TRANSFERASE / GNAT / N-ACETYLTRANSFERASE / HYPOTHETICAL PROTEIN / PHOSPHINOTHRICIN / GCN5 FAMILY / PSEUDOMONAS AERUGINOSA
Function / homology
Function and homology information
acyltransferase activity, transferring groups other than amino-acyl groups / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 213 / Source method: isolated from a natural source / Formula: H2O
Sequence details
IN STRAIN PAC1, RESIDUE 47 IS ALA, AS OPPOSED TO THR IN STRAIN PAO1 : SEQUENCE DISCREPANCY BETWEEN ...IN STRAIN PAC1, RESIDUE 47 IS ALA, AS OPPOSED TO THR IN STRAIN PAO1 : SEQUENCE DISCREPANCY BETWEEN PAC1 AND PAO1. RESIDUE 33 IS MODELLED AS ALA DUE TO DISORDER
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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: 2.23 Å3/Da / Density % sol: 44.39 % / Description: NONE
Crystal grow
Method: vapor diffusion, hanging drop / pH: 7.3 Details: PROTEIN WAS CRYSTALLISED USING HANGING DROP VAPOUR DIFFUSION. RESERVOIR SOLUTION CONTAINED 1ML OF 0.1M HEPES AT PH7.3, 23-27% PEG 8000 AND 0.1% AZIDE. DROP SIZE WAS 1 MICROLITRE, TO WHICH 1 ...Details: PROTEIN WAS CRYSTALLISED USING HANGING DROP VAPOUR DIFFUSION. RESERVOIR SOLUTION CONTAINED 1ML OF 0.1M HEPES AT PH7.3, 23-27% PEG 8000 AND 0.1% AZIDE. DROP SIZE WAS 1 MICROLITRE, TO WHICH 1 MICROLITRE OF PROTEIN SOLUTION AT 10 MG/ML WAS ADDED.
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 0.975 Å / Relative weight: 1
Reflection
Resolution: 2→70 Å / Num. obs: 13388 / % possible obs: 96.1 % / Observed criterion σ(I): 0 / Redundancy: 12.8 % / Biso Wilson estimate: 21.11 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 4.6
Reflection shell
Resolution: 2→2.05 Å / Redundancy: 12.7 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 2.6 / % possible all: 96.1
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Processing
Software
Name
Version
Classification
CNS
1.1
refinement
DENZO
datareduction
SCALA
datascaling
SOLVE
phasing
Refinement
Method to determine structure: SAD Starting model: NONE Resolution: 2→6 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: RESIDUES A 1 AND A 2 WERE DISORDERED AND THEREFORE NOT MODELLED
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.2294
659
4.92 %
RANDOM
Rwork
0.1974
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-
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obs
0.1974
13388
96.1 %
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Solvent computation
Bsol: 61.36 Å2 / ksol: 0.345 e/Å3
Displacement parameters
Biso mean: 24.04 Å2
Refine analyze
Luzzati coordinate error obs: 0.22 Å / Luzzati d res low obs: 6 Å / Luzzati sigma a obs: 0.18 Å
Refinement step
Cycle: LAST / Resolution: 2→6 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1303
0
35
213
1551
Refine LS restraints
Refine-ID
Type
Dev ideal
X-RAY DIFFRACTION
c_bond_d
0.019
X-RAY DIFFRACTION
c_bond_d_na
X-RAY DIFFRACTION
c_bond_d_prot
X-RAY DIFFRACTION
c_angle_d
X-RAY DIFFRACTION
c_angle_d_na
X-RAY DIFFRACTION
c_angle_d_prot
X-RAY DIFFRACTION
c_angle_deg
1.41
X-RAY DIFFRACTION
c_angle_deg_na
X-RAY DIFFRACTION
c_angle_deg_prot
X-RAY DIFFRACTION
c_dihedral_angle_d
24.68
X-RAY DIFFRACTION
c_dihedral_angle_d_na
X-RAY DIFFRACTION
c_dihedral_angle_d_prot
X-RAY DIFFRACTION
c_improper_angle_d
1.06
X-RAY DIFFRACTION
c_improper_angle_d_na
X-RAY DIFFRACTION
c_improper_angle_d_prot
X-RAY DIFFRACTION
c_mcbond_it
X-RAY DIFFRACTION
c_mcangle_it
X-RAY DIFFRACTION
c_scbond_it
X-RAY DIFFRACTION
c_scangle_it
LS refinement shell
Resolution: 2→2.05 Å / Total num. of bins used: 13 /
Rfactor
Num. reflection
Rfree
0.2509
57
Rwork
0.2656
954
+
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