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Biological Magnetic Resonance Data Bank


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BMRB Entry 15999

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15999
MolProbity Validation Chart

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Title: Solution NMR structure of HTH_XRE family transcriptional regulator BT_p548217 from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium Target BtR244.

Deposition date: 2008-10-23 Original release date: 2008-12-03

Authors: Ramelot, Theresa; Cort, John; Zhao, Li; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Cort, John; Zhao, Li; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of HTH_XRE family transcriptional regulator BT_p548217 from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium Target BtR244."  Not known ., .-..

Assembly members:
XRE, polymer, 77 residues, 8888 Da.

Natural source:   Common Name: Bacteroides thetaiotaomicron   Taxonomy ID: 818   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacteroides thetaiotaomicron

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
XRE: MELSNELKVERIRLSLTAKS VAEEMGISRQQLCNIEQSET APVVVKYIAFLRSKGVDLNA LFDRIIVNKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts338
15N chemical shifts83
1H chemical shifts559

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, chain A1
2entity_1, chain B1

Entities:

Entity 1, entity_1, chain A 77 residues - 8888 Da.

homodimer

1   METGLULEUSERASNGLULEULYSVALGLU
2   ARGILEARGLEUSERLEUTHRALALYSSER
3   VALALAGLUGLUMETGLYILESERARGGLN
4   GLNLEUCYSASNILEGLUGLNSERGLUTHR
5   ALAPROVALVALVALLYSTYRILEALAPHE
6   LEUARGSERLYSGLYVALASPLEUASNALA
7   LEUPHEASPARGILEILEVALASNLYSLEU
8   GLUHISHISHISHISHISHIS

Samples:

NC_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.9 ± .05 mM; H2O 95%; D2O 5%

NC_sample_in_D2O: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], .9 ± .05 mM; D2O 100%

NC50_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], .5 ± 0.03 mM; protein .5 ± 0.03 mM; H2O 95%; D2O 5%

NC5_sample: ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 1 ± 0.05 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC (aliph)NC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC50_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
4D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQCNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-13C HSQCNC_sample_in_D2Oisotropicsample_conditions_1
3D 1H-13C ED-FILT_NOESYNC50_sampleisotropicsample_conditions_1
2D 1H-13C HSQC (arom)NC_sampleisotropicsample_conditions_1

Software:

NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Bruker AvanceIII 850 MHz
  • Varian INOVA 500 MHz

Related Database Links:

SWS Q8ABY1_BACTN
UNP Q8ABY1
PDB
EMBL CUP04950 CUP86193 CUQ25051
GB AAO45315 EES65484 EEX44071 EFG18118 EFK63747
REF NP_818970 WP_005842174

Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts