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- PDB-4ac9: CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METH... -

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Basic information

Entry
Database: PDB / ID: 4ac9
TitleCRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS IN COMPLEX WITH GDP
ComponentsMJ0495-LIKE PROTEIN
KeywordsTRANSLATION / SELENOCYSTEINE / SECIS ELEMENT / EF-SEC / SEC-TRNA(SEC)
Function / homology
Function and homology information


selenocysteine incorporation / translation elongation factor activity / GTPase activity / GTP binding / RNA binding / cytoplasm
Similarity search - Function
: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Ribosomal protein L35A superfamily / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain ...: / Archaeal selenocysteine-specific elongation factor, domain III / translation elongation factor selb, chain A, domain 4 / Translation elongation factor, selenocysteine-specific / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation factors / Ribosomal protein L35A superfamily / Translation elongation factor EFTu-like, domain 2 / Elongation factor Tu domain 2 / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Elongation Factor Tu (Ef-tu); domain 3 / Small GTP-binding protein domain / Thrombin, subunit H / Translation protein, beta-barrel domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-MONOPHOSPHATE / GUANOSINE-5'-DIPHOSPHATE / Selenocysteine-specific elongation factor
Similarity search - Component
Biological speciesMETHANOCOCCUS MARIPALUDIS (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.03 Å
AuthorsLeibundgut, M. / Frick, C. / Thanbichler, M. / Boeck, A. / Ban, N.
CitationJournal: Embo J. / Year: 2005
Title: Selenocysteine tRNA-Specific Elongation Factor Selb is a Structural Chimaera of Elongation and Initiation Factors.
Authors: Leibundgut, M. / Frick, C. / Thanbichler, M. / Bock, A. / Ban, N.
History
DepositionDec 14, 2011Deposition site: PDBE / Processing site: PDBE
SupersessionAug 22, 2012ID: 1WB1
Revision 1.0Aug 22, 2012Provider: repository / Type: Initial release
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "AE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -7-STRANDED BARREL THIS IS REPRESENTED BY A -6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -1-STRANDED BARREL THIS IS REPRESENTED BY A 0-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CD" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 0-STRANDED BARREL THIS IS REPRESENTED BY A 1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DF" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -3-STRANDED BARREL THIS IS REPRESENTED BY A -2-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MJ0495-LIKE PROTEIN
B: MJ0495-LIKE PROTEIN
C: MJ0495-LIKE PROTEIN
D: MJ0495-LIKE PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)221,77225
Polymers216,5864
Non-polymers5,18621
Water21612
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A: MJ0495-LIKE PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,6143
Polymers54,1471
Non-polymers4682
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: MJ0495-LIKE PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,5627
Polymers54,1471
Non-polymers1,4156
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: MJ0495-LIKE PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,45014
Polymers54,1471
Non-polymers3,30313
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: MJ0495-LIKE PROTEIN


Theoretical massNumber of molelcules
Total (without water)54,1471
Polymers54,1471
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)146.920, 146.920, 297.480
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number151
Space group name H-MP3112

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
MJ0495-LIKE PROTEIN / TRANSLATION ELONGATION FACTOR SELB


Mass: 54146.504 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) METHANOCOCCUS MARIPALUDIS (archaea) / Strain: JJ / Description: GERMAN COLLECTION OF MICROORGANISMS (DSM 2067) / Plasmid: PT7-7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q8J307

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Non-polymers , 6 types, 33 molecules

#2: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#5: Chemical
ChemComp-DXC / (3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC ACID / DEOXYCHOLIC ACID / Deoxycholic acid


Mass: 392.572 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C24H40O4 / Comment: detergent*YM
#6: Chemical ChemComp-5GP / GUANOSINE-5'-MONOPHOSPHATE / Guanosine monophosphate


Mass: 363.221 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H14N5O8P
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 12 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsN-TERMINAL RESIDUES ORIGINATING FROM 6XHIS TAG

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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: 4.28 Å3/Da / Density % sol: 71.26 %
Description: THE INCREASED MERGING R VALUE IN THE HIGHEST RESOLUTION SHELL OF 1.27 IS OWING TO ANISOTROPY OF THE DATA
Crystal growDetails: 10 MM KCL,20 MM TRIS/HCL (PH 7.5),40 MM MGSO4,2 MM DTT,3 MM GDP,1.8 - 2.0 M AMMONIUM SULFATE,100 MM SODIUM CITRATE (PH 6.0),1 MM DEOXYCHOLIC ACID.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: MARRESEARCH MAR165 / Detector: CCD / Date: Feb 21, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.03→50 Å / Num. obs: 139069 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 8 % / Biso Wilson estimate: 84.94 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 14.37
Reflection shellResolution: 3.03→3.21 Å / Redundancy: 7.8 % / Rmerge(I) obs: 1.27 / Mean I/σ(I) obs: 2 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8_1069)refinement
XDSdata reduction
XSCALEdata scaling
CNSphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 3.03→19.975 Å / SU ML: 0.36 / σ(F): 0.75 / Phase error: 24.29 / Stereochemistry target values: ML
Details: A FOBS OVER SIGMA_FOBS CUTOFF OF 0.75 WAS APPLIED OWING TO ANISOTROPY OF THE DATA. THE MODEL WAS REFINED AGAINST ANOMALOUSLY SCALED DATA
RfactorNum. reflection% reflection
Rfree0.2221 5159 4.2 %
Rwork0.1899 --
obs0.1913 123933 89.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 147.9 Å2
Baniso -1Baniso -2Baniso -3
1-8.7713 Å20 Å20 Å2
2--8.7713 Å20 Å2
3----17.5426 Å2
Refinement stepCycle: LAST / Resolution: 3.03→19.975 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14274 0 342 12 14628
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00414820
X-RAY DIFFRACTIONf_angle_d0.97820033
X-RAY DIFFRACTIONf_dihedral_angle_d15.1295665
X-RAY DIFFRACTIONf_chiral_restr0.0652421
X-RAY DIFFRACTIONf_plane_restr0.0042451
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.03-3.06430.35631410.3423320X-RAY DIFFRACTION74
3.0643-3.10020.36831470.33543338X-RAY DIFFRACTION75
3.1002-3.13790.34511330.30923291X-RAY DIFFRACTION74
3.1379-3.17750.31321480.29793373X-RAY DIFFRACTION76
3.1775-3.21910.3111650.27653552X-RAY DIFFRACTION80
3.2191-3.2630.31171500.27063647X-RAY DIFFRACTION80
3.263-3.30940.3351510.26193535X-RAY DIFFRACTION82
3.3094-3.35860.27571610.25173655X-RAY DIFFRACTION82
3.3586-3.41080.2951530.24793649X-RAY DIFFRACTION81
3.4108-3.46650.27641660.24233845X-RAY DIFFRACTION87
3.4665-3.52590.27951570.2363666X-RAY DIFFRACTION82
3.5259-3.58970.27581730.21993788X-RAY DIFFRACTION85
3.5897-3.65830.25121540.20583839X-RAY DIFFRACTION86
3.6583-3.73250.27061690.19813998X-RAY DIFFRACTION90
3.7325-3.81310.24551760.18744011X-RAY DIFFRACTION91
3.8131-3.90120.18331590.18974066X-RAY DIFFRACTION91
3.9012-3.9980.24261880.17824011X-RAY DIFFRACTION90
3.998-4.10520.21811910.17034139X-RAY DIFFRACTION93
4.1052-4.22490.17091860.1614173X-RAY DIFFRACTION94
4.2249-4.35990.17391840.14494270X-RAY DIFFRACTION96
4.3599-4.5140.18621910.14424203X-RAY DIFFRACTION96
4.514-4.69250.1761910.13984325X-RAY DIFFRACTION97
4.6925-4.90310.17631940.14514419X-RAY DIFFRACTION98
4.9031-5.15730.18361890.15174324X-RAY DIFFRACTION98
5.1573-5.47420.2361880.16924397X-RAY DIFFRACTION98
5.4742-5.88680.19841910.18314387X-RAY DIFFRACTION98
5.8868-6.4610.26071930.20194376X-RAY DIFFRACTION99
6.461-7.35470.25491990.20364453X-RAY DIFFRACTION100
7.3547-9.11720.15941900.17114423X-RAY DIFFRACTION100
9.1172-19.97560.20691810.19244301X-RAY DIFFRACTION97
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)
13.8796-0.2813-0.20025.01831.5153.3983-0.192-0.64520.10.388-0.00540.45520.196-0.78330.1540.519-0.06930.03011.3032-0.01190.542428.7681-37.4572-50.6364
23.4672-0.90470.97094.2468-1.65932.9042-0.16510.08280.21120.08090.33080.2848-0.5511-0.5126-0.08461.00460.4316-0.01660.75790.01950.617144.2293-13.3694-9.5726
34.01080.2292-1.49981.9852-1.06114.5453-0.01330.4847-0.0774-0.40440.05080.04150.2349-0.2925-0.0420.64160.0825-0.07140.4881-0.00990.340969.0417-50.031324.0861
41.7036-0.7893-0.10335.202-1.53611.7173-0.20040.08170.44490.09990.46920.9785-0.8048-0.6028-0.26122.07070.8461-0.05681.224-0.0811.268631.064915.7481-17.7785
55.1989-0.5434-1.12064.80613.17083.7765-0.5062-2.68620.61941.24270.0946-0.85490.3942-2.1240.09291.1440.462-0.18163.247-0.59910.685918.7342-25.2079-27.5867
64.90260.4302-0.18884.1746-0.82263.5646-0.1611-0.4578-0.04060.21550.11140.1133-0.5626-0.19250.11520.81280.2697-0.03910.55540.00370.371658.759-27.48998.5088
76.6653-1.25180.92064.95071.79918.38830.18750.34810.3429-0.627-0.0334-0.5826-0.32161.1783-0.16890.532-0.01610.09610.67140.05040.48192.7078-46.269311.8633
84.1344-2.64440.07423.20551.19340.896-0.323-0.13640.6171-0.46120.284-0.1539-1.3665-0.04050.10162.86510.6632-0.14131.14290.06391.575739.728432.1057-35.8225
97.1631-1.72930.42774.15160.64070.847-0.4604-0.67930.2115-0.8553-0.30220.30520.2225-1.63770.41520.73110.3386-0.18313.1547-0.50291.1760.6591-28.2522-51.7151
106.63561.0845-2.60465.84820.55144.29030.41480.3358-0.2679-1.11370.13311.5230.0781-2.2404-0.45291.06640.0479-0.30821.56650.29280.941730.3508-37.24331.6851
112.371-0.0758-1.05611.8612-1.87213.84130.0248-0.3913-0.050.2541-0.2725-0.3115-0.38890.51080.15690.58380.0408-0.06170.89320.00070.473994.4614-53.359641.8886
127.41853.90421.83575.5042.05990.5966-0.2949-0.71850.9401-0.08030.0207-1.3277-0.89760.30850.16682.15980.0117-0.31370.9508-0.16291.460561.952114.9965-25.1015
138.3217-0.29547.41673.9303-0.12347.3655-0.3292-1.52430.75350.64260.143-0.7028-0.82860.44550.22440.91430.0208-0.14732.4283-0.25741.2618-24.7104-22.5441-76.2041
142.57833.574-1.99664.6593-1.48887.0662-0.02691.141.8406-0.4580.02281.90320.6544-2.33210.15771.5731-0.1712-0.24832.1360.29972.3188-1.542-50.0663-1.1349
157.71840.29124.82448.1571-1.63155.9554-0.0826-0.9767-0.24761.0379-0.0736-1.41640.13071.46080.14570.90440.1-0.20931.53610.020.8929111.373-55.244174.0806
160.11780.302-0.50332.3139-2.94111.10420.3642-0.57090.43970.0099-0.6811-1.3285-0.24360.44130.03942.5478-0.4189-0.04842.0333-0.16453.103796.35937.12-15.996
172.00294.6573.71352.0041-0.42560.93850.0848-1.00740.43241.3039-0.1942-1.2052-0.91272.61290.13492.12670.1294-1.39382.0187-0.46113.451329.9422-21.8543-14.5523
186.51268.37785.25922.00082.72162.0043-0.4631-0.11490.5797-0.04060.48420.16510.08090.60540.01961.4931-0.239-0.73480.81260.54441.600875.3035-24.84284.7275
194.066-8.5854-1.15982.01654.47792.00730.9879-1.2144-1.12650.7938-0.87891.08581.1299-1.0308-0.16210.9896-0.18720.11850.66640.14410.755370.159-61.838340.5836
202.00264.1686-3.24162.00812.00542.0056-0.59080.6748-0.7982-0.39390.64460.31161.4515-1.39940.09180.9126-0.1703-0.37161.0723-0.06970.765748.6559-56.832327.2072
212.00048.4158-2.66742.00858.69632.0035-0.37320.78780.5848-1.06490.01340.7493-1.2752-1.59980.24980.8223-0.18970.05851.0458-0.08850.487449.3218-49.795630.5379
222.00172.37291.99082.0281-6.38212.02050.2458-0.2885-1.21360.1734-0.1864-0.41730.3729-0.18280.00451.23340.10480.01060.49930.01690.463879.6854-58.518553.7107
232.0006222.00052.00022.000710.3569-15.1287.237624.8059-6.9873-15.6737-2.9841-51.4276-3.3642.5081-0.3730.04642.6565-0.28111.083449.2787-36.0757-10.6148
242.00021.99932.00022.00121.99972.0013.2757-60.6123-12.74864.36714.492647.438-3.3289-21.8593-7.82051.12820.03930.30082.94230.74742.891572.9833-38.14224.9523
251.99981.9998-5.1924222.0001-2.6967-1.77443.54731.34191.63925.9416-6.4295-18.321.04581.5119-0.0056-1.00291.76910.33821.125979.7227-49.252343.6793
262.00022.00022.00022.00012.00022.0003-1.268515.84235.790937.42316.4348-12.27326.88070.4892-5.18711.69260.2063-0.50131.38020.31990.821275.877-45.123247.0393
272.00092.00042.00012.000222.0003-3.4712-5.4785-11.02288.05512.3548-47.85517.889-22.05731.12311.0050.12740.00111.7471-0.35781.9929113.3473-54.723557.6637
282.000422.00032.00041.99992.000320.430627.2398-6.5571-10.2299-10.92563.690626.164124.226-9.4982.00790.4516-0.51922.22031.23421.755672.6322-66.88932.7758
292.00032-5.07682.00031.99982.00033.764912.1187-14.2884-14.176-6.1145.1808-26.55859.74082.35111.41880.6585-0.00231.66780.45411.272290.3702-65.73454.394
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1((CHAIN A AND RESID 0:179) OR (CHAIN A AND RESID 1469:1470) OR (CHAIN A AND RESID 2001:2004))
2X-RAY DIFFRACTION2((CHAIN B AND RESID 1:179) OR (CHAIN B AND RESID 1469:1470) OR (CHAIN B AND RESID 2001:2004))
3X-RAY DIFFRACTION3((CHAIN C AND RESID -2:179) OR (CHAIN C AND RESID 1469:1470) OR (CHAIN C AND RESID 2001:2004))
4X-RAY DIFFRACTION4(CHAIN D AND RESID 2:179)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 180:270)
6X-RAY DIFFRACTION6((CHAIN B AND RESID 180:270) OR (CHAIN B AND RESID 1473))
7X-RAY DIFFRACTION7((CHAIN C AND RESID 180:270) OR (CHAIN C AND RESID 1475))
8X-RAY DIFFRACTION8(CHAIN D AND RESID 180:270)
9X-RAY DIFFRACTION9(CHAIN A AND RESID 271:388)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 271:388)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 271:388)
12X-RAY DIFFRACTION12(CHAIN D AND RESID 271:388)
13X-RAY DIFFRACTION13(CHAIN A AND RESID 389:468)
14X-RAY DIFFRACTION14(CHAIN B AND RESID 389:468)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 389:468)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 389:468)
17X-RAY DIFFRACTION17(CHAIN B AND RESID 1474)
18X-RAY DIFFRACTION18(CHAIN C AND RESID 1476)
19X-RAY DIFFRACTION19(CHAIN C AND RESID 1477)
20X-RAY DIFFRACTION20(CHAIN C AND RESID 1478)
21X-RAY DIFFRACTION21(CHAIN C AND RESID 1479)
22X-RAY DIFFRACTION22(CHAIN C AND RESID 1480)
23X-RAY DIFFRACTION23(CHAIN B AND RESID 1471)
24X-RAY DIFFRACTION24(CHAIN B AND RESID 1472)
25X-RAY DIFFRACTION25(CHAIN C AND RESID 1471)
26X-RAY DIFFRACTION26(CHAIN C AND RESID 1472)
27X-RAY DIFFRACTION27(CHAIN C AND RESID 1473)
28X-RAY DIFFRACTION28(CHAIN C AND RESID 1474)
29X-RAY DIFFRACTION29(CHAIN C AND RESID 1481)

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