BMRB Entry 30063
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30063
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Title: Structure of calmodulin in a complex with a peptide derived from a calmodulin-dependent kinase PubMed: 27499441
Deposition date: 2016-04-07 Original release date: 2016-09-01
Authors: Alphonse, S.; Lee, K.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.
Citation: Lee, K.; Alphonse, S.; Piserchio, A.; Tavares, C.; Giles, D.; Wellmann, R.; Dalby, K.; Ghose, R.. "Structural Basis for the Recognition of Eukaryotic Elongation Factor 2 Kinase by Calmodulin" Structure 24, 1441-1451 (2016).
Assembly members:
Calmodulin, polymer, 148 residues, 16721.350 Da.
Eukaryotic elongation factor 2 kinase, polymer, 27 residues, 3167.618 Da.
CALCIUM ION, non-polymer, 40.078 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):
Calmodulin: ADQLTEEQIAEFKEAFSLFD
KDGDGTITTKELGTVMRSLG
QNPTEAELQDMINEVDADGN
GTIDFPEFLTMMARKMKDTD
SEEEIREAFRVFDKDGNGYI
SAAELRHVMTNLGEKLTDEE
VDEMIREADIDGDGQVNYEE
FVQMMTAK
Eukaryotic elongation factor 2 kinase: SPANSFHFKEAWKHAIQKAK
HMPDPWA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 737 |
| 15N chemical shifts | 183 |
| 1H chemical shifts | 1125 |