BMRB Entry 16942

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16942
MolProbity Validation Chart

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Title:
Solution NMR Structure () from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518
Deposition date:
2010-05-21
Original release date:
2012-08-02
Authors:
Eletsky, Alexander; Sukumaran, Dinesh; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Liu, Jinfeng; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Sukumaran, Dinesh; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Liu, Jinfeng; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of ydhK C-terminal Domain from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518"  To be published ., .-..

Assembly members:

Assembly members:
SR518, polymer, 132 residues, 14611.442 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SR518: MKVGSQVIINTSHMKGMKGA EATVTGAYDTTAYVVSYTPT NGGQRVDHHKWVIQEEIKDA GDKTLQPGDQVILEASHMKG MKGATAEIDSAEKTTVYMVD YTSTTSGEKVKNHKWVTEDE LSAKLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts542
15N chemical shifts135
1H chemical shifts862
residual dipolar couplings195

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SR5181

Entities:

Entity 1, SR518 132 residues - 14611.442 Da.

Residues 2-124 correspond to the range 83-205 of the native protein. Residues 125-132 represent a non-native affinity tag, and residue one is due to the initiation codon.

1   METLYSVALGLYSERGLNVALILEILEASN
2   THRSERHISMETLYSGLYMETLYSGLYALA
3   GLUALATHRVALTHRGLYALATYRASPTHR
4   THRALATYRVALVALSERTYRTHRPROTHR
5   ASNGLYGLYGLNARGVALASPHISHISLYS
6   TRPVALILEGLNGLUGLUILELYSASPALA
7   GLYASPLYSTHRLEUGLNPROGLYASPGLN
8   VALILELEUGLUALASERHISMETLYSGLY
9   METLYSGLYALATHRALAGLUILEASPSER
10   ALAGLULYSTHRTHRVALTYRMETVALASP
11   TYRTHRSERTHRTHRSERGLYGLULYSVAL
12   LYSASNHISLYSTRPVALTHRGLUASPGLU
13   LEUSERALALYSLEUGLUHISHISHISHIS
14   HISHIS

Samples:

NC5-phage_sample: SR518, [U-5% 13C; U-100% 15N], 0.5 mM; sodium chloride 180 mM; DTT 3.5 mM; TRIS 7 mM; sodium azide 0.014%; DSS 14 uM; Pf1 phage 10.5 g/L; H2O 88%; D2O 12%

NC_sample: SR518, [U-100% 13C; U-100% 15N], 0.4 mM; sodium chloride 100 mM; DTT 5 mM; TRIS 10 mM; sodium azide 0.02%; DSS 20 uM; H2O 95%; D2O 5%

NC5_sample: SR518, [U-5% 13C; U-100% 15N], 0.7 mM; sodium chloride 100 mM; DTT 5 mM; TRIS 10 mM; sodium azide 0.02%; DSS 20 uM; H2O 95%; D2O 5%

NC5-PEG_sample: SR518, [U-5% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; DTT 5 mM; TRIS 10 mM; sodium azide 0.02%; DSS 20 uM; PEG 3.5%; H2O 88%; D2O 12%

sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 180 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HN(CA)CONC_sampleisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNC_sampleisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNC_sampleisotropicsample_conditions_1
3D (H)CCH-COSY aliphaticNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticNC_sampleisotropicsample_conditions_1
3D (H)CCH-COSY aromaticNC_sampleisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5_sampleisotropicsample_conditions_1
2D 1H-15N LR-HSQC for HistidineNC5_sampleisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5-PEG_sampleanisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCNC5-phage_sampleanisotropicsample_conditions_2

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

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

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

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

XEASY, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection

VNMRJ, Varian - collection

CARA v1.8.4, Keller and Wuthrich - data analysis,peak picking,chemical shift assignment

PROSA v6.4, Guntert - processing

Molmol v2K.2, Koradi, Billeter and Wuthrich - visualization

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis

PSVS v1.3, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 700 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