Evidence: gel filtration, BiP V461F appeared as monomer by gel filtration.
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Buried area
600 Å2
ΔGint
8 kcal/mol
Surface area
24130 Å2
Method
PISA
Unit cell
Length a, b, c (Å)
50.610, 52.500, 91.730
Angle α, β, γ (deg.)
90.00, 97.34, 90.00
Int Tables number
4
Space group name H-M
P1211
-
Components
#1: Protein
EndoplasmicreticulumchaperoneBiP / 78 kDa glucose-regulated protein / GRP-78 / Binding-immunoglobulin protein / BiP / Heat shock ...78 kDa glucose-regulated protein / GRP-78 / Binding-immunoglobulin protein / BiP / Heat shock protein 70 family protein 5 / HSP70 family protein 5 / Heat shock protein family A member 5 / Immunoglobulin heavy chain-binding protein
Mass: 57485.980 Da / Num. of mol.: 1 / Mutation: V461F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cricetulus griseus (Chinese hamster) / Gene: HSPA5, GRP78, I79_019946 / Production host: Escherichia coli (E. coli) References: UniProt: G3I8R9, non-chaperonin molecular chaperone ATPase
Resolution: 2.08→50.2 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.941 / SU B: 8.026 / SU ML: 0.202 / Cross valid method: THROUGHOUT / ESU R: 0.278 / ESU R Free: 0.213 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.27102
1367
4.8 %
RANDOM
Rwork
0.23676
-
-
-
obs
0.23833
27313
99.06 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å