4MBN

REFINEMENT OF MYOGLOBIN AND CYTOCHROME C


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.172 

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Ligand Structure Quality Assessment 


This is version 2.2 of the entry. See complete history


Literature

Refinement of Myoglobin and Cytochrome C

Takano, T.

(1984) Methods And Applications In Crystallographic Computing : 262


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MYOGLOBIN153Physeter macrocephalusMutation(s): 0 
EC: 1.11.1 (UniProt), 1.7 (UniProt)
UniProt
Find proteins for P02185 (Physeter macrocephalus)
Explore P02185 
Go to UniProtKB:  P02185
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02185
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.172 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 64.56α = 90
b = 30.97β = 105.86
c = 34.86γ = 90
Software Package:
Software NamePurpose
EREFrefinement

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

  • Released Date: 1989-07-12 
  • Deposition Author(s): Takano, T.
  • This entry supersedes: 2MBN

Revision History  (Full details and data files)

  • Version 1.0: 1989-07-12
    Type: Initial release
  • Version 1.1: 2008-03-25
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 2.0: 2023-02-08
    Type: Remediation
    Changes: Atomic model, Data collection, Database references, Derived calculations, Other
  • Version 2.1: 2023-03-15
    Changes: Advisory
  • Version 2.2: 2024-05-22
    Changes: Data collection