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Database: PDB
Entry: 6MJM
LinkDB: 6MJM
Original site: 6MJM 
HEADER    OXIDOREDUCTASE                          21-SEP-18   6MJM              
TITLE     SUBSTRATE FREE CYTOCHROME P450 3A5 (CYP3A5)                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 3A5;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP 24-497;                                                
COMPND   5 SYNONYM: CYPIIIA5,CYTOCHROME P450 HLP2,CYTOCHROME P450-PCN3;         
COMPND   6 EC: 1.14.14.1;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: SEQADV 5VEU MET A 22 UNP P20815 INITIATING METHIONINE 
COMPND   9 SEQADV 5VEU ALA A 23 UNP P20815 EXPRESSION TAG SEQADV 5VEU HIS A 498 
COMPND  10 UNP P20815 EXPRESSION TAG SEQADV 5VEU HIS A 499 UNP P20815 EXPRESSION
COMPND  11 TAG SEQADV 5VEU HIS A 500 UNP P20815 EXPRESSION TAG SEQADV 5VEU HIS A
COMPND  12 501 UNP P20815 EXPRESSION TAG                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP3A5;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA];                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCWORI                                    
KEYWDS    CYTOCHROME P450, MONOOXYGENASE, MEMBRANE PROTEIN, DRUG METABOLISM,    
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.H.HSU,E.F.JOHNSON                                                   
REVDAT   4   01-JAN-20 6MJM    1       REMARK                                   
REVDAT   3   29-MAY-19 6MJM    1       JRNL                                     
REVDAT   2   10-APR-19 6MJM    1       JRNL                                     
REVDAT   1   03-APR-19 6MJM    0                                                
JRNL        AUTH   M.H.HSU,E.F.JOHNSON                                          
JRNL        TITL   ACTIVE-SITE DIFFERENCES BETWEEN SUBSTRATE-FREE AND           
JRNL        TITL 2 RITONAVIR-BOUND CYTOCHROME P450 (CYP) 3A5 REVEAL PLASTICITY  
JRNL        TITL 3 DIFFERENCES BETWEEN CYP3A5 AND CYP3A4.                       
JRNL        REF    J.BIOL.CHEM.                  V. 294  8015 2019              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30926609                                                     
JRNL        DOI    10.1074/JBC.RA119.007928                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.27                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26710                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1353                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.2740 -  4.7368    1.00     2666   150  0.1790 0.1804        
REMARK   3     2  4.7368 -  3.7612    1.00     2572   136  0.1757 0.2275        
REMARK   3     3  3.7612 -  3.2862    1.00     2536   141  0.2209 0.2788        
REMARK   3     4  3.2862 -  2.9860    1.00     2522   137  0.2587 0.3508        
REMARK   3     5  2.9860 -  2.7720    1.00     2535   134  0.2650 0.3221        
REMARK   3     6  2.7720 -  2.6087    1.00     2508   148  0.2588 0.3002        
REMARK   3     7  2.6087 -  2.4781    1.00     2514   131  0.2474 0.2854        
REMARK   3     8  2.4781 -  2.3702    1.00     2491   137  0.2521 0.3026        
REMARK   3     9  2.3702 -  2.2790    1.00     2531   115  0.2463 0.3241        
REMARK   3    10  2.2790 -  2.2004    0.99     2482   124  0.2700 0.3292        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3782                                  
REMARK   3   ANGLE     :  0.744           5129                                  
REMARK   3   CHIRALITY :  0.045            570                                  
REMARK   3   PLANARITY :  0.004            643                                  
REMARK   3   DIHEDRAL  : 11.912           2296                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 26 THROUGH 496)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5489  23.7448  15.6501              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4282 T22:   0.4517                                     
REMARK   3      T33:   0.4284 T12:  -0.0411                                     
REMARK   3      T13:  -0.1226 T23:   0.0348                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7754 L22:   3.0686                                     
REMARK   3      L33:   1.7375 L12:   0.5858                                     
REMARK   3      L13:   0.1710 L23:   0.2870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0066 S12:   0.0952 S13:   0.2524                       
REMARK   3      S21:   0.3603 S22:  -0.1017 S23:  -0.3749                       
REMARK   3      S31:  -0.3035 S32:   0.2141 S33:   0.0836                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6MJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237056.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-FEB-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97946                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26713                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 9.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.4700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.870                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1TQN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, ADA, ANAPOE 20, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 297K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       37.83500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       50.34500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       68.01000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       37.83500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       50.34500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.01000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       37.83500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       50.34500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.01000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       37.83500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       50.34500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       68.01000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     TYR A    25                                                      
REMARK 465     ARG A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     ASN A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     GLN A   265                                                      
REMARK 465     LYS A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     LEU A   269                                                      
REMARK 465     ASN A   280                                                      
REMARK 465     SER A   281                                                      
REMARK 465     LYS A   282                                                      
REMARK 465     GLU A   283                                                      
REMARK 465     THR A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     SER A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     GLY A   497                                                      
REMARK 465     HIS A   498                                                      
REMARK 465     HIS A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
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    LEU A  46      -52.69     70.50                                   
REMARK 500    VAL A  95      -62.01   -122.30                                   
REMARK 500    VAL A 101      -55.68   -134.94                                   
REMARK 500    PHE A 102       62.99   -101.50                                   
REMARK 500    ARG A 105     -143.13    -92.61                                   
REMARK 500    VAL A 111       -1.59   -140.23                                   
REMARK 500    ASP A 123     -126.96     58.14                                   
REMARK 500    ASP A 194       76.72   -106.64                                   
REMARK 500    LEU A 216       17.55     55.85                                   
REMARK 500    ILE A 371      -42.74     71.84                                   
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                             HEM A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 441   SG                                                     
REMARK 620 2 HEM A 601   NA  100.3                                              
REMARK 620 3 HEM A 601   NB   89.2  88.3                                        
REMARK 620 4 HEM A 601   NC   87.8 170.3  86.5                                  
REMARK 620 5 HEM A 601   ND   96.7  92.3 173.9  92.0                            
REMARK 620 6 HOH A 743   O   171.2  84.0  83.2  87.2  90.8                      
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 HEM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VEU   RELATED DB: PDB                                   
REMARK 900 P450 3A5 RITONAVIR COMPLEX                                           
DBREF  6MJM A   24   497  UNP    P20815   CP3A5_HUMAN     24    497             
SEQADV 6MJM MET A   22  UNP  P20815              INITIATING METHIONINE          
SEQADV 6MJM ALA A   23  UNP  P20815              EXPRESSION TAG                 
SEQADV 6MJM HIS A  498  UNP  P20815              EXPRESSION TAG                 
SEQADV 6MJM HIS A  499  UNP  P20815              EXPRESSION TAG                 
SEQADV 6MJM HIS A  500  UNP  P20815              EXPRESSION TAG                 
SEQADV 6MJM HIS A  501  UNP  P20815              EXPRESSION TAG                 
SEQRES   1 A  480  MET ALA LEU TYR GLY THR ARG THR HIS GLY LEU PHE LYS          
SEQRES   2 A  480  ARG LEU GLY ILE PRO GLY PRO THR PRO LEU PRO LEU LEU          
SEQRES   3 A  480  GLY ASN VAL LEU SER TYR ARG GLN GLY LEU TRP LYS PHE          
SEQRES   4 A  480  ASP THR GLU CYS TYR LYS LYS TYR GLY LYS MET TRP GLY          
SEQRES   5 A  480  THR TYR GLU GLY GLN LEU PRO VAL LEU ALA ILE THR ASP          
SEQRES   6 A  480  PRO ASP VAL ILE ARG THR VAL LEU VAL LYS GLU CYS TYR          
SEQRES   7 A  480  SER VAL PHE THR ASN ARG ARG SER LEU GLY PRO VAL GLY          
SEQRES   8 A  480  PHE MET LYS SER ALA ILE SER LEU ALA GLU ASP GLU GLU          
SEQRES   9 A  480  TRP LYS ARG ILE ARG SER LEU LEU SER PRO THR PHE THR          
SEQRES  10 A  480  SER GLY LYS LEU LYS GLU MET PHE PRO ILE ILE ALA GLN          
SEQRES  11 A  480  TYR GLY ASP VAL LEU VAL ARG ASN LEU ARG ARG GLU ALA          
SEQRES  12 A  480  GLU LYS GLY LYS PRO VAL THR LEU LYS ASP ILE PHE GLY          
SEQRES  13 A  480  ALA TYR SER MET ASP VAL ILE THR GLY THR SER PHE GLY          
SEQRES  14 A  480  VAL ASN ILE ASP SER LEU ASN ASN PRO GLN ASP PRO PHE          
SEQRES  15 A  480  VAL GLU SER THR LYS LYS PHE LEU LYS PHE GLY PHE LEU          
SEQRES  16 A  480  ASP PRO LEU PHE LEU SER ILE ILE LEU PHE PRO PHE LEU          
SEQRES  17 A  480  THR PRO VAL PHE GLU ALA LEU ASN VAL SER LEU PHE PRO          
SEQRES  18 A  480  LYS ASP THR ILE ASN PHE LEU SER LYS SER VAL ASN ARG          
SEQRES  19 A  480  MET LYS LYS SER ARG LEU ASN ASP LYS GLN LYS HIS ARG          
SEQRES  20 A  480  LEU ASP PHE LEU GLN LEU MET ILE ASP SER GLN ASN SER          
SEQRES  21 A  480  LYS GLU THR GLU SER HIS LYS ALA LEU SER ASP LEU GLU          
SEQRES  22 A  480  LEU ALA ALA GLN SER ILE ILE PHE ILE PHE ALA GLY TYR          
SEQRES  23 A  480  GLU THR THR SER SER VAL LEU SER PHE THR LEU TYR GLU          
SEQRES  24 A  480  LEU ALA THR HIS PRO ASP VAL GLN GLN LYS LEU GLN LYS          
SEQRES  25 A  480  GLU ILE ASP ALA VAL LEU PRO ASN LYS ALA PRO PRO THR          
SEQRES  26 A  480  TYR ASP ALA VAL VAL GLN MET GLU TYR LEU ASP MET VAL          
SEQRES  27 A  480  VAL ASN GLU THR LEU ARG LEU PHE PRO VAL ALA ILE ARG          
SEQRES  28 A  480  LEU GLU ARG THR CYS LYS LYS ASP VAL GLU ILE ASN GLY          
SEQRES  29 A  480  VAL PHE ILE PRO LYS GLY SER MET VAL VAL ILE PRO THR          
SEQRES  30 A  480  TYR ALA LEU HIS HIS ASP PRO LYS TYR TRP THR GLU PRO          
SEQRES  31 A  480  GLU GLU PHE ARG PRO GLU ARG PHE SER LYS LYS LYS ASP          
SEQRES  32 A  480  SER ILE ASP PRO TYR ILE TYR THR PRO PHE GLY THR GLY          
SEQRES  33 A  480  PRO ARG ASN CYS ILE GLY MET ARG PHE ALA LEU MET ASN          
SEQRES  34 A  480  MET LYS LEU ALA LEU ILE ARG VAL LEU GLN ASN PHE SER          
SEQRES  35 A  480  PHE LYS PRO CYS LYS GLU THR GLN ILE PRO LEU LYS LEU          
SEQRES  36 A  480  ASP THR GLN GLY LEU LEU GLN PRO GLU LYS PRO ILE VAL          
SEQRES  37 A  480  LEU LYS VAL ASP SER ARG ASP GLY HIS HIS HIS HIS              
HET    HEM  A 601      43                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     HEM HEME                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3  GOL    3(C3 H8 O3)                                                  
FORMUL   6  HOH   *49(H2 O)                                                     
HELIX    1 AA1 GLY A   31  GLY A   37  1                                   7    
HELIX    2 AA2 ASN A   49  ARG A   54  5                                   6    
HELIX    3 AA3 GLY A   56  GLY A   69  1                                  14    
HELIX    4 AA4 ASP A   86  VAL A   95  1                                  10    
HELIX    5 AA5 VAL A  111  ALA A  117  5                                   7    
HELIX    6 AA6 GLU A  122  SER A  134  1                                  13    
HELIX    7 AA7 PRO A  135  PHE A  137  5                                   3    
HELIX    8 AA8 THR A  138  GLN A  151  1                                  14    
HELIX    9 AA9 GLN A  151  GLU A  165  1                                  15    
HELIX   10 AB1 LEU A  172  GLY A  190  1                                  19    
HELIX   11 AB2 ASP A  194  ASN A  198  5                                   5    
HELIX   12 AB3 ASP A  201  LYS A  209  1                                   9    
HELIX   13 AB4 ASP A  217  PHE A  226  1                                  10    
HELIX   14 AB5 LEU A  229  LEU A  236  1                                   8    
HELIX   15 AB6 PRO A  242  SER A  259  1                                  18    
HELIX   16 AB7 PHE A  271  SER A  278  1                                   8    
HELIX   17 AB8 SER A  291  HIS A  324  1                                  34    
HELIX   18 AB9 HIS A  324  LEU A  339  1                                  16    
HELIX   19 AC1 THR A  346  GLN A  352  1                                   7    
HELIX   20 AC2 MET A  353  PHE A  367  1                                  15    
HELIX   21 AC3 PRO A  397  HIS A  403  1                                   7    
HELIX   22 AC4 ARG A  415  SER A  420  5                                   6    
HELIX   23 AC5 GLY A  443  ASN A  461  1                                  19    
SHEET    1 AA1 4 MET A  71  GLU A  76  0                                        
SHEET    2 AA1 4 LEU A  79  ILE A  84 -1  O  VAL A  81   N  THR A  74           
SHEET    3 AA1 4 MET A 393  ILE A 396  1  O  MET A 393   N  LEU A  82           
SHEET    4 AA1 4 LEU A 373  THR A 376 -1  N  ARG A 375   O  VAL A 394           
SHEET    1 AA2 3 VAL A 170  THR A 171  0                                        
SHEET    2 AA2 3 VAL A 489  SER A 494 -1  O  LEU A 490   N  VAL A 170           
SHEET    3 AA2 3 PHE A 462  LYS A 465 -1  N  LYS A 465   O  LYS A 491           
SHEET    1 AA3 2 VAL A 381  ILE A 383  0                                        
SHEET    2 AA3 2 VAL A 386  ILE A 388 -1  O  ILE A 388   N  VAL A 381           
LINK         SG  CYS A 441                FE   HEM A 601     1555   1555  2.41  
LINK        FE   HEM A 601                 O   HOH A 743     1555   1555  2.44  
CISPEP   1 ILE A  472    PRO A  473          0        -3.28                     
SITE     1 AC1 23 ARG A 105  ILE A 118  SER A 119  TRP A 126                    
SITE     2 AC1 23 ARG A 130  PHE A 137  ALA A 305  GLY A 306                    
SITE     3 AC1 23 THR A 309  VAL A 369  ALA A 370  ARG A 375                    
SITE     4 AC1 23 PRO A 433  PHE A 434  GLY A 435  ARG A 439                    
SITE     5 AC1 23 ASN A 440  CYS A 441  ILE A 442  ALA A 447                    
SITE     6 AC1 23 MET A 451  HOH A 729  HOH A 743                               
SITE     1 AC2  1 GOL A 603                                                     
SITE     1 AC3  3 VAL A  50  ARG A  54  GOL A 602                               
CRYST1   75.670  100.690  136.020  90.00  90.00  90.00 I 2 2 2       8          
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      0.013215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009931  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007352        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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