BMRB Entry 16671
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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/BMR16671
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Title: Mechanism for the selective interaction of C-terminal EH-domain proteins with specific NPF-containing partners PubMed: 20106972
Deposition date: 2010-01-11 Original release date: 2010-02-23
Authors: KIEKEN, Fabien; SHARMA, Mahak; JOVIC, Marko; PANAPAKKAM GIRIDHARAN, Sai Srnivas; NASLAVSKY, Naava; CAPLAN, Steve; SORGEN, Paul
Citation: Kieken, Fabien; Sharma, Mahak; Jovic, Marko; Giridharan, Sai Srinivas Panapakkam; Naslavsky, Naava; Caplan, Steve; Sorgen, Paul. "Mechanism for the Selective Interaction of C-terminal Eps15 Homology Domain Proteins with Specific Asn-Pro-Phe-containing Partners." J. Biol. Chem. 285, 8687-8694 (2010).
Assembly members:
EH_domain_of_EHD1, polymer, 105 residues, 11654.459 Da.
MICAL_L1_like_peptide, polymer, 15 residues, 1419.530 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):
EH_domain_of_EHD1: GPLGSDDVEWVVGKDKPTYD
EIFYTLSPVNGKITGANAKK
EMVKSKLPNTVLGKIWKLAD
VDKDGLLDDEEFALANHLIK
VKLEGHELPADLPPHLVPPS
KRRHE
MICAL_L1_like_peptide: LESKPYNPFEEEEED
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 365 |
15N chemical shifts | 92 |
1H chemical shifts | 823 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EH_domain_of_EHD1 | 1 |
2 | MICAL_L1_like_peptide | 2 |
3 | Calcium ion | 3 |
Entities:
Entity 1, EH_domain_of_EHD1 105 residues - 11654.459 Da.
1 | GLY | PRO | LEU | GLY | SER | ASP | ASP | VAL | GLU | TRP | ||||
2 | VAL | VAL | GLY | LYS | ASP | LYS | PRO | THR | TYR | ASP | ||||
3 | GLU | ILE | PHE | TYR | THR | LEU | SER | PRO | VAL | ASN | ||||
4 | GLY | LYS | ILE | THR | GLY | ALA | ASN | ALA | LYS | LYS | ||||
5 | GLU | MET | VAL | LYS | SER | LYS | LEU | PRO | ASN | THR | ||||
6 | VAL | LEU | GLY | LYS | ILE | TRP | LYS | LEU | ALA | ASP | ||||
7 | VAL | ASP | LYS | ASP | GLY | LEU | LEU | ASP | ASP | GLU | ||||
8 | GLU | PHE | ALA | LEU | ALA | ASN | HIS | LEU | ILE | LYS | ||||
9 | VAL | LYS | LEU | GLU | GLY | HIS | GLU | LEU | PRO | ALA | ||||
10 | ASP | LEU | PRO | PRO | HIS | LEU | VAL | PRO | PRO | SER | ||||
11 | LYS | ARG | ARG | HIS | GLU |
Entity 2, MICAL_L1_like_peptide 15 residues - 1419.530 Da.
1 | LEU | GLU | SER | LYS | PRO | TYR | ASN | PRO | PHE | GLU | ||||
2 | GLU | GLU | GLU | GLU | ASP |
Entity 3, Calcium ion - Ca - 40.078 Da.
1 | CA |
Samples:
sample_1: EH domain of EHD1, [U-99% 13C; U-99% 15N], 0.6 mM; MICAL L1 like peptide 2 mM; Tris 20 mM; Kcl 100 mM; Cac12 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 13CFiltered-13CfilteredNOESY | sample_1 | isotropic | sample_conditions_1 |
2D 13C-filtered-15N editedNOESY | sample_1 | isotropic | sample_conditions_1 |
2D 15N filtered Noesy | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ProcheckNMR, Laskowski and MacArthur - data analysis
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
BMRB | 15279 16179 16180 16181 |
PDB | |
DBJ | BAB28540 BAC40684 BAE32742 BAE35499 BAE35852 |
EMBL | CAH90816 |
GB | AAB81204 AAD45423 AAF24223 AAG02009 AAH37094 |
REF | NP_001011939 NP_001015578 NP_001125465 NP_001162473 NP_001248124 |
SP | Q5E9R3 Q5RBP4 Q641Z6 Q9H4M9 Q9WVK4 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts