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- PDB-4u0b: Hexamer HIV-1 CA in complex with CPSF6 peptide, P212121 crystal form -

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Basic information

Entry
Database: PDB / ID: 4u0b
TitleHexamer HIV-1 CA in complex with CPSF6 peptide, P212121 crystal form
Components
  • Capsid protein p24
  • Cleavage and polyadenylation specificity factor subunit 6
KeywordsVIRAL PROTEIN / Capsid / Complex
Function / homology
Function and homology information


exon-exon junction complex binding / : / positive regulation of RNA export from nucleus / mRNA cleavage factor complex / interchromatin granule / Processing of Intronless Pre-mRNAs / perichromatin fibrils / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / paraspeckles ...exon-exon junction complex binding / : / positive regulation of RNA export from nucleus / mRNA cleavage factor complex / interchromatin granule / Processing of Intronless Pre-mRNAs / perichromatin fibrils / mRNA cleavage and polyadenylation specificity factor complex / mRNA alternative polyadenylation / paraspeckles / mRNA 3'-end processing / mRNA 3'-end processing / Signaling by cytosolic FGFR1 fusion mutants / protein heterotetramerization / RNA Polymerase II Transcription Termination / viral budding via host ESCRT complex / ribosomal large subunit binding / Processing of Capped Intron-Containing Pre-mRNA / localization / Signaling by FGFR1 in disease / protein tetramerization / ISG15 antiviral mechanism / mRNA processing / host multivesicular body / viral nucleocapsid / nuclear speck / ribonucleoprotein complex / mRNA binding / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / cytoplasm
Similarity search - Function
Cleavage and polyadenylation specificity factor subunit 6 / CPSF6/7 family / Retrovirus capsid C-terminal domain / Human Immunodeficiency Virus Type 1 Capsid Protein / Human Immunodeficiency Virus Type 1 Capsid Protein / Gag protein p6 / Gag protein p6 / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / gag protein p24 N-terminal domain / RNA recognition motif ...Cleavage and polyadenylation specificity factor subunit 6 / CPSF6/7 family / Retrovirus capsid C-terminal domain / Human Immunodeficiency Virus Type 1 Capsid Protein / Human Immunodeficiency Virus Type 1 Capsid Protein / Gag protein p6 / Gag protein p6 / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / gag protein p24 N-terminal domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Immunodeficiency lentiviral matrix, N-terminal / gag gene protein p17 (matrix protein) / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / 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. / Nucleotide-binding alpha-beta plait domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Gag polyprotein / Cleavage and polyadenylation specificity factor subunit 6
Similarity search - Component
Biological speciesHuman immunodeficiency virus type 1 group M subtype B
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsPrice, A.J. / Jacques, D.A. / James, L.C.
CitationJournal: Plos Pathog. / Year: 2014
Title: Host Cofactors and Pharmacologic Ligands Share an Essential Interface in HIV-1 Capsid That Is Lost upon Disassembly.
Authors: Price, A.J. / Jacques, D.A. / McEwan, W.A. / Fletcher, A.J. / Essig, S. / Chin, J.W. / Halambage, U.D. / Aiken, C. / James, L.C.
History
DepositionJul 11, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Nov 12, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 20, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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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
M: Cleavage and polyadenylation specificity factor subunit 6
N: Cleavage and polyadenylation specificity factor subunit 6
O: Cleavage and polyadenylation specificity factor subunit 6
P: Cleavage and polyadenylation specificity factor subunit 6
Q: Cleavage and polyadenylation specificity factor subunit 6
R: Cleavage and polyadenylation specificity factor subunit 6
S: Cleavage and polyadenylation specificity factor subunit 6
T: Cleavage and polyadenylation specificity factor subunit 6
U: Cleavage and polyadenylation specificity factor subunit 6
V: Cleavage and polyadenylation specificity factor subunit 6
W: Cleavage and polyadenylation specificity factor subunit 6
X: Cleavage and polyadenylation specificity factor subunit 6


Theoretical massNumber of molelcules
Total (without water)324,14524
Polymers324,14524
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
M: Cleavage and polyadenylation specificity factor subunit 6
N: Cleavage and polyadenylation specificity factor subunit 6
O: Cleavage and polyadenylation specificity factor subunit 6
P: Cleavage and polyadenylation specificity factor subunit 6
Q: Cleavage and polyadenylation specificity factor subunit 6
R: Cleavage and polyadenylation specificity factor subunit 6


Theoretical massNumber of molelcules
Total (without water)162,07212
Polymers162,07212
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22440 Å2
ΔGint-176 kcal/mol
Surface area58870 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
S: Cleavage and polyadenylation specificity factor subunit 6
T: Cleavage and polyadenylation specificity factor subunit 6
U: Cleavage and polyadenylation specificity factor subunit 6
V: Cleavage and polyadenylation specificity factor subunit 6
W: Cleavage and polyadenylation specificity factor subunit 6
X: Cleavage and polyadenylation specificity factor subunit 6


Theoretical massNumber of molelcules
Total (without water)162,07212
Polymers162,07212
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22360 Å2
ΔGint-176 kcal/mol
Surface area59220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)135.130, 135.890, 208.190
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L
12A
22B
32C
42D
52E
62F
72G
82H
92I
102J
112K
122L

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 145
2114B1 - 145
3114C1 - 145
4114D1 - 145
5114E1 - 145
6114F1 - 145
7114G1 - 145
8114H1 - 145
9114I1 - 145
10114J1 - 145
11114K1 - 145
12114L1 - 145
1124A146 - 999
2124B146 - 999
3124C146 - 999
4124D146 - 999
5124E146 - 999
6124F146 - 999
7124G146 - 999
8124H146 - 999
9124I146 - 999
10124J146 - 999
11124K146 - 999
12124L146 - 999

NCS ensembles :
ID
1
2

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Components

#1: Protein
Capsid protein p24 / / Pr55Gag


Mass: 25461.271 Da / Num. of mol.: 12 / Mutation: yes
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 group M subtype B
Strain: isolate NY5 / Gene: gag / Plasmid: pET11a / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P12493
#2: Protein/peptide
Cleavage and polyadenylation specificity factor subunit 6 / / Cleavage and polyadenylation specificity factor 68 kDa subunit / CPSF 68 kDa subunit / Pre-mRNA ...Cleavage and polyadenylation specificity factor 68 kDa subunit / CPSF 68 kDa subunit / Pre-mRNA cleavage factor Im 68 kDa subunit / Protein HPBRII-4/7


Mass: 1550.796 Da / Num. of mol.: 12 / Fragment: UNP residues 276-290 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q16630

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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: 2.95 Å3/Da / Density % sol: 58.28 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 20% v/v PEG 300, 10% v/v glycerol, 5% w/v PEG 8K, 0.1 M TRIS

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9686 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 6, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9686 Å / Relative weight: 1
ReflectionResolution: 2.8→48.6 Å / Num. obs: 89373 / % possible obs: 95.1 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 11.7
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.588 / % possible all: 97.6

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
PDB_EXTRACT3.14data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4U0A
Resolution: 2.8→48.6 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.91 / SU B: 36.856 / SU ML: 0.315 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.33 / ESU R Free: 0.369 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2619 4479 5 %RANDOM
Rwork0.2295 84854 --
obs0.2311 89333 94.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 229.13 Å2 / Biso mean: 85.338 Å2 / Biso min: 37.05 Å2
Baniso -1Baniso -2Baniso -3
1--0.17 Å20 Å2-0 Å2
2--0.39 Å2-0 Å2
3----0.21 Å2
Refinement stepCycle: final / Resolution: 2.8→48.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19931 0 0 0 19931
Num. residues----2596
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.01920452
X-RAY DIFFRACTIONr_bond_other_d0.0010.0219496
X-RAY DIFFRACTIONr_angle_refined_deg0.7391.96427838
X-RAY DIFFRACTIONr_angle_other_deg0.673.00144943
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.92752569
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.12624.847848
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.242153355
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.77915110
X-RAY DIFFRACTIONr_chiral_restr0.040.23130
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.02122972
X-RAY DIFFRACTIONr_gen_planes_other0.0010.024372
X-RAY DIFFRACTIONr_mcbond_it3.2027.25410357
X-RAY DIFFRACTIONr_mcbond_other3.2017.25410356
X-RAY DIFFRACTIONr_mcangle_it5.17212.22512872
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1995MEDIUM POSITIONAL0.160.5
12B1995MEDIUM POSITIONAL0.150.5
13C1995MEDIUM POSITIONAL0.130.5
14D1995MEDIUM POSITIONAL0.110.5
15E1995MEDIUM POSITIONAL0.110.5
16F1995MEDIUM POSITIONAL0.110.5
17G1995MEDIUM POSITIONAL0.210.5
18H1995MEDIUM POSITIONAL0.180.5
19I1995MEDIUM POSITIONAL0.10.5
1101995MEDIUM POSITIONAL0.110.5
111A1995MEDIUM POSITIONAL0.10.5
112B1995MEDIUM POSITIONAL0.130.5
11A1995MEDIUM THERMAL7.32
12B1995MEDIUM THERMAL7.442
13C1995MEDIUM THERMAL6.972
14D1995MEDIUM THERMAL5.842
15E1995MEDIUM THERMAL6.282
16F1995MEDIUM THERMAL5.152
17G1995MEDIUM THERMAL6.862
18H1995MEDIUM THERMAL7.182
19I1995MEDIUM THERMAL5.742
1101995MEDIUM THERMAL5.822
111A1995MEDIUM THERMAL9.212
112B1995MEDIUM THERMAL5.252
21A976MEDIUM POSITIONAL0.230.5
22B976MEDIUM POSITIONAL0.160.5
23C976MEDIUM POSITIONAL0.140.5
24D976MEDIUM POSITIONAL0.130.5
25E976MEDIUM POSITIONAL0.130.5
26F976MEDIUM POSITIONAL0.250.5
27G976MEDIUM POSITIONAL0.180.5
28H976MEDIUM POSITIONAL0.20.5
29I976MEDIUM POSITIONAL0.130.5
210976MEDIUM POSITIONAL0.210.5
211A976MEDIUM POSITIONAL0.180.5
212B976MEDIUM POSITIONAL0.260.5
21A976MEDIUM THERMAL13.372
22B976MEDIUM THERMAL11.692
23C976MEDIUM THERMAL8.022
24D976MEDIUM THERMAL7.872
25E976MEDIUM THERMAL7.142
26F976MEDIUM THERMAL12.782
27G976MEDIUM THERMAL8.72
28H976MEDIUM THERMAL10.562
29I976MEDIUM THERMAL6.932
210976MEDIUM THERMAL15.32
211A976MEDIUM THERMAL8.832
212B976MEDIUM THERMAL12.662
LS refinement shellResolution: 2.8→2.873 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.381 369 -
Rwork0.331 6359 -
all-6728 -
obs--97.07 %
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)
12.34460.78650.05122.91610.98511.2424-0.28980.11150.3486-0.23970.01860.43190.1106-0.00940.27130.11590.0004-0.01440.1081-0.00740.1846-17.435847.0768-5.2531
21.3959-0.1094-0.5052.3314-0.20193.061-0.275-0.0179-0.34160.1241-0.00210.58710.5529-0.14540.27710.1991-0.0020.22860.0543-0.00350.4122-30.90530.60529.6332
31.1391-0.03881.0930.5027-0.26913.8461-0.3521-0.388-0.38870.1750.13190.14950.1916-0.24650.22020.3370.2430.33290.22130.23220.341-27.082429.15536.2981
40.67890.6229-0.7961.2482-0.92351.8562-0.2434-0.5387-0.19650.1607-0.14220.02380.22820.62050.38560.32880.41710.17580.63730.26290.197-10.186545.327147.7056
53.25671.4957-2.38970.9773-0.83453.81630.0979-0.46960.31260.2340.05940.1708-0.23751.0426-0.15730.18190.0890.01710.49620.02210.07074.575562.128232.566
61.2176-0.6333-0.02030.7941.53775.3716-0.11820.02240.1989-0.23680.0537-0.0951-0.99160.05460.06450.231-0.0047-0.0540.1497-0.00770.12320.539464.19085.9816
71.9646-0.05710.63290.68760.05882.3727-0.0414-0.0141-0.4286-0.0209-0.1630.30050.1563-0.45640.20440.04180.009-0.0080.2249-0.23880.3923-71.384670.283642.9009
80.8523-0.1109-0.26431.5714-1.17143.12130.17440.3053-0.0129-0.454-0.28860.3250.4333-0.13640.11420.23250.2192-0.17160.3463-0.2650.2976-72.787173.611516.0921
91.39990.34690.45931.9879-0.10491.80060.05250.4752-0.097-0.4918-0.27010.1262-0.3209-0.06650.21760.35220.2787-0.10490.3841-0.06510.1185-56.806989.94274.3329
101.09111.28461.05542.05112.02624.5980.01560.3644-0.1503-0.25350.2066-0.2006-1.29330.3245-0.22220.5040.0109-0.00930.241-0.03750.0821-40.4334106.252919.4308
110.3694-0.5255-0.57061.13020.26185.95440.1144-0.02630.0352-0.0584-0.1633-0.0484-0.31430.84190.04880.0958-0.04960.01920.17440.00720.0227-38.2415102.328745.7227
123.36480.6411-1.28122.48010.14341.3488-0.0171-0.3207-0.48190.0816-0.2892-0.1611-0.043-0.10890.30630.02790.00840.00120.134-0.01870.1441-54.731784.21157.5394
137.7402-5.7892-2.42215.1491.38620.97910.09270.13580.8188-0.1677-0.116-1.1590.0114-0.03780.02330.307-0.1193-0.10530.10130.11230.5931-5.398566.8271-6.974
147.28240.2246-4.62071.2909-1.99235.59850.02550.37250.4018-0.3378-0.3511-0.36610.47440.30640.32560.20880.06450.00230.20290.07720.3332-29.598940.45-9.7373
151.1038-1.1093-1.59691.16361.5272.4387-0.03150.0834-0.0311-0.0501-0.01330.04040.2075-0.20170.04480.2189-0.07170.07710.19880.06160.2626-40.204423.890318.0164
1610.6818-5.1694-1.81192.54541.13921.8869-0.2048-0.2185-0.83250.16250.09750.39870.39890.00180.10730.29750.02420.13140.22480.16930.2223-27.67332.101551.069
172.76390.6842-0.63610.1856-0.15660.14710.2597-0.92230.14470.117-0.22630.078-0.04530.2207-0.03340.39660.02610.10250.5295-0.01950.1432-2.179156.196753.6181
189.6507-7.24033.255.4319-2.43841.201-0.4968-0.78570.00140.37050.5896-0-0.273-0.0829-0.09280.4585-0.1707-0.01330.3767-0.14940.11619.011873.763424.9523
193.15014.38134.15086.15035.83245.53240.4636-0.4016-0.13750.4575-0.3369-0.19780.4064-0.3771-0.12660.5452-0.08570.0580.65270.07430.2913-60.900971.869662.4532
204.3485-0.3125-0.80977.58684.24712.4764-0.4585-0.3810.36930.53730.32640.45310.38090.23150.13220.3493-0.1357-0.0650.3682-0.02080.3729-77.310760.514934.2406
212.0026-2.4076-0.83143.6874-0.31922.55210.60170.4193-0.9643-0.9668-0.42171.51870.1637-0.3859-0.180.34140.0167-0.34610.4395-0.26710.671-69.849773.12541.4049
223.4385-3.8443-0.65754.33580.75070.13360.5080.5019-0.178-0.6815-0.52510.161-0.1523-0.09840.01710.48460.05110.07020.3208-0.03090.0781-46.526599.1712-1.4468
237.562-5.5703-0.13474.10860.11110.03010.65150.78140.361-0.5538-0.5688-0.28-0.12740.0575-0.08270.5461-0.25950.19670.45430.04710.1723-28.5926110.820527.0704
246.9596-5.9399-3.97115.14353.38222.30970.3233-0.34831.2973-0.15460.1818-1.1887-0.13920.1813-0.50510.1162-0.1635-0.02560.51730.00440.9343-35.258196.604759.2038
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 220
2X-RAY DIFFRACTION2B1 - 220
3X-RAY DIFFRACTION3C1 - 220
4X-RAY DIFFRACTION4D1 - 220
5X-RAY DIFFRACTION5E1 - 220
6X-RAY DIFFRACTION6F1 - 220
7X-RAY DIFFRACTION7G1 - 220
8X-RAY DIFFRACTION8H1 - 220
9X-RAY DIFFRACTION9I1 - 220
10X-RAY DIFFRACTION10J1 - 220
11X-RAY DIFFRACTION11K1 - 220
12X-RAY DIFFRACTION12L1 - 220
13X-RAY DIFFRACTION13M313 - 326
14X-RAY DIFFRACTION14N313 - 325
15X-RAY DIFFRACTION15O313 - 326
16X-RAY DIFFRACTION16P313 - 326
17X-RAY DIFFRACTION17Q313 - 326
18X-RAY DIFFRACTION18R313 - 326
19X-RAY DIFFRACTION19S313 - 326
20X-RAY DIFFRACTION20T313 - 326
21X-RAY DIFFRACTION21U313 - 326
22X-RAY DIFFRACTION22V313 - 326
23X-RAY DIFFRACTION23W313 - 326
24X-RAY DIFFRACTION24X313 - 326

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

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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

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