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 16007

Title: NMR structure of the protein TM1367   PubMed: 20944235

Authors: Mohanty, Biswaranjan; Pedrini, Bill; Serrano, Pedro; Geralt, Michel; Horst, Reto; Wilson, Ian; Wuthrich, Kurt

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Pedrini, Bill; Jaudzems, Kristaps; Geralt, Michael; Horst, Reto; Herrmann, Torsten; Elsliger, Marc Andre; Wilson, Ian; Wuthrich, Kurt. "Comparison of NMR and crystal structures for the proteins TM1112 and TM1367."  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66, 1381-1392 (2010).

Assembly members:
TM1367, polymer, 124 residues, 13923 Da.

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: thermotogae   Genus/species: Thermotoga maritima

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

Entity Sequences (FASTA):
TM1367: MRVELLFESGKCVIDLNEEY EVVKLLKEKIPFESVVNTWG EEIYFSTPVNVQKMENPREV VEIGDVGYWPPGKALCLFFG KTPMSDDKIQPASAVNVIGK IVEGLEDLKKIKDGEKVAVR FASS

Data sets:
Data typeCount
13C chemical shifts439
15N chemical shifts126
1H chemical shifts920

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM13671

Entities:

Entity 1, TM1367 124 residues - 13923 Da.

1   METARGVALGLULEULEUPHEGLUSERGLY
2   LYSCYSVALILEASPLEUASNGLUGLUTYR
3   GLUVALVALLYSLEULEULYSGLULYSILE
4   PROPHEGLUSERVALVALASNTHRTRPGLY
5   GLUGLUILETYRPHESERTHRPROVALASN
6   VALGLNLYSMETGLUASNPROARGGLUVAL
7   VALGLUILEGLYASPVALGLYTYRTRPPRO
8   PROGLYLYSALALEUCYSLEUPHEPHEGLY
9   LYSTHRPROMETSERASPASPLYSILEGLN
10   PROALASERALAVALASNVALILEGLYLYS
11   ILEVALGLUGLYLEUGLUASPLEULYSLYS
12   ILELYSASPGLYGLULYSVALALAVALARG
13   PHEALASERSER

Samples:

sample_1: DTT 0.5 mM; D10-DTT 4.5 mM; sodium azide 0.03%; sodium chloride 50 mM; sodium phosphate 25 mM; D2O 10%; H2O 90%; TM1367, [U-98% 13C; U-98% 15N], 1.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D [15N,1H] HSQCsample_1isotropicsample_conditions_1
2D [13C,1H] HSQCsample_1isotropicsample_conditions_1
3D 15N - resolved [1H,1H] NOESYsample_1isotropicsample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aliphatic 13Csample_1isotropicsample_conditions_1
3D 13C-resolved [1H,1H] NOESY, aromatic 13Csample_1isotropicsample_conditions_1
4D-APSY-HACANHsample_1isotropicsample_conditions_1
5D-APSY-HACACONHsample_1isotropicsample_conditions_1
5D-APSY-CBCACONHsample_1isotropicsample_conditions_1

Software:

CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - data analysis

Molmol, Koradi, Billeter and Wuthrich - data analysis

TOPSPIN v1.3, Bruker Biospin - processing

ASCAN, (ASCAN)-Fiorito,Herrmann,Damberger and Wuthrich - chemical shift assignment

MATCH, (MATCH)-Volk, Herrmann and K. Wuthrich - chemical shift assignment

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAD36437 ABQ47429 ACB09806 ADA67518 AGL50298
REF NP_229168 WP_004081563 WP_011943885 WP_012311149 WP_038034479