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- PDB-3snk: Crystal structure of a Response regulator CheY-like protein (mll6... -

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Basic information

Entry
Database: PDB / ID: 3snk
TitleCrystal structure of a Response regulator CheY-like protein (mll6475) from MESORHIZOBIUM LOTI at 2.02 A resolution
ComponentsResponse regulator CheY-like protein
KeywordsSIGNALING PROTEIN / P-loop containing nucleoside triphosphate hydrolases / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
Function / homologyAAA domain / AAA domain / CheY-like superfamily / Response regulator / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Alpha Beta / Pilus assembly protein
Function and homology information
Biological speciesMesorhizobium loti (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.02 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of a Response regulator CheY-like protein (mll6475) from MESORHIZOBIUM LOTI at 2.02 A resolution
Authors: Joint Center for Structural Genomics (JCSG) / Shapiro, L.
History
DepositionJun 29, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 20, 2011Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2012Group: Structure summary
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software
Revision 1.3Jan 24, 2018Group: Database references / Category: citation_author / Item: _citation_author.name
Revision 1.4Feb 1, 2023Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _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

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Assembly

Deposited unit
A: Response regulator CheY-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,8872
Polymers14,7901
Non-polymers961
Water59433
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)64.859, 64.859, 69.982
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Components on special symmetry positions
IDModelComponents
11A-138-

HOH

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Components

#1: Protein Response regulator CheY-like protein / Pilus assembly protein


Mass: 14790.498 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mesorhizobium loti (bacteria) / Gene: mll6475 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q989D4
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 33 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE CONSTRUCT (RESIDUES 1-134) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 1-134) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

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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: 2.87 Å3/Da / Density % sol: 57.19 %
Description: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS SEPARATE WHEN COMPUTING R MERGE, COMPLETENESS AND
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 2.0% polyethylene glycol 400, 2.0M ammonium sulfate, 0.1M HEPES pH 7.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9791
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 21, 2011
Details: Rhodium-coated vertical and horizontal focusing mirrors; liquid-nitrogen cooled double crystal Si(111) monochromator
RadiationMonochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.02→43.805 Å / Num. obs: 11550 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 44.186 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 18.05
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.02-2.090.9692.721507206398.8
2.09-2.180.6444.426243230999.7
2.18-2.270.4646.321991195999.3
2.27-2.390.398.427209218599.8
2.39-2.540.2271330209215299.7
2.54-2.740.16117.131728220799.9
2.74-3.020.11622.430708218799.7
3.02-3.450.08229.2266142132100
3.45-4.340.06436.7291192177100
4.340.05639.228813218699.9

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
PDB_EXTRACT3.1data extraction
SHELXphasing
SHARPphasing
XSCALEDecember 6, 2010data scaling
BUSTER-TNT2.8.0refinement
XDSdata reduction
SHELXDphasing
BUSTER2.8.0refinement
RefinementMethod to determine structure: SAD / Resolution: 2.02→43.805 Å / Cor.coef. Fo:Fc: 0.9542 / Cor.coef. Fo:Fc free: 0.9504 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0
Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED ...Details: 1. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 2. SULFATE (SO4) MODELED ARE PRESENT IN CRYO CONDITION. 3. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
RfactorNum. reflection% reflectionSelection details
Rfree0.2221 553 4.82 %RANDOM
Rwork0.1977 ---
obs0.1988 11480 --
Displacement parametersBiso max: 133.62 Å2 / Biso mean: 63.9552 Å2 / Biso min: 21.96 Å2
Baniso -1Baniso -2Baniso -3
1-5.9033 Å20 Å20 Å2
2--5.9033 Å20 Å2
3----11.8066 Å2
Refinement stepCycle: LAST / Resolution: 2.02→43.805 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms902 0 5 33 940
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d429SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes22HARMONIC2
X-RAY DIFFRACTIONt_gen_planes137HARMONIC5
X-RAY DIFFRACTIONt_it932HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion124SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact1059SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d932HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg1273HARMONIC21.04
X-RAY DIFFRACTIONt_omega_torsion3.27
X-RAY DIFFRACTIONt_other_torsion2.92
LS refinement shellResolution: 2.02→2.21 Å / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.2556 122 4.56 %
Rwork0.2528 2555 -
all0.2529 2677 -
Refinement TLS params.Method: refined / Origin x: 24.3851 Å / Origin y: 21.0972 Å / Origin z: 27.0893 Å
111213212223313233
T-0.0157 Å20.1635 Å20.1304 Å2--0.0827 Å20.107 Å2---0.1057 Å2
L5.1545 °2-2.5382 °2-1.0535 °2-5.5678 °21.7755 °2--2.7507 °2
S0.0515 Å °0.0157 Å °0.0203 Å °-0.5653 Å °-0.2424 Å °-0.3574 Å °0.1312 Å °0.348 Å °0.1909 Å °
Refinement TLS groupSelection details: { A|12 - 130 }

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