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- PDB-2iz3: Solution structure of human beta-microseminoprotein -

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Basic information

Entry
Database: PDB / ID: 2iz3
TitleSolution structure of human beta-microseminoprotein
ComponentsBETA-MICROSEMINOPROTEIN
KeywordsINHIBITOR / POLYMORPHISM / ALTERNATIVE SPLICING
Function / homology
Function and homology information


extracellular space / nucleus
Similarity search - Function
N-terminal domain of TfIIb - #590 / Beta-microseminoprotein / Beta-microseminoprotein (PSP-94) / Complement Module, domain 1 / Complement Module; domain 1 / N-terminal domain of TfIIb / Single Sheet / Ribbon / Mainly Beta
Similarity search - Domain/homology
Beta-microseminoprotein
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / ANNEALING
AuthorsGhasriani, H. / Teilum, K. / Johnsson, Y. / Fernlund, P. / Drakenberg, T.
CitationJournal: J.Mol.Biol. / Year: 2006
Title: Solution Structure of Human and Porcine Beta-Microseminoprotein
Authors: Ghasriani, H. / Teilum, K. / Johnsson, Y. / Fernlund, P. / Drakenberg, T.
History
DepositionJul 24, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 24, 2006Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 15, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_software.name
Revision 1.4Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.5Oct 23, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BETA-MICROSEMINOPROTEIN


Theoretical massNumber of molelcules
Total (without water)10,9551
Polymers10,9551
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)10 / 200LOW ENERGY AND NO VIOLATIONS > 0.5 A
Representative

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Components

#1: Protein BETA-MICROSEMINOPROTEIN / PROSTATE SECRETED SEMINAL PLASMA PROTEIN / PROSTATE SECRETORY PROTEIN PSP94 / PSP-94 / IGBF / PN44 ...PROSTATE SECRETED SEMINAL PLASMA PROTEIN / PROSTATE SECRETORY PROTEIN PSP94 / PSP-94 / IGBF / PN44 / IMMUNOGLOBULIN-BINDING FACTOR / SEMINAL PLASMA BETA-INHIBIN


Mass: 10955.430 Da / Num. of mol.: 1 / Fragment: RESIDUES 21-114
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Organ: PROSTATE / Plasmid: PET30 XA/LIC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): NOVABLUE / References: UniProt: P08118
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: NOESY
NMR detailsText: NOE-RESTRAINTS WERE COLLECTED FROM 3D-15N-EDITED NOESY, 3D-1EC-EDITED NOESY AND 2D NOESY SPECTRA

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Sample preparation

DetailsContents: 90% WATER/10% D2O
Sample conditionspH: 6 / Temperature: 310.0 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
Xplor-NIHCLORErefinement
Xplor-NIHstructure solution
RefinementMethod: ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: LOW ENERGY AND NO VIOLATIONS > 0.5 A
Conformers calculated total number: 200 / Conformers submitted total number: 10

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