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Database: PDB
Entry: 1HWJ
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Original site: 1HWJ 
HEADER    OXIDOREDUCTASE                          09-JAN-01   1HWJ              
TITLE     COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE           
TITLE    2 WITH CERIVASTATIN                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HMG-COA REDUCTASE;                                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC PORTION;                                         
COMPND   5 SYNONYM: 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE,            
COMPND   6 HYDROXYMETHYLGLUTARYL-COA REDUCTASE;                                 
COMPND   7 EC: 1.1.1.34;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HMGCR;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-CS                                   
KEYWDS    PROTEIN-INHIBITOR COMPLEX, OXIDOREDUCTASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.S.ISTVAN,J.DEISENHOFER                                              
REVDAT   2   24-FEB-09 1HWJ    1       VERSN                                    
REVDAT   1   11-MAY-01 1HWJ    0                                                
JRNL        AUTH   E.S.ISTVAN,J.DEISENHOFER                                     
JRNL        TITL   STRUCTURAL MECHANISM FOR STATIN INHIBITION OF                
JRNL        TITL 2 HMG-COA REDUCTASE.                                           
JRNL        REF    SCIENCE                       V. 292  1160 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11349148                                                     
JRNL        DOI    10.1126/SCIENCE.1059344                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.26 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2264580.470                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 80409                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2029                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10569                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3660                       
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 269                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11938                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 294                                     
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.11000                                              
REMARK   3    B22 (A**2) : -3.52000                                             
REMARK   3    B33 (A**2) : 2.41000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 12.55000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.40                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.35                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.38                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.39                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.830 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.440 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.240 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.880 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 27.87                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; 250                  
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; 5                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : ADP_PAR:ADP.PARAM                              
REMARK   3  PARAMETER FILE  5  : CER_PAR:CER.PARAM                              
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : ADP_PAR:ADP.TOP                                
REMARK   3  TOPOLOGY FILE  5   : CER_PAR:CER.TOP                                
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NCS-RESTRAINTS WERE USED                  
REMARK   4                                                                      
REMARK   4 1HWJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB012629.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 123.0                              
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.942                              
REMARK 200  MONOCHROMATOR                  : HORIZONTALLY BENT SI (111)         
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80912                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.260                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 28.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.26                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER           
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1DQA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE,              
REMARK 280  GLYCEROL, DTT, HEPES, MICROSEEDING, PH 7.5 AT 294 K,                
REMARK 280  MICROSEEDING                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
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       86.49150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31090 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 50930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -213.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     GLY A   422                                                      
REMARK 465     ALA A   423                                                      
REMARK 465     MET A   424                                                      
REMARK 465     ALA A   425                                                      
REMARK 465     SER A   426                                                      
REMARK 465     SER A   427                                                      
REMARK 465     VAL A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     VAL A   430                                                      
REMARK 465     THR A   431                                                      
REMARK 465     GLN A   432                                                      
REMARK 465     GLU A   433                                                      
REMARK 465     PRO A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     ILE A   436                                                      
REMARK 465     GLU A   437                                                      
REMARK 465     LEU A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     ARG A   440                                                      
REMARK 465     GLU A   441                                                      
REMARK 465     LEU A   452                                                      
REMARK 465     GLY A   453                                                      
REMARK 465     ASN A   454                                                      
REMARK 465     ALA A   455                                                      
REMARK 465     GLU A   456                                                      
REMARK 465     LYS A   457                                                      
REMARK 465     GLY A   458                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     LYS A   460                                                      
REMARK 465     PHE A   461                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     VAL A   863                                                      
REMARK 465     LYS A   864                                                      
REMARK 465     SER A   865                                                      
REMARK 465     HIS A   866                                                      
REMARK 465     MET A   867                                                      
REMARK 465     ILE A   868                                                      
REMARK 465     HIS A   869                                                      
REMARK 465     ASN A   870                                                      
REMARK 465     ARG A   871                                                      
REMARK 465     SER A   872                                                      
REMARK 465     LYS A   873                                                      
REMARK 465     ILE A   874                                                      
REMARK 465     ASN A   875                                                      
REMARK 465     LEU A   876                                                      
REMARK 465     GLN A   877                                                      
REMARK 465     ASP A   878                                                      
REMARK 465     LEU A   879                                                      
REMARK 465     GLN A   880                                                      
REMARK 465     GLY A   881                                                      
REMARK 465     ALA A   882                                                      
REMARK 465     CYS A   883                                                      
REMARK 465     THR A   884                                                      
REMARK 465     LYS A   885                                                      
REMARK 465     LYS A   886                                                      
REMARK 465     THR A   887                                                      
REMARK 465     ALA A   888                                                      
REMARK 465     GLY B   422                                                      
REMARK 465     ALA B   423                                                      
REMARK 465     MET B   424                                                      
REMARK 465     ALA B   425                                                      
REMARK 465     SER B   426                                                      
REMARK 465     SER B   427                                                      
REMARK 465     VAL B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     VAL B   430                                                      
REMARK 465     THR B   431                                                      
REMARK 465     GLN B   432                                                      
REMARK 465     GLU B   433                                                      
REMARK 465     PRO B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     ILE B   436                                                      
REMARK 465     GLU B   437                                                      
REMARK 465     LEU B   438                                                      
REMARK 465     PRO B   439                                                      
REMARK 465     ARG B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     PRO B   442                                                      
REMARK 465     ARG B   443                                                      
REMARK 465     PRO B   444                                                      
REMARK 465     ASN B   445                                                      
REMARK 465     GLU B   446                                                      
REMARK 465     GLU B   447                                                      
REMARK 465     CYS B   448                                                      
REMARK 465     LEU B   449                                                      
REMARK 465     GLN B   450                                                      
REMARK 465     ILE B   451                                                      
REMARK 465     LEU B   452                                                      
REMARK 465     GLY B   453                                                      
REMARK 465     ASN B   454                                                      
REMARK 465     ALA B   455                                                      
REMARK 465     GLU B   456                                                      
REMARK 465     LYS B   457                                                      
REMARK 465     GLY B   458                                                      
REMARK 465     ALA B   459                                                      
REMARK 465     LYS B   460                                                      
REMARK 465     PHE B   461                                                      
REMARK 465     LEU B   462                                                      
REMARK 465     HIS B   861                                                      
REMARK 465     LEU B   862                                                      
REMARK 465     VAL B   863                                                      
REMARK 465     LYS B   864                                                      
REMARK 465     SER B   865                                                      
REMARK 465     HIS B   866                                                      
REMARK 465     MET B   867                                                      
REMARK 465     ILE B   868                                                      
REMARK 465     HIS B   869                                                      
REMARK 465     ASN B   870                                                      
REMARK 465     ARG B   871                                                      
REMARK 465     SER B   872                                                      
REMARK 465     LYS B   873                                                      
REMARK 465     ILE B   874                                                      
REMARK 465     ASN B   875                                                      
REMARK 465     LEU B   876                                                      
REMARK 465     GLN B   877                                                      
REMARK 465     ASP B   878                                                      
REMARK 465     LEU B   879                                                      
REMARK 465     GLN B   880                                                      
REMARK 465     GLY B   881                                                      
REMARK 465     ALA B   882                                                      
REMARK 465     CYS B   883                                                      
REMARK 465     THR B   884                                                      
REMARK 465     LYS B   885                                                      
REMARK 465     LYS B   886                                                      
REMARK 465     THR B   887                                                      
REMARK 465     ALA B   888                                                      
REMARK 465     GLY C   422                                                      
REMARK 465     ALA C   423                                                      
REMARK 465     MET C   424                                                      
REMARK 465     ALA C   425                                                      
REMARK 465     SER C   426                                                      
REMARK 465     SER C   427                                                      
REMARK 465     VAL C   428                                                      
REMARK 465     LEU C   429                                                      
REMARK 465     VAL C   430                                                      
REMARK 465     THR C   431                                                      
REMARK 465     GLN C   432                                                      
REMARK 465     GLU C   433                                                      
REMARK 465     PRO C   434                                                      
REMARK 465     GLU C   435                                                      
REMARK 465     ILE C   436                                                      
REMARK 465     GLU C   437                                                      
REMARK 465     LEU C   438                                                      
REMARK 465     PRO C   439                                                      
REMARK 465     ARG C   440                                                      
REMARK 465     GLU C   441                                                      
REMARK 465     ILE C   451                                                      
REMARK 465     LEU C   452                                                      
REMARK 465     GLY C   453                                                      
REMARK 465     ASN C   454                                                      
REMARK 465     ALA C   455                                                      
REMARK 465     GLU C   456                                                      
REMARK 465     LYS C   457                                                      
REMARK 465     GLY C   458                                                      
REMARK 465     ALA C   459                                                      
REMARK 465     LYS C   460                                                      
REMARK 465     PHE C   461                                                      
REMARK 465     HIS C   861                                                      
REMARK 465     LEU C   862                                                      
REMARK 465     VAL C   863                                                      
REMARK 465     LYS C   864                                                      
REMARK 465     SER C   865                                                      
REMARK 465     HIS C   866                                                      
REMARK 465     MET C   867                                                      
REMARK 465     ILE C   868                                                      
REMARK 465     HIS C   869                                                      
REMARK 465     ASN C   870                                                      
REMARK 465     ARG C   871                                                      
REMARK 465     SER C   872                                                      
REMARK 465     LYS C   873                                                      
REMARK 465     ILE C   874                                                      
REMARK 465     ASN C   875                                                      
REMARK 465     LEU C   876                                                      
REMARK 465     GLN C   877                                                      
REMARK 465     ASP C   878                                                      
REMARK 465     LEU C   879                                                      
REMARK 465     GLN C   880                                                      
REMARK 465     GLY C   881                                                      
REMARK 465     ALA C   882                                                      
REMARK 465     CYS C   883                                                      
REMARK 465     THR C   884                                                      
REMARK 465     LYS C   885                                                      
REMARK 465     LYS C   886                                                      
REMARK 465     THR C   887                                                      
REMARK 465     ALA C   888                                                      
REMARK 465     GLY D   422                                                      
REMARK 465     ALA D   423                                                      
REMARK 465     MET D   424                                                      
REMARK 465     ALA D   425                                                      
REMARK 465     SER D   426                                                      
REMARK 465     SER D   427                                                      
REMARK 465     VAL D   428                                                      
REMARK 465     LEU D   429                                                      
REMARK 465     VAL D   430                                                      
REMARK 465     THR D   431                                                      
REMARK 465     GLN D   432                                                      
REMARK 465     GLU D   433                                                      
REMARK 465     PRO D   434                                                      
REMARK 465     GLU D   435                                                      
REMARK 465     ILE D   436                                                      
REMARK 465     GLU D   437                                                      
REMARK 465     LEU D   438                                                      
REMARK 465     PRO D   439                                                      
REMARK 465     ARG D   440                                                      
REMARK 465     GLU D   441                                                      
REMARK 465     PRO D   442                                                      
REMARK 465     ARG D   443                                                      
REMARK 465     PRO D   444                                                      
REMARK 465     ASN D   445                                                      
REMARK 465     GLU D   446                                                      
REMARK 465     GLU D   447                                                      
REMARK 465     CYS D   448                                                      
REMARK 465     LEU D   449                                                      
REMARK 465     GLN D   450                                                      
REMARK 465     ILE D   451                                                      
REMARK 465     LEU D   452                                                      
REMARK 465     GLY D   453                                                      
REMARK 465     ASN D   454                                                      
REMARK 465     ALA D   455                                                      
REMARK 465     GLU D   456                                                      
REMARK 465     LYS D   457                                                      
REMARK 465     GLY D   458                                                      
REMARK 465     ALA D   459                                                      
REMARK 465     LYS D   460                                                      
REMARK 465     PHE D   461                                                      
REMARK 465     LYS D   474                                                      
REMARK 465     HIS D   475                                                      
REMARK 465     ILE D   476                                                      
REMARK 465     PRO D   477                                                      
REMARK 465     ALA D   478                                                      
REMARK 465     TYR D   479                                                      
REMARK 465     LYS D   480                                                      
REMARK 465     HIS D   861                                                      
REMARK 465     LEU D   862                                                      
REMARK 465     VAL D   863                                                      
REMARK 465     LYS D   864                                                      
REMARK 465     SER D   865                                                      
REMARK 465     HIS D   866                                                      
REMARK 465     MET D   867                                                      
REMARK 465     ILE D   868                                                      
REMARK 465     HIS D   869                                                      
REMARK 465     ASN D   870                                                      
REMARK 465     ARG D   871                                                      
REMARK 465     SER D   872                                                      
REMARK 465     LYS D   873                                                      
REMARK 465     ILE D   874                                                      
REMARK 465     ASN D   875                                                      
REMARK 465     LEU D   876                                                      
REMARK 465     GLN D   877                                                      
REMARK 465     ASP D   878                                                      
REMARK 465     LEU D   879                                                      
REMARK 465     GLN D   880                                                      
REMARK 465     GLY D   881                                                      
REMARK 465     ALA D   882                                                      
REMARK 465     CYS D   883                                                      
REMARK 465     THR D   884                                                      
REMARK 465     LYS D   885                                                      
REMARK 465     LYS D   886                                                      
REMARK 465     THR D   887                                                      
REMARK 465     ALA D   888                                                      
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    CYS A 448        2.83    -66.18                                   
REMARK 500    GLN A 450     -125.34    -69.61                                   
REMARK 500    TYR A 514      -21.66   -149.17                                   
REMARK 500    ALA A 525      -43.77   -148.87                                   
REMARK 500    CYS A 561       -5.71     79.53                                   
REMARK 500    SER A 651       42.65   -152.80                                   
REMARK 500    LYS A 735      -64.40   -102.12                                   
REMARK 500    LEU A 737      -66.55   -104.22                                   
REMARK 500    TYR A 749       57.41    -98.21                                   
REMARK 500    HIS A 752       44.69   -160.30                                   
REMARK 500    ASN A 830       77.17   -157.65                                   
REMARK 500    LYS B 474      -57.49     18.26                                   
REMARK 500    HIS B 475      -64.15    -11.71                                   
REMARK 500    LEU B 484      -82.00    -77.65                                   
REMARK 500    THR B 487      132.86    168.22                                   
REMARK 500    TYR B 514      -17.79   -163.23                                   
REMARK 500    ALA B 525      -37.55   -152.95                                   
REMARK 500    CYS B 561       -5.32     80.22                                   
REMARK 500    LEU B 631      109.84    -56.88                                   
REMARK 500    SER B 651       45.44   -154.14                                   
REMARK 500    LYS B 735      -64.84   -100.35                                   
REMARK 500    LEU B 737      -66.34   -106.59                                   
REMARK 500    TYR B 749       56.30    -97.54                                   
REMARK 500    HIS B 752       44.57   -160.25                                   
REMARK 500    SER B 799       58.88   -141.95                                   
REMARK 500    ARG C 443      159.92    -49.15                                   
REMARK 500    GLU C 447      -47.13   -157.28                                   
REMARK 500    LEU C 449       11.90   -168.17                                   
REMARK 500    TYR C 514      -19.18   -150.85                                   
REMARK 500    ALA C 525      -40.93   -143.15                                   
REMARK 500    CYS C 561       -6.12     80.38                                   
REMARK 500    ALA C 629       90.01    -64.99                                   
REMARK 500    GLN C 632     -145.81   -100.70                                   
REMARK 500    SER C 651       43.55   -153.91                                   
REMARK 500    LYS C 735      -66.07   -100.84                                   
REMARK 500    LEU C 737      -65.05   -105.48                                   
REMARK 500    TYR C 749       56.10    -95.11                                   
REMARK 500    HIS C 752       45.55   -162.05                                   
REMARK 500    SER C 799       59.36   -142.66                                   
REMARK 500    SER D 463     -161.81    -79.33                                   
REMARK 500    TYR D 514      -21.53   -161.67                                   
REMARK 500    ALA D 525      -39.15   -153.78                                   
REMARK 500    CYS D 561       -4.82     79.31                                   
REMARK 500    ALA D 629      107.22    -58.52                                   
REMARK 500    GLN D 632      -60.87    -90.96                                   
REMARK 500    SER D 651       42.27   -154.44                                   
REMARK 500    LYS D 735      -65.47   -100.72                                   
REMARK 500    LEU D 737      -67.55   -105.71                                   
REMARK 500    TYR D 749       57.22    -98.84                                   
REMARK 500    HIS D 752       45.34   -162.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 101                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 102                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 103                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 104                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 105                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 106                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 116 B 1                   
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 116 A 2                   
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 116 D 3                   
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 116 C 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DQ8   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX              
REMARK 900 WITH HMG AND COA                                                     
REMARK 900 RELATED ID: 1DQ9   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX              
REMARK 900 WITH HMG-COA                                                         
REMARK 900 RELATED ID: 1DQA   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX              
REMARK 900 WITH HMG, COA, AND NADP+                                             
REMARK 900 RELATED ID: 1HW8   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH                 
REMARK 900 COMAPCTIN                                                            
REMARK 900 RELATED ID: 1HW9   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH                 
REMARK 900 SIMVASTATIN                                                          
REMARK 900 RELATED ID: 1HWI   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH                 
REMARK 900 FLUVASTATIN                                                          
REMARK 900 RELATED ID: 1HWK   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN WITH                 
REMARK 900 ATORVASTATIN                                                         
REMARK 900 RELATED ID: 1HWL   RELATED DB: PDB                                   
REMARK 900 CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE IN COMPLEX              
REMARK 900 WITH ROSUVASTATIN                                                    
DBREF  1HWJ A  426   888  UNP    P04035   HMDH_HUMAN     426    888             
DBREF  1HWJ B  426   888  UNP    P04035   HMDH_HUMAN     426    888             
DBREF  1HWJ C  426   888  UNP    P04035   HMDH_HUMAN     426    888             
DBREF  1HWJ D  426   888  UNP    P04035   HMDH_HUMAN     426    888             
SEQADV 1HWJ GLY A  422  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA A  423  UNP  P04035              INSERTION                      
SEQADV 1HWJ MET A  424  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA A  425  UNP  P04035              INSERTION                      
SEQADV 1HWJ ILE A  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 1HWJ GLY B  422  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA B  423  UNP  P04035              INSERTION                      
SEQADV 1HWJ MET B  424  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA B  425  UNP  P04035              INSERTION                      
SEQADV 1HWJ ILE B  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 1HWJ GLY C  422  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA C  423  UNP  P04035              INSERTION                      
SEQADV 1HWJ MET C  424  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA C  425  UNP  P04035              INSERTION                      
SEQADV 1HWJ ILE C  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 1HWJ GLY D  422  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA D  423  UNP  P04035              INSERTION                      
SEQADV 1HWJ MET D  424  UNP  P04035              INSERTION                      
SEQADV 1HWJ ALA D  425  UNP  P04035              INSERTION                      
SEQADV 1HWJ ILE D  485  UNP  P04035    MET   485 ENGINEERED                     
SEQRES   1 A  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 A  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 A  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 A  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 A  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 A  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 A  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 A  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 A  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 A  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 A  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 A  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 A  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 A  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 A  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 A  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 A  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 A  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 A  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 A  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 A  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 A  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 A  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 A  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 A  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 A  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 A  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 A  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 A  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 A  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 A  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 A  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 A  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 A  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 A  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 A  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 B  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 B  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 B  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 B  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 B  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 B  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 B  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 B  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 B  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 B  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 B  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 B  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 B  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 B  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 B  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 B  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 B  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 B  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 B  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 B  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 B  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 B  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 B  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 B  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 B  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 B  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 B  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 B  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 B  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 B  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 B  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 B  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 B  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 B  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 B  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 B  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 C  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 C  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 C  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 C  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 C  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 C  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 C  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 C  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 C  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 C  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 C  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 C  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 C  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 C  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 C  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 C  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 C  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 C  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 C  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 C  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 C  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 C  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 C  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 C  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 C  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 C  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 C  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 C  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 C  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 C  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 C  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 C  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 C  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 C  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 C  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 C  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
SEQRES   1 D  467  GLY ALA MET ALA SER SER VAL LEU VAL THR GLN GLU PRO          
SEQRES   2 D  467  GLU ILE GLU LEU PRO ARG GLU PRO ARG PRO ASN GLU GLU          
SEQRES   3 D  467  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   4 D  467  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   5 D  467  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   6 D  467  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   7 D  467  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   8 D  467  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   9 D  467  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES  10 D  467  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  11 D  467  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  12 D  467  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  13 D  467  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  14 D  467  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  15 D  467  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  16 D  467  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  17 D  467  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  18 D  467  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  19 D  467  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  20 D  467  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  21 D  467  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  22 D  467  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  23 D  467  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  24 D  467  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  25 D  467  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  26 D  467  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  27 D  467  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  28 D  467  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  29 D  467  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  30 D  467  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  31 D  467  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  32 D  467  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  33 D  467  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  34 D  467  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  35 D  467  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN LEU          
SEQRES  36 D  467  GLN ASP LEU GLN GLY ALA CYS THR LYS LYS THR ALA              
HET    ADP  A 101      27                                                       
HET    ADP  A 102      27                                                       
HET    ADP  C 103      27                                                       
HET    ADP  C 104      27                                                       
HET    ADP  B 105      27                                                       
HET    ADP  D 106      27                                                       
HET    116  B   1      33                                                       
HET    116  A   2      33                                                       
HET    116  D   3      33                                                       
HET    116  C   4      33                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     116 7-[4-(4-FLUORO-PHENYL)-5-HYDROXYMETHYL-2,6-                      
HETNAM   2 116  DIISOPROPYL-PYRIDIN-3-YL]-3,5-DIHYDROXY-HEPTANOIC ACID          
HETSYN     116 CERIVASTATIN                                                     
FORMUL   5  ADP    6(C10 H15 N5 O10 P2)                                         
FORMUL  11  116    4(C26 H36 F N O5)                                            
FORMUL  15  HOH   *186(H2 O)                                                    
HELIX    1   1 GLU A  446  GLN A  450  5                                   5    
HELIX    2   2 SER A  463  LYS A  474  1                                  12    
HELIX    3   3 PRO A  477  LEU A  484  5                                   8    
HELIX    4   4 HIS A  488  LYS A  502  1                                  15    
HELIX    5   5 ASN A  518  VAL A  522  5                                   5    
HELIX    6   6 CYS A  561  GLY A  576  1                                  16    
HELIX    7   7 ARG A  598  GLU A  610  1                                  13    
HELIX    8   8 THR A  611  SER A  624  1                                  14    
HELIX    9   9 GLY A  656  PHE A  675  1                                  20    
HELIX   10  10 ALA A  694  GLY A  701  1                                   8    
HELIX   11  11 PRO A  713  VAL A  720  1                                   8    
HELIX   12  12 THR A  724  LEU A  737  1                                  14    
HELIX   13  13 LEU A  737  ALA A  743  1                                   7    
HELIX   14  14 HIS A  752  CYS A  764  1                                  13    
HELIX   15  15 ASP A  767  ALA A  769  5                                   3    
HELIX   16  16 GLN A  770  SER A  775  1                                   6    
HELIX   17  17 GLY A  806  ASN A  810  5                                   5    
HELIX   18  18 LEU A  811  GLY A  822  1                                  12    
HELIX   19  19 GLY A  832  GLY A  860  1                                  29    
HELIX   20  20 SER B  463  ALA B  473  1                                  11    
HELIX   21  21 PRO B  477  TYR B  479  5                                   3    
HELIX   22  22 LYS B  480  ILE B  485  1                                   6    
HELIX   23  23 THR B  487  LYS B  501  1                                  15    
HELIX   24  24 SER B  507  LEU B  512  5                                   6    
HELIX   25  25 CYS B  561  LEU B  575  1                                  15    
HELIX   26  26 ARG B  598  THR B  611  1                                  14    
HELIX   27  27 THR B  611  SER B  624  1                                  14    
HELIX   28  28 GLY B  656  PHE B  675  1                                  20    
HELIX   29  29 ALA B  694  GLY B  701  1                                   8    
HELIX   30  30 PRO B  713  VAL B  720  1                                   8    
HELIX   31  31 THR B  724  LEU B  737  1                                  14    
HELIX   32  32 LEU B  737  ALA B  743  1                                   7    
HELIX   33  33 HIS B  752  CYS B  764  1                                  13    
HELIX   34  34 ASP B  767  ALA B  769  5                                   3    
HELIX   35  35 GLN B  770  SER B  775  1                                   6    
HELIX   36  36 GLY B  806  ASN B  810  5                                   5    
HELIX   37  37 LEU B  811  LEU B  821  1                                  11    
HELIX   38  38 GLY B  832  GLY B  860  1                                  29    
HELIX   39  39 SER C  463  HIS C  475  1                                  13    
HELIX   40  40 PRO C  477  TYR C  479  5                                   3    
HELIX   41  41 LYS C  480  ILE C  485  1                                   6    
HELIX   42  42 HIS C  488  LYS C  501  1                                  14    
HELIX   43  43 SER C  507  LEU C  512  5                                   6    
HELIX   44  44 ASN C  518  MET C  523  1                                   6    
HELIX   45  45 CYS C  561  LEU C  575  1                                  15    
HELIX   46  46 ARG C  598  GLU C  610  1                                  13    
HELIX   47  47 THR C  611  SER C  624  1                                  14    
HELIX   48  48 GLY C  656  PHE C  675  1                                  20    
HELIX   49  49 ALA C  694  GLY C  701  1                                   8    
HELIX   50  50 PRO C  713  VAL C  720  1                                   8    
HELIX   51  51 THR C  724  LEU C  737  1                                  14    
HELIX   52  52 LEU C  737  ALA C  743  1                                   7    
HELIX   53  53 HIS C  752  CYS C  764  1                                  13    
HELIX   54  54 ASP C  767  ALA C  769  5                                   3    
HELIX   55  55 GLN C  770  SER C  775  1                                   6    
HELIX   56  56 GLY C  806  ASN C  810  5                                   5    
HELIX   57  57 LEU C  811  LEU C  821  1                                  11    
HELIX   58  58 GLY C  832  GLY C  860  1                                  29    
HELIX   59  59 SER D  463  ALA D  473  1                                  11    
HELIX   60  60 THR D  487  LYS D  501  1                                  15    
HELIX   61  61 GLU D  505  LEU D  512  5                                   8    
HELIX   62  62 CYS D  561  GLY D  576  1                                  16    
HELIX   63  63 ARG D  598  GLU D  610  1                                  13    
HELIX   64  64 THR D  611  SER D  624  1                                  14    
HELIX   65  65 GLY D  656  PHE D  675  1                                  20    
HELIX   66  66 ALA D  694  GLY D  701  1                                   8    
HELIX   67  67 PRO D  713  VAL D  720  1                                   8    
HELIX   68  68 THR D  724  LEU D  737  1                                  14    
HELIX   69  69 LEU D  737  ALA D  743  1                                   7    
HELIX   70  70 HIS D  752  CYS D  764  1                                  13    
HELIX   71  71 ASP D  767  ALA D  769  5                                   3    
HELIX   72  72 GLN D  770  SER D  775  1                                   6    
HELIX   73  73 GLY D  806  ASN D  810  5                                   5    
HELIX   74  74 LEU D  811  LEU D  821  1                                  11    
HELIX   75  75 GLY D  832  GLY D  860  1                                  29    
SHEET    1   A 4 LYS A 549  ALA A 556  0                                        
SHEET    2   A 4 VAL A 530  LEU A 546 -1  N  GLY A 539   O  MET A 555           
SHEET    3   A 4 VAL B 530  LEU B 546 -1  N  ILE B 531   O  VAL A 538           
SHEET    4   A 4 LYS B 549  ALA B 556 -1  O  LYS B 549   N  LEU B 546           
SHEET    1   B 8 GLY A 748  TYR A 749  0                                        
SHEET    2   B 8 CYS A 777  SER A 784  1  O  CYS A 777   N  TYR A 749           
SHEET    3   B 8 ASP A 790  ILE A 800 -1  O  ASP A 790   N  SER A 784           
SHEET    4   B 8 GLY A 703  ILE A 712 -1  N  LYS A 704   O  ILE A 800           
SHEET    5   B 8 SER A 580  ARG A 590 -1  N  SER A 580   O  GLU A 709           
SHEET    6   B 8 ASN A 642  ARG A 650 -1  N  PHE A 647   O  ARG A 590           
SHEET    7   B 8 VAL A 593  ARG A 595 -1  N  VAL A 594   O  LEU A 643           
SHEET    8   B 8 GLN A 679  ALA A 682 -1  N  GLN A 679   O  ARG A 595           
SHEET    1   C 7 GLY A 748  TYR A 749  0                                        
SHEET    2   C 7 CYS A 777  SER A 784  1  O  CYS A 777   N  TYR A 749           
SHEET    3   C 7 ASP A 790  ILE A 800 -1  O  ASP A 790   N  SER A 784           
SHEET    4   C 7 GLY A 703  ILE A 712 -1  N  LYS A 704   O  ILE A 800           
SHEET    5   C 7 SER A 580  ARG A 590 -1  N  SER A 580   O  GLU A 709           
SHEET    6   C 7 ASN A 642  ARG A 650 -1  N  PHE A 647   O  ARG A 590           
SHEET    7   C 7 ARG A 630  ALA A 639 -1  O  ARG A 630   N  ARG A 650           
SHEET    1   D 8 GLY B 748  TYR B 749  0                                        
SHEET    2   D 8 CYS B 777  SER B 784  1  O  CYS B 777   N  TYR B 749           
SHEET    3   D 8 ASP B 790  ILE B 800 -1  N  ASP B 790   O  SER B 784           
SHEET    4   D 8 GLY B 703  ILE B 712 -1  N  LYS B 704   O  ILE B 800           
SHEET    5   D 8 SER B 580  ARG B 590 -1  N  SER B 580   O  GLU B 709           
SHEET    6   D 8 ASN B 642  ARG B 650 -1  N  PHE B 647   O  ARG B 590           
SHEET    7   D 8 VAL B 593  ARG B 595 -1  N  VAL B 594   O  LEU B 643           
SHEET    8   D 8 GLN B 679  ALA B 682 -1  N  GLN B 679   O  ARG B 595           
SHEET    1   E 7 GLY B 748  TYR B 749  0                                        
SHEET    2   E 7 CYS B 777  SER B 784  1  O  CYS B 777   N  TYR B 749           
SHEET    3   E 7 ASP B 790  ILE B 800 -1  N  ASP B 790   O  SER B 784           
SHEET    4   E 7 GLY B 703  ILE B 712 -1  N  LYS B 704   O  ILE B 800           
SHEET    5   E 7 SER B 580  ARG B 590 -1  N  SER B 580   O  GLU B 709           
SHEET    6   E 7 ASN B 642  ARG B 650 -1  N  PHE B 647   O  ARG B 590           
SHEET    7   E 7 ARG B 630  ALA B 639 -1  O  ARG B 630   N  ARG B 650           
SHEET    1   F 4 LYS C 549  ALA C 556  0                                        
SHEET    2   F 4 VAL C 530  LEU C 546 -1  N  GLY C 539   O  MET C 555           
SHEET    3   F 4 VAL D 530  LEU D 546 -1  N  ILE D 531   O  VAL C 538           
SHEET    4   F 4 LYS D 549  ALA D 556 -1  O  LYS D 549   N  LEU D 546           
SHEET    1   G 8 GLY C 748  TYR C 749  0                                        
SHEET    2   G 8 CYS C 777  SER C 784  1  O  CYS C 777   N  TYR C 749           
SHEET    3   G 8 ASP C 790  ILE C 800 -1  O  ASP C 790   N  SER C 784           
SHEET    4   G 8 GLY C 703  ILE C 712 -1  N  LYS C 704   O  ILE C 800           
SHEET    5   G 8 SER C 580  ARG C 590 -1  N  SER C 580   O  GLU C 709           
SHEET    6   G 8 ASN C 642  ARG C 650 -1  N  PHE C 647   O  ARG C 590           
SHEET    7   G 8 VAL C 593  ARG C 595 -1  N  VAL C 594   O  LEU C 643           
SHEET    8   G 8 GLN C 679  ALA C 682 -1  N  GLN C 679   O  ARG C 595           
SHEET    1   H 7 GLY C 748  TYR C 749  0                                        
SHEET    2   H 7 CYS C 777  SER C 784  1  O  CYS C 777   N  TYR C 749           
SHEET    3   H 7 ASP C 790  ILE C 800 -1  O  ASP C 790   N  SER C 784           
SHEET    4   H 7 GLY C 703  ILE C 712 -1  N  LYS C 704   O  ILE C 800           
SHEET    5   H 7 SER C 580  ARG C 590 -1  N  SER C 580   O  GLU C 709           
SHEET    6   H 7 ASN C 642  ARG C 650 -1  N  PHE C 647   O  ARG C 590           
SHEET    7   H 7 ARG C 630  ALA C 639 -1  O  ARG C 630   N  ARG C 650           
SHEET    1   I 8 GLY D 748  TYR D 749  0                                        
SHEET    2   I 8 CYS D 777  SER D 784  1  O  CYS D 777   N  TYR D 749           
SHEET    3   I 8 ASP D 790  ILE D 800 -1  O  ASP D 790   N  SER D 784           
SHEET    4   I 8 GLY D 703  ILE D 712 -1  N  LYS D 704   O  ILE D 800           
SHEET    5   I 8 SER D 580  ARG D 590 -1  N  SER D 580   O  GLU D 709           
SHEET    6   I 8 ASN D 642  ARG D 650 -1  N  PHE D 647   O  ARG D 590           
SHEET    7   I 8 VAL D 593  ARG D 595 -1  N  VAL D 594   O  LEU D 643           
SHEET    8   I 8 GLN D 679  ALA D 682 -1  N  GLN D 679   O  ARG D 595           
SHEET    1   J 7 GLY D 748  TYR D 749  0                                        
SHEET    2   J 7 CYS D 777  SER D 784  1  O  CYS D 777   N  TYR D 749           
SHEET    3   J 7 ASP D 790  ILE D 800 -1  O  ASP D 790   N  SER D 784           
SHEET    4   J 7 GLY D 703  ILE D 712 -1  N  LYS D 704   O  ILE D 800           
SHEET    5   J 7 SER D 580  ARG D 590 -1  N  SER D 580   O  GLU D 709           
SHEET    6   J 7 ASN D 642  ARG D 650 -1  N  PHE D 647   O  ARG D 590           
SHEET    7   J 7 ARG D 630  ALA D 639 -1  O  ARG D 630   N  ARG D 650           
CISPEP   1 GLY A  542    PRO A  543          0         0.83                     
CISPEP   2 CYS A  688    THR A  689          0        -1.46                     
CISPEP   3 GLY B  542    PRO B  543          0         1.06                     
CISPEP   4 CYS B  688    THR B  689          0        -1.56                     
CISPEP   5 GLY C  542    PRO C  543          0         1.50                     
CISPEP   6 CYS C  688    THR C  689          0        -1.17                     
CISPEP   7 GLY D  542    PRO D  543          0         0.97                     
CISPEP   8 CYS D  688    THR D  689          0        -1.26                     
SITE     1 AC1  8 TYR A 479  GLU A 528  ASN A 529  ALA B 564                    
SITE     2 AC1  8 ASN B 567  ARG B 568  ARG B 571  LYS B 722                    
SITE     1 AC2  7 ALA A 564  ASN A 567  ARG A 568  ARG A 571                    
SITE     2 AC2  7 LYS A 722  TYR B 479  ASN B 529                               
SITE     1 AC3  8 TYR C 479  GLU C 528  ASN C 529  ALA D 564                    
SITE     2 AC3  8 ASN D 567  ARG D 568  ARG D 571  LYS D 722                    
SITE     1 AC4 14 PHE C 628  SER C 651  GLY C 652  ASP C 653                    
SITE     2 AC4 14 ALA C 654  MET C 655  GLY C 656  MET C 657                    
SITE     3 AC4 14 ASN C 658  MET C 659  VAL C 805  GLY C 806                    
SITE     4 AC4 14 ALA C 826  HOH C1110                                          
SITE     1 AC5 15 PHE B 628  SER B 651  GLY B 652  ASP B 653                    
SITE     2 AC5 15 ALA B 654  MET B 655  GLY B 656  MET B 657                    
SITE     3 AC5 15 ASN B 658  MET B 659  VAL B 805  GLY B 806                    
SITE     4 AC5 15 GLY B 807  ALA B 826  HOH B1034                               
SITE     1 AC6 12 PHE D 628  SER D 651  GLY D 652  ASP D 653                    
SITE     2 AC6 12 ALA D 654  MET D 655  GLY D 656  MET D 657                    
SITE     3 AC6 12 ASN D 658  VAL D 805  ALA D 826  HOH D1116                    
SITE     1 AC7 18 GLU A 559  GLY A 560  CYS A 561  LEU A 562                    
SITE     2 AC7 18 LYS A 735  ALA A 751  HIS A 752  ASN A 755                    
SITE     3 AC7 18 LEU A 853  ALA A 856  ARG B 590  SER B 661                    
SITE     4 AC7 18 VAL B 683  SER B 684  ASP B 690  LYS B 691                    
SITE     5 AC7 18 LYS B 692  HOH B1131                                          
SITE     1 AC8 16 ARG A 590  VAL A 683  SER A 684  ASP A 690                    
SITE     2 AC8 16 LYS A 691  LYS A 692  HOH A1002  GLU B 559                    
SITE     3 AC8 16 GLY B 560  CYS B 561  LEU B 562  LYS B 735                    
SITE     4 AC8 16 ALA B 751  ASN B 755  LEU B 853  ALA B 856                    
SITE     1 AC9 17 GLU C 559  GLY C 560  CYS C 561  LEU C 562                    
SITE     2 AC9 17 SER C 565  LYS C 735  ALA C 751  ASN C 755                    
SITE     3 AC9 17 LEU C 853  ARG D 590  VAL D 683  SER D 684                    
SITE     4 AC9 17 ASN D 686  ASP D 690  LYS D 691  LYS D 692                    
SITE     5 AC9 17 HOH D1163                                                     
SITE     1 BC1 17 ARG C 590  VAL C 683  SER C 684  ASP C 690                    
SITE     2 BC1 17 LYS C 691  LYS C 692  HOH C1111  GLU D 559                    
SITE     3 BC1 17 GLY D 560  CYS D 561  LEU D 562  LYS D 735                    
SITE     4 BC1 17 ALA D 751  HIS D 752  ASN D 755  LEU D 853                    
SITE     5 BC1 17 ALA D 856                                                     
CRYST1   74.616  172.983   80.159  90.00 117.35  90.00 P 1 21 1      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      0.013402  0.000000  0.006933        0.00000                         
SCALE2      0.000000  0.005781  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014045        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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