BMRB Entry 15404
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15404
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Title: Backbone and sidechain 1H, 13C, and 15N Chemical Shift Assignments for H. capsulatum CBP PubMed: 18361504
Deposition date: 2007-07-23 Original release date: 2007-08-13
Authors: Beck, Moriah; DeKoster, Gregory; Cistola, David; Goldman, William
Citation: Beck, Moriah; DeKoster, Gregory; Hambly, David; Gross, Micheal; Cistola, David; Goldman, William. "Structural features responsible for the biological stability of Histoplasma's virulence factor CBP" Biochemistry 47, 4427-4438 (2008).
Assembly members:
CBP, polymer, 78 residues, 7855 Da.
Natural source: Common Name: Ajellomyces capsulata Taxonomy ID: 5037 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Histoplasma capsulatum
Experimental source: Production method: purified from the natural source Host organism: Histoplasma capsulatum
Entity Sequences (FASTA):
CBP: DQPSVGDAFDKYNEAVRVFT
QLSSAANCDWAACLSSLSAS
SAACIAAVGELGLDVPLDLA
CAATATSSATEACKGCLW
- assigned_chemical_shifts
- coupling_constants
Data type | Count |
13C chemical shifts | 276 |
15N chemical shifts | 80 |
1H chemical shifts | 455 |
coupling constants | 66 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | CBP, monomer 1 | 1 |
2 | CBP, monomer 2 | 1 |
Entities:
Entity 1, CBP, monomer 1 78 residues - 7855 Da.
G186AR strain mature peptide
1 | ASP | GLN | PRO | SER | VAL | GLY | ASP | ALA | PHE | ASP | ||||
2 | LYS | TYR | ASN | GLU | ALA | VAL | ARG | VAL | PHE | THR | ||||
3 | GLN | LEU | SER | SER | ALA | ALA | ASN | CYS | ASP | TRP | ||||
4 | ALA | ALA | CYS | LEU | SER | SER | LEU | SER | ALA | SER | ||||
5 | SER | ALA | ALA | CYS | ILE | ALA | ALA | VAL | GLY | GLU | ||||
6 | LEU | GLY | LEU | ASP | VAL | PRO | LEU | ASP | LEU | ALA | ||||
7 | CYS | ALA | ALA | THR | ALA | THR | SER | SER | ALA | THR | ||||
8 | GLU | ALA | CYS | LYS | GLY | CYS | LEU | TRP |
Samples:
CBP-13C_15N: CBP, [U-99% 13C; U-99% 15N], 2 ± 1 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%
CBP-15N: CBP, [U-99% 15N], 1 ± 0.2 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%
CBP-13C_15N-cys: CBP, [U-99% 13C; U-99% 15N], 2 ± 1 mM; D2O, [U-99% 2H], 5%; H2O 95%; potassium chloride 100 mM; HEPES, [U-98% 2H], 10 mM; sodium azide 0.05%
CBP-normal: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | CBP-15N | isotropic | CBP-normal |
3D HNCACB | CBP-13C_15N | isotropic | CBP-normal |
3D CBCA(CO)NH | CBP-13C_15N-cys | isotropic | CBP-normal |
3D HBHA(CO)NH | CBP-13C_15N-cys | isotropic | CBP-normal |
3D HNCO | CBP-13C_15N | isotropic | CBP-normal |
3D CBCA(CO)CAHA | CBP-13C_15N | isotropic | CBP-normal |
3D HCCH-TOCSY | CBP-13C_15N | isotropic | CBP-normal |
3D HCC(TOCSY)NNH | CBP-13C_15N | isotropic | CBP-normal |
3D CC(TOCSY)NNH | CBP-13C_15N | isotropic | CBP-normal |
3D aromatic HC(C)H-TOCSY | CBP-13C_15N | isotropic | CBP-normal |
2D aromatic 13C-HSQC | CBP-13C_15N | isotropic | CBP-normal |
2D hbCBcgcdHD | CBP-13C_15N | isotropic | CBP-normal |
2D hbCBcgcdHDHE | CBP-13C_15N | isotropic | CBP-normal |
3D 1H-13C NOESY | CBP-13C_15N-cys | isotropic | CBP-normal |
3D HNHA | CBP-13C_15N-cys | isotropic | CBP-normal |
Software:
FELIX v2001, Accelrys Software Inc. - chemical shift assignment, peak picking, processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 700 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts