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 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" 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. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "EA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 7-STRANDED BARREL THIS IS REPRESENTED BY A 8-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.
Mass: 18.015 Da / Num. of mol.: 555 / Source method: isolated from a natural source / Formula: H2O
Sequence details
THE FIRST 3 AMINO ACIDS GSH -2 TO 0 ARE A REMAINDER OF A LINKER AFTER THROMBIN CLEAVAGE. THE ...THE FIRST 3 AMINO ACIDS GSH -2 TO 0 ARE A REMAINDER OF A LINKER AFTER THROMBIN CLEAVAGE. THE UNIPROT ENTRY B2D1S8 INCLUDES A SIGNAL PEPTIDE IN ITS SEQUENCE. THIS PROTEIN HAS BEEN OVEREXPRESSED IN ITS ACTIVE FORM (D.C DE GEUS ET AL.(2008)ACTA CRYSTALLOGRAPHICA SECTION F, IN PRESS) AND DOES NOT INCLUDE THIS SIGNAL PEPTIDE.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.54 Å3/Da / Density % sol: 51.6 % / Description: NONE
Crystal grow
pH: 5.5 Details: 100 MM MES PH 5.5, 25 %(W/V) PEG MME 2000, 0.3 M KSCN, 5 %(V/V) GLYCEROL, 180 MM AMMONIUM SULPHATE
Resolution: 2.1→40.13 Å / Num. obs: 100003 / % possible obs: 100 % / Redundancy: 13.8 % / Biso Wilson estimate: 26.559 Å2 / Rmerge(I) obs: 0.11
Reflection shell
Resolution: 2.1→2.21 Å / Redundancy: 14.09 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 3.8 / % possible all: 100
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Processing
Software
Name
Version
Classification
REFMAC
5.2.0019
refinement
MOSFLM
datareduction
SCALA
datascaling
CRANK
phasing
Refinement
Method to determine structure: MAD Starting model: NONE Resolution: 2.1→50.68 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.909 / Cross valid method: THROUGHOUT / ESU R: 0.232 / ESU R Free: 0.192 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FOLLOWING DISORDERED REGIONS WERE NOT MODELED. CHAIN A -2 TO 7 AND 230 TO 248 CHAIN B -2 TO 8 AND 227 TO 248 CHAIN C -2 TO 10 AND 228 ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE FOLLOWING DISORDERED REGIONS WERE NOT MODELED. CHAIN A -2 TO 7 AND 230 TO 248 CHAIN B -2 TO 8 AND 227 TO 248 CHAIN C -2 TO 10 AND 228 TO 248 CHAIN D -2 TO 7 AND 228 TO 248 CHAIN E -2 TO 7 AND 228 TO 251 CHAIN F -2 TO 8 AND 228 TO 251.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.25486
4994
5 %
RANDOM
Rwork
0.2187
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obs
0.2205
94936
99.97 %
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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