[English] 日本語
Yorodumi
- PDB-6anq: STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WIT... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6anq
TitleSTRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WITH A DOUBLE STRANDED DNA AND AN INCOMING D4TTP AT PH 8.5
Components
  • (HIV-1 REVERSE TRANSCRIPTASE ...) x 2
  • DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')
  • DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')
Keywordstransferase/dna / TERNARY N SITE COMPLEX / D4T (STAVUDINE) / DNA TEMPLATE/PRIMER / CROSSLINK / VIRAL PROTEIN / viral protein-dna complex / transferase-dna complex
Function / homology
Function and homology information


HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency ...HIV-1 retropepsin / symbiont-mediated activation of host apoptosis / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / viral genome integration into host DNA / RNA-directed DNA polymerase / establishment of integrated proviral latency / symbiont-mediated suppression of host gene expression / viral penetration into host nucleus / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / host cell / viral nucleocapsid / DNA recombination / DNA-directed DNA polymerase / Hydrolases; Acting on ester bonds / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / viral translational frameshifting / lipid binding / host cell nucleus / host cell plasma membrane / structural molecule activity / virion membrane / proteolysis / DNA binding / zinc ion binding / membrane
Similarity search - Function
HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. ...HIV Type 1 Reverse Transcriptase, subunit A, domain 1 / HIV Type 1 Reverse Transcriptase; Chain A, domain 1 / Reverse transcriptase/Diguanylate cyclase domain / Ribonuclease H-like superfamily/Ribonuclease H / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / Immunodeficiency lentiviral matrix, N-terminal / gag gene protein p17 (matrix protein) / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Retropepsin-like catalytic domain / RNase H type-1 domain profile. / Ribonuclease H domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Reverse transcriptase (RNA-dependent DNA polymerase) / Retroviral matrix protein / Retrovirus capsid, C-terminal / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Nucleotidyltransferase; domain 5 / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Ribonuclease H superfamily / Aspartic peptidase domain superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / Alpha-Beta Plaits / Roll / DNA/RNA polymerase superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-D4T / DNA / DNA (> 10) / Gag-Pol polyprotein
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 BH10
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.586 Å
AuthorsMartinez, S.E. / Das, K. / Arnold, E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R37 A1027690 United States
CitationJournal: Protein Sci. / Year: 2019
Title: Structure of HIV-1 reverse transcriptase/d4TTP complex: Novel DNA cross-linking site and pH-dependent conformational changes.
Authors: Martinez, S.E. / Bauman, J.D. / Das, K. / Arnold, E.
History
DepositionAug 14, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 15, 2018Provider: repository / Type: Initial release
Revision 1.1Dec 19, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Feb 20, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.3Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_conn_type
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
B: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
T: DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')
P: DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')
C: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
E: DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')
F: DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)263,61826
Polymers261,4878
Non-polymers2,13118
Water11,638646
1
A: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
B: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
T: DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')
P: DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,90114
Polymers130,7444
Non-polymers1,15710
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15630 Å2
ΔGint-59 kcal/mol
Surface area47650 Å2
MethodPISA
2
C: HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT
D: HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT
E: DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')
F: DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,71712
Polymers130,7444
Non-polymers9738
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14890 Å2
ΔGint-66 kcal/mol
Surface area48210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)89.853, 132.723, 139.471
Angle α, β, γ (deg.)90.000, 98.060, 90.000
Int Tables number4
Space group name H-MP1211

-
Components

-
HIV-1 REVERSE TRANSCRIPTASE ... , 2 types, 4 molecules ACBD

#1: Protein HIV-1 REVERSE TRANSCRIPTASE P66 SUBUNIT / Pr160Gag-Pol


Mass: 64038.367 Da / Num. of mol.: 2 / Mutation: C280S, I63C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Strain: isolate BH10 / Gene: gag-pol / Plasmid: pCDF-2 Ek/LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): BL21 CodonPlus RIL
References: UniProt: P03366, RNA-directed DNA polymerase, DNA-directed DNA polymerase
#2: Protein HIV-1 REVERSE TRANSCRIPTASE P51 SUBUNIT / Pr160Gag-Pol


Mass: 51928.629 Da / Num. of mol.: 2 / Mutation: C879S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Strain: isolate BH10 / Gene: gag-pol / Plasmid: pCDF-2 Ek/LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): BL21 CodonPlus RIL
References: UniProt: P03366, RNA-directed DNA polymerase, DNA-directed DNA polymerase

-
DNA chain , 2 types, 4 molecules TEPF

#3: DNA chain DNA TEMPLATE (5'- D(*AP*TP*GP*AP*AP*CP*GP*GP*CP*GP*CP*CP*CP*GP*AP*AP*CP*AP*GP*GP*GP*AP*CP*TP*GP*TP*G)-3')


Mass: 8376.399 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: COMMERCIAL DNA OLIGO SYNTHESIS: INTEGRATED DNA TECHNOLOGIES
Source: (synth.) Human immunodeficiency virus type 1 BH10
#4: DNA chain DNA PRIMER (5'- D(*AP*CP*AP*GP*TP*CP*CP*CP*TP*GP*TP*TP*CP*GP*GP*GP*CP*GP*CP*CP*GP)-3')


Mass: 6400.123 Da / Num. of mol.: 2 / Source method: obtained synthetically
Details: COMMERCIAL DNA OLIGO SYNTHESIS: MIDLAND CERTIFIED REAGENT COMPANY
Source: (synth.) Homo sapiens (human)

-
Non-polymers , 4 types, 664 molecules

#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#6: Chemical ChemComp-D4T / 2',3'-DEHYDRO-2',3'-DEOXY-THYMIDINE 5'-TRIPHOSPHATE


Mass: 464.153 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N2O13P3
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 646 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.15 Å3/Da / Density % sol: 60.94 % / Description: PARALLELOGRAMS
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 9.5
Details: PEG 8000, NaCl, CHES (N-Cyclohexyl-2-aminoethanesulfonic acid), TRIS, MgCl2, d4T triphosphate
PH range: 9.5 - 10.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.9177 Å
DetectorType: ADSC QUANTUM 270 / Detector: CCD / Date: Jul 10, 2010
Details: White beam collimating mirror, horizontally focusing monochromator using single bent triangular Si(111) crystal, vertically focusing Rh-coated Si mirror
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9177 Å / Relative weight: 1
ReflectionResolution: 2.586→50 Å / Num. obs: 100112 / % possible obs: 99.5 % / Redundancy: 6.5 % / Biso Wilson estimate: 55.81 Å2 / Rmerge(I) obs: 0.091 / Χ2: 1.043 / Net I/σ(I): 18.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsΧ2% possible all
2.6-2.694.90.7361.797640.95597.3
2.69-2.85.50.6252.499970.95499.7
2.8-2.935.80.4843.299621.00699.6
2.93-3.0860.3584.6100211.08199.9
3.08-3.286.40.2417.7100091.16799.9
3.28-3.536.90.15113.6100411.218100
3.53-3.887.30.09720.9100461.121100
3.88-4.457.30.06427.4100850.956100
4.45-5.67.40.05335.2100941.023100
5.6-507.30.04832.9100930.91898.6

-
Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.76 Å43.44 Å
Translation8.76 Å43.44 Å

-
Processing

Software
NameVersionClassification
HKL-2000data reduction
HKL-2000data scaling
PHASER2.5.6phasing
PHENIX1.11.1 2575refinement
PDB_EXTRACT3.22data extraction
Coot0.8.8model building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDBID 6AMO
Resolution: 2.586→43.445 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.39 / Phase error: 24.73
RfactorNum. reflection% reflection
Rfree0.2189 1781 1.78 %
Rwork0.1796 --
obs0.1803 100068 98.9 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 279.55 Å2 / Biso mean: 89.785 Å2 / Biso min: 22.38 Å2
Refinement stepCycle: final / Resolution: 2.586→43.445 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15778 1716 132 646 18272
Biso mean--91.7 64.12 -
Num. residues----2008
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00618270
X-RAY DIFFRACTIONf_angle_d0.44125129
X-RAY DIFFRACTIONf_chiral_restr0.042722
X-RAY DIFFRACTIONf_plane_restr0.0032859
X-RAY DIFFRACTIONf_dihedral_angle_d13.2810627
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 13

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5855-2.65540.3861210.31726758687989
2.6554-2.73350.34361350.287775467681100
2.7335-2.82180.3061380.26276127750100
2.8218-2.92260.30021380.244876007738100
2.9226-3.03960.31131410.229276057746100
3.0396-3.17790.26631370.21775927729100
3.1779-3.34540.26861370.20976577794100
3.3454-3.55490.23791390.18176107749100
3.5549-3.82920.19911360.162676527788100
3.8292-4.21430.17741400.148876577797100
4.2143-4.82340.15721400.135976537793100
4.8234-6.07430.19151380.15877047842100
6.0743-43.45090.18991410.16087641778298
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.919-0.0141-0.05490.06850.00390.00650.1946-0.52391.0532-0.60.14260.4428-0.4968-0.0889-0.26591.4355-0.17330.03850.75660.06391.031433.424422.432818.3023
20.0893-0.04960.01210.0253-0.00560.00210.00550.80680.3988-0.85890.13010.8221-0.5645-0.1272-0.2531.843-0.2841-0.20731.34070.24590.96529.584819.669827.074
31.45010.0808-0.59670.8584-0.37661.76230.15160.24220.719-0.54370.23270.1455-0.88910.1421-0.21581.188-0.23210.02670.55060.05860.851135.673223.303143.5846
43.48451.0585-1.16011.0528-0.32111.6595-0.0567-0.03420.2512-0.04690.13480.1777-0.1954-0.1279-0.00650.32910.0499-0.06430.3421-0.10360.444711.436-0.235171.0803
51.28880.3723-0.50513.4337-0.06682.5402-0.21450.3272-0.2247-0.81750.3254-0.28970.02080.5223-0.14430.6276-0.17440.09270.7089-0.22090.569240.6158-12.825439.9284
60.9942-1.2988-0.60142.43221.13141.9426-0.109-0.459-0.2601-0.1020.3061-0.69130.27050.8304-0.17490.5290.1429-0.05320.8722-0.14580.909639.7753-30.240655.7614
70.8965-0.5708-1.20090.97550.11262.2976-0.42760.0468-0.44460.06240.07440.22840.6761-0.14150.26250.4752-0.06860.05220.3713-0.11990.622812.0358-26.990966.5184
82.3182-0.30050.80633.37941.65642.4016-0.2069-0.1392-0.1879-0.205-0.02040.24780.0373-0.04030.15670.307-0.0659-0.00790.4032-0.13430.480126.6234-14.646257.2944
90.25280.06410.18241.6793-0.94671.20970.0440.2237-0.0425-0.6790.04130.36990.0647-0.653-0.06631.55020.1257-0.00351.0818-0.09850.633422.5758-63.1405-14.1456
100.61990.6947-0.2150.8037-0.35340.5658-0.71261.0545-0.0686-0.82050.77310.8178-0.1413-0.5828-0.14072.32430.0484-0.33551.50940.01551.138215.286-56.5135-22.7082
111.5612-0.3727-1.03531.7102-1.02752.57340.22880.9074-0.0362-0.58610.13870.44780.2619-0.7946-0.26161.35970.1376-0.04460.99970.0510.597919.636-48.8484-3.4764
122.32860.38661.26561.70350.62280.791-0.04550.7708-0.1095-0.58230.11340.20231.1388-1.1437-0.17522.0123-0.1128-0.08411.6776-0.07040.551318.5797-59.3332-18.7693
131.6568-0.586-0.50051.5548-0.44563.02740.47040.70090.4988-0.8612-0.09830.049-0.5826-0.4643-0.33371.2990.17540.08530.71660.09980.576622.6101-38.39010.8064
143.35931.1834-0.33932.7555-0.1934.11560.3080.04480.3953-0.7202-0.1210.8966-0.4713-1.2158-0.24550.80390.0846-0.05890.70650.05180.86595.2315-42.206519.6129
152.1193-0.1406-1.48952.512-0.92423.38210.10570.02070.2864-0.3902-0.0075-0.0986-0.3080.0221-0.07570.4856-0.0398-0.00810.2844-0.12740.443220.2763-44.699631.815
161.51520.5839-0.26172.0663-0.99061.1558-0.1-0.3687-0.1773-0.21150.21730.19570.0855-0.2837-0.12450.2502-0.0736-0.07190.632-0.00360.45965.0458-67.59151.817
172.08030.50240.05732.8426-0.39882.6813-0.0729-0.188-0.2083-0.08680.09260.17310.1018-0.2517-0.00940.2385-0.0254-0.04520.48170.00230.43857.6019-66.358150.0145
182.51850.10230.13962.74360.51912.50240.09590.0421-0.1492-0.6257-0.1157-0.45220.51670.991-0.10781.03080.1810.20510.7914-0.00910.629341.4361-61.16312.2778
190.7651-0.051-0.31751.9289-0.150.93950.1614-0.0196-0.0769-0.6245-0.3701-0.71110.33381.30420.05711.00190.34590.38351.37710.15130.860353.4743-67.30419.5564
200.97080.0356-0.28030.8678-0.55630.4227-0.12420.0159-0.0388-0.2697-0.071-0.30930.21250.65780.04720.40150.00090.01130.92960.04140.640536.789-71.150150.1094
211.5001-0.5016-0.13761.5622-1.41733.76440.0288-0.0537-0.3744-0.3617-0.2756-0.2190.51370.45290.17010.37150.029-0.02870.5066-0.0510.44632.98-74.326448.0562
222.4045-0.33490.52235.1627-0.14564.0360.1178-0.1389-0.0563-0.2135-0.3540.15580.20350.33730.23790.55540.03920.05180.642-0.08070.473732.6916-64.178132.9751
233.38293.4873-0.71513.79610.0848.6640.44130.90951.07590.3231-0.09131.9844-0.6593-0.4177-0.14141.6986-0.0961-0.18151.08730.31721.350225.714619.34734.1689
245.04571.38621.12562.1444-0.77691.5242-0.77270.5839-0.065-1.0240.56010.91440.5669-0.59360.17531.1172-0.2219-0.03130.8939-0.0271.01469.80251.612950.0839
251.38660.10091.33510.03140.10751.2983-0.35930.09020.0262-0.3592-0.35020.2556-0.3809-0.99980.53611.8085-0.64180.07672.2486-0.39582.4653-12.2347-15.83651.7422
263.21350.3220.12041.61411.65832.87070.67120.7159-1.114-0.7120.5134-0.01561.7497-0.2255-0.87971.9915-0.4027-0.48481.8372-0.25841.0808-4.8556-14.211247.1363
272.0572.225-0.54292.4089-0.58830.1433-0.8120.71710.488-1.75290.63640.3039-0.0422-0.37440.20171.2557-0.2935-0.02951.04630.20051.033914.94359.446747.9558
281.75940.5436-1.57161.99730.31794.43380.48530.7426-0.1656-1.12450.08730.48170.8726-0.9658-0.44981.4834-0.039-0.1771.06450.08340.817313.2987-54.67196.9156
295.46450.5139-0.16517.2814-1.26716.23510.64950.2064-1.4126-1.3778-0.12190.10641.41741.132-0.44611.3659-0.11620.18221.05330.04271.501912.6736-74.468828.1397
304.17442.9681.69042.70890.30072.7363-0.4130.3875-0.7152-0.0037-0.33050.20151.09750.12830.52242.176-0.50490.1991.80090.31752.87117.7467-90.763639.5801
312.6364-0.05411.62120.4393-0.5641.737-0.46560.0023-1.11310.21680.3389-0.70670.83180.9856-0.1531.9758-0.1180.46651.3069-0.41461.862212.8838-87.766932.8991
320.8669-1.27930.34443.2079-2.23932.39770.16270.5921-0.0231-2.0527-0.150.32811.3371-0.3646-0.15021.4323-0.1809-0.11750.957-0.00170.737311.4521-61.062917.3328
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 49 )A-1 - 49
2X-RAY DIFFRACTION2chain 'A' and (resid 50 through 96 )A50 - 96
3X-RAY DIFFRACTION3chain 'A' and (resid 97 through 325 )A97 - 325
4X-RAY DIFFRACTION4chain 'A' and (resid 326 through 553 )A326 - 553
5X-RAY DIFFRACTION5chain 'B' and (resid 4 through 174 )B4 - 174
6X-RAY DIFFRACTION6chain 'B' and (resid 175 through 253 )B175 - 253
7X-RAY DIFFRACTION7chain 'B' and (resid 254 through 363 )B254 - 363
8X-RAY DIFFRACTION8chain 'B' and (resid 364 through 428 )B364 - 428
9X-RAY DIFFRACTION9chain 'C' and (resid -1 through 27 )C-1 - 27
10X-RAY DIFFRACTION10chain 'C' and (resid 28 through 59 )C28 - 59
11X-RAY DIFFRACTION11chain 'C' and (resid 60 through 114 )C60 - 114
12X-RAY DIFFRACTION12chain 'C' and (resid 115 through 153 )C115 - 153
13X-RAY DIFFRACTION13chain 'C' and (resid 154 through 269 )C154 - 269
14X-RAY DIFFRACTION14chain 'C' and (resid 270 through 325 )C270 - 325
15X-RAY DIFFRACTION15chain 'C' and (resid 326 through 421 )C326 - 421
16X-RAY DIFFRACTION16chain 'C' and (resid 422 through 473 )C422 - 473
17X-RAY DIFFRACTION17chain 'C' and (resid 474 through 553 )C474 - 553
18X-RAY DIFFRACTION18chain 'D' and (resid 4 through 88 )D4 - 88
19X-RAY DIFFRACTION19chain 'D' and (resid 89 through 210 )D89 - 210
20X-RAY DIFFRACTION20chain 'D' and (resid 211 through 269 )D211 - 269
21X-RAY DIFFRACTION21chain 'D' and (resid 270 through 382 )D270 - 382
22X-RAY DIFFRACTION22chain 'D' and (resid 383 through 428 )D383 - 428
23X-RAY DIFFRACTION23chain 'T' and (resid 704 through 708 )T704 - 708
24X-RAY DIFFRACTION24chain 'T' and (resid 709 through 723 )T709 - 723
25X-RAY DIFFRACTION25chain 'T' and (resid 724 through 725 )T724 - 725
26X-RAY DIFFRACTION26chain 'P' and (resid 803 through 807 )P803 - 807
27X-RAY DIFFRACTION27chain 'P' and (resid 808 through 821 )P808 - 821
28X-RAY DIFFRACTION28chain 'E' and (resid 704 through 713 )E704 - 713
29X-RAY DIFFRACTION29chain 'E' and (resid 714 through 723 )E714 - 723
30X-RAY DIFFRACTION30chain 'E' and (resid 724 through 725 )E724 - 725
31X-RAY DIFFRACTION31chain 'F' and (resid 803 through 807 )F803 - 807
32X-RAY DIFFRACTION32chain 'F' and (resid 808 through 821 )F808 - 821

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more