BMRB Entry 16221

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for Collagen Binding domain of MMP2
Deposition date:
2009-03-23
Original release date:
2009-06-02
Authors:
Xu, Xiaoping
Citation:

Citation: Xu, Xiaoping; Mikhailova, Margarita; Ilangovan, Udayar; Chen, Zhihua; Yu, Agnes; Pal, Sanjay; Hinck, Andrew; Steffensen, Bjorn. "Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2"  Biochemistry ., 5822-5831 (2009).
PubMed: 19459623

Assembly members:

Assembly members:
CBD_of_MMP2, polymer, 190 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   Vector: pGYMX

Data sets:
Data typeCount
13C chemical shifts123
15N chemical shifts43
1H chemical shifts89

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBD domain1

Entities:

Entity 1, CBD domain 190 residues - Formula weight is not available

1   METALATHRSERHISHISHISHISHISHIS
2   ILEGLUGLYARGALASERVALVALARGVAL
3   LYSTYRGLYASNALAASPGLYGLUTYRCYS
4   LYSPHEPROPHELEUPHEASNGLYLYSGLU
5   TYRASNSERCYSTHRASPTHRGLYARGSER
6   ASPGLYPHELEUTRPCYSSERTHRTHRTYR
7   ASNPHEGLULYSASPGLYLYSTYRGLYPHE
8   CYSPROHISGLUALALEUPHETHRMETGLY
9   GLYASNALAGLUGLYGLNPROCYSLYSPHE
10   PROPHEARGPHEGLNGLYTHRSERTYRASP
11   SERCYSTHRTHRGLUGLYARGTHRASPGLY
12   TYRARGTRPCYSGLYTHRTHRGLUASPTYR
13   ASPARGASPLYSLYSTYRGLYPHECYSPRO
14   GLUTHRALAMETSERTHRVALGLYGLYASN
15   SERGLUGLYALAPROCYSVALPHEPROPHE
16   THRPHELEUGLYASNLYSTYRGLUSERCYS
17   THRSERALAGLYARGSERASPGLYLYSMET
18   TRPCYSALATHRTHRALAASNTYRASPASP
19   ASPARGLYSTRPGLYPHECYSPROASPGLN

Samples:

15N_CBD: CBD_of_MMP2, [U-15N], 0.5 ± 0.05 mM; H2O 95%; D2O 5%

13C15N_CBD: CBD_of_MMP2, [U-95% 13C; U-95% 15N], 0.5 ± 0.05 mM; H2O 95%; D2O 5%

label1: pH: 7.0; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_CBDisotropiclabel1
2D 1H-13C HSQC13C15N_CBDisotropiclabel1
3D HNCACB13C15N_CBDisotropiclabel1
3D CBCA(CO)NH13C15N_CBDisotropiclabel1
3D C(CO)NH13C15N_CBDisotropiclabel1
3D HNCA13C15N_CBDisotropiclabel1
3D HNCO13C15N_CBDisotropiclabel1
3D HNHA15N_CBDisotropiclabel1
3D HCACO13C15N_CBDisotropiclabel1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

xwinnmr, Bruker Biospin - collection

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 700 MHz

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