BMRB Entry 4959
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4959
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Koshiba, Seizo; Kigawa, Takanori; Kikuchi, Akira; Yokoyama, Shigeyuki. "Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin" J. Struct. Func. Genomics 2, 1-8 (2001).
Assembly members:
epsin ENTH domain, polymer, 148 residues, Formula weight is not available
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 Vector: pGEX2T
Entity Sequences (FASTA):
epsin ENTH domain: GSSRMSTSSLRRQMKNIVHN
YSEAEIKVREATSNDPWGPS
SSLMSEIADLTYNVVAFSEI
MSMIWKRLNDHGKNWRHVYK
AMTLMEYLIKTGSERVSQQC
KENMYAVQTLKDFQYVDRDG
KDQGVNVREKAKQLVALLRD
EDRLREER
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 920 |
| 13C chemical shifts | 606 |
| 15N chemical shifts | 142 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | epsin ENTH domain | 1 |
Entities:
Entity 1, epsin ENTH domain 148 residues - Formula weight is not available
| 1 | GLY | SER | SER | ARG | MET | SER | THR | SER | SER | LEU | ||||
| 2 | ARG | ARG | GLN | MET | LYS | ASN | ILE | VAL | HIS | ASN | ||||
| 3 | TYR | SER | GLU | ALA | GLU | ILE | LYS | VAL | ARG | GLU | ||||
| 4 | ALA | THR | SER | ASN | ASP | PRO | TRP | GLY | PRO | SER | ||||
| 5 | SER | SER | LEU | MET | SER | GLU | ILE | ALA | ASP | LEU | ||||
| 6 | THR | TYR | ASN | VAL | VAL | ALA | PHE | SER | GLU | ILE | ||||
| 7 | MET | SER | MET | ILE | TRP | LYS | ARG | LEU | ASN | ASP | ||||
| 8 | HIS | GLY | LYS | ASN | TRP | ARG | HIS | VAL | TYR | LYS | ||||
| 9 | ALA | MET | THR | LEU | MET | GLU | TYR | LEU | ILE | LYS | ||||
| 10 | THR | GLY | SER | GLU | ARG | VAL | SER | GLN | GLN | CYS | ||||
| 11 | LYS | GLU | ASN | MET | TYR | ALA | VAL | GLN | THR | LEU | ||||
| 12 | LYS | ASP | PHE | GLN | TYR | VAL | ASP | ARG | ASP | GLY | ||||
| 13 | LYS | ASP | GLN | GLY | VAL | ASN | VAL | ARG | GLU | LYS | ||||
| 14 | ALA | LYS | GLN | LEU | VAL | ALA | LEU | LEU | ARG | ASP | ||||
| 15 | GLU | ASP | ARG | LEU | ARG | GLU | GLU | ARG |
Samples:
sample1: epsin ENTH domain, [U-13C; U-15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 400 mM; dithiothreitol, [U-2H], 2 mM; sodium azide 0.01%; H2O 90%; D2O 10%
sample2: epsin ENTH domain, [U-15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 400 mM; dithiothreitol, [U-2H], 2 mM; sodium azide 0.01%; H2O 90%; D2O 10%
cond1: pH: 6.5; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 15N HSQC | not available | not available | not available |
| 3D 15N NOESY-HSQC | not available | not available | not available |
| 3D 15N TOCSY-HSQC | not available | not available | not available |
| 3D HNHB | not available | not available | not available |
| 2D 13C HSQC | not available | not available | not available |
| 3D HNCA | not available | not available | not available |
| 3D HN(CO)CA | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HCACO | not available | not available | not available |
| 3D CBCANH | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D HBHA(CO)NH | not available | not available | not available |
| 3D C(CO)NH | not available | not available | not available |
| 3D H(CCO)NH | not available | not available | not available |
| 3D HCCH-TOCSY | not available | not available | not available |
| 3D HCCH-COSY | not available | not available | not available |
| 3D 13C NOESY-HSQC | not available | not available | not available |
| 4D 13C/15N NOESY | not available | not available | not available |
| 4D 13C/13C NOESY | not available | not available | not available |
Software:
NMRPipe - data processing
NMRView - peak assignments
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAB14041 BAG62253 BAI45694 |
| GB | AAC33823 AAD38326 AAH44651 AAH46962 AAH67206 |
| REF | NP_001033759 NP_001123543 NP_001123544 NP_001239383 NP_034277 |
| SP | O88339 Q80VP1 Q9Y6I3 |
| TPG | DAA19370 |
| AlphaFold | Q80VP1 O88339 Q9Y6I3 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks