[English] 日本語
Yorodumi
- PDB-2zak: Orthorhombic crystal structure of precursor E. coli isoaspartyl p... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2zak
TitleOrthorhombic crystal structure of precursor E. coli isoaspartyl peptidase/L-asparaginase (EcAIII) with active-site T179A mutation
ComponentsL-asparaginase precursor
KeywordsHYDROLASE / isoaspartyl peptidase / asparaginase / Ntn-hydrolase / autoproteolysis / precursor
Function / homology
Function and homology information


beta-aspartyl-peptidase / asparagine catabolic process via L-aspartate / asparaginase activity / beta-aspartyl-peptidase activity / protein autoprocessing / hydrolase activity / cytoplasm
Similarity search - Function
Peptidase T2, asparaginase 2 / Asparaginase / Nucleophile aminohydrolases, N-terminal
Similarity search - Domain/homology
Isoaspartyl peptidase
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.01 Å
AuthorsMichalska, K. / Hernandez-Santoyo, A. / Jaskolski, M.
Citation
Journal: Acta Crystallogr.,Sect.D / Year: 2008
Title: Crystal packing of plant-type L-asparaginase from Escherichia coli
Authors: Michalska, K. / Borek, D. / Hernandez-Santoyo, A. / Jaskolski, M.
#1: Journal: J.Biol.Chem. / Year: 2005
Title: Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate
Authors: Michalska, K. / Brzezinski, K. / Jaskolski, M.
#2: Journal: Acta Crystallogr.,Sect.D / Year: 2000
Title: Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome
Authors: Borek, D. / Jaskolski, M.
#3: Journal: J.Mol.Biol. / Year: 2006
Title: Crystal structure of plant asparaginase
Authors: Michalska, K. / Bujacz, G. / Jaskolski, M.
#4: Journal: Nature / Year: 1995
Title: A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
Authors: Brannigan, J.A. / Dodson, G. / Duggleby, H.J. / Moody, P.C. / Smith, J.L. / Tomchick, D.R. / Murzin, A.G.
#5: Journal: Acta Crystallogr.,Sect.D / Year: 2004
Title: Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli
Authors: Prahl, A. / Pazgier, M. / Hejazi, M. / Lockau, W. / Lubkowski, J.
#6: Journal: Cell(Cambridge,Mass.) / Year: 1999
Title: Structural insights into the mechanism of intramolecular proteolysis
Authors: Xu, Q. / Buckley, D. / Guan, C. / Guo, H.-C.
#7: Journal: J.Biol.Chem. / Year: 1998
Title: Characterization and functional analysis of the cis-autoproteolysis active center of glycosylasparaginase
Authors: Guan, C. / Liu, Y. / Shao, Y. / Cui, T. / Liao, W. / Ewel, A. / Whitaker, R. / Paulus, H.
#8: Journal: J.Biol.Chem. / Year: 1998
Title: Activation and oligomerization of aspartylglucosaminidase
Authors: Saarela, J. / Laine, M. / Tikkanen, R. / Oinonen, C. / Jalanko, A. / Rouvinen, J. / Peltonen, L.
#9: Journal: Structure / Year: 2003
Title: A dual role for an aspartic acid in glycosylasparaginase autoproteolysis
Authors: Qian, X. / Guan, C. / Guo, H.-C.
History
DepositionOct 7, 2007Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 25, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Source and taxonomy / Version format compliance
Revision 1.2Nov 10, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / diffrn_source ...database_2 / diffrn_source / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Nov 1, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: L-asparaginase precursor
B: L-asparaginase precursor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,7647
Polymers66,5252
Non-polymers2395
Water2,522140
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3470 Å2
ΔGint-39 kcal/mol
Surface area20780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)51.350, 77.780, 147.930
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein L-asparaginase precursor / L-asparagine amidohydrolase


Mass: 33262.676 Da / Num. of mol.: 2 / Mutation: T179A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12
Description: The N-terminal methionine has been removed by an intracellular aminopeptidase (E. COLI).
Gene: ybiK (iaaA) / Plasmid: pET11d / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS
References: UniProt: P37595, beta-aspartyl-peptidase, asparaginase
#2: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 140 / 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: 2.22 Å3/Da / Density % sol: 44.6 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 200mM MgCl2, 100mM Tris/HCl, 15% PEG 4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X12 / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 2, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→25 Å / Num. all: 38010 / Num. obs: 38010 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 3 % / Rmerge(I) obs: 0.103 / Net I/σ(I): 9.2
Reflection shellResolution: 2→2.07 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 2.1 / % possible all: 69.1

-
Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MAR345dtbdata collection
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1K2X
Resolution: 2.01→25 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.913 / SU B: 10.862 / SU ML: 0.145 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / ESU R: 0.2 / ESU R Free: 0.184 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS. MAXIMUM LIKELIHOOD TARGET. THE REFINEMENT INCLUDED TLS PARAMETERS. THE RESIDUES 164-177 AND 314-321 FROM CHAIN A AS WELL AS 159-177 AND 314-321 ...Details: HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS. MAXIMUM LIKELIHOOD TARGET. THE REFINEMENT INCLUDED TLS PARAMETERS. THE RESIDUES 164-177 AND 314-321 FROM CHAIN A AS WELL AS 159-177 AND 314-321 FROM CHAIN B WERE NOT MODELED DUE TO POOR ELECTRON DENSITY.
RfactorNum. reflection% reflectionSelection details
Rfree0.25285 1524 4 %RANDOM
Rwork0.19741 ---
obs0.19961 36439 93.72 %-
all-36440 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 23.628 Å2
Baniso -1Baniso -2Baniso -3
1-4.84 Å20 Å20 Å2
2---2.37 Å20 Å2
3----2.47 Å2
Refinement stepCycle: LAST / Resolution: 2.01→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4286 0 12 140 4438
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0224366
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5481.9725911
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3865591
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.74324.023174
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.57915698
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.5411531
X-RAY DIFFRACTIONr_chiral_restr0.10.2682
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.023293
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2070.22269
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2980.23066
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1440.2237
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.1120.25
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2480.241
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2450.26
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6881.52906
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.09924582
X-RAY DIFFRACTIONr_scbond_it2.06331486
X-RAY DIFFRACTIONr_scangle_it3.0854.51327
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.006→2.058 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.287 97 -
Rwork0.259 1802 -
obs--64.66 %
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)
13.6662.6393-1.44565.384-0.10212.9392-0.1798-0.2664-0.06790.59930.1574-0.5882-0.30040.27070.02240.01740.0012-0.04880.00950.0096-0.059513.8587-6.307182.7353
218.52088.8145-5.41148.90542.02146.06710.1090.91050.4233-0.75680.9232-0.0121-2.7195-0.9945-1.03220.80480.0584-0.03230.27660.04860.431110.531710.064295.5701
34.88054.90282.5698.94.76349.60310.0768-0.68340.48811.3212-0.21990.46120.0702-0.73640.14310.19820.00760.05590.13370.01920.06265.5691-0.185194.6473
43.4465-5.6838-1.286724.80995.15221.0752-0.1289-0.6505-0.46891.33720.1894-0.04120.1298-0.0227-0.06050.09070.01470.0170.04140.05090.07517.7267-16.414485.9634
51.6129-0.8960.1042.26250.21491.2743-0.0194-0.0394-0.08560.07870.01560.11960.0191-0.10030.0038-0.057-0.00790.019-0.02370.00850.01852.2337-2.812575.5435
63.74240.0019-0.99383.25080.69263.6397-0.04010.1764-0.2552-0.01460.04390.35510.1378-0.1097-0.0039-0.0869-0.0182-0.0045-0.01190.0070.0945-2.9482-5.015465.5546
71.37390.3772-0.30118.61332.09831.2004-0.1807-0.16770.07670.1046-0.05080.86180.0566-0.23240.2315-0.02770.03470.00890.0860.00340.1398-6.74877.217478.2028
840.964422.7292-19.393914.331-0.214573.8580.5355-0.46750.30590.10330.3892-0.7712-1.54693.86-0.92470.1759-0.0251-0.06240.2327-0.10080.37144.637526.760681.5015
95.2684-2.79510.48811.7817-1.25733.3808-0.0440.0680.06830.2035-0.0093-0.34630.17360.07460.0533-0.1106-0.00630.0137-0.03770.00220.022911.7645-11.288676.1119
107.9984-16.96660.940436.5298-0.812.71270.06690.22990.2704-0.4251-0.1534-0.5254-0.38410.50640.08660.0405-0.0080.012-0.0031-0.03420.03472.594411.295174.5705
111.8926-1.48680.04351.5241-0.32031.2758-0.09570.0638-0.00020.09130.0456-0.1039-0.10280.10770.05-0.0475-0.0103-0.0057-0.0133-0.00130.028214.56090.868968.9361
124.3469-5.34080.16087.0194-2.389710.5098-0.05320.05260.01050.0532-0.0502-0.5415-0.06350.50540.1034-0.1153-0.0358-0.00310.0475-0.01650.172928.3646-3.618372.3457
136.06862.75381.191216.8643-5.91566.1989-0.42880.2638-0.21730.6160.3247-0.4701-0.53560.24870.10410.0075-0.0508-0.01480.0022-0.0220.113923.98638.716173.9947
140.32541.31940.54048.93371.13381.20890.0518-0.1306-0.16380.3512-0.0693-0.3784-0.1140.20670.0175-0.04640.0033-0.00410.01480.0060.088720.3477-4.056879.5055
159.18962.7229-2.53678.3658-2.987111.50820.0534-0.81720.58580.2456-0.3477-0.2213-0.6679-0.63230.2943-0.0350.0337-0.07030.0366-0.06590.042513.84252.833186.9671
161.53492.6440.646323.07229.75346.02220.3073-0.3103-0.34951.10470.0804-1.26780.0010.5262-0.38770.23320.0449-0.05670.14380.02720.068916.7232-6.316890.3694
176.68393.83741.386710.48872.56478.22550.47680.1918-0.4637-0.0562-0.124-0.7558-0.06870.3976-0.35280.1755-0.04240.05650.0762-0.0130.018620.84324.993442.4453
183.14850.61911.62436.9364-8.270611.66570.8619-1.3191-0.90390.7514-0.8687-0.06570.521-0.8850.00670.7252-0.22960.06480.48820.04360.19439.302-7.283529.7117
190.83031.79023.13759.03617.295611.9104-0.14260.2964-0.1146-1.09910.0323-0.2943-0.39740.3010.11020.4262-0.0250.06190.17810.02720.013613.51016.139631.1833
208.08711.1574-0.27674.6169-0.85632.6486-0.08180.71980.5847-0.92420.31510.0453-0.87870.2167-0.23340.3224-0.12260.05240.1040.01420.137422.371317.882643.6616
213.08550.35410.02981.66810.33930.0696-0.20.24550.0976-0.56840.0376-0.0183-0.2828-0.15960.16240.192-0.0573-0.01050.1170.025-0.00577.854910.349841.4482
221.7148-0.56250.05261.99140.4832.4503-0.01750.05040.1306-0.12030.03810.1315-0.148-0.2305-0.02060.0214-0.0052-0.01640.02920.01120.04354.69511.730255.2046
234.42973.92472.559617.45311.481711.8409-0.10770.12890.6818-0.5418-0.63221.2004-0.1689-0.86360.73990.22510.0668-0.07790.18420.07520.124-3.37915.385847.512
2413.05947.1715-1.118615.3654-6.40253.02780.20830.2937-1.0098-1.14320.30840.77341.2758-0.218-0.51670.72-0.0937-0.23790.2906-0.09240.2751-6.1276-4.182738.8656
258.7911-0.7346-0.25230.1007-0.33663.265-0.0872-0.0778-0.1332-0.44660.0272-0.2275-0.06320.13810.060.1027-0.0350.06810.0242-0.01070.012618.15068.927848.7796
265.9104-0.9031.05430.9924-1.3771.9182-0.21020.11280.1759-0.44450.20720.18760.0797-0.03890.0030.0476-0.03090.00390.0006-0.02930.00934.5356-0.810354.3795
271.7470.2307-0.01450.92940.80974.9275-0.07270.2415-0.1355-0.270.2164-0.0439-0.03010.1688-0.1436-0.03350.0060.04080.0427-0.01540.093419.41272.461554.072
2811.21280.7444-0.10392.8972-4.32412.0310.1271-0.1816-0.3847-0.27320.1052-0.1282-0.06150.0729-0.23240.01520.0401-0.0031-0.0158-0.0216-0.00514.2521-6.361457.3381
295.9315-0.3446-4.7833.10432.516610.02220.07690.002-0.1243-0.36570.0066-0.41540.07250.5278-0.0836-0.0365-0.01310.0270.0909-0.01890.105228.0922-4.07856.0422
301.37411.5718-0.5666.6012-0.61822.68190.12380.1645-0.27450.12020.0757-0.56320.1910.2567-0.19950.0834-0.00440.03280.1103-0.0440.082423.1537-4.302649.9767
313.9834-4.4222.88365.7735-1.06597.3617-0.06330.2212-0.3995-0.60460.03490.28040.36540.06540.02840.1633-0.02610.0690.1017-0.05860.011517.5783-4.441440.3914
3213.127714.85376.202822.786910.57396.49320.02180.1673-0.4535-0.38750.426-1.1956-0.05430.7219-0.44780.3796-0.07340.11170.32670.00530.084624.00742.846835.1887
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA2 - 141 - 13
2X-RAY DIFFRACTION2AA15 - 2214 - 21
3X-RAY DIFFRACTION3AA23 - 3422 - 33
4X-RAY DIFFRACTION4AA35 - 4634 - 45
5X-RAY DIFFRACTION5AA47 - 9446 - 93
6X-RAY DIFFRACTION6AA95 - 13394 - 132
7X-RAY DIFFRACTION7AA134 - 157133 - 156
8X-RAY DIFFRACTION8AA158 - 163157 - 162
9X-RAY DIFFRACTION9AA178 - 196177 - 195
10X-RAY DIFFRACTION10AA197 - 203196 - 202
11X-RAY DIFFRACTION11AA204 - 247203 - 246
12X-RAY DIFFRACTION12AA248 - 263247 - 262
13X-RAY DIFFRACTION13AA264 - 273263 - 272
14X-RAY DIFFRACTION14AA274 - 292273 - 291
15X-RAY DIFFRACTION15AA293 - 298292 - 297
16X-RAY DIFFRACTION16AA299 - 313298 - 312
17X-RAY DIFFRACTION17BB2 - 141 - 13
18X-RAY DIFFRACTION18BB15 - 2214 - 21
19X-RAY DIFFRACTION19BB23 - 3822 - 37
20X-RAY DIFFRACTION20BB39 - 5338 - 52
21X-RAY DIFFRACTION21BB54 - 7153 - 70
22X-RAY DIFFRACTION22BB72 - 13371 - 132
23X-RAY DIFFRACTION23BB134 - 146133 - 145
24X-RAY DIFFRACTION24BB147 - 158146 - 157
25X-RAY DIFFRACTION25BB178 - 200177 - 199
26X-RAY DIFFRACTION26BB201 - 217200 - 216
27X-RAY DIFFRACTION27BB218 - 234217 - 233
28X-RAY DIFFRACTION28BB235 - 241234 - 240
29X-RAY DIFFRACTION29BB242 - 262241 - 261
30X-RAY DIFFRACTION30BB263 - 287262 - 286
31X-RAY DIFFRACTION31BB288 - 298287 - 297
32X-RAY DIFFRACTION32BB299 - 313298 - 312

+
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://pdbjlvh1.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