BMRB Entry 15361

Name: Solution Structure of MMP20 complexed with NNGH
Published: 2008-03-13

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PDB ID: 2jsd
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15361
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of MMP20 complexed with NNGH PubMed: 17869250

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: 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).

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: 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):
MMP-20: GEPKWKKNTLTYRISKYTPS MSSVEVDKAVEMALQAWSSA VPLSFVRINSGEADIMISFE NGDHGDSYPFDGPRGTLAHA FAPGEGLGGDTHFDNAEKWT MGTNGFNLFTVAAHEFGHAL GLAHSTDPSALMYPTYKYKN PYGFHLPKDDVKGIQALYGP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	579
15N chemical shifts	161
1H chemical shifts	1080

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Entity Assembly ID	Entity Name	Entity ID
1	mmp20-nngh	1
2	ZINC ION, 1	2
3	ZINC ION, 2	2
4	CALCIUM ION, 1	3
5	CALCIUM ION, 2	3
6	NGH	4

1	GLY	GLU	PRO	LYS	TRP	LYS	LYS	ASN	THR	LEU
2	THR	TYR	ARG	ILE	SER	LYS	TYR	THR	PRO	SER
3	MET	SER	SER	VAL	GLU	VAL	ASP	LYS	ALA	VAL
4	GLU	MET	ALA	LEU	GLN	ALA	TRP	SER	SER	ALA
5	VAL	PRO	LEU	SER	PHE	VAL	ARG	ILE	ASN	SER
6	GLY	GLU	ALA	ASP	ILE	MET	ILE	SER	PHE	GLU
7	ASN	GLY	ASP	HIS	GLY	ASP	SER	TYR	PRO	PHE
8	ASP	GLY	PRO	ARG	GLY	THR	LEU	ALA	HIS	ALA
9	PHE	ALA	PRO	GLY	GLU	GLY	LEU	GLY	GLY	ASP
10	THR	HIS	PHE	ASP	ASN	ALA	GLU	LYS	TRP	THR
11	MET	GLY	THR	ASN	GLY	PHE	ASN	LEU	PHE	THR
12	VAL	ALA	ALA	HIS	GLU	PHE	GLY	HIS	ALA	LEU
13	GLY	LEU	ALA	HIS	SER	THR	ASP	PRO	SER	ALA
14	LEU	MET	TYR	PRO	THR	TYR	LYS	TYR	LYS	ASN
15	PRO	TYR	GLY	PHE	HIS	LEU	PRO	LYS	ASP	ASP
16	VAL	LYS	GLY	ILE	GLN	ALA	LEU	TYR	GLY	PRO

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
r2,r1, 15n-noe	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_3	isotropic	sample_conditions_1

PDB	2JSD
DBJ	BAI45518
EMBL	CAA73317
GB	AAI52742 AAT70722 EAW67024
REF	NP_004762 XP_001153208 XP_002822444 XP_003253094 XP_003828430
SP	O60882

Biological Magnetic Resonance Data Bank

BMRB Entry 15361

Title: Solution Structure of MMP20 complexed with NNGH PubMed: 17869250

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	GLY	GLU	PRO	LYS	TRP	LYS	LYS	ASN	THR	LEU
2	THR	TYR	ARG	ILE	SER	LYS	TYR	THR	PRO	SER
3	MET	SER	SER	VAL	GLU	VAL	ASP	LYS	ALA	VAL
4	GLU	MET	ALA	LEU	GLN	ALA	TRP	SER	SER	ALA
5	VAL	PRO	LEU	SER	PHE	VAL	ARG	ILE	ASN	SER
6	GLY	GLU	ALA	ASP	ILE	MET	ILE	SER	PHE	GLU
7	ASN	GLY	ASP	HIS	GLY	ASP	SER	TYR	PRO	PHE
8	ASP	GLY	PRO	ARG	GLY	THR	LEU	ALA	HIS	ALA
9	PHE	ALA	PRO	GLY	GLU	GLY	LEU	GLY	GLY	ASP
10	THR	HIS	PHE	ASP	ASN	ALA	GLU	LYS	TRP	THR
11	MET	GLY	THR	ASN	GLY	PHE	ASN	LEU	PHE	THR
12	VAL	ALA	ALA	HIS	GLU	PHE	GLY	HIS	ALA	LEU
13	GLY	LEU	ALA	HIS	SER	THR	ASP	PRO	SER	ALA
14	LEU	MET	TYR	PRO	THR	TYR	LYS	TYR	LYS	ASN
15	PRO	TYR	GLY	PHE	HIS	LEU	PRO	LYS	ASP	ASP
16	VAL	LYS	GLY	ILE	GLN	ALA	LEU	TYR	GLY	PRO

1	GLY	GLU	PRO	LYS	TRP	LYS	LYS	ASN	THR	LEU
2	THR	TYR	ARG	ILE	SER	LYS	TYR	THR	PRO	SER
3	MET	SER	SER	VAL	GLU	VAL	ASP	LYS	ALA	VAL
4	GLU	MET	ALA	LEU	GLN	ALA	TRP	SER	SER	ALA
5	VAL	PRO	LEU	SER	PHE	VAL	ARG	ILE	ASN	SER
6	GLY	GLU	ALA	ASP	ILE	MET	ILE	SER	PHE	GLU
7	ASN	GLY	ASP	HIS	GLY	ASP	SER	TYR	PRO	PHE
8	ASP	GLY	PRO	ARG	GLY	THR	LEU	ALA	HIS	ALA
9	PHE	ALA	PRO	GLY	GLU	GLY	LEU	GLY	GLY	ASP
10	THR	HIS	PHE	ASP	ASN	ALA	GLU	LYS	TRP	THR
11	MET	GLY	THR	ASN	GLY	PHE	ASN	LEU	PHE	THR
12	VAL	ALA	ALA	HIS	GLU	PHE	GLY	HIS	ALA	LEU
13	GLY	LEU	ALA	HIS	SER	THR	ASP	PRO	SER	ALA
14	LEU	MET	TYR	PRO	THR	TYR	LYS	TYR	LYS	ASN
15	PRO	TYR	GLY	PHE	HIS	LEU	PRO	LYS	ASP	ASP
16	VAL	LYS	GLY	ILE	GLN	ALA	LEU	TYR	GLY	PRO

1	GLY	GLU	PRO	LYS	TRP	LYS	LYS	ASN	THR	LEU
2	THR	TYR	ARG	ILE	SER	LYS	TYR	THR	PRO	SER
3	MET	SER	SER	VAL	GLU	VAL	ASP	LYS	ALA	VAL
4	GLU	MET	ALA	LEU	GLN	ALA	TRP	SER	SER	ALA
5	VAL	PRO	LEU	SER	PHE	VAL	ARG	ILE	ASN	SER
6	GLY	GLU	ALA	ASP	ILE	MET	ILE	SER	PHE	GLU
7	ASN	GLY	ASP	HIS	GLY	ASP	SER	TYR	PRO	PHE
8	ASP	GLY	PRO	ARG	GLY	THR	LEU	ALA	HIS	ALA
9	PHE	ALA	PRO	GLY	GLU	GLY	LEU	GLY	GLY	ASP
10	THR	HIS	PHE	ASP	ASN	ALA	GLU	LYS	TRP	THR
11	MET	GLY	THR	ASN	GLY	PHE	ASN	LEU	PHE	THR
12	VAL	ALA	ALA	HIS	GLU	PHE	GLY	HIS	ALA	LEU
13	GLY	LEU	ALA	HIS	SER	THR	ASP	PRO	SER	ALA
14	LEU	MET	TYR	PRO	THR	TYR	LYS	TYR	LYS	ASN
15	PRO	TYR	GLY	PHE	HIS	LEU	PRO	LYS	ASP	ASP
16	VAL	LYS	GLY	ILE	GLN	ALA	LEU	TYR	GLY	PRO