BMRB Entry 17552

Name: Backbone resonance chemical shift assignments of Ph SAM linker
Published: 2012-05-10

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17552

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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:

Backbone resonance chemical shift assignments of Ph SAM linker

Deposition date:

2011-03-28

Original release date:

2012-05-10

Authors:

Ilangovan, Udayar; Kim, Chongwoo

Citation:

Citation: Robinson, Angela; Leal, Belinda; Chadwell, Linda; Wang, Renjing; Ilangovan, Udayar; Kaur, Yogeet; Junco, Sarah; Schirf, Virgil; Osmulski, Pawel; Gaczynska, Maria; Hinck, Andrew; Demeler, Borries; McEwen, Donald; Kim, Chongwoo. "The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain." J. Biol. Chem. 287, 8702-8713 (2012).
PubMed: 22275371

Assembly members:

Assembly members:
Ph_SAM_Linker, polymer, 108 residues, Formula weight is not available

Natural source:

Natural source: Common Name: fruit fly Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-3c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ph_SAM_Linker: GTRGVGSGETNGLGTGGIVG VDAMALVDRLDEAMAEEKMQ TEATPKLSESFILGASTEVP MSLPVQAAISALAAPLGSLS VALPTLAPLSVVTSGAAPKS SEVNGTDR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	203
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Ph SAM linker	1

Entities:

Entity 1, Ph SAM linker 108 residues - Formula weight is not available

1

GLY

THR

ARG

GLY

VAL

GLY

SER

GLY

GLU

THR

2

ASN

GLY

LEU

GLY

THR

GLY

ILE

VAL

GLY

3

VAL

ASP

ALA

MET

ALA

LEU

VAL

ASP

ARG

LEU

4

ASP

GLU

ALA

MET

ALA

GLU

LYS

MET

GLN

5

THR

GLU

ALA

THR

PRO

LYS

LEU

SER

GLU

SER

6

PHE

ILE

LEU

GLY

ALA

SER

THR

GLU

VAL

PRO

7

MET

SER

LEU

PRO

VAL

GLN

ALA

ILE

SER

8

ALA

LEU

ALA

PRO

LEU

GLY

SER

LEU

SER

9

VAL

ALA

LEU

PRO

THR

LEU

ALA

PRO

LEU

SER

10

VAL

THR

SER

GLY

ALA

PRO

LYS

SER

11

SER

GLU

VAL

ASN

GLY

THR

ASP

ARG

Samples:

sample_1: Ph SAM Linker, [U-100% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_2: Ph SAM Linker, [U-100% 13C; U-100% 15N], 1.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 5; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCANH	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - Spectral Visualization

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker Avance 700 MHz
Bruker DRX 600 MHz

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