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- PDB-3h4e: X-ray Structure of Hexameric HIV-1 CA -

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Basic information

Entry
Database: PDB / ID: 3h4e
TitleX-ray Structure of Hexameric HIV-1 CA
ComponentsCapsid protein p24
KeywordsVIRAL PROTEIN / capsid protein / hexamer / engineered disulfide bonds
Function / homology
Function and homology information


HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA ...HIV-1 retropepsin / : / retroviral ribonuclease H / exoribonuclease H / : / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral genome integration into host DNA / viral penetration into host nucleus / establishment of integrated proviral latency / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / RNA-DNA hybrid ribonuclease activity / viral nucleocapsid / DNA recombination / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / symbiont entry into host cell / symbiont-mediated suppression of host gene expression / lipid binding / host cell nucleus / structural molecule activity / host cell plasma membrane / virion membrane / proteolysis / DNA binding / RNA binding / zinc ion binding / membrane
Similarity search - Function
Retrovirus capsid C-terminal domain / Human Immunodeficiency Virus Type 1 Capsid Protein / Human Immunodeficiency Virus Type 1 Capsid Protein / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / Reverse transcriptase connection / Reverse transcriptase connection domain / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. ...Retrovirus capsid C-terminal domain / Human Immunodeficiency Virus Type 1 Capsid Protein / Human Immunodeficiency Virus Type 1 Capsid Protein / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / 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. / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Retropepsin-like catalytic domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Ribonuclease H domain / RNase H type-1 domain profile. / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Retrovirus capsid, C-terminal / Retroviral matrix protein / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Ribonuclease H superfamily / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHuman immunodeficiency virus type 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.704 Å
AuthorsPornillos, O.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2009
Title: X-ray structures of the hexameric building block of the HIV capsid.
Authors: Pornillos, O. / Ganser-Pornillos, B.K. / Kelly, B.N. / Hua, Y. / Whitby, F.G. / Stout, C.D. / Sundquist, W.I. / Hill, C.P. / Yeager, M.
History
DepositionApr 19, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 23, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 13, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.3Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Capsid protein p24
B: Capsid protein p24
C: Capsid protein p24
D: Capsid protein p24
E: Capsid protein p24
F: Capsid protein p24
G: Capsid protein p24
H: Capsid protein p24
I: Capsid protein p24
J: Capsid protein p24
K: Capsid protein p24
L: Capsid protein p24


Theoretical massNumber of molelcules
Total (without water)305,53512
Polymers305,53512
Non-polymers00
Water0
1
A: Capsid protein p24
B: Capsid protein p24
C: Capsid protein p24
D: Capsid protein p24
E: Capsid protein p24
F: Capsid protein p24


Theoretical massNumber of molelcules
Total (without water)152,7686
Polymers152,7686
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14950 Å2
ΔGint-104 kcal/mol
Surface area58380 Å2
MethodPISA
2
G: Capsid protein p24
H: Capsid protein p24
I: Capsid protein p24
J: Capsid protein p24
K: Capsid protein p24
L: Capsid protein p24


Theoretical massNumber of molelcules
Total (without water)152,7686
Polymers152,7686
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14540 Å2
ΔGint-106 kcal/mol
Surface area58140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)136.062, 136.657, 208.454
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11E
21B
31C
41D
51A
61F
71G
81H
91I
101J
111K
121L
12A
22B
32C
42D
52E
62F
72G
82H
92I
102J
112K
122L
13E
23A
33B
43C
53D
63F
73G
83H
93I
103J
113K
123L
14E
24F
34G
44H
54I
64J
74K
84L
94A
104B
114C
124D
15E
25A
35B
45C
55D
65F
75G
85H
95I
105J
115K
125L
16C
26A
36B
46D
56E
66F
76G
86H
96I
106J
116K
126L
17C
27J
18B
28I
19D
29K
110L
210A
310E
410F
510G
610H

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain E resseq 1:3 or resseq 11-12 or (resseq 13...E0
211chain B resseq 1:3 or resseq 11-12 or (resseq 13...B0
311chain C resseq 1:3 or resseq 11-12 or (resseq 13...C0
411chain D resseq 1:3 or resseq 11-12 or (resseq 13...D0
511chain A resseq 1:3 or resseq 11-12 or (resseq 13...A0
611chain F resseq 1:3 or resseq 11-12 or (resseq 13...F0
711chain G resseq 1:3 or resseq 11-12 or (resseq 13...G0
811chain H resseq 1:3 or resseq 11-12 or (resseq 13...H0
911chain I resseq 1:3 or resseq 11-12 or (resseq 13...I0
1011chain J resseq 1:3 or resseq 11-12 or (resseq 13...J0
1111chain K resseq 1:3 or resseq 11-12 or (resseq 13...K0
1211chain L resseq 1:3 or resseq 11-12 or (resseq 13...L0
112chain A resseq 116:125A0
212chain B resseq 116:125B0
312chain C resseq 116:125C0
412chain D resseq 116:125D0
512chain E resseq 116:125E0
612chain F resseq 116:125F0
712chain G resseq 116:125G0
812chain H resseq 116:125H0
912chain I resseq 116:125I0
1012chain J resseq 116:125J0
1112chain K resseq 116:125K0
1212chain L resseq 116:125L0
113chain E resseq 149:153 or (resseq 154 and backbone) or...E0
213chain A resseq 149:153 or (resseq 154 and backbone) or...A0
313chain B resseq 149:153 or (resseq 154 and backbone) or...B0
413chain C resseq 149:153 or (resseq 154 and backbone) or...C0
513chain D resseq 149:153 or (resseq 154 and backbone) or...D0
613chain F resseq 149:153 or (resseq 154 and backbone) or...F0
713chain G resseq 149:153 or (resseq 154 and backbone) or...G0
813chain H resseq 149:153 or (resseq 154 and backbone) or...H0
913chain I resseq 149:153 or (resseq 154 and backbone) or...I0
1013chain J resseq 149:153 or (resseq 154 and backbone) or...J0
1113chain K resseq 149:153 or (resseq 154 and backbone) or...K0
1213chain L resseq 149:153 or (resseq 154 and backbone) or...L0
114chain E resseq 190:191 or (resseq 192 and backbone) or...E0
214chain F resseq 190:191 or (resseq 192 and backbone) or...F0
314chain G resseq 190:191 or (resseq 192 and backbone) or...G0
414chain H resseq 190:191 or (resseq 192 and backbone) or...H0
514chain I resseq 190:191 or (resseq 192 and backbone) or...I0
614chain J resseq 190:191 or (resseq 192 and backbone) or...J0
714chain K resseq 190:191 or (resseq 192 and backbone) or...K0
814chain L resseq 190:191 or (resseq 192 and backbone) or...L0
914chain A resseq 190:191 or (resseq 192 and backbone) or...A0
1014chain B resseq 190:191 or (resseq 192 and backbone) or...B0
1114chain C resseq 190:191 or (resseq 192 and backbone) or...C0
1214chain D resseq 190:191 or (resseq 192 and backbone) or...D0
115chain E resseq 206:218 or (resseq 219 and backbone)E0
215chain A resseq 206:218 or (resseq 219 and backbone)A0
315chain B resseq 206:218 or (resseq 219 and backbone)B0
415chain C resseq 206:218 or (resseq 219 and backbone)C0
515chain D resseq 206:218 or (resseq 219 and backbone)D0
615chain F resseq 206:218 or (resseq 219 and backbone)F0
715chain G resseq 206:218 or (resseq 219 and backbone)G0
815chain H resseq 206:218 or (resseq 219 and backbone)H0
915chain I resseq 206:218 or (resseq 219 and backbone)I0
1015chain J resseq 206:218 or (resseq 219 and backbone)J0
1115chain K resseq 206:218 or (resseq 219 and backbone)K0
1215chain L resseq 206:218 or (resseq 219 and backbone)L0
116chain C (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)C0
216chain A (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)A0
316chain B (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)B0
416chain D (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)D0
516chain E (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)E0
616chain F (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)F0
716chain G (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)G0
816chain H (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)H0
916chain I (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)I0
1016chain J (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)J0
1116chain K (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)K0
1216chain L (resseq 4 and backbone) or resseq 5 or (resseq 6:10 and backbone)L0
117chain C resseq 175:189C0
217chain J resseq 175:189J0
118chain B resseq 175:189B0
218chain I resseq 175:189I0
119chain D resseq 175:189D0
219chain K resseq 175:189K0
1110chain L resseq 175:181 or (resseq 182 and backbone) or resseq 183:189L0
2110chain A resseq 175:181 or (resseq 182 and backbone) or resseq 183:189A0
3110chain E resseq 175:181 or (resseq 182 and backbone) or resseq 183:189E0
4110chain F resseq 175:181 or (resseq 182 and backbone) or resseq 183:189F0
5110chain G resseq 175:181 or (resseq 182 and backbone) or resseq 183:189G0
6110chain H resseq 175:181 or (resseq 182 and backbone) or resseq 183:189H0

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10

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Components

#1: Protein
Capsid protein p24 / / CA


Mass: 25461.271 Da / Num. of mol.: 12 / Fragment: UNP residues 133-363 / Mutation: A14C,E45C,W184A,M185A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)
Strain: NL4-3 / Gene: CA, gag-pol / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P12497

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.17 Å3/Da / Density % sol: 61.22 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 10-12% PEG 8,000, 100 mM Tris, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL7-1 / Wavelength: 0.9773 Å
DetectorDate: Jun 27, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9773 Å / Relative weight: 1
ReflectionResolution: 2.7→50 Å / Num. obs: 102201

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Processing

Software
NameVersionClassification
MOLREPphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3H47
Resolution: 2.704→34.742 Å / SU ML: 0.39 / σ(F): 1.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2632 2565 2.51 %Thin shell
Rwork0.2385 ---
obs0.2391 102181 95.87 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 35.268 Å2 / ksol: 0.301 e/Å3
Refinement stepCycle: LAST / Resolution: 2.704→34.742 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19082 0 0 0 19082
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11E825X-RAY DIFFRACTIONPOSITIONAL
12B825X-RAY DIFFRACTIONPOSITIONAL0.11
13C837X-RAY DIFFRACTIONPOSITIONAL0.101
14D837X-RAY DIFFRACTIONPOSITIONAL0.117
15A837X-RAY DIFFRACTIONPOSITIONAL0.12
16F837X-RAY DIFFRACTIONPOSITIONAL0.109
17G837X-RAY DIFFRACTIONPOSITIONAL0.104
18H837X-RAY DIFFRACTIONPOSITIONAL0.094
19I837X-RAY DIFFRACTIONPOSITIONAL0.112
110J837X-RAY DIFFRACTIONPOSITIONAL0.11
111K837X-RAY DIFFRACTIONPOSITIONAL0.111
112L837X-RAY DIFFRACTIONPOSITIONAL0.095
21A77X-RAY DIFFRACTIONPOSITIONAL
22B77X-RAY DIFFRACTIONPOSITIONAL0.099
23C77X-RAY DIFFRACTIONPOSITIONAL0.077
24D77X-RAY DIFFRACTIONPOSITIONAL0.094
25E77X-RAY DIFFRACTIONPOSITIONAL0.103
26F77X-RAY DIFFRACTIONPOSITIONAL0.072
27G77X-RAY DIFFRACTIONPOSITIONAL0.092
28H77X-RAY DIFFRACTIONPOSITIONAL0.072
29I77X-RAY DIFFRACTIONPOSITIONAL0.081
210J77X-RAY DIFFRACTIONPOSITIONAL0.086
211K77X-RAY DIFFRACTIONPOSITIONAL0.091
212L77X-RAY DIFFRACTIONPOSITIONAL0.083
31E208X-RAY DIFFRACTIONPOSITIONAL
32A208X-RAY DIFFRACTIONPOSITIONAL0.077
33B208X-RAY DIFFRACTIONPOSITIONAL0.112
34C208X-RAY DIFFRACTIONPOSITIONAL0.09
35D205X-RAY DIFFRACTIONPOSITIONAL0.094
36F208X-RAY DIFFRACTIONPOSITIONAL0.071
37G208X-RAY DIFFRACTIONPOSITIONAL0.086
38H208X-RAY DIFFRACTIONPOSITIONAL0.089
39I208X-RAY DIFFRACTIONPOSITIONAL0.112
310J208X-RAY DIFFRACTIONPOSITIONAL0.098
311K208X-RAY DIFFRACTIONPOSITIONAL0.101
312L208X-RAY DIFFRACTIONPOSITIONAL0.068
41E96X-RAY DIFFRACTIONPOSITIONAL
42F96X-RAY DIFFRACTIONPOSITIONAL0.075
43G94X-RAY DIFFRACTIONPOSITIONAL0.078
44H95X-RAY DIFFRACTIONPOSITIONAL0.08
45I98X-RAY DIFFRACTIONPOSITIONAL0.085
46J96X-RAY DIFFRACTIONPOSITIONAL0.099
47K90X-RAY DIFFRACTIONPOSITIONAL0.102
48L98X-RAY DIFFRACTIONPOSITIONAL0.073
49A95X-RAY DIFFRACTIONPOSITIONAL0.084
410B98X-RAY DIFFRACTIONPOSITIONAL0.081
411C96X-RAY DIFFRACTIONPOSITIONAL0.104
412D87X-RAY DIFFRACTIONPOSITIONAL0.078
51E89X-RAY DIFFRACTIONPOSITIONAL
52A89X-RAY DIFFRACTIONPOSITIONAL0.064
53B91X-RAY DIFFRACTIONPOSITIONAL0.075
54C91X-RAY DIFFRACTIONPOSITIONAL0.067
55D91X-RAY DIFFRACTIONPOSITIONAL0.069
56F91X-RAY DIFFRACTIONPOSITIONAL0.061
57G91X-RAY DIFFRACTIONPOSITIONAL0.068
58H91X-RAY DIFFRACTIONPOSITIONAL0.068
59I91X-RAY DIFFRACTIONPOSITIONAL0.084
510J87X-RAY DIFFRACTIONPOSITIONAL0.068
511K91X-RAY DIFFRACTIONPOSITIONAL0.074
512L91X-RAY DIFFRACTIONPOSITIONAL0.06
61C32X-RAY DIFFRACTIONPOSITIONAL
62A32X-RAY DIFFRACTIONPOSITIONAL0.098
63B32X-RAY DIFFRACTIONPOSITIONAL0.127
64D32X-RAY DIFFRACTIONPOSITIONAL0.146
65E32X-RAY DIFFRACTIONPOSITIONAL0.072
66F32X-RAY DIFFRACTIONPOSITIONAL0.149
67G32X-RAY DIFFRACTIONPOSITIONAL0.07
68H32X-RAY DIFFRACTIONPOSITIONAL0.1
69I32X-RAY DIFFRACTIONPOSITIONAL0.09
610J32X-RAY DIFFRACTIONPOSITIONAL0.132
611K32X-RAY DIFFRACTIONPOSITIONAL0.068
612L32X-RAY DIFFRACTIONPOSITIONAL0.104
71C102X-RAY DIFFRACTIONPOSITIONAL
72J102X-RAY DIFFRACTIONPOSITIONAL0.08
81B42X-RAY DIFFRACTIONPOSITIONAL
82I42X-RAY DIFFRACTIONPOSITIONAL0.071
91D28X-RAY DIFFRACTIONPOSITIONAL
92K28X-RAY DIFFRACTIONPOSITIONAL0.071
101L87X-RAY DIFFRACTIONPOSITIONAL
102A87X-RAY DIFFRACTIONPOSITIONAL0.076
103E96X-RAY DIFFRACTIONPOSITIONAL0.067
104F96X-RAY DIFFRACTIONPOSITIONAL0.074
105G87X-RAY DIFFRACTIONPOSITIONAL0.078
106H28X-RAY DIFFRACTIONPOSITIONAL0.086
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.704-2.75610.33421710.3134871X-RAY DIFFRACTION86
2.7561-2.81240.32171710.28465485X-RAY DIFFRACTION97
2.8124-2.873500.28015726X-RAY DIFFRACTION98
2.8735-2.94030.3191710.27595519X-RAY DIFFRACTION98
2.9403-3.01380.32111710.26825584X-RAY DIFFRACTION98
3.0138-3.09520.30131710.26775534X-RAY DIFFRACTION97
3.0952-3.18620.31881710.26895566X-RAY DIFFRACTION98
3.1862-3.2890.32811710.27255516X-RAY DIFFRACTION97
3.289-3.406500.26535725X-RAY DIFFRACTION97
3.4065-3.54270.27491710.25245538X-RAY DIFFRACTION97
3.5427-3.70380.28721710.23725564X-RAY DIFFRACTION97
3.7038-3.89880.2721710.23135554X-RAY DIFFRACTION97
3.8988-4.14270.23511710.2165538X-RAY DIFFRACTION96
4.1427-4.4620.21031710.19685522X-RAY DIFFRACTION96
4.462-4.909900.18025719X-RAY DIFFRACTION96
4.9099-5.61780.22311710.20865530X-RAY DIFFRACTION95
5.6178-7.0680.26911710.22985543X-RAY DIFFRACTION95
7.068-34.74520.15981710.18375582X-RAY DIFFRACTION92

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