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 50218

Title: UvrD_CTD

Deposition date: 2020-03-29 Original release date: 2020-10-12

Authors: Kawale, Ashish; Burmann, Bjorn

Citation: Kawale, Ashish; Burmann, Bjorn. "UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain"  Commun. Biol. ., .-..

Assembly members:
entity_1, polymer, 76 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: RLRATVSRPVSHQRMGTPMV ENDSGYKLGQRVRHAKFGEG TIVNMEGSGEHSRLQVAFQG QGIKWLVAAYARLESV

Data sets:
Data typeCount
13C chemical shifts315
15N chemical shifts71
1H chemical shifts482

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UvrD_CTD1

Entities:

Entity 1, UvrD_CTD 76 residues - Formula weight is not available

1   ARGLEUARGALATHRVALSERARGPROVAL
2   SERHISGLNARGMETGLYTHRPROMETVAL
3   GLUASNASPSERGLYTYRLYSLEUGLYGLN
4   ARGVALARGHISALALYSPHEGLYGLUGLY
5   THRILEVALASNMETGLUGLYSERGLYGLU
6   HISSERARGLEUGLNVALALAPHEGLNGLY
7   GLNGLYILELYSTRPLEUVALALAALATYR
8   ALAARGLEUGLUSERVAL

Samples:

sample_1: UvrD_CTD, [U-100% 13C; U-100% 15N], 650 uM; potassium phosphate buffer 20 mM; KCl 50 mM

sample_conditions_1: ionic strength: 0.070 M; pH: 6.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
2D HBCBCGCDHDsample_1isotropicsample_conditions_1
2D HBCBCGCDCEHEsample_1isotropicsample_conditions_1
15N-(1H) NOEsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRFAM-SPARKY v1.413 - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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