BMRB: 30425

MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs

Authors

Marcink, T.C., Van Doren, S.R.

Assembly

Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I

Entity

1. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity 1 (polymer), 196 monomers, 23099.06 Da Detail

PNICDGNFDT VAMLRGEMFV FKERWFWRVR NNQVMDGYPM PIGQFWRGLP ASINTAYERK DGKFVFFKGD KHWVFDEASL EPGYPKHIKE LGRGLPTDKI DAALFWMPNG KTYFFRGNKY YRFNEELRAV DSEYPKNIKV WEGIPESPRG SFMGSDEVFT YFYKGNKYWK FNNQKLKVEP GYPKSALRDW MGCPSG

2. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity 2 (polymer), 211 monomers, 24871.79 × 2 Da Detail

STFSKLREQL GPVTQEFWDN LEKETEGLRQ EMSKDLEEVK AKVQPYLDDF QKKWQEEMEL YRQKVEPYLD DFQKKWQEEM ELYRQKVEPL RAELQEGARQ KLHELQEKLS PLGEEMRDRA RAHVDALRTH LAPYSDELRQ RLAARLEALK ENGGARLAEY HAKATEHLST LSEKAKPALE DLRQGLLPVL ESFKVSFLSA LEEYTKKLNT Q

3. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity PX4 (non-polymer), 678.940 × 218 Da
4. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity NA (non-polymer), 22.990 Da
5. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity CL (non-polymer), 35.453 Da

Total weight

220910.0 Da

Max. entity weight

24871.79 Da

Source organism

Homo sapiens

Exptl. method

solution NMR

Refine. method

molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 28.5 %, Completeness: 7.4 %, Completeness (bb): 10.6 % Detail

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Polymer type: polypeptide(L)

	Total	1H	13C	15N
All	7.4 % (371 of 5036)	6.8 % (181 of 2664)	4.5 % (87 of 1942)	24.0 % (103 of 430)
Backbone	10.6 % (253 of 2398)	13.9 % (114 of 818)	3.0 % (36 of 1195)	26.8 % (103 of 385)
Sidechain	4.1 % (125 of 3019)	3.6 % (67 of 1846)	5.1 % (58 of 1128)	0.0 % (0 of 45)
Aromatic	1.5 % (8 of 534)	1.5 % (4 of 267)	1.6 % (4 of 256)	0.0 % (0 of 11)
Methyl	21.5 % (73 of 340)	21.2 % (36 of 170)	21.8 % (37 of 170)

1. entity 1

PNICDGNFDT VAMLRGEMFV FKERWFWRVR NNQVMDGYPM PIGQFWRGLP ASINTAYERK DGKFVFFKGD KHWVFDEASL EPGYPKHIKE LGRGLPTDKI DAALFWMPNG KTYFFRGNKY YRFNEELRAV DSEYPKNIKV WEGIPESPRG SFMGSDEVFT YFYKGNKYWK FNNQKLKVEP GYPKSALRDW MGCPSG

2. entity 2

STFSKLREQL GPVTQEFWDN LEKETEGLRQ EMSKDLEEVK AKVQPYLDDF QKKWQEEMEL YRQKVEPYLD DFQKKWQEEM ELYRQKVEPL RAELQEGARQ KLHELQEKLS PLGEEMRDRA RAHVDALRTH LAPYSDELRQ RLAARLEALK ENGGARLAEY HAKATEHLST LSEKAKPALE DLRQGLLPVL ESFKVSFLSA LEEYTKKLNT Q

Show sample condition

Sample

Solvent system 93% H2O/7% D2O, Pressure 1 atm, Temperature 303 K, pH 7.2, Details 20 mM Tris-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O

#	Name	Isotope labeling	Type	Concentration
1	Tris-HCl	natural abundance		20 mM
2	NaCl	natural abundance		300 mM
3	sodium azide	natural abundance		0.02 %
4	H2O	natural abundance		93 %
5	D2O	[U-100% 2H]		7 %
6	MT1-MMP hemopexin-like domain	[U-2H; U-13C; U-15N]		90 (±10.0) uM
7	MSP1D1	natural abundance		180 (±10.0) uM
8	PX4	natural abundance		14.4 mM

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Protein Blocks Logo

Calculated from 15 models in PDB: 6CLZ, Strand ID: A, B, C Detail

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Release date

2018-08-30

Citation

MT1-MMP Binds Membranes by Opposite Tips of Its β Propeller to Position It for Pericellular Proteolysis
Marcink, T.C., Simoncic, J.A., An, B., Knapinska, A.M., Fulcher, Y.G., Akkaladevi, N., Fields, G.B., Van Doren, S.R.
Structure (2018), 27, 281-292, PubMed 30471921 , DOI 10.1016/j.str.2018.10.008 , Abstract

Entries sharing articles BMRB: 1 entries Detail

Related entities 1. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity 1, : 1 : 5 : 5 : 186 entities Detail

Related entities 2. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity 2, : 19 entities Detail

Interaction partners 1. Matrix metalloproteinase-14 (E.C.3.4.24.80), Apolipoprotein A-I, entity 1, : 32 interactors Detail

Experiments performed 3 experiments Detail