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 15933

Title: NOGO66 in DPC.   PubMed: 20351248

Authors: Cocco, Melanie; Schulz, Jessica; Vasudevan, Sheeja

Citation: Vasudevan, Sheeja; Schulz, Jessica; Zhou, Chunyi; Cocco, Melanie. "Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface."  Proc. Natl. Acad. Sci. U.S.A. 107, 6847-6851 (2010).

Assembly members:
NOGO, polymer, 79 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: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
NOGO: MHHHHHHLVPRGMRIYKGVI QAIQKSDEGHPFRAYLESEV AISEELVQKYSNSALGHVNS TIKELRRLFLVDDLVDSLK

Data sets:
Data typeCount
13C chemical shifts200
15N chemical shifts67
1H chemical shifts432

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NOGO1

Entities:

Entity 1, NOGO 79 residues - Formula weight is not available

1   METHISHISHISHISHISHISLEUVALPRO
2   ARGGLYMETARGILETYRLYSGLYVALILE
3   GLNALAILEGLNLYSSERASPGLUGLYHIS
4   PROPHEARGALATYRLEUGLUSERGLUVAL
5   ALAILESERGLUGLULEUVALGLNLYSTYR
6   SERASNSERALALEUGLYHISVALASNSER
7   THRILELYSGLULEUARGARGLEUPHELEU
8   VALASPASPLEUVALASPSERLEULYS

Samples:

sample_1: NOGO 0.5-1.0 mM; NOGO, [U-100% 15N], 0.5-1.0 mM; NOGO, [U-100% 13C], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.0 M; pH: 4.0; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

ANALYSIS v1.0.15, CCPN - chemical shift assignment, data analysis, peak picking

NMRDraw v2.2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

BMRB 16257
PDB
DBJ BAA74909 BAA83712 BAB18927 BAB18928 BAC75974
EMBL CAB71027 CAB71028 CAB99248 CAB99249 CAH93187
GB AAD31019 AAD31020 AAD31021 AAG12176 AAG12177
REF NP_001106692 NP_001126875 NP_001192056 NP_065393 NP_114019
SP Q99P72 Q9JK11 Q9NQC3
TPG DAA24679