BMRB Entry 5262

Title:
Backbone 1H and 15N Chemical Shift Assignements for the first fibronectin type II module of MMP-2 (col-1)
Deposition date:
2002-01-20
Original release date:
2002-06-13
Authors:
Gehrmann, Marion; Briknarova, Klara; Banyai, Laszlo; Patthy, Laszlo; Llinas, Miguel
Citation:

Citation: Gehrmann, Marion; Briknarova, Klara; Banyai, Laszlo; Patthy, Laszlo; Llinas, Miguel. "The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-binding Fibronectin Type II Modules and Lysine-binding Kringle Domains"  Biol. Chem. 383, 137-148 (2002).
PubMed: 11928808

Assembly members:

Assembly members:
the first fibronectin type II module of human matrix metalloproteinase, polymer, 60 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   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
the first fibronectin type II module of human matrix metalloproteinase: RIPVKYGNADGEYCKFPFLF NGKEYNSCTDTGRSDGFLWC STTYNFEKDGKYGFCPHEAL

Data sets:
Data typeCount
15N chemical shifts62
1H chemical shifts397

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1col-11

Entities:

Entity 1, col-1 60 residues - Formula weight is not available

1   ARGILEPROVALLYSTYRGLYASNALAASP
2   GLYGLUTYRCYSLYSPHEPROPHELEUPHE
3   ASNGLYLYSGLUTYRASNSERCYSTHRASP
4   THRGLYARGSERASPGLYPHELEUTRPCYS
5   SERTHRTHRTYRASNPHEGLULYSASPGLY
6   LYSTYRGLYPHECYSPROHISGLUALALEU

Samples:

sample_1: the first fibronectin type II module of human matrix metalloproteinase 0.5 mM; H2O 90%; acetone, [U-2H], 10%

sample_2: the first fibronectin type II module of human matrix metalloproteinase 0.5 mM

sample_3: the first fibronectin type II module of human matrix metalloproteinase, [U-15N], 0.7 mM

condition_1: pH*: 7.3; temperature: 298 K

condition_2: pH*: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D COSYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D HNHAnot availablenot availablenot available
3D HNHBnot availablenot availablenot available
3D 15N-edited TOCSYnot availablenot availablenot available
3D 15N-edited NOESYnot availablenot availablenot available

Software:

XWINNMR v2.0 - experiment acquisition

FELIX v98 - data processing and assignment

XPLOR v3.851 - structure calculation

NMR spectrometers:

  • Bruker AvanceDMX 500 MHz

Related Database Links:

PDB

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