BMRB Entry 16544
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16544
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Title: RECQL4 AMINO-TERMINAL DOMAIN PubMed: 22730300
Deposition date: 2009-10-07 Original release date: 2012-08-03
Authors: Ohlenschlager, Oliver; Gorlach, Matthias; Pospiech, Helmut
Citation: Ohlenschlager, Oliver; Kuhnert, Anja; Schneider, Annerose; Haumann, Sebastian; Bellstedt, Peter; Keller, Heidi; Saluz, Hans-Peter; Hortschansky, Peter; Hanel, Frank; Grosse, Frank; Gorlach, Matthias; Pospiech, Helmut. "The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif." Nucleic Acids Res. 40, 8309-8324 (2012).
Assembly members:
RECQL4NT, polymer, 56 residues, 6850.708 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 Vector: pGEX1lambdaT
Entity Sequences (FASTA):
RECQL4NT: GSMERLRDVRERLQAWERAF
RRQRGRRPSQDDVEAAPEET
RALYREYRTLKRTTGQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 243 |
| 15N chemical shifts | 52 |
| 1H chemical shifts | 377 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RECQL4NT | 1 |
Entities:
Entity 1, RECQL4NT 56 residues - 6850.708 Da.
Residues 1-2 are non-native
| 1 | GLY | SER | MET | GLU | ARG | LEU | ARG | ASP | VAL | ARG | ||||
| 2 | GLU | ARG | LEU | GLN | ALA | TRP | GLU | ARG | ALA | PHE | ||||
| 3 | ARG | ARG | GLN | ARG | GLY | ARG | ARG | PRO | SER | GLN | ||||
| 4 | ASP | ASP | VAL | GLU | ALA | ALA | PRO | GLU | GLU | THR | ||||
| 5 | ARG | ALA | LEU | TYR | ARG | GLU | TYR | ARG | THR | LEU | ||||
| 6 | LYS | ARG | THR | THR | GLY | GLN |
Samples:
sample_1: RECQL4NT, [U-99% 15N], 1.2 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM
sample_2: RECQL4NT, [U-99% 13C; U-99% 15N], 1.0 mM; TRIS, [U-2H], 20 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.100 M; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
CARA, Keller and Wuthrich - chemical shift assignment
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAA74453 BAA86899 |
| GB | AAZ85145 EAW82071 |
| REF | NP_004251 XP_004047747 XP_011515682 XP_011515683 XP_011515684 |
| SP | O94761 |
| AlphaFold | O94761 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts