BMRB Entry 16444

Name: NMR Chemical Shifts of GB1-SC35
Published: 2010-10-07

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16444

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR Chemical Shifts of GB1-SC35

Deposition date:

2009-08-06

Original release date:

2010-10-07

Authors:

Clayton, Jonathan; Goult, Benjamin; Lian, Lu-Yun

Citation:

Citation: Clayton, Jonathan; Phelan, Marie; Goult, Benjamin; Hautbergue, Guillaume; Wilson, Stuart; Lian, Lu-Yun. "The (1)H, (13)C and (15)N backbone and side-chain assignment of the RRM domain of SC35, a regulator of pre-mRNA splicing." Biomol. NMR Assignments 5, 7-10 (2011).
PubMed: 20703835

Assembly members:

Assembly members:
SC35, polymer, 158 residues, Formula weight is not available

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: pET24b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SC35: MQYKLILNGKTLKGETTTEA VDAATAEKVFKQYANDNGVD GEWTYDDATKTFTVTEGSHH HHHHMDVEGMTSLKVDNLTY RTSPDTLRRVFEKYGRVGDV YIPRDRYTKESRGFAFVRFH DKRDAEDAMDAMDGAVLDGR ELRVQMARYGRPPDSHHS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	668
15N chemical shifts	155
1H chemical shifts	1028

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SC35	1

Entities:

Entity 1, SC35 158 residues - Formula weight is not available

Residues 1-65 represent a Protein GB1 solubility tag plus a hexa-His tag for purification.

1

MET

GLN

TYR

LYS

LEU

ILE

LEU

ASN

GLY

LYS

2

THR

LEU

LYS

GLY

GLU

THR

GLU

ALA

3

VAL

ASP

ALA

THR

ALA

GLU

LYS

VAL

PHE

4

LYS

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

5

GLY

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

6

THR

PHE

THR

VAL

THR

GLU

GLY

SER

HIS

7

HIS

MET

ASP

VAL

GLU

GLY

MET

8

THR

SER

LEU

LYS

VAL

ASP

ASN

LEU

THR

TYR

9

ARG

THR

SER

PRO

ASP

THR

LEU

ARG

VAL

10

PHE

GLU

LYS

TYR

GLY

ARG

VAL

GLY

ASP

VAL

11

TYR

ILE

PRO

ARG

ASP

ARG

TYR

THR

LYS

GLU

12

SER

ARG

GLY

PHE

ALA

PHE

VAL

ARG

PHE

HIS

13

ASP

LYS

ARG

ASP

ALA

GLU

ASP

ALA

MET

ASP

14

ALA

MET

ASP

GLY

ALA

VAL

LEU

ASP

GLY

ARG

15

GLU

LEU

ARG

VAL

GLN

MET

ALA

ARG

TYR

GLY

16

ARG

PRO

ASP

SER

HIS

SER

Samples:

cn_H2O: SC35, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

cn_D2O: SC35, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 100%; NaCl 100 mM

n_H2O: SC35, [U-100% 15N], 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

un_D2O: SC35 0.5 mM; D2O 100%; NaCl 100 mM

un_H2O: SC35 0.5 mM; H2O 90%; D2O 10%; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	cn_H2O	isotropic	sample_conditions_1
2D 1H-13C HSQC	cn_D2O	isotropic	sample_conditions_1
3D CBCA(CO)NH	cn_H2O	isotropic	sample_conditions_1
3D HNCO	cn_H2O	isotropic	sample_conditions_1
3D HNCA	cn_H2O	isotropic	sample_conditions_1
3D HNCACB	cn_H2O	isotropic	sample_conditions_1
3D HBHA(CO)NH	cn_H2O	isotropic	sample_conditions_1
3D HN(CO)CA	cn_H2O	isotropic	sample_conditions_1
3D HBHANH	cn_H2O	isotropic	sample_conditions_1
3D HCCH-TOCSY	cn_D2O	isotropic	sample_conditions_1
2D 1H-1H TOCSY	un_D2O	isotropic	sample_conditions_1
2D 1H-1H NOESY	un_D2O	isotropic	sample_conditions_1
3D 1H-15N NOESY	n_H2O	isotropic	sample_conditions_1
3D 1H-13C NOESY	cn_H2O	isotropic	sample_conditions_1
3D 1H-13C NOESY	cn_D2O	isotropic	sample_conditions_1
3D HN(CA)CO	cn_H2O	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CCPN_Analysis v1, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

BMRB	17705 17706 17707
PDB	2KN4 2LEA 2LEB 2LEC
DBJ	BAC03903 BAC36346 BAC39610 BAC40111 BAD74033
EMBL	CAA44306 CAA44307 CAA53383 CAA67134 CAJ82901
GB	AAA60306 AAC71000 AAH00339 AAH01303 AAH05493
PIR	A42701
PRF	1805195A 1805195B
REF	NP_001001305 NP_001009720 NP_001029290 NP_001029490 NP_001070697
SP	P30352 Q01130 Q06A98 Q3MHR5 Q5R1W5
TPG	DAA18198
AlphaFold	P30352 Q01130 Q06A98 Q3MHR5 Q5R1W5