Evidence: gel filtration, Elutes as a monomeric peak with a small dimeric shoulder
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Unit cell
Length a, b, c (Å)
87.220, 87.220, 318.850
Angle α, β, γ (deg.)
90.00, 90.00, 120.00
Int Tables number
179
Space group name H-M
P6522
Noncrystallographic symmetry (NCS)
NCS domain:
ID
Ens-ID
Details
1
1
A
2
1
B
NCS domain segments:
Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: ASP / Beg label comp-ID: ASP / End auth comp-ID: LEU / End label comp-ID: LEU / Refine code: _ / Auth seq-ID: 35 - 297 / Label seq-ID: 14 - 276
Dom-ID
Auth asym-ID
Label asym-ID
1
A
A
2
B
B
-
Components
-
Protein , 1 types, 2 molecules AB
#1: Protein
NAD-dependentproteindeacylasesirtuin-5, mitochondrial / Regulatory protein SIR2 homolog 5
Mass: 31495.012 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Danio rerio (zebrafish) / Gene: sirt5, si:ch211-121a2.1 / Production host: Escherichia coli (E. coli) References: UniProt: Q6DHI5, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides
-
Protein/peptide , 2 types, 2 molecules EH
#2: Protein/peptide
3(S)-(phenylthio)succinyl-CPS1peptide
Mass: 1210.398 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
#3: Protein/peptide
3(R)-(phenylthio)succinyl-CPS1peptide
Mass: 1176.338 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
Resolution: 3.3→48.73 Å / Cor.coef. Fo:Fc: 0.913 / Cor.coef. Fo:Fc free: 0.902 / SU B: 79.323 / SU ML: 0.596 / Cross valid method: THROUGHOUT / ESU R Free: 0.605 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.28431
573
5 %
RANDOM
Rwork
0.22189
-
-
-
obs
0.22517
10922
98.97 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK