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 5328

Title: Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase

Authors: Sahota, Gurmukh; Dixon, Bonnie; Huang, Yuanpeng; Aramini, James; Bhattacharya, Aneerban; Monleon, Daniel; Swapna, Gurla; Yin, Cuifeng; Anderson, Steve; Tejero, Roberto; Montelione, Gaetano

Citation: Sahota, Gurmukh; Dixon, Bonnie; Huang, Yuanpeng; Aramini, James; Bhattacharya, Aneerban; Monleon, Daniel; Swapna, Gurla; Yin, Cuifeng; Anderson, Steve; Montelione, Gaetano; Tejero, Roberto. "Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase"  J. Biomol. NMR ., .-..

Assembly members:
DNA Ligase Thermus Thermophilus BRCT, polymer, 92 residues, 10013 Da.

Natural source:   Common Name: T. thermophilus   Taxonomy ID: 274   Superkingdom: Eubacteria   Kingdom: Monera   Genus/species: Thermus thermophilus

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

Entity Sequences (FASTA):
DNA Ligase Thermus Thermophilus BRCT: MEKGGEALKGLTFVITGELS RPREEVKALLRRLGAKVTDS VSRKTSYLVVGENPGSKLEK ARALGVPTLTEEELYRLLEA RTGKKAEELVGS

Data sets:
Data typeCount
13C chemical shifts370
1H chemical shifts555
15N chemical shifts87

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1BRCT1

Entities:

Entity 1, BRCT 92 residues - 10013 Da.

1   METGLULYSGLYGLYGLUALALEULYSGLY
2   LEUTHRPHEVALILETHRGLYGLULEUSER
3   ARGPROARGGLUGLUVALLYSALALEULEU
4   ARGARGLEUGLYALALYSVALTHRASPSER
5   VALSERARGLYSTHRSERTYRLEUVALVAL
6   GLYGLUASNPROGLYSERLYSLEUGLULYS
7   ALAARGALALEUGLYVALPROTHRLEUTHR
8   GLUGLUGLULEUTYRARGLEULEUGLUALA
9   ARGTHRGLYLYSLYSALAGLUGLULEUVAL
10   GLYSER

Samples:

sample_1: DNA Ligase Thermus Thermophilus BRCT, [U-99% 13C; U-99% 15N], 1.3 mM

sample_2: DNA Ligase Thermus Thermophilus BRCT, [U-99% 15N], 1.3 mM

sample_conditions_1: pH: 6.2; temperature: 293 K; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
H_COTOCSYsample_1not availablesample_conditions_1
HBHA(CBCACO)NHsample_1not availablesample_conditions_1
13C-edited NOESYsample_1not availablesample_conditions_1
HNCOsample_1not availablesample_conditions_1
C_CBCA(CO)NHsample_1not availablesample_conditions_1
C_CBCANHsample_1not availablesample_conditions_1
NH_HSQCsample_1not availablesample_conditions_1
NH_HSQCsample_2not availablesample_conditions_1
H_CABBsample_1not availablesample_conditions_1
C_COBBsample_1not availablesample_conditions_1
HACACOCANHsample_1not availablesample_conditions_1
H_COBBsample_1not availablesample_conditions_1
C_COTOCSYsample_1not availablesample_conditions_1

Software:

VNMR6.1B v6.1B, Varian - data processing

NMRPipe v97.231.15.18, NIH Protein NMR Group - spectral processing

SPARKY v3.91 - peak picking

AutoAssign v1.7.6, Montelione - automated backbone 1H, 13C and 15N assignments

NMR spectrometers:

  • Varian UNITY Inova 500 MHz
  • Varian UNITY Inova 600 MHz

Related Database Links:

PDB
DBJ BAD70920
GB AAA27486 AAA27487 AAS81080 AEG33516 AFH38862
PIR A40363
REF WP_008632525 WP_011173171 WP_011228436 WP_014510389 WP_014629535
SP P26996 Q72JN8