BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17263

Title: Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans.   PubMed: 21112336

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

Data sets:
Data typeCount
13C chemical shifts443
15N chemical shifts101
1H chemical shifts734
H exchange protection factors41
H exchange rates41
heteronuclear NOE values76

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Small archaeal modifier protein 1 from Methanosarcina acetivorans1

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   GLYHISMETALAGLUVALLYSVALLYSLEU
2   PHEALAASNLEUARGGLUALAALAGLYTHR
3   PROGLULEUPROLEUSERGLYGLULYSVAL
4   ILEASPVALLEULEUSERLEUTHRASPLYS
5   TYRPROALALEULYSTYRVALILEPHEGLU
6   LYSGLYASPGLULYSSERGLUILELEUILE
7   LEUCYSGLYSERILEASNILELEUILEASN
8   GLYASNASNILEARGHISLEUGLUGLYLEU
9   GLUTHRLEULEULYSASPSERASPGLUILE
10   GLYILELEUPROPROVALSERGLYGLY

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:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-HC(CC-TOCSY)CONHsample_1isotropicsample_conditions_1
4D APSY-HCCH-COSYsample_1isotropicsample_conditions_1
4D aromatic APSY-HCCH-COSYsample_1isotropicsample_conditions_1
4D APSY-HBCB(CG)CDHDsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 15N{1H}-NOE-[15N,1H]-HSQCsample_1isotropicsample_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

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