+Open data
-Basic information
Entry | Database: PDB / ID: 2spz | |||||||||
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Title | STAPHYLOCOCCAL PROTEIN A, Z-DOMAIN, NMR, 10 STRUCTURES | |||||||||
Components | IMMUNOGLOBULIN G BINDING PROTEIN A | |||||||||
Keywords | IMMUNE SYSTEM / IMMUNOGLOBULIN-BINDING PROTEIN / THREE-HELICAL BUNDLE STRUCTURE | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Staphylococcus aureus (bacteria) | |||||||||
Method | SOLUTION NMR / SIMULATED ANNEALING WITH RESTRAINED MOLECULAR DYNAMICS | |||||||||
Authors | Montelione, G.T. / Tashiro, M. / Tejero, R. / Lyons, B.A. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: High-resolution solution NMR structure of the Z domain of staphylococcal protein A. Authors: Tashiro, M. / Tejero, R. / Zimmerman, D.E. / Celda, B. / Nilsson, B. / Montelione, G.T. #1: Journal: Biochemistry / Year: 1996 Title: The Mechanism of Binding Staphylococcal Protein a to Immunoglobin G Does not Involve Helix Unwinding Authors: Jendeberg, L. / Tashiro, M. / Tejero, R. / Lyons, B.A. / Uhlen, M. / Montelione, G.T. / Nilsson, B. #2: Journal: Curr.Opin.Struct.Biol. / Year: 1995 Title: Structures of Bacterial Immunoglobulin-Binding Domains and Their Complexes with Immunoglobulin Authors: Tashiro, M. / Montelione, G.T. #3: Journal: Biochemistry / Year: 1993 Title: An Improved Strategy for Determining Resonance Assignments for Isotopically Enriched Proteins and its Application to an Engineered Domain of Staphylococcal Protein A Authors: Lyons, B.A. / Tashiro, M. / Cedergren, L. / Nilsson, B. / Montelione, G.T. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2spz.cif.gz | 185.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2spz.ent.gz | 153.4 KB | Display | PDB format |
PDBx/mmJSON format | 2spz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2spz_validation.pdf.gz | 354.6 KB | Display | wwPDB validaton report |
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Full document | 2spz_full_validation.pdf.gz | 418 KB | Display | |
Data in XML | 2spz_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | 2spz_validation.cif.gz | 18.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sp/2spz ftp://data.pdbj.org/pub/pdb/validation_reports/sp/2spz | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Antibody | Mass: 6648.316 Da / Num. of mol.: 1 / Fragment: Z DOMAIN / Mutation: A1V, G29A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus (bacteria) / Cellular location: CELL WALL / Plasmid: PDHZ / Production host: Escherichia coli (E. coli) / Strain (production host): RV308 / References: UniProt: P38507 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: SEE REMARKS |
NMR details | Text: NULL NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG-HNCO, 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH, 3D PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-HN(CA)CO, 3D ...Text: NULL NMR EXPERIMENTS CONDUCTED: 2D PFG-[15N]HSQC, 3D PFG-HNCO, 3D PFG-(HA)CA(CO)NH, 3D PFG-HA(CA)(CO)NH, 3D PFG-HA(CA)NH, 3D PFG-CBCANH, 3D PFG-CBCA(CO)NH, 3D PFG- (HA)CANH, 3D PFG-HN(CA)CO, 3D PFG-HCCNH-TOCSY, 3D PFG-HCC (CO)NH-TOCSY, 2D CT |
-Sample preparation
Sample conditions | Ionic strength: 10 MILLIMOLAR K2HPO4 / pH: 6.5 / Pressure: 1 atm / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian MODIFIED UNITY 500 / Manufacturer: Varian / Model: MODIFIED UNITY 500 / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING WITH RESTRAINED MOLECULAR DYNAMICS Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST CONFORMATIONAL ENERGY / Conformers calculated total number: 40 / Conformers submitted total number: 10 |