BMRB Entry 21010

Name: The Binding Mechanism of a Peptidylic Cyclic Serine Protease Inhibitor - extended upain
Published: 2012-08-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR21010

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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:

The Binding Mechanism of a Peptidylic Cyclic Serine Protease Inhibitor - extended upain

Deposition date:

2011-04-29

Original release date:

2012-08-07

Authors:

Svane, Anna; Jensen, Jan; Nielsen, Jakob; Nielsen, Niels; Malmendal, Anders

Citation:

Citation: Jiang, Longguang; Svane, Anna; Sorensen, Hans Peter; Jensen, Jan; Hosseini, Masood; Chen, Zhuo; Weydert, Caroline; Nielsen, Jakob; Christensen, Anni; Yuan, Cai; Jensen, Knud; Nielsen, Niels; Malmendal, Anders; Huang, Mingdong; Andreasen, Peter. "The binding mechanism of a peptidic cyclic serine protease inhibitor" J. Mol. Biol. 412, 235-250 (2011).
PubMed: 21802428

Assembly members:

Assembly members:
extended_upain, polymer, 25 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
extended_upain: XMGSADGACSWRGLENHAMC GAAGX

Data sets:

assigned_chemical_shifts
- assigned_chem_shift

Data type	Count
13C chemical shifts	48
1H chemical shifts	129

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	extended upain	1

Entities:

Entity 1, extended upain 25 residues - Formula weight is not available

N-terminal acetyl, C-terminal amide

1

ACE

MET

GLY

SER

ALA

ASP

GLY

ALA

CYS

SER

2

TRP

ARG

GLY

LEU

GLU

ASN

HIS

ALA

MET

CYS

3

GLY

ALA

GLY

NH2

Samples:

sample: extended upain 2 mM; H2O 90%; D2O 10%

sample_conditions: pH: 7.4; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample	isotropic	sample_conditions
2D 1H-13C HSQC	sample	isotropic	sample_conditions
2D 1H-1H NOESY	sample	isotropic	sample_conditions
2D 1H-1H COSY	sample	isotropic	sample_conditions

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Bruker Avance 800 MHz