BMRB Entry 5785

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5785
MolProbity Validation Chart

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Title:
Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings
Deposition date:
2003-04-25
Original release date:
2004-03-15
Authors:
Arumugam, S.; Van Doren, Steven
Citation:

Citation: Arumugam, S.; Van Doren, Steven. "Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings "  Biochemistry 42, 7950-7958 (2003).
PubMed: 12834347

Assembly members:

Assembly members:
Matrix MetalloProteinases-3 or stromelysin 1, polymer, 173 residues, 19492 Da.
N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1, polymer, 126 residues, 14252 Da.
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   Host organism: Escherichia coli   Vector: pGEMEX-MMP-3(DC)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Matrix MetalloProteinases-3 or stromelysin 1: FRTFPGIPKWRKTHLTYRIV NYTPDLPKDAVDSAVEKALK VWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGN VLAHAYAPGPGINGDAHFDD DEQWTKDTTGTNLFLVAAHQ IGHSLGLFHSANTEALMYPL YHSLTDLTRFRLSQDDINGI QSLYGPPPDSPET
N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1: CTCVPPHPQTAFCNSDLVIR AKFVGTPEVNQTTLYQRYEI KMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRS EEFLIAGKLQDGLLHITTCS FVAPWNSLSLAQRRGFTKTY TVGCEE

Data sets:
Data typeCount
1H chemical shifts729
13C chemical shifts495
15N chemical shifts138

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Matrix MetalloProteinase-3 catalytic domain1
2N-TIMP-1, inhibitor2
3CALCIUM (II) ION, I3
4CALCIUM (II) ION, II3
5CALCIUM (II) ION, III3
6ZINC (II) ION, I4
7ZINC (II) ION, II4

Entities:

Entity 1, Matrix MetalloProteinase-3 catalytic domain 173 residues - 19492 Da.

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 2, N-TIMP-1, inhibitor 126 residues - 14252 Da.

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 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: Matrix MetalloProteinases-3 or stromelysin 1, [U-98% 15N], 0.8 mM; N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1 0.8 mM

sample_2: Matrix MetalloProteinases-3 or stromelysin 1, [U-98% 13C; U-98% 15N], 0.8 mM; N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1 0.8 mM

sample_3: Matrix MetalloProteinases-3 or stromelysin 1, [U-96% 2H], 0.6 mM; N-terminal domain of Tissue Inhibitor of MatrixmetalloProteinases-1 0.6 mM

EXP-COND_1: pH: 6.6; temperature: 310 K; ionic strength: 0.145 M

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availableEXP-COND_1

Software:

SYBYL TRIAD v6.2, 6.3, 6.6 - data process, data analysis

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 4327 5154 5153 5154 4327 5099
PDB
DBJ BAA01913 BAG34878 BAG52016 BAG52016 BAA01913 BAG34878
EMBL CAA26443 CAA26902 CAG28566 CAG46779 CAH90650 CAG46779 CAH90650 CAA26902 CAG28566 CAA26443
GB AAA52436 AAA63234 AAA99943 AAD14009 AAH00866
PIR JC4303 JC4303
PRF 1107278A 1308125A 1107278A 1308125A
REF NP_001028111 NP_001125351 NP_003245 XP_003271098 XP_003917687 NP_001028111 NP_003245
SP P01033 P49061 Q5RC60 Q95KL9
SWISS-PROT Q5RC60 Q95KL9 P01033 P49061
GenBank AAH00866 AAA99943 AAD14009 AAA52436 AAA63234
AlphaFold P01033 P49061 Q5RC60 Q95KL9

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