Mass: 18.015 Da / Num. of mol.: 217 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
THE SEQUENCE ON THE DATABASE HAS A SIGNAL PEPTIDE, THE SEQUENCE OF THE STRUCTURE PRESENTED STARTS ...THE SEQUENCE ON THE DATABASE HAS A SIGNAL PEPTIDE, THE SEQUENCE OF THE STRUCTURE PRESENTED STARTS ON RESIDUE 29
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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: 3.6 Å3/Da / Density % sol: 66.2 % / Description: NONE
Crystal grow
pH: 8.5 Details: CRYSTALLIZATION SOLUTION: 100MM TRIS-HCL PH8.5, 2M AMMONIUM SULFATE. THE DROP WAS MADE BY ADDING 1UL OF PROTEIN PLUS 2UL OF CRYSTALLIZATION SOLUTION.
Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.934 Å / Relative weight: 1
Reflection
Resolution: 1.9→42.8 Å / Num. obs: 35365 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 28 % / Biso Wilson estimate: 25.5 Å2 / Rmerge(I) obs: 0.08 / Net I/σ(I): 7.6
Reflection shell
Resolution: 1.9→2 Å / Redundancy: 20.3 % / Rmerge(I) obs: 0.83 / Mean I/σ(I) obs: 0.9 / % possible all: 99.2
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Processing
Software
Name
Version
Classification
REFMAC
5.5.0063
refinement
XDS
datareduction
SCALEPACK
datascaling
PHASER
phasing
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: MODEL OBTAINED WITH THE PROTEIN CO- CRYSTALLIZED WITH COBALT. Resolution: 1.9→85.6 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.95 / SU B: 2.276 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.105 / ESU R Free: 0.102 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.THE SIDE-CHAINS OF THE AMINO ACID RESIDUES- GLU22, GLU23, ARG25, LYS30, ARG36, LYS51, MET52, LYS110, GLU184, GLU225 WERE MODELLED WITH 0.5 ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.THE SIDE-CHAINS OF THE AMINO ACID RESIDUES- GLU22, GLU23, ARG25, LYS30, ARG36, LYS51, MET52, LYS110, GLU184, GLU225 WERE MODELLED WITH 0.5 OF OCCUPANCY DUE TO THE LACK OF ELECTRON DENSITY PROBABLY DUE TO DISORDER. THE FOLLOWING AMINO ACID RESIDUES WERE MODELLED WITH DOUBLE CONFORMATION- MET31, SER138, ARG173, ARG236, GLU239, HIS245.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.19875
1768
5 %
RANDOM
Rwork
0.17351
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obs
0.17477
33596
99.86 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK