BMRB Entry 25970

Name: NMR structure of the Acidic domain of SYNCRIP (24-140)
Published: 2016-05-31

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PDB ID: 2nbb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25970
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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:

NMR structure of the Acidic domain of SYNCRIP (24-140)

Deposition date:

2016-02-02

Original release date:

2016-05-31

Authors:

Serrano, Pedro; Wuthrich, Kurt; Beuck, Christine

Citation:

Citation: Beuck, Christine; Williamson, James; Wuthrich, Kurt; Serrano, Pedro. "The acidic domain is a unique structural feature of the splicing factor SYNCRIP" Protein Sci. 25, 1545-1550 (2016).
PubMed: 27081926

Assembly members:

Assembly members:
entity, polymer, 118 residues, 12932.589 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSENFQTLLDAGLPQKVAEK LDEIYVAGLVAHSDLDERAI EALKEFNEDGALAVLQQFKD SDLSHVQNKSAFLCGVMKTY RQREKQGTKVADSSKGPDEA KIKALLERTGYTLDVTTG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	478
15N chemical shifts	127
1H chemical shifts	777

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 118 residues - 12932.589 Da.

1

GLY

SER

GLU

ASN

PHE

GLN

THR

LEU

ASP

2

ALA

GLY

LEU

PRO

GLN

LYS

VAL

ALA

GLU

LYS

3

LEU

ASP

GLU

ILE

TYR

VAL

ALA

GLY

LEU

VAL

4

ALA

HIS

SER

ASP

LEU

ASP

GLU

ARG

ALA

ILE

5

GLU

ALA

LEU

LYS

GLU

PHE

ASN

GLU

ASP

GLY

6

ALA

LEU

ALA

VAL

LEU

GLN

PHE

LYS

ASP

7

SER

ASP

LEU

SER

HIS

VAL

GLN

ASN

LYS

SER

8

ALA

PHE

LEU

CYS

GLY

VAL

MET

LYS

THR

TYR

9

ARG

GLN

ARG

GLU

LYS

GLN

GLY

THR

LYS

VAL

10

ALA

ASP

SER

LYS

GLY

PRO

ASP

GLU

ALA

11

LYS

ILE

LYS

ALA

LEU

GLU

ARG

THR

GLY

12

TYR

THR

LEU

ASP

VAL

THR

GLY

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

DYANA, G??ntert P. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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