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- PDB-1g91: SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1) -

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Basic information

Entry
Database: PDB / ID: 1g91
TitleSOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)
ComponentsMYELOID PROGENITOR INHIBITORY FACTOR-1
KeywordsCYTOKINE / chemokine / MPIF-1 / CKb8 / CCL23
Function / homology
Function and homology information


negative regulation of C-C chemokine binding / CCR1 chemokine receptor binding / CCR chemokine receptor binding / lymphocyte chemotaxis / Formyl peptide receptors bind formyl peptides and many other ligands / chemokine-mediated signaling pathway / chemokine activity / monocyte chemotaxis / cellular response to interleukin-1 / neutrophil chemotaxis ...negative regulation of C-C chemokine binding / CCR1 chemokine receptor binding / CCR chemokine receptor binding / lymphocyte chemotaxis / Formyl peptide receptors bind formyl peptides and many other ligands / chemokine-mediated signaling pathway / chemokine activity / monocyte chemotaxis / cellular response to interleukin-1 / neutrophil chemotaxis / positive regulation of GTPase activity / cellular response to type II interferon / intracellular calcium ion homeostasis / chemotaxis / cell-cell signaling / cellular response to tumor necrosis factor / heparin binding / G alpha (i) signalling events / G alpha (q) signalling events / positive regulation of ERK1 and ERK2 cascade / inflammatory response / immune response / G protein-coupled receptor signaling pathway / negative regulation of cell population proliferation / signal transduction / extracellular space / extracellular region
Similarity search - Function
CC chemokine, conserved site / Small cytokines (intercrine/chemokine) C-C subfamily signature. / Chemokine beta/gamma/delta / Intercrine alpha family (small cytokine C-X-C) (chemokine CXC). / Chemokine interleukin-8-like domain / Chemokine interleukin-8-like superfamily / Small cytokines (intecrine/chemokine), interleukin-8 like / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #40 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
C-C motif chemokine 23
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / distance geometry, simulated annealing, molecular dynamics
AuthorsRajarathnam, K. / Li, Y. / Rohrer, T. / Gentz, R.
CitationJournal: J.Biol.Chem. / Year: 2001
Title: Solution structure and dynamics of myeloid progenitor inhibitory factor-1 (MPIF-1), a novel monomeric CC chemokine.
Authors: Rajarathnam, K. / Li, Y. / Rohrer, T. / Gentz, R.
History
DepositionNov 21, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 7, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 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 1.4Dec 21, 2022Group: Database references / Category: struct_ref_seq_dif / Item: _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MYELOID PROGENITOR INHIBITORY FACTOR-1


Theoretical massNumber of molelcules
Total (without water)8,8691
Polymers8,8691
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)30 / 50structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein MYELOID PROGENITOR INHIBITORY FACTOR-1 / MPIF-1


Mass: 8869.375 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): K12-DERIVED STRAIN SGI3009 / References: UniProt: P55773

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
121HN(CA)CB
131CBCA(CO)NH
141(H)CCH-TOCSY
2523D 15N-separated NOESY
262HNHA
3732D NOESY
383DQF-COSY

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Sample preparation

Details
Solution-IDContentsSolvent system
12 mM MPIF-1 U-13C,15N90% H2O, 10% D2O, pH 5.2
22 mM MPIF-1 U-15N90% H2O, 10% D2O, pH 5.2
32 mM MPIF-199.99 % D2O, pH 5.2
Sample conditionsIonic strength: 20 mM sodium acetate / pH: 5.2 / Pressure: ambient / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYVarianUNITY6001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1Brungerstructure solution
X-PLOR3.1Brungerrefinement
RefinementMethod: distance geometry, simulated annealing, molecular dynamics
Software ordinal: 1
Details: The structures are based on a total of 711 NOE, 82 dihedral, and 36 H-bonding restraints
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 30

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