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- PDB-7oad: conserved hypothetical protein residues 311-335 from Candidatus M... -

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Entry
Database: PDB / ID: 7oad
Titleconserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form II
ComponentsGeneral control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A,General control transcription factor GCN4
KeywordsPROTEIN FIBRIL / Coiled Coil / beta layer / hexad repeat
Function / homology
Function and homology information


protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding ...protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / amino acid biosynthetic process / cellular response to amino acid starvation / RNA polymerase II transcription regulator complex / : / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / regulation of cell cycle / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus
Similarity search - Function
Basic region leucine zipper / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. / basic region leucin zipper / Basic-leucine zipper domain superfamily / Basic-leucine zipper domain
Similarity search - Domain/homology
Secreted protein / General control transcription factor GCN4
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Candidatus Magnetomorum sp. HK-1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsAdlakha, J. / Albrecht, R. / Hartmann, M.D.
CitationJournal: To Be Published
Title: conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form II
Authors: Adlakha, J.
History
DepositionApr 19, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 4, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A,General control transcription factor GCN4
B: General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A,General control transcription factor GCN4
C: General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A,General control transcription factor GCN4


Theoretical massNumber of molelcules
Total (without water)30,1973
Polymers30,1973
Non-polymers00
Water1267
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10580 Å2
ΔGint-83 kcal/mol
Surface area14800 Å2
MethodPISA
Unit cell
Length a, b, c (Å)36.351, 38.561, 99.254
Angle α, β, γ (deg.)90.000, 98.877, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13B
23C

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: LYS / End label comp-ID: LYS / Refine code: _ / Auth seq-ID: 282 - 361 / Label seq-ID: 5 - 84

Dom-IDEns-IDAuth asym-IDLabel asym-ID
11AA
21BB
12AA
22CC
13BB
23CC

NCS ensembles :
ID
1
2
3

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Components

#1: Protein General control transcription factor GCN4,conserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A,General control transcription factor GCN4 / Amino acid biosynthesis regulatory protein / General control protein GCN4


Mass: 10065.771 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast), (gene. exp.) Candidatus Magnetomorum sp. HK-1 (bacteria)
Strain: ATCC 204508 / S288c / Gene: GCN4, AAS101, AAS3, ARG9, YEL009C, MHK_004959 / Production host: Escherichia coli (E. coli) / References: UniProt: P03069, UniProt: A0A0N0D484
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 7 / 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: 2.28 Å3/Da / Density % sol: 45.96 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop / Details: 0.1M tri-sodium citrate pH 4.5, 7.1% PEG 10000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9998 Å
DetectorType: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Jun 15, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9998 Å / Relative weight: 1
ReflectionResolution: 2→49.03 Å / Num. obs: 18659 / % possible obs: 99.7 % / Redundancy: 6.71 % / CC1/2: 1 / Rmerge(I) obs: 0.047 / Net I/σ(I): 19.67
Reflection shellResolution: 2→2.12 Å / Redundancy: 6.63 % / Rmerge(I) obs: 0.753 / Mean I/σ(I) obs: 2.44 / Num. unique obs: 2993 / CC1/2: 0.95 / % possible all: 99.7

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Processing

Software
NameVersionClassification
REFMAC5.8.0049 2013/06/30refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 7OAA
Resolution: 2→49.03 Å / Cor.coef. Fo:Fc: 0.945 / Cor.coef. Fo:Fc free: 0.926 / SU B: 18.818 / SU ML: 0.213 / Cross valid method: FREE R-VALUE / ESU R: 0.236 / ESU R Free: 0.202
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2939 933 -
Rwork0.2535 17724 -
all0.256 --
obs-18657 99.711 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL PLUS MASK
Displacement parametersBiso mean: 75.374 Å2
Baniso -1Baniso -2Baniso -3
1--2.155 Å20 Å27.131 Å2
2---0.534 Å2-0 Å2
3---0.44 Å2
Refinement stepCycle: LAST / Resolution: 2→49.03 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2007 0 0 7 2014
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0192028
X-RAY DIFFRACTIONr_bond_other_d0.0040.022103
X-RAY DIFFRACTIONr_angle_refined_deg1.3681.9672703
X-RAY DIFFRACTIONr_angle_other_deg1.07634869
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.8745237
X-RAY DIFFRACTIONr_dihedral_angle_2_deg41.04226.45293
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.47515471
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.273156
X-RAY DIFFRACTIONr_chiral_restr0.0750.2306
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.022169
X-RAY DIFFRACTIONr_gen_planes_other0.0030.02405
X-RAY DIFFRACTIONr_nbd_refined0.2330.2479
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1450.21891
X-RAY DIFFRACTIONr_nbtor_refined0.1910.2955
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0840.21166
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1120.218
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2010.222
X-RAY DIFFRACTIONr_nbd_other0.2060.271
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2190.21
X-RAY DIFFRACTIONr_mcbond_it1.7753.309957
X-RAY DIFFRACTIONr_mcbond_other1.773.308956
X-RAY DIFFRACTIONr_mcangle_it2.5364.9551191
X-RAY DIFFRACTIONr_mcangle_other2.5374.9571192
X-RAY DIFFRACTIONr_scbond_it2.913.7551071
X-RAY DIFFRACTIONr_scbond_other2.9083.7571072
X-RAY DIFFRACTIONr_scangle_it4.5135.4711512
X-RAY DIFFRACTIONr_scangle_other4.5115.4741513
X-RAY DIFFRACTIONr_lrange_it5.74526.1792344
X-RAY DIFFRACTIONr_lrange_other5.74326.0842339
X-RAY DIFFRACTIONr_ncsr_local_group_10.120.054259
X-RAY DIFFRACTIONr_ncsr_local_group_20.10.054330
X-RAY DIFFRACTIONr_ncsr_local_group_30.120.054235
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A42590.12
12B42590.12
21A43300.1
22C43300.1
31B42350.12
32C42350.12
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)WRfactor Rwork
2-2.0520.389690.401131013791000.357
2.052-2.1080.373670.3741262133199.84970.337
2.108-2.1690.362640.3361221128699.92220.312
2.169-2.2360.317630.295119212551000.262
2.236-2.3090.264610.271117412351000.235
2.309-2.390.293590.2651121118299.83080.233
2.39-2.480.34570.266106811251000.237
2.48-2.5810.294560.253107111271000.224
2.581-2.6950.231510.23898010311000.216
2.695-2.8260.373520.268970102399.90230.25
2.826-2.9780.324480.23491496499.79250.218
2.978-3.1580.286460.26587392099.89130.254
3.158-3.3750.309420.2978078491000.284
3.375-3.6440.284410.2447688091000.255
3.644-3.990.353370.23470774699.73190.252
3.99-4.4570.219330.20263867299.85120.236
4.457-5.140.295300.19156860099.66670.235
5.14-6.2780.325260.29249051799.80660.351
6.278-8.8060.227200.24638240599.25930.328
8.806-49.0330.246110.2919924585.71430.444
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)
16.8318-3.045-2.27287.75521.378510.137-0.07761.1514-0.3104-1.0189-0.4127-0.78210.00870.31710.49030.6566-0.05480.00860.55960.00840.608539.62440.1816-11.6804
27.48940.6909-4.69027.3463-0.66385.9366-0.16550.5092-0.3241-0.42350.06730.23280.0434-0.49790.09820.41-0.0143-0.1030.3031-0.03690.373429.3980.0527-0.5681
39.81283.564-7.75137.9632-0.611410.51880.15920.3971-0.19690.0298-0.05890.332-0.3019-0.4209-0.10020.39220.0087-0.04280.4053-0.0120.450119.34910.004810.1332
414.4562-2.1072-12.25750.32921.789710.39810.3380.15690.2362-0.0022-0.11380.0208-0.312-0.1747-0.22410.5052-0.04320.03220.55330.02050.59298.4973-0.02821.5028
514.3954-0.8152-8.13352.4606-0.113611.2375-0.35130.1338-0.6057-0.7226-0.1831-0.65260.1551.07510.53440.38960.0170.05110.23830.03250.4336-1.490.043931.7676
68.04372.0978-6.09092.0378-0.26178.4460.0007-0.3504-0.4122-0.3168-0.1227-0.2912-0.14290.56930.1220.25360.0332-0.18190.05790.00730.3136-11.69120.132242.4867
78.3961-0.1802-4.45775.0808-0.64425.8190.1445-0.50450.12170.2379-0.1224-0.109-0.08670.5677-0.02210.184-0.0249-0.14790.0606-0.00510.1974-21.820.34152.9649
812.4116-2.0944-5.58411.54461.869711.4537-0.042-1.34290.06081.19790.14690.6414-0.25470.1751-0.10480.3929-0.0382-0.05920.17990.00080.2703-31.14040.385163.0003
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionLabel asym-IDLabel seq-ID
1X-RAY DIFFRACTION1ALLA281 - 292
2X-RAY DIFFRACTION1ALLB281 - 292
3X-RAY DIFFRACTION1ALLC281 - 292
4X-RAY DIFFRACTION2ALLA293 - 302
5X-RAY DIFFRACTION2ALLB293 - 302
6X-RAY DIFFRACTION2ALLC293 - 302
7X-RAY DIFFRACTION3ALLA303 - 312
8X-RAY DIFFRACTION3ALLB303 - 312
9X-RAY DIFFRACTION3ALLC303 - 312
10X-RAY DIFFRACTION4ALLA313 - 322
11X-RAY DIFFRACTION4ALLB313 - 322
12X-RAY DIFFRACTION4ALLC313 - 322
13X-RAY DIFFRACTION5ALLA323 - 332
14X-RAY DIFFRACTION5ALLB323 - 332
15X-RAY DIFFRACTION5ALLC323 - 332
16X-RAY DIFFRACTION6ALLA333 - 342
17X-RAY DIFFRACTION6ALLB333 - 342
18X-RAY DIFFRACTION6ALLC333 - 342
19X-RAY DIFFRACTION7ALLA343 - 352
20X-RAY DIFFRACTION7ALLB343 - 352
21X-RAY DIFFRACTION7ALLC343 - 352
22X-RAY DIFFRACTION8ALLA353 - 363
23X-RAY DIFFRACTION8ALLB353 - 363
24X-RAY DIFFRACTION8ALLC353 - 363

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