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- PDB-13gn: Crystal Structure of L-erythrulose-1-phosphate isomerase from Bru... -

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Basic information

Entry
Database: PDB / ID: 13gn
TitleCrystal Structure of L-erythrulose-1-phosphate isomerase from Brucella melitensis in complex with SN-GLYCEROL-1-PHOSPHATE
ComponentsL-erythrulose-1-phosphate isomerase
KeywordsISOMERASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / L-erythrulose-1-phosphate isomerase / Brucella melitensis
Function / homology
Function and homology information


L-erythrulose-1-phosphate isomerase / triose-phosphate isomerase activity / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / glycolytic process / gluconeogenesis / cytosol
Similarity search - Function
Triosephosphate isomerase, active site / Triosephosphate isomerase active site. / Triosephosphate isomerase / Triosephosphate isomerase superfamily / Triosephosphate isomerase / Triosephosphate isomerase (TIM) family profile. / Aldolase-type TIM barrel
Similarity search - Domain/homology
SN-GLYCEROL-1-PHOSPHATE / L-erythrulose-1-phosphate isomerase
Similarity search - Component
Biological speciesBrucella abortus 2308 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)75N93022C00036 United States
National Institutes of Health/Office of the DirectorS10OD030394 United States
CitationJournal: To be published
Title: Crystal Structure of L-erythrulose-1-phosphate isomerase from Brucella melitensis in complex with SN-GLYCEROL-1-PHOSPHATE
Authors: Liu, L. / Lovell, S. / Battaile, K.P.
History
DepositionMay 5, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 20, 2026Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: L-erythrulose-1-phosphate isomerase
B: L-erythrulose-1-phosphate isomerase
C: L-erythrulose-1-phosphate isomerase
D: L-erythrulose-1-phosphate isomerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)115,37213
Polymers114,9794
Non-polymers3939
Water10,323573
1
A: L-erythrulose-1-phosphate isomerase
D: L-erythrulose-1-phosphate isomerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,8018
Polymers57,4892
Non-polymers3126
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4520 Å2
ΔGint-81 kcal/mol
Surface area17530 Å2
MethodPISA
2
B: L-erythrulose-1-phosphate isomerase
C: L-erythrulose-1-phosphate isomerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,5715
Polymers57,4892
Non-polymers813
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3790 Å2
ΔGint-53 kcal/mol
Surface area18360 Å2
MethodPISA
Unit cell
Length a, b, c (Å)45.802, 49.525, 104.793
Angle α, β, γ (deg.)92.72, 96.10, 93.72
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
L-erythrulose-1-phosphate isomerase / D-3-tetrulose-4-phosphate isomerase


Mass: 28744.627 Da / Num. of mol.: 4 / Fragment: K3-N256 / Mutation: A173D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Brucella abortus 2308 (bacteria) / Gene: eryH, tpiA-2, BAB2_0367 / Plasmid: BrabA.00276.a.B2 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: Q2YIQ6, L-erythrulose-1-phosphate isomerase
#2: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#3: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-1GP / SN-GLYCEROL-1-PHOSPHATE


Mass: 172.074 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H9O6P / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 573 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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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: 2.05 Å3/Da / Density % sol: 39.95 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 70 mM MES pH 6.5, 70 mM CaCl2, 14% PEG 1500, 8.4% hexanediol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. 20 hour soak in 10 mM glycerol 3-phosphate (D/L mixture), 1GP fit best to the electron ...Details: 70 mM MES pH 6.5, 70 mM CaCl2, 14% PEG 1500, 8.4% hexanediol. BrabA.00276.a.B2.PW39519 at 15.2 mg/mL. 20 hour soak in 10 mM glycerol 3-phosphate (D/L mixture), 1GP fit best to the electron density, plate Liu-S-202 E9-F10, Puck: PSL-0208, Cryo: 100 mM MES, pH 6.5, 100 mM CaCl2, 20% PEG 1500, 12% hexanediol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
DetectorType: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Feb 22, 2026
RadiationMonochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 1.95→45.56 Å / Num. obs: 64555 / % possible obs: 97 % / Redundancy: 3.6 % / CC1/2: 0.996 / Rmerge(I) obs: 0.112 / Rpim(I) all: 0.07 / Rrim(I) all: 0.133 / Χ2: 1.05 / Net I/σ(I): 9 / Num. measured all: 230370
Reflection shellResolution: 1.95→2 Å / % possible obs: 96.6 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.888 / Num. measured all: 17637 / Num. unique obs: 4781 / CC1/2: 0.644 / Rpim(I) all: 0.538 / Rrim(I) all: 1.04 / Χ2: 0.95 / Net I/σ(I) obs: 1.6

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Processing

Software
NameVersionClassification
PHENIX(2.1rc2_6044: ???)refinement
Aimlessdata scaling
XDSdata reduction
PHASERphasing
PDB_EXTRACTdata extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.95→45.56 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 23.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2163 3331 5.16 %
Rwork0.1622 --
obs0.165 64538 96.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.95→45.56 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7392 0 18 573 7983
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.017586
X-RAY DIFFRACTIONf_angle_d1.02710289
X-RAY DIFFRACTIONf_dihedral_angle_d16.7272778
X-RAY DIFFRACTIONf_chiral_restr0.0571163
X-RAY DIFFRACTIONf_plane_restr0.0121338
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.95-1.980.37121390.27232626X-RAY DIFFRACTION96
1.98-2.010.33921160.25552459X-RAY DIFFRACTION96
2.01-2.040.291480.23182556X-RAY DIFFRACTION97
2.04-2.070.29731310.21722569X-RAY DIFFRACTION97
2.07-2.110.25841410.20272542X-RAY DIFFRACTION96
2.11-2.150.24291360.19932509X-RAY DIFFRACTION96
2.15-2.190.26831490.19352569X-RAY DIFFRACTION97
2.19-2.230.26971480.18472489X-RAY DIFFRACTION97
2.23-2.280.2331430.17852569X-RAY DIFFRACTION97
2.28-2.330.24411410.17452540X-RAY DIFFRACTION97
2.33-2.390.27241280.16972566X-RAY DIFFRACTION97
2.39-2.460.24721420.15812517X-RAY DIFFRACTION97
2.46-2.530.22251200.16152615X-RAY DIFFRACTION98
2.53-2.610.22371440.14762557X-RAY DIFFRACTION97
2.61-2.70.25031320.16442540X-RAY DIFFRACTION97
2.7-2.810.22561210.16062610X-RAY DIFFRACTION98
2.81-2.940.1921240.16422564X-RAY DIFFRACTION97
2.94-3.10.22241380.16432598X-RAY DIFFRACTION98
3.1-3.290.18921290.1552560X-RAY DIFFRACTION97
3.29-3.540.18891410.1512549X-RAY DIFFRACTION97
3.54-3.90.19731710.13832486X-RAY DIFFRACTION97
3.9-4.460.15941520.12442505X-RAY DIFFRACTION96
4.46-5.620.18341330.13132570X-RAY DIFFRACTION97
5.62-45.560.19981640.16722542X-RAY DIFFRACTION98
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)
11.16890.41510.62196.21962.51833.9492-0.06340.0672-0.0566-0.4579-0.07170.239-0.1573-0.17740.13570.1778-0.0013-0.03240.2140.00940.189717.786929.630278.5153
26.35444.07755.80166.16354.52236.1585-0.1066-0.04250.4414-0.4053-0.08910.8285-0.1746-0.5480.18810.23760.0217-0.07740.2370.02680.309410.659640.062378.184
31.9174-1.5314-1.26983.3886-0.4351.8103-0.00520.341-0.4923-0.4863-0.02690.66430.1199-0.27860.04280.3719-0.0347-0.10890.2476-0.00840.33398.811327.187875.9073
44.4061-0.2972.951.70160.3344.3079-0.0176-0.1747-0.1309-0.20870.05740.3762-0.1416-0.358-0.01950.24390.017-0.03630.23980.02650.256412.531532.55387.0531
51.415-0.32550.98541.99150.88443.2394-0.017-0.2262-0.11260.05320.02120.11930.2459-0.281-0.01330.2211-0.0277-0.01830.21020.02690.244818.674327.922695.7477
62.56460.7766-1.26862.23940.11562.3683-0.0992-0.06530.0625-0.16620.0962-0.26340.18750.19950.01560.24450.03-0.00510.20820.03040.289827.738419.257388.2358
73.4389-1.1625-4.82645.32141.73886.7762-0.201-0.2944-0.6912-0.58720.0621-0.03510.23850.38080.10.29870.0152-0.00410.23460.02270.282828.91369.653686.2082
81.6045-0.1236-1.56871.9044-0.11744.2659-0.07510.0413-0.0814-0.3780.00260.06450.09590.04580.06230.33320.0047-0.060.17420.00570.280320.971913.965285.0967
90.19020.3832-0.28053.7347-2.60262.49880.0020.0669-0.0458-0.6933-0.00130.05350.2209-0.04790.01650.39170.0114-0.02620.1948-0.01280.257421.998712.376876.2747
101.85981.88580.13224.58590.47032.1686-0.18780.2457-0.0324-0.42920.31670.10280.2114-0.0122-0.1020.47-0.0106-0.0710.2168-0.00880.216919.906422.273370.5731
116.7757-2.3384-1.10065.45411.75428.35670.06160.3997-0.1842-0.3101-0.27960.19940.6497-0.56840.27180.4627-0.0152-0.10420.2847-0.01920.316912.952326.856766.4702
122.76830.7409-0.15783.75482.33655.5427-0.06190.2155-0.0812-0.0424-0.06660.28490.3452-0.09950.11550.1983-0.0034-0.01530.19660.01230.201516.361724.405735.9746
135.67012.8752-0.11958.17684.03666.675-0.047-0.2131-0.10720.8805-0.0090.23860.6014-0.4560.04560.3017-0.01970.00160.22930.00120.254811.469620.989547.0217
143.3098-0.13740.83151.8459-0.30325.15860.0597-0.1387-0.150.1871-0.01350.08470.1333-0.1786-0.02530.1714-0.00370.02820.1898-0.0110.201419.124119.628441.6041
152.71641.2177-0.98722.0326-0.3951.60240.00160.0981-0.1772-0.09740.084-0.24160.10070.0563-0.06760.23590.0135-0.02010.1904-0.0070.217830.458526.452840.8121
161.627-0.60240.29132.0567-0.52553.0493-0.01790.15960.02130.0623-0.0406-0.0163-0.0536-0.01810.04890.2173-0.0247-0.00370.2129-0.01430.211630.912528.690634.6108
173.5686-0.93930.16943.5252-1.04344.361-0.01720.57230.3885-0.4827-0.05770.2499-0.2046-0.07090.1210.3093-0.0192-0.06230.30350.01850.296725.158331.889822.1026
185.8526-3.87994.82683.8666-3.35238.6517-0.0080.48150.2232-0.355-0.2247-0.2653-0.40250.22990.22230.3524-0.0105-0.0010.40470.00210.222631.240129.358817.9521
195.6126-0.7991.8172.7857-0.36923.50560.01680.33640.0303-0.2180.0515-0.07620.27050.226-0.06920.3188-0.0040.01110.2575-0.04530.213829.985522.215624.2919
206.1407-1.1935-0.56682.32540.3223.18540.18650.3235-0.1162-0.4139-0.09860.22020.18280.0063-0.07840.2997-0.0087-0.0440.2521-0.00230.205320.988122.305318.8921
213.8403-0.7881-0.98793.28071.61838.0206-0.23460.26890.0135-0.44390.06890.3725-0.1162-0.39710.16240.3055-0.0511-0.07350.21350.02490.270712.07622.743825.9603
225.38860.74241.64695.19940.54788.4143-0.20590.3935-0.1834-0.19180.38160.11390.1559-0.3232-0.13760.2351-0.06-0.00830.26330.02070.36816.378217.45531.0996
232.02431.01640.77037.14672.56213.33270.0115-0.0422-0.0030.660.0928-0.25770.21560.3059-0.06860.24940.0016-0.0340.22080.02320.199336.620538.974955.8921
241.112-0.226-1.06394.77254.71686.53170.0724-0.0622-0.11170.5473-0.03780.0010.92660.0778-0.00040.40420.0206-0.06380.22230.01930.234134.873429.381263.546
250.91060.04750.35631.4464-0.4852.5070.0142-0.09610.0340.2089-0.02490.0424-0.0722-0.0810.03480.26130.011-0.01520.1568-0.01010.187526.098838.448953.5859
262.5245-1.1558-1.81462.58710.6753.49890.08220.10740.0341-0.2623-0.08810.0718-0.3405-0.0204-0.02250.3021-0.0117-0.03180.1981-0.00830.233328.205347.302641.8371
279.49774.3129-3.94793.6539-1.67362.4877-0.05090.43930.18270.0940.1934-0.0732-0.0411-0.0361-0.19030.2909-0.0124-0.04110.2149-0.01190.249436.961453.315244.6283
284.05971.0918-0.67780.7705-0.48021.46360.1773-0.0810.22370.1672-0.0367-0.03240.01440.133-0.1310.40310.0014-0.02580.1726-0.03160.249731.862756.070748.364
292.8381-0.5705-0.44583.0112-0.65171.61030.1378-0.15840.21220.1835-0.1521-0.2588-0.37180.2830.02290.3538-0.0534-0.08250.2157-0.00920.262939.126656.600154.2726
302.62951.23060.97441.82271.5213.3501-0.18510.2607-0.00510.12630.2588-0.4292-0.33520.668-0.08640.3197-0.0656-0.08150.34080.01470.276343.989546.903458.1352
319.19224.55721.93377.39973.64619.1808-0.1482-0.2508-0.02170.86090.2697-0.7818-0.00640.381-0.10260.39780.0023-0.15560.30590.00810.28644.70241.453965.7801
322.81760.0644-0.21991.55580.03172.23350.0056-0.1970.19750.1778-0.0320.0707-0.1985-0.07020.04240.15940.02830.0140.2036-0.01730.193219.587847.185106.8842
331.3711-0.802-0.74592.23950.94762.9255-0.10690.08370.0886-0.00210.04960.1491-0.2746-0.12980.08660.19340.0096-0.030.2030.03080.277520.448546.014997.3542
341.46180.51590.7961.3953-0.01631.27390.01440.008-0.0809-0.13550.0089-0.14650.08110.0759-0.01060.18740.02190.02250.2168-0.01360.223732.063939.69192.0575
352.9221-1.15420.66575.0295-2.46332.8856-0.1225-0.1362-0.010.5524-0.1508-0.4688-0.11960.26310.24690.1838-0.0183-0.0260.2710.010.261640.595238.2232105.4025
362.878-2.1562.85324.4401-3.60938.83150.0226-0.23920.07810.2205-0.2305-0.53130.06010.34690.1640.1668-0.02480.00050.3880.01970.399647.686840.0758102.7542
373.09490.2263-0.81655.928-2.24875.72040.0791-0.04310.13680.1494-0.2276-0.3643-0.26080.41040.12550.0814-0.0391-0.01710.2019-0.00140.275540.67347.585899.7647
384.6114-0.045-1.06523.3564-2.01948.19560.0812-0.42170.25940.38770.0103-0.5235-0.24160.5093-0.06660.2633-0.049-0.08480.2982-0.0710.377845.508146.4079110.3637
396.08632.5182-4.72122.9756-3.17716.98180.2574-0.57380.36860.4699-0.0390.1258-0.47350.102-0.16950.24050.0243-0.06310.2778-0.0390.2935.3446.7119112.1274
407.51833.60630.95483.83110.45412.8460.1862-0.68310.04030.3715-0.0603-0.1005-0.0623-0.0363-0.13890.2760.0145-0.04050.2718-0.02220.217230.822345.4776115.6429
417.13180.35252.7286.79771.12792.03930.0604-1.06130.36070.6608-0.18940.2721-0.5881-0.52690.07750.39370.00710.08510.3736-0.02570.213623.143250.3726118.2367
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 15 )
2X-RAY DIFFRACTION2chain 'A' and (resid 16 through 28 )
3X-RAY DIFFRACTION3chain 'A' and (resid 29 through 44 )
4X-RAY DIFFRACTION4chain 'A' and (resid 45 through 68 )
5X-RAY DIFFRACTION5chain 'A' and (resid 69 through 96 )
6X-RAY DIFFRACTION6chain 'A' and (resid 97 through 139 )
7X-RAY DIFFRACTION7chain 'A' and (resid 140 through 152 )
8X-RAY DIFFRACTION8chain 'A' and (resid 153 through 183 )
9X-RAY DIFFRACTION9chain 'A' and (resid 184 through 217 )
10X-RAY DIFFRACTION10chain 'A' and (resid 218 through 238 )
11X-RAY DIFFRACTION11chain 'A' and (resid 239 through 253 )
12X-RAY DIFFRACTION12chain 'B' and (resid 3 through 15 )
13X-RAY DIFFRACTION13chain 'B' and (resid 16 through 29 )
14X-RAY DIFFRACTION14chain 'B' and (resid 30 through 54 )
15X-RAY DIFFRACTION15chain 'B' and (resid 55 through 80 )
16X-RAY DIFFRACTION16chain 'B' and (resid 81 through 119 )
17X-RAY DIFFRACTION17chain 'B' and (resid 120 through 139 )
18X-RAY DIFFRACTION18chain 'B' and (resid 140 through 152 )
19X-RAY DIFFRACTION19chain 'B' and (resid 153 through 182 )
20X-RAY DIFFRACTION20chain 'B' and (resid 183 through 217 )
21X-RAY DIFFRACTION21chain 'B' and (resid 218 through 238 )
22X-RAY DIFFRACTION22chain 'B' and (resid 239 through 253 )
23X-RAY DIFFRACTION23chain 'C' and (resid 3 through 15 )
24X-RAY DIFFRACTION24chain 'C' and (resid 16 through 32 )
25X-RAY DIFFRACTION25chain 'C' and (resid 33 through 96 )
26X-RAY DIFFRACTION26chain 'C' and (resid 97 through 119 )
27X-RAY DIFFRACTION27chain 'C' and (resid 120 through 139 )
28X-RAY DIFFRACTION28chain 'C' and (resid 140 through 182 )
29X-RAY DIFFRACTION29chain 'C' and (resid 183 through 217 )
30X-RAY DIFFRACTION30chain 'C' and (resid 218 through 238 )
31X-RAY DIFFRACTION31chain 'C' and (resid 239 through 253 )
32X-RAY DIFFRACTION32chain 'D' and (resid 3 through 44 )
33X-RAY DIFFRACTION33chain 'D' and (resid 45 through 68 )
34X-RAY DIFFRACTION34chain 'D' and (resid 69 through 119 )
35X-RAY DIFFRACTION35chain 'D' and (resid 120 through 139 )
36X-RAY DIFFRACTION36chain 'D' and (resid 140 through 151 )
37X-RAY DIFFRACTION37chain 'D' and (resid 152 through 182 )
38X-RAY DIFFRACTION38chain 'D' and (resid 183 through 201 )
39X-RAY DIFFRACTION39chain 'D' and (resid 202 through 217 )
40X-RAY DIFFRACTION40chain 'D' and (resid 218 through 238 )
41X-RAY DIFFRACTION41chain 'D' and (resid 239 through 254 )

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