BMRB Entry 16250
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16250
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Title: NMR solution structure of the EH 1 domain from human intersectin-1 protein. Northeast Structural Genomics Consortium target HR3646e.
Deposition date: 2009-04-09 Original release date: 2009-06-11
Authors: Mills, Jeffrey; Ghosh, Arindam; Garcia, Erwin; Zhang, Qi; Shastry, Ritu; Foote, Erica; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Mills, Jeffrey; Ghosh, Arindam; Garcia, Erwin; Zhang, Qi; Shastry, Ritu; Foote, Erica; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "NMR solution structure of the EH 1 domain from human intersectin-1 protein. Northeast Structural Genomics Consortium target HR3646e." Not known ., .-..
Assembly members:
HR3646E, polymer, 121 residues, 13614.668 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):
HR3646E: MGHHHHHHSHMAQFPTPFGG
SLDTWAITVEERAKHDQQFH
SLKPISGFITGDQARNFFFQ
SGLPQPVLAQIWALADMNND
GRMDQVEFSIAMKLIKLKLQ
GYQLPSALPPVMKQQPVAIS
S
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 352 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 741 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3646E | 1 |
Entities:
Entity 1, HR3646E 121 residues - 13614.668 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ALA | GLN | PHE | PRO | THR | PRO | PHE | GLY | GLY | ||||
| 3 | SER | LEU | ASP | THR | TRP | ALA | ILE | THR | VAL | GLU | ||||
| 4 | GLU | ARG | ALA | LYS | HIS | ASP | GLN | GLN | PHE | HIS | ||||
| 5 | SER | LEU | LYS | PRO | ILE | SER | GLY | PHE | ILE | THR | ||||
| 6 | GLY | ASP | GLN | ALA | ARG | ASN | PHE | PHE | PHE | GLN | ||||
| 7 | SER | GLY | LEU | PRO | GLN | PRO | VAL | LEU | ALA | GLN | ||||
| 8 | ILE | TRP | ALA | LEU | ALA | ASP | MET | ASN | ASN | ASP | ||||
| 9 | GLY | ARG | MET | ASP | GLN | VAL | GLU | PHE | SER | ILE | ||||
| 10 | ALA | MET | LYS | LEU | ILE | LYS | LEU | LYS | LEU | GLN | ||||
| 11 | GLY | TYR | GLN | LEU | PRO | SER | ALA | LEU | PRO | PRO | ||||
| 12 | VAL | MET | LYS | GLN | GLN | PRO | VAL | ALA | ILE | SER | ||||
| 13 | SER |
Samples:
NC: HR3646E, [U-98% 13C; U-98% 15N], 0.87 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H20 90%; D20 10%
NC5: HR3646E, [U-5% 13C; U-98% 15N], 0.81 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; H20 90%; D20 10%
sample_conditions_1: ionic strength: 430 mM; pH: 6.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 3D sim. 15N,13C NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5 | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D HNCABCA | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D CABCA(CO)NH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D arom. HCCH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D aliph. HCCH | NC | isotropic | sample_conditions_1 |
| GFT (4,3)D HABCAB(CO)NH | NC | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPSCAN, Glaser - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis
PSVS, Bhattacharya and Montelione - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts