Mass: 8880.119 Da / Num. of mol.: 1 / Fragment: IGAMMA SUBDOMAIN, RESIDUES 174 - 247 / Source method: isolated from a natural source / Details: MUA OF PHAGE MU TRANSPOSASE / Source: (natural) Enterobacteria phage Mu (virus) / Genus: Mu-like viruses / References: UniProt: P07636
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Type: SEE BELOW
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Sample preparation
Sample conditions
pH: 6.3 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type
Manufacturer
Model
Field strength (MHz)
Spectrometer-ID
Bruker AMX500
Bruker
AMX500
500
1
Bruker AMX600
Bruker
AMX600
600
2
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Processing
Software
Name
Version
Classification
X-PLOR
3.1
modelbuilding
X-PLOR
3.1
refinement
X-PLOR
3.1
phasing
NMR software
Name
Version
Classification
X-PLOR (SEE ABOVE)
ABOVE)
structuresolution
X-PLOR (SEE ABOVE)
ABOVE)
refinement
Refinement
Method: simulated annealing / Software ordinal: 1 Details: THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS: 264 SEQUENTIAL (|I- J|=1), ...Details: THE 3D STRUCTURE OF THE IGAMMA SUBDOMAIN OF MU A TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 1293 EXPERIMENTAL NMR RESTRAINTS: 264 SEQUENTIAL (|I- J|=1), 282 MEDIUM RANGE (1 < |I-J| <=5) AND 178 LONG RANGE (|I-J| >5) INTERRESIDUES AND 245 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 40 DISTANCE RESTRAINTS FOR 20 BACKBONE H-BONDS; 108 TORSION ANGLE RESTRAINTS; 47 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 129 (66 CALPHA AND 63 CBETA) 13C SHIFT RESTRAINTS. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE POTENTIAL (KUSZEWSKI ET AL. (1996) PROTEIN SCI. 5, 1067-1080; KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125, 171-177). THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN ENTRY 2EZH AND 30 STRUCTURES ARE PRESENTED IN ENTRY 2EZI, AND THE EXPERIMENTAL RESTRAINTS IN 2EZHMR. IN THE RESTRAINED REGULARIZED MEAN COORDINATES (2EZH) THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 180 - 240. NOTE THAT THE OCCUPANCY FIELD HAS NO MEANING.
NMR ensemble
Conformers submitted total number: 1
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