BMRB Entry 5065
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5065
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Title: Quail Cysteine and Glycine-rich Protein, NMR, 15 Minimized Model Structures PubMed: 11583159
Deposition date: 2001-06-29 Original release date: 2001-11-14
Authors: Schuler, Wolfgang; Kloiber, Karin; Matt, Theresia; Bister, Klaus; Konrat, Robert
Citation: Schuler, Wolfgang; Kloiber, Karin; Matt, Theresia; Bister, Klaus; Konrat, Robert. "Application of Cross-correlated NMR Spin Relaxation to the Zinc-finger Protein CRP2(LIM2): Evidence for Collective Motions in LIM Domains" Biochemistry 40, 9596-9604 (2001).
Assembly members:
CYSTEINE-RICH PROTEIN CRP2(LIM2), polymer, 113 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Japanese Quail Taxonomy ID: 93934 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Coturnix japonica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CYSTEINE-RICH PROTEIN CRP2(LIM2): MDRGERLGIKPESSPSPHRP
TTNPNTSKFAQKFGGAEKCS
RCGDSVYAAEKVIGAGKPWH
KNCFRCAKCGKSLESTTLTE
KEGEIYCKGCYAKNFGPKGF
GYGQGAGALVHAQ
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 231 |
15N chemical shifts | 56 |
1H chemical shifts | 336 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CYSTEINE-RICH PROTEIN | 1 |
2 | ZINC ION, I | 2 |
3 | ZINC ION, II | 2 |
Entities:
Entity 1, CYSTEINE-RICH PROTEIN 113 residues - Formula weight is not available
1 | MET | ASP | ARG | GLY | GLU | ARG | LEU | GLY | ILE | LYS | ||||
2 | PRO | GLU | SER | SER | PRO | SER | PRO | HIS | ARG | PRO | ||||
3 | THR | THR | ASN | PRO | ASN | THR | SER | LYS | PHE | ALA | ||||
4 | GLN | LYS | PHE | GLY | GLY | ALA | GLU | LYS | CYS | SER | ||||
5 | ARG | CYS | GLY | ASP | SER | VAL | TYR | ALA | ALA | GLU | ||||
6 | LYS | VAL | ILE | GLY | ALA | GLY | LYS | PRO | TRP | HIS | ||||
7 | LYS | ASN | CYS | PHE | ARG | CYS | ALA | LYS | CYS | GLY | ||||
8 | LYS | SER | LEU | GLU | SER | THR | THR | LEU | THR | GLU | ||||
9 | LYS | GLU | GLY | GLU | ILE | TYR | CYS | LYS | GLY | CYS | ||||
10 | TYR | ALA | LYS | ASN | PHE | GLY | PRO | LYS | GLY | PHE | ||||
11 | GLY | TYR | GLY | GLN | GLY | ALA | GLY | ALA | LEU | VAL | ||||
12 | HIS | ALA | GLN |
Entity 2, ZINC ION, I - Zn - 65.409 Da.
1 | ZN |
Samples:
sample_1: CYSTEINE-RICH PROTEIN CRP2(LIM2), [U-13C; U-15N], 1.0 2.0 mM; H2O 90%; D2O, [U-2H], 10%; potassium phosphate 20 mM; KCl 50 mM; dithiothreitol 0.5 mM
sample_2: CYSTEINE-RICH PROTEIN CRP2(LIM2), [U-15N], 1.0 2.0 mM; H2O 90%; D2O, [U-2H], 10%; potassium phosphate 20 mM; KCl 50 mM; dithiothreitol 0.5 mM
sample_cond_1: ionic strength: 70.5 mM; pH: 7.2; pressure: 1 atm; temperature: 299 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
15N-HSQC | not available | not available | sample_cond_1 |
3D HNCA | not available | not available | sample_cond_1 |
3D HNCACB | not available | not available | sample_cond_1 |
3D HNCO | not available | not available | sample_cond_1 |
3D CBCA(CO)NH | not available | not available | sample_cond_1 |
3D HCCH-TOCSY | not available | not available | sample_cond_1 |
3D CCH-TOCSY-NNH | not available | not available | sample_cond_1 |
3D 13C-NOESY-HSQC (CA-centered) | not available | not available | sample_cond_1 |
3D 13C-NOESY-HSQC (methyl-centered) | not available | not available | sample_cond_1 |
3D 15N-NOESY-HSQC | not available | not available | sample_cond_1 |
Software:
VNMR vv6.1 Rev.B - collection
NMRPipe vv1.8 Rev 2001.030.21.27 - processing
ANSIG vv3.3 - data analysis
CNS v1.0 - structure solution
X-PLOR v3.851 - refinement
NMR spectrometers:
- VARIAN UNITYPLUS 500 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts