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- PDB-4dad: Crystal structure of a Putative pilus assembly-related protein (B... -

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Basic information

Entry
Database: PDB / ID: 4dad
TitleCrystal structure of a Putative pilus assembly-related protein (BPSS2195) from Burkholderia pseudomallei K96243 at 2.50 A resolution (PSI Community Target, Shapiro L.)
ComponentsPutative pilus assembly-related protein
KeywordsSIGNALING PROTEIN / SIGNAL TRANSDUCTION / Response regulator receiver domain / CheY-related protein / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY
Function / homology
Function and homology information


phosphorelay signal transduction system
Similarity search - Function
AAA domain / AAA domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Response regulator / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Putative pilus assembly-related protein
Similarity search - Component
Biological speciesBurkholderia pseudomallei (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.5 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be Published
Title: Crystal structure of a Putative pilus assembly-related protein (BPSS2195) from Burkholderia pseudomallei K96243 at 2.50 A resolution (PSI Community Target, Shapiro L.)
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionJan 12, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 7, 2012Group: Data collection
Revision 1.2Mar 21, 2012Group: Database references
Revision 1.3Apr 17, 2013Group: Database references / Structure summary
Revision 1.4Nov 15, 2017Group: Refinement description / Category: software
Revision 1.5Feb 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

Downloads & links

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Assembly

Deposited unit
A: Putative pilus assembly-related protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)16,5986
Polymers16,2391
Non-polymers3595
Water79344
1
A: Putative pilus assembly-related protein
hetero molecules

A: Putative pilus assembly-related protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)33,19612
Polymers32,4782
Non-polymers71810
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555y,x,-z1
Buried area3260 Å2
ΔGint-101 kcal/mol
Surface area13890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)65.589, 65.589, 65.642
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
DetailsCRYSTAL PACKING SUPPORTS THE ASSIGNMENT OF A DIMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

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Components

#1: Protein Putative pilus assembly-related protein


Mass: 16238.903 Da / Num. of mol.: 1 / Fragment: UNP residues 1-127
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia pseudomallei (bacteria) / Gene: BPSS2195 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): PB1 / References: UniProt: Q63I75
#2: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#3: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 44 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG FOLLOWED BY ...THE CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG FOLLOWED BY RESIDUES 1-127 OF THE FULL LENGTH PROTEIN.

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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: 2.51 Å3/Da / Density % sol: 50.99 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 2.00M (NH4)2SO4, 0.1M TRIS pH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97947,0.91837,0.97894
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 8, 2011
Details: FLAT MIRROR (VERTICAL FOCUSING); SINGLE CRYSTAL SI(111) BENT MONOCHROMATOR (HORIZONTAL FOCUSING)
RadiationMonochromator: SINGLE CRYSTAL SI(111) BENT / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.979471
20.918371
30.978941
ReflectionResolution: 2.5→42.953 Å / Num. obs: 5865 / % possible obs: 98.7 % / Observed criterion σ(I): -3 / Redundancy: 4.77 % / Biso Wilson estimate: 61.811 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 16.22
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.5-2.594.830.6432.56270055997.4
2.59-2.690.4723.4276954899.6
2.69-2.810.3794.2295858799.2
2.81-2.960.2416.4279055798.8
2.96-3.150.1529.5289161499
3.15-3.390.09215254055999.3
3.39-3.730.05821.9298859699.5
3.73-4.260.04228282658798.8
4.26-5.350.03632.4259259198
5.35-42.9530.03234.8285165897.9

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Phasing

PhasingMethod: MAD

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Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
PDB_EXTRACT3.1data extraction
SHELXphasing
SHARPphasing
XSCALEDecember 29, 2011data scaling
BUSTER-TNT2.10.0refinement
XDSdata reduction
SHELXDphasing
BUSTER2.10.0refinement
RefinementMethod to determine structure: MAD / Resolution: 2.5→42.953 Å / Cor.coef. Fo:Fc: 0.9426 / Cor.coef. Fo:Fc free: 0.8994 / 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) FROM CRYSTALLIZATION CONDITION AND CHLORIDE (CL) FROM THE EXPRESSION OR PURIFICATION BUFFERS ARE MODELED INTO THE STRUCTURE 3. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
RfactorNum. reflection% reflectionSelection details
Rfree0.2546 267 4.57 %RANDOM
Rwork0.1908 ---
obs0.1936 5847 98.75 %-
Displacement parametersBiso max: 152.49 Å2 / Biso mean: 62.3187 Å2 / Biso min: 30.17 Å2
Baniso -1Baniso -2Baniso -3
1--4.8932 Å20 Å20 Å2
2---4.8932 Å20 Å2
3---9.7865 Å2
Refine analyzeLuzzati coordinate error obs: 0.358 Å
Refinement stepCycle: LAST / Resolution: 2.5→42.953 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1011 0 17 44 1072
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d504SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes27HARMONIC2
X-RAY DIFFRACTIONt_gen_planes158HARMONIC5
X-RAY DIFFRACTIONt_it1049HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion142SEMIHARMONIC5
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_contact1149SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d1049HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg1427HARMONIC21.07
X-RAY DIFFRACTIONt_omega_torsion2.87
X-RAY DIFFRACTIONt_other_torsion3
LS refinement shellResolution: 2.5→2.79 Å / Total num. of bins used: 5
RfactorNum. reflection% reflection
Rfree0.2947 85 5.29 %
Rwork0.2145 1522 -
all0.2187 1607 -
obs--98.75 %
Refinement TLS params.Method: refined / Origin x: 11.5045 Å / Origin y: 43.1199 Å / Origin z: 3.2493 Å
111213212223313233
T-0.0563 Å2-0.0084 Å2-0.0131 Å2--0.1731 Å20.0446 Å2---0.0779 Å2
L4.7251 °2-2.1691 °2-1.9079 °2-2.6563 °22.0738 °2--3.0294 °2
S0.0067 Å °-0.0833 Å °0.4477 Å °-0.105 Å °0.0941 Å °-0.3756 Å °-0.1712 Å °0.1661 Å °-0.1008 Å °

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