Mass: 21005.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P05231
Has protein modification
Y
-
Experimental details
-
Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
2/3/4D NOESY
1
2
1
TOCSY
1
3
1
ETC.
-
Sample preparation
Sample conditions
pH: 6.1 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR
-
NMR measurement
NMR spectrometer
Type: Varian UNITY PLUS 600 / Manufacturer: Varian / Model: UNITY PLUS 600 / Field strength: 600 MHz
-
Processing
Software
Name
Version
Classification
X-PLOR
3.1
modelbuilding
X-PLOR
3.1
refinement
X-PLOR
3.1
phasing
NMR software
Name
Version
Developer
Classification
X-PLOR
3.1
BRUNGER
refinement
X-PLOR
structuresolution
Refinement
Method: DISTANCE GEOMETRY, SIMULATED ANNEALING. / Software ordinal: 1 Details: STRUCTURES ARE BASED ON 2961 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NMR MEASUREMENTS INCLUDING 138 HYDROGEN BOND RESTRAINTS FROM 69 HYDROGEN BONDS IDENTIFIED USING AMIDE EXCHANGE DATA ...Details: STRUCTURES ARE BASED ON 2961 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NMR MEASUREMENTS INCLUDING 138 HYDROGEN BOND RESTRAINTS FROM 69 HYDROGEN BONDS IDENTIFIED USING AMIDE EXCHANGE DATA AND INITIAL STRUCTURE CALCULATIONS. IN ADDITION, 83 PHI BACKBONE TORSION ANGLE RESTRAINTS WERE DERIVED FROM COUPLING CONSTANTS. THE METHOD USED TO DERIVE THE FINAL ENSEMBLE OF STRUCTURES IS THE HYBRID METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD (M. NILGES, G.M. CLORE, AND A.M. GRONENBORN (1988) FEBS LETT. 229, 317-324.
NMR ensemble
Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 75 / Conformers submitted total number: 32
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