BMRB Entry 6498

Click here to enlarge.

PDB ID: 1ysm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6498
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:

Backbone and side-chain 1H, 13C, and 15N Chemical Shift Assignments for SIP (1-77)

Deposition date:

2005-02-08

Original release date:

2005-08-16

Authors:

Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter

Citation:

Citation: Bhattacharya, Shibani; Lee, Young-Tae; Michowski, Wojciech; Filipek, Anna; Kuznicki, Jacek; Chazin, Walter. "The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies(,)." Biochemistry 44, 9462-9471 (2005).
PubMed: 15996101

Assembly members:

Assembly members:
single chain biopolymer, polymer, 77 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
single chain biopolymer: MASVLEELQKDLEEVKVLLE KSTRKRLRDTLTSEKSKIET ELKNKMQQKSQKKPELDNEK PAAVVAPLTTGYTVKIS

Data sets:

assigned_chemical_shifts
- CSR_1

Data type	Count
1H chemical shifts	561
13C chemical shifts	335
15N chemical shifts	77

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SIP N-Domain, SIP (1-77)	1

Entities:

Entity 1, SIP N-Domain, SIP (1-77) 77 residues - Formula weight is not available

1

MET

ALA

SER

VAL

LEU

GLU

LEU

GLN

LYS

2

ASP

LEU

GLU

VAL

LYS

VAL

LEU

GLU

3

LYS

SER

THR

ARG

LYS

ARG

LEU

ARG

ASP

THR

4

LEU

THR

SER

GLU

LYS

SER

LYS

ILE

GLU

THR

5

GLU

LEU

LYS

ASN

LYS

MET

GLN

LYS

SER

6

GLN

LYS

PRO

GLU

LEU

ASP

ASN

GLU

LYS

7

PRO

ALA

VAL

ALA

PRO

LEU

THR

8

GLY

TYR

THR

VAL

LYS

ILE

SER

Samples:

Sample_1: single chain biopolymer, [U-100% 13C; U-100% 15N], 1.0 mM; NaPi 20.0 mM; NaCl 50 mM; H2O 90%

Sample_2: single chain biopolymer, [U-100% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

Sample_3: single chain biopolymer, [U-10% 13C], 1 mM; NaPi 20 mM; NaCl 50 mM; D2O 100%

Exp_cond_1: pH: 7.0; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	not available	not available	not available
1H-13C CT-HSQC	not available	not available	not available
3D-HNCO	not available	not available	not available
3D-HNCACB	not available	not available	not available
3D-CBCA(CO)NH	not available	not available	not available
3D-HC(CCO)NH	not available	not available	not available
3D-(H)CC(CO)NH	not available	not available	not available
3D-HCCH-TOCSY	not available	not available	not available

Software:

FELIX v2000 - processing, analysis

NMR spectrometers:

Bruker AVANCE 600 MHz

PDB	1YSM
GB	AAC16757 AAH25948 EDL39341
REF	NP_033916
SP	Q9CXW3
AlphaFold	Q9CXW3