structures with the least restraint violations, structures with the lowest energy
Representative
Model #1
closest to the average
-
Components
#1: Protein
PTSsystem, galactitol-specificIIBcomponent / EIIB-Gat / Galacticol-permease IIB component / Phosphotransferase enzyme II / B component / GatB
Mass: 12481.328 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: GATB, C2618, Z3256, ECS2896, SF2155, S2281 / Plasmid: pHIVTEV / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) References: UniProt: Q8X7H5, UniProt: P0A435*PLUS, protein-Npi-phosphohistidine-sugar phosphotransferase
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Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
2
2D NOESY
1
2
2
Mother-NOESY (1H-13C region)
1
3
1
3D 15N-separated NOESY
1
4
3
IPAP-HSQC
NMR details
Text: This structure was determined using standard 2D homonuclear and 3D heteronuclear techniques.
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
1 mM U-15N,13C GatB, 100 mM phosphate buffer, 75 mM KCl, 75 mM NaCl, 1 mM DTT, 1 mM sodium azide, 90% H2O, 10 % D2O
90% H2O/10% D2O
2
1 mM U-15N,13C GatB, 100 mM phosphate buffer, 75 mM KCl, 75 mM NaCl, 1 mM DTT, 1 mM sodium azide, 100 % D2O
100% D2O
3
1 mM U-15N,13C GatB, 100 mM phosphate buffer, 75 mM KCl, 75 mM NaCl, 1 mM DTT, 1 mM sodium azide, 5 mg/ml of Pf1 phage, 90% H2O, 10 % D2O
90% H2O/10% D2O
Sample conditions
Ionic strength: 100 mM Phosphate, 75 mM NaCl, 75 mM KCl / pH: 6.8 / Pressure: ambient / Temperature: 298 K
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NMR measurement
Radiation
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelength
Relative weight: 1
NMR spectrometer
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz
-
Processing
NMR software
Name
Version
Developer
Classification
XwinNMR
3.5
collection
XwinNMR
3.5
processing
NMRView
4
processing
Sparky
3.106
dataanalysis
TALOS
2003.027.13.05
BAX
refinement
CNS
1.1
Brunger
refinement
Refinement
Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 1377 restraints: 1119 NOE-derived distance constraints, 120 dihedral angle restraints, 56 distance restraints from hydrogen bonds (28 hydrogen bonds), ...Details: the structures are based on a total of 1377 restraints: 1119 NOE-derived distance constraints, 120 dihedral angle restraints, 56 distance restraints from hydrogen bonds (28 hydrogen bonds), and 82 15N-1H residual dipolar couplings.
NMR representative
Selection criteria: closest to the average
NMR ensemble
Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20
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