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 18550

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18550
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Solution-state NMR of prion protein mutant V210I at pH 7   PubMed: 22947063

Deposition date: 2012-06-26 Original release date: 2012-09-17

Authors: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Legname, Giuseppe; Plavec, Janez

Citation: Biljan, Ivana; Ilc, Gregor; Giachin, Gabriele; Plavec, Janez; Legname, Giuseppe. "Structural Rearrangements at Physiological pH: Nuclear Magnetic Resonance Insights from the V210I Human Prion Protein Mutant."  Biochemistry 51, 7465-7474 (2012).

Assembly members:
V210I, polymer, 147 residues, 16654.660 Da.

Natural source:   Common Name: Humans   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
V210I: GAMDPGQGGGTHSQWNKPSK PKTNMKHMAGAAAAGAVVGG LGGYMLGSAMSRPIIHFGSD YEDRYYRENMHRYPNQVYYR PMDEYSNQNNFVHDCVNITI KQHTVTTTTKGENFTETDVK MMERVIEQMCITQYERESQA YYQRGSS

Data sets:
Data typeCount
13C chemical shifts460
15N chemical shifts132
1H chemical shifts915

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1V210I1

Entities:

Entity 1, V210I 147 residues - 16654.660 Da.

The five extra residues at the N-terminus are remnant of the tobacco etch virus (TEV) cleavege.

1   GLYALAMETASPPROGLYGLNGLYGLYGLY
2   THRHISSERGLNTRPASNLYSPROSERLYS
3   PROLYSTHRASNMETLYSHISMETALAGLY
4   ALAALAALAALAGLYALAVALVALGLYGLY
5   LEUGLYGLYTYRMETLEUGLYSERALAMET
6   SERARGPROILEILEHISPHEGLYSERASP
7   TYRGLUASPARGTYRTYRARGGLUASNMET
8   HISARGTYRPROASNGLNVALTYRTYRARG
9   PROMETASPGLUTYRSERASNGLNASNASN
10   PHEVALHISASPCYSVALASNILETHRILE
11   LYSGLNHISTHRVALTHRTHRTHRTHRLYS
12   GLYGLUASNPHETHRGLUTHRASPVALLYS
13   METMETGLUARGVALILEGLUGLNMETCYS
14   ILETHRGLNTYRGLUARGGLUSERGLNALA
15   TYRTYRGLNARGGLYSERSER

Samples:

v210i_pH7: V210I, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 90%; D2O, [U-2H], 10%; Tris buffer 20 mM; KCl 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.2; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCv210i_pH7isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlyv210i_pH7isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticv210i_pH7isotropicsample_conditions_1
2D 1H-13C HSQC aromaticv210i_pH7isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticv210i_pH7isotropicsample_conditions_1
3D CBCA(CO)NHv210i_pH7isotropicsample_conditions_1
3D C(CO)NHv210i_pH7isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, Elmar Krieger - geometry optimization

NMR spectrometers:

  • Varian VNMRS 800 MHz

Related Database Links:

PDB
BMRB 15676 16743 16757 17714 17756 17757 17780 18426 19268 4379 4402 4434 4620 4641 4736
DBJ BAA00011 BAF62360 BAG32276 BAG32277 BAG32278
EMBL CAA58442 CAG46836 CAG46869
GB AAA19664 AAA60182 AAA68632 AAA68633 AAB59442
REF NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592
SP P04156 P40252 P61766 P61767 P61768

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