BMRB Entry 18726
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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/BMR18726
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Title: Repetitive domain (RP) of aciniform spidroin 1 from Nephila antipodiana PubMed: 23129012
Deposition date: 2012-09-18 Original release date: 2013-01-15
Authors: Wang, Shujing; Huang, Weidong; Yang, Daiwen
Citation: Wang, Shujing; Huang, Weidong; Yang, Daiwen. "NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana" J. Biomol. NMR 54, 415-420 (2012).
Assembly members:
AcSp1-RP, polymer, 167 residues, 17079.383 Da.
Natural source: Common Name: Spiders Taxonomy ID: 171624 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila antipodiana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
AcSp1-RP: MHHHHHHSGSLGDQLTSTLA
SALTKTNTLKAVSASKPSAN
VAVAIVTSGLKKALGALRIN
AGVSSQLTSAVSQAVANVRP
GSSPAVYAKAIAAPSVQILV
SSGSVNNNNAKQVASTLSEN
LVREMANTARRYRVNVPEAS
VQADVSLVTSMTSTFVISSQ
TSVQMGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 487 |
| 15N chemical shifts | 165 |
| 1H chemical shifts | 1070 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AcSp1-RP | 1 |
Entities:
Entity 1, AcSp1-RP 167 residues - 17079.383 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | GLY | SER | ||||
| 2 | LEU | GLY | ASP | GLN | LEU | THR | SER | THR | LEU | ALA | ||||
| 3 | SER | ALA | LEU | THR | LYS | THR | ASN | THR | LEU | LYS | ||||
| 4 | ALA | VAL | SER | ALA | SER | LYS | PRO | SER | ALA | ASN | ||||
| 5 | VAL | ALA | VAL | ALA | ILE | VAL | THR | SER | GLY | LEU | ||||
| 6 | LYS | LYS | ALA | LEU | GLY | ALA | LEU | ARG | ILE | ASN | ||||
| 7 | ALA | GLY | VAL | SER | SER | GLN | LEU | THR | SER | ALA | ||||
| 8 | VAL | SER | GLN | ALA | VAL | ALA | ASN | VAL | ARG | PRO | ||||
| 9 | GLY | SER | SER | PRO | ALA | VAL | TYR | ALA | LYS | ALA | ||||
| 10 | ILE | ALA | ALA | PRO | SER | VAL | GLN | ILE | LEU | VAL | ||||
| 11 | SER | SER | GLY | SER | VAL | ASN | ASN | ASN | ASN | ALA | ||||
| 12 | LYS | GLN | VAL | ALA | SER | THR | LEU | SER | GLU | ASN | ||||
| 13 | LEU | VAL | ARG | GLU | MET | ALA | ASN | THR | ALA | ARG | ||||
| 14 | ARG | TYR | ARG | VAL | ASN | VAL | PRO | GLU | ALA | SER | ||||
| 15 | VAL | GLN | ALA | ASP | VAL | SER | LEU | VAL | THR | SER | ||||
| 16 | MET | THR | SER | THR | PHE | VAL | ILE | SER | SER | GLN | ||||
| 17 | THR | SER | VAL | GLN | MET | GLY | GLY |
Samples:
sample_1: AcSp1-RP, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; pH: 6.0; 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-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 4D time shared 13C/15N-edited NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRspy, Yu Zheng, Daiwen Yang - chemical shift assignment
TOPSPIN, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB |
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