BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15217

Title: NMR SOLUTION STRUCTURE OF YKVR PROTEIN FROM BACILLUS SUBTILIS: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SR358

Authors: Swapna, G.; Chi Ho, K.; Cunningham, K.; Ma, L.; Xiao, R.; Baran, M.; Acton, T.; Liu, J.; Rost, B.; Montelione, G.

Citation: Swapna, G.; Chi Ho, K.; Cunningham, K.; Ma, L.; Xiao, R.; Baran, M.; Acton, T.; Liu, J.; Rost, B.; Montelione, G.. "NMR Solution Structure of Ykvr Protein from Bacillus Subtilis: Northeast Structural Genomics Consortium Target SR358"  . ., .-..

Assembly members:
YKVR_PROTEIN, polymer, 105 residues, 12246.754 Da.

Natural source:   Common Name: Bacteria   Taxonomy ID: 1423   Superkingdom: not available   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
YKVR_PROTEIN: MVKTLRLNNVTLEMAAYQEE SEPKRKIAFTLNVTSETYHD IAVLLYEKTFNVEVPERDLA FRGEMTNYSTSLTNLYEPGA VSEFYIEITEIDKNADSLEH HHHHH

Data sets:
Data typeCount
13C chemical shifts353
15N chemical shifts101
1H chemical shifts716

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1full length protein1

Entities:

Entity 1, full length protein 105 residues - 12246.754 Da.

1   METVALLYSTHRLEUARGLEUASNASNVAL
2   THRLEUGLUMETALAALATYRGLNGLUGLU
3   SERGLUPROLYSARGLYSILEALAPHETHR
4   LEUASNVALTHRSERGLUTHRTYRHISASP
5   ILEALAVALLEULEUTYRGLULYSTHRPHE
6   ASNVALGLUVALPROGLUARGASPLEUALA
7   PHEARGGLYGLUMETTHRASNTYRSERTHR
8   SERLEUTHRASNLEUTYRGLUPROGLYALA
9   VALSERGLUPHETYRILEGLUILETHRGLU
10   ILEASPLYSASNALAASPSERLEUGLUHIS
11   HISHISHISHISHIS

Samples:

sample_1: YKVR PROTEIN, [U-10% 13C; U-100% 15N], 1.17 mM; SODIUM AZIDE 0.02 mM; MES 20 mM; DTT 100 mM; NaCl 100 mM; CaCl2 5 mM

sample_2: YKVR PROTEIN, [U-100% 13C; U-100% 15N], 1.17 ± 0.2 mM; SODIUM AZIDE 0.02 mM; MES 20 mM; DTT 100 mM; NaCl 100 mM; CaCl2 5 mM

sample_3: YKVR PROTEIN, [U-100% 13C; U-100% 15N], 1.17 ± 0.2 mM; SODIUM AZIDE 0.02 mM; MES 20 mM; DTT 100 mM; NaCl 100 mM; CaCl2 5 mM

sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HBHANHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_3isotropicsample_conditions_1
3D HcccoNH-TOCSYsample_2isotropicsample_conditions_1
3D CccoNH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_3isotropicsample_conditions_1

Software:

CNS_1.1,_X-PLOR v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski, Montelione - chemical shift assignment

AVS, Moseley and Montelione - validation of assignments

AutoStruct v2.1.1, Huang,Y-J.,Powers,R.,Montelione, G.T., Huang,Y-J, Tejero,R.,Powers,R.,Montelione, G.T. - structure solution

NMR spectrometers:

  • VARIAN INOVA 600 MHz
  • BRUKER AVANCE 600 MHz

Related Database Links:

PDB
DBJ BAI84986 BAM52020 BAM57597
EMBL CAB13253 CCU57937 CEI56537 CEJ76960 CJS27153
GB ADV96396 AFQ57311 AGA22143 AGE63229 AGG60748
REF NP_389263 WP_003245399 WP_015252208 WP_017695059 WP_024572583
SP O31683