BMRB Entry 19653

Name: RRM domain from C. elegans SUP-12
Published: 2014-02-11

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PDB ID: 4ch1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19653
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

RRM domain from C. elegans SUP-12

Deposition date:

2013-12-03

Original release date:

2014-02-11

Authors:

Amrane, S.; Mackereth, Cameron

Citation:

Citation: Amrane, Samir; Mackereth, Cameron. "Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans." Biomol. NMR Assignments 8, 109-112 (2013).
PubMed: 23334698

Assembly members:

Assembly members:
PROTEIN_SUP-12_ISOFORM_B, polymer, 97 residues, 10819.1904 Da.
GGTGTGC, polymer, 7 residues, 2106.4793 Da.

Natural source:

Natural source: Common Name: nematodes Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-His1a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PROTEIN_SUP-12_ISOFORM_B: GAMGSRDTMFTKIFVGGLPY HTSDKTLHEYFEQFGDIEEA VVITDRNTQKSRGYGFVTMK DRASAERACKDPNPIIDGRK ANVNLAYLGAKPRTNVQ
GGTGTGC: GGTGTGC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	420
15N chemical shifts	99
1H chemical shifts	731

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PROTEIN SUP-12, ISOFORM B	1
2	GGTGTGC	2

Entities:

Entity 1, PROTEIN SUP-12, ISOFORM B 97 residues - 10819.1904 Da.

1

GLY

ALA

MET

GLY

SER

ARG

ASP

THR

MET

PHE

2

THR

LYS

ILE

PHE

VAL

GLY

LEU

PRO

TYR

3

HIS

THR

SER

ASP

LYS

THR

LEU

HIS

GLU

TYR

4

PHE

GLU

GLN

PHE

GLY

ASP

ILE

GLU

ALA

5

VAL

ILE

THR

ASP

ARG

ASN

THR

GLN

LYS

6

SER

ARG

GLY

TYR

GLY

PHE

VAL

THR

MET

LYS

7

ASP

ARG

ALA

SER

ALA

GLU

ARG

ALA

CYS

LYS

8

ASP

PRO

ASN

PRO

ILE

ASP

GLY

ARG

LYS

9

ALA

ASN

VAL

ASN

LEU

ALA

TYR

LEU

GLY

ALA

10

LYS

PRO

ARG

THR

ASN

VAL

GLN

Entity 2, GGTGTGC 7 residues - 2106.4793 Da.

1

DG

DT

DG

DT

DG

DC

Samples:

sample_1: PROTEIN SUP-12, ISOFORM B, [U-13C; U-15N], 0.8 mM; GGTGTGC 0.8 mM; sodium phosphate 20 mM; sodium chloride 300 mM; H2O 10%; D2O, [U-100% 2H], 90%

sample_2: PROTEIN SUP-12, ISOFORM B, [U-13C; U-15N], 0.4 mM; GGTGTGC 0.4 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-100% 2H], 100%

sample_3: PROTEIN SUP-12, ISOFORM B, [U-100% 2H], 0.6 mM; GGTGTGC 0.6 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-100% 2H], 100%

sample_conditions_1: ionic strength: 300.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-NOESY	sample_1	solution	sample_conditions_1
13C-NOESY	sample_2	solution	sample_conditions_1
double-filtered 1H	sample_2	solution	sample_conditions_1
1H-NOESY	sample_2	solution	sample_conditions_1
1H-TOCSY	sample_2	solution	sample_conditions_1
1H	sample_3	solution	sample_conditions_1
1H-NOESY	sample_3	solution	sample_conditions_1

Software:

CNS1.1 vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

SPARKY vany, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 800 MHz

UNP	O45189 H2L051_CAEEL
BMRB	11541 18845 18846
PDB	2MGZ 2RU3 4CH0 4CH1 4CIO 4CH1
EMBL	CCD71425 CCD71429
GB	KIH66793
REF	NP_001129938 NP_508674
AlphaFold	H2L051 O45189