PROBABLEWRKYTRANSCRIPTIONFACTOR52 / DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW ...DISEASE RESISTANCE PROTEIN RRS1 / DISEASE RESISTANCE PROTEIN SLH1 / PROTEIN SENSITIVE TO LOW HUMIDITY 1 / RESISTANCE TO RALSTONI A SOLANACEARUM 1 PROTEIN / WRKY DNA-BINDING PROTEIN 52
Mass: 17250.496 Da / Num. of mol.: 2 Fragment: TOLL/INTERLEUKIN-1 RECEPTOR DOMAIN, RESIDUES 6-153 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PMCSG7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q9FH83, UniProt: P0DKH5*PLUS
#2: Protein
DISEASERESISTANCEPROTEINRPS4
Mass: 19686.801 Da / Num. of mol.: 2 Fragment: TOLL/INTERLEUKIN-1 RECEPTOR DOMAIN, RESIDUES 11-178 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ARABIDOPSIS THALIANA (thale cress) / Plasmid: PMCSG7 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q9XGM3
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.9539 Å / Relative weight: 1
Reflection
Resolution: 2.65→29.84 Å / Num. obs: 32619 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 23 % / Biso Wilson estimate: 73.73 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 27.5
Reflection shell
Resolution: 2.65→2.78 Å / Redundancy: 24 % / Rmerge(I) obs: 1.5 / Mean I/σ(I) obs: 2 / % possible all: 100
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Processing
Software
Name
Version
Classification
PHENIX
(PHENIX.REFINE)
refinement
XDS
datareduction
Aimless
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: RPS4 TIR AND RRS1 TIR Resolution: 2.65→29.794 Å / SU ML: 0.36 / σ(F): 1.34 / Phase error: 21.13 / Stereochemistry target values: ML Details: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING ...Details: CRYSTALS OF THE RRS1 AND RPS4 TIR DOMAIN HETERODIMER WERE OBTAINED BY LINKING RRS1(6-153) AND RPS4(10-178) WITH A FIVE-RESIDUE (GSGGS) LINKER . A REGION ENCOMPASSING 11 RESIDUES INCLUDING THE LINKER COULD NOT BE MODELED DUE TO THE LACK OF INTERPRETABLE ELECTRON DENSITY. WE FAVOR THE INTERPRETATION THAT THE LINKED CHAIN OCCURS BETWEEN MOLECULES A-D, B-C. HOWEVER, AS IT IS NOT POSSIBLE TO MODEL THE LINKER REGION WITH CERTAINTY WE CANNOT EXPLICITLY DETERMINE WHICH MOLECULES ARE LINKED IN THE CRYSTAL. FOR THIS REASON, WE HAVE LABELLED THE RRS1 AND RPS4 TIR DOMAIN MOLECULES AS SEPARATE CHAINS IN THE COORDINATE FILE DEPOSITED. THE FUNCTIONALLY IMPORTANT HETERODIMERISATION INTERFACE BETWEEN RRS1 AND RPS4 TIR DOMAINS OCCURS BETWEEN PROTEIN CHAINS A-B AND C-D.
Rfactor
Num. reflection
% reflection
Rfree
0.2267
1997
6.1 %
Rwork
0.1823
-
-
obs
0.185
32498
99.98 %
Solvent computation
Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL