BMRB Entry 25047

Name: RRM-Peptide and RES Complex
Published: 2014-08-26

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PDB ID: 4uqt
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25047
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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-Peptide and RES Complex

Deposition date:

2014-06-25

Original release date:

2014-08-26

Authors:

Tripsianes, Konstantinos; Friberg, A.; Barrandon, C.; Seraphin, B.; Sattler, M.

Citation:

Citation: Tripsianes, Konstantinos; Friberg, A.; Barrandon, C.; Seraphin, B.; Sattler, M.. "A Novel RRM-Peptide Interaction in the RES Complex" J. Biol. Chem. ., .-..

Assembly members:

Assembly members:
RRM, polymer, 93 residues, 10207.3111 Da.
RES, polymer, 39 residues, 4209.7028 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
RRM: GAMGNEYKDNAYIYIGNLNR ELTEGDILTVFSEYGVPVDV ILSRDENTGESQGFAYLKYE DQRSTILAVDNLNGFKIGGR ALKIDHTFYRPKR
RES: GAMGNRFAIMPGSRWDGVHR SNGFEEKWFAKQNEINEKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
1H chemical shifts	861
13C chemical shifts	427
15N chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RRM	1
2	RES	2

Entities:

Entity 1, RRM 93 residues - 10207.3111 Da.

1

GLY

ALA

MET

GLY

ASN

GLU

TYR

LYS

ASP

ASN

2

ALA

TYR

ILE

TYR

ILE

GLY

ASN

LEU

ASN

ARG

3

GLU

LEU

THR

GLU

GLY

ASP

ILE

LEU

THR

VAL

4

PHE

SER

GLU

TYR

GLY

VAL

PRO

VAL

ASP

VAL

5

ILE

LEU

SER

ARG

ASP

GLU

ASN

THR

GLY

GLU

6

SER

GLN

GLY

PHE

ALA

TYR

LEU

LYS

TYR

GLU

7

ASP

GLN

ARG

SER

THR

ILE

LEU

ALA

VAL

ASP

8

ASN

LEU

ASN

GLY

PHE

LYS

ILE

GLY

ARG

9

ALA

LEU

LYS

ILE

ASP

HIS

THR

PHE

TYR

ARG

10

PRO

LYS

ARG

Entity 2, RES 39 residues - 4209.7028 Da.

1

GLY

ALA

MET

GLY

ASN

ARG

PHE

ALA

ILE

MET

2

PRO

GLY

SER

ARG

TRP

ASP

GLY

VAL

HIS

ARG

3

SER

ASN

GLY

PHE

GLU

LYS

TRP

PHE

ALA

4

LYS

GLN

ASN

GLU

ILE

ASN

GLU

LYS

Samples:

sample_new_1: RRM, [U-13C; U-15N], 0.5 mM; RES, [U-13C; U-15N], 0.5 mM; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_new_1: ionic strength: 25.000 mM; pH: 6.300; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
15N-EDITED 3D NOESY	sample_new_1	solution	sample_conditions_new_1
13C- EDITED 3D NOESY (ALIPHATICS)	sample_new_1	solution	sample_conditions_new_1
13C-EDITED 3D NOESY (AROMATICS)	sample_new_1	solution	sample_conditions_new_1
13C- EDITED 3D NOESY (ALIPHATICS) F1 15N/13C FILTERED	sample_new_1	solution	sample_conditions_new_1

Software:

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

CYANA vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

CcpNmr_Analysis v2.1, CCPN - chemical shift assignment

TALOS vany, Cornilescu, Delaglio and Bax - chemical shift assignment

NMR spectrometers:

BRUKER AVANCE 800 MHz

UNP	IST3_YEAST CWC26_YEAST
BMRB	19766 25442 25443
PDB	2MKC 2MY2 2MY3 4UQT 4UQT
DBJ	GAA23224
EMBL	CAA59179 CAA96886 CAY79593
GB	AAS56830 AHY79214 EDN61950 EDV10384 EDZ72293
REF	NP_011341
SP	P46947
TPG	DAA07939
AlphaFold	D6VVT5 D6VTX8 P46947