BMRB Entry 5857

Name: NMR assignment of human Sip(7-50)
Published: 2006-06-26

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5857

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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:

NMR assignment of human Sip(7-50)

Deposition date:

2003-07-03

Original release date:

2006-06-26

Authors:

Santelli, E.; Liddington, R.; Preece, N.

Citation:

Citation: Santelli, E.; Leone, M.; Li, C.; Fukushima, T.; Preece, N.; Olson, A.; Ely, K.; Reed, J.; Pellecchia, M.; Liddington, R.; Matsuzawa, S.. "Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex" J. Biol. Chem. 280, 34278-34287 (2005).
PubMed: 16085652

Assembly members:

Assembly members:
GSH-SIP(short), polymer, 51 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GSH-SIP(short): GSHMAASEELQKDLEEVKVL LEKATRKRVRDALTAEKSKI ETEIKNKMQQK

Data sets:

assigned_chemical_shifts
- cs_set_1
coupling_constants
- cc_set_1

Data type	Count
13C chemical shifts	175
15N chemical shifts	43
1H chemical shifts	226
coupling constants	6

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GSH-SIP7-50 subunit1	1
2	GSH-SIP7-50 subunit2	1

Entities:

Entity 1, GSH-SIP7-50 subunit1 51 residues - Formula weight is not available

1

GLY

SER

HIS

MET

ALA

SER

GLU

LEU

2

GLN

LYS

ASP

LEU

GLU

VAL

LYS

VAL

LEU

3

LEU

GLU

LYS

ALA

THR

ARG

LYS

ARG

VAL

ARG

4

ASP

ALA

LEU

THR

ALA

GLU

LYS

SER

LYS

ILE

5

GLU

THR

GLU

ILE

LYS

ASN

LYS

MET

GLN

6

LYS

Samples:

sample_1: GSH-SIP(short), [U-15N; U-13C], 1.0 mM

sample_cond_1: ionic strength: 1.0 M; pH: 5.1; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
watergate/presat H1-H1 NOESY	not available	not available	not available
N15-HSQC	not available	not available	not available
N15-TOCSYHSQC	not available	not available	not available
N15-NOESYHSQC	not available	not available	not available
C13-HSQC	not available	not available	not available
C(CO)NH/C(CC-TOCSY-CO)N-NH	not available	not available	not available
H(CCO)NH/H(CC-TOCSY-CO)N-NH	not available	not available	not available
CBCA(CO)NH	not available	not available	not available
HNCO	not available	not available	not available
HNHA	not available	not available	not available
HNHB	not available	not available	not available
HNCA	not available	not available	not available
HNCACB	not available	not available	not available

Software:

VNMR v6.1C - collection

FELIX v2000 - processing, spectral display

NMR spectrometers:

Varian UNITYplus 500 MHz

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