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

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Entry
Database: PDB / ID: 7oac
Titleconserved hypothetical protein residues 311-335 from Candidatus Magnetomorum sp. HK-1 fused to GCN4 adaptors, mutant beta1/A, crystal form I
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: 2.15 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 I
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 area10680 Å2
ΔGint-90 kcal/mol
Surface area15380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)36.811, 37.365, 90.232
Angle α, β, γ (deg.)90.000, 98.981, 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 - 362 / Label seq-ID: 5 - 85

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: 2.03 Å3/Da / Density % sol: 39.4 %
Crystal growTemperature: 294 K / Method: vapor diffusion, sitting drop
Details: 0.1M tri-sodium citrate pH 4.5, 7.1 % (w/v) 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: 2.15→34.46 Å / Num. obs: 13455 / % possible obs: 99.7 % / Redundancy: 6.61 % / CC1/2: 1 / Rmerge(I) obs: 0.072 / Net I/σ(I): 13.37
Reflection shellResolution: 2.15→2.28 Å / Redundancy: 6.78 % / Rmerge(I) obs: 1.128 / Mean I/σ(I) obs: 1.61 / Num. unique obs: 2156 / CC1/2: 0.7 / % possible all: 99.9

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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: 2.15→34.459 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.946 / SU B: 24.489 / SU ML: 0.261 / Cross valid method: FREE R-VALUE / ESU R: 0.344 / ESU R Free: 0.225
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2576 673 -
Rwork0.2366 12781 -
all0.238 --
obs-13454 99.755 %
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: 60.836 Å2
Baniso -1Baniso -2Baniso -3
1--2.614 Å2-0 Å2-4.382 Å2
2---0.931 Å2-0 Å2
3---4.696 Å2
Refinement stepCycle: LAST / Resolution: 2.15→34.459 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2034 0 0 7 2041
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0192055
X-RAY DIFFRACTIONr_bond_other_d0.0060.022142
X-RAY DIFFRACTIONr_angle_refined_deg1.4171.9692736
X-RAY DIFFRACTIONr_angle_other_deg1.19634962
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.7115240
X-RAY DIFFRACTIONr_dihedral_angle_2_deg43.78626.45293
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.42315483
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.097156
X-RAY DIFFRACTIONr_chiral_restr0.0750.2309
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.022190
X-RAY DIFFRACTIONr_gen_planes_other0.0040.02408
X-RAY DIFFRACTIONr_nbd_refined0.2320.2411
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1640.21714
X-RAY DIFFRACTIONr_nbtor_refined0.1860.2927
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0710.21124
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2050.217
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1550.221
X-RAY DIFFRACTIONr_nbd_other0.2920.290
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.2970.24
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0170.21
X-RAY DIFFRACTIONr_mcbond_it3.8764.369969
X-RAY DIFFRACTIONr_mcbond_other3.8774.366968
X-RAY DIFFRACTIONr_mcangle_it5.326.541206
X-RAY DIFFRACTIONr_mcangle_other5.3186.5431207
X-RAY DIFFRACTIONr_scbond_it5.4695.281086
X-RAY DIFFRACTIONr_scbond_other5.4675.2831087
X-RAY DIFFRACTIONr_scangle_it8.6547.5651530
X-RAY DIFFRACTIONr_scangle_other8.6517.5681531
X-RAY DIFFRACTIONr_lrange_it10.44234.4612283
X-RAY DIFFRACTIONr_lrange_other10.4334.4312278
X-RAY DIFFRACTIONr_ncsr_local_group_10.120.054253
X-RAY DIFFRACTIONr_ncsr_local_group_20.1070.054276
X-RAY DIFFRACTIONr_ncsr_local_group_30.1260.054224
Refine LS restraints NCS

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

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A42530.12
12B42530.12
21A42760.11
22C42760.11
31B42240.13
32C42240.13
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
2.15-2.2050.364490.42192898099.69390.398
2.205-2.2660.442480.4069219691000.372
2.266-2.3310.358470.3548849311000.316
2.331-2.4020.373440.3228378811000.276
2.402-2.4810.232450.3438689131000.297
2.481-2.5670.238420.297828241000.254
2.567-2.6640.336420.26180584899.88210.234
2.664-2.7720.313390.257347731000.223
2.772-2.8940.242380.2417317691000.222
2.894-3.0340.342360.2516867221000.234
3.034-3.1970.29350.2596596941000.247
3.197-3.3890.318330.2566246571000.246
3.389-3.6210.292310.2195966271000.221
3.621-3.9070.268290.20254157399.47640.206
3.907-4.2750.177260.185065321000.2
4.275-4.770.121250.16547249899.79920.198
4.77-5.490.33220.21540843399.30720.255
5.49-6.6820.271180.2763543721000.312
6.682-9.2770.167150.1972903051000.268
9.277-34.4590.31890.2415518290.10990.324
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)
12.77690.40881.26933.6626-0.13013.34130.19610.20920.1421-0.2157-0.03410.30720.2658-0.0308-0.1620.07230.02250.00350.14560.03540.064-42.0538-0.0372-11.7293
24.5866-0.28473.12690.9127-0.37462.16960.1208-0.0304-0.03920.0133-0.0894-0.01530.0789-0.0174-0.03140.12730.01980.06280.1380.00370.035-31.606-0.0244-2.2678
33.9759-0.25672.53420.2295-0.48092.1486-0.0431-0.12130.2045-0.0915-0.0503-0.02080.1293-0.03620.09330.1206-0.00470.03410.06050.01080.0672-20.3932-0.03037.0162
44.8161-0.71452.1430.4857-1.08662.5414-0.056-0.03810.17210.0123-0.0144-0.0227-0.0464-0.0340.07040.1272-0.01120.02930.087-0.02040.0369-9.0078-0.07815.9489
54.57370.45383.67650.05560.4153.295-0.01980.04220.18760.022-0.06730.01310.2185-0.16560.08710.1727-0.0826-0.00130.16620.02640.04423.08270.2926.2464
63.41320.74513.30130.28450.82583.33050.1127-0.06310.11370.0108-0.0984-0.06180.152-0.0742-0.01430.10020.00550.03550.0836-0.00110.103613.08510.467535.6734
73.34180.25122.89260.08540.18692.51830.276-0.0748-0.10350.0661-0.13530.03420.2379-0.0208-0.14070.1753-0.03530.05240.1642-0.050.041623.45540.316246.0653
81.9124-1.91580.66211.9569-0.55253.1768-0.00410.05530.00190.0876-0.06810.0047-0.01470.14870.07210.1767-0.06340.00990.08750.01270.00735.17490.032758.1347
Refinement TLS group
IDRefine-IDRefine TLS-IDSelectionLabel asym-IDLabel seq-ID
1X-RAY DIFFRACTION1ALLA281 - 290
2X-RAY DIFFRACTION1ALLB281 - 290
3X-RAY DIFFRACTION1ALLC281 - 290
4X-RAY DIFFRACTION2ALLA291 - 300
5X-RAY DIFFRACTION2ALLB291 - 300
6X-RAY DIFFRACTION2ALLC291 - 300
7X-RAY DIFFRACTION3ALLA301 - 310
8X-RAY DIFFRACTION3ALLB301 - 310
9X-RAY DIFFRACTION3ALLC301 - 310
10X-RAY DIFFRACTION4ALLA311 - 320
11X-RAY DIFFRACTION4ALLB311 - 320
12X-RAY DIFFRACTION4ALLC311 - 320
13X-RAY DIFFRACTION5ALLA321 - 330
14X-RAY DIFFRACTION5ALLB321 - 330
15X-RAY DIFFRACTION5ALLC321 - 330
16X-RAY DIFFRACTION6ALLA331 - 340
17X-RAY DIFFRACTION6ALLB331 - 340
18X-RAY DIFFRACTION6ALLC331 - 340
19X-RAY DIFFRACTION7ALLA341 - 350
20X-RAY DIFFRACTION7ALLB341 - 350
21X-RAY DIFFRACTION7ALLC341 - 350
22X-RAY DIFFRACTION8ALLA351 - 363
23X-RAY DIFFRACTION8ALLB351 - 363
24X-RAY DIFFRACTION8ALLC351 - 363

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