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 7055

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR7055

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Title: 1H, 13C, and 15N Chemical Shift Assignments for PTH from Mycobacterium tuberculosis H37Rv   PubMed: 16821126

Deposition date: 2006-04-07 Original release date: 2006-08-07

Authors: Bal, Naresh; Agrawal, Himanshu; Meher, Akshaya; Pulavarti, Surya; Jain, Anupam; Kelly, Geoff; Frenkiel, Thomas; Pastore, Annalisa; Arora, Ashish

Citation: Bal, Naresh; Agrawal, Himanshu; Meher, Akshaya; Pulavarti, Surya; Jain, Anupam; Kelly, Geoff; Frenkiel, Thomas; Pastore, Annalisa; Arora, Ashish. "NMR assignment of peptidyl-tRNA hydrolase from Mycobacterium tuberculosis H37Rv"  J. Biomol. NMR 36, 53-53 (2006).

Assembly members:
PTH, polymer, 191 residues, 20455.3301 Da.

Natural source:   Common Name: Mycobacterium tuberculosis H37Rv   Taxonomy ID: 83332   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
PTH: MAEPLLVVGLGNPGANYART RHNLGFVVADLLAARLGAKF KAHKRSGAEVATGRSAGRSL VLAKPRCYMNESGRQIGPLA KFYSVAPANIIVIHDDLDLE FGRIRLKIGGGEGGHNGLRS VVAALGTKDFQRVRIGIGRP PGRKDPAAFVLENFTPAERA EVPTICEQAADATELLIEQG MEPAQNRVHAW

Data sets:
Data typeCount
13C chemical shifts730
15N chemical shifts171
1H chemical shifts1058

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTH monomer1

Entities:

Entity 1, PTH monomer 191 residues - 20455.3301 Da.

1   METALAGLUPROLEULEUVALVALGLYLEU
2   GLYASNPROGLYALAASNTYRALAARGTHR
3   ARGHISASNLEUGLYPHEVALVALALAASP
4   LEULEUALAALAARGLEUGLYALALYSPHE
5   LYSALAHISLYSARGSERGLYALAGLUVAL
6   ALATHRGLYARGSERALAGLYARGSERLEU
7   VALLEUALALYSPROARGCYSTYRMETASN
8   GLUSERGLYARGGLNILEGLYPROLEUALA
9   LYSPHETYRSERVALALAPROALAASNILE
10   ILEVALILEHISASPASPLEUASPLEUGLU
11   PHEGLYARGILEARGLEULYSILEGLYGLY
12   GLYGLUGLYGLYHISASNGLYLEUARGSER
13   VALVALALAALALEUGLYTHRLYSASPPHE
14   GLNARGVALARGILEGLYILEGLYARGPRO
15   PROGLYARGLYSASPPROALAALAPHEVAL
16   LEUGLUASNPHETHRPROALAGLUARGALA
17   GLUVALPROTHRILECYSGLUGLNALAALA
18   ASPALATHRGLULEULEUILEGLUGLNGLY
19   METGLUPROALAGLNASNARGVALHISALA
20   TRP

Samples:

sample_1: PTH, [U-15N; U-13C], 0.8 mM; sodium phosphate 20 mM; sodium chloride 50 mM; NaN3 0.1%

conditions_1: ionic strength: 50 mM; pH: 6.5; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
1H15N HSQCsample_1not availableconditions_1
HNCAsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
CBCA(CO)NHsample_1not availableconditions_1
HCCH-TOCSYsample_1not availableconditions_1
H(CCCO)NH-TOCSYsample_1not availableconditions_1
(H)CC(CO)NH-TOCSYsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HN(CA)COsample_1not availableconditions_1
15N-edited NOESY-HSQCsample_1not availableconditions_1

Software:

No software information available

NMR spectrometers:

  • Varian UnityINOVA 600 MHz
  • Bruker Avance 600 MHz
  • Varian UnityINOVA 800 MHz

Related Database Links:

PDB
DBJ BAH25334 BAL64931 BAQ04946 GAA44770
EMBL CAD93902 CAL71058 CCC26096 CCC43355 CCC63630
GB AAK45293 ABQ72757 ABR05375 ACT26062 AEB05122
REF NP_215530 NP_335479 NP_854698 WP_003405251 WP_003916286
SP A1KHF2 A5U157 C1AM05 P65866 P9WHN6

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