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 16016

Title: NMR structure of TM0212 at 40 C

Deposition date: 2008-10-31 Original release date: 2012-07-19

Authors: Pedrini, Bill; Herrmann, Torsten; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt

Citation: Pedrini, Bill; Herrmann, Torsten; Mohanty, Biswaranjan; Geralt, Michael; Wuthrich, Kurt. "Chemical shift assignment of TM0212"  Not known ., .-..

Assembly members:
TM0212, polymer, 124 residues, Formula weight is not available

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

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

Entity Sequences (FASTA):
TM0212: MKMKKYTKTHEWVSIEDKVA TVGITNHAQEQLGDVVYVDL PEVGREVKKGEVVASIESVK AAADVYAPLSGKIVEVNEKL DTEPELINKDPEGEGWLFKM EISDEGELEDLLDEQAYQEF CAQE

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts128
1H chemical shifts825

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TM02121

Entities:

Entity 1, TM0212 124 residues - Formula weight is not available

1   METLYSMETLYSLYSTYRTHRLYSTHRHIS
2   GLUTRPVALSERILEGLUASPLYSVALALA
3   THRVALGLYILETHRASNHISALAGLNGLU
4   GLNLEUGLYASPVALVALTYRVALASPLEU
5   PROGLUVALGLYARGGLUVALLYSLYSGLY
6   GLUVALVALALASERILEGLUSERVALLYS
7   ALAALAALAASPVALTYRALAPROLEUSER
8   GLYLYSILEVALGLUVALASNGLULYSLEU
9   ASPTHRGLUPROGLULEUILEASNLYSASP
10   PROGLUGLYGLUGLYTRPLEUPHELYSMET
11   GLUILESERASPGLUGLYGLULEUGLUASP
12   LEULEUASPGLUGLNALATYRGLNGLUPHE
13   CYSALAGLNGLU

Samples:

sample_1: TM0212, [U-100% 13C; U-100% 15N], 2.4 ± 0.2 mM; NaP 25 mM; NaCl 50 mM; DTT, [U-2H], 5 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 313.0 K

Experiments:

NameSampleSample stateSample conditions
6D APSY HNCOCANHsample_1isotropicsample_conditions_1
5D APSY HACACONHsample_1isotropicsample_conditions_1
5D APSY CBCACONHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aliphatic NOESYsample_1isotropicsample_conditions_1
3D 1H-13C aromatic NOESYsample_1isotropicsample_conditions_1

Software:

GAPRO, Hiller and Fiorito - Automated analysis of 2D APSY NMR projection

MATCH, Volk and Herrmann - Automated backbone assignment

ASCAN, Fiorito and Herrmann - NOESY-based sidechain assignment

ATHNOS-CANDID, Herrmann and Guntert - peak assignment and constraint collection, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAD35304 ACB09088 AGL49136 AHD18024 AKE26151
REF NP_228027 WP_004082886 WP_010865076 WP_012310713
SP Q9WY55

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