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Database: PDB
Entry: 2FRC
LinkDB: 2FRC
Original site: 2FRC 
HEADER    ELECTRON TRANSPORT                      02-JUL-96   2FRC              
TITLE     CYTOCHROME C (REDUCED) FROM EQUUS CABALLUS, NMR, MINIMIZED AVERAGE    
TITLE    2 STRUCTURE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 OTHER_DETAILS: REDUCED                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: HORSE;                                              
SOURCE   4 ORGANISM_TAXID: 9796;                                                
SOURCE   5 ORGAN: HEART                                                         
KEYWDS    ELECTRON TRANSPORT                                                    
EXPDTA    SOLUTION NMR                                                          
AUTHOR    P.X.QI,D.L.DI STEFANO,A.J.WAND                                        
REVDAT   3   29-NOV-17 2FRC    1       REMARK HELIX                             
REVDAT   2   24-FEB-09 2FRC    1       VERSN                                    
REVDAT   1   29-JUL-97 2FRC    0                                                
SPRSDE     29-JUL-97 2FRC      1FRC                                             
JRNL        AUTH   P.X.QI,R.A.BECKMAN,A.J.WAND                                  
JRNL        TITL   SOLUTION STRUCTURE OF HORSE HEART FERRICYTOCHROME C AND      
JRNL        TITL 2 DETECTION OF REDOX-RELATED STRUCTURAL CHANGES BY             
JRNL        TITL 3 HIGH-RESOLUTION 1H NMR.                                      
JRNL        REF    BIOCHEMISTRY                  V.  35 12275 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8823161                                                      
JRNL        DOI    10.1021/BI961042W                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.X.QI,J.L.URBAUER,E.J.FUENTES,M.F.LEOPOLD,A.J.WAND          
REMARK   1  TITL   STRUCTURAL WATER IN OXIDIZED AND REDUCED HORSE HEART         
REMARK   1  TITL 2 CYTOCHROME C                                                 
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   1   378 1994              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.X.QI,D.L.DI STEFANO,A.J.WAND                               
REMARK   1  TITL   SOLUTION STRUCTURE OF HORSE HEART FERROCYTOCHROME C          
REMARK   1  TITL 2 DETERMINED BY HIGH-RESOLUTION NMR AND RESTRAINED SIMULATED   
REMARK   1  TITL 3 ANNEALING                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  33  6408 1994              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   A.J.WAND,D.L.DI STEFANO,Y.Q.FENG,H.RODER,S.W.ENGLANDER       
REMARK   1  TITL   PROTON RESONANCE ASSIGNMENTS OF HORSE FERROCYTOCHROME C      
REMARK   1  REF    BIOCHEMISTRY                  V.  28   186 1989              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FRC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178105.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 293                                
REMARK 210  PH                             : 5.7                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : COSY; NOESY; TOCSY                 
REMARK 210  SPECTROMETER FIELD STRENGTH    : 500 MHZ; 600 MHZ                   
REMARK 210  SPECTROMETER MODEL             : AMX                                
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : FELIX/DSPACE/XPLOR/ANCILL          
REMARK 210   METHOD USED                   : SIMMULATED ANNEALING               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 256                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : LOWEST PENALTY                     
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HE2  TYR A    74     H2   HOH A   204              1.33            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   8      -83.55    -82.17                                   
REMARK 500    ILE A   9      -32.42    -39.73                                   
REMARK 500    GLU A  21     -158.37   -150.05                                   
REMARK 500    LYS A  25       95.95    -45.20                                   
REMARK 500    HIS A  26      173.75    -55.38                                   
REMARK 500    LYS A  27     -152.93   -135.36                                   
REMARK 500    ASN A  31       97.91    -49.50                                   
REMARK 500    LEU A  32       35.15    -76.59                                   
REMARK 500    TYR A  48      158.84    -31.68                                   
REMARK 500    ASP A  50      -31.63    -33.37                                   
REMARK 500    LYS A  55      -95.52    -79.99                                   
REMARK 500    ILE A  57     -164.76   -110.03                                   
REMARK 500    GLU A  61      -42.76    -23.67                                   
REMARK 500    ILE A  75      -62.43   -159.50                                   
REMARK 500    PRO A  76       87.25    -43.51                                   
REMARK 500    THR A  78      -85.65    -65.78                                   
REMARK 500    ALA A  83       25.88   -170.18                                   
REMARK 500    LYS A  86      -72.53    -48.43                                   
REMARK 500    LYS A  87      -93.14    -74.98                                   
REMARK 500    LYS A  88      -44.13   -179.73                                   
REMARK 500    LYS A  99      -36.54    -34.05                                   
REMARK 500    ALA A 101      -73.48    -61.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  38         0.31    SIDE CHAIN                              
REMARK 500    ARG A  91         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC A 105  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 HEC A 105   NA   97.5                                              
REMARK 620 3 HEC A 105   NB   82.4  89.8                                        
REMARK 620 4 HEC A 105   NC   84.9 177.6  90.4                                  
REMARK 620 5 HEC A 105   ND  100.7  89.7 176.8  89.9                            
REMARK 620 6 MET A  80   SD  161.4  97.8  87.1  79.8  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 105                 
DBREF  2FRC A    1   104  UNP    P00004   CYC_HORSE        1    104             
SEQRES   1 A  104  GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS          
SEQRES   2 A  104  CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS          
SEQRES   3 A  104  LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS          
SEQRES   4 A  104  THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN          
SEQRES   5 A  104  LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET          
SEQRES   6 A  104  GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR          
SEQRES   7 A  104  LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG          
SEQRES   8 A  104  GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU          
HET    HEC  A 105      75                                                       
HETNAM     HEC HEME C                                                           
FORMUL   2  HEC    C34 H34 FE N4 O4                                             
FORMUL   3  HOH   *6(H2 O)                                                      
HELIX    1 HNR LYS A    5  CYS A   14  1                                  10    
HELIX    2 H5R THR A   49  ASN A   54  1                                   6    
HELIX    3 H6R LYS A   60  THR A   63  5                                   4    
HELIX    4 H7R THR A   63  ASN A   70  1                                   8    
HELIX    5 HCR LYS A   88  ARG A   91  5                                   4    
HELIX    6 HC2 ARG A   91  GLU A  104  1                                  14    
LINK         CAB HEC A 105                 SG  CYS A  14     1555   1555  1.81  
LINK         CAC HEC A 105                 SG  CYS A  17     1555   1555  1.80  
LINK        FE   HEC A 105                 NE2 HIS A  18     1555   1555  1.93  
LINK        FE   HEC A 105                 SD  MET A  80     1555   1555  2.23  
SITE     1 AC1 24 LYS A  13  CYS A  14  CYS A  17  HIS A  18                    
SITE     2 AC1 24 THR A  28  LEU A  32  LEU A  35  LYS A  39                    
SITE     3 AC1 24 THR A  40  GLY A  41  PHE A  46  TYR A  48                    
SITE     4 AC1 24 THR A  49  ASN A  52  TRP A  59  TYR A  67                    
SITE     5 AC1 24 THR A  78  LYS A  79  MET A  80  ILE A  81                    
SITE     6 AC1 24 PHE A  82  LEU A  94  HOH A 201  HOH A 203                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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