BMRB Entry 16221

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Collagen Binding domain of MMP2
Published: 2009-06-02

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16221

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for Collagen Binding domain of MMP2

Deposition date:

2009-03-23

Original release date:

2009-06-02

Authors:

Xu, Xiaoping

Citation:

Citation: Xu, Xiaoping; Mikhailova, Margarita; Ilangovan, Udayar; Chen, Zhihua; Yu, Agnes; Pal, Sanjay; Hinck, Andrew; Steffensen, Bjorn. "Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2" Biochemistry ., 5822-5831 (2009).
PubMed: 19459623

Assembly members:

Assembly members:
CBD_of_MMP2, polymer, 190 residues, Formula weight is not available

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: pGYMX

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CBD_of_MMP2: MATSHHHHHHIEGRASVVRV KYGNADGEYCKFPFLFNGKE YNSCTDTGRSDGFLWCSTTY NFEKDGKYGFCPHEALFTMG GNAEGQPCKFPFRFQGTSYD SCTTEGRTDGYRWCGTTEDY DRDKKYGFCPETAMSTVGGN SEGAPCVFPFTFLGNKYESC TSAGRSDGKMWCATTANYDD DRKWGFCPDQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	123
15N chemical shifts	43
1H chemical shifts	89

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CBD domain	1

Entities:

Entity 1, CBD domain 190 residues - Formula weight is not available

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

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	15N_CBD	isotropic	label1
2D 1H-13C HSQC	13C15N_CBD	isotropic	label1
3D HNCACB	13C15N_CBD	isotropic	label1
3D CBCA(CO)NH	13C15N_CBD	isotropic	label1
3D C(CO)NH	13C15N_CBD	isotropic	label1
3D HNCA	13C15N_CBD	isotropic	label1
3D HNCO	13C15N_CBD	isotropic	label1
3D HNHA	15N_CBD	isotropic	label1
3D HCACO	13C15N_CBD	isotropic	label1

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

BMRB Entry 16221

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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

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

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