BMRB Entry 5217

Title:
Solution Structure and DNA Binding Properties of the C-Terminal Domain of UvrC from E. coli
Deposition date:
2001-11-23
Original release date:
2003-01-14
Authors:
Singh, Shanteri; Folkers, Gert; Bonvin, Alexandre; Wechselberger, Rainer; Niztayev, Alidin; Boelens, Rolf; Kaptein, Robert
Citation:

Citation: Singh, Shanteri; Folkers, Gert; Bonvin, Alexandre; Boelens, Rolf; Wechselberger, Rainer; Niztayev, Alidin; Kaptein, Robert. "Solution Structure and DNA-binding Properties of the C-Terminal Domain of UvrC from E. coli"  EMBO J. 21, 6257-6266 (2002).
PubMed: 12426397

Assembly members:

Assembly members:
UV Repair protein C, polymer, 78 residues, 8562.82 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts67
1H chemical shifts447

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UvrC CTD1

Entities:

Entity 1, UvrC CTD 78 residues - 8562.82 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METASNTHRSERSERLEUGLUTHRILEGLU
4   GLYVALGLYPROLYSARGARGGLNMETLEU
5   LEULYSTYRMETGLYGLYLEUGLNGLYLEU
6   ARGASNALASERVALGLUGLUILEALALYS
7   VALPROGLYILESERGLNGLYLEUALAGLU
8   LYSILEPHETRPSERLEULYSHIS

Samples:

sample_1: UV Repair protein C, [U-15N], 1.0 mM; NaCl 300 mM; sodium phosphate buffer 50 mM

sample_2: UV Repair protein C, [U-15N; U-13C], 1.0 mM; NaCl 300 mM; sodium phosphate buffer 50 mM

Ex-cond_1: ionic strength: 0.3 M; pH: 6.8 na; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
HNCAnot availablenot availableEx-cond_1
HNCOnot availablenot availableEx-cond_1
HN(CO)CAnot availablenot availableEx-cond_1
CBCANHnot availablenot availableEx-cond_1
1H-15N TOCSY HSQCnot availablenot availableEx-cond_1
1H-15N NOESY HSQCnot availablenot availableEx-cond_1
1H-13C-H(C)CH TOCSYnot availablenot availableEx-cond_1
1H-13C-(H)CCH TOCSYnot availablenot availableEx-cond_1
1H-15N NOESY HSQCnot availablenot availableEx-cond_1
2D-NOESYnot availablenot availableEx-cond_1

Software:

NMRPipe v1.8 - NMR data processing

NMRView v4.1.3 - NMR data analysis

ARIA v1.0 - ambiguous NOE assignment, structure calculation

CNS v1.0 - structure calculation

NMR spectrometers:

  • Bruker DRX 500 MHz
  • Bruker AMX 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
GB AHR43889 AHS24459 AHS50436 AHS52317 EFZ51080
REF WP_001345512 WP_023252848

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks