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- PDB-3hu1: Structure of p97 N-D1 R95G mutant in complex with ATPgS -

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Basic information

Entry
Database: PDB / ID: 3hu1
TitleStructure of p97 N-D1 R95G mutant in complex with ATPgS
ComponentsTransitional endoplasmic reticulum ATPase
KeywordsTRANSPORT PROTEIN / p97 / VCP
Function / homology
Function and homology information


positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of protein K63-linked deubiquitination / protein-DNA covalent cross-linking repair / positive regulation of oxidative phosphorylation / ATPase complex / VCP-NSFL1C complex / deubiquitinase activator activity / endosome to lysosome transport via multivesicular body sorting pathway / endoplasmic reticulum stress-induced pre-emptive quality control ...positive regulation of Lys63-specific deubiquitinase activity / flavin adenine dinucleotide catabolic process / positive regulation of protein K63-linked deubiquitination / protein-DNA covalent cross-linking repair / positive regulation of oxidative phosphorylation / ATPase complex / VCP-NSFL1C complex / deubiquitinase activator activity / endosome to lysosome transport via multivesicular body sorting pathway / endoplasmic reticulum stress-induced pre-emptive quality control / cellular response to arsenite ion / Derlin-1 retrotranslocation complex / BAT3 complex binding / ERAD pathway / mitotic spindle disassembly / VCP-NPL4-UFD1 AAA ATPase complex / NADH metabolic process / aggresome assembly / vesicle-fusing ATPase / regulation of protein localization to chromatin / ER-associated misfolded protein catabolic process / K48-linked polyubiquitin modification-dependent protein binding / stress granule disassembly / positive regulation of mitochondrial membrane potential / retrograde protein transport, ER to cytosol / autophagosome maturation / regulation of aerobic respiration / MHC class I protein binding / regulation of synapse organization / positive regulation of ATP biosynthetic process / negative regulation of smoothened signaling pathway / ubiquitin-specific protease binding / ubiquitin-like protein ligase binding / RHOH GTPase cycle / ATP metabolic process / Attachment and Entry / polyubiquitin modification-dependent protein binding / proteasomal protein catabolic process / endoplasmic reticulum to Golgi vesicle-mediated transport / Protein methylation / translesion synthesis / HSF1 activation / proteasome complex / interstrand cross-link repair / endoplasmic reticulum unfolded protein response / lipid droplet / ubiquitin-dependent ERAD pathway / Josephin domain DUBs / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / macroautophagy / ADP binding / Hh mutants are degraded by ERAD / Defective CFTR causes cystic fibrosis / Hedgehog ligand biogenesis / Translesion Synthesis by POLH / ABC-family proteins mediated transport / positive regulation of protein catabolic process / positive regulation of protein-containing complex assembly / double-strand break repair / Aggrephagy / establishment of protein localization / cytoplasmic stress granule / autophagy / positive regulation of canonical Wnt signaling pathway / azurophil granule lumen / activation of cysteine-type endopeptidase activity involved in apoptotic process / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / site of double-strand break / viral genome replication / Attachment and Entry / Ovarian tumor domain proteases / E3 ubiquitin ligases ubiquitinate target proteins / proteasome-mediated ubiquitin-dependent protein catabolic process / cellular response to heat / secretory granule lumen / protein phosphatase binding / regulation of apoptotic process / protein ubiquitination / ficolin-1-rich granule lumen / lipid binding / : / glutamatergic synapse / DNA repair / intracellular membrane-bounded organelle / protein domain specific binding / cellular response to DNA damage stimulus / ubiquitin protein ligase binding / Neutrophil degranulation / endoplasmic reticulum membrane / perinuclear region of cytoplasm / endoplasmic reticulum / protein-containing complex / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / identical protein binding / nucleus / cytosol
Similarity search - Function
Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / AAA ATPase, CDC48 family / Barwin-like endoglucanases - #20 / Cell division protein 48 (CDC48), N-terminal domain / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 ...Vcp-like ATPase; Chain A, domain 2 - #10 / Vcp-like ATPase; Chain A, domain 2 / AAA ATPase, CDC48 family / Barwin-like endoglucanases - #20 / Cell division protein 48 (CDC48), N-terminal domain / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Helicase, Ruva Protein; domain 3 - #60 / Vps4 C terminal oligomerisation domain / Vps4 oligomerisation, C-terminal / Barwin-like endoglucanases / Aspartate decarboxylase-like domain superfamily / AAA+ lid domain / AAA ATPase, AAA+ lid domain / AAA-protein family signature. / ATPase, AAA-type, conserved site / Helicase, Ruva Protein; domain 3 / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleotide triphosphate hydrolases / Roll / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / Transitional endoplasmic reticulum ATPase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.81 Å
AuthorsTang, W.-K.
CitationJournal: Embo J. / Year: 2010
Title: A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants.
Authors: Tang, W.K. / Li, D. / Li, C.C. / Esser, L. / Dai, R. / Guo, L. / Xia, D.
History
DepositionJun 12, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 16, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Feb 15, 2012Group: Non-polymer description

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Transitional endoplasmic reticulum ATPase
B: Transitional endoplasmic reticulum ATPase
C: Transitional endoplasmic reticulum ATPase
D: Transitional endoplasmic reticulum ATPase
E: Transitional endoplasmic reticulum ATPase
F: Transitional endoplasmic reticulum ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)330,17218
Polymers326,8876
Non-polymers3,28512
Water2,180121
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area30640 Å2
ΔGint-178 kcal/mol
Surface area120110 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)92.756, 103.279, 107.688
Angle α, β, γ (deg.)97.66, 91.88, 89.75
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
12A
22B
32C
42D
52E
62F
13A
23B
33C
43D
53E
63F
14A
24B
34C
44D
54E
64F
15A
25B
35C
45D
55E
65F

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A12 - 189
2111B12 - 189
3111C12 - 189
4111D12 - 189
5111E12 - 189
6111F12 - 189
1121A190 - 201
2121B190 - 201
3121C190 - 201
4121D190 - 201
5121E190 - 201
6121F190 - 201
1131A202 - 371
2131B202 - 371
3131C202 - 371
4131D202 - 371
5131E202 - 371
6131F202 - 371
1141A372 - 403
2141B372 - 403
3141C372 - 403
4141D372 - 403
5141E372 - 403
6141F372 - 403
1241A405 - 462
2241B405 - 462
3241C405 - 462
4241D405 - 462
5241E405 - 462
6241F405 - 462
1151A800 - 801
2151B800 - 801
3151C800 - 801
4151D800 - 801
5151E800 - 801
6151F800 - 801

NCS ensembles :
ID
1
2
3
4
5

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Components

#1: Protein
Transitional endoplasmic reticulum ATPase / TER ATPase / 15S Mg(2+)-ATPase p97 subunit / Valosin-containing protein / VCP


Mass: 54481.172 Da / Num. of mol.: 6 / Fragment: residues 1-481 / Mutation: R95G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Strain: Human / Gene: P97, VCP / Plasmid: pQE60 / Production host: Escherichia coli (E. coli) / Strain (production host): M15 / References: UniProt: P55072
#2: Chemical
ChemComp-AGS / PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-GAMMA-S / ADENOSINE 5'-(3-THIOTRIPHOSPHATE) / ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE) / ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE


Mass: 523.247 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H16N5O12P3S / Comment: ATP-gamma-S, energy-carrying molecule analogue*YM
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 121 / Source method: isolated from a natural source / Formula: H2O

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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: 3.13 Å3/Da / Density % sol: 60.65 %
Crystal growTemperature: 288 K / Method: vapor diffusion, hanging drop / pH: 5.8
Details: 100mM NaCl, 4% benzamidine, 100mM citrate, pH 5.8, 16.5% PEG3350 and 20% glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 288K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.81→43.92 Å / Num. all: 151406 / Num. obs: 87240 / Rmerge(I) obs: 0.05 / Net I/σ(I): 12.3

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
PHASERphasing
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.81→25 Å / Cor.coef. Fo:Fc: 0.929 / Cor.coef. Fo:Fc free: 0.909 / SU B: 37.79 / SU ML: 0.351 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.408 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.27144 4323 5 %RANDOM
Rwork0.23988 ---
obs0.24141 82809 90.15 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 64.976 Å2
Baniso -1Baniso -2Baniso -3
1-1.72 Å20.74 Å21.17 Å2
2---0.23 Å2-1.27 Å2
3----1.75 Å2
Refinement stepCycle: LAST / Resolution: 2.81→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21132 0 192 121 21445
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.02221654
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5071.99729304
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.02752700
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.36824.303990
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.019153972
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.78615192
X-RAY DIFFRACTIONr_chiral_restr0.1290.23348
X-RAY DIFFRACTIONr_gen_planes_refined0.0140.0216158
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1610.28450
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.2630.214524
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1080.2515
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.1870.217
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2280.240
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3060.23
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4721.514031
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.698221852
X-RAY DIFFRACTIONr_scbond_it1.21638545
X-RAY DIFFRACTIONr_scangle_it1.7854.57452
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

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1407tight positional0.080.05
12B1407tight positional0.090.05
13C1407tight positional0.080.05
14D1407tight positional0.070.05
15E1407tight positional0.070.05
16F1407tight positional0.070.05
21A102tight positional0.060.05
22B102tight positional0.070.05
23C102tight positional0.060.05
24D102tight positional0.060.05
25E102tight positional0.060.05
26F102tight positional0.050.05
31A1318tight positional0.080.05
32B1318tight positional0.080.05
33C1318tight positional0.080.05
34D1318tight positional0.080.05
35E1318tight positional0.080.05
36F1318tight positional0.080.05
41A685tight positional0.070.05
42B685tight positional0.070.05
43C685tight positional0.080.05
44D685tight positional0.070.05
45E685tight positional0.080.05
46F685tight positional0.080.05
51A32tight positional0.080.05
52B32tight positional0.070.05
53C32tight positional0.050.05
54D32tight positional0.070.05
55E32tight positional0.070.05
56F32tight positional0.050.05
11A1407tight thermal0.140.5
12B1407tight thermal0.190.5
13C1407tight thermal0.150.5
14D1407tight thermal0.130.5
15E1407tight thermal0.130.5
16F1407tight thermal0.120.5
21A102tight thermal0.090.5
22B102tight thermal0.120.5
23C102tight thermal0.080.5
24D102tight thermal0.10.5
25E102tight thermal0.110.5
26F102tight thermal0.110.5
31A1318tight thermal0.190.5
32B1318tight thermal0.20.5
33C1318tight thermal0.20.5
34D1318tight thermal0.180.5
35E1318tight thermal0.20.5
36F1318tight thermal0.20.5
41A685tight thermal0.150.5
42B685tight thermal0.150.5
43C685tight thermal0.170.5
44D685tight thermal0.150.5
45E685tight thermal0.170.5
46F685tight thermal0.170.5
51A32tight thermal0.320.5
52B32tight thermal0.30.5
53C32tight thermal0.360.5
54D32tight thermal0.380.5
55E32tight thermal0.270.5
56F32tight thermal0.340.5
LS refinement shellResolution: 2.807→2.879 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.441 215 -
Rwork0.391 4381 -
obs--64.93 %
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)
12.3553-0.13970.10295.9091-1.237.5680.1826-0.33450.46160.3856-0.0824-0.1194-0.6006-0.3448-0.10030.01140.1220.1211-0.0050.01110.15121.694681.01530.9596
29.54220.05670.253710.17293.315314.9974-0.30470.46060.3229-0.23910.13760.0282-0.63110.5820.167-0.20140.13280.1624-0.12330.19020.16111.798682.4567-19.481
35.0113-10.883422.671123.6365-49.2368102.564-0.5443-0.7276-0.95790.3411.601-0.62551.9348-2.8817-1.05670.37530.09460.01850.23610.21770.52626.351464.3602-16.2402
43.97470.27930.13783.72530.67184.11610.01050.05260.03880.22380.0453-0.25080.04750.231-0.0558-0.20110.0492-0.0081-0.23970.0399-0.203819.594750.32873.2704
54.9107-0.39042.20463.99831.271811.765-0.0002-0.03260.1733-0.3962-0.03210.4228-0.2558-0.99560.0323-0.21680.04640.02040.1562-0.01660.0911-11.592350.1372-13.0964
63.0798-1.0619-3.33154.088-1.66488.1250.08130.17970.06760.11320.05140.7512-0.3168-1.1682-0.1327-0.29550.003-0.12780.22640.01910.0219-10.37749.4502-52.7088
79.0481-4.0592-1.474912.77492.26017.38450.2202-0.0079-0.0646-0.8429-0.0536-0.5376-0.21030.1296-0.1667-0.3267-0.0826-0.0597-0.01010.037-0.25879.779549.0866-63.3744
820.0382-1.8589-35.24781.64685.411265.112-2.21940.1335-1.10280.8095-0.3634-0.15912.49-0.86062.58290.38870.0449-0.08440.25660.11330.07628.775534.386-50.6342
94.1213-0.34380.21034.53770.4272.8783-0.1797-0.18910.15360.35920.2599-0.1077-0.2041-0.1067-0.0802-0.18730.0351-0.0053-0.15340.0453-0.2768.500540.2162-23.7555
104.4882-2.5125-1.66475.75223.39355.88450.19890.6295-0.3258-0.1466-0.47230.36610.4433-0.65680.2734-0.0952-0.1122-0.10060.0905-0.0330.1534-2.64414.4689-45.017
118.5225-1.03530.16842.81810.62457.05380.3210.4727-0.1289-0.5213-0.09130.1734-0.4034-0.6292-0.22970.227-0.0930.0408-0.1899-0.0369-0.031324.8443-1.7526-68.3275
125.81060.39793.05128.7438-0.758911.3964-0.05880.39530.05510.169-0.0371-0.7035-0.33891.03330.09590.2054-0.32380.1934-0.0833-0.13650.16746.30595.8723-66.5633
1373.5237-20.6527-14.34425.80134.02932.7985-0.63310.0553-4.28350.43530.23520.114-1.5753-0.56670.39790.5068-0.02130.16840.3822-0.04750.454640.1628-0.3725-49.1468
143.1259-0.04980.63784.9172-0.43954.3214-0.140.00130.2131-0.02580.0843-0.0293-0.3299-0.26090.0558-0.22220.02950.0108-0.2267-0.0046-0.222520.933815.4108-37.3322
1511.0613-2.31780.59745.1114-0.51034.2644-0.10990.2582-0.9220.16210.0841-0.07410.54180.53370.02580.0221-0.0605-0.0141-0.1691-0.0419-0.056932.6647-17.7373-35.8083
1610.1250.31560.97233.46271.52585.40250.2631.0998-1.0218-0.2157-0.1327-0.36180.5530.4027-0.13030.12120.2364-0.03570.10950.00770.297271.2247-22.3686-28.925
178.3821-0.9530.814610.80254.07178.2337-0.19321.34191.0692-0.35060.1135-1.1104-1.24381.57820.07970.2823-0.13490.05390.44910.41310.725384.272-3.8387-26.2952
1827.653812.425814.98815.58346.73478.12341.0291-0.52870.70161.0272-0.61680.0148-0.896-1.8278-0.41230.2720.13760.02710.64730.06050.646169.4652-3.4032-13.5461
192.47110.2046-0.21583.2185-0.37795.1739-0.03880.2657-0.0194-0.178-0.07870.1078-0.1202-0.09340.1175-0.24090.0659-0.0533-0.1768-0.0387-0.097744.36550.4429-23.6456
208.10220.75283.32493.61661.27976.63510.1882-0.5848-0.16130.3824-0.0437-0.25070.59340.2897-0.14450.13170.1006-0.0196-0.1660.10770.021359.5082-13.78984.6356
216.3621.9411.55385.4721.94751.9951-0.14520.2918-0.9520.5210.4234-1.06050.43990.634-0.27820.08390.1056-0.23080.3083-0.08870.153283.26479.587226.3034
227.7104-1.91110.502212.13312.507710.4314-0.1020.68730.4343-0.39530.3339-0.9472-1.20340.7233-0.2320.2474-0.3739-0.15490.36810.0891-0.021786.948731.244820.1092
2311.342623.80288.396450.05717.75426.3852-1.12761.55441.6659-0.67341.3812.9565-1.360.8724-0.25340.33-0.2658-0.1060.47430.06850.282367.836827.852721.5638
243.5899-0.6112-0.73393.73040.17865.06570.20860.4227-0.2714-0.3456-0.1441-0.04920.07290.0976-0.0645-0.29670.024-0.045-0.2304-0.0086-0.185955.584510.64063.366
254.0893-1.1265-1.088312.01113.18614.8732-0.1657-0.54870.50980.58780.0598-0.2491-0.08310.16050.1059-0.17170.028-0.0821-0.0730.0644-0.169750.621422.166636.2659
261.33020.09560.79746.6574-1.00813.86030.0594-0.42560.08980.79290.3406-1.0399-0.40490.5523-0.40.133-0.0306-0.06770.1055-0.25930.232848.324761.22541.4381
279.8449-4.10190.8466.0015-2.170811.0390.20040.43531.1155-0.6607-0.0834-1.0986-1.01780.4406-0.1170.648-0.27680.47330.0575-0.14450.469650.563275.217523.5343
280.44932.8962-1.753418.6678-11.30196.84240.15810.6299-0.1408-3.03691.38-0.49030.1714-1.2036-1.53810.6967-0.14250.07790.2365-0.00750.406136.381162.157320.0722
295.1429-0.2562-0.15272.8386-0.11433.60040.14750.1506-0.073-0.1615-0.0474-0.37040.13970.2303-0.1001-0.2634-0.0074-0.0247-0.3101-0.0187-0.156243.154235.578716.8951
305.3107-3.18840.26299.2259-0.51354.8848-0.19230.02750.29180.12120.22150.2017-0.5857-0.2955-0.0292-0.1706-0.01440.0313-0.1113-0.0172-0.192415.338854.317927.2446
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A14 - 107
2X-RAY DIFFRACTION2A108 - 189
3X-RAY DIFFRACTION3A190 - 201
4X-RAY DIFFRACTION4A202 - 371
5X-RAY DIFFRACTION5A372 - 462
6X-RAY DIFFRACTION6B14 - 107
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