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1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2
Authors
Feng, Y., Likos, J.J., Zhu, L., Woodward, H., McDonald, J., Stevens, A.M., Howard, S.C., Welsch, D.J.
Assembly
truncated catalytic domain of matrix metalloproteinase-2
Entity
1. mmp2 (polymer, Thiol state: not present), 163 monomers, 18471.20 Da Detail

MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTNTSA NYSLFLVAAH EFGHAMGLEH SQDPGALMAP IYTYTKNFRL SQDDIKGIQE LYG


2. I52 (non-polymer), 574.732 Da
Total weight
19045.932 Da
Max. entity weight
18471.2 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.9 %, Completeness: 82.7 %, Completeness (bb): 95.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All82.7 % (1569 of 1898)83.1 % (809 of 974)82.2 % (615 of 748)82.4 % (145 of 176)
Backbone95.2 % (899 of 944)95.6 % (303 of 317)95.6 % (452 of 473)93.5 % (144 of 154)
Sidechain73.8 % (812 of 1101)77.0 % (506 of 657)72.3 % (305 of 422) 4.5 % (1 of 22)
Aromatic26.2 % (68 of 260)30.0 % (39 of 130)22.2 % (28 of 126)25.0 % (1 of 4)
Methyl98.6 % (142 of 144)98.6 % (71 of 72)98.6 % (71 of 72)

1. mmp2

MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTNTSA NYSLFLVAAH EFGHAMGLEH SQDPGALMAP IYTYTKNFRL SQDDIKGIQE LYG

Sample

Pressure 1 atm, Temperature 303 K, pH 7.4 (±0.1)


#NameIsotope labelingTypeConcentration
1mmp2[U-13C; U-15N]0.35 mM

Release date
2000-06-18
Citation
1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2
Feng, Y., Likos, J.J., Zhu, L., Woodward, H., McDonald, J., Stevens, A.M., Howard, S.C., Welsch, D.J.
J. Biomol. NMR (2000), 17, 85-86, PubMed 10909870 ,
Related entities 1. mmp2, : 1 : 184 entities Detail
Experiments performed 1 experiments Detail
Keywords gelatinase, matrix metalloproteinase, mmp, mmp2, NMR, nuclear magnetic resonance, protein, protein-ligand interaction, resonance assignments