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Yorodumi- PDB-1qq3: THE SOLUTION STRUCTURE OF THE HEME BINDING VARIANT ARG98CYS OF OX... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qq3 | ||||||
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Title | THE SOLUTION STRUCTURE OF THE HEME BINDING VARIANT ARG98CYS OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562 | ||||||
Components | CYTOCHROME B562 | ||||||
Keywords | ELECTRON TRANSPORT / FOUR HELIX BUNDLE / HEMOPROTEIN | ||||||
Function / homology | Function and homology information electron transport chain / periplasmic space / electron transfer activity / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, ENERGY MINIMIZATION | ||||||
Model type details | minimized average | ||||||
Authors | Arnesano, F. / Banci, L. / Bertini, I. / Ciofi-Baffoni, S. / Barker, P.D. / Woodyear, T. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: Structural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b562. Authors: Arnesano, F. / Banci, L. / Bertini, I. / Ciofi-Baffoni, S. / Woodyear, T.L. / Johnson, C.M. / Barker, P.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qq3.cif.gz | 47.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qq3.ent.gz | 32.4 KB | Display | PDB format |
PDBx/mmJSON format | 1qq3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1qq3_validation.pdf.gz | 469.8 KB | Display | wwPDB validaton report |
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Full document | 1qq3_full_validation.pdf.gz | 472.4 KB | Display | |
Data in XML | 1qq3_validation.xml.gz | 4.5 KB | Display | |
Data in CIF | 1qq3_validation.cif.gz | 5.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qq/1qq3 ftp://data.pdbj.org/pub/pdb/validation_reports/qq/1qq3 | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11745.190 Da / Num. of mol.: 1 / Mutation: R98C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PCEB562 / Production host: Escherichia coli (E. coli) / References: UniProt: P0ABE7 |
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#2: Chemical | ChemComp-HEB / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: TORSION ANGLE DYNAMICS, ENERGY MINIMIZATION / Software ordinal: 1 Details: A TOTAL OF 4325 NOESY CROSS-PEAKS WAS ASSIGNED, INTEGRATED AND TRANSFORMED IN UPPER DISTANCE LIMITS; 23 DISTANCE CONSTRAINTS WERE DERIVED FROM 1D NOE EXPERIMENTS INVOLVING FAST RELAXING ...Details: A TOTAL OF 4325 NOESY CROSS-PEAKS WAS ASSIGNED, INTEGRATED AND TRANSFORMED IN UPPER DISTANCE LIMITS; 23 DISTANCE CONSTRAINTS WERE DERIVED FROM 1D NOE EXPERIMENTS INVOLVING FAST RELAXING PARAMAGNETIC SHIFTED SIGNALS. TOTALLY, THEY CORRESPONDED TO 2595 UPPER DISTANCE LIMITS, OF WHICH 2145 WERE FOUND TO BE MEANINGFUL. IN ADDITION, 45 3JHNHA COUPLINGS OBTAINED FROM THE HNHA 3D SPECTRUM AND 397 PCS WERE USED FOR THE STRUCTURE CALCULATIONS. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: ENERGY MINIMIZED AVERAGE STRUCTURE Conformers submitted total number: 1 |