BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25358

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25358

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Resonance assignments of the periplasmic domain of a cellulose-sensing trans-membrane anti-sigma factor from Clostridium thermocellum   PubMed: 25682099

Deposition date: 2014-11-20 Original release date: 2015-06-04

Authors: Ding, Xiaoke; Chen, Chao; Cui, Qiu; Li, Wenli; Feng, Yingang

Citation: Ding, Xiaoke; Chen, Chao; Cui, Qiu; Li, Wenli; Feng, Yingang. "Resonance assignments of the periplasmic domain of a cellulose-sensing trans-membrane anti-sigma factor from Clostridium thermocellum"  Biomol. NMR Assign. 9, 321-324 (2015).

Assembly members:
RsgI2-PD, polymer, 169 residues, Formula weight is not available

Natural source:   Common Name: Ruminiclostridium thermocellum   Taxonomy ID: 1515   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium thermocellum

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

Entity Sequences (FASTA):
RsgI2-PD: MYAYIDVDINPSIGLVIDKK EKVIDAKPLNNDAKPILDEA APKDMPLYDALSKILDISKK NGYINSADNIVLFSASINSG RNNVSESDKGIQEIISTLKD VAKDAGVKFEIIPSTEEDRQ KALDQNLSMGRYAIYVKAVE EGVNLNLEDARNLSVSEILG KLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts741
15N chemical shifts180
1H chemical shifts1207

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1RsgI2-PD1

Entities:

Entity 1, RsgI2-PD 169 residues - Formula weight is not available

1   METTYRALATYRILEASPVALASPILEASN
2   PROSERILEGLYLEUVALILEASPLYSLYS
3   GLULYSVALILEASPALALYSPROLEUASN
4   ASNASPALALYSPROILELEUASPGLUALA
5   ALAPROLYSASPMETPROLEUTYRASPALA
6   LEUSERLYSILELEUASPILESERLYSLYS
7   ASNGLYTYRILEASNSERALAASPASNILE
8   VALLEUPHESERALASERILEASNSERGLY
9   ARGASNASNVALSERGLUSERASPLYSGLY
10   ILEGLNGLUILEILESERTHRLEULYSASP
11   VALALALYSASPALAGLYVALLYSPHEGLU
12   ILEILEPROSERTHRGLUGLUASPARGGLN
13   LYSALALEUASPGLNASNLEUSERMETGLY
14   ARGTYRALAILETYRVALLYSALAVALGLU
15   GLUGLYVALASNLEUASNLEUGLUASPALA
16   ARGASNLEUSERVALSERGLUILELEUGLY
17   LYSLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: RsgI2-PD, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 150 mM; DSS 0.02 % w/v

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

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