BMRB Entry 18166
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Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18166
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Title: Solution NMR Structure of Stress-induced-phosphoprotein 1 STI1 from Homo sapiens, Northeast Structural Genomics Consortium Target HR4403E
Deposition date: 2011-12-28 Original release date: 2012-02-17
Authors: Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Tang, Yuefeng; Liu, Gaohua; Hamilton, Keith; Ciccosanti, Colleen; Shastry, Ritu; Rost, Burkhard; Acton, Tom; Xiao, Rong; Everett, John; Montelione, Gaetano. "Northeast Structural Genomics Consortium Target HR4403E" To be published ., .-..
Assembly members:
HR4403E, polymer, 133 residues, 15365.743 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):
HR4403E: MGHHHHHHSHMNPDLALMVK
NKGNECFQKGDYPQAMKHYT
EAIKRNPKDAKLYSNRAACY
TKLLEFQLALKDCEECIQLE
PTFIKGYTRKAAALEAMKDY
TKAMDVYQKALDLDSSCKEA
ADGYQRCMMAQYN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 434 |
| 15N chemical shifts | 141 |
| 1H chemical shifts | 909 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR4403E | 1 |
Entities:
Entity 1, HR4403E 133 residues - 15365.743 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | ASN | PRO | ASP | LEU | ALA | LEU | MET | VAL | LYS | ||||
| 3 | ASN | LYS | GLY | ASN | GLU | CYS | PHE | GLN | LYS | GLY | ||||
| 4 | ASP | TYR | PRO | GLN | ALA | MET | LYS | HIS | TYR | THR | ||||
| 5 | GLU | ALA | ILE | LYS | ARG | ASN | PRO | LYS | ASP | ALA | ||||
| 6 | LYS | LEU | TYR | SER | ASN | ARG | ALA | ALA | CYS | TYR | ||||
| 7 | THR | LYS | LEU | LEU | GLU | PHE | GLN | LEU | ALA | LEU | ||||
| 8 | LYS | ASP | CYS | GLU | GLU | CYS | ILE | GLN | LEU | GLU | ||||
| 9 | PRO | THR | PHE | ILE | LYS | GLY | TYR | THR | ARG | LYS | ||||
| 10 | ALA | ALA | ALA | LEU | GLU | ALA | MET | LYS | ASP | TYR | ||||
| 11 | THR | LYS | ALA | MET | ASP | VAL | TYR | GLN | LYS | ALA | ||||
| 12 | LEU | ASP | LEU | ASP | SER | SER | CYS | LYS | GLU | ALA | ||||
| 13 | ALA | ASP | GLY | TYR | GLN | ARG | CYS | MET | MET | ALA | ||||
| 14 | GLN | TYR | ASN |
Samples:
sample_1: HR4403E, [U-100% 13C; U-100% 15N], 0.807 mM; H2O 95%; D2O 5%
sample_2: HR4403E, [U-5% 13C; U-100% 15N], 0.763 mM; H2O 95%; D2O 5%
sample_3: HR4403E, [U-100% 13C; U-100% 15N], 0.4 mM; D2O 100%
sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 293 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
REDCAT, Valafar, Prestegard - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts