BMRB Entry 11367

Name: Assigned chemical shifts of the human spliceosomal protein SF3b155
Published: 2011-09-07

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PDB ID: 2fho
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11367
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Assigned chemical shifts of the human spliceosomal protein SF3b155

Deposition date:

2010-09-08

Original release date:

2011-09-07

Authors:

Kuwasako, K.; Dohmae, N.; Inoue, M.; Shirouzu, M.; Guntert, P.; Seraphin, B.; Muto, Y.; Yokoyama, S.

Citation:

Citation: Kuwasako, K.; Dohmae, N.; Inoue, M.; Shirouzu, M.; Guntert, P.; Seraphin, B.; Muto, Y.; Yokoyama, S.. "NMR solution structure of the human spliceosomal protein complex p14-SF3b155" .

Assembly members:

Assembly members:
spliceosomal protein SF3b155, residues in database 379-424, polymer, 47 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: cell free synthesis Host organism: E. coli - cell free Vector: PGEX6P-1-SF3B155(379-424)-HIS6-P14(8-93)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
spliceosomal protein SF3b155, residues in database 379-424: GTPEQLQAWRWEREIDERNR PLSDEELDAMFPEGYKVLPP PAGYVPI

Data sets:

assigned_chemical_shifts
- chemical_shift_1

Data type	Count
13C chemical shifts	206
15N chemical shifts	42
1H chemical shifts	323

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spliceosomal protein SF3b155, residues in database 379-424	1

Entities:

Entity 1, spliceosomal protein SF3b155, residues in database 379-424 47 residues - Formula weight is not available

1

GLY

THR

PRO

GLU

GLN

LEU

GLN

ALA

TRP

ARG

2

TRP

GLU

ARG

GLU

ILE

ASP

GLU

ARG

ASN

ARG

3

PRO

LEU

SER

ASP

GLU

LEU

ASP

ALA

MET

4

PHE

PRO

GLU

GLY

TYR

LYS

VAL

LEU

PRO

5

PRO

ALA

GLY

TYR

VAL

PRO

ILE

Samples:

sample_1: spliceosomal protein SF3b155, residues in database 379-424 300 mM; Sodium Phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 15N-separated NOESY	sample_1	isotropic	condition_1
3D 13C-separated NOESY	sample_1	isotropic	condition_1

Software:

xwinnmr v3.5, Bruker - collection

NMRPipe v20030801, Delaglio, F - processing

NMRView v5.0.4, Johnson, B.A - data analysis

Kujira v0.8995, Kobayashi, N - data analysis

CYANA v2.1, Guntert, P - refinement, structure solution

OPALP v1.4, Koradi, R. - refinement, structure solution

NMR spectrometers:

Bruker AVANCE 700 MHz

BMRB	11366
PDB	2F9D 2F9J 2FHO 3LQV
DBJ	BAB28369 BAB40140 BAE24537 BAE27592
EMBL	CAA70201
GB	AAC97189 AAG01404 AAH03419 AAH15530 AAH28959
REF	NP_001084150 NP_001179923 NP_001252892 NP_036565 NP_112456
SP	O57683 O75533 Q99NB9
TPG	DAA32571
AlphaFold	O57683 O75533 Q99NB9