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Database: PDB
Entry: 1I5T
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Original site: 1I5T 
HEADER    ELECTRON TRANSPORT                      28-FEB-01   1I5T              
TITLE     SOLUTION STRUCTURE OF CYANOFERRICYTOCHROME C                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME C;                                              
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;                                 
SOURCE   3 ORGANISM_COMMON: HORSE;                                              
SOURCE   4 ORGANISM_TAXID: 9796;                                                
SOURCE   5 TISSUE: HEART                                                        
KEYWDS    CYTOCHROME C, CYANIDE, NMR STRUCTURE, CONFORMATIONAL                  
KEYWDS   2 TRANSITION, ELECTRON TRANSPORT                                       
EXPDTA    SOLUTION NMR                                                          
MDLTYP    MINIMIZED AVERAGE                                                     
AUTHOR    Y.YAO,C.QIAN,K.YE,J.WANG,W.TANG                                       
REVDAT   5   24-FEB-09 1I5T    1       VERSN                                    
REVDAT   4   01-APR-03 1I5T    1       JRNL                                     
REVDAT   3   31-DEC-02 1I5T    1       REMARK                                   
REVDAT   2   31-JUL-02 1I5T    1       JRNL                                     
REVDAT   1   21-MAR-01 1I5T    0                                                
JRNL        AUTH   Y.YAO,C.QIAN,K.YE,J.WANG,Z.BAI,W.TANG                        
JRNL        TITL   SOLUTION STRUCTURE OF CYANOFERRICYTOCHROME C:                
JRNL        TITL 2 LIGAND-CONTROLLED CONFORMATIONAL FLEXIBILITY AND             
JRNL        TITL 3 ELECTRONIC STRUCTURE OF THE HEME MOIETY.                     
JRNL        REF    J.BIOL.INORG.CHEM.            V.   7   539 2002              
JRNL        REFN                   ISSN 0949-8257                               
JRNL        PMID   11941512                                                     
JRNL        DOI    10.1007/S00775-001-0334-Y                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 5.0                                            
REMARK   3   AUTHORS     : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,       
REMARK   3                 SEIBEL,SINGH,WEINER,KOLLMAN                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I5T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012940.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 303                                
REMARK 210  PH                             : 7.0                                
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : 5MM CYTOCHROME C,50MM              
REMARK 210                                   POTASSIUM CYANIDE; 5MM             
REMARK 210                                   CYTOCHROME C, 50MM POTASSIUM       
REMARK 210                                   CYANIDE                            
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : DMX, DRX                           
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : XWINNMR 2.6, DYANA 1.5             
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS             
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 35                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : ALL CALCULATED STRUCTURES          
REMARK 210                                   SUBMITTED                          
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 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  13       28.02   -142.57                                   
REMARK 500    CYS A  14      -49.80   -133.92                                   
REMARK 500    LYS A  27     -146.19   -107.21                                   
REMARK 500    HIS A  33       84.69     13.86                                   
REMARK 500    LYS A  60      -94.55   -126.02                                   
REMARK 500    GLU A  61      -52.94   -147.76                                   
REMARK 500    MET A  80      -84.25    -66.37                                   
REMARK 500    ILE A  81      -50.09   -150.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   78     LYS A   79                  149.32                    
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    HIS A  18         0.09    SIDE_CHAIN                              
REMARK 500    TYR A  48         0.08    SIDE_CHAIN                              
REMARK 500    TYR A  67         0.07    SIDE_CHAIN                              
REMARK 500    TYR A  74         0.08    SIDE_CHAIN                              
REMARK 500    ARG A  91         0.14    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 110  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  18   NE2                                                    
REMARK 620 2 CYN A 105   C   176.8                                              
REMARK 620 3 CYN A 105   N   175.6   1.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 105                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 110                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AKK   RELATED DB: PDB                                   
REMARK 900 1AKK CONTAINS SOLUTION STRUCTURE OF THE NATIVE OXIDIZED              
REMARK 900 HORSE HEART CYTOCHROME C                                             
REMARK 900 RELATED ID: 1I5U   RELATED DB: PDB                                   
REMARK 900 1I5U CONTAINS SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE             
REMARK 900 MUTANT (E48A/E56A/D60A)                                              
DBREF  1I5T 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    CYN  A 105       2                                                       
HET    HEC  A 110      75                                                       
HETNAM     CYN CYANIDE ION                                                      
HETNAM     HEC HEME C                                                           
FORMUL   2  CYN    C N 1-                                                       
FORMUL   3  HEC    C34 H34 FE N4 O4                                             
HELIX    1   1 ASP A    2  CYS A   14  1                                  13    
HELIX    2   2 THR A   49  GLY A   56  1                                   8    
HELIX    3   3 GLU A   61  LEU A   68  1                                   8    
HELIX    4   4 ASN A   70  ILE A   75  1                                   6    
HELIX    5   5 LYS A   87  GLU A  104  1                                  18    
LINK        FE   HEC A 110                 NE2 HIS A  18     1555   1555  1.96  
LINK        FE   HEC A 110                 C   CYN A 105     1555   1555  1.84  
LINK         SG  CYS A  14                 CAB HEC A 110     1555   1555  1.84  
LINK         SG  CYS A  17                 CAC HEC A 110     1555   1555  1.83  
LINK        FE   HEC A 110                 N   CYN A 105     1555   1555  3.09  
CISPEP   1 MET A   80    ILE A   81          0       -13.23                     
SITE     1 AC1  2 TYR A  67  HEC A 110                                          
SITE     1 AC2 11 LYS A  13  CYS A  14  GLN A  16  CYS A  17                    
SITE     2 AC2 11 HIS A  18  THR A  28  PRO A  30  TRP A  59                    
SITE     3 AC2 11 TYR A  67  LEU A  68  CYN A 105                               
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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