 0.0276  0.0622  -0.0776 176 LYS A CG  
1461 C CD  . LYS A 176 ? 0.4768 0.6091 0.5742 0.0285  0.0704  -0.0749 176 LYS A CD  
1462 C CE  . LYS A 176 ? 0.5178 0.6524 0.6470 0.0333  0.0775  -0.0773 176 LYS A CE  
1463 N NZ  . LYS A 176 ? 0.5841 0.7126 0.7241 0.0362  0.0829  -0.0916 176 LYS A NZ  
1464 N N   . LYS A 177 ? 0.3027 0.4100 0.3406 0.0161  0.0313  -0.0520 177 LYS A N   
1465 C CA  . LYS A 177 ? 0.2906 0.3994 0.3083 0.0122  0.0266  -0.0460 177 LYS A CA  
1466 C C   . LYS A 177 ? 0.2757 0.3786 0.2958 0.0107  0.0177  -0.0349 177 LYS A C   
1467 O O   . LYS A 177 ? 0.2720 0.3781 0.2889 0.0088  0.0150  -0.0265 177 LYS A O   
1468 C CB  . LYS A 177 ? 0.2968 0.4164 0.3079 0.0112  0.0324  -0.0438 177 LYS A CB  
1469 C CG  . LYS A 177 ? 0.3168 0.4389 0.3062 0.0075  0.0294  -0.0401 177 LYS A CG  
1470 C CD  . LYS A 177 ? 0.3397 0.4726 0.3229 0.0063  0.0353  -0.0362 177 LYS A CD  
1471 C CE  . LYS A 177 ? 0.3651 0.5015 0.3263 0.0031  0.0340  -0.0352 177 LYS A CE  
1472 N NZ  . LYS A 177 ? 0.3506 0.4962 0.3067 0.0013  0.0379  -0.0271 177 LYS A NZ  
1473 N N   . PRO A 178 ? 0.2641 0.3581 0.2906 0.0114  0.0132  -0.0349 178 PRO A N   
1474 C CA  . PRO A 178 ? 0.2501 0.3388 0.2784 0.0100  0.0056  -0.0249 178 PRO A CA  
1475 C C   . PRO A 178 ? 0.2489 0.3361 0.2590 0.0062  0.0011  -0.0212 178 PRO A C   
1476 O O   . PRO A 178 ? 0.2544 0.3399 0.2533 0.0050  0.0015  -0.0263 178 PRO A O   
1477 C CB  . PRO A 178 ? 0.2604 0.3404 0.2977 0.0116  0.0037  -0.0271 178 PRO A CB  
1478 C CG  . PRO A 178 ? 0.2701 0.3494 0.3025 0.0120  0.0082  -0.0388 178 PRO A CG  
1479 C CD  . PRO A 178 ? 0.2714 0.3600 0.3028 0.0131  0.0154  -0.0445 178 PRO A CD  
1480 N N   . THR A 179 ? 0.2427 0.3305 0.2515 0.0042  -0.0032 -0.0126 179 THR A N   
1481 C CA  . THR A 179 ? 0.2405 0.3259 0.2357 0.0007  -0.0074 -0.0087 179 THR A CA  
1482 C C   . THR A 179 ? 0.2279 0.3053 0.2233 -0.0004 -0.0132 -0.0043 179 THR A C   
1483 O O   . THR A 179 ? 0.2151 0.2921 0.2205 0.0005  -0.0157 0.0002  179 THR A O   
1484 C CB  . THR A 179 ? 0.2490 0.3412 0.2434 -0.0010 -0.0071 -0.0037 179 THR A CB  
1485 O OG1 . THR A 179 ? 0.2940 0.3936 0.2864 0.0000  -0.0007 -0.0079 179 THR A OG1 
1486 C CG2 . THR A 179 ? 0.2570 0.3466 0.2408 -0.0046 -0.0112 0.0004  179 THR A CG2 
1487 N N   . VAL A 180 ? 0.2331 0.3050 0.2181 -0.0023 -0.0149 -0.0053 180 VAL A N   
1488 C CA  . VAL A 180 ? 0.2181 0.2827 0.2003 -0.0039 -0.0191 -0.0014 180 VAL A CA  
1489 C C   . VAL A 180 ? 0.2261 0.2894 0.1970 -0.0073 -0.0210 0.0006  180 VAL A C   
1490 O O   . VAL A 180 ? 0.2035 0.2679 0.1683 -0.0079 -0.0194 -0.0023 180 VAL A O   
1491 C CB  . VAL A 180 ? 0.2148 0.2731 0.1992 -0.0027 -0.0182 -0.0048 180 VAL A CB  
1492 C CG1 . VAL A 180 ? 0.2212 0.2724 0.2007 -0.0048 -0.0211 -0.0003 180 VAL A CG1 
1493 C CG2 . VAL A 180 ? 0.2249 0.2833 0.2237 0.0006  -0.0162 -0.0066 180 VAL A CG2 
1494 N N   . ILE A 181 ? 0.2198 0.2808 0.1885 -0.0094 -0.0248 0.0056  181 ILE A N   
1495 C CA  . ILE A 181 ? 0.2318 0.2908 0.1919 -0.0127 -0.0264 0.0069  181 ILE A CA  
1496 C C   . ILE A 181 ? 0.2304 0.2818 0.1841 -0.0143 -0.0274 0.0074  181 ILE A C   
1497 O O   . ILE A 181 ? 0.2195 0.2685 0.1739 -0.0144 -0.0297 0.0106  181 ILE A O   
1498 C CB  . ILE A 181 ? 0.2521 0.3149 0.2143 -0.0147 -0.0294 0.0105  181 ILE A CB  
1499 C CG1 . ILE A 181 ? 0.2691 0.3400 0.2384 -0.0134 -0.0270 0.0105  181 ILE A CG1 
1500 C CG2 . ILE A 181 ? 0.2714 0.3305 0.2257 -0.0184 -0.0310 0.0106  181 ILE A CG2 
1501 C CD1 . ILE A 181 ? 0.3020 0.3777 0.2786 -0.0147 -0.0299 0.0144  181 ILE A CD1 
1502 N N   . VAL A 182 ? 0.2149 0.2630 0.1629 -0.0157 -0.0257 0.0050  182 VAL A N   
1503 C CA  . VAL A 182 ? 0.2290 0.2702 0.1711 -0.0174 -0.0253 0.0052  182 VAL A CA  
1504 C C   . VAL A 182 ? 0.2182 0.2579 0.1548 -0.0204 -0.0252 0.0044  182 VAL A C   
1505 O O   . VAL A 182 ? 0.2242 0.2664 0.1630 -0.0203 -0.0242 0.0030  182 VAL A O   
1506 C CB  . VAL A 182 ? 0.2331 0.2712 0.1773 -0.0161 -0.0224 0.0023  182 VAL A CB  
1507 C CG1 . VAL A 182 ? 0.2378 0.2694 0.1772 -0.0181 -0.0207 0.0028  182 VAL A CG1 
1508 C CG2 . VAL A 182 ? 0.2431 0.2821 0.1949 -0.0133 -0.0221 0.0016  182 VAL A CG2 
1509 N N   . GLY A 183 ? 0.2219 0.2575 0.1517 -0.0231 -0.0260 0.0052  183 GLY A N   
1510 C CA  . GLY A 183 ? 0.2444 0.2781 0.1705 -0.0260 -0.0253 0.0030  183 GLY A CA  
1511 C C   . GLY A 183 ? 0.2471 0.2770 0.1744 -0.0259 -0.0211 0.0002  183 GLY A C   
1512 O O   . GLY A 183 ? 0.2449 0.2711 0.1705 -0.0255 -0.0185 -0.0002 183 GLY A O   
1513 N N   . GLY A 184 ? 0.2513 0.2822 0.1828 -0.0266 -0.0204 -0.0011 184 GLY A N   
1514 C CA  . GLY A 184 ? 0.2626 0.2906 0.1981 -0.0265 -0.0170 -0.0031 184 GLY A CA  
1515 C C   . GLY A 184 ? 0.3132 0.3353 0.2463 -0.0293 -0.0138 -0.0063 184 GLY A C   
1516 O O   . GLY A 184 ? 0.2986 0.3193 0.2387 -0.0296 -0.0117 -0.0078 184 GLY A O   
1517 N N   . PHE A 185 ? 0.3567 0.3759 0.2802 -0.0314 -0.0137 -0.0075 185 PHE A N   
1518 C CA  . PHE A 185 ? 0.3551 0.3692 0.2734 -0.0347 -0.0105 -0.0120 185 PHE A CA  
1519 C C   . PHE A 185 ? 0.3713 0.3817 0.2805 -0.0354 -0.0068 -0.0124 185 PHE A C   
1520 O O   . PHE A 185 ? 0.4058 0.4178 0.3117 -0.0340 -0.0087 -0.0083 185 PHE A O   
1521 C CB  . PHE A 185 ? 0.3485 0.3637 0.2623 -0.0376 -0.0145 -0.0134 185 PHE A CB  
1522 C CG  . PHE A 185 ? 0.3499 0.3695 0.2583 -0.0375 -0.0203 -0.0092 185 PHE A CG  
1523 C CD1 . PHE A 185 ? 0.3551 0.3734 0.2511 -0.0392 -0.0216 -0.0084 185 PHE A CD1 
1524 C CD2 . PHE A 185 ? 0.3190 0.3444 0.2355 -0.0355 -0.0242 -0.0056 185 PHE A CD2 
1525 C CE1 . PHE A 185 ? 0.3373 0.3601 0.2315 -0.0386 -0.0275 -0.0033 185 PHE A CE1 
1526 C CE2 . PHE A 185 ? 0.3137 0.3435 0.2285 -0.0349 -0.0290 -0.0017 185 PHE A CE2 
1527 C CZ  . PHE A 185 ? 0.3206 0.3490 0.2253 -0.0363 -0.0310 -0.0004 185 PHE A CZ  
1528 N N   . PRO A 186 ? 0.3872 0.3925 0.2933 -0.0374 -0.0006 -0.0169 186 PRO A N   
1529 C CA  . PRO A 186 ? 0.4050 0.4072 0.3035 -0.0379 0.0043  -0.0164 186 PRO A CA  
1530 C C   . PRO A 186 ? 0.4466 0.4485 0.3278 -0.0407 0.0023  -0.0146 186 PRO A C   
1531 O O   . PRO A 186 ? 0.4755 0.4768 0.3512 -0.0404 0.0039  -0.0103 186 PRO A O   
1532 C CB  . PRO A 186 ? 0.4073 0.4047 0.3089 -0.0394 0.0124  -0.0225 186 PRO A CB  
1533 C CG  . PRO A 186 ? 0.4055 0.4024 0.3101 -0.0412 0.0106  -0.0274 186 PRO A CG  
1534 C CD  . PRO A 186 ? 0.3853 0.3876 0.2966 -0.0392 0.0027  -0.0228 186 PRO A CD  
1535 N N   . HIS A 187 ? 0.4600 0.4627 0.3334 -0.0436 -0.0014 -0.0175 187 HIS A N   
1536 C CA  . HIS A 187 ? 0.5309 0.5346 0.3875 -0.0466 -0.0052 -0.0153 187 HIS A CA  
1537 C C   . HIS A 187 ? 0.5522 0.5590 0.4075 -0.0488 -0.0127 -0.0174 187 HIS A C   
1538 O O   . HIS A 187 ? 0.5291 0.5361 0.3956 -0.0485 -0.0131 -0.0212 187 HIS A O   
1539 C CB  . HIS A 187 ? 0.5278 0.5272 0.3694 -0.0500 0.0020  -0.0192 187 HIS A CB  
1540 C CG  . HIS A 187 ? 0.5769 0.5722 0.4214 -0.0520 0.0082  -0.0292 187 HIS A CG  
1541 N ND1 . HIS A 187 ? 0.6514 0.6466 0.4934 -0.0551 0.0048  -0.0359 187 HIS A ND1 
1542 C CD2 . HIS A 187 ? 0.6100 0.6013 0.4630 -0.0511 0.0174  -0.0336 187 HIS A CD2 
1543 C CE1 . HIS A 187 ? 0.6381 0.6287 0.4871 -0.0559 0.0121  -0.0442 187 HIS A CE1 
1544 N NE2 . HIS A 187 ? 0.6617 0.6502 0.5180 -0.0533 0.0197  -0.0427 187 HIS A NE2 
1545 N N   . GLY A 188 ? 0.5556 0.5652 0.3982 -0.0512 -0.0187 -0.0140 188 GLY A N   
1546 C CA  . GLY A 188 ? 0.5297 0.5429 0.3705 -0.0540 -0.0268 -0.0157 188 GLY A CA  
1547 C C   . GLY A 188 ? 0.4935 0.5128 0.3465 -0.0508 -0.0341 -0.0084 188 GLY A C   
1548 O O   . GLY A 188 ? 0.4692 0.4899 0.3281 -0.0469 -0.0336 -0.0020 188 GLY A O   
1549 N N   . ASP A 189 ? 0.5003 0.5232 0.3574 -0.0529 -0.0405 -0.0102 189 ASP A N   
1550 C CA  . ASP A 189 ? 0.4920 0.5216 0.3603 -0.0508 -0.0475 -0.0039 189 ASP A CA  
1551 C C   . ASP A 189 ? 0.4115 0.4423 0.2973 -0.0475 -0.0446 -0.0046 189 ASP A C   
1552 O O   . ASP A 189 ? 0.3768 0.4038 0.2657 -0.0484 -0.0399 -0.0102 189 ASP A O   
1553 C CB  . ASP A 189 ? 0.5265 0.5601 0.3917 -0.0553 -0.0561 -0.0054 189 ASP A CB  
1554 C CG  . ASP A 189 ? 0.6494 0.6832 0.4949 -0.0596 -0.0608 -0.0049 189 ASP A CG  
1555 O OD1 . ASP A 189 ? 0.6776 0.7098 0.5135 -0.0582 -0.0585 0.0001  189 ASP A OD1 
1556 O OD2 . ASP A 189 ? 0.6898 0.7253 0.5293 -0.0646 -0.0668 -0.0096 189 ASP A OD2 
1557 N N   . PHE A 190 ? 0.3822 0.4187 0.2794 -0.0442 -0.0476 0.0012  190 PHE A N   
1558 C CA  . PHE A 190 ? 0.3672 0.4069 0.2794 -0.0421 -0.0462 0.0014  190 PHE A CA  
1559 C C   . PHE A 190 ? 0.3991 0.4397 0.3158 -0.0460 -0.0490 -0.0025 190 PHE A C   
1560 O O   . PHE A 190 ? 0.3823 0.4234 0.2927 -0.0500 -0.0544 -0.0045 190 PHE A O   
1561 C CB  . PHE A 190 ? 0.3561 0.4025 0.2782 -0.0385 -0.0490 0.0076  190 PHE A CB  
1562 C CG  . PHE A 190 ? 0.3433 0.3890 0.2670 -0.0339 -0.0449 0.0101  190 PHE A CG  
1563 C CD1 . PHE A 190 ? 0.3087 0.3543 0.2384 -0.0312 -0.0397 0.0087  190 PHE A CD1 
1564 C CD2 . PHE A 190 ? 0.3407 0.3856 0.2601 -0.0328 -0.0467 0.0140  190 PHE A CD2 
1565 C CE1 . PHE A 190 ? 0.3221 0.3671 0.2535 -0.0276 -0.0366 0.0097  190 PHE A CE1 
1566 C CE2 . PHE A 190 ? 0.3120 0.3556 0.2349 -0.0289 -0.0429 0.0155  190 PHE A CE2 
1567 C CZ  . PHE A 190 ? 0.3251 0.3688 0.2541 -0.0264 -0.0380 0.0126  190 PHE A CZ  
1568 N N   . LYS A 191 ? 0.4009 0.4420 0.3291 -0.0451 -0.0457 -0.0033 191 LYS A N   
1569 C CA  . LYS A 191 ? 0.4486 0.4910 0.3856 -0.0486 -0.0483 -0.0057 191 LYS A CA  
1570 C C   . LYS A 191 ? 0.4588 0.5096 0.4088 -0.0470 -0.0514 0.0002  191 LYS A C   
1571 O O   . LYS A 191 ? 0.5308 0.5848 0.4875 -0.0502 -0.0563 -0.0002 191 LYS A O   
1572 C CB  . LYS A 191 ? 0.5283 0.5664 0.4728 -0.0488 -0.0428 -0.0087 191 LYS A CB  
1573 C CG  . LYS A 191 ? 0.6036 0.6342 0.5401 -0.0486 -0.0373 -0.0135 191 LYS A CG  
1574 C CD  . LYS A 191 ? 0.6923 0.7180 0.6383 -0.0505 -0.0335 -0.0180 191 LYS A CD  
1575 C CE  . LYS A 191 ? 0.7022 0.7317 0.6649 -0.0487 -0.0327 -0.0124 191 LYS A CE  
1576 N NZ  . LYS A 191 ? 0.6900 0.7156 0.6648 -0.0521 -0.0318 -0.0163 191 LYS A NZ  
1577 N N   . SER A 192 ? 0.4046 0.4589 0.3585 -0.0423 -0.0482 0.0050  192 SER A N   
1578 C CA  . SER A 192 ? 0.4339 0.4964 0.4003 -0.0402 -0.0489 0.0101  192 SER A CA  
1579 C C   . SER A 192 ? 0.5116 0.5784 0.4776 -0.0384 -0.0531 0.0135  192 SER A C   
1580 O O   . SER A 192 ? 0.5692 0.6356 0.5317 -0.0347 -0.0507 0.0150  192 SER A O   
1581 C CB  . SER A 192 ? 0.3795 0.4440 0.3500 -0.0363 -0.0426 0.0125  192 SER A CB  
1582 O OG  . SER A 192 ? 0.3267 0.3879 0.2998 -0.0377 -0.0394 0.0113  192 SER A OG  
1583 N N   . LYS A 193 ? 0.5025 0.5739 0.4751 -0.0410 -0.0595 0.0150  193 LYS A N   
1584 C CA  . LYS A 193 ? 0.5089 0.5858 0.4860 -0.0392 -0.0641 0.0197  193 LYS A CA  
1585 C C   . LYS A 193 ? 0.4986 0.5834 0.4925 -0.0357 -0.0607 0.0236  193 LYS A C   
1586 O O   . LYS A 193 ? 0.5936 0.6832 0.5994 -0.0375 -0.0610 0.0245  193 LYS A O   
1587 C CB  . LYS A 193 ? 0.6006 0.6797 0.5774 -0.0438 -0.0736 0.0199  193 LYS A CB  
1588 C CG  . LYS A 193 ? 0.6501 0.7221 0.6084 -0.0481 -0.0765 0.0148  193 LYS A CG  
1589 C CD  . LYS A 193 ? 0.6634 0.7289 0.6072 -0.0456 -0.0717 0.0144  193 LYS A CD  
1590 C CE  . LYS A 193 ? 0.7138 0.7757 0.6398 -0.0492 -0.0765 0.0130  193 LYS A CE  
1591 N NZ  . LYS A 193 ? 0.7138 0.7706 0.6299 -0.0544 -0.0761 0.0048  193 LYS A NZ  
1592 N N   . VAL A 194 ? 0.4161 0.5019 0.4110 -0.0309 -0.0565 0.0253  194 VAL A N   
1593 C CA  . VAL A 194 ? 0.3761 0.4692 0.3851 -0.0272 -0.0519 0.0278  194 VAL A CA  
1594 C C   . VAL A 194 ? 0.3422 0.4382 0.3583 -0.0243 -0.0550 0.0311  194 VAL A C   
1595 O O   . VAL A 194 ? 0.3027 0.3937 0.3096 -0.0245 -0.0589 0.0316  194 VAL A O   
1596 C CB  . VAL A 194 ? 0.3548 0.4465 0.3591 -0.0241 -0.0433 0.0254  194 VAL A CB  
1597 C CG1 . VAL A 194 ? 0.3547 0.4441 0.3545 -0.0268 -0.0407 0.0240  194 VAL A CG1 
1598 C CG2 . VAL A 194 ? 0.3676 0.4527 0.3608 -0.0218 -0.0420 0.0231  194 VAL A CG2 
1599 N N   . ASP A 195 ? 0.3197 0.4236 0.3528 -0.0214 -0.0526 0.0336  195 ASP A N   
1600 C CA  . ASP A 195 ? 0.3502 0.4566 0.3936 -0.0178 -0.0545 0.0368  195 ASP A CA  
1601 C C   . ASP A 195 ? 0.3262 0.4270 0.3622 -0.0140 -0.0488 0.0339  195 ASP A C   
1602 O O   . ASP A 195 ? 0.3477 0.4479 0.3798 -0.0123 -0.0410 0.0296  195 ASP A O   
1603 C CB  . ASP A 195 ? 0.3557 0.4718 0.4215 -0.0151 -0.0514 0.0393  195 ASP A CB  
1604 C CG  . ASP A 195 ? 0.4279 0.5511 0.5073 -0.0185 -0.0584 0.0435  195 ASP A CG  
1605 O OD1 . ASP A 195 ? 0.4281 0.5483 0.4982 -0.0234 -0.0667 0.0439  195 ASP A OD1 
1606 O OD2 . ASP A 195 ? 0.4405 0.5723 0.5404 -0.0163 -0.0553 0.0458  195 ASP A OD2 
1607 N N   . GLY A 196 ? 0.2946 0.3914 0.3287 -0.0130 -0.0532 0.0365  196 GLY A N   
1608 C CA  . GLY A 196 ? 0.2749 0.3666 0.3068 -0.0093 -0.0483 0.0342  196 GLY A CA  
1609 C C   . GLY A 196 ? 0.2585 0.3465 0.2911 -0.0087 -0.0541 0.0396  196 GLY A C   
1610 O O   . GLY A 196 ? 0.2492 0.3378 0.2780 -0.0118 -0.0624 0.0447  196 GLY A O   
1611 N N   . VAL A 197 ? 0.2409 0.3252 0.2782 -0.0049 -0.0497 0.0383  197 VAL A N   
1612 C CA  . VAL A 197 ? 0.2409 0.3213 0.2811 -0.0038 -0.0540 0.0443  197 VAL A CA  
1613 C C   . VAL A 197 ? 0.2303 0.3022 0.2501 -0.0065 -0.0542 0.0435  197 VAL A C   
1614 O O   . VAL A 197 ? 0.2061 0.2734 0.2207 -0.0055 -0.0478 0.0375  197 VAL A O   
1615 C CB  . VAL A 197 ? 0.2459 0.3258 0.3042 0.0016  -0.0485 0.0428  197 VAL A CB  
1616 C CG1 . VAL A 197 ? 0.2562 0.3316 0.3205 0.0028  -0.0529 0.0505  197 VAL A CG1 
1617 C CG2 . VAL A 197 ? 0.2636 0.3520 0.3425 0.0045  -0.0459 0.0420  197 VAL A CG2 
1618 N N   . LYS A 198 ? 0.2414 0.3115 0.2507 -0.0099 -0.0613 0.0497  198 LYS A N   
1619 C CA  . LYS A 198 ? 0.2633 0.3258 0.2539 -0.0125 -0.0599 0.0487  198 LYS A CA  
1620 C C   . LYS A 198 ? 0.2487 0.3059 0.2445 -0.0098 -0.0580 0.0528  198 LYS A C   
1621 O O   . LYS A 198 ? 0.2280 0.2868 0.2345 -0.0084 -0.0627 0.0612  198 LYS A O   
1622 C CB  . LYS A 198 ? 0.3269 0.3897 0.3016 -0.0177 -0.0672 0.0525  198 LYS A CB  
1623 C CG  . LYS A 198 ? 0.3703 0.4364 0.3391 -0.0211 -0.0684 0.0471  198 LYS A CG  
1624 C CD  . LYS A 198 ? 0.4520 0.5187 0.4064 -0.0265 -0.0761 0.0494  198 LYS A CD  
1625 C CE  . LYS A 198 ? 0.5499 0.6191 0.5013 -0.0300 -0.0772 0.0433  198 LYS A CE  
1626 N NZ  . LYS A 198 ? 0.6270 0.6967 0.5640 -0.0358 -0.0850 0.0439  198 LYS A NZ  
1627 N N   . ILE A 199 ? 0.2341 0.2849 0.2230 -0.0096 -0.0515 0.0474  199 ILE A N   
1628 C CA  . ILE A 199 ? 0.2382 0.2832 0.2336 -0.0073 -0.0482 0.0495  199 ILE A CA  
1629 C C   . ILE A 199 ? 0.2439 0.2825 0.2220 -0.0105 -0.0461 0.0496  199 ILE A C   
1630 O O   . ILE A 199 ? 0.2397 0.2765 0.2073 -0.0122 -0.0422 0.0422  199 ILE A O   
1631 C CB  . ILE A 199 ? 0.2373 0.2817 0.2456 -0.0035 -0.0414 0.0411  199 ILE A CB  
1632 C CG1 . ILE A 199 ? 0.2361 0.2872 0.2619 -0.0001 -0.0417 0.0400  199 ILE A CG1 
1633 C CG2 . ILE A 199 ? 0.2457 0.2833 0.2620 -0.0017 -0.0381 0.0422  199 ILE A CG2 
1634 C CD1 . ILE A 199 ? 0.2496 0.3016 0.2943 0.0027  -0.0453 0.0487  199 ILE A CD1 
1635 N N   . SER A 200 ? 0.2520 0.2875 0.2279 -0.0114 -0.0483 0.0586  200 SER A N   
1636 C CA  . SER A 200 ? 0.2661 0.2953 0.2295 -0.0138 -0.0443 0.0593  200 SER A CA  
1637 C C   . SER A 200 ? 0.2595 0.2833 0.2375 -0.0108 -0.0390 0.0588  200 SER A C   
1638 O O   . SER A 200 ? 0.2605 0.2845 0.2560 -0.0077 -0.0405 0.0640  200 SER A O   
1639 C CB  . SER A 200 ? 0.2859 0.3149 0.2361 -0.0171 -0.0490 0.0696  200 SER A CB  
1640 O OG  . SER A 200 ? 0.3029 0.3258 0.2434 -0.0190 -0.0435 0.0710  200 SER A OG  
1641 N N   . LEU A 201 ? 0.2636 0.2826 0.2360 -0.0120 -0.0331 0.0536  201 LEU A N   
1642 C CA  . LEU A 201 ? 0.2856 0.2992 0.2720 -0.0100 -0.0284 0.0534  201 LEU A CA  
1643 C C   . LEU A 201 ? 0.2966 0.3052 0.2757 -0.0126 -0.0260 0.0615  201 LEU A C   
1644 O O   . LEU A 201 ? 0.3270 0.3307 0.3182 -0.0116 -0.0219 0.0621  201 LEU A O   
1645 C CB  . LEU A 201 ? 0.2742 0.2867 0.2636 -0.0092 -0.0236 0.0413  201 LEU A CB  
1646 C CG  . LEU A 201 ? 0.2715 0.2892 0.2679 -0.0066 -0.0245 0.0332  201 LEU A CG  
1647 C CD1 . LEU A 201 ? 0.2721 0.2889 0.2699 -0.0064 -0.0204 0.0224  201 LEU A CD1 
1648 C CD2 . LEU A 201 ? 0.2732 0.2921 0.2886 -0.0029 -0.0261 0.0358  201 LEU A CD2 
1649 N N   . TYR A 202 ? 0.3031 0.3130 0.2628 -0.0162 -0.0281 0.0669  202 TYR A N   
1650 C CA  . TYR A 202 ? 0.3400 0.3460 0.2893 -0.0192 -0.0247 0.0742  202 TYR A CA  
1651 C C   . TYR A 202 ? 0.3780 0.3874 0.3048 -0.0231 -0.0291 0.0795  202 TYR A C   
1652 O O   . TYR A 202 ? 0.3623 0.3755 0.2800 -0.0242 -0.0322 0.0731  202 TYR A O   
1653 C CB  . TYR A 202 ? 0.3305 0.3327 0.2762 -0.0206 -0.0169 0.0657  202 TYR A CB  
1654 C CG  . TYR A 202 ? 0.3381 0.3353 0.2823 -0.0226 -0.0106 0.0721  202 TYR A CG  
1655 C CD1 . TYR A 202 ? 0.3414 0.3351 0.3031 -0.0208 -0.0093 0.0798  202 TYR A CD1 
1656 C CD2 . TYR A 202 ? 0.3465 0.3423 0.2738 -0.0262 -0.0050 0.0698  202 TYR A CD2 
1657 C CE1 . TYR A 202 ? 0.3446 0.3339 0.3064 -0.0228 -0.0029 0.0863  202 TYR A CE1 
1658 C CE2 . TYR A 202 ? 0.3472 0.3391 0.2739 -0.0281 0.0020  0.0758  202 TYR A CE2 
1659 C CZ  . TYR A 202 ? 0.3447 0.3334 0.2887 -0.0265 0.0030  0.0842  202 TYR A CZ  
1660 O OH  . TYR A 202 ? 0.3768 0.3617 0.3221 -0.0285 0.0106  0.0904  202 TYR A OH  
1661 N N   . ARG A 203 ? 0.4653 0.4735 0.3821 -0.0256 -0.0291 0.0908  203 ARG A N   
1662 C CA  . ARG A 203 ? 0.5333 0.5457 0.4270 -0.0297 -0.0342 0.0946  203 ARG A CA  
1663 C C   . ARG A 203 ? 0.5022 0.5121 0.3742 -0.0341 -0.0271 0.0893  203 ARG A C   
1664 O O   . ARG A 203 ? 0.4758 0.4875 0.3264 -0.0383 -0.0286 0.0946  203 ARG A O   
1665 C CB  . ARG A 203 ? 0.6982 0.7130 0.5896 -0.0306 -0.0407 0.1108  203 ARG A CB  
1666 C CG  . ARG A 203 ? 0.8177 0.8387 0.6872 -0.0347 -0.0491 0.1140  203 ARG A CG  
1667 C CD  . ARG A 203 ? 0.9124 0.9373 0.7790 -0.0351 -0.0532 0.1020  203 ARG A CD  
1668 N NE  . ARG A 203 ? 0.9720 0.9959 0.8141 -0.0400 -0.0492 0.0937  203 ARG A NE  
1669 C CZ  . ARG A 203 ? 0.8138 0.8402 0.6319 -0.0450 -0.0526 0.0984  203 ARG A CZ  
1670 N NH1 . ARG A 203 ? 0.8658 0.8889 0.6641 -0.0488 -0.0445 0.0932  203 ARG A NH1 
1671 N NH2 . ARG A 203 ? 0.6788 0.7112 0.4937 -0.0462 -0.0636 0.1090  203 ARG A NH2 
1672 N N   . GLU A 204 ? 0.4373 0.4437 0.3155 -0.0331 -0.0196 0.0786  204 GLU A N   
1673 C CA  . GLU A 204 ? 0.4422 0.4469 0.3038 -0.0365 -0.0132 0.0702  204 GLU A CA  
1674 C C   . GLU A 204 ? 0.4129 0.4182 0.2825 -0.0347 -0.0131 0.0574  204 GLU A C   
1675 O O   . GLU A 204 ? 0.3799 0.3858 0.2678 -0.0309 -0.0150 0.0551  204 GLU A O   
1676 C CB  . GLU A 204 ? 0.4368 0.4366 0.2991 -0.0375 -0.0029 0.0719  204 GLU A CB  
1677 C CG  . GLU A 204 ? 0.4908 0.4899 0.3465 -0.0393 -0.0019 0.0862  204 GLU A CG  
1678 C CD  . GLU A 204 ? 0.5246 0.5270 0.3520 -0.0441 -0.0044 0.0907  204 GLU A CD  
1679 O OE1 . GLU A 204 ? 0.5400 0.5444 0.3539 -0.0463 -0.0062 0.0810  204 GLU A OE1 
1680 O OE2 . GLU A 204 ? 0.5455 0.5486 0.3645 -0.0460 -0.0050 0.1041  204 GLU A OE2 
1681 N N   . PRO A 205 ? 0.4178 0.4232 0.2741 -0.0376 -0.0108 0.0489  205 PRO A N   
1682 C CA  . PRO A 205 ? 0.3963 0.4020 0.2610 -0.0361 -0.0099 0.0382  205 PRO A CA  
1683 C C   . PRO A 205 ? 0.3728 0.3752 0.2534 -0.0334 -0.0034 0.0348  205 PRO A C   
1684 O O   . PRO A 205 ? 0.3617 0.3607 0.2422 -0.0343 0.0032  0.0374  205 PRO A O   
1685 C CB  . PRO A 205 ? 0.4206 0.4257 0.2688 -0.0401 -0.0070 0.0310  205 PRO A CB  
1686 C CG  . PRO A 205 ? 0.4704 0.4738 0.3011 -0.0437 -0.0031 0.0365  205 PRO A CG  
1687 C CD  . PRO A 205 ? 0.4635 0.4689 0.2962 -0.0425 -0.0090 0.0491  205 PRO A CD  
1688 N N   . LEU A 206 ? 0.3484 0.3526 0.2430 -0.0303 -0.0060 0.0298  206 LEU A N   
1689 C CA  . LEU A 206 ? 0.3325 0.3349 0.2415 -0.0282 -0.0016 0.0250  206 LEU A CA  
1690 C C   . LEU A 206 ? 0.3072 0.3116 0.2178 -0.0280 -0.0021 0.0167  206 LEU A C   
1691 O O   . LEU A 206 ? 0.2903 0.2977 0.1953 -0.0285 -0.0064 0.0149  206 LEU A O   
1692 C CB  . LEU A 206 ? 0.3367 0.3399 0.2615 -0.0247 -0.0047 0.0275  206 LEU A CB  
1693 C CG  . LEU A 206 ? 0.3465 0.3473 0.2745 -0.0245 -0.0044 0.0369  206 LEU A CG  
1694 C CD1 . LEU A 206 ? 0.3468 0.3484 0.2924 -0.0209 -0.0078 0.0376  206 LEU A CD1 
1695 C CD2 . LEU A 206 ? 0.3534 0.3497 0.2825 -0.0262 0.0031  0.0389  206 LEU A CD2 
1696 N N   . MET A 207 ? 0.2933 0.2963 0.2133 -0.0272 0.0021  0.0123  207 MET A N   
1697 C CA  . MET A 207 ? 0.2753 0.2804 0.1994 -0.0267 0.0015  0.0060  207 MET A CA  
1698 C C   . MET A 207 ? 0.2534 0.2629 0.1854 -0.0239 -0.0041 0.0050  207 MET A C   
1699 O O   . MET A 207 ? 0.2286 0.2384 0.1669 -0.0221 -0.0058 0.0072  207 MET A O   
1700 C CB  . MET A 207 ? 0.3065 0.3095 0.2400 -0.0268 0.0070  0.0029  207 MET A CB  
1701 C CG  . MET A 207 ? 0.3541 0.3528 0.2802 -0.0295 0.0143  0.0038  207 MET A CG  
1702 S SD  . MET A 207 ? 0.4648 0.4627 0.3803 -0.0322 0.0171  -0.0015 207 MET A SD  
1703 C CE  . MET A 207 ? 0.4529 0.4536 0.3553 -0.0331 0.0095  -0.0006 207 MET A CE  
1704 N N   . ALA A 208 ? 0.2347 0.2473 0.1667 -0.0238 -0.0063 0.0015  208 ALA A N   
1705 C CA  . ALA A 208 ? 0.2288 0.2465 0.1658 -0.0216 -0.0107 0.0005  208 ALA A CA  
1706 C C   . ALA A 208 ? 0.2241 0.2429 0.1716 -0.0194 -0.0108 -0.0016 208 ALA A C   
1707 O O   . ALA A 208 ? 0.2263 0.2480 0.1776 -0.0174 -0.0133 -0.0019 208 ALA A O   
1708 C CB  . ALA A 208 ? 0.2271 0.2475 0.1629 -0.0223 -0.0118 -0.0018 208 ALA A CB  
1709 N N   . TRP A 209 ? 0.2233 0.2400 0.1765 -0.0199 -0.0080 -0.0036 209 TRP A N   
1710 C CA  . TRP A 209 ? 0.2159 0.2341 0.1793 -0.0184 -0.0090 -0.0067 209 TRP A CA  
1711 C C   . TRP A 209 ? 0.2147 0.2301 0.1837 -0.0175 -0.0083 -0.0054 209 TRP A C   
1712 O O   . TRP A 209 ? 0.2018 0.2192 0.1778 -0.0159 -0.0104 -0.0087 209 TRP A O   
1713 C CB  . TRP A 209 ? 0.2315 0.2491 0.2021 -0.0193 -0.0072 -0.0088 209 TRP A CB  
1714 C CG  . TRP A 209 ? 0.2413 0.2536 0.2132 -0.0210 -0.0015 -0.0069 209 TRP A CG  
1715 C CD1 . TRP A 209 ? 0.2605 0.2691 0.2393 -0.0215 0.0021  -0.0056 209 TRP A CD1 
1716 C CD2 . TRP A 209 ? 0.2726 0.2830 0.2394 -0.0227 0.0022  -0.0065 209 TRP A CD2 
1717 N NE1 . TRP A 209 ? 0.2591 0.2640 0.2355 -0.0234 0.0083  -0.0039 209 TRP A NE1 
1718 C CE2 . TRP A 209 ? 0.2842 0.2901 0.2530 -0.0241 0.0085  -0.0051 209 TRP A CE2 
1719 C CE3 . TRP A 209 ? 0.3230 0.3349 0.2843 -0.0232 0.0012  -0.0074 209 TRP A CE3 
1720 C CZ2 . TRP A 209 ? 0.3296 0.3326 0.2940 -0.0260 0.0143  -0.0057 209 TRP A CZ2 
1721 C CZ3 . TRP A 209 ? 0.3641 0.3726 0.3223 -0.0251 0.0063  -0.0081 209 TRP A CZ3 
1722 C CH2 . TRP A 209 ? 0.3525 0.3567 0.3116 -0.0265 0.0130  -0.0078 209 TRP A CH2 
1723 N N   . THR A 210 ? 0.2063 0.2172 0.1718 -0.0187 -0.0053 -0.0005 210 THR A N   
1724 C CA  . THR A 210 ? 0.2207 0.2283 0.1924 -0.0179 -0.0045 0.0029  210 THR A CA  
1725 C C   . THR A 210 ? 0.2220 0.2324 0.1940 -0.0158 -0.0084 0.0037  210 THR A C   
1726 O O   . THR A 210 ? 0.2395 0.2495 0.2223 -0.0139 -0.0092 0.0022  210 THR A O   
1727 C CB  . THR A 210 ? 0.2293 0.2326 0.1944 -0.0199 -0.0006 0.0095  210 THR A CB  
1728 O OG1 . THR A 210 ? 0.2346 0.2359 0.1995 -0.0219 0.0043  0.0080  210 THR A OG1 
1729 C CG2 . THR A 210 ? 0.2446 0.2444 0.2176 -0.0193 0.0005  0.0152  210 THR A CG2 
1730 N N   . ILE A 211 ? 0.2205 0.2338 0.1823 -0.0161 -0.0107 0.0057  211 ILE A N   
1731 C CA  . ILE A 211 ? 0.2209 0.2377 0.1849 -0.0141 -0.0142 0.0066  211 ILE A CA  
1732 C C   . ILE A 211 ? 0.2151 0.2361 0.1860 -0.0120 -0.0151 -0.0003 211 ILE A C   
1733 O O   . ILE A 211 ? 0.2101 0.2322 0.1899 -0.0096 -0.0157 -0.0018 211 ILE A O   
1734 C CB  . ILE A 211 ? 0.2283 0.2479 0.1813 -0.0154 -0.0168 0.0096  211 ILE A CB  
1735 C CG1 . ILE A 211 ? 0.2429 0.2591 0.1874 -0.0177 -0.0166 0.0162  211 ILE A CG1 
1736 C CG2 . ILE A 211 ? 0.2398 0.2646 0.1979 -0.0131 -0.0201 0.0097  211 ILE A CG2 
1737 C CD1 . ILE A 211 ? 0.2496 0.2636 0.2009 -0.0164 -0.0172 0.0225  211 ILE A CD1 
1738 N N   . VAL A 212 ? 0.2137 0.2372 0.1808 -0.0128 -0.0151 -0.0045 212 VAL A N   
1739 C CA  . VAL A 212 ? 0.2094 0.2376 0.1803 -0.0114 -0.0161 -0.0108 212 VAL A CA  
1740 C C   . VAL A 212 ? 0.2229 0.2488 0.2051 -0.0103 -0.0153 -0.0151 212 VAL A C   
1741 O O   . VAL A 212 ? 0.2253 0.2538 0.2126 -0.0084 -0.0156 -0.0195 212 VAL A O   
1742 C CB  . VAL A 212 ? 0.2156 0.2467 0.1818 -0.0129 -0.0168 -0.0128 212 VAL A CB  
1743 C CG1 . VAL A 212 ? 0.2098 0.2458 0.1786 -0.0121 -0.0184 -0.0188 212 VAL A CG1 
1744 C CG2 . VAL A 212 ? 0.2149 0.2489 0.1728 -0.0137 -0.0177 -0.0096 212 VAL A CG2 
1745 N N   . ASN A 213 ? 0.2325 0.2534 0.2200 -0.0116 -0.0137 -0.0144 213 ASN A N   
1746 C CA  . ASN A 213 ? 0.2515 0.2696 0.2520 -0.0110 -0.0130 -0.0187 213 ASN A CA  
1747 C C   . ASN A 213 ? 0.2442 0.2595 0.2536 -0.0089 -0.0122 -0.0170 213 ASN A C   
1748 O O   . ASN A 213 ? 0.2580 0.2735 0.2778 -0.0075 -0.0122 -0.0235 213 ASN A O   
1749 C CB  . ASN A 213 ? 0.2560 0.2691 0.2626 -0.0129 -0.0107 -0.0166 213 ASN A CB  
1750 C CG  . ASN A 213 ? 0.2759 0.2916 0.2787 -0.0147 -0.0114 -0.0186 213 ASN A CG  
1751 O OD1 . ASN A 213 ? 0.2900 0.3112 0.2887 -0.0145 -0.0145 -0.0230 213 ASN A OD1 
1752 N ND2 . ASN A 213 ? 0.2761 0.2879 0.2811 -0.0164 -0.0080 -0.0148 213 ASN A ND2 
1753 N N   . GLU A 214 ? 0.2394 0.2520 0.2461 -0.0089 -0.0115 -0.0083 214 GLU A N   
1754 C CA  . GLU A 214 ? 0.2428 0.2532 0.2595 -0.0068 -0.0115 -0.0044 214 GLU A CA  
1755 C C   . GLU A 214 ? 0.2387 0.2541 0.2583 -0.0042 -0.0127 -0.0094 214 GLU A C   
1756 O O   . GLU A 214 ? 0.2254 0.2394 0.2593 -0.0019 -0.0118 -0.0124 214 GLU A O   
1757 C CB  . GLU A 214 ? 0.2618 0.2701 0.2720 -0.0077 -0.0119 0.0068  214 GLU A CB  
1758 C CG  . GLU A 214 ? 0.2607 0.2637 0.2688 -0.0102 -0.0091 0.0124  214 GLU A CG  
1759 C CD  . GLU A 214 ? 0.2919 0.2893 0.3167 -0.0098 -0.0067 0.0152  214 GLU A CD  
1760 O OE1 . GLU A 214 ? 0.2977 0.2912 0.3227 -0.0119 -0.0034 0.0189  214 GLU A OE1 
1761 O OE2 . GLU A 214 ? 0.3003 0.2969 0.3390 -0.0073 -0.0077 0.0140  214 GLU A OE2 
1762 N N   . VAL A 215 ? 0.2280 0.2493 0.2358 -0.0044 -0.0142 -0.0100 215 VAL A N   
1763 C CA  . VAL A 215 ? 0.2288 0.2558 0.2389 -0.0021 -0.0143 -0.0139 215 VAL A CA  
1764 C C   . VAL A 215 ? 0.2365 0.2657 0.2509 -0.0013 -0.0127 -0.0252 215 VAL A C   
1765 O O   . VAL A 215 ? 0.2290 0.2592 0.2540 0.0011  -0.0109 -0.0303 215 VAL A O   
1766 C CB  . VAL A 215 ? 0.2309 0.2636 0.2278 -0.0031 -0.0159 -0.0113 215 VAL A CB  
1767 C CG1 . VAL A 215 ? 0.2389 0.2785 0.2379 -0.0011 -0.0149 -0.0159 215 VAL A CG1 
1768 C CG2 . VAL A 215 ? 0.2313 0.2627 0.2236 -0.0042 -0.0182 -0.0018 215 VAL A CG2 
1769 N N   . ILE A 216 ? 0.2335 0.2640 0.2401 -0.0034 -0.0135 -0.0293 216 ILE A N   
1770 C CA  . ILE A 216 ? 0.2592 0.2936 0.2660 -0.0033 -0.0133 -0.0399 216 ILE A CA  
1771 C C   . ILE A 216 ? 0.2692 0.2985 0.2914 -0.0025 -0.0120 -0.0463 216 ILE A C   
1772 O O   . ILE A 216 ? 0.2795 0.3111 0.3070 -0.0011 -0.0104 -0.0551 216 ILE A O   
1773 C CB  . ILE A 216 ? 0.2656 0.3028 0.2617 -0.0059 -0.0158 -0.0410 216 ILE A CB  
1774 C CG1 . ILE A 216 ? 0.2557 0.2989 0.2389 -0.0063 -0.0166 -0.0367 216 ILE A CG1 
1775 C CG2 . ILE A 216 ? 0.2747 0.3146 0.2725 -0.0067 -0.0171 -0.0513 216 ILE A CG2 
1776 C CD1 . ILE A 216 ? 0.2511 0.2971 0.2261 -0.0086 -0.0192 -0.0358 216 ILE A CD1 
1777 N N   . VAL A 217 ? 0.2726 0.2950 0.3029 -0.0036 -0.0121 -0.0419 217 VAL A N   
1778 C CA  . VAL A 217 ? 0.2728 0.2897 0.3202 -0.0034 -0.0110 -0.0474 217 VAL A CA  
1779 C C   . VAL A 217 ? 0.2931 0.3073 0.3549 -0.0003 -0.0085 -0.0471 217 VAL A C   
1780 O O   . VAL A 217 ? 0.3052 0.3178 0.3799 0.0006  -0.0069 -0.0569 217 VAL A O   
1781 C CB  . VAL A 217 ? 0.2842 0.2948 0.3384 -0.0055 -0.0109 -0.0418 217 VAL A CB  
1782 C CG1 . VAL A 217 ? 0.3042 0.3082 0.3797 -0.0051 -0.0092 -0.0454 217 VAL A CG1 
1783 C CG2 . VAL A 217 ? 0.2842 0.2975 0.3305 -0.0084 -0.0131 -0.0445 217 VAL A CG2 
1784 N N   . SER A 218 ? 0.3065 0.3200 0.3673 0.0011  -0.0083 -0.0362 218 SER A N   
1785 C CA  . SER A 218 ? 0.3287 0.3403 0.4049 0.0043  -0.0067 -0.0336 218 SER A CA  
1786 C C   . SER A 218 ? 0.3119 0.3291 0.3905 0.0067  -0.0045 -0.0437 218 SER A C   
1787 O O   . SER A 218 ? 0.3080 0.3228 0.4051 0.0092  -0.0017 -0.0489 218 SER A O   
1788 C CB  . SER A 218 ? 0.3440 0.3553 0.4168 0.0047  -0.0085 -0.0193 218 SER A CB  
1789 O OG  . SER A 218 ? 0.4286 0.4470 0.4881 0.0050  -0.0098 -0.0182 218 SER A OG  
1790 N N   . TYR A 219 ? 0.2872 0.3120 0.3483 0.0059  -0.0052 -0.0461 219 TYR A N   
1791 C CA  . TYR A 219 ? 0.2860 0.3175 0.3456 0.0076  -0.0022 -0.0551 219 TYR A CA  
1792 C C   . TYR A 219 ? 0.2914 0.3228 0.3541 0.0070  -0.0003 -0.0700 219 TYR A C   
1793 O O   . TYR A 219 ? 0.2880 0.3204 0.3612 0.0092  0.0038  -0.0793 219 TYR A O   
1794 C CB  . TYR A 219 ? 0.2791 0.3184 0.3189 0.0063  -0.0035 -0.0522 219 TYR A CB  
1795 C CG  . TYR A 219 ? 0.2765 0.3240 0.3130 0.0079  0.0004  -0.0590 219 TYR A CG  
1796 C CD1 . TYR A 219 ? 0.2818 0.3308 0.3322 0.0112  0.0040  -0.0585 219 TYR A CD1 
1797 C CD2 . TYR A 219 ? 0.2727 0.3271 0.2925 0.0060  0.0006  -0.0646 219 TYR A CD2 
1798 C CE1 . TYR A 219 ? 0.2841 0.3412 0.3321 0.0127  0.0087  -0.0642 219 TYR A CE1 
1799 C CE2 . TYR A 219 ? 0.2830 0.3456 0.2983 0.0072  0.0050  -0.0696 219 TYR A CE2 
1800 C CZ  . TYR A 219 ? 0.2907 0.3546 0.3199 0.0105  0.0095  -0.0695 219 TYR A CZ  
1801 O OH  . TYR A 219 ? 0.2913 0.3635 0.3170 0.0116  0.0152  -0.0749 219 TYR A OH  
1802 N N   . GLU A 220 ? 0.2894 0.3198 0.3436 0.0039  -0.0034 -0.0725 220 GLU A N   
1803 C CA  . GLU A 220 ? 0.3155 0.3464 0.3714 0.0024  -0.0035 -0.0866 220 GLU A CA  
1804 C C   . GLU A 220 ? 0.3397 0.3643 0.4185 0.0044  0.0000  -0.0943 220 GLU A C   
1805 O O   . GLU A 220 ? 0.3834 0.4100 0.4656 0.0048  0.0027  -0.1083 220 GLU A O   
1806 C CB  . GLU A 220 ? 0.3042 0.3322 0.3575 -0.0010 -0.0079 -0.0854 220 GLU A CB  
1807 C CG  . GLU A 220 ? 0.2922 0.3271 0.3251 -0.0035 -0.0116 -0.0835 220 GLU A CG  
1808 C CD  . GLU A 220 ? 0.2838 0.3163 0.3174 -0.0066 -0.0158 -0.0818 220 GLU A CD  
1809 O OE1 . GLU A 220 ? 0.2548 0.2923 0.2747 -0.0083 -0.0190 -0.0782 220 GLU A OE1 
1810 O OE2 . GLU A 220 ? 0.2803 0.3057 0.3302 -0.0071 -0.0156 -0.0834 220 GLU A OE2 
1811 N N   . TRP A 221 ? 0.3622 0.3789 0.4574 0.0054  0.0000  -0.0853 221 TRP A N   
1812 C CA  . TRP A 221 ? 0.4288 0.4382 0.5487 0.0067  0.0026  -0.0917 221 TRP A CA  
1813 C C   . TRP A 221 ? 0.4355 0.4456 0.5691 0.0109  0.0076  -0.0950 221 TRP A C   
1814 O O   . TRP A 221 ? 0.4459 0.4505 0.6015 0.0124  0.0109  -0.1034 221 TRP A O   
1815 C CB  . TRP A 221 ? 0.4670 0.4680 0.5993 0.0059  0.0009  -0.0795 221 TRP A CB  
1816 C CG  . TRP A 221 ? 0.5341 0.5352 0.6551 0.0019  -0.0028 -0.0785 221 TRP A CG  
1817 C CD1 . TRP A 221 ? 0.5755 0.5824 0.6810 -0.0009 -0.0056 -0.0873 221 TRP A CD1 
1818 C CD2 . TRP A 221 ? 0.5415 0.5368 0.6671 0.0001  -0.0039 -0.0666 221 TRP A CD2 
1819 N NE1 . TRP A 221 ? 0.5208 0.5259 0.6234 -0.0039 -0.0085 -0.0821 221 TRP A NE1 
1820 C CE2 . TRP A 221 ? 0.6244 0.6223 0.7389 -0.0034 -0.0069 -0.0698 221 TRP A CE2 
1821 C CE3 . TRP A 221 ? 0.5818 0.5707 0.7197 0.0012  -0.0025 -0.0532 221 TRP A CE3 
1822 C CZ2 . TRP A 221 ? 0.6940 0.6879 0.8109 -0.0056 -0.0073 -0.0607 221 TRP A CZ2 
1823 C CZ3 . TRP A 221 ? 0.6209 0.6060 0.7582 -0.0014 -0.0030 -0.0439 221 TRP A CZ3 
1824 C CH2 . TRP A 221 ? 0.6986 0.6861 0.8260 -0.0046 -0.0048 -0.0482 221 TRP A CH2 
1825 N N   . GLU A 222 ? 0.4076 0.4247 0.5293 0.0125  0.0086  -0.0898 222 GLU A N   
1826 C CA  . GLU A 222 ? 0.4355 0.4552 0.5694 0.0164  0.0138  -0.0937 222 GLU A CA  
1827 C C   . GLU A 222 ? 0.4405 0.4687 0.5603 0.0161  0.0177  -0.1080 222 GLU A C   
1828 O O   . GLU A 222 ? 0.4334 0.4621 0.5661 0.0185  0.0237  -0.1196 222 GLU A O   
1829 C CB  . GLU A 222 ? 0.4332 0.4556 0.5671 0.0185  0.0125  -0.0780 222 GLU A CB  
1830 C CG  . GLU A 222 ? 0.4543 0.4689 0.6034 0.0192  0.0093  -0.0639 222 GLU A CG  
1831 C CD  . GLU A 222 ? 0.4965 0.5035 0.6763 0.0220  0.0126  -0.0676 222 GLU A CD  
1832 O OE1 . GLU A 222 ? 0.4601 0.4691 0.6543 0.0252  0.0177  -0.0761 222 GLU A OE1 
1833 O OE2 . GLU A 222 ? 0.5864 0.5854 0.7770 0.0208  0.0104  -0.0613 222 GLU A OE2 
1834 N N   . VAL A 223 ? 0.4143 0.4495 0.5083 0.0133  0.0149  -0.1065 223 VAL A N   
1835 C CA  . VAL A 223 ? 0.4406 0.4856 0.5198 0.0134  0.0189  -0.1151 223 VAL A CA  
1836 C C   . VAL A 223 ? 0.4584 0.5054 0.5293 0.0109  0.0197  -0.1324 223 VAL A C   
1837 O O   . VAL A 223 ? 0.4999 0.5536 0.5633 0.0113  0.0251  -0.1436 223 VAL A O   
1838 C CB  . VAL A 223 ? 0.4221 0.4744 0.4791 0.0118  0.0158  -0.1041 223 VAL A CB  
1839 C CG1 . VAL A 223 ? 0.3841 0.4367 0.4232 0.0077  0.0095  -0.1029 223 VAL A CG1 
1840 C CG2 . VAL A 223 ? 0.4477 0.5102 0.4944 0.0128  0.0215  -0.1092 223 VAL A CG2 
1841 N N   . ILE A 224 ? 0.4949 0.5368 0.5656 0.0079  0.0142  -0.1342 224 ILE A N   
1842 C CA  . ILE A 224 ? 0.5376 0.5812 0.6012 0.0048  0.0128  -0.1500 224 ILE A CA  
1843 C C   . ILE A 224 ? 0.6033 0.6392 0.6923 0.0063  0.0170  -0.1630 224 ILE A C   
1844 O O   . ILE A 224 ? 0.5784 0.6050 0.6870 0.0063  0.0148  -0.1593 224 ILE A O   
1845 C CB  . ILE A 224 ? 0.5200 0.5624 0.5744 0.0008  0.0043  -0.1451 224 ILE A CB  
1846 C CG1 . ILE A 224 ? 0.4760 0.5247 0.5095 -0.0004 0.0006  -0.1314 224 ILE A CG1 
1847 C CG2 . ILE A 224 ? 0.5490 0.5940 0.5972 -0.0029 0.0014  -0.1615 224 ILE A CG2 
1848 C CD1 . ILE A 224 ? 0.4937 0.5409 0.5219 -0.0038 -0.0069 -0.1258 224 ILE A CD1 
1849 N N   . LYS A 225 ? 0.7472 0.7871 0.8366 0.0075  0.0238  -0.1783 225 LYS A N   
1850 C CA  . LYS A 225 ? 0.8127 0.8452 0.9293 0.0099  0.0296  -0.1907 225 LYS A CA  
1851 C C   . LYS A 225 ? 0.8100 0.8352 0.9375 0.0066  0.0252  -0.2010 225 LYS A C   
1852 O O   . LYS A 225 ? 0.8676 0.8831 1.0242 0.0083  0.0276  -0.2043 225 LYS A O   
1853 C CB  . LYS A 225 ? 0.9433 0.9825 1.0559 0.0114  0.0387  -0.2070 225 LYS A CB  
1854 C CG  . LYS A 225 ? 1.0221 1.0614 1.1521 0.0169  0.0471  -0.2018 225 LYS A CG  
1855 C CD  . LYS A 225 ? 1.0486 1.0921 1.1704 0.0185  0.0446  -0.1805 225 LYS A CD  
1856 C CE  . LYS A 225 ? 1.0932 1.1417 1.2251 0.0230  0.0531  -0.1786 225 LYS A CE  
1857 N NZ  . LYS A 225 ? 1.1419 1.1819 1.3102 0.0276  0.0569  -0.1772 225 LYS A NZ  
1858 N N   . LYS A 226 ? 0.7748 0.8048 0.8815 0.0017  0.0182  -0.2050 226 LYS A N   
1859 C CA  . LYS A 226 ? 0.7740 0.7981 0.8914 -0.0020 0.0129  -0.2144 226 LYS A CA  
1860 C C   . LYS A 226 ? 0.7503 0.7653 0.8850 -0.0020 0.0085  -0.1983 226 LYS A C   
1861 O O   . LYS A 226 ? 0.6936 0.7030 0.8416 -0.0050 0.0045  -0.2040 226 LYS A O   
1862 C CB  . LYS A 226 ? 0.7816 0.8148 0.8723 -0.0072 0.0061  -0.2231 226 LYS A CB  
1863 C CG  . LYS A 226 ? 0.7681 0.8067 0.8387 -0.0091 -0.0014 -0.2062 226 LYS A CG  
1864 C CD  . LYS A 226 ? 0.7778 0.8255 0.8258 -0.0141 -0.0090 -0.2140 226 LYS A CD  
1865 C CE  . LYS A 226 ? 0.7632 0.8146 0.7983 -0.0159 -0.0167 -0.1973 226 LYS A CE  
1866 N NZ  . LYS A 226 ? 0.7536 0.8121 0.7748 -0.0211 -0.0259 -0.2049 226 LYS A NZ  
1867 N N   . PHE A 227 ? 0.6944 0.7086 0.8285 0.0009  0.0091  -0.1788 227 PHE A N   
1868 C CA  . PHE A 227 ? 0.6526 0.6580 0.8044 0.0015  0.0071  -0.1632 227 PHE A CA  
1869 C C   . PHE A 227 ? 0.6684 0.6663 0.8469 0.0061  0.0131  -0.1588 227 PHE A C   
1870 O O   . PHE A 227 ? 0.7634 0.7636 0.9469 0.0088  0.0190  -0.1697 227 PHE A O   
1871 C CB  . PHE A 227 ? 0.6041 0.6133 0.7371 0.0010  0.0031  -0.1447 227 PHE A CB  
1872 C CG  . PHE A 227 ? 0.5648 0.5791 0.6786 -0.0034 -0.0036 -0.1449 227 PHE A CG  
1873 C CD1 . PHE A 227 ? 0.5954 0.6117 0.7075 -0.0071 -0.0072 -0.1601 227 PHE A CD1 
1874 C CD2 . PHE A 227 ? 0.5298 0.5470 0.6285 -0.0040 -0.0067 -0.1296 227 PHE A CD2 
1875 C CE1 . PHE A 227 ? 0.5627 0.5844 0.6597 -0.0109 -0.0142 -0.1587 227 PHE A CE1 
1876 C CE2 . PHE A 227 ? 0.5129 0.5346 0.5973 -0.0076 -0.0127 -0.1289 227 PHE A CE2 
1877 C CZ  . PHE A 227 ? 0.5332 0.5574 0.6172 -0.0110 -0.0166 -0.1428 227 PHE A CZ  
# 
