BMRB Entry 17263

Name: Solution structure of the small archaeal modifier protein 1 (SAMP1) from Methanosarcina acetivorans.
Published: 2011-01-18

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PDB ID: 2l52
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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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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 Vector: pROEX (Invitrogen)

Entity Sequences (FASTA):
Small archaeal modifier protein 1 from Methanosarcina acetivorans: GHMAEVKVKLFANLREAAGT PELPLSGEKVIDVLLSLTDK YPALKYVIFEKGDEKSEILI LCGSINILINGNNIRHLEGL ETLLKDSDEIGILPPVSGG

Data sets:

H_exch_protection_factors
- H_exch_protection_factors
H_exch_rates
- H_exch_rates
assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- 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

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

GLY

THR

3

PRO

GLU

LEU

PRO

LEU

SER

GLY

GLU

LYS

VAL

4

ILE

ASP

VAL

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

ILE

ARG

HIS

LEU

GLU

GLY

LEU

9

GLU

THR

LEU

LYS

ASP

SER

ASP

GLU

ILE

10

GLY

ILE

LEU

PRO

VAL

SER

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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts