BMRB Entry 53446
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53446
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Yang, Yuan; Murrali, Maria; Galvan, Sabrina; Wang, Yaqiang; Stephen, Christine; Ajjampore, Neha; Wang, Xiaoyu; Feigon, Juli. "HEXIM1 inter-monomer autoinhibition governs 7SK RNA binding specificity and P-TEFb inactivation" Nat. Comm. ., .-. (2025).
Assembly members:
entity_1, polymer, 75 residues, Formula weight is not available
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 Vector: pETDuet-1
Entity Sequences (FASTA):
entity_1: GGGEEEWGQQQRQLGKKKHR
RRPSKKKRHWKPYYKLTWEE
KKKFDEKQSLRASRIRAEMF
AKGQPVAPYNTTQFL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 298 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 478 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hexim1 BR-L | 1 |
Entities:
Entity 1, Hexim1 BR-L 75 residues - Formula weight is not available
Amino acids 136 through 209 from human Hexim1. A non-native glycine remains at the N-terminus of the final BR-L after TEV protease cleavage.
| 1 | GLY | GLY | GLY | GLU | GLU | GLU | TRP | GLY | GLN | GLN | ||||
| 2 | GLN | ARG | GLN | LEU | GLY | LYS | LYS | LYS | HIS | ARG | ||||
| 3 | ARG | ARG | PRO | SER | LYS | LYS | LYS | ARG | HIS | TRP | ||||
| 4 | LYS | PRO | TYR | TYR | LYS | LEU | THR | TRP | GLU | GLU | ||||
| 5 | LYS | LYS | LYS | PHE | ASP | GLU | LYS | GLN | SER | LEU | ||||
| 6 | ARG | ALA | SER | ARG | ILE | ARG | ALA | GLU | MET | PHE | ||||
| 7 | ALA | LYS | GLY | GLN | PRO | VAL | ALA | PRO | TYR | ASN | ||||
| 8 | THR | THR | GLN | PHE | LEU |
Samples:
sample_1: sodium phosphate 50 mM; sodium azide 0.02 % w/v; D2O 5 % v/v; Hexim1 BR-L, [U-98% 13C; U-98% 15N], 0.55 mM; potassium chloride 150 mM
sample_conditions_1: ionic strength: 200 mM; pH: 6.2; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN - collection
NMRPipe - processing
istHMS - processing
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
- Bruker AVANCE NEO 800 MHz
Related Database Links:
| NCBI | NP_006451.1 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks