BMRB Entry 4679

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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/BMR4679
MolProbity Validation Chart

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Title:
1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Collagenase-3 (MMP-13) Complexed with a Hydroxamic acid Inhibitor
Deposition date:
2000-03-06
Original release date:
2002-04-01
Authors:
Moy, Franklin; Chanda, Pranab; Cosmi, Scott; Edris, Wade; Levin, Jeremy; Powers, Robert
Citation:

Citation: Moy, Franklin; Chanda, Pranab; Cosmi, Scott; Edris, Wade; Levin, Jeremy; Powers, Robert. "Letter to the Editor: 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Collagenase-3 (MMP-13) Complexed with a Hydroxamic acid Inhibitor"  J. Biomol. NMR 17, 269-270 (2000).

Assembly members:

Assembly members:
Human Collagenase-3, polymer, 165 residues, Formula weight is not available
WAY-151693, non-polymer, 427.474 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: pProMMP-13

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human Collagenase-3: YNVFPRTLKWSKMNLTYRIV NYTPDMTHSEVEKAFKKAFK VWSDVTPLNFTRLHDGIADI MISFGIKEHGDFYPFDGPSG LLAHAFPPGPNYGGDAHFDD DETWTSSSKGYNLFLVAAHE FGHSLGLDHSKDPGALMFPI YTYTGKSHFMLPDDDVQGIQ SLYGP

Data sets:
Data typeCount
13C chemical shifts635
1H chemical shifts928
15N chemical shifts140

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1Human Collagenase-31
2WAY-1516932

Entities:

Entity 1, Human Collagenase-3 165 residues - Formula weight is not available

1   TYRASNVALPHEPROARGTHRLEULYSTRP
2   SERLYSMETASNLEUTHRTYRARGILEVAL
3   ASNTYRTHRPROASPMETTHRHISSERGLU
4   VALGLULYSALAPHELYSLYSALAPHELYS
5   VALTRPSERASPVALTHRPROLEUASNPHE
6   THRARGLEUHISASPGLYILEALAASPILE
7   METILESERPHEGLYILELYSGLUHISGLY
8   ASPPHETYRPROPHEASPGLYPROSERGLY
9   LEULEUALAHISALAPHEPROPROGLYPRO
10   ASNTYRGLYGLYASPALAHISPHEASPASP
11   ASPGLUTHRTRPTHRSERSERSERLYSGLY
12   TYRASNLEUPHELEUVALALAALAHISGLU
13   PHEGLYHISSERLEUGLYLEUASPHISSER
14   LYSASPPROGLYALALEUMETPHEPROILE
15   TYRTHRTYRTHRGLYLYSSERHISPHEMET
16   LEUPROASPASPASPVALGLNGLYILEGLN
17   SERLEUTYRGLYPRO

Entity 2, WAY-151693 1 residues - C21 H21 N3 O5 S - 427.474 Da.

1   WAY

Samples:

sample_1: Human Collagenase-3, [U-15N], 1.0 mM; WAY-151693 1.0 mM; Tris-Base, [U-2H], 10 mM; NaCl 100 mM; CaCl2 5 mM; ZnCl2 0.1 mM; NaN3 2 mM; DTT, [U-2H], 10 mM; H2O 90%; D2O 10%

sample_2: Human Collagenase-3, [U-13C; U-15N], 1.0 mM; WAY-151693 1.0 mM; Tris-Base, [U-2H], 10 mM; NaCl 100 mM; CaCl2 5 mM; ZnCl2 0.1 mM; NaN3 2 mM; DTT, [U-2H], 10 mM; H2O 90%; D2O 10%

Ex-cond_1: pH: 6.5; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availableEx-cond_1

Software:

No software information available

NMR spectrometers:

  • Bruker AMX-2 600 MHz

Related Database Links:

PDB
DBJ BAD96468 BAF84900 BAG37740 BAQ35474
EMBL CAA53056 CAA57108
GB AAD38037 AAF17559 AAH67522 AAH67523 AAH74807
REF NP_002418 XP_001098794 XP_001098996 XP_001154361 XP_003253103
SP P45452
AlphaFold P45452 P45452

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