The protein is a dimer and the coordinates provided are for two sets of dimers, each representing an alternative protein conformation. Each model has 4 chains A,B,C and D. Chains A and B form one dimer in WT conformation, chains C and D form a second dimer in the distorted conformation
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Components
#1: Protein
Trpoperonrepressor
Mass: 12370.131 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Gene: trpR, Z5995, ECs5351 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A882
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Sample state
Spectrometer-ID
Type
1
1
1
isotropic
1
2D 1H-15N HSQC
1
2
1
isotropic
1
2D 1H-13C HSQC
1
3
1
isotropic
1
3D HNCO
1
4
1
isotropic
1
3D HNCA
1
5
1
isotropic
1
3DCBCA(CO)NH
1
10
1
isotropic
1
3D (H)CCH-TOCSY
1
9
1
isotropic
1
3D 1H-13C NOESY aliphatic
1
8
1
isotropic
1
3D 1H-13C NOESY aromatic
1
7
1
isotropic
1
3D 1H-15N NOESY
1
6
1
isotropic
1
3DHN(CO)CA
1
12
1
isotropic
1
3DHBHA(CO)NH
1
11
1
isotropic
1
3D HN(CA)CB
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Sample preparation
Details
Type: solution Contents: 0.5 mM [U-100% 13C; U-100% 15N] Tryptohan aporepressor, 10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT, 0.02 % sodium azide, 90% H2O/10% D2O Details: 10 mM Tris-HCl buffer pH 5.7, 100 mM NaCl, 5 mM DTT and 0.02 % NaN3 Label: apoTrpR / Solvent system: 90% H2O/10% D2O
Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz / Details: Equipped with a 5mm cryoprobe
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Processing
NMR software
Name
Version
Developer
Classification
AutoAssign
2.1.1
Zimmerman, Moseley, KulikowskiandMontelione
chemicalshiftassignment
TopSpin
2.3
BrukerBiospin
collection
NMRPipe
Delaglio, Grzesiek, Vuister, Zhu, PfeiferandBax
processing
Sparky
3
Goddard
peakpicking
GROMACS
4.6.5
BerendsenH, vanderSpoelD, vanDrunenR.
structurecalculation
GROMACS
4.6.5
BerendsenH, vanderSpoelD, vanDrunenR.
refinement
Refinement
Method: molecular dynamics / Software ordinal: 5 Details: The coordinates provided are for two sets of models, each representing an alternative protein conformation that differ particularly in the segment of the protein sequence corresponding to helix E.
NMR representative
Selection criteria: fewest violations
NMR ensemble
Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 15 / Conformers submitted total number: 15
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