BMRB Entry 15361

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15361
MolProbity Validation Chart

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Title:
Solution Structure of MMP20 complexed with NNGH
Deposition date:
2007-07-03
Original release date:
2008-03-13
Authors:
Arendt, Yvonne; Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Cozzi, Roberta; Del Conte, Rebecca; Gonnelli, Leonardo
Citation:

Citation: Arendt, Yvonne; Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Cozzi, Roberta; Del Conte, Rebecca; Gonnelli, Leonardo. "Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase."  FEBS Lett. 518, 4723-4726 (2007).
PubMed: 17869250

Assembly members:

Assembly members:
MMP-20, polymer, 160 residues, 17507.721 Da.
ZN, non-polymer, 65.409 Da.
CA, non-polymer, 40.078 Da.
NGH, non-polymer, 316.373 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: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MMP-20: GEPKWKKNTLTYRISKYTPS MSSVEVDKAVEMALQAWSSA VPLSFVRINSGEADIMISFE NGDHGDSYPFDGPRGTLAHA FAPGEGLGGDTHFDNAEKWT MGTNGFNLFTVAAHEFGHAL GLAHSTDPSALMYPTYKYKN PYGFHLPKDDVKGIQALYGP

Data sets:
Data typeCount
13C chemical shifts579
15N chemical shifts161
1H chemical shifts1080

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1mmp20-nngh1
2ZINC ION, 12
3ZINC ION, 22
4CALCIUM ION, 13
5CALCIUM ION, 23
6NGH4

Entities:

Entity 1, mmp20-nngh 160 residues - 17507.721 Da.

1   GLYGLUPROLYSTRPLYSLYSASNTHRLEU
2   THRTYRARGILESERLYSTYRTHRPROSER
3   METSERSERVALGLUVALASPLYSALAVAL
4   GLUMETALALEUGLNALATRPSERSERALA
5   VALPROLEUSERPHEVALARGILEASNSER
6   GLYGLUALAASPILEMETILESERPHEGLU
7   ASNGLYASPHISGLYASPSERTYRPROPHE
8   ASPGLYPROARGGLYTHRLEUALAHISALA
9   PHEALAPROGLYGLUGLYLEUGLYGLYASP
10   THRHISPHEASPASNALAGLULYSTRPTHR
11   METGLYTHRASNGLYPHEASNLEUPHETHR
12   VALALAALAHISGLUPHEGLYHISALALEU
13   GLYLEUALAHISSERTHRASPPROSERALA
14   LEUMETTYRPROTHRTYRLYSTYRLYSASN
15   PROTYRGLYPHEHISLEUPROLYSASPASP
16   VALLYSGLYILEGLNALALEUTYRGLYPRO

Entity 2, ZINC ION, 1 - Zn - 65.409 Da.

1   ZN

Entity 3, CALCIUM ION, 1 - Ca - 40.078 Da.

1   CA

Entity 4, NGH - C13 H20 N2 O5 S - 316.373 Da.

1   NGH

Samples:

sample_1: MMP-20, [U-99% 15N], 0.6 mM; Tris 20 mM; ZnCl2 0.1 mM; CaCl2 5 mM; NaCl 300 mM; acetohydroxamic acid 0.3 M

sample_2: MMP-20 1 mM; Tris 20 mM; ZnCl2 0.1 mM; CaCl2 5 mM; NaCl 300 mM; acetohydroxamic acid 0.3 M

sample_3: MMP-20, [U-13C; U-15N], 0.6 mM; Tris 20 mM; ZnCl2 0.1 mM; CaCl2 5 mM; NaCl 300 mM; acetohydroxamic acid 0.3 M

sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
r2,r1, 15n-noesample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

TOPSPIN, Bruker Biospin - processing

CARA v1.8, (CARA) by Rochus Keller - chemical shift assignment, collection

QUEEN, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - refinement

AQUA, Rullmann, Doreleijers and Kaptein - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAI45518
EMBL CAA73317
GB AAI52742 AAT70722 EAW67024
REF NP_004762 XP_001153208 XP_002822444 XP_003253094 XP_003828430
SP O60882
AlphaFold O60882

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