BMRB Entry 5153

Title:
Backbone dynamics of the N-TIMP-1 bound to MMP-3 catalytic domain
Deposition date:
2001-09-16
Original release date:
2003-01-29
Authors:
Gao, Guanghua; Arumugam, Sengodagounder; Van Doren, Steven
Citation:

Citation: Gao, Guanghua; Arumugam, Sengodagounder; Patton, Brian; Semenchenko, Valentyna; Brew, Keith; Van Doren, Steven. "Binding of the MMP-3 catalytic domain to N-TIMP-1 is driven by a large gain in entropy that includes modest contributions from the hydrophobic effect and the TIMP-1 backbone"  J. Mol. Biol. ., .-..

Assembly members:

Assembly members:
N-terminal domain of Tissue Inhibitor of Metalloproteinases-1, polymer, 126 residues, Formula weight is not available
MatrixMetalloProteinases-3(catalytic domain), polymer, 173 residues, Formula weight is not available
CA, non-polymer, 40.078 Da.
ZN, non-polymer, 65.409 Da.

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

Data sets:
Data typeCount
T1 relaxation values85
T2 relaxation values85
order parameters86

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-TIMP-1, inhibitor1
2MMP-3, metalloproteinase2
3CALCIUM (II) ION, I3
4CALCIUM (II) ION, II3
5CALCIUM (II) ION, III3
6ZINC (II) ION, I4
7ZINC (II) ION, II4

Entities:

Entity 1, N-TIMP-1, inhibitor 126 residues - Formula weight is not available

1   CYSTHRCYSVALPROPROHISPROGLNTHR
2   ALAPHECYSASNSERASPLEUVALILEARG
3   ALALYSPHEVALGLYTHRPROGLUVALASN
4   GLNTHRTHRLEUTYRGLNARGTYRGLUILE
5   LYSMETTHRLYSMETTYRLYSGLYPHEGLN
6   ALALEUGLYASPALAALAASPILEARGPHE
7   VALTYRTHRPROALAMETGLUSERVALCYS
8   GLYTYRPHEHISARGSERHISASNARGSER
9   GLUGLUPHELEUILEALAGLYLYSLEUGLN
10   ASPGLYLEULEUHISILETHRTHRCYSSER
11   PHEVALALAPROTRPASNSERLEUSERLEU
12   ALAGLNARGARGGLYPHETHRLYSTHRTYR
13   THRVALGLYCYSGLUGLU

Entity 2, MMP-3, metalloproteinase 173 residues - Formula weight is not available

1   PHEARGTHRPHEPROGLYILEPROLYSTRP
2   ARGLYSTHRHISLEUTHRTYRARGILEVAL
3   ASNTYRTHRPROASPLEUPROLYSASPALA
4   VALASPSERALAVALGLULYSALALEULYS
5   VALTRPGLUGLUVALTHRPROLEUTHRPHE
6   SERARGLEUTYRGLUGLYGLUALAASPILE
7   METILESERPHEALAVALARGGLUHISGLY
8   ASPPHETYRPROPHEASPGLYPROGLYASN
9   VALLEUALAHISALATYRALAPROGLYPRO
10   GLYILEASNGLYASPALAHISPHEASPASP
11   ASPGLUGLNTRPTHRLYSASPTHRTHRGLY
12   THRASNLEUPHELEUVALALAALAHISGLN
13   ILEGLYHISSERLEUGLYLEUPHEHISSER
14   ALAASNTHRGLUALALEUMETTYRPROLEU
15   TYRHISSERLEUTHRASPLEUTHRARGPHE
16   ARGLEUSERGLNASPASPILEASNGLYILE
17   GLNSERLEUTYRGLYPROPROPROASPSER
18   PROGLUTHR

Entity 3, CALCIUM (II) ION, I - Ca - 40.078 Da.

1   CA

Entity 4, ZINC (II) ION, I - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: N-terminal domain of Tissue Inhibitor of Metalloproteinases-1, [U-98% 15N; U-98% 2H], 0.3 mM; MatrixMetalloProteinases-3(catalytic domain), [U-98% 15N; U-98% 2H], 0.3 mM; Tris, [U-2H], 20 mM; NaCl 125 mM; CaCl2 10 mM; NaN3 1 mM; ZnCl2 50 mM; H2O 93%; D2O 7%

condition_1: pH: 6.22; temperature: 307 K

Experiments:

NameSampleSample stateSample conditions
15N T1 relaxationsample_1not availablecondition_1
15N T2 relaxationsample_1not availablecondition_1
heteronuclear 1H-15N NOEsample_1not availablecondition_1

Software:

Sybyl TRIAD v6.3 -

ModelFree v4.1 -

NMR spectrometers:

  • Varian Inova 600 MHz

Related Database Links:

BMRB 15120 15395 15396 4173 4364 4365 4366 5099 5231 5785 5231 5099 4366 4365 4364 4173 15396 15395 15120
PDB
DBJ BAD97003 BAD97011 BAG36115 BAG36115 BAD97011 BAD97003
EMBL CAA28859 CAA28859
GB AAA00036 AAA36321 AAB36942 AAD45887 AAH69676
REF NP_002413 XP_002822450 XP_003253099 XP_003828425 XP_004052086 XP_508723 XP_001154004 XP_001153941 NP_002413
SP P08254
SWISS-PROT P08254
GenBank AAH69676 AAD45887 AAB36942 AAA36321 AAA00036
AlphaFold P08254