BMRB Entry 16592

Title:
Solution NMR structure of a domain from BT9727_4915 from Bacillus thuringiensis, Northeast Structural Genomics Consortium Target BuR95A
Deposition date:
2009-10-30
Original release date:
2009-11-30
Authors:
He, Yunfen; Mills, Jeffrey; Wu, Yibing; Eletsky, Alexander; Wang, Huang; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas
Citation:

Citation: He, Yunfen; Mills, Jeffrey; Wu, Yibing; Eletsky, Alexander; Wang, Huang; Ciccosanti, Colleen; Hamilton, Keith; Acton, T.; Xiao, R.; Everett, J.; Montelione, G.; Szyperski, Thomas. "Solution NMR structure of a domain from BT9727_4915 from Bacillus thuringiensis, Northeast Structural Genomics Consortium Target BuR95A"  .

Assembly members:

Assembly members:
BT9727_4915, polymer, 70 residues, 7893.819 Da.

Natural source:

Natural source:   Common Name: B. thuringiensis   Taxonomy ID: 1428   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus thuringiensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts149
15N chemical shifts53
1H chemical shifts314

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BT9727_49151

Entities:

Entity 1, BT9727_4915 70 residues - 7893.819 Da.

1   METILEGLYASPTYRTYRILEASNALASER
2   ALALEUASNVALARGSERGLYGLUGLYTHR
3   ASNTYRARGILEILEGLYALALEUPROGLN
4   GLYGLNLYSVALGLNVALILESERGLUASN
5   SERGLYTRPSERLYSILEASNTYRASNGLY
6   GLNTHRGLYTYRILEGLYTHRARGTYRLEU
7   SERLYSLEUGLUHISHISHISHISHISHIS

Samples:

NC: BuR95A, [U-98% 13C; U-98% 15N], 0.905 mM; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v; NH4OAc 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM

NC5: BuR95A, [U-5% 13C; U-98% 15N], 1.041 mM; H2O 90 % v/v; D2O, [U-100% 2H], 10 % v/v; NH4OAc 20 mM; NaCl 200 mM; CaCl2 5 mM; DTT 10 mM; DSS 50 uM

sample_conditions_1: ionic strength: 217.5 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQCNCisotropicsample_conditions_1
GFT (4,3)D CABCA(CO)NHNNCisotropicsample_conditions_1
GFT (4,3)D HNNCABCANCisotropicsample_conditions_1
GFT (4,3)D HABCAB(CO)NHNNCisotropicsample_conditions_1
3D HNCANCisotropicsample_conditions_1
simNOESYNCisotropicsample_conditions_1
3D 1H-15N TOCSYNC5isotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
2D 1H-13C HSQCNC5isotropicsample_conditions_1

Software:

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct, Huang, Tejero, Powers and Montelione - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

PSVS, Bhattacharya and Montelione - refinement

TALOS, Cornilescu, Delaglio and Bax - refinement

XEASY, Bartels et al. - chemical shift assignment

VNMRJ, Varian - collection

TOPSPIN, Bruker Biospin - collection

PROSA, Guntert - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Molmol, Koradi, Billeter and Wuthrich - refinement

SPSCAN, Glaser - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks