BMRB Entry 17518
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17518
MolProbity Validation Chart
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Title: Solution Strucuture of CBM25-1 of beta/alpha-amylase from Paenibacillus polymyxa
Deposition date: 2011-03-09 Original release date: 2012-08-07
Authors: Horibe, Ippei; Takahashi, Ryosuke; Yoshida, Takuya; Ohkubo, Tadayasu; Sumitani, Jun-ichi; Nishimura, Shigenori
Citation: Takahashi, Ryosuke; Horibe, Ippei; Fukada, Harumi; Yoshida, Takuya; Ohkubo, Tadayasu; Inui, Takashi; Nishimura, Shigenori; Sumitani, Jun-ichi. "A functional and structural analysis of tundem family 25 carbohydrate-binding modules from Paenibacillus polymyxa beta/alpha-amylase" Protein Sci. ., .-..
Assembly members:
entity, polymer, 104 residues, 10745.604 Da.
Natural source: Common Name: Bacillus polymyxa Taxonomy ID: 1406 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus polymyxa
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GGTGNKVTIYYKKGFNSPYI
HYRPAGGSWTAAPGVKMQDA
EISGYAKITVDIGSASQLEA
AFNDGNNNWDSNNTKNYSFS
TGTSTYTPGNSGNAGTITSG
APAG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 599 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CBM25-1 of beta/alpha-amylase | 1 |
Entities:
Entity 1, CBM25-1 of beta/alpha-amylase 104 residues - 10745.604 Da.
| 1 | GLY | GLY | THR | GLY | ASN | LYS | VAL | THR | ILE | TYR | ||||
| 2 | TYR | LYS | LYS | GLY | PHE | ASN | SER | PRO | TYR | ILE | ||||
| 3 | HIS | TYR | ARG | PRO | ALA | GLY | GLY | SER | TRP | THR | ||||
| 4 | ALA | ALA | PRO | GLY | VAL | LYS | MET | GLN | ASP | ALA | ||||
| 5 | GLU | ILE | SER | GLY | TYR | ALA | LYS | ILE | THR | VAL | ||||
| 6 | ASP | ILE | GLY | SER | ALA | SER | GLN | LEU | GLU | ALA | ||||
| 7 | ALA | PHE | ASN | ASP | GLY | ASN | ASN | ASN | TRP | ASP | ||||
| 8 | SER | ASN | ASN | THR | LYS | ASN | TYR | SER | PHE | SER | ||||
| 9 | THR | GLY | THR | SER | THR | TYR | THR | PRO | GLY | ASN | ||||
| 10 | SER | GLY | ASN | ALA | GLY | THR | ILE | THR | SER | GLY | ||||
| 11 | ALA | PRO | ALA | GLY |
Samples:
sample_1: sodium acetate, [U-100% 15N], 0.5-1.2 mM; sodium acetate, [U-99% 13C; U-99% 15N], 0.5-1.2 mM
sample_2: sodium acetate, [U-100% 15N], 0.6 mM
sample_conditions_1: ionic strength: 20 mM; pH: 5.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
SPARKY, Guntert, Braun and Wuthrich - chemical shift assignment
DYANA, Guntert, Braun and Wuthrich - chemical shift assignment
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts