SHC-transformingprotein1 / SHC-transforming protein 3 / SHC-transforming protein A / Src homology 2 domain-containing- ...SHC-transforming protein 3 / SHC-transforming protein A / Src homology 2 domain-containing-transforming protein C1 / SH2 domain protein C1
Mass: 18133.912 Da / Num. of mol.: 1 / Fragment: residues 37-201 Source method: isolated from a genetically manipulated source Details: residues 37-201 / Source: (gene. exp.) Homo sapiens (human) / Gene: SHC1, SHC, SHCA / Plasmid: pNIC28-BSA4 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): R3 / References: UniProt: P29353
Monochromator: Si (111) double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.97949 Å / Relative weight: 1
Reflection
Resolution: 1.87→28.98 Å / Num. all: 17585 / Num. obs: 17581 / % possible obs: 99.9 % / Redundancy: 5.3 % / Biso Wilson estimate: 35.1 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 13.4
Reflection shell
Resolution: 1.87→1.97 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.823 / Mean I/σ(I) obs: 2.1 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0103
refinement
MOSFLM
datareduction
SCALA
datascaling
SHARP
phasing
Refinement
Resolution: 1.87→28.98 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.968 / SU B: 7.053 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.11 / ESU R Free: 0.103 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.19096
912
5.2 %
RANDOM
Rwork
0.16764
-
-
-
obs
0.16887
16660
99.84 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK