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- PDB-1w09: Solution structure of the cis form of the human alpha-hemoglobin ... -

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Basic information

Entry
Database: PDB / ID: 1w09
TitleSolution structure of the cis form of the human alpha-hemoglobin stabilizing protein (AHSP)
ComponentsALPHA-HEMOGLOBIN STABILIZING PROTEIN
KeywordsCHAPERONE / AHSP NMR STRUCTURE / PROLINE CIS/TRANS ISOMERIZATION / ALPHA-THALASSAEMIA / ALPHA-HEMOGLOBIN BINDING
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 / CNS
AuthorsSantiveri, C.M. / Perez-Canadillas, J.M. / Vadivelu, M.K. / Allen, M.D. / Rutherford, T.J. / Watkins, N.A. / Bycroft, M.
CitationJournal: J. Biol. Chem. / Year: 2004
Title: NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding.
Authors: Santiveri, C.M. / Perez-Canadillas, J.M. / Vadivelu, M.K. / Allen, M.D. / Rutherford, T.J. / Watkins, N.A. / Bycroft, M.
History
DepositionMay 25, 2004Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 10, 2004Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 24, 2018Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name ..._entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_variant
Revision 1.4May 2, 2018Group: Data collection / Database references / Category: citation / pdbx_nmr_spectrometer
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _pdbx_nmr_spectrometer.model
Revision 1.5May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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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)10,8621
Polymers10,8621
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 40NO DISTANCE VIOLATIONS WERE GREATER THAN 0.3 A, NO ANGLE VIOLATIONS WERE GREATER THAN 5.0 DEGREES, AND NO RDC VIOLATIONS WERE GREATER THAN 2.5 HZ
RepresentativeModel #1

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Components

#1: Protein ALPHA-HEMOGLOBIN STABILIZING PROTEIN / ERYTHROID ASSOCIATED FACTOR / ERYTHROID DIFFERENTIATION RELATED FACTOR


Mass: 10862.253 Da / Num. of mol.: 1 / Fragment: RESIDUES 3-94
Source method: isolated from a genetically manipulated source
Details: ASP 29-PRO 30 PEPTIDE BOND IN CIS CONFORMATION / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PRSET (A) / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: Q9NZD4
Compound detailsACTS AS A CHAPERONE TO PREVENT THE HARMFUL AGGREGATION OF ALPHA-HEMOGLOBIN DURING NORMAL ERYTHROID ...ACTS AS A CHAPERONE TO PREVENT THE HARMFUL AGGREGATION OF ALPHA-HEMOGLOBIN DURING NORMAL ERYTHROID CELL DEVELOPMENT.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HSQC
121HNCO
131HN(CA)CO
141HN(CA)CB
151CBCA(CO)NH
161(H)CCH-COSY
271DQF- COSY
281TOCSY
291HSQC
2101NOESY
21113D- 15N-HSQC-NOESY
21213D-13C-HSQC- NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY

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Sample preparation

Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1120 mM6.0 1.0 atm298.0 K
2120 mM6.0 1.0 atm298.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE6001
Bruker AVANCEBrukerAVANCE8002

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Processing

NMR software
NameVersionDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE,SIMONSON,WARRENrefinement
NMRPipestructure solution
ANSIGWINDOWSstructure solution
RefinementMethod: CNS / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: NO DISTANCE VIOLATIONS WERE GREATER THAN 0.3 A, NO ANGLE VIOLATIONS WERE GREATER THAN 5.0 DEGREES, AND NO RDC VIOLATIONS WERE GREATER THAN 2.5 HZ
Conformers calculated total number: 40 / Conformers submitted total number: 20

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