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- PDB-3o4z: Tel2 structure and function in the Hsp90-dependent maturation of ... -

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Basic information

Entry
Database: PDB / ID: 3o4z
TitleTel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes
ComponentsTelomere length regulation protein TEL2
KeywordsPROTEIN BINDING / HEAT like helical repeats
Function / homology
Function and homology information


positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / protein localization to chromosome / TTT Hsp90 cochaperone complex / telomeric DNA binding / telomere maintenance via telomerase / telomere maintenance / Hsp90 protein binding / chromosome, telomeric region / protein stabilization ...positive regulation of DNA damage checkpoint / 'de novo' cotranslational protein folding / protein localization to chromosome / TTT Hsp90 cochaperone complex / telomeric DNA binding / telomere maintenance via telomerase / telomere maintenance / Hsp90 protein binding / chromosome, telomeric region / protein stabilization / nucleus / cytosol
Similarity search - Function
Tel2 C-terminal domain / Telomere length regulation protein, conserved domain / TEL2, C-terminal domain superfamily / : / Telomere length regulation protein / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Mainly Alpha
Similarity search - Domain/homology
Telomere length regulation protein TEL2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.1 Å
AuthorsXie, Y. / Pavletich, N.P.
CitationJournal: Genes Dev. / Year: 2010
Title: Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes.
Authors: Takai, H. / Xie, Y. / de Lange, T. / Pavletich, N.P.
History
DepositionJul 27, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 15, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 9, 2017Group: Data collection / Refinement description / Source and taxonomy
Category: diffrn_detector / entity_src_gen / software / Item: _diffrn_detector.detector
Revision 1.3Feb 21, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Telomere length regulation protein TEL2
B: Telomere length regulation protein TEL2
C: Telomere length regulation protein TEL2
D: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)297,3844
Polymers297,3844
Non-polymers00
Water00
1
A: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)74,3461
Polymers74,3461
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)74,3461
Polymers74,3461
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)74,3461
Polymers74,3461
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)74,3461
Polymers74,3461
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
A: Telomere length regulation protein TEL2
C: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)148,6922
Polymers148,6922
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3210 Å2
ΔGint-15 kcal/mol
Surface area53270 Å2
MethodPISA
6
B: Telomere length regulation protein TEL2
D: Telomere length regulation protein TEL2


Theoretical massNumber of molelcules
Total (without water)148,6922
Polymers148,6922
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3270 Å2
ΔGint-15 kcal/mol
Surface area53160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)91.400, 123.300, 162.300
Angle α, β, γ (deg.)90.00, 95.17, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
12A
22B
32C
42D
13A
23B
33C
43D
14A
24B
34C
44D
15A
25B
35C
45D
16A
26B
36C
46D
17A
27B
37C
47D
18A
28B
38C
48D

NCS ensembles :
ID
1
2
3
4
5
6
7
8

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Components

#1: Protein
Telomere length regulation protein TEL2


Mass: 74345.922 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: TEL2, YGR099W / Cell line (production host): HI-5 INSECT CELLS / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P53038

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.06 Å3/Da / Density % sol: 59.84 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1 M Tris-HCl, 7% (w/v) polyethylene glycol (PEG) 8000, 0.8 M NaCl and 1.5% (v/v) ethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 14, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 3.1→39.2 Å / Num. obs: 60224 / Redundancy: 4.8 % / Rsym value: 0.05 / Net I/σ(I): 24.2
Reflection shellResolution: 3.1→3.21 Å / Mean I/σ(I) obs: 2.5 / Rsym value: 0.42 / % possible all: 97.6

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SHELXSphasing
REFMAC5.4.0069refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 3.1→39.2 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.935 / SU B: 41.947 / SU ML: 0.326 / Cross valid method: THROUGHOUT / ESU R Free: 0.42 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.23857 2526 4 %RANDOM
Rwork0.222 ---
obs0.22267 60224 96.23 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 105.176 Å2
Baniso -1Baniso -2Baniso -3
1--0.26 Å20 Å2-0.2 Å2
2--2.2 Å20 Å2
3----1.98 Å2
Refinement stepCycle: LAST / Resolution: 3.1→39.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18452 0 0 0 18452
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.02218784
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1861.9825324
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.57152260
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.32323.942832
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.303153544
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.49615116
X-RAY DIFFRACTIONr_chiral_restr0.080.22948
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.02113656
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5920.7511396
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.1851.518436
X-RAY DIFFRACTIONr_scbond_it1.2961.57388
X-RAY DIFFRACTIONr_scangle_it2.2732.56888
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
11A224TIGHT POSITIONAL0.010.03
12B224TIGHT POSITIONAL0.010.03
13C224TIGHT POSITIONAL0.010.03
14D224TIGHT POSITIONAL0.010.03
11A224TIGHT THERMAL1.3610
12B224TIGHT THERMAL0.9110
13C224TIGHT THERMAL1.2110
14D224TIGHT THERMAL0.910
21A400TIGHT POSITIONAL0.010.03
22B400TIGHT POSITIONAL0.010.03
23C400TIGHT POSITIONAL0.010.03
24D400TIGHT POSITIONAL0.010.03
21A400TIGHT THERMAL1.410
22B400TIGHT THERMAL1.1110
23C400TIGHT THERMAL1.0310
24D400TIGHT THERMAL1.0210
31A1026TIGHT POSITIONAL0.010.03
32B1026TIGHT POSITIONAL0.010.03
33C1026TIGHT POSITIONAL0.010.03
34D1026TIGHT POSITIONAL0.010.03
31A1026TIGHT THERMAL1.5710
32B1026TIGHT THERMAL1.3210
33C1026TIGHT THERMAL1.1510
34D1026TIGHT THERMAL1.5310
41A513TIGHT POSITIONAL0.010.03
42B513TIGHT POSITIONAL0.010.03
43C513TIGHT POSITIONAL0.010.03
44D513TIGHT POSITIONAL0.010.03
41A513TIGHT THERMAL1.810
42B513TIGHT THERMAL1.5710
43C513TIGHT THERMAL1.410
44D513TIGHT THERMAL1.8710
51A793TIGHT POSITIONAL0.020.03
52B793TIGHT POSITIONAL0.010.03
53C793TIGHT POSITIONAL0.010.03
54D793TIGHT POSITIONAL0.010.03
51A793TIGHT THERMAL2.0410
52B793TIGHT THERMAL1.9310
53C793TIGHT THERMAL1.9810
54D793TIGHT THERMAL1.9810
61A98TIGHT POSITIONAL0.010.03
62B98TIGHT POSITIONAL0.010.03
63C98TIGHT POSITIONAL0.010.03
64D98TIGHT POSITIONAL0.010.03
61A98TIGHT THERMAL2.5410
62B98TIGHT THERMAL1.9910
63C98TIGHT THERMAL1.9610
64D98TIGHT THERMAL1.210
71A687TIGHT POSITIONAL0.010.03
72B687TIGHT POSITIONAL0.010.03
73C687TIGHT POSITIONAL0.010.03
74D687TIGHT POSITIONAL0.020.03
71A687TIGHT THERMAL1.4610
72B687TIGHT THERMAL1.3210
73C687TIGHT THERMAL1.4410
74D687TIGHT THERMAL2.4810
81A872TIGHT POSITIONAL0.010.03
82B872TIGHT POSITIONAL0.010.03
83C872TIGHT POSITIONAL0.010.03
84D872TIGHT POSITIONAL0.010.03
81A872TIGHT THERMAL1.8310
82B872TIGHT THERMAL1.6810
83C872TIGHT THERMAL1.6910
84D872TIGHT THERMAL1.8810
LS refinement shellResolution: 3.1→3.18 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.386 168 -
Rwork0.335 3934 -
obs--86.03 %
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)
11.3331-0.7425-1.74596.0339-1.526211.0688-0.07280.9006-0.3181-1.2595-0.2237-0.49660.6510.54080.29650.32590.19320.1850.4196-0.1699-0.06360.67360.54317.881
26.7323-1.6293-2.32444.49991.23127.1674-0.15750.8555-0.1317-0.5819-0.10750.08740.406-0.01450.2651-0.21640.1579-0.1228-0.2529-0.0217-0.479448.65766.65436.441
31.18380.2247-1.73641.6503-1.15157.04080.00920.0798-0.0099-0.2010.00170.1785-0.0743-0.3777-0.0109-0.43540.1373-0.056-0.3129-0.0529-0.270631.03272.37967.838
45.11321.84743.80122.61652.72518.4016-0.15940.2830.4438-0.46480.08680.0548-0.4252-0.06180.0727-0.25140.0462-0.0402-0.46090.1271-0.023266.05397.00663.368
54.6774-3.18930.954.9876-0.303910.5422-0.5329-0.9240.39451.02040.40770.4325-0.6301-0.53780.12520.51830.08670.25120.6997-0.0176-0.112640.48469.895154.033
64.1879-1.5388-1.31537.06321.81696.6287-0.0545-0.5764-0.08560.5542-0.12140.40170.1658-0.45540.1758-0.067-0.13370.10510.16260.1873-0.405646.52658.759134.873
71.90190.08480.72070.7181-0.515710.02820.2258-0.314-0.41240.1629-0.2077-0.00470.535-0.0194-0.0181-0.1764-0.04880.0216-0.28410.1465-0.13152.28143.295102.508
84.38782.7611-3.00314.9172-2.88916.45540.2471-0.6418-0.03770.4481-0.1225-0.2591-0.00030.1144-0.1246-0.3314-0.0275-0.0944-0.1907-0.0147-0.161181.9672.868112.715
94.8029-0.32821.33872.14620.29266.0798-0.0946-1.8123-0.63111.8150.05390.15221.3010.74270.04061.66440.1672-0.21461.37570.2930.49874.55675.176156.984
104.3123-1.3480.52958.3768-1.01946.71180.072-1.10280.01171.4604-0.1436-0.39530.15880.63550.07170.2393-0.173-0.06030.3856-0.0869-0.13871.76487.738137.756
112.0602-0.0422-1.48821.7169-0.3427.55860.1355-0.37880.38360.2377-0.27130.1559-0.1106-0.34190.1359-0.3163-0.1593-0.0592-0.2581-0.13440.120870.487105.553105.884
124.01881.45072.68663.62842.22857.5810.2063-0.55390.28110.3871-0.3170.3129-0.004-0.12210.1106-0.3362-0.01260.1227-0.23210.0653-0.361439.67675.798110.315
131.28230.57141.77582.8143-3.125710.5353-0.00031.590.5543-1.3171-0.22720.6599-1.339-0.73850.22761.16110.2617-0.10371.16720.45510.472871.68592.88719.001
147.4885-1.73560.44834.1797-0.9436.4843-0.02141.46150.7468-0.9763-0.0063-0.0612-0.83050.09440.02780.1097-0.08880.1079-0.03560.2725-0.086981.40186.33738.783
151.16030.04760.87071.63541.64379.2411-0.06320.0818-0.0092-0.24270.0915-0.2909-0.19080.2176-0.0283-0.4198-0.04790.0116-0.41930.0332-0.013295.29479.24271.766
165.62610.9914-3.04582.8167-1.13916.4248-0.14260.2888-0.3263-0.13140.08480.07050.1504-0.1430.0577-0.47420.093-0.1149-0.4952-0.0369-0.447361.23854.77361.76
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 78
2X-RAY DIFFRACTION2A83 - 209
3X-RAY DIFFRACTION3A210 - 386
4X-RAY DIFFRACTION4A428 - 688
5X-RAY DIFFRACTION5B1 - 78
6X-RAY DIFFRACTION6B83 - 209
7X-RAY DIFFRACTION7B210 - 386
8X-RAY DIFFRACTION8B428 - 688
9X-RAY DIFFRACTION9C1 - 78
10X-RAY DIFFRACTION10C83 - 209
11X-RAY DIFFRACTION11C210 - 386
12X-RAY DIFFRACTION12C428 - 688
13X-RAY DIFFRACTION13D1 - 78
14X-RAY DIFFRACTION14D83 - 209
15X-RAY DIFFRACTION15D210 - 386
16X-RAY DIFFRACTION16D428 - 688

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