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- PDB-3h0l: Structure of trna-dependent amidotransferase gatcab from aquifex ... -

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Basic information

Entry
Database: PDB / ID: 3h0l
TitleStructure of trna-dependent amidotransferase gatcab from aquifex aeolicus
Components
  • (Glutamyl-tRNA(Gln) amidotransferase subunit ...) x 2
  • Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
KeywordsLIGASE / MULTI PROTEIN COMPLEX / Protein biosynthesis
Function / homologyGlutamine synthetase/guanido kinase, catalytic domain / Glu-tRNAGln amidotransferase superfamily, subunit C / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, C-terminal / Amidase, conserved site / Asn/Gln amidotransferase / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E / Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site / Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit / Glutamyl-tRNA(Gln) amidotransferase A subunit ...Glutamine synthetase/guanido kinase, catalytic domain / Glu-tRNAGln amidotransferase superfamily, subunit C / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B, C-terminal / Amidase, conserved site / Asn/Gln amidotransferase / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, subunit B /E / Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site / Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit / Glutamyl-tRNA(Gln) amidotransferase A subunit / Glu-tRNAGln amidotransferase C subunit / Aspartyl/glutamyl-tRNA amidotransferase subunit B-like / Amidase / Amidase signature (AS) superfamily / Amidase / GatB domain / Glu-tRNAGln amidotransferase C subunit / GatB/GatE catalytic domain / Amidases signature. / Glutamyl-tRNA(Gln) amidotransferase subunit B signature. / Amidase signature domain / glutaminyl-tRNAGln biosynthesis via transamidation / glutamyl-tRNA(Gln) amidotransferase complex / glutaminyl-tRNA synthase (glutamine-hydrolysing) / Ligases, Forming carbon-nitrogen bonds, Carbon-nitrogen ligases with glutamine as amido-N-donor / glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity / mitochondrial translation / amidase activity / regulation of translational fidelity / translation / mitochondrion / ATP binding / Glutamyl-tRNA(Gln) amidotransferase subunit A / Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B / Glutamyl-tRNA(Gln) amidotransferase subunit C
Function and homology information
Specimen sourceAquifex aeolicus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / 2.3 Å resolution
AuthorsWu, J. / Bu, W. / Sheppard, K. / Kitabatake, M. / Soll, D. / Smith, J.L.
CitationJournal: J.Mol.Biol. / Year: 2009
Title: Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
Authors: Wu, J. / Bu, W. / Sheppard, K. / Kitabatake, M. / Kwon, S.T. / Soll, D. / Smith, J.L.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: Apr 9, 2009 / Release: Jul 21, 2009
RevisionDateData content typeGroupProviderType
1.0Jul 21, 2009Structure modelrepositoryInitial release
1.1Jul 13, 2011Structure modelVersion format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Glutamyl-tRNA(Gln) amidotransferase subunit A
B: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
C: Glutamyl-tRNA(Gln) amidotransferase subunit C
D: Glutamyl-tRNA(Gln) amidotransferase subunit A
E: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
F: Glutamyl-tRNA(Gln) amidotransferase subunit C
G: Glutamyl-tRNA(Gln) amidotransferase subunit A
H: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
I: Glutamyl-tRNA(Gln) amidotransferase subunit C
J: Glutamyl-tRNA(Gln) amidotransferase subunit A
K: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
L: Glutamyl-tRNA(Gln) amidotransferase subunit C
M: Glutamyl-tRNA(Gln) amidotransferase subunit A
N: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
O: Glutamyl-tRNA(Gln) amidotransferase subunit C
P: Glutamyl-tRNA(Gln) amidotransferase subunit A
Q: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
R: Glutamyl-tRNA(Gln) amidotransferase subunit C
S: Glutamyl-tRNA(Gln) amidotransferase subunit A
T: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
U: Glutamyl-tRNA(Gln) amidotransferase subunit C
V: Glutamyl-tRNA(Gln) amidotransferase subunit A
W: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
X: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)964,76456
Polyers959,57124
Non-polymers5,19232
Water0
1
A: Glutamyl-tRNA(Gln) amidotransferase subunit A
B: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
C: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11780
ΔGint (kcal/M)-79
Surface area (Å2)39390
MethodPISA
2
D: Glutamyl-tRNA(Gln) amidotransferase subunit A
E: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
F: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11830
ΔGint (kcal/M)-80
Surface area (Å2)39190
MethodPISA
3
G: Glutamyl-tRNA(Gln) amidotransferase subunit A
H: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
I: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11870
ΔGint (kcal/M)-81
Surface area (Å2)39060
MethodPISA
4
J: Glutamyl-tRNA(Gln) amidotransferase subunit A
K: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
L: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11740
ΔGint (kcal/M)-79
Surface area (Å2)39240
MethodPISA
5
M: Glutamyl-tRNA(Gln) amidotransferase subunit A
N: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
O: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11800
ΔGint (kcal/M)-79
Surface area (Å2)39230
MethodPISA
6
P: Glutamyl-tRNA(Gln) amidotransferase subunit A
Q: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
R: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11820
ΔGint (kcal/M)-76
Surface area (Å2)39110
MethodPISA
7
S: Glutamyl-tRNA(Gln) amidotransferase subunit A
T: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
U: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11830
ΔGint (kcal/M)-85
Surface area (Å2)39240
MethodPISA
8
V: Glutamyl-tRNA(Gln) amidotransferase subunit A
W: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
X: Glutamyl-tRNA(Gln) amidotransferase subunit C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,5957
Polyers119,9463
Non-polymers6494
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area (Å2)11780
ΔGint (kcal/M)-77
Surface area (Å2)39300
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)127.482, 131.012, 154.668
Angle α, β, γ (deg.)90.02, 90.00, 89.91
Int Tables number1
Space group name H-MP 1

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Components

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Glutamyl-tRNA(Gln) amidotransferase subunit ... , 2 types, 16 molecules ADGJMPSVCFILORUX

#1: Protein/peptide
Glutamyl-tRNA(Gln) amidotransferase subunit A / Glu-ADT subunit A


Mass: 53589.160 Da / Num. of mol.: 8 / Source: (gene. exp.) Aquifex aeolicus (bacteria) / Strain: VF5 / Gene: aq_247, gatA, GATCA / Plasmid name: pET17b-CA / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O66610, Ligases, Forming carbon-nitrogen bonds, Carbon-nitrogen ligases with glutamine as amido-N-donor
#3: Protein/peptide
Glutamyl-tRNA(Gln) amidotransferase subunit C / Glu-ADT subunit C


Mass: 11228.740 Da / Num. of mol.: 8 / Source: (gene. exp.) Aquifex aeolicus (bacteria) / Strain: VF5 / Gene: gatC, aq_2149 / Plasmid name: pET17b-CA / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O67904, Ligases, Forming carbon-nitrogen bonds, Carbon-nitrogen ligases with glutamine as amido-N-donor

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Protein/peptide , 1 types, 8 molecules BEHKNQTW

#2: Protein/peptide
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B / Asp/Glu-ADT subunit B


Mass: 55128.535 Da / Num. of mol.: 8 / Source: (gene. exp.) Aquifex aeolicus (bacteria) / Strain: VF5 / Gene: aq_461, gatB / Plasmid name: pET17b-B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O66766, Ligases, Forming carbon-nitrogen bonds, Carbon-nitrogen ligases with glutamine as amido-N-donor

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Non-polymers , 4 types, 32 molecules

#4: Chemical
ChemComp-ASN / ASPARAGINE


Mass: 132.118 Da / Num. of mol.: 8 / Formula: C4H8N2O3 / Asparagine
#5: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 8 / Formula: C10H15N5O10P2 / Adenosine diphosphate / Comment: ADP (energy-carrying molecule) *YM
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Formula: Mg / Magnesium
#7: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Formula: Zn / Zinc

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 3

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Sample preparation

CrystalDensity Matthews: 2.69 / Density percent sol: 54.31 %
Crystal growTemp: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 1:1 ratio of Protein solution (6-9mg/ml GatCAB,10mM HEPES, 50uM Zn acetate,10mM Asn, 0.6mM ATP) mix with well solution (10-12% PEG3350, 10mM Mg formate), pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

Diffraction
IDMean temperatureCrystal ID
11001
21001
Source
SourceSiteBeamlineIdWavelength
SYNCHROTRONAPS 23-ID-D11.0274,0.9804
SYNCHROTRONAPS 23-ID-D20.97934
Detector
TypeIdDetailsDetectorCollection date
MARMOSAIC 300 mm CCD1MONOCHROMATOR: MIRRORSCCD2006-03-24
MARMOSAIC 300 mm CCD2MONOCHROMATOR: MIRRORSCCD2007-03-20
Radiation
IdMonochromatorDiffraction protocolMonochromatic or laue m lScattering typeWavelength ID
1MIRRORSMADMx-ray1
2MIRRORSSINGLE WAVELENGTHx-ray2
Radiation wavelength
IDWavelengthRelative weight
11.02741.0
20.98041.0
30.979341.0
ReflectionD resolution high: 2.3 Å / D resolution low: 40.5 Å / Number all: 405875 / Number obs: 405875 / Observed criterion sigma F: 0 / Observed criterion sigma I: 0 / Rmerge I obs: 0.06 / Rsym value: 0.06 / NetI over sigmaI: 11.5 / Redundancy: 1.9 % / Percent possible obs: 91.5
Reflection shellRmerge I obs: 0.347 / Highest resolution: 2.3 Å / Lowest resolution: 2.35 Å / MeanI over sigI obs: 1.8 / Rsym value: 0.347 / Redundancy: 1.7 % / Percent possible all: 73.7

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
REFMAC5.2.0019refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefineMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entries 2GI3 and 2G5H
Correlation coeff Fo to Fc: 0.941 / Correlation coeff Fo to Fc free: 0.923 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS / Overall SU B: 11.215 / Overall SU ML: 0.258 / R Free selection details: RANDOM / Cross valid method: THROUGHOUT / Overall ESU R: 0.408 / Overall ESU R Free: 0.268 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Solvent computationSolvent ion probe radii: 0.8 Å / Solvent shrinkage radii: 0.8 Å / Solvent vdw probe radii: 1.4 Å / Solvent model details: BABINET MODEL WITH MASK
Displacement parametersB iso mean: 50.929 Å2 / Aniso B11: -4.63 Å2 / Aniso B12: -0.01 Å2 / Aniso B13: -0.26 Å2 / Aniso B22: 9.07 Å2 / Aniso B23: 0.04 Å2 / Aniso B33: -4.44 Å2
Least-squares processR factor R free: 0.2726 / R factor R work: 0.24004 / R factor obs: 0.24169 / Highest resolution: 2.3 Å / Lowest resolution: 40.5 Å / Number reflection R free: 20322 / Number reflection all: 405875 / Number reflection obs: 385553 / Percent reflection R free: 5 / Percent reflection obs: 91.69
Refine analyzeLuzzati coordinate error free: 0.198 Å / Luzzati coordinate error obs: 0.359 Å
Refine hist #LASTHighest resolution: 2.3 Å / Lowest resolution: 40.5 Å
Number of atoms included #LASTProtein: 62848 / Nucleic acid: 0 / Ligand: 296 / Solvent: 0 / Total: 63144
Refine LS restraints
Refine IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.02264481
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.3961.98987106
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.1495.0007808
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.07224.4962936
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.65615.00011946
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.93315.000400
X-RAY DIFFRACTIONr_chiral_restr0.0940.2009520
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02048240
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2200.20030945
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3090.20043623
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1660.2002694
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0980.20015
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2150.200122
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2060.20030
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6721.50040352
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.1102.00063456
X-RAY DIFFRACTIONr_scbond_it1.4543.00027450
X-RAY DIFFRACTIONr_scangle_it2.3054.50023650
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints ncs

Refine ID: X-RAY DIFFRACTION

Dom IDAuth asym IDEns IDNumberTypeRms dev positionWeight position
1A11904tight positional0.040.05
2D11904tight positional0.030.05
3G11904tight positional0.030.05
4J11904tight positional0.030.05
5M11904tight positional0.030.05
6P11904tight positional0.040.05
7S11904tight positional0.040.05
8V11904tight positional0.040.05
1B21164tight positional0.040.05
2E21164tight positional0.030.05
3H21164tight positional0.040.05
4K21164tight positional0.040.05
5N21164tight positional0.030.05
6Q21164tight positional0.040.05
7T21164tight positional0.030.05
8W21164tight positional0.030.05
1B3476tight positional0.020.05
2E3476tight positional0.020.05
3H3476tight positional0.030.05
4K3476tight positional0.030.05
5N3476tight positional0.020.05
6Q3476tight positional0.020.05
7T3476tight positional0.020.05
8W3476tight positional0.020.05
1C4364tight positional0.030.05
2F4364tight positional0.030.05
3I4364tight positional0.030.05
4L4364tight positional0.030.05
5O4364tight positional0.030.05
6R4364tight positional0.030.05
7U4364tight positional0.030.05
8X4364tight positional0.030.05
1A11864medium positional0.340.50
2D11864medium positional0.340.50
3G11864medium positional0.340.50
4J11864medium positional0.340.50
5M11864medium positional0.340.50
6P11864medium positional0.340.50
7S11864medium positional0.350.50
8V11864medium positional0.330.50
1B21187medium positional0.370.50
2E21187medium positional0.350.50
3H21187medium positional0.370.50
4K21187medium positional0.360.50
5N21187medium positional0.370.50
6Q21187medium positional0.380.50
7T21187medium positional0.370.50
8W21187medium positional0.350.50
1B3481medium positional0.350.50
2E3481medium positional0.360.50
3H3481medium positional0.350.50
4K3481medium positional0.370.50
5N3481medium positional0.320.50
6Q3481medium positional0.360.50
7T3481medium positional0.330.50
8W3481medium positional0.380.50
1C4400medium positional0.410.50
2F4400medium positional0.370.50
3I4400medium positional0.360.50
4L4400medium positional0.360.50
5O4400medium positional0.350.50
6R4400medium positional0.560.50
7U4400medium positional0.390.50
8X4400medium positional0.340.50
1A11904tight thermal0.090.50
2D11904tight thermal0.090.50
3G11904tight thermal0.090.50
4J11904tight thermal0.100.50
5M11904tight thermal0.090.50
6P11904tight thermal0.100.50
7S11904tight thermal0.100.50
8V11904tight thermal0.090.50
1B21164tight thermal0.070.50
2E21164tight thermal0.090.50
3H21164tight thermal0.070.50
4K21164tight thermal0.090.50
5N21164tight thermal0.070.50
6Q21164tight thermal0.090.50
7T21164tight thermal0.090.50
8W21164tight thermal0.070.50
1B3476tight thermal0.040.50
2E3476tight thermal0.050.50
3H3476tight thermal0.040.50
4K3476tight thermal0.040.50
5N3476tight thermal0.040.50
6Q3476tight thermal0.040.50
7T3476tight thermal0.050.50
8W3476tight thermal0.040.50
1C4364tight thermal0.070.50
2F4364tight thermal0.070.50
3I4364tight thermal0.060.50
4L4364tight thermal0.070.50
5O4364tight thermal0.070.50
6R4364tight thermal0.080.50
7U4364tight thermal0.070.50
8X4364tight thermal0.070.50
1A11864medium thermal0.642.00
2D11864medium thermal0.662.00
3G11864medium thermal0.612.00
4J11864medium thermal0.682.00
5M11864medium thermal0.622.00
6P11864medium thermal0.692.00
7S11864medium thermal0.622.00
8V11864medium thermal0.672.00
1B21187medium thermal0.572.00
2E21187medium thermal0.612.00
3H21187medium thermal0.552.00
4K21187medium thermal0.652.00
5N21187medium thermal0.562.00
6Q21187medium thermal0.682.00
7T21187medium thermal0.622.00
8W21187medium thermal0.592.00
1B3481medium thermal0.352.00
2E3481medium thermal0.372.00
3H3481medium thermal0.322.00
4K3481medium thermal0.352.00
5N3481medium thermal0.282.00
6Q3481medium thermal0.322.00
7T3481medium thermal0.372.00
8W3481medium thermal0.322.00
1C4400medium thermal0.512.00
2F4400medium thermal0.492.00
3I4400medium thermal0.462.00
4L4400medium thermal0.572.00
5O4400medium thermal0.482.00
6R4400medium thermal0.612.00
7U4400medium thermal0.502.00
8X4400medium thermal0.542.00
Refine LS shellHighest resolution: 2.3 Å / R factor R free: 0.384 / R factor R work: 0.337 / Lowest resolution: 2.363 Å / Number reflection R free: 1185 / Number reflection R work: 22441 / Total number of bins used: 20 / Percent reflection obs: 72.25

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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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