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- PDB-1kun: SOLUTION STRUCTURE OF THE HUMAN ALPHA3-CHAIN TYPE VI COLLAGEN C-T... -

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Entry
Database: PDB / ID: 1kun
TitleSOLUTION STRUCTURE OF THE HUMAN ALPHA3-CHAIN TYPE VI COLLAGEN C-TERMINAL KUNITZ DOMAIN, NMR, 20 STRUCTURES
ComponentsALPHA3-CHAIN TYPE VI COLLAGEN
KeywordsEXTRACELLULAR MATRIX / COLLAGEN TYPE VI FRAGMENT / KUNITZ-TYPE DOMAIN / CONNECTIVE TISSUE
Function / homology
Function and homology information


collagen type VI trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / muscle organ development / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / ECM proteoglycans ...collagen type VI trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / muscle organ development / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / ECM proteoglycans / Integrin cell surface interactions / response to glucose / response to UV / phosphatidylinositol 3-kinase/protein kinase B signal transduction / extracellular matrix / serine-type endopeptidase inhibitor activity / sarcolemma / extracellular vesicle / collagen-containing extracellular matrix / neuron apoptotic process / cell adhesion / endoplasmic reticulum lumen / extracellular space / extracellular exosome / extracellular region
Similarity search - Function
Collagen alpha-3(VI) chain, vWA domain / : / Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / von Willebrand factor type A domain / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. ...Collagen alpha-3(VI) chain, vWA domain / : / Pancreatic trypsin inhibitor Kunitz domain / Factor Xa Inhibitor / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / von Willebrand factor type A domain / Proteinase inhibitor I2, Kunitz, conserved site / Pancreatic trypsin inhibitor (Kunitz) family signature. / BPTI/Kunitz family of serine protease inhibitors. / Pancreatic trypsin inhibitor Kunitz domain / Kunitz/Bovine pancreatic trypsin inhibitor domain / Pancreatic trypsin inhibitor (Kunitz) family profile. / Pancreatic trypsin inhibitor Kunitz domain superfamily / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Few Secondary Structures / Irregular / Immunoglobulin-like fold
Similarity search - Domain/homology
Collagen alpha-3(VI) chain
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsSorensen, M.D. / Bjorn, S. / Norris, K. / Olsen, O. / Petersen, L. / James, T.L. / Led, J.J.
Citation
Journal: Biochemistry / Year: 1997
Title: Solution structure and backbone dynamics of the human alpha3-chain type VI collagen C-terminal Kunitz domain,.
Authors: Sorensen, M.D. / Bjorn, S. / Norris, K. / Olsen, O. / Petersen, L. / James, T.L. / Led, J.J.
#1: Journal: J.Biomol.NMR / Year: 1996
Title: Elucidation of the Origin of Multiple Conformations of the Human Alpha 3-Chain Type Vi Collagen C-Terminal Kunitz Domain. The Reorientation of the Trp21 Ring
Authors: Sorensen, M.D. / Kristensen, S.M. / Bjorn, S. / Norris, K. / Olsen, O. / Led, J.J.
History
DepositionMar 4, 1997Processing site: BNL
Revision 1.0Nov 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Oct 16, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Assembly

Deposited unit
A: ALPHA3-CHAIN TYPE VI COLLAGEN


Theoretical massNumber of molelcules
Total (without water)6,6401
Polymers6,6401
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50
Representative

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Components

#1: Protein ALPHA3-CHAIN TYPE VI COLLAGEN


Mass: 6639.508 Da / Num. of mol.: 1 / Fragment: C-TERMINAL KUNITZ DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: POTENTIAL / Production host: Saccharomyces cerevisiae (brewer's yeast) / Strain (production host): MT-663 / References: UniProt: P12111
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Sample conditionspH: 3 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AM500 / Manufacturer: Bruker / Model: AM500 / Field strength: 500.13 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementSoftware ordinal: 1
Details: THREE-DIMENSIONAL STRUCTURE IN AQUEOUS SOLUTION AS DETERMINED BY NUCLEAR MAGNETIC RESONANCE, DISTANCE GEOMETRY AND SIMULATED ANNEALING.
NMR ensembleConformers calculated total number: 50 / Conformers submitted total number: 20

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