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- PDB-1bo9: NMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I -

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Basic information

Entry
Database: PDB / ID: 1bo9
TitleNMR SOLUTION STRUCTURE OF DOMAIN 1 OF HUMAN ANNEXIN I
ComponentsPROTEIN (ANNEXIN I)
KeywordsMETAL TRANSPORT / DOMAIN 1
Function / homology
Function and homology information


regulation of interleukin-1 production / myoblast migration involved in skeletal muscle regeneration / regulation of leukocyte migration / granulocyte chemotaxis / positive regulation of T-helper 1 cell differentiation / phospholipase A2 inhibitor activity / regulation of hormone secretion / positive regulation of vesicle fusion / neutrophil clearance / negative regulation of T-helper 2 cell differentiation ...regulation of interleukin-1 production / myoblast migration involved in skeletal muscle regeneration / regulation of leukocyte migration / granulocyte chemotaxis / positive regulation of T-helper 1 cell differentiation / phospholipase A2 inhibitor activity / regulation of hormone secretion / positive regulation of vesicle fusion / neutrophil clearance / negative regulation of T-helper 2 cell differentiation / positive regulation of neutrophil apoptotic process / negative regulation of interleukin-8 production / neutrophil activation / cadherin binding involved in cell-cell adhesion / peptide cross-linking / cornified envelope / neutrophil homeostasis / calcium-dependent phospholipid binding / Formyl peptide receptors bind formyl peptides and many other ligands / motile cilium / negative regulation of exocytosis / cellular response to glucocorticoid stimulus / vesicle membrane / alpha-beta T cell differentiation / arachidonate secretion / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of wound healing / phosphatidylserine binding / monocyte chemotaxis / phagocytic cup / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / lateral plasma membrane / Smooth Muscle Contraction / cellular response to vascular endothelial growth factor stimulus / positive regulation of G1/S transition of mitotic cell cycle / phagocytosis / positive regulation of T cell proliferation / keratinocyte differentiation / positive regulation of interleukin-2 production / adherens junction / sarcolemma / phospholipid binding / calcium-dependent protein binding / regulation of cell shape / regulation of inflammatory response / early endosome membrane / G alpha (i) signalling events / actin cytoskeleton organization / Interleukin-4 and Interleukin-13 signaling / basolateral plasma membrane / G alpha (q) signalling events / collagen-containing extracellular matrix / vesicle / adaptive immune response / cell surface receptor signaling pathway / endosome / inflammatory response / apical plasma membrane / innate immune response / signaling receptor binding / focal adhesion / lipid binding / calcium ion binding / negative regulation of apoptotic process / cell surface / signal transduction / extracellular space / extracellular exosome / extracellular region / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Annexin A1 / Annexin / Annexin repeat, conserved site / Annexin repeat signature. / Annexin / Annexin / Annexin repeats / Annexin repeat / Annexin superfamily / Annexin repeat profile. ...Annexin A1 / Annexin / Annexin repeat, conserved site / Annexin repeat signature. / Annexin / Annexin / Annexin repeats / Annexin repeat / Annexin superfamily / Annexin repeat profile. / Annexin V; domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry
AuthorsGao, J. / Yan Li, H.
CitationJournal: J.Biol.Chem. / Year: 1999
Title: NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit.
Authors: Gao, J. / Li, Y. / Yan, H.
History
DepositionAug 10, 1998Deposition site: BNL / Processing site: RCSB
Revision 1.0Aug 19, 1998Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (ANNEXIN I)


Theoretical massNumber of molelcules
Total (without water)8,0231
Polymers8,0231
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)21 / 50LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein PROTEIN (ANNEXIN I) / LIPOCORTIN I / CALPACTIN II / CHROMOBINDIN 9 / P35 / PHOSPHOLIPASE A2 INHIBITORY PROTEIN


Mass: 8023.305 Da / Num. of mol.: 1 / Fragment: DOMAIN 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P04083

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN.

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Sample preparation

Sample conditionspH: 7 / Pressure: 1 atm / Temperature: 300 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX600 / Manufacturer: Bruker / Model: DMX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: distance geometry / Software ordinal: 1 / Details: DG/SA
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 50 / Conformers submitted total number: 21

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