CRYSTAL PACKING ANALYSIS SUGGESTS THAT A MONOMER IS THE STABLE OLIGOMERIC FORM IN SOLUTION. SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
-
Components
#1: Protein
putativeacetyltransferase
Mass: 22416.271 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus subsp. aureus Mu50 (bacteria) Gene: NP_371943.1, SAV1419 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q99U68, UniProt: A0A0H3JZG0*PLUS
Resolution: 2.5→27.661 Å / Num. obs: 10262 / % possible obs: 99.9 % / Redundancy: 5.4 % / Biso Wilson estimate: 71.685 Å2 / Rmerge(I) obs: 0.056 / Rsym value: 0.056 / Net I/σ(I): 9.491
Reflection shell
Diffraction-ID: 1
Resolution (Å)
Redundancy (%)
Rmerge(I) obs
Mean I/σ(I) obs
Num. measured all
Num. unique all
Rsym value
% possible all
2.5-2.56
5.6
0.779
1
4064
732
0.779
100
2.56-2.64
5.5
0.648
1.2
4020
730
0.648
100
2.64-2.71
5.5
0.542
1.4
3889
708
0.542
100
2.71-2.8
5.5
0.373
2
3804
686
0.373
100
2.8-2.89
5.5
0.274
2.8
3733
678
0.274
100
2.89-2.99
5.5
0.219
3.5
3467
627
0.219
100
2.99-3.1
5.5
0.162
4.7
3553
643
0.162
100
3.1-3.23
5.5
0.133
5.6
3305
602
0.133
100
3.23-3.37
5.5
0.087
8.5
3146
577
0.087
100
3.37-3.54
5.5
0.068
10.5
3069
558
0.068
100
3.54-3.73
5.5
0.061
10.2
2837
518
0.061
100
3.73-3.95
5.4
0.054
11.4
2801
515
0.054
100
3.95-4.23
5.5
0.05
11.1
2597
476
0.05
100
4.23-4.56
5.4
0.04
15
2386
441
0.04
100
4.56-5
5.4
0.034
18.3
2230
415
0.034
100
5-5.59
5.4
0.032
19.5
2001
373
0.032
100
5.59-6.45
5.3
0.04
15
1763
335
0.04
100
6.45-7.91
5.1
0.039
16.2
1457
284
0.039
100
7.91-11.18
5
0.026
24.1
1168
233
0.026
100
11.18-27.66
4.4
0.033
17.7
578
131
0.033
94.5
-
Phasing
Phasing
Method: MAD
-
Processing
Software
Name
Version
Classification
NB
REFMAC
5.2.0019
refinement
PHENIX
refinement
SOLVE
phasing
MolProbity
3beta29
modelbuilding
SCALA
3.2.5
datascaling
PDB_EXTRACT
3.006
dataextraction
MOSFLM
datareduction
Refinement
Method to determine structure: MAD / Resolution: 2.5→27.661 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.924 / Occupancy max: 1 / Occupancy min: 0.19 / SU B: 12.76 / SU ML: 0.14 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.274 / ESU R Free: 0.226 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4.AN UNIDENTIFIED LIGAND (UNL) HAS BEEN MODELED IN THE VICINITY OF THE PUTATIVE ACTIVE SITE BASED ON COMPARISON WITH LIGAND BOUND STRUCTURES OF SIMILAR PROTEINS. 5.A PEG FRAGMENT (P33, HEPTAETHYLENE GLYCOL, PEG330) FROM THE CRYSTALLIZATION CONDITION HAS BEEN MODELED IN THE SOLVENT STRUCTURE. 6.THERE ARE UNMODELED ELECTRON DENSITY BLOBS IN SEVERAL REGIONS OF THE PROTEIN INCLUDING RESIDUES H142/K143 AND D49. THESE RESIDUES ARE NOT IN THE VICINITY OF THE PUTATIVE ACTIVE SITE.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.253
492
4.8 %
RANDOM
Rwork
0.219
-
-
-
obs
0.22
10246
99.91 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
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