BMRB Entry 4973

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4973

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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:

Sequential Assignment and Secondary Structure of Saratin, an Inhibitor of von Willebrand factor-dependent Platelet Adhesion to Collagen

Deposition date:

2001-03-16

Original release date:

2002-04-04

Authors:

Maurer, Till; Bomke, Joerg; Frech, Matthias; Rysoik, Thomas; Kalbitzer, Hans

Citation:

Citation: Maurer, Till; Bomke, Joerg; Frech, Matthias; Rysoik, Thomas; Kalbitzer, Hans. "Letter to the editor: Sequential Assignment and Secondary Structure of Saratin, an Inhibitor of von Willebrand factor-dependent Platelet Adhesion to Collagen" J. Biomol. NMR 21, 77-78 (2001).
PubMed: 11693575

Assembly members:

Assembly members:
saratin, polymer, 103 residues, 12068 Da.

Natural source:

Natural source: Common Name: leech Taxonomy ID: 6421 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Hirudo medicinalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Hansenula polymorpha

Entity Sequences (FASTA):

Entity Sequences (FASTA):
saratin: EEREDCWTFYANRKYTDFDK SFKKSSDLDECKKTCFKTEY CYIVFEDTVNKECYYNVVDG EELDQEKFVVDENFTENYLT DCEGKDAGNAAGTGDESDEV DED

Data sets:

assigned_chemical_shifts
- set_1

Data type	Count
13C chemical shifts	436
15N chemical shifts	112
1H chemical shifts	667

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	saratin	1

Entities:

Entity 1, saratin 103 residues - 12068 Da.

1

GLU

ARG

GLU

ASP

CYS

TRP

THR

PHE

TYR

2

ALA

ASN

ARG

LYS

TYR

THR

ASP

PHE

ASP

LYS

3

SER

PHE

LYS

SER

ASP

LEU

ASP

GLU

4

CYS

LYS

THR

CYS

PHE

LYS

THR

GLU

TYR

5

CYS

TYR

ILE

VAL

PHE

GLU

ASP

THR

VAL

ASN

6

LYS

GLU

CYS

TYR

ASN

VAL

ASP

GLY

7

GLU

LEU

ASP

GLN

GLU

LYS

PHE

VAL

8

ASP

GLU

ASN

PHE

THR

GLU

ASN

TYR

LEU

THR

9

ASP

CYS

GLU

GLY

LYS

ASP

ALA

GLY

ASN

ALA

10

ALA

GLY

THR

GLY

ASP

GLU

SER

ASP

GLU

VAL

11

ASP

GLU

ASP

Samples:

sample_1: saratin 1.5 mM; H2O 100%

sample_2: saratin, [U-15N], 1.5 mM; H2O 100%

sample_3: saratin, [U-5% 13C; U-15N], 1.7 mM; H2O 100%

sample_4: saratin 1.5 mM; D2O 100%

sample_5: saratin, [U-15N], 1.5 mM; D2O 100%

sample_6: saratin, [U-5% 13C; U-15N], 1.7 mM; D2O 100%

Ex-cond_1: ionic strength: 0.067 M; pH: 6.5; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N NOESY	not available	not available	Ex-cond_1
HNCA	not available	not available	Ex-cond_1
HNCO	not available	not available	Ex-cond_1
CBCA(CO)NH	not available	not available	Ex-cond_1
HCCH-TOCSY	not available	not available	Ex-cond_1
NOESY	not available	not available	Ex-cond_1
TOCSY	not available	not available	Ex-cond_1

Software:

xwinnmr v2.6 - data acqusition, data processing

AURELIA v2.7.10 - automated peak assignment, sequential and sequence specific assignment

NMR spectrometers:

Bruker DRX 800 MHz
Bruker DRX 500 MHz

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