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- PDB-1ayk: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ayk | ||||||
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Title | INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, 30 STRUCTURES | ||||||
![]() | COLLAGENASE | ||||||
![]() | METALLOPROTEASE / MATRIX METALLOPROTEASE / HYDROLASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization ...interstitial collagenase / cellular response to UV-A / protein metabolic process / Basigin interactions / Activation of Matrix Metalloproteinases / Collagen degradation / collagen catabolic process / extracellular matrix disassembly / Degradation of the extracellular matrix / extracellular matrix organization / extracellular matrix / positive regulation of protein-containing complex assembly / metalloendopeptidase activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / peptidase activity / Interleukin-4 and Interleukin-13 signaling / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / zinc ion binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD | ||||||
![]() | Powers, R. / Moy, F.J. | ||||||
![]() | ![]() Title: High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR. Authors: Moy, F.J. / Chanda, P.K. / Cosmi, S. / Pisano, M.R. / Urbano, C. / Wilhelm, J. / Powers, R. #1: ![]() Title: Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase Authors: Moy, F.J. / Pisano, M.R. / Chanda, P.K. / Urbano, C. / Killar, L.M. / Sung, M.-L. / Powers, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.5 MB | Display | ![]() |
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PDB format | ![]() | 1.2 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 345.4 KB | Display | ![]() |
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Full document | ![]() | 529.7 KB | Display | |
Data in XML | ![]() | 96.5 KB | Display | |
Data in CIF | ![]() | 126.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 18865.541 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | #3: Chemical | ChemComp-CA / | |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 6.5 / Pressure: 1 atm / Temperature: 308 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX2600 / Manufacturer: Bruker / Model: AMX2600 / Field strength: 600 MHz |
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Processing
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NMR software |
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Refinement | Method: HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING METHOD Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY, LOWEST VIOLATIONS, CONSISTENT FOLD Conformers calculated total number: 100 / Conformers submitted total number: 30 |