BMRB Entry 18702

Name: RNA BINDING PROTEIN Solution structure of the third KH domain of KSRP in complex with the G-rich target sequence.
Published: 2012-11-05

Click here to enlarge.

PDB ID: 4b8t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18702
MolProbity Validation Chart

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:

RNA BINDING PROTEIN Solution structure of the third KH domain of KSRP in complex with the G-rich target sequence.

Deposition date:

2012-09-05

Original release date:

2012-11-05

Authors:

Nicastro, Giuseppe; Garcia-mayoral, M.; Hollingworth, D.; Kelly, G.; Martin, S.; Briata, P.; Gherzi, R.; Ramos, A.

Citation:

Citation: Nicastro, Giuseppe; Garcia-Mayoral, Maria Flor; Hollingworth, David; Kelly, Geoff; Martin, Stephen; Briata, Paola; Gherzi, Roberto; Ramos, Andres. "Noncanonical G recognition mediates KSRP regulation of let-7 biogenesis." Nat. Struct. Mol. Biol. 19, 1282-1286 (2012).
PubMed: 23142982

Assembly members:

Assembly members:
KH-TYPE_SPLICING_REGULATORY_PROTEIN, polymer, 106 residues, 10903.4744 Da.
5'-R(*AP*GP*GP*GP*UP)-3', polymer, 5 residues, 1690.0234 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KH-TYPE_SPLICING_REGULATORY_PROTEIN: GAMAYGSRIGGGIDVPVPRH SVGVVIGRSGEMIKKIQNDA GVRIQFKQDDGTGPEKIAHI MGPPDRCEHAARIINDLLQS LRSGPPGPPGGPGMPPGGRG RGRGQG
5'-R(*AP*GP*GP*GP*UP)-3': AGGGU

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	235
1H chemical shifts	523

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KH-TYPE SPLICING REGULATORY PROTEIN	1
2	5'-R(APGPGPGP*UP)-3'	2

Entities:

Entity 1, KH-TYPE SPLICING REGULATORY PROTEIN 106 residues - 10903.4744 Da.

1

GLY

ALA

MET

ALA

TYR

GLY

SER

ARG

ILE

GLY

2

GLY

ILE

ASP

VAL

PRO

VAL

PRO

ARG

HIS

3

SER

VAL

GLY

VAL

ILE

GLY

ARG

SER

GLY

4

GLU

MET

ILE

LYS

ILE

GLN

ASN

ASP

ALA

5

GLY

VAL

ARG

ILE

GLN

PHE

LYS

GLN

ASP

6

GLY

THR

GLY

PRO

GLU

LYS

ILE

ALA

HIS

ILE

7

MET

GLY

PRO

ASP

ARG

CYS

GLU

HIS

ALA

8

ALA

ARG

ILE

ASN

ASP

LEU

GLN

SER

9

LEU

ARG

SER

GLY

PRO

GLY

PRO

GLY

10

GLY

PRO

GLY

MET

PRO

GLY

ARG

GLY

11

ARG

GLY

ARG

GLY

GLN

GLY

Entity 2, 5'-R(*AP*GP*GP*GP*UP)-3' 5 residues - 1690.0234 Da.

1

A

G

U

Samples:

sample_1: KH-TYPE SPLICING REGULATORY PROTEIN, [U-13C; U-15N], 300 uM; 5'-R(*AP*GP*GP*GP*UP)-3', [U-13C; U-15N], 300 uM

sample_conditions_1: ionic strength: 100.000 mM; pH: 7.400; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
Experiment-1	sample_1	solution	sample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - chemical shift assignment

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - data analysis

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

SPARKY vany, Goddard - chemical shift assignment

UXNMR v3.5, Bruker Biospin - chemical shift assignment

VNMR vany, Varian - chemical shift assignment

NMR spectrometers:

Bruker Avance 700 MHz

UNP	FUBP2_HUMAN
PDB	2HH3 4B8T 4B8T
AlphaFold	Q9UQH5