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 17989

Title: NMR resonance assignment of the UUP protein C-terminal domain   PubMed: 22287065

Deposition date: 2011-10-11 Original release date: 2012-01-31

Authors: Carlier, Ludovic; Haase, Sander; Lequin, Olivier

Citation: Carlier, Ludovic; Haase, A. Sander; Burgos Zepeda, Monica; Dassa, Elie; Lequin, Olivier. "Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein."  Biomol. NMR Assignments 6, 197-200 (2012).

Assembly members:
UUP, polymer, 112 residues, 12563 Da.

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):
UUP: GSHMGQQEQYVALKQPAVKK TEEAAAAKAETVKRSSSKLS YKLQRELEQLPQLLEDLEAK LEALQTQVADASFFSQPHEQ TQKVLADMAAAEQELEQAFE RWEYLEALKNGG

Data sets:
Data typeCount
13C chemical shifts478
15N chemical shifts113
1H chemical shifts771

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UUP protein C-terminal domain1

Entities:

Entity 1, UUP protein C-terminal domain 112 residues - 12563 Da.

Residues 1-4 represent a non-native affinity tag. Gly-5 corresponds to Gly-528 in the native UUP protein sequence.

1   GLYSERHISMETGLYGLNGLNGLUGLNTYR
2   VALALALEULYSGLNPROALAVALLYSLYS
3   THRGLUGLUALAALAALAALALYSALAGLU
4   THRVALLYSARGSERSERSERLYSLEUSER
5   TYRLYSLEUGLNARGGLULEUGLUGLNLEU
6   PROGLNLEULEUGLUASPLEUGLUALALYS
7   LEUGLUALALEUGLNTHRGLNVALALAASP
8   ALASERPHEPHESERGLNPROHISGLUGLN
9   THRGLNLYSVALLEUALAASPMETALAALA
10   ALAGLUGLNGLULEUGLUGLNALAPHEGLU
11   ARGTRPGLUTYRLEUGLUALALEULYSASN
12   GLYGLY

Samples:

sample_1: UUP, [U-100% 15N], 0.7 mM; sodium chloride 170 mM; sodium phosphate 30 mM; DSS 0.111 mM; leupeptine 1 uM; pepstatine 1 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: UUP, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 170 mM; sodium phosphate 30 mM; DSS 0.111 mM; leupeptine 1 uM; pepstatine A 1 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: UUP, [U-100% 13C; U-100% 15N], 0.8 mM; sodium chloride 170 mM; sodium phosphate 30 mM; leupeptine 1 uM; pepstatine A 1 uM; sodium azide 0.02%; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment, collection, peak picking

TOPSPIN v2.0, Bruker Biospin - geometry optimization

NMR spectrometers:

  • Bruker Avance III 500 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA35707 BAB34456 BAG76534 BAI24392 BAI29842
EMBL CAA70589 CAP75412 CAQ31477 CAQ88615 CAQ97854
GB AAC74035 AAG55435 AAN42579 AAN79553 AAP16463
REF NP_309060 NP_415469 NP_706872 WP_000053029 WP_000053031
SP P43672

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