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- PDB-2tmp: N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-T... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2tmp | ||||||
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Title | N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP-2), NMR, 49 STRUCTURES | ||||||
![]() | TISSUE INHIBITOR OF METALLOPROTEINASES-2 | ||||||
![]() | METALLOPROTEASE INHIBITOR / TIMP / METALLOPROTEINASE INHIBITOR / OB PROTEIN FOLD | ||||||
Function / homology | ![]() negative regulation of metallopeptidase activity / negative regulation of membrane protein ectodomain proteolysis / peptidase inhibitor activity / metalloendopeptidase inhibitor activity / molecular function inhibitor activity / Activation of Matrix Metalloproteinases / extracellular matrix / response to hormone / response to cytokine / specific granule lumen ...negative regulation of metallopeptidase activity / negative regulation of membrane protein ectodomain proteolysis / peptidase inhibitor activity / metalloendopeptidase inhibitor activity / molecular function inhibitor activity / Activation of Matrix Metalloproteinases / extracellular matrix / response to hormone / response to cytokine / specific granule lumen / tertiary granule lumen / protease binding / collagen-containing extracellular matrix / ficolin-1-rich granule lumen / Neutrophil degranulation / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING USING TORSION ANGLE DYNAMICS | ||||||
![]() | Muskett, F.W. / Frenkiel, T.A. / Feeney, J. / Freedman, R.B. / Carr, M.D. / Williamson, R.A. | ||||||
![]() | ![]() Title: High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3. Authors: Muskett, F.W. / Frenkiel, T.A. / Feeney, J. / Freedman, R.B. / Carr, M.D. / Williamson, R.A. #1: ![]() Title: Mapping the Binding Site for Matrix Metalloproteinase on the N-Terminal Domain of the Tissue Inhibitor of Metalloproteinases-2 by NMR Chemical Shift Perturbation Authors: Williamson, R.A. / Carr, M.D. / Frenkiel, T.A. / Feeney, J. / Freedman, R.B. #2: ![]() Title: Chemically and Conformationally Authentic Active Domain of Human Tissue Inhibitor of Metalloproteinases-2 Refolded from Bacterial Inclusion Bodies Authors: Williamson, R.A. / Natalia, D. / Gee, C.K. / Murphy, G. / Carr, M.D. / Freedman, R.B. #3: ![]() Title: Solution Structure of the Active Domain of Tissue Inhibitor of Metalloproteinases-2. A New Member of the Ob Fold Protein Family Authors: Williamson, R.A. / Martorell, G. / Carr, M.D. / Murphy, G. / Docherty, A.J. / Freedman, R.B. / Feeney, J. #4: ![]() Title: Disulphide Bond Assignment in Human Tissue Inhibitor of Metalloproteinases (Timp) Authors: Williamson, R.A. / Marston, F.A. / Angal, S. / Koklitis, P. / Panico, M. / Morris, H.R. / Carne, A.F. / Smith, B.J. / Harris, T.J. / Freedman, R.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.8 MB | Display | ![]() |
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PDB format | ![]() | 1.6 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14109.167 Da / Num. of mol.: 1 / Fragment: N-TERMINAL DOMAIN, RESIDUES 1-127 / Mutation: A21T Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Cellular location (production host): INTRACELLULAR INCLUSION BODIES Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE CLOSEST TO THE MEAN OF THE 49 CONFORMERS |
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Sample preparation
Details | Contents: AQUEOUS |
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Sample conditions | Ionic strength: 125 mM / pH: 6.7 / Pressure: 1 ATMOSPHERE / Temperature: 308 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS & INOVA / Manufacturer: Varian / Model: UNITYPLUS & INOVA / Field strength: 600 MHz |
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Processing
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NMR software |
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Refinement | Method: SIMULATED ANNEALING USING TORSION ANGLE DYNAMICS / Software ordinal: 1 Details: SEE GUNTERT ET AL. (1997) J. MOL. BIOL. 273(1), 283-298 | ||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 49 |