BMRB Entry 30065
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PDB ID: 5jdp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30065
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Title: E73V mutant of the human voltage-dependent anion channel PubMed: 27461260
Deposition date: 2016-04-17 Original release date: 2016-08-08
Authors: Jaremko, M.; Jaremko, L.; Villinger, S.; Schmidt, C.; Giller, K.; Griesinger, C.; Becker, S.; Zweckstetter, M.
Citation: Jaremko, M.; Jaremko, L.; Villinger, S.; Schmidt, C.; Giller, K.; Griesinger, C.; Becker, S.; Zweckstetter, M.. "High resolution determination of the dynamic structure of membrane proteins" Angew. Chem. Int. Ed. Engl. 55, 10518-10521 (2016).
Assembly members:
Voltage-dependent anion-selective channel protein 1, polymer, 285 residues, 30977.699 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Voltage-dependent anion-selective channel protein 1: SAVPPTYADLGKSARDVFTK
GYGFGLIKLDLKTKSENGLE
FTSSGSANTETTKVTGSLET
KYRWTEYGLTFTVKWNTDNT
LGTEITVEDQLARGLKLTFD
SSFSPNTGKKNAKIKTGYKR
EHINLGCDMDFDIAGPSIRG
ALVLGYEGWLAGYQMNFETA
KSRVTQSNFAVGYKTDEFQL
HTNVNDGTEFGGSIYQKVNK
KLETAVNLAWTAGNSNTRFG
IAAKYQIDPDACFSAKVNNS
SLIGLGYTQTLKPGIKLTLS
ALLDGKNVNAGGHKLGLGLE
FQARS
- assigned_chemical_shifts
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 466 |
| 15N chemical shifts | 252 |
| 1H chemical shifts | 253 |
| T1 relaxation values | 534 |
| T2 relaxation values | 534 |
Additional metadata:
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