BMRB Entry 18605
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18605
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Title: Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain, Northeast Structural Genomics Consortium (NESG) Target HR8682B
Deposition date: 2012-07-20 Original release date: 2012-08-27
Authors: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain" To be published ., .-..
Assembly members:
HR8682B, polymer, 113 residues, 12736.705 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):
HR8682B: SHMPVPVTCDAVRNKCREML
TAALQTDHDHVAIGADCERL
SAQIEECIFRDVGNTDMKYK
NRVRSRISNLKDAKNPDLRR
NVLCGAITPQQIAVMTSEEM
ASDELKEIRKAMT
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 447 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 740 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR8682B | 1 |
Entities:
Entity 1, HR8682B 113 residues - 12736.705 Da.
Residues 4-113 correspond to residues 130-239 of the native protein. Residues 1-3 represent the remainder of the purification tag following its cleavage
| 1 | SER | HIS | MET | PRO | VAL | PRO | VAL | THR | CYS | ASP | ||||
| 2 | ALA | VAL | ARG | ASN | LYS | CYS | ARG | GLU | MET | LEU | ||||
| 3 | THR | ALA | ALA | LEU | GLN | THR | ASP | HIS | ASP | HIS | ||||
| 4 | VAL | ALA | ILE | GLY | ALA | ASP | CYS | GLU | ARG | LEU | ||||
| 5 | SER | ALA | GLN | ILE | GLU | GLU | CYS | ILE | PHE | ARG | ||||
| 6 | ASP | VAL | GLY | ASN | THR | ASP | MET | LYS | TYR | LYS | ||||
| 7 | ASN | ARG | VAL | ARG | SER | ARG | ILE | SER | ASN | LEU | ||||
| 8 | LYS | ASP | ALA | LYS | ASN | PRO | ASP | LEU | ARG | ARG | ||||
| 9 | ASN | VAL | LEU | CYS | GLY | ALA | ILE | THR | PRO | GLN | ||||
| 10 | GLN | ILE | ALA | VAL | MET | THR | SER | GLU | GLU | MET | ||||
| 11 | ALA | SER | ASP | GLU | LEU | LYS | GLU | ILE | ARG | LYS | ||||
| 12 | ALA | MET | THR |
Samples:
NC: HR8682B.004, [U-100% 13C; U-100% 15N], 1.0 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; TRIS 10 mM
NC5: HR8682B.004, [5% 13C; U-100% 15N], 1.0 mM; NaCl 100 mM; DTT 5 mM; NaN3 0.02%; TRIS 10 mM
sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| 3D (H)C(CO)NH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 1D 15N T1 | NC | isotropic | sample_conditions_1 |
| 1D 15N T2 | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl | NC5 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution, geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, geometry optimization, structure solution
ASDP v1.0, Huang, Tejero, Powers and Montelione - data analysis, refinement
XEASY v1.3.13, Bartels et al. - data analysis
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
VNMRJ v2.2D, Varian - collection
PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| UNP | Q15560 |
| PDB | |
| DBJ | BAA09089 BAG51383 BAJ20194 |
| EMBL | CAG33221 CAH59746 |
| GB | AAH18896 ABZ92433 EAW75168 EAW75170 EHH19498 |
| PRF | 2204253A |
| REF | NP_001244428 NP_003186 NP_942016 XP_001153063 XP_003787843 |
| SP | Q15560 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts