BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 5099

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5099

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Title: Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for N-TIMP-1 in N-TIMP-1/MMP-3(E202Q) Complex   PubMed: 12634064

Deposition date: 2001-08-03 Original release date: 2003-05-20

Authors: Arumugam, S.; Van Doren, Steven

Citation: Arumugam, S.; Gao, G.; Patton, B.; Semenchenko, V.; Brew, K.; Van Doren, Steven. "Increased backbone mobility in Beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3"  J. Mol. Biol. 327, 719-734 (2003).

Assembly members:
N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex, polymer, 126 residues, Formula weight is not available
Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255), polymer, 173 residues, Formula weight is not available
CA, non-polymer, 40.078 Da.
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex: CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE
Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255): FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHQ IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET

Data sets:
Data typeCount
1H chemical shifts488
13C chemical shifts327
15N chemical shifts113

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) ION3
4ZINC (II) ION4

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 - Ca - 40.078 Da.

1   CA

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

1   ZN

Samples:

sample_1: N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex, [U-13C; U-15N], 0.66 mM; Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255) 0.66 mM; Tris, [U-2H], 20 mM; NaCl 125 mM; CaCl2 10 mM; NaN3 1 mM; ZnCl2 50 uM; D2O 7%; H2O 93%

sample_2: N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex, [U-50% 2H; U-13C; U-15N], 0.52 mM; Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255) 0.52 mM; Tris, [U-2H], 20 mM; NaCl 125 mM; CaCl2 10 mM; NaN3 1 mM; ZnCl2 50 uM; D2O 7%; H2O 93%

sample_3: N-terminus of Tissue Inhibitor of Metalloproteinases-1/Matrix MetalloProteinases-3(catalytic domain) complex, [U-2H; U-13C; U-15N], 0.30 mM; Metalloproteinases-1/Matrix MetalloProteinase-3(catalytic domain, residue 83-255) 0.30 mM; Tris, [U-2H], 20 mM; NaCl 125 mM; CaCl2 10 mM; NaN3 1 mM; ZnCl2 50 uM; D2O 7%; H2O 93%

EX-COND-1: pH: 6.22; temperature: 307 K; ionic strength: 0.186 M

Experiments:

NameSampleSample stateSample conditions
2D 15N HSQCnot availablenot availableEX-COND-1
3D HNCAnot availablenot availableEX-COND-1
3D HN(CO)CAnot availablenot availableEX-COND-1
3D HNCOnot availablenot availableEX-COND-1
3D TROSY-HNCAnot availablenot availableEX-COND-1
NOESY-HSQCnot availablenot availableEX-COND-1

Software:

SYBYL TRIAD v6.2, 6.3, 6.6 - process NMR spectra, interpret NMR spectra

NMR spectrometers:

  • Bruker DRX 750 MHz
  • Bruker DRX 500 MHz
  • Varian Inova 600 MHz
  • Varian UnityPlus 720 MHz

Related Database Links:

BMRB 15120 15395 15396 4173 4364 4365 4366 5153 5231
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
. 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 5099 . . . . . . . . . . . . . . . . . . . . . . . . .

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts