BMRB Entry 17148
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17148
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Title: N-terminal domain of Nephila clavipes major ampulate spidroin 1 PubMed: 21152998
Deposition date: 2010-08-25 Original release date: 2010-09-13
Authors: Parnham, Stuart; Hennig, Mirko
Citation: Parnham, Stuart; Gaines, William; Duggan, Brendan; Marcotte, William; Hennig, Mirko. "NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1." Biomol. NMR Assignments 5, 131-133 (2011).
Assembly members:
Spn-1, polymer, 144 residues, 14961.5253 Da.
Natural source: Common Name: Nephila clavipes Taxonomy ID: 6915 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila clavipes
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Spn-1: GPLGSPGIPGQNTPWSSTEL
ADAFINAFMNEAGRTGAFTA
DQLDDMSTIGDTIKTAMDKM
ARSNKSSKGKLQALNMAFAS
SMAEIAAVEQGGLSVDAKTN
AIADSLNSAFYQTTGAANPQ
FVNEIRSLINMFAQSSANEV
SYGG
- assigned_chemical_shifts
- coupling_constants
- spectral_peak_list
Data type | Count |
13C chemical shifts | 539 |
15N chemical shifts | 160 |
1H chemical shifts | 872 |
coupling constants | 98 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Spn-1 | 1 |
Entities:
Entity 1, Spn-1 144 residues - 14961.5253 Da.
1 | GLY | PRO | LEU | GLY | SER | PRO | GLY | ILE | PRO | GLY | ||||
2 | GLN | ASN | THR | PRO | TRP | SER | SER | THR | GLU | LEU | ||||
3 | ALA | ASP | ALA | PHE | ILE | ASN | ALA | PHE | MET | ASN | ||||
4 | GLU | ALA | GLY | ARG | THR | GLY | ALA | PHE | THR | ALA | ||||
5 | ASP | GLN | LEU | ASP | ASP | MET | SER | THR | ILE | GLY | ||||
6 | ASP | THR | ILE | LYS | THR | ALA | MET | ASP | LYS | MET | ||||
7 | ALA | ARG | SER | ASN | LYS | SER | SER | LYS | GLY | LYS | ||||
8 | LEU | GLN | ALA | LEU | ASN | MET | ALA | PHE | ALA | SER | ||||
9 | SER | MET | ALA | GLU | ILE | ALA | ALA | VAL | GLU | GLN | ||||
10 | GLY | GLY | LEU | SER | VAL | ASP | ALA | LYS | THR | ASN | ||||
11 | ALA | ILE | ALA | ASP | SER | LEU | ASN | SER | ALA | PHE | ||||
12 | TYR | GLN | THR | THR | GLY | ALA | ALA | ASN | PRO | GLN | ||||
13 | PHE | VAL | ASN | GLU | ILE | ARG | SER | LEU | ILE | ASN | ||||
14 | MET | PHE | ALA | GLN | SER | SER | ALA | ASN | GLU | VAL | ||||
15 | SER | TYR | GLY | GLY |
Samples:
Spn-1: Spn-1, [U-98% 13C; U-98% 15N], 1.0 mM; H2O 1.0 mM; D2O 1.0 mM
sample_conditions_1: ionic strength: 500 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
aro_d20noesy (H[c]_H[c].NOESY) | Spn-1 | isotropic | sample_conditions_1 |
3D C(CO)NH | Spn-1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC/HMQC | Spn-1 | isotropic | sample_conditions_1 |
cbca_500mM (H[N[co[{CA|ca[C]}]]]) | Spn-1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | Spn-1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | Spn-1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | Spn-1 | isotropic | sample_conditions_1 |
500mM_aro (h[C]_H.TOCSY) | Spn-1 | isotropic | sample_conditions_1 |
HCaN_prolines (HCA[N]) | Spn-1 | isotropic | sample_conditions_1 |
hnco_500mM (HNCO) | Spn-1 | isotropic | sample_conditions_1 |
hnha (H{[N]+[HA]}) | Spn-1 | isotropic | sample_conditions_1 |
hbhaconh_500 (H{ca|cca}[co[N]]HA) | Spn-1 | isotropic | sample_conditions_1 |
Software:
NMRDraw vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum analysis, Spectrum display
NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectrum processing
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
ANALYSIS v2.0, CCPN - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts