[English] 日本語
Yorodumi
- PDB-5udq: LarE, a sulfur transferase involved in synthesis of the cofactor ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 5udq
TitleLarE, a sulfur transferase involved in synthesis of the cofactor for lactate racemase, apo form
ComponentsLactate racemization operon protein LarE
KeywordsTRANSFERASE / Lar / sulfur transferase / LarE / AMPylation / hexamer / trimer / PP-loop / ATP pyrophophatase domain / lactate / lactate racemization / lactate racemase
Function / homology
Function and homology information


pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase / sulfurtransferase activity / lyase activity / ATP binding
Similarity search - Function
Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase LarE / : / NAD/GMP synthase / NAD synthase / Rossmann-like alpha/beta/alpha sandwich fold
Similarity search - Domain/homology
PHOSPHATE ION / Pyridinium-3,5-bisthiocarboxylic acid mononucleotide synthase
Similarity search - Component
Biological speciesLactobacillus plantarum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.09 Å
AuthorsFellner, M. / Desguin, B. / Hausinger, R.P. / Hu, J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States) United States
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017
Title: Structural insights into the catalytic mechanism of a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family, LarE.
Authors: Fellner, M. / Desguin, B. / Hausinger, R.P. / Hu, J.
History
DepositionDec 28, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 23, 2017Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Nov 27, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Lactate racemization operon protein LarE
B: Lactate racemization operon protein LarE
C: Lactate racemization operon protein LarE
D: Lactate racemization operon protein LarE
E: Lactate racemization operon protein LarE
F: Lactate racemization operon protein LarE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)191,65120
Polymers190,3136
Non-polymers1,33814
Water11,403633
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16640 Å2
ΔGint-231 kcal/mol
Surface area61690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.401, 107.401, 317.042
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number91
Space group name H-MP4122
Components on special symmetry positions
IDModelComponents
11E-448-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 2 through 15 or (resid 16...
21(chain B and (resid 2 through 6 or (resid 7...
31(chain C and (resid 2 through 6 or (resid 7...
41(chain D and (resid 2 through 6 or (resid 7...
51(chain E and (resid 2 through 6 or (resid 7...
61(chain F and (resid 2 through 6 or (resid 7...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 2 through 15 or (resid 16...A2 - 15
121(chain A and (resid 2 through 15 or (resid 16...A16 - 17
131(chain A and (resid 2 through 15 or (resid 16...A2 - 276
141(chain A and (resid 2 through 15 or (resid 16...A2 - 276
151(chain A and (resid 2 through 15 or (resid 16...A2 - 276
161(chain A and (resid 2 through 15 or (resid 16...A2 - 276
211(chain B and (resid 2 through 6 or (resid 7...B2 - 6
221(chain B and (resid 2 through 6 or (resid 7...B7
231(chain B and (resid 2 through 6 or (resid 7...B2 - 259
241(chain B and (resid 2 through 6 or (resid 7...B2 - 259
251(chain B and (resid 2 through 6 or (resid 7...B2 - 259
261(chain B and (resid 2 through 6 or (resid 7...B2 - 259
311(chain C and (resid 2 through 6 or (resid 7...C2 - 6
321(chain C and (resid 2 through 6 or (resid 7...C7
331(chain C and (resid 2 through 6 or (resid 7...C2 - 259
341(chain C and (resid 2 through 6 or (resid 7...C2 - 259
351(chain C and (resid 2 through 6 or (resid 7...C2 - 259
361(chain C and (resid 2 through 6 or (resid 7...C2 - 259
411(chain D and (resid 2 through 6 or (resid 7...D2 - 6
421(chain D and (resid 2 through 6 or (resid 7...D7
431(chain D and (resid 2 through 6 or (resid 7...D2 - 259
441(chain D and (resid 2 through 6 or (resid 7...D2 - 259
451(chain D and (resid 2 through 6 or (resid 7...D2 - 259
461(chain D and (resid 2 through 6 or (resid 7...D2 - 259
511(chain E and (resid 2 through 6 or (resid 7...E2 - 6
521(chain E and (resid 2 through 6 or (resid 7...E7
531(chain E and (resid 2 through 6 or (resid 7...E2 - 279
541(chain E and (resid 2 through 6 or (resid 7...E2 - 279
551(chain E and (resid 2 through 6 or (resid 7...E2 - 279
561(chain E and (resid 2 through 6 or (resid 7...E2 - 279
611(chain F and (resid 2 through 6 or (resid 7...F2 - 6
621(chain F and (resid 2 through 6 or (resid 7...F7
631(chain F and (resid 2 through 6 or (resid 7...F2 - 260
641(chain F and (resid 2 through 6 or (resid 7...F2 - 260
651(chain F and (resid 2 through 6 or (resid 7...F2 - 260
661(chain F and (resid 2 through 6 or (resid 7...F2 - 260

-
Components

#1: Protein
Lactate racemization operon protein LarE


Mass: 31718.766 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) (bacteria)
Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1 / Gene: larE, lp_0109 / Plasmid: pGIR076 / Production host: Escherichia coli (E. coli) / Strain (production host): Arctic express DE3 / References: UniProt: F9UST4
#2: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 633 / 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: 2.4 Å3/Da / Density % sol: 48.79 %
Crystal growTemperature: 294.15 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 4 ul ~39 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) mixed with 4 ul reservoir solution. Hanging drop reservoir contained 100 ul of 37.5% v/v pentaerythritol ethoxylate (15/4 EO/OH), 50 ...Details: 4 ul ~39 mg/ml LarE (100 mM Tris-HCl pH 7.5, 300 mM NaCl) mixed with 4 ul reservoir solution. Hanging drop reservoir contained 100 ul of 37.5% v/v pentaerythritol ethoxylate (15/4 EO/OH), 50 mM BIS-TRIS pH 6.5, 105 mM ammonium sulfate.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.9787 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 19, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9787 Å / Relative weight: 1
ReflectionResolution: 2.09→48.03 Å / Num. obs: 110015 / % possible obs: 99.3 % / Redundancy: 6.3 % / Biso Wilson estimate: 35.97 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.076 / Net I/σ(I): 15.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Diffraction-ID% possible all
2.09-2.125.40.5760.702194.9
11.43-48.034.80.0370.995186.1

-
Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.24 Å47.49 Å
Translation8.24 Å47.49 Å

-
Processing

Software
NameVersionClassification
Aimless0.5.25data scaling
PHENIX1.11.1-2575refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASER2.6.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.09→47.489 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.94 / Phase error: 22.32
RfactorNum. reflection% reflection
Rfree0.231 10071 4.86 %
Rwork0.1866 --
obs0.1888 103709 98.46 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 102.94 Å2 / Biso mean: 46.0055 Å2 / Biso min: 19.67 Å2
Refinement stepCycle: final / Resolution: 2.09→47.489 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11559 0 70 633 12262
Biso mean--50.11 47.22 -
Num. residues----1509
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00711880
X-RAY DIFFRACTIONf_angle_d0.87416119
X-RAY DIFFRACTIONf_chiral_restr0.0561872
X-RAY DIFFRACTIONf_plane_restr0.0062082
X-RAY DIFFRACTIONf_dihedral_angle_d13.7714200
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A6088X-RAY DIFFRACTION10.704TORSIONAL
12B6088X-RAY DIFFRACTION10.704TORSIONAL
13C6088X-RAY DIFFRACTION10.704TORSIONAL
14D6088X-RAY DIFFRACTION10.704TORSIONAL
15E6088X-RAY DIFFRACTION10.704TORSIONAL
16F6088X-RAY DIFFRACTION10.704TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.087-2.11070.36722950.28625885618088
2.1107-2.13550.30133750.26336528690399
2.1355-2.16160.30263400.249366516991100
2.1616-2.18890.29793470.249266747021100
2.1889-2.21770.2873120.24666676979100
2.2177-2.24810.27333570.244566687025100
2.2481-2.28020.28053180.229666666984100
2.2802-2.31430.24193410.212366597000100
2.3143-2.35040.24823280.212266807008100
2.3504-2.3890.30023000.212167697069100
2.389-2.43010.23982900.210167096999100
2.4301-2.47430.27753720.214466437015100
2.4743-2.52190.2853600.208566266986100
2.5219-2.57340.253100.205366987008100
2.5734-2.62930.28283110.209167487059100
2.6293-2.69050.26764180.205765887006100
2.6905-2.75780.24493580.198866356993100
2.7578-2.83230.25383250.19766663698899
2.8323-2.91570.2453210.19446641696299
2.9157-3.00980.24073260.20216640696699
3.0098-3.11730.26723560.20166570692699
3.1173-3.24210.24343740.1896538691298
3.2421-3.38960.22043290.18236521685098
3.3896-3.56830.22593160.1776527684398
3.5683-3.79170.19013010.16676535683697
3.7917-4.08440.17182910.15066534682597
4.0844-4.49510.19283930.14726444683797
4.4951-5.14490.19753470.14866504685197
5.1449-6.47940.21673500.18266507685798
6.4794-47.50160.21483100.186230654093
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)
17.4717-0.17747.42610.0389-0.15162.1069-0.64010.81380.25541.0170.455-1.144-1.90550.93340.3350.9269-0.1122-0.29010.5413-0.16060.69332.282510.4151-17.4478
24.3723.6365-0.9693.83782.00539.21390.14470.0893-0.08731.77830.1688-0.2169-0.8605-0.2892-0.24160.83960.2249-0.24420.3536-0.14740.394121.42414.3178-15.2973
33.43093.2434-0.24496.8229-4.01323.4340.31710.07780.27160.58140.01381.5291-0.7048-0.4839-0.27310.58150.22970.05070.4087-0.00590.282713.7663-3.9624-16.9021
44.66912.56771.55487.89512.32315.6102-0.2408-0.0542-0.15931.00810.5520.6558-0.74380.0975-0.20041.050.23280.07590.6338-0.09440.399412.4007-5.6105-8.6781
52.2535-0.83140.41946.44831.27665.42550.23550.3761-0.1811-0.9323-0.01770.43750.08340.299-0.18910.33760.0856-0.02280.46950.01840.234115.8543-15.9406-23.2137
67.0761-7.7264-1.73622.2835-0.36993.0974-0.6737-0.83550.42560.12670.8101-0.83180.12090.1172-0.15210.30550.0266-0.08510.5266-0.06870.317418.6602-8.571-26.8645
72.1205-7.36940.00286.0511-2.75296.2935-0.33660.60950.6017-0.1564-0.033-1.14690.87690.57650.68360.4905-0.01610.0030.559-0.21690.75126.0175-4.2534-26.017
84.82374.42381.95096.77520.67023.86550.167-0.5439-0.511.5272-0.2297-1.0632-0.49290.33380.03130.78080.104-0.29170.488-0.09440.639429.58050.4748-11.0247
93.0772-0.19760.32311.1469-0.92795.37080.130.23270.0346-0.2822-0.07780.0975-0.0422-0.1163-0.03840.31040.0636-0.02580.1703-0.02130.257617.7618-29.1832-5.0257
108.937-0.7856-0.72944.068-0.87342.52480.02640.44430.565-0.2314-0.1726-0.7045-0.19160.63150.11170.4764-0.0027-0.03510.43360.07680.38331.5135-32.7-5.2284
111.437-0.3230.6073.1589-3.19275.3513-0.05610.03920.46560.1814-0.2122-0.3035-0.31290.15140.26590.2486-0.0212-0.01960.22970.00790.49869.35642.702321.9784
124.16174.1243-2.09377.5827-6.57288.3887-0.1132-0.16340.43510.40060.2240.3086-0.4486-0.5845-0.0960.22560.0363-0.01210.3429-0.04430.3961-0.7771.012528.6928
130.0695-0.12730.42334.93-3.89233.26830.04270.10120.1526-0.5024-0.08190.08740.31110.09050.04560.3248-0.01110.00290.301-0.01990.45657.5304-4.082216.6599
144.72740.3008-1.5013.40082.55195.5156-0.01810.10360.0937-0.2683-0.04810.15260.0004-0.19540.05590.21650.0023-0.05010.13570.03660.235216.9195-25.101428.0642
157.6053-2.0482-1.21965.85930.92153.7057-0.0443-0.4803-0.18120.1250.13570.4611-0.1604-0.0686-0.07470.3260.04070.02550.20920.04660.148337.768513.946711.5643
166.812-4.42361.93672.6651-1.58243.31930.58720.3728-0.9309-1.0815-0.33810.5340.3593-0.0127-0.16930.41420.0178-0.02830.2393-0.04820.346344.88830.91793.3135
172.07180.4227-2.39986.4248-9.2762.11170.1483-0.9499-0.13210.5051-0.437-1.1030.17840.29810.50040.42480.0006-0.12120.49810.06910.487359.9902-7.705217.975
186.6233-4.73284.7496.3309-2.80867.4306-0.1757-0.6045-0.19220.23590.0171-0.7302-0.0699-0.35850.0530.2729-0.0212-0.02510.2325-0.01950.200755.38464.23313.5453
192.2791-0.8906-1.97974.80492.5631.6498-0.1419-1.2519-0.28530.68530.1138-0.14890.01730.208-0.05030.3916-0.0003-0.00230.42070.05410.250144.513710.650219.4454
203.7815-0.86621.25111.02440.45050.9695-0.1836-0.3536-1.1080.17780.2260.88320.3795-0.0593-0.13360.36220.02020.06120.43020.12030.615831.79231.742613.7023
212.66812.0615-0.1482.9963-0.00551.76770.0603-0.06270.185-0.0073-0.00970.022-0.0611-0.007-0.05010.27190.0433-0.03230.17730.03780.279645.8015-24.237313.8205
222.9749-3.0836-0.49026.63330.3040.9034-0.0852-0.2283-0.15390.08950.20670.15440.29340.0807-0.12830.4856-0.05910.03180.3157-0.01680.234911.7445-69.287534.0103
237.58266.283-5.47637.9164-5.94526.71980.2346-0.92940.44820.4228-0.45880.04210.2241.08990.08930.59080.0785-0.02710.4974-0.06030.410824.6961-71.035935.414
243.4419-5.2329-1.48228.16633.17943.4897-0.2943-0.0716-0.3803-0.03240.25870.17290.42090.48270.02880.4715-0.08030.05820.32470.00410.305812.5669-55.411730.2609
256.32381.1228-0.9853.22510.11934.1835-0.1102-0.0144-0.3335-0.06190.05830.08730.3679-0.12660.05780.2901-0.0239-0.0140.1283-0.00260.221611.1466-42.053422.9074
261.48531.31690.85735.02952.27183.00130.0204-0.0267-0.39510.2612-0.0754-0.44980.9150.3370.04170.57760.12010.05540.33990.02370.389353.6745-65.884326.852
270.81932.25150.33427.64472.89961.3274-0.17240.1749-0.0359-0.10570.08790.0020.43590.17040.09690.53370.0640.0350.32580.03550.305350.1942-62.029919.3443
284.1682-0.32670.59793.0757-0.51774.83540.05890.2221-0.0442-0.2462-0.0802-0.29290.13090.3030.0130.25320.0076-0.03180.17590.03810.298143.6872-39.16821.7839
291.37630.4736-0.54983.8816-1.82242.27370.0480.19330.0119-0.4204-0.03190.37090.1451-0.0779-0.00870.47630.036-0.05290.2136-0.08170.273123.5315-75.7441-4.5573
302.98430.42141.0850.07570.67752.1539-0.09080.09860.38020.16420.11070.0471-0.65690.1147-0.08690.6018-0.00640.04010.3163-0.04670.343223.2638-71.46489.9771
312.7162-0.150.26894.40840.99222.06940.02150.1362-0.3167-0.12250.0140.08580.44070.0409-0.03350.35690.0372-0.03780.17660.01350.282928.0895-46.342-3.7522
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 18 )A2 - 18
2X-RAY DIFFRACTION2chain 'A' and (resid 19 through 42 )A19 - 42
3X-RAY DIFFRACTION3chain 'A' and (resid 43 through 58 )A43 - 58
4X-RAY DIFFRACTION4chain 'A' and (resid 59 through 72 )A59 - 72
5X-RAY DIFFRACTION5chain 'A' and (resid 73 through 95 )A73 - 95
6X-RAY DIFFRACTION6chain 'A' and (resid 96 through 115 )A96 - 115
7X-RAY DIFFRACTION7chain 'A' and (resid 116 through 142 )A116 - 142
8X-RAY DIFFRACTION8chain 'A' and (resid 143 through 177 )A143 - 177
9X-RAY DIFFRACTION9chain 'A' and (resid 178 through 245 )A178 - 245
10X-RAY DIFFRACTION10chain 'A' and (resid 246 through 276 )A246 - 276
11X-RAY DIFFRACTION11chain 'B' and (resid 2 through 95 )B2 - 95
12X-RAY DIFFRACTION12chain 'B' and (resid 96 through 115 )B96 - 115
13X-RAY DIFFRACTION13chain 'B' and (resid 116 through 189 )B116 - 189
14X-RAY DIFFRACTION14chain 'B' and (resid 190 through 259 )B190 - 259
15X-RAY DIFFRACTION15chain 'C' and (resid 2 through 42 )C2 - 42
16X-RAY DIFFRACTION16chain 'C' and (resid 43 through 80 )C43 - 80
17X-RAY DIFFRACTION17chain 'C' and (resid 81 through 95 )C81 - 95
18X-RAY DIFFRACTION18chain 'C' and (resid 96 through 115 )C96 - 115
19X-RAY DIFFRACTION19chain 'C' and (resid 116 through 154 )C116 - 154
20X-RAY DIFFRACTION20chain 'C' and (resid 155 through 177 )C155 - 177
21X-RAY DIFFRACTION21chain 'C' and (resid 178 through 259 )C178 - 259
22X-RAY DIFFRACTION22chain 'D' and (resid 2 through 115 )D2 - 115
23X-RAY DIFFRACTION23chain 'D' and (resid 116 through 164 )D116 - 164
24X-RAY DIFFRACTION24chain 'D' and (resid 165 through 189 )D165 - 189
25X-RAY DIFFRACTION25chain 'D' and (resid 190 through 259 )D190 - 259
26X-RAY DIFFRACTION26chain 'E' and (resid 2 through 115 )E2 - 115
27X-RAY DIFFRACTION27chain 'E' and (resid 116 through 189 )E116 - 189
28X-RAY DIFFRACTION28chain 'E' and (resid 190 through 279 )E190 - 279
29X-RAY DIFFRACTION29chain 'F' and (resid 2 through 154 )F2 - 154
30X-RAY DIFFRACTION30chain 'F' and (resid 155 through 177 )F155 - 177
31X-RAY DIFFRACTION31chain 'F' and (resid 178 through 260 )F178 - 260

+
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