BMRB Entry 19749
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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/BMR19749
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Title: Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A.
Deposition date: 2014-01-23 Original release date: 2014-03-03
Authors: Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Yang, Yunhuang; Ramelot, Theresa; Janjua, Haleema; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of N-terminal domain (SH2 domain) of human Inositol polyphosphate phosphatase-like protein 1 (INPPL1) (fragment 20-117), Northeast Structural Genomics Consortium Target HR9134A." To be published ., .-..
Assembly members:
HR9134A, polymer, 109 residues, 12198.978 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):
HR9134A: MGHHHHHHSHMSWYHRDLSR
AAAEELLARAGRDGSFLVRD
SESVAGAFALCVLYQKHVHT
YRILPDGEDFLAVQTSQGVP
VRRFQTLGELIGLYAQPNQG
LVCALLLPV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 427 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 704 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR9134A | 1 |
Entities:
Entity 1, HR9134A 109 residues - 12198.978 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | SER | TRP | TYR | HIS | ARG | ASP | LEU | SER | ARG | ||||
| 3 | ALA | ALA | ALA | GLU | GLU | LEU | LEU | ALA | ARG | ALA | ||||
| 4 | GLY | ARG | ASP | GLY | SER | PHE | LEU | VAL | ARG | ASP | ||||
| 5 | SER | GLU | SER | VAL | ALA | GLY | ALA | PHE | ALA | LEU | ||||
| 6 | CYS | VAL | LEU | TYR | GLN | LYS | HIS | VAL | HIS | THR | ||||
| 7 | TYR | ARG | ILE | LEU | PRO | ASP | GLY | GLU | ASP | PHE | ||||
| 8 | LEU | ALA | VAL | GLN | THR | SER | GLN | GLY | VAL | PRO | ||||
| 9 | VAL | ARG | ARG | PHE | GLN | THR | LEU | GLY | GLU | LEU | ||||
| 10 | ILE | GLY | LEU | TYR | ALA | GLN | PRO | ASN | GLN | GLY | ||||
| 11 | LEU | VAL | CYS | ALA | LEU | LEU | LEU | PRO | VAL |
Samples:
sample_1: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; H2O 90%; D2O 10%
sample_2: HR9134A, [U-100% 13C; U-100% 15N], 0.58 mM; D2O 100%
sample_3: HR9134A, [U-5% 13C; U-100% 15N], 1.05 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC NH2 only | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC histidine | sample_3 | 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
AutoStructure 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 850 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA81818 BAA82308 |
| EMBL | CAA74743 |
| GB | AAF28187 AAH63080 AAI40854 ADG23056 EAW74854 |
| REF | NP_001116211 NP_001177208 NP_001178105 NP_001247768 NP_001257772 |
| SP | O15357 Q6P549 Q9WVR3 |
| TPG | DAA21965 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts