BMRB Entry 17308

Name: drosophila CstF-50 (1-65)
Published: 2011-01-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17308

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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:

drosophila CstF-50 (1-65)

Deposition date:

2010-11-19

Original release date:

2011-01-18

Authors:

Mackereth, Cameron

Citation:

Citation: Moreno-Morcillo, Maria; Minvielle-Sebastia, Lionel; Mackereth, Cameron; Fribourg, Sebastien. "Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure." RNA 17, 412-418 (2011).
PubMed: 21233223

Assembly members:

Assembly members:
dCstF-50, polymer, 68 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
dCstF-50: MRDEILDPSNLVKNREILYR LMISQLMYDGLEKFAMELSM LVKADQCAPSERLLHVMIAG MQTLSLGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	198
15N chemical shifts	65
1H chemical shifts	117
heteronuclear NOE values	58
T1 relaxation values	55
T2 relaxation values	52

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein	1

Entities:

Entity 1, protein 68 residues - Formula weight is not available

C-terminal -LGS arises from the cloning site in the vector Protein is expressed with an N-terminal His6-tag which is removed by TEV protease, leaving a GH- at the N-terminus

1

MET

ARG

ASP

GLU

ILE

LEU

ASP

PRO

SER

ASN

2

LEU

VAL

LYS

ASN

ARG

GLU

ILE

LEU

TYR

ARG

3

LEU

MET

ILE

SER

GLN

LEU

MET

TYR

ASP

GLY

4

LEU

GLU

LYS

PHE

ALA

MET

GLU

LEU

SER

MET

5

LEU

VAL

LYS

ALA

ASP

GLN

CYS

ALA

PRO

SER

6

GLU

ARG

LEU

HIS

VAL

MET

ILE

ALA

GLY

7

MET

GLN

THR

LEU

SER

LEU

GLY

SER

Samples:

sample_1: dCstF-50, [U-99% 13C; U-99% 15N], 2 mM; d-Tris 50 mM; NaCl 150 mM; DTT 2 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 295 K

sample_conditions_2: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC hetnoe	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC T1	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC T2	sample_1	isotropic	sample_conditions_2

Software:

TOPSPIN v2.0, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	17313
PDB	2XZ2
GB	AAF57183 AAM11155 ACL84511 ACL89448 ALC45969
REF	NP_651883 XP_001358995 XP_001964574 XP_001981061 XP_002013189