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 19625

Title: TNPX

Deposition date: 2013-11-20 Original release date: 2014-11-24

Authors: Headey, S.; Sivakumaran, A.; Adams, V.; Rodgers, A.; Rood, J.; Scanlon, M.; Wilce, M.

Citation: Headey, S.; Sivakumaran, A.; Adams, V.; Rodgers, A.; Scanlon, J.; Wilce, M.. "Solution Structure and DNA Binding of the Catalytic of the Large Serine Resolvase Tnpx"  To be Published ., .-..

Assembly members:
TNPX, polymer, 120 residues, 13793.345 Da.

Natural source:   Common Name: firmicutes   Taxonomy ID: 1502   Superkingdom: Bacteria   Kingdom: not available   Genus/species: CLOSTRIDIUM PERFRINGENS

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
TNPX: GSRTSRITALYERLSRDDDL TGESNSITNQKKYLEDYARR NGFENIRHFTDDGFSGVNFN RPGFQSLIKEVEAGNVETLI VKDMSRLGRNYLQVGFYTEV LFPQKNVRFLAINNSIDSNN

Data sets:
Data typeCount
13C chemical shifts494
15N chemical shifts130
1H chemical shifts824

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TNPX1

Entities:

Entity 1, TNPX 120 residues - 13793.345 Da.

1   GLYSERARGTHRSERARGILETHRALALEU
2   TYRGLUARGLEUSERARGASPASPASPLEU
3   THRGLYGLUSERASNSERILETHRASNGLN
4   LYSLYSTYRLEUGLUASPTYRALAARGARG
5   ASNGLYPHEGLUASNILEARGHISPHETHR
6   ASPASPGLYPHESERGLYVALASNPHEASN
7   ARGPROGLYPHEGLNSERLEUILELYSGLU
8   VALGLUALAGLYASNVALGLUTHRLEUILE
9   VALLYSASPMETSERARGLEUGLYARGASN
10   TYRLEUGLNVALGLYPHETYRTHRGLUVAL
11   LEUPHEPROGLNLYSASNVALARGPHELEU
12   ALAILEASNASNSERILEASPSERASNASN

Samples:

sample_1: TNPX, [U-99% 13C; U-99% 15N], 0.4 mM; D2O 10%; sodium chloride 150 mM; sodium phosphate 20 mM; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)CO 3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)C(CO)NHsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSY 2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1 NOESYsample_1isotropicsample_conditions_1
2D 1H-15N NOEsample_1isotropicsample_conditions_1

Software:

CNSSOLVE v1.2, BRUNGER, ADAMS, CLORE, GROS, NILGES - refinement

XEASY v1.4, Bartels et al. - structure solution

TOPSPIN, Bruker Biospin - processing

VNMRJ, Varian - collection

NMR spectrometers:

  • VARIAN INOVA 600 MHz

Related Database Links:

PDB
EMBL CUP39613 CUQ38785
GB AAB51419 EEA83356 EEF93031 ENZ31332 EQJ53319
REF WP_002570991 WP_004611674 WP_006506523

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