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- PDB-3no0: Aquifex aeolicus type IIA topoisomerase C-terminal domain -

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Basic information

Entry
Database: PDB / ID: 3no0
TitleAquifex aeolicus type IIA topoisomerase C-terminal domain
ComponentsDNA gyrase subunit A
KeywordsISOMERASE / DNA topology / topoisomerase / Aquifex aeolicus / C-terminal domain / gyrase / DNA binding protein
Function / homology
Function and homology information


DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / DNA topological change / DNA binding / ATP binding / cytoplasm
Similarity search - Function
DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA topoisomerase, type IIA-like domain superfamily ...DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA topoisomerase, type IIA-like domain superfamily / 6 Propeller / Neuraminidase / Mainly Beta
Similarity search - Domain/homology
NITRATE ION / Type 2 topoisomerase subunit A
Similarity search - Component
Biological speciesAquifex aeolicus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 1.3004 Å
AuthorsTretter, E.M. / Lerman, J.C. / Berger, J.M.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2010
Title: A naturally chimeric type IIA topoisomerase in Aquifex aeolicus highlights an evolutionary path for the emergence of functional paralogs.
Authors: Tretter, E.M. / Lerman, J.C. / Berger, J.M.
History
DepositionJun 24, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 1, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 27, 2023Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA gyrase subunit A
B: DNA gyrase subunit A
C: DNA gyrase subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,18516
Polymers92,1083
Non-polymers1,07713
Water17,078948
1
A: DNA gyrase subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,9494
Polymers30,7031
Non-polymers2463
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: DNA gyrase subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,0115
Polymers30,7031
Non-polymers3084
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: DNA gyrase subunit A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,2257
Polymers30,7031
Non-polymers5226
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)43.513, 49.624, 120.350
Angle α, β, γ (deg.)91.57, 99.75, 113.48
Int Tables number1
Space group name H-MP1

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Components

#1: Protein DNA gyrase subunit A


Mass: 30702.777 Da / Num. of mol.: 3 / Fragment: UNP Residues 494-732
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Aquifex aeolicus (bacteria) / Strain: VF5 / Gene: aq_980, gyrA, ParC / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O67108, EC: 5.99.1.3
#2: Chemical
ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: NO3
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 948 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE UNP SEQUENCE FOR THIS ENTRY TERMINATES PREMATURELY DUE TO A SEQUENCE FRAME SHIFT. THE CORRECT C- ...THE UNP SEQUENCE FOR THIS ENTRY TERMINATES PREMATURELY DUE TO A SEQUENCE FRAME SHIFT. THE CORRECT C-TERMINUS SEQUENCE CONTINUES WITH DKINQKDIPLSTKKSIPRTRWKLEDDEIIKVVIKKSE

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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

Crystal
IDDensity Matthews3/Da)Density % sol (%)
12.5451.5
2
3
4
Crystal grow
Temperature (K)Crystal-IDMethodpHDetails
2911vapor diffusion, hanging drop7.550 mM NaCL, 10mM Tris-HCl pH 7.5, 225 mM NH4NO3, 20% PEG 3500, VAPOR DIFFUSION, HANGING DROP, temperature 291K
2912vapor diffusion, hanging drop7.550 mM NaCL, 10mM Tris-HCl pH 7.5, 50mM NaNO3, 20% PEG 3500, 10mM K2Pt(CN4), VAPOR DIFFUSION, HANGING DROP, temperature 291K
2913vapor diffusion, hanging drop7.550 mM NaCL, 10mM Tris-HCl pH 7.5, 50mM NaNO3, 20% PEG 3500, 10 mM K2PtCl4, VAPOR DIFFUSION, HANGING DROP, temperature 291K
2914vapor diffusion, hanging drop7.550 mM NaCL, 10mM Tris-HCl pH 7.5, 50mM NaNO3, 20% PEG 3500, 10 mM NaWO4, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
31001
41001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONALS 8.3.111.1
SYNCHROTRONALS 8.3.121.071
SYNCHROTRONALS 8.3.131.071
SYNCHROTRONALS 8.3.141.214
Detector
TypeIDDetectorDate
ADSC QUANTUM 315r1CCDApr 20, 2007
ADSC QUANTUM 315r2CCDMay 9, 2007
ADSC QUANTUM 315r3CCDMay 9, 2007
ADSC QUANTUM 315r4CCDMay 9, 2007
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1Double flat crystal, Si(111)SINGLE WAVELENGTHMx-ray1
2Double flat crystal, Si(111)SINGLE WAVELENGTHMx-ray1
3Double flat crystal, Si(111)SINGLE WAVELENGTHMx-ray1
4Double flat crystal, Si(111)SINGLE WAVELENGTHMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
11.11
21.0711
31.2141
ReflectionResolution: 1.3→40.851 Å / Num. all: 222500 / Num. obs: 208073 / % possible obs: 93.6 % / Observed criterion σ(I): -3 / Redundancy: 3.4 % / Biso Wilson estimate: 15.36 Å2 / Rmerge(I) obs: 0.031 / Net I/σ(I): 28.2
Reflection shellResolution: 1.3→1.315 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.357 / Mean I/σ(I) obs: 2.4 / Num. unique all: 18736 / % possible all: 84.8

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Processing

Software
NameVersionClassification
HKL-2000data collection
SOLVEphasing
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
SCALAdata scaling
RefinementMethod to determine structure: MIRAS / Resolution: 1.3004→40.851 Å / SU ML: 0.2 / Phase error: 18.05 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1894 10451 5.02 %random, 5%
Rwork0.1725 ---
obs0.1734 208073 93.51 %-
all-222500 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 36.454 Å2 / ksol: 0.354 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.4513 Å21.3291 Å20.0436 Å2
2--1.8789 Å2-1.5534 Å2
3----1.4276 Å2
Refinement stepCycle: LAST / Resolution: 1.3004→40.851 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6489 0 70 948 7507
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0147249
X-RAY DIFFRACTIONf_angle_d1.5019882
X-RAY DIFFRACTIONf_dihedral_angle_d15.4152952
X-RAY DIFFRACTIONf_chiral_restr0.0891166
X-RAY DIFFRACTIONf_plane_restr0.0081248
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.3004-1.31520.24832830.23665320X-RAY DIFFRACTION75
1.3152-1.33060.25733500.22436099X-RAY DIFFRACTION88
1.3306-1.34690.21813210.20646362X-RAY DIFFRACTION90
1.3469-1.36390.2023340.20796341X-RAY DIFFRACTION91
1.3639-1.38190.22873320.20946454X-RAY DIFFRACTION91
1.3819-1.40080.24913480.1996446X-RAY DIFFRACTION91
1.4008-1.42080.20543370.19116442X-RAY DIFFRACTION92
1.4208-1.4420.21873340.1846475X-RAY DIFFRACTION92
1.442-1.46450.19293610.17486505X-RAY DIFFRACTION92
1.4645-1.48860.18183430.16566439X-RAY DIFFRACTION92
1.4886-1.51420.19723430.17146597X-RAY DIFFRACTION93
1.5142-1.54180.19283520.17116506X-RAY DIFFRACTION93
1.5418-1.57140.18763590.16066560X-RAY DIFFRACTION93
1.5714-1.60350.18993350.16726719X-RAY DIFFRACTION94
1.6035-1.63840.213390.16626482X-RAY DIFFRACTION94
1.6384-1.67650.18533640.16376630X-RAY DIFFRACTION94
1.6765-1.71840.18253930.15896653X-RAY DIFFRACTION94
1.7184-1.76490.16453520.16196684X-RAY DIFFRACTION95
1.7649-1.81680.17413270.15976714X-RAY DIFFRACTION95
1.8168-1.87540.1783200.15996698X-RAY DIFFRACTION95
1.8754-1.94250.17883690.15746690X-RAY DIFFRACTION96
1.9425-2.02020.17373360.15436781X-RAY DIFFRACTION96
2.0202-2.11220.17173740.1546783X-RAY DIFFRACTION96
2.1122-2.22350.1723870.15746786X-RAY DIFFRACTION97
2.2235-2.36280.19023520.1646831X-RAY DIFFRACTION97
2.3628-2.54520.18723280.16856893X-RAY DIFFRACTION97
2.5452-2.80130.17323530.17876880X-RAY DIFFRACTION98
2.8013-3.20650.18123650.16866929X-RAY DIFFRACTION98
3.2065-4.03930.15994220.14986898X-RAY DIFFRACTION99
4.0393-40.87090.1723380.15147025X-RAY DIFFRACTION99
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)
10.4388-0.1086-0.33050.2688-0.27381.3146-0.1089-0.0997-0.03960.0310.0480.03330.2925-0.03630.05990.17330.01040.01760.11690.00810.116844.1286-9.491987.4761
20.74380.0886-0.15890.87270.86522.1316-0.06030.0431-0.25370.1839-0.06450.07380.5177-0.19050.14760.1999-0.03750.03860.0983-0.00440.174243.2853-14.383576.6594
31.42330.0365-0.20370.87980.7672.0282-0.0250.2282-0.1835-0.0150.02-0.08420.13760.071-0.00530.11330.00510.01060.1256-0.03710.12149.2228-10.52664.9726
40.70770.0222-0.3291.23920.30410.55290.02630.28460.0406-0.34980.0097-0.0565-0.18660.0071-0.04470.1669-0.00690.01990.15730.00160.10150.79070.94461.0998
51.49180.6695-1.94444.01960.02252.7819-0.3723-0.2205-0.3359-0.08840.1976-1.0287-0.08051.75170.13660.1327-0.06080.08450.4327-0.05030.344665.45932.752265.5712
60.6217-0.21080.03081.19080.32271.0211-0.00660.05830.1352-0.13870.0475-0.1476-0.37160.0317-0.01950.1873-0.01660.01450.10180.03070.133250.703410.878469.8063
70.49480.0278-0.33790.56650.52071.4360.0294-0.0420.09540.04280.0433-0.0873-0.3489-0.0015-0.06360.18070.00750.00060.08240.02030.140847.164511.83780.9066
80.21140.4464-0.4081.0341-0.32141.520.01060.0046-0.0110.08390.0095-0.1624-0.15350.19570.00230.14120.0012-0.03050.11530.01190.143348.34476.519383.0549
90.5926-0.1726-0.57480.40490.87121.69430.1274-0.07860.05510.01750.0871-0.0682-0.13370.1031-0.14960.1367-0.01590.01580.1771-0.03890.118238.07929.040647.4184
100.6479-0.0778-0.47891.61680.98320.81020.0573-0.08870.00550.0183-0.14370.0441-0.042-0.19940.09260.1128-0.0001-0.00390.2238-0.02470.096929.71421.482644.9508
110.60530.3825-0.05630.79310.61331.21710.0550.0059-0.16420.0401-0.12380.04070.0781-0.23780.05930.0753-0.0321-0.01750.1486-0.00880.107530.77849.861737.9678
121.24130.1208-0.25950.30220.35251.3490.01020.3016-0.2338-0.0513-0.07530.01850.0872-0.08550.04550.1192-0.0022-0.02560.1862-0.06610.162736.42187.796227.2699
135.4141.44132.19190.53211.10253.25250.26380.2453-1.06480.52860.0028-0.35480.56210.452-0.35330.2690.0917-0.08790.1981-0.02470.327749.35260.946233.6705
140.88620.0885-0.61840.46630.2441.28620.05720.2342-0.0504-0.08380.0419-0.0861-0.11190.1161-0.10020.10850.0079-0.00510.2232-0.03870.103846.798115.534724.2835
150.7628-0.0636-0.57070.42240.47281.47440.1278-0.08570.1475-0.06570.154-0.1962-0.16670.3165-0.20640.1349-0.04760.05050.2048-0.03870.134150.70726.106128.5689
161.6455-0.4508-1.32370.73780.83861.3980.196-0.08450.0057-0.11440.0314-0.0981-0.10770.2135-0.20640.1124-0.03280.0190.187-0.03230.131949.573325.094335.1295
170.8869-0.3263-0.64620.5896-0.13881.53960.09460.1087-0.0333-0.0225-0.00570.021-0.0955-0.1206-0.07990.1040.001700.08220.01090.101557.357714.8657-21.6275
181.6899-0.3281-0.91630.3693-0.20692.11350.07240.17740.0772-0.04660.00350.0381-0.1278-0.257-0.06660.08170.0121-0.0180.07110.02940.102248.713916.1983-13.3325
190.768-0.2169-0.17280.3437-0.32331.0325-0.0008-0.12120.03590.03350.01310.0678-0.0392-0.0687-0.01770.0879-0.00510.00760.0763-0.00080.117849.412615.1478-0.0982
200.6206-0.46780.24580.6024-0.25060.6491-0.0691-0.1909-0.05020.05620.07270.05910.0019-0.0456-0.01080.0996-0.00690.01210.11050.01930.102955.65086.51516.3895
217.43444.5941.30914.28072.06751.39070.1441-0.77640.25260.2166-0.0288-0.1741-0.260.4569-0.09970.1492-0.0269-0.02820.2183-0.05980.156768.169514.90969.7294
220.7475-0.37-0.03630.3308-0.25080.4557-0.0358-0.0739-0.0748-0.045-0.00020.00260.09680.07760.03670.0628-0.00460.00380.04820.03020.079165.9150.25020.5001
230.6711-0.53620.52631.3153-0.63260.86560.05080.0834-0.0075-0.1501-0.08450.01470.17580.14470.01870.10080.01640.02080.06310.02830.086370.047-0.7052-10.823
241.3626-1.29710.92281.4242-1.17541.51550.04310.09440.0529-0.0578-0.1291-0.01570.12750.15070.07390.07410.00240.00860.06030.02060.083467.8274.9396-12.7029
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1CHAIN A AND RESSEQ 494:523A494 - 523
2X-RAY DIFFRACTION2CHAIN A AND RESSEQ 524:574A524 - 574
3X-RAY DIFFRACTION3CHAIN A AND RESSEQ 575:617A575 - 617
4X-RAY DIFFRACTION4CHAIN A AND RESSEQ 618:653A618 - 653
5X-RAY DIFFRACTION5CHAIN A AND RESSEQ 654:660A654 - 660
6X-RAY DIFFRACTION6CHAIN A AND RESSEQ 661:718A661 - 718
7X-RAY DIFFRACTION7CHAIN A AND RESSEQ 719:750A719 - 750
8X-RAY DIFFRACTION8CHAIN A AND RESSEQ 751:769A751 - 769
9X-RAY DIFFRACTION9CHAIN B AND RESSEQ 492:523B492 - 523
10X-RAY DIFFRACTION10CHAIN B AND RESSEQ 524:574B524 - 574
11X-RAY DIFFRACTION11CHAIN B AND RESSEQ 575:617B575 - 617
12X-RAY DIFFRACTION12CHAIN B AND RESSEQ 618:653B618 - 653
13X-RAY DIFFRACTION13CHAIN B AND RESSEQ 654:660B654 - 660
14X-RAY DIFFRACTION14CHAIN B AND RESSEQ 661:718B661 - 718
15X-RAY DIFFRACTION15CHAIN B AND RESSEQ 719:750B719 - 750
16X-RAY DIFFRACTION16CHAIN B AND RESSEQ 751:769B751 - 769
17X-RAY DIFFRACTION17CHAIN C AND RESSEQ 494:523C494 - 523
18X-RAY DIFFRACTION18CHAIN C AND RESSEQ 524:574C524 - 574
19X-RAY DIFFRACTION19CHAIN C AND RESSEQ 575:617C575 - 617
20X-RAY DIFFRACTION20CHAIN C AND RESSEQ 618:653C618 - 653
21X-RAY DIFFRACTION21CHAIN C AND RESSEQ 654:660C654 - 660
22X-RAY DIFFRACTION22CHAIN C AND RESSEQ 661:718C661 - 718
23X-RAY DIFFRACTION23CHAIN C AND RESSEQ 719:750C719 - 750
24X-RAY DIFFRACTION24CHAIN C AND RESSEQ 751:769C751 - 769

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