BMRB Entry 16808
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16808
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H
Deposition date: 2010-03-31 Original release date: 2010-04-28
Authors: Ertekin, Asli; Aramini, James; Rossi, Paolo; Lee, Hsiau-Wei; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Swapna, Gurla; Rost, Burkhard; Everett, John; Acton, Thomas; Prestegard, James; Montelione, Gaetano
Citation: Ertekin, Asli; Aramini, James; Rossi, Paolo; Lee, Hsiau-Wei; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Swapna, Gurla; Rost, Burkhard; Everett, John; Acton, Thomas; Prestegard, James; Montelione, Gaetano. "Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H" To be published ., .-..
Assembly members:
HR3057H, polymer, 65 residues, 14863.186 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):
HR3057H: MGHHHHHHSHSKYAELLAII
EELGKEIRPTYAGSKSAMER
LKRGIIHARGLVRECLAETE
RNARS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 233 |
| 15N chemical shifts | 54 |
| 1H chemical shifts | 370 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3057H | 1 |
Entities:
Entity 1, HR3057H 65 residues - 14863.186 Da.
the protein is a dimer in solution
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | SER | LYS | TYR | ALA | GLU | LEU | LEU | ALA | ILE | ILE | ||||
| 3 | GLU | GLU | LEU | GLY | LYS | GLU | ILE | ARG | PRO | THR | ||||
| 4 | TYR | ALA | GLY | SER | LYS | SER | ALA | MET | GLU | ARG | ||||
| 5 | LEU | LYS | ARG | GLY | ILE | ILE | HIS | ALA | ARG | GLY | ||||
| 6 | LEU | VAL | ARG | GLU | CYS | LEU | ALA | GLU | THR | GLU | ||||
| 7 | ARG | ASN | ALA | ARG | SER |
Samples:
sample_4: HR3057H, [U-5% 13C; U-100% 15N], 0.68 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; Polyacrylamide Gel 7%; H2O 95%; D2O 5%
sample_5: HR3057H, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; PEG 4.2%; H2O 95%; D2O 5%
sample_1: HR3057H, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_2: HR3057H, [U-5% 13C; U-100% 15N], 0.68 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_3: HR3057H, [U-100% 13C; U-100% 15N], 0.92 mM; HR3057H, unlabeled, 0.92 mM; MES 20 mM; DSS 50 uM; NaCl 200 mM; DTT 10 mM; CaCl2 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.5; 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 simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HC(C)H-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high res. (L/V methyl stereospecific assignment) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N T1 relaxation | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N T2 relaxation | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_2 | isotropic | sample_conditions_1 |
| X-filtered 13C NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | sample_4 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_5 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, 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
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
SPARKY v3, Goddard - data analysis, peak picking
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
PSVS v1.4, Bhattacharya and Montelione - structure quality analysis
TALOS v+, Cornilescu, Delaglio and Bax - Dihedral Angle Constraints
NMR spectrometers:
- Bruker Avance 800 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