BMRB Entry 17263
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17263
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Title: Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans. PubMed: 21112336
Deposition date: 2010-10-24 Original release date: 2011-01-18
Authors: Damberger, Fred; Ranjan, Namit; Sutter, Markus; Allain, Frederic; Weber-Ban, Eilika
Citation: Ranjan, Namit; Damberger, Fred; Sutter, Markus; Allain, Frederic H-T; Weber-Ban, Eilika. "Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins." J. Mol. Biol. 405, 1040-1055 (2011).
Assembly members:
Small archaeal modifier protein 1 from Methanosarcina acetivorans, polymer, 99 residues, 10708.505 Da.
Natural source: Common Name: Methanosarcina acetivorans Taxonomy ID: 2214 Superkingdom: Archaea Kingdom: not available Genus/species: Methanosarcina acetivorans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Small archaeal modifier protein 1 from Methanosarcina acetivorans: GHMAEVKVKLFANLREAAGT
PELPLSGEKVIDVLLSLTDK
YPALKYVIFEKGDEKSEILI
LCGSINILINGNNIRHLEGL
ETLLKDSDEIGILPPVSGG
- assigned_chemical_shifts
- H_exch_protection_factors
- H_exch_rates
- assigned_chemical_shifts
- heteronucl_NOEs
| Data type | Count |
| 13C chemical shifts | 443 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 734 |
| H exchange protection factors | 41 |
| H exchange rates | 41 |
| heteronuclear NOE values | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Small archaeal modifier protein 1 from Methanosarcina acetivorans | 1 |
Entities:
Entity 1, Small archaeal modifier protein 1 from Methanosarcina acetivorans 99 residues - 10708.505 Da.
The first two residues at the N-terminus represent the remainder of a His-Tag cleaved by a protease and are not part of the native sequence.
| 1 | GLY | HIS | MET | ALA | GLU | VAL | LYS | VAL | LYS | LEU | ||||
| 2 | PHE | ALA | ASN | LEU | ARG | GLU | ALA | ALA | GLY | THR | ||||
| 3 | PRO | GLU | LEU | PRO | LEU | SER | GLY | GLU | LYS | VAL | ||||
| 4 | ILE | ASP | VAL | LEU | LEU | SER | LEU | THR | ASP | LYS | ||||
| 5 | TYR | PRO | ALA | LEU | LYS | TYR | VAL | ILE | PHE | GLU | ||||
| 6 | LYS | GLY | ASP | GLU | LYS | SER | GLU | ILE | LEU | ILE | ||||
| 7 | LEU | CYS | GLY | SER | ILE | ASN | ILE | LEU | ILE | ASN | ||||
| 8 | GLY | ASN | ASN | ILE | ARG | HIS | LEU | GLU | GLY | LEU | ||||
| 9 | GLU | THR | LEU | LEU | LYS | ASP | SER | ASP | GLU | ILE | ||||
| 10 | GLY | ILE | LEU | PRO | PRO | VAL | SER | GLY | GLY |
Samples:
sample_1: SAMP1, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; EDTA 0.1 mM; H2O 90%; D2O 10%
sample_2: SAMP1, [U-99% 15N], 1 mM; sodium chloride 150 mM; sodium phosphate 20 mM; EDTA 0.1 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HC(CC-TOCSY)CONH | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 4D aromatic APSY-HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HBCB(CG)CDHD | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 15N{1H}-NOE-[15N,1H]-HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
AMBER v8, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
CYANA v3, CYANA (Peter Guntert) - structure solution
UNIO v10, (Torsten Herrmann) - peak picking, structure solution
CARA v1.8, Keller and Wuthrich - chemical shift assignment, data analysis
GAPRO v0.9.8, Sebastian Hiller & Gerhard Wider - chemical shift assignment, peak picking
TOPSPIN v2.1, Bruker Biospin - processing
Molmol v2.2K, Koradi, Billeter and Wuthrich - data analysis
MATCH, Herrmann and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker Avance 600 MHz
- Bruker Avance 500 MHz
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts