Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Type: TRIPLE RESONANCE
NMR details
Text: TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN 12C- FILTERED NOE, 12C-FILTERED HOHAHA AND 1H-1H NOE FOR DNA. QUANTITATIVE J CORRELATION FOR COUPLING CONSTANTS 3D 15N- SEPARATED, 3D 13C-SEPARATED, ...Text: TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN 12C- FILTERED NOE, 12C-FILTERED HOHAHA AND 1H-1H NOE FOR DNA. QUANTITATIVE J CORRELATION FOR COUPLING CONSTANTS 3D 15N- SEPARATED, 3D 13C-SEPARATED, 3D 12C-FILTERED 3D 13C- SEPARATED/12C-FILTERED, AND 2D 1H-1H NOE EXPERIMENTS.
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Sample preparation
Sample conditions
pH: 6.00 / Temperature: 303.50 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)
ABOVE)
structuresolution
X-PLOR (SEE ABOVE) ABOVE)
ABOVE)
refinement
Refinement
Method: simulated annealing / Software ordinal: 1 Details: THE 3D STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR AND IS BASED ON 1475 EXPERIMENTAL NMR RESTRAINTS: (A) INTRAPROTEIN: 188 ...Details: THE 3D STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR AND IS BASED ON 1475 EXPERIMENTAL NMR RESTRAINTS: (A) INTRAPROTEIN: 188 SEQUENTIAL (|I- J|=1), 134 MEDIUM RANGE (1 < |I-J| <=5) AND 95 LONG RANGE (|I-J| >5) INTERRESIDUES AND 275 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 140 TORSION ANGLE RESTRAINTS; 33 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 94 (48 CALPHA AND 46 CBETA) 13C SHIFT RESTRAINTS. (NUMBERS OF RESIDUES 10 - 61) (B) INTRA-DNA: 124 INTRARESIDUE, 112 SEQUENTIAL INTRASTRAND, 21 INTERSTRAND INTERPROTON DISTANCE RESTRAINTS; 102 TORSION ANGLE RESTRAINTS (FOR ALPHA, BETA, GAMMA, DELTA, EPSILON AND AND ZETA BACKBONE TORSION ANGLES). (C) INTERMOLECULAR: 75 INTERPROTON DISTANCE RESTRAINTS. THE EXPERIMENTAL NMR RESTRAINTS ARE SUPPLEMENTED BY HYDROGEN BONDING RESTRAINTS: 24 DISTANCES FOR 12 BACKBONE HYDROGEN BONDS WITHIN THE PROTEIN, 58 DISTANCES FOR WATSON-CRICK BASE-PAIRING WITHIN THE DNA, AND 10 AMBIGUOUS DISTANCE RESTRAINTS BETWEEN THE PROTEIN AND THE DNA. THE RESTRAINTS HAVE BEEN DEPOSITED. 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 THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN ENTRY 1YUI AND 50 STRUCTURES ARE PRESENTED IN THIS ENTRY. IN THE RESTRAINED REGULARIZED MEAN COORDINATES 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 HAS NO MEANING. BEST FITTING TO GENERATE THE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 14 - 58 OF THE PROTEIN AND BASE PAIRS 1 - 11 OF THE DNA (RESIDUES 10 - 13 AND 59 - 61 ARE DISORDERED IN SOLUTION). RESIDUE 10 CORRESPONDS TO RESIDUE 319 OF THE NATURAL SEQUENCE. NOTE THE OCCUPANCY FIELD HAS NO MEANING.
NMR ensemble
Conformers submitted total number: 50
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