BMRB Entry 17832
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17832
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Title: 1H, 15N and 13C resonance assignments for the N-terminal dimeric region of budding yeast histone chaperone Rtt106 PubMed: 22307274
Deposition date: 2011-08-04 Original release date: 2012-01-25
Authors: Hu, Q.; Cui, G.; Mer, G.
Citation: Su, Dan; Hu, Qi; Li, Qing; Thompson, James; Cui, Gaofeng; Fazly, Ahmed; Davies, Brian; Botuyan, Maria; Zhang, Zhiguo; Mer, Georges. "Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106" Nature 483, 104-107 (2012).
Assembly members:
HISTONE_CHAPERONE_RTT106, polymer, 70 residues, 8129.245 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI
Entity Sequences (FASTA):
HISTONE_CHAPERONE_RTT106: GHMMSKLFLDELPESLSRKI
GTVVRVLPSSLEIFEELYKY
ALNENSNDRSEHHKKPRIDD
SSDLLKTDEI
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 286 |
15N chemical shifts | 66 |
1H chemical shifts | 451 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HISTONE CHAPERONE RTT106_1 | 1 |
2 | HISTONE CHAPERONE RTT106_2 | 1 |
Entities:
Entity 1, HISTONE CHAPERONE RTT106_1 70 residues - 8129.245 Da.
1 | GLY | HIS | MET | MET | SER | LYS | LEU | PHE | LEU | ASP | |
2 | GLU | LEU | PRO | GLU | SER | LEU | SER | ARG | LYS | ILE | |
3 | GLY | THR | VAL | VAL | ARG | VAL | LEU | PRO | SER | SER | |
4 | LEU | GLU | ILE | PHE | GLU | GLU | LEU | TYR | LYS | TYR | |
5 | ALA | LEU | ASN | GLU | ASN | SER | ASN | ASP | ARG | SER | |
6 | GLU | HIS | HIS | LYS | LYS | PRO | ARG | ILE | ASP | ASP | |
7 | SER | SER | ASP | LEU | LEU | LYS | THR | ASP | GLU | ILE |
Samples:
sample_1: HISTONE CHAPERONE RTT106, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 10%; NaCl 30 mM; Sodium Phosphate 20 mM
sample_2: HISTONE CHAPERONE RTT106, [U-100% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 30 mM; Sodium Phosphate 20 mM
sample_3: HISTONE CHAPERONE RTT106, [U-100% 13C; U-100% 15N], 0.6 mM; HISTONE CHAPERONE RTT106 0.6 mM; D2O 100%; NaCl 30 mM; Sodium Phosphate 20 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6.95; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | 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 HNCACB | sample_1 | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H- 15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 13C- FILTERED-EDITED NOESY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- BRUKER AVANCE 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts