BMRB Entry 17753
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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/BMR17753
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Title: Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A
Deposition date: 2011-06-30 Original release date: 2011-08-03
Authors: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Wang, Dongyan; Kohan, Eitan; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A" To be published ., .-..
Assembly members:
HR3111A, polymer, 68 residues, 7639.775 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):
HR3111A: MGHHHHHHSHMGGGKGPAAE
EPLSLLDDMNHCYSRLRELV
PGVPRGTQLSQVEILQRVID
YILDLQVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 236 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 389 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HR3111A, strand 1 | 1 |
| 2 | HR3111A, strand 2 | 1 |
Entities:
Entity 1, HR3111A, strand 1 68 residues - 7639.775 Da.
Residues 14-68 correspond to the range 29-83 in the native protein. Residues 1-13 represent a non-native affinity tag.
| 1 | MET | GLY | HIS | HIS | HIS | HIS | HIS | HIS | SER | HIS | ||||
| 2 | MET | GLY | GLY | GLY | LYS | GLY | PRO | ALA | ALA | GLU | ||||
| 3 | GLU | PRO | LEU | SER | LEU | LEU | ASP | ASP | MET | ASN | ||||
| 4 | HIS | CYS | TYR | SER | ARG | LEU | ARG | GLU | LEU | VAL | ||||
| 5 | PRO | GLY | VAL | PRO | ARG | GLY | THR | GLN | LEU | SER | ||||
| 6 | GLN | VAL | GLU | ILE | LEU | GLN | ARG | VAL | ILE | ASP | ||||
| 7 | TYR | ILE | LEU | ASP | LEU | GLN | VAL | VAL |
Samples:
NC: HR3111A, [U-100% 13C; U-100% 15N], 0.9 mM; sodium chloride 100 mM; DTT 10 mM; TRIS 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%
NC5: HR3111A, [5% 13C; U-100% 15N], 0.5 mM; sodium chloride 100 mM; DTT 10 mM; TRIS 10 mM; sodium azide 0.02%; 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 | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT CABCA(CO)NHN | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HNNCABCA | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC for histidines | 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
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
XEASY v1.3.13, Bartels et al. - data analysis
PROSA v6.4, Guntert - processing
VNMRJ v2.2D, Varian - collection
TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAF82692 BAI46669 |
| EMBL | CAA47360 CAA48862 CAA51827 CAB70600 CAQ64597 |
| GB | AAH03107 AAP35437 AAP36573 AAX32359 AAX32360 |
| PIR | S71405 |
| PRF | 2104289A |
| REF | NP_001003025 NP_001230531 NP_002158 XP_002716031 XP_002811352 |
| SP | Q02535 Q712G9 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts