BMRB Entry 11592
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11592
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Title: Solution structure of chitosan-binding module 2 derived from chitosanase/glucanase from Paenibacillus sp. IK-5 PubMed: 26936968
Deposition date: 2015-05-13 Original release date: 2016-04-04
Authors: Shinya, Shoko; Nishimura, Shigenori; Fukamizo, Tamo
Citation: Shinya, Shoko; Nishimura, Shigenori; Kitaoku, Yoshihito; Ohnuma, Takayuki; Numata, Tomoyuki; Kimoto, Hisashi; Kusaoke, Hideo; Fukamizo, Tamo. "Mechanism of chitosan recognition by CBM32 carbohydrate-binding modules from a Paenibacillus sp. IK-5 chitosanase/glucanase" Biochem. J. ., .-. (2016).
Assembly members:
DD2, polymer, 131 residues, 14081.312 Da.
Natural source: Common Name: Paenibacillus sp. Taxonomy ID: 44249 Superkingdom: Bacteria Kingdom: not available Genus/species: Paenibacillus sp.
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DD2: NLALNKATATSSIETAGHEG
DKAVDGNAATRWASAYGASP
QWIYINLGSTQSISRVKLNW
EDAYATAYSIQVSNDSGSTP
TNWTTVYSTTTGDGAIDDIT
FAATNAKFVRVYATTRATAY
GYSLWEFEVYG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 469 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 671 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 131 residues - 14081.312 Da.
| 1 | ASN | LEU | ALA | LEU | ASN | LYS | ALA | THR | ALA | THR | ||||
| 2 | SER | SER | ILE | GLU | THR | ALA | GLY | HIS | GLU | GLY | ||||
| 3 | ASP | LYS | ALA | VAL | ASP | GLY | ASN | ALA | ALA | THR | ||||
| 4 | ARG | TRP | ALA | SER | ALA | TYR | GLY | ALA | SER | PRO | ||||
| 5 | GLN | TRP | ILE | TYR | ILE | ASN | LEU | GLY | SER | THR | ||||
| 6 | GLN | SER | ILE | SER | ARG | VAL | LYS | LEU | ASN | TRP | ||||
| 7 | GLU | ASP | ALA | TYR | ALA | THR | ALA | TYR | SER | ILE | ||||
| 8 | GLN | VAL | SER | ASN | ASP | SER | GLY | SER | THR | PRO | ||||
| 9 | THR | ASN | TRP | THR | THR | VAL | TYR | SER | THR | THR | ||||
| 10 | THR | GLY | ASP | GLY | ALA | ILE | ASP | ASP | ILE | THR | ||||
| 11 | PHE | ALA | ALA | THR | ASN | ALA | LYS | PHE | VAL | ARG | ||||
| 12 | VAL | TYR | ALA | THR | THR | ARG | ALA | THR | ALA | TYR | ||||
| 13 | GLY | TYR | SER | LEU | TRP | GLU | PHE | GLU | VAL | TYR | ||||
| 14 | GLY |
Samples:
sample_1: DD2, [U-95% 13C; U-95% 15N], 0.4 mM; TRIS 10 mM; H2O 90%; D2O, [U-2H], 10%
sample_2: DD2, [U-95% 13C; U-95% 15N], 0.4 mM; D2O, [U-2H], 100%
sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - dihedral angle prediction
NMR spectrometers:
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts