Bileacidreceptor / Farnesoid X-activated receptor / Farnesol receptor HRR-1 / Nuclear receptor subfamily 1 group H ...Farnesoid X-activated receptor / Farnesol receptor HRR-1 / Nuclear receptor subfamily 1 group H member 4 / Retinoid X receptor-interacting protein 14 / RXR-interacting protein 14
Mass: 26802.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NR1H4, BAR, FXR, HRR1, RIP14 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96RI1
#2: Protein/peptide
PeptidefromNuclearreceptorcoactivator2
Mass: 1349.576 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: E7EWM1, UniProt: Q15596*PLUS
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.005 Å / Relative weight: 1
Reflection
Resolution: 2.95→86.4 Å / Num. obs: 6401 / % possible obs: 99.7 % / Redundancy: 13.2 % / Net I/σ(I): 4.1
-
Processing
Software
Name
Version
Classification
SCALEPACK
datascaling
REFMAC
5.8.0189
refinement
PDB_EXTRACT
3.24
dataextraction
HKL-2000
datareduction
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.95→86.4 Å / Cor.coef. Fo:Fc: 0.867 / Cor.coef. Fo:Fc free: 0.824 / SU B: 16.835 / SU ML: 0.323 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.486 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2821
349
5.5 %
RANDOM
Rwork
0.2465
-
-
-
obs
0.2486
5994
99.09 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
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