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 10121

Title: Solution structure of a putative peptidyl-tRNA hydrolase domain in a mouse hypothetical protein

Authors: Nameki, N.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.

Citation: Nameki, N.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.. "Solution structure of a peptidyl-tRNA hydrolase domain of a hypothetical protein"  Not known ., .-..

Assembly members:
peptidyl-tRNA hydrolase domain, polymer, 112 residues, Formula weight is not available

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
peptidyl-tRNA hydrolase domain: GSSGSSGEHAKQASSYIPLD RLSISYCRSSGPGGQNVNKV NSKAEVRFHLASADWIEEPV RQKIALTHKNKINKAGELVL TSESSRYQFRNLAECLQKIR DMIAEASGPSSG

Data sets:
Data typeCount
13C chemical shifts455
15N chemical shifts117
1H chemical shifts740

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1immature colon carcinoma transcript 11

Entities:

Entity 1, immature colon carcinoma transcript 1 112 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUHISALA
2   LYSGLNALASERSERTYRILEPROLEUASP
3   ARGLEUSERILESERTYRCYSARGSERSER
4   GLYPROGLYGLYGLNASNVALASNLYSVAL
5   ASNSERLYSALAGLUVALARGPHEHISLEU
6   ALASERALAASPTRPILEGLUGLUPROVAL
7   ARGGLNLYSILEALALEUTHRHISLYSASN
8   LYSILEASNLYSALAGLYGLULEUVALLEU
9   THRSERGLUSERSERARGTYRGLNPHEARG
10   ASNLEUALAGLUCYSLEUGLNLYSILEARG
11   ASPMETILEALAGLUALASERGLYPROSER
12   SERGLY

Samples:

sample_1: peptidyl-tRNA hydrolase domain, [U-13C; U-15N], 1.7 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.704, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - structure solution

OPALp, Guntert, P. - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB22632 BAB22691 BAE35961
GB AAH28523 EDL34481 EDL34486
REF NP_081005 XP_006534127 XP_006997809
SP Q8R035