BMRB Entry 16348
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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/BMR16348
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Title: SOLUTION STRUCTURE OF DEAD RINGER-LIKE PROTEIN 1 (AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A) FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR4394C
Deposition date: 2009-06-14 Original release date: 2009-08-06
Authors: Liu, Gaohua; Wang, Dongyan; NWOSU, CHIOMA; OWENS, LEAH; Xiao, Rong; Liu, Jinfeng; Baran, Micheal; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Liu, Gaohua; Xiao, Rong; Montelione, Gaetano. "SOLUTION STRUCTURE OF DEAD RINGER-LIKE PROTEIN 1 (AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A) FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR4394C" Not known ., .-..
Assembly members:
HR4394C, polymer, 145 residues, 17162.803 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):
HR4394C: MGHHHHHHSHMPDHGDWTYE
EQFKQLYELDGDPKRKEFLD
DLFSFMQKRGTPVNRIPIMA
KQVLDLFMLYVLVTEKGGLV
EVINKKLWREITKGLNLPTS
ITSAAFTLRTQYMKYLYPYE
CEKRGLSNPNELQAAIDSNR
REGRR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 587 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 990 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR4394C | 1 |
Entities:
Entity 1, HR4394C 145 residues - 17162.803 Da.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | PRO | ASP | HIS | GLY | ASP | TRP | THR | TYR | GLU | ||||
| 3 | GLU | GLN | PHE | LYS | GLN | LEU | TYR | GLU | LEU | ASP | ||||
| 4 | GLY | ASP | PRO | LYS | ARG | LYS | GLU | PHE | LEU | ASP | ||||
| 5 | ASP | LEU | PHE | SER | PHE | MET | GLN | LYS | ARG | GLY | ||||
| 6 | THR | PRO | VAL | ASN | ARG | ILE | PRO | ILE | MET | ALA | ||||
| 7 | LYS | GLN | VAL | LEU | ASP | LEU | PHE | MET | LEU | TYR | ||||
| 8 | VAL | LEU | VAL | THR | GLU | LYS | GLY | GLY | LEU | VAL | ||||
| 9 | GLU | VAL | ILE | ASN | LYS | LYS | LEU | TRP | ARG | GLU | ||||
| 10 | ILE | THR | LYS | GLY | LEU | ASN | LEU | PRO | THR | SER | ||||
| 11 | ILE | THR | SER | ALA | ALA | PHE | THR | LEU | ARG | THR | ||||
| 12 | GLN | TYR | MET | LYS | TYR | LEU | TYR | PRO | TYR | GLU | ||||
| 13 | CYS | GLU | LYS | ARG | GLY | LEU | SER | ASN | PRO | ASN | ||||
| 14 | GLU | LEU | GLN | ALA | ALA | ILE | ASP | SER | ASN | ARG | ||||
| 15 | ARG | GLU | GLY | ARG | ARG |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.92 mM; NACL 200 mM
sample_2: entity, [U-100% 13C; U-100% 15N], 0.92 mM; NACL 200 mM
sample_3: entity, [U-10% 13C; U-100% 15N], 0.95 mM; NACL 200 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 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 aliphatic | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C-15N simutaneous NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v1.2, Huang, Tejero, Powers and Montelione - data analysis, refinement
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
XEASY v1.3, Bartels et al. - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| GB | AAC28918 AAC32888 AAC69994 AAH33163 AAH60828 |
| REF | NP_001192624 NP_005215 XP_001374625 XP_002828411 XP_003460928 |
| SP | Q99856 |
| TPG | DAA27511 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts