SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Resolution: 1.9→82.5 Å / Num. obs: 10376 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 11.9 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 21
Reflection shell
Resolution: 1.9→1.94 Å / Redundancy: 12 % / Rmerge(I) obs: 0.83 / Mean I/σ(I) obs: 3.7 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0033
refinement
MOSFLM
datareduction
SCALA
datascaling
SHELX
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 1.9→82.47 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.96 / SU B: 2.731 / SU ML: 0.079 / Cross valid method: THROUGHOUT / ESU R: 0.122 / ESU R Free: 0.115 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE PROTEIN STRUCTURE IS VAPD-CORE IN WHICH THE DISORDERED N-TERMINUS (RESIDUE 1-19) IS ABSENT FROM THE PROTEIN CONSTRUCT.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.19078
497
4.8 %
RANDOM
Rwork
0.15923
-
-
-
obs
0.16077
9823
99.54 %
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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