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- PDB-1xzy: Solution structure of the P30-trans form of Alpha Hemoglobin Stab... -

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Basic information

Entry
Database: PDB / ID: 1xzy
TitleSolution structure of the P30-trans form of Alpha Hemoglobin Stabilizing Protein (AHSP)
ComponentsAlpha-hemoglobin stabilizing protein
KeywordsCHAPERONE / helical bundle / three-helix bundle
Function / homology
Function and homology information


hemoglobin metabolic process / hemoglobin binding / hemoglobin complex / hemopoiesis / erythrocyte differentiation / unfolded protein binding / protein folding / protein stabilization / cytoplasm
Similarity search - Function
Alpha-haemoglobin stabilising protein / AHSP superfamily / Alpha-haemoglobin stabilising protein / AHSP / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Alpha-hemoglobin-stabilizing protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsGell, D.A. / Feng, L. / Zhou, S. / Kong, Y. / Lee, C. / Weiss, M.J. / Shi, Y. / Mackay, J.P.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2004
Title: Molecular mechanism of AHSP-mediated stabilization of alpha-hemoglobin
Authors: Feng, L. / Gell, D.A. / Zhou, S. / Gu, L. / Kong, Y. / Li, J. / Hu, M. / Yan, N. / Lee, C. / Rich, A.M. / Armstrong, R.S. / Lay, P.A. / Gow, A.J. / Weiss, M.J. / Mackay, J.P. / Shi, Y.
History
DepositionNov 12, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Dec 21, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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 29, 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: Alpha-hemoglobin stabilizing protein


Theoretical massNumber of molelcules
Total (without water)10,5971
Polymers10,5971
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 / 100structures with the lowest energy
Representative

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Components

#1: Protein Alpha-hemoglobin stabilizing protein / AHSP / Erythroid associated factor / Erythroid differentiation related factor


Mass: 10597.030 Da / Num. of mol.: 1 / Fragment: Residues 1-90
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AHSP / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9NZD4

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1212D NOESY
1313D 13C-separated NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

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Sample preparation

DetailsContents: 20mM sodium phosphate, 100mM NaCl, 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 20mM phosphate, 100mM NaCl / pH: 6.9 / Pressure: ambient / Temperature: 288 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX8002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1Brungerstructure solution
DYANA1Guntertstructure solution
Sparky3.111Goddarddata analysis
DYANA1Guntertrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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