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Database: PDB
Entry: 3BGL
LinkDB: 3BGL
Original site: 3BGL 
HEADER    OXIDOREDUCTASE                          26-NOV-07   3BGL              
TITLE     HEPATOSELECTIVITY OF STATINS: DESIGN AND SYNTHESIS OF 4-SULFAMOYL     
TITLE    2 PYRROLES AS HMG-COA REDUCTASE INHIBITORS                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE;           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 441-875);                       
COMPND   5 SYNONYM: HMG-COA REDUCTASE;                                          
COMPND   6 EC: 1.1.1.34;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: BL21 STAR                                  
KEYWDS    OXIDOREDUCTASE, CHOLESTEROL BIOSYNTHESIS, HMG-COA, NADPH, STATIN,     
KEYWDS   2 ALTERNATIVE SPLICING, ENDOPLASMIC RETICULUM, GLYCOPROTEIN, LIPID     
KEYWDS   3 SYNTHESIS, MEMBRANE, PEROXISOME, POLYMORPHISM, STEROID BIOSYNTHESIS, 
KEYWDS   4 TRANSMEMBRANE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.C.FINZEL,A.PAVLOVSKY,W.K.C.PARK                                     
REVDAT   4   25-OCT-17 3BGL    1       REMARK                                   
REVDAT   3   24-FEB-09 3BGL    1       VERSN                                    
REVDAT   2   29-APR-08 3BGL    1       JRNL                                     
REVDAT   1   29-JAN-08 3BGL    0                                                
JRNL        AUTH   W.K.PARK,R.M.KENNEDY,S.D.LARSEN,S.MILLER,B.D.ROTH,Y.SONG,    
JRNL        AUTH 2 B.A.STEINBAUGH,K.SUN,B.D.TAIT,M.C.KOWALA,B.K.TRIVEDI,        
JRNL        AUTH 3 B.AUERBACH,V.ASKEW,L.DILLON,J.C.HANSELMAN,Z.LIN,G.H.LU,      
JRNL        AUTH 4 A.ROBERTSON,C.SEKERKE                                        
JRNL        TITL   HEPATOSELECTIVITY OF STATINS: DESIGN AND SYNTHESIS OF        
JRNL        TITL 2 4-SULFAMOYL PYRROLES AS HMG-COA REDUCTASE INHIBITORS.        
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  1151 2008              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   18155906                                                     
JRNL        DOI    10.1016/J.BMCL.2007.11.124                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 64927                          
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 + TEST SET) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3345                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1895                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 107                          
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12389                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 679                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.34000                                              
REMARK   3    B22 (A**2) : -2.88000                                             
REMARK   3    B33 (A**2) : -2.82000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -2.58000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.623         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.282         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.217         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.070         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12748 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 11820 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17245 ; 1.189 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 27545 ; 0.742 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1660 ; 5.510 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1978 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14216 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2359 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2789 ; 0.171 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 14262 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7805 ; 0.080 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   715 ; 0.160 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    32 ; 0.205 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    87 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  8241 ; 0.313 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13176 ; 0.599 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4507 ; 0.827 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4069 ; 1.484 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3BGL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045494.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-03                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64967                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.7                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 34.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19100                            
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       86.07800            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 25310 ANGSTROM**2                         
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     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
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     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
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     HIS C   435                                                      
REMARK 465     HIS C   436                                                      
REMARK 465     HIS C   437                                                      
REMARK 465     HIS C   438                                                      
REMARK 465     HIS C   439                                                      
REMARK 465     HIS C   440                                                      
REMARK 465     GLU C   441                                                      
REMARK 465     PRO C   442                                                      
REMARK 465     ARG C   443                                                      
REMARK 465     ALA C   455                                                      
REMARK 465     GLU C   456                                                      
REMARK 465     LYS C   457                                                      
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     HIS D   435                                                      
REMARK 465     HIS D   436                                                      
REMARK 465     HIS D   437                                                      
REMARK 465     HIS D   438                                                      
REMARK 465     HIS D   439                                                      
REMARK 465     HIS D   440                                                      
REMARK 465     GLU D   441                                                      
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   860                                                      
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   933     O    HOH C   954              1.85            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 457      -88.82   -135.12                                   
REMARK 500    ALA A 473       23.75     84.65                                   
REMARK 500    LYS A 474      172.49     38.28                                   
REMARK 500    HIS A 475      -54.30    133.66                                   
REMARK 500    ALA A 478      -42.76    156.97                                   
REMARK 500    GLU A 486      -68.72    -27.33                                   
REMARK 500    TYR A 514      -22.04   -144.01                                   
REMARK 500    ALA A 525      -40.91   -156.12                                   
REMARK 500    CYS A 561       -8.49     82.70                                   
REMARK 500    ALA A 694      134.47   -170.66                                   
REMARK 500    LYS A 735      -65.24   -102.58                                   
REMARK 500    TYR A 749       55.58    -95.56                                   
REMARK 500    HIS A 752       41.13   -154.45                                   
REMARK 500    PRO A 786      -92.08    -37.55                                   
REMARK 500    SER A 799       53.07   -146.34                                   
REMARK 500    ASN A 830       76.70   -153.61                                   
REMARK 500    LYS B 457      -77.29   -112.11                                   
REMARK 500    LYS B 474       -0.43     77.32                                   
REMARK 500    TYR B 514      -27.15   -154.12                                   
REMARK 500    ALA B 525      -45.27   -156.83                                   
REMARK 500    CYS B 561       -8.45     80.18                                   
REMARK 500    SER B 651       29.20   -140.42                                   
REMARK 500    THR B 723     -166.90   -160.40                                   
REMARK 500    LYS B 735      -69.21   -101.80                                   
REMARK 500    LEU B 737      -66.84   -106.82                                   
REMARK 500    TYR B 749       59.85    -96.66                                   
REMARK 500    HIS B 752       45.62   -151.43                                   
REMARK 500    SER B 799       50.25   -143.43                                   
REMARK 500    ASN C 445      -64.76    -96.62                                   
REMARK 500    ALA C 478       48.93    -95.99                                   
REMARK 500    GLU C 482      -62.61    -27.66                                   
REMARK 500    TYR C 514      -30.56   -162.82                                   
REMARK 500    ALA C 525      -50.15   -150.88                                   
REMARK 500    CYS C 561       -6.86     74.09                                   
REMARK 500    ALA C 629       96.83    -68.14                                   
REMARK 500    SER C 651       28.41   -140.58                                   
REMARK 500    LYS C 735      -67.06    -99.26                                   
REMARK 500    LEU C 737      -69.03    -94.00                                   
REMARK 500    TYR C 749       55.11    -95.14                                   
REMARK 500    HIS C 752       42.27   -159.57                                   
REMARK 500    SER C 799       52.85   -144.52                                   
REMARK 500    ASN C 830       79.30   -155.01                                   
REMARK 500    TYR D 514      -19.97   -146.53                                   
REMARK 500    ALA D 525      -46.13   -162.14                                   
REMARK 500    GLU D 548       -6.81     71.40                                   
REMARK 500    CYS D 561       -8.66     79.14                                   
REMARK 500    SER D 651       31.04   -147.64                                   
REMARK 500    ASN D 686       17.07     58.66                                   
REMARK 500    LYS D 735      -68.69   -105.71                                   
REMARK 500    LEU D 737      -72.47   -108.26                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 RAMACHANDRAN OUTLIERS.                        
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 RID A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RID B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RID C 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RID D 3                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Q1L   RELATED DB: PDB                                   
REMARK 900 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A COMPLEXED WITH 882             
REMARK 900 RELATED ID: 2Q6B   RELATED DB: PDB                                   
REMARK 900 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A COMPLEXED WITH HR2             
REMARK 900 RELATED ID: 2Q6C   RELATED DB: PDB                                   
REMARK 900 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A COMPLEXED WITH HR1             
REMARK 900 RELATED ID: 2R4F   RELATED DB: PDB                                   
REMARK 900 3-HYDROXY-3-METHYLGLUTARYL-COENZYME A COMPLEXED WITH RIE             
DBREF  3BGL A  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3BGL B  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3BGL C  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3BGL D  441   875  UNP    P04035   HMDH_HUMAN     441    875             
SEQADV 3BGL HIS A  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS A  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS A  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS A  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS A  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS A  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL ILE A  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3BGL HIS B  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS B  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS B  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS B  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS B  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS B  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL ILE B  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3BGL HIS C  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS C  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS C  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS C  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS C  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS C  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL ILE C  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3BGL HIS D  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS D  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS D  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS D  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS D  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL HIS D  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3BGL ILE D  485  UNP  P04035    MET   485 ENGINEERED                     
SEQRES   1 A  441  HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU          
SEQRES   2 A  441  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   3 A  441  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   4 A  441  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   5 A  441  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   6 A  441  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   7 A  441  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   8 A  441  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES   9 A  441  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  10 A  441  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  11 A  441  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  12 A  441  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  13 A  441  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  14 A  441  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  15 A  441  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  16 A  441  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  17 A  441  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  18 A  441  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  19 A  441  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  20 A  441  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  21 A  441  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  22 A  441  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  23 A  441  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  24 A  441  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  25 A  441  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  26 A  441  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  27 A  441  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  28 A  441  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  29 A  441  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  30 A  441  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  31 A  441  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  32 A  441  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  33 A  441  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  34 A  441  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN              
SEQRES   1 B  441  HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU          
SEQRES   2 B  441  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   3 B  441  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   4 B  441  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   5 B  441  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   6 B  441  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   7 B  441  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   8 B  441  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES   9 B  441  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  10 B  441  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  11 B  441  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  12 B  441  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  13 B  441  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  14 B  441  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  15 B  441  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  16 B  441  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  17 B  441  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  18 B  441  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  19 B  441  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  20 B  441  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  21 B  441  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  22 B  441  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  23 B  441  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  24 B  441  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  25 B  441  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  26 B  441  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  27 B  441  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  28 B  441  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  29 B  441  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  30 B  441  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  31 B  441  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  32 B  441  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  33 B  441  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  34 B  441  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN              
SEQRES   1 C  441  HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU          
SEQRES   2 C  441  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   3 C  441  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   4 C  441  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   5 C  441  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   6 C  441  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   7 C  441  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   8 C  441  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES   9 C  441  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  10 C  441  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  11 C  441  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  12 C  441  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  13 C  441  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  14 C  441  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  15 C  441  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  16 C  441  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  17 C  441  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  18 C  441  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  19 C  441  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  20 C  441  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  21 C  441  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  22 C  441  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  23 C  441  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  24 C  441  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  25 C  441  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  26 C  441  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  27 C  441  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  28 C  441  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  29 C  441  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  30 C  441  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  31 C  441  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  32 C  441  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  33 C  441  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  34 C  441  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN              
SEQRES   1 D  441  HIS HIS HIS HIS HIS HIS GLU PRO ARG PRO ASN GLU GLU          
SEQRES   2 D  441  CYS LEU GLN ILE LEU GLY ASN ALA GLU LYS GLY ALA LYS          
SEQRES   3 D  441  PHE LEU SER ASP ALA GLU ILE ILE GLN LEU VAL ASN ALA          
SEQRES   4 D  441  LYS HIS ILE PRO ALA TYR LYS LEU GLU THR LEU ILE GLU          
SEQRES   5 D  441  THR HIS GLU ARG GLY VAL SER ILE ARG ARG GLN LEU LEU          
SEQRES   6 D  441  SER LYS LYS LEU SER GLU PRO SER SER LEU GLN TYR LEU          
SEQRES   7 D  441  PRO TYR ARG ASP TYR ASN TYR SER LEU VAL MET GLY ALA          
SEQRES   8 D  441  CYS CYS GLU ASN VAL ILE GLY TYR MET PRO ILE PRO VAL          
SEQRES   9 D  441  GLY VAL ALA GLY PRO LEU CYS LEU ASP GLU LYS GLU PHE          
SEQRES  10 D  441  GLN VAL PRO MET ALA THR THR GLU GLY CYS LEU VAL ALA          
SEQRES  11 D  441  SER THR ASN ARG GLY CYS ARG ALA ILE GLY LEU GLY GLY          
SEQRES  12 D  441  GLY ALA SER SER ARG VAL LEU ALA ASP GLY MET THR ARG          
SEQRES  13 D  441  GLY PRO VAL VAL ARG LEU PRO ARG ALA CYS ASP SER ALA          
SEQRES  14 D  441  GLU VAL LYS ALA TRP LEU GLU THR SER GLU GLY PHE ALA          
SEQRES  15 D  441  VAL ILE LYS GLU ALA PHE ASP SER THR SER ARG PHE ALA          
SEQRES  16 D  441  ARG LEU GLN LYS LEU HIS THR SER ILE ALA GLY ARG ASN          
SEQRES  17 D  441  LEU TYR ILE ARG PHE GLN SER ARG SER GLY ASP ALA MET          
SEQRES  18 D  441  GLY MET ASN MET ILE SER LYS GLY THR GLU LYS ALA LEU          
SEQRES  19 D  441  SER LYS LEU HIS GLU TYR PHE PRO GLU MET GLN ILE LEU          
SEQRES  20 D  441  ALA VAL SER GLY ASN TYR CYS THR ASP LYS LYS PRO ALA          
SEQRES  21 D  441  ALA ILE ASN TRP ILE GLU GLY ARG GLY LYS SER VAL VAL          
SEQRES  22 D  441  CYS GLU ALA VAL ILE PRO ALA LYS VAL VAL ARG GLU VAL          
SEQRES  23 D  441  LEU LYS THR THR THR GLU ALA MET ILE GLU VAL ASN ILE          
SEQRES  24 D  441  ASN LYS ASN LEU VAL GLY SER ALA MET ALA GLY SER ILE          
SEQRES  25 D  441  GLY GLY TYR ASN ALA HIS ALA ALA ASN ILE VAL THR ALA          
SEQRES  26 D  441  ILE TYR ILE ALA CYS GLY GLN ASP ALA ALA GLN ASN VAL          
SEQRES  27 D  441  GLY SER SER ASN CYS ILE THR LEU MET GLU ALA SER GLY          
SEQRES  28 D  441  PRO THR ASN GLU ASP LEU TYR ILE SER CYS THR MET PRO          
SEQRES  29 D  441  SER ILE GLU ILE GLY THR VAL GLY GLY GLY THR ASN LEU          
SEQRES  30 D  441  LEU PRO GLN GLN ALA CYS LEU GLN MET LEU GLY VAL GLN          
SEQRES  31 D  441  GLY ALA CYS LYS ASP ASN PRO GLY GLU ASN ALA ARG GLN          
SEQRES  32 D  441  LEU ALA ARG ILE VAL CYS GLY THR VAL MET ALA GLY GLU          
SEQRES  33 D  441  LEU SER LEU MET ALA ALA LEU ALA ALA GLY HIS LEU VAL          
SEQRES  34 D  441  LYS SER HIS MET ILE HIS ASN ARG SER LYS ILE ASN              
HET    RID  A   2      41                                                       
HET    RID  B   1      41                                                       
HET    RID  C   4      41                                                       
HET    RID  D   3      41                                                       
HETNAM     RID (3R,5R)-7-[2-(4-FLUOROPHENYL)-5-(1-METHYLETHYL)-4-               
HETNAM   2 RID  (MORPHOLIN-4-YLSULFONYL)-3-PHENYL-1H-PYRROL-1-YL]-3,5-          
HETNAM   3 RID  DIHYDROXYHEPTANOIC ACID                                         
FORMUL   5  RID    4(C30 H37 F N2 O7 S)                                         
FORMUL   9  HOH   *679(H2 O)                                                    
HELIX    1   1 PRO A  444  ASN A  454  1                                  11    
HELIX    2   2 LYS A  457  LEU A  462  5                                   6    
HELIX    3   3 SER A  463  ASN A  472  1                                  10    
HELIX    4   4 LYS A  480  ILE A  485  1                                   6    
HELIX    5   5 THR A  487  LYS A  502  1                                  16    
HELIX    6   6 ASN A  518  VAL A  522  5                                   5    
HELIX    7   7 CYS A  561  LEU A  575  1                                  15    
HELIX    8   8 ARG A  598  THR A  611  1                                  14    
HELIX    9   9 THR A  611  SER A  624  1                                  14    
HELIX   10  10 GLY A  656  PHE A  675  1                                  20    
HELIX   11  11 ALA A  694  GLY A  701  1                                   8    
HELIX   12  12 PRO A  713  VAL A  720  1                                   8    
HELIX   13  13 THR A  724  LYS A  735  1                                  12    
HELIX   14  14 LEU A  737  ALA A  743  1                                   7    
HELIX   15  15 HIS A  752  CYS A  764  1                                  13    
HELIX   16  16 ASP A  767  ALA A  769  5                                   3    
HELIX   17  17 GLN A  770  SER A  775  1                                   6    
HELIX   18  18 GLY A  806  ASN A  810  5                                   5    
HELIX   19  19 LEU A  811  GLY A  822  1                                  12    
HELIX   20  20 GLY A  832  GLY A  860  1                                  29    
HELIX   21  21 PRO B  444  GLY B  453  1                                  10    
HELIX   22  22 GLY B  458  LEU B  462  5                                   5    
HELIX   23  23 SER B  463  ALA B  473  1                                  11    
HELIX   24  24 PRO B  477  TYR B  479  5                                   3    
HELIX   25  25 LYS B  480  ILE B  485  1                                   6    
HELIX   26  26 THR B  487  LYS B  501  1                                  15    
HELIX   27  27 CYS B  561  GLY B  576  1                                  16    
HELIX   28  28 ARG B  598  THR B  611  1                                  14    
HELIX   29  29 THR B  611  SER B  624  1                                  14    
HELIX   30  30 GLY B  656  PHE B  675  1                                  20    
HELIX   31  31 ALA B  694  GLY B  701  1                                   8    
HELIX   32  32 PRO B  713  VAL B  720  1                                   8    
HELIX   33  33 THR B  724  LYS B  735  1                                  12    
HELIX   34  34 LEU B  737  ALA B  743  1                                   7    
HELIX   35  35 HIS B  752  CYS B  764  1                                  13    
HELIX   36  36 ASP B  767  ALA B  769  5                                   3    
HELIX   37  37 GLN B  770  SER B  775  1                                   6    
HELIX   38  38 GLY B  806  ASN B  810  5                                   5    
HELIX   39  39 LEU B  811  LEU B  821  1                                  11    
HELIX   40  40 GLY B  832  GLY B  860  1                                  29    
HELIX   41  41 ASN C  445  ASN C  454  1                                  10    
HELIX   42  42 GLY C  458  LEU C  462  5                                   5    
HELIX   43  43 SER C  463  ILE C  468  1                                   6    
HELIX   44  44 LYS C  480  ILE C  485  1                                   6    
HELIX   45  45 THR C  487  LEU C  503  1                                  17    
HELIX   46  46 GLU C  505  LEU C  512  5                                   8    
HELIX   47  47 CYS C  561  GLY C  576  1                                  16    
HELIX   48  48 ARG C  598  GLU C  610  1                                  13    
HELIX   49  49 THR C  611  SER C  624  1                                  14    
HELIX   50  50 GLY C  656  PHE C  675  1                                  20    
HELIX   51  51 ALA C  694  GLY C  701  1                                   8    
HELIX   52  52 PRO C  713  VAL C  720  1                                   8    
HELIX   53  53 THR C  724  LYS C  735  1                                  12    
HELIX   54  54 LEU C  737  ALA C  743  1                                   7    
HELIX   55  55 HIS C  752  CYS C  764  1                                  13    
HELIX   56  56 ASP C  767  ALA C  769  5                                   3    
HELIX   57  57 GLN C  770  SER C  775  1                                   6    
HELIX   58  58 GLY C  806  ASN C  810  5                                   5    
HELIX   59  59 LEU C  811  LEU C  821  1                                  11    
HELIX   60  60 GLY C  832  GLY C  860  1                                  29    
HELIX   61  61 PRO D  444  LEU D  449  1                                   6    
HELIX   62  62 GLY D  458  LEU D  462  5                                   5    
HELIX   63  63 SER D  463  ALA D  473  1                                  11    
HELIX   64  64 PRO D  477  TYR D  479  5                                   3    
HELIX   65  65 LYS D  480  ILE D  485  1                                   6    
HELIX   66  66 THR D  487  LYS D  501  1                                  15    
HELIX   67  67 SER D  507  LEU D  512  5                                   6    
HELIX   68  68 CYS D  561  GLY D  576  1                                  16    
HELIX   69  69 ARG D  598  THR D  611  1                                  14    
HELIX   70  70 THR D  611  SER D  624  1                                  14    
HELIX   71  71 GLY D  656  PHE D  675  1                                  20    
HELIX   72  72 ALA D  694  GLY D  701  1                                   8    
HELIX   73  73 PRO D  713  VAL D  720  1                                   8    
HELIX   74  74 THR D  724  LEU D  737  1                                  14    
HELIX   75  75 LEU D  737  ALA D  743  1                                   7    
HELIX   76  76 HIS D  752  CYS D  764  1                                  13    
HELIX   77  77 ASP D  767  ALA D  769  5                                   3    
HELIX   78  78 GLN D  770  SER D  775  1                                   6    
HELIX   79  79 GLY D  806  ASN D  810  5                                   5    
HELIX   80  80 LEU D  811  LEU D  821  1                                  11    
HELIX   81  81 GLY D  832  ALA D  859  1                                  28    
SHEET    1   A 4 LYS A 549  ALA A 556  0                                        
SHEET    2   A 4 VAL A 530  LEU A 546 -1  N  LEU A 544   O  PHE A 551           
SHEET    3   A 4 VAL B 530  LEU B 546 -1  O  ILE B 531   N  VAL A 538           
SHEET    4   A 4 LYS B 549  ALA B 556 -1  O  PHE B 551   N  LEU B 544           
SHEET    1   B 4 HIS A 635  ALA A 639  0                                        
SHEET    2   B 4 ASN A 642  SER A 649 -1  O  ARG A 646   N  HIS A 635           
SHEET    3   B 4 VAL A 593  ARG A 595 -1  N  VAL A 594   O  LEU A 643           
SHEET    4   B 4 GLN A 679  ALA A 682 -1  O  GLN A 679   N  ARG A 595           
SHEET    1   C 7 HIS A 635  ALA A 639  0                                        
SHEET    2   C 7 ASN A 642  SER A 649 -1  O  ARG A 646   N  HIS A 635           
SHEET    3   C 7 ALA A 579  ARG A 590 -1  N  ARG A 590   O  PHE A 647           
SHEET    4   C 7 GLY A 703  ILE A 712 -1  O  SER A 705   N  LEU A 584           
SHEET    5   C 7 ASP A 790  ILE A 800 -1  O  MET A 797   N  VAL A 706           
SHEET    6   C 7 CYS A 777  SER A 784 -1  N  LEU A 780   O  SER A 794           
SHEET    7   C 7 GLY A 748  TYR A 749  1  N  TYR A 749   O  THR A 779           
SHEET    1   D 4 ARG B 630  LEU B 631  0                                        
SHEET    2   D 4 ASN B 642  ARG B 650 -1  O  ARG B 650   N  ARG B 630           
SHEET    3   D 4 VAL B 593  ARG B 595 -1  N  VAL B 594   O  LEU B 643           
SHEET    4   D 4 GLN B 679  ALA B 682 -1  O  GLN B 679   N  ARG B 595           
SHEET    1   E 7 HIS B 635  ALA B 639  0                                        
SHEET    2   E 7 ASN B 642  ARG B 650 -1  O  ARG B 646   N  HIS B 635           
SHEET    3   E 7 SER B 580  ARG B 590 -1  N  ARG B 590   O  PHE B 647           
SHEET    4   E 7 GLY B 703  ILE B 712 -1  O  VAL B 707   N  ARG B 582           
SHEET    5   E 7 ASP B 790  ILE B 800 -1  O  ILE B 800   N  LYS B 704           
SHEET    6   E 7 CYS B 777  SER B 784 -1  N  GLU B 782   O  TYR B 792           
SHEET    7   E 7 GLY B 748  TYR B 749  1  N  TYR B 749   O  THR B 779           
SHEET    1   F 4 LYS C 549  ALA C 556  0                                        
SHEET    2   F 4 VAL C 530  LEU C 546 -1  N  ALA C 541   O  VAL C 553           
SHEET    3   F 4 VAL D 530  LEU D 546 -1  O  VAL D 538   N  ILE C 531           
SHEET    4   F 4 LYS D 549  ALA D 556 -1  O  PHE D 551   N  LEU D 544           
SHEET    1   G 4 ARG C 630  LEU C 631  0                                        
SHEET    2   G 4 ASN C 642  ARG C 650 -1  O  ARG C 650   N  ARG C 630           
SHEET    3   G 4 VAL C 593  ARG C 595 -1  N  VAL C 594   O  LEU C 643           
SHEET    4   G 4 GLN C 679  ALA C 682 -1  O  GLN C 679   N  ARG C 595           
SHEET    1   H 7 HIS C 635  ALA C 639  0                                        
SHEET    2   H 7 ASN C 642  ARG C 650 -1  O  TYR C 644   N  SER C 637           
SHEET    3   H 7 SER C 580  ARG C 590 -1  N  ARG C 590   O  PHE C 647           
SHEET    4   H 7 GLY C 703  ILE C 712 -1  O  SER C 705   N  ALA C 585           
SHEET    5   H 7 ASP C 790  ILE C 800 -1  O  ILE C 800   N  LYS C 704           
SHEET    6   H 7 CYS C 777  SER C 784 -1  N  LEU C 780   O  SER C 794           
SHEET    7   H 7 GLY C 748  TYR C 749  1  N  TYR C 749   O  THR C 779           
SHEET    1   I 4 ARG D 630  LEU D 631  0                                        
SHEET    2   I 4 ASN D 642  ARG D 650 -1  O  ARG D 650   N  ARG D 630           
SHEET    3   I 4 VAL D 593  ARG D 595 -1  N  VAL D 594   O  LEU D 643           
SHEET    4   I 4 GLN D 679  ALA D 682 -1  O  GLN D 679   N  ARG D 595           
SHEET    1   J 7 HIS D 635  ALA D 639  0                                        
SHEET    2   J 7 ASN D 642  ARG D 650 -1  O  TYR D 644   N  SER D 637           
SHEET    3   J 7 SER D 580  ARG D 590 -1  N  ARG D 590   O  PHE D 647           
SHEET    4   J 7 GLY D 703  ILE D 712 -1  O  SER D 705   N  LEU D 584           
SHEET    5   J 7 ASP D 790  ILE D 800 -1  O  MET D 797   N  VAL D 706           
SHEET    6   J 7 CYS D 777  SER D 784 -1  N  LEU D 780   O  SER D 794           
SHEET    7   J 7 GLY D 748  TYR D 749  1  N  TYR D 749   O  THR D 779           
CISPEP   1 GLY A  542    PRO A  543          0         2.10                     
CISPEP   2 CYS A  688    THR A  689          0        -5.76                     
CISPEP   3 GLY B  542    PRO B  543          0        -0.62                     
CISPEP   4 CYS B  688    THR B  689          0         3.21                     
CISPEP   5 GLY C  542    PRO C  543          0        -1.63                     
CISPEP   6 CYS C  688    THR C  689          0        -6.83                     
CISPEP   7 GLY D  542    PRO D  543          0         0.11                     
CISPEP   8 CYS D  688    THR D  689          0        -6.08                     
SITE     1 AC1 19 ARG A 590  SER A 661  VAL A 683  SER A 684                    
SITE     2 AC1 19 ASN A 686  ASP A 690  LYS A 691  LYS A 692                    
SITE     3 AC1 19 HOH A 878  GLU B 559  GLY B 560  CYS B 561                    
SITE     4 AC1 19 SER B 565  LYS B 735  ALA B 751  ASN B 755                    
SITE     5 AC1 19 ALA B 856  LEU B 857  HOH B1034                               
SITE     1 AC2 20 GLU A 559  GLY A 560  CYS A 561  LEU A 562                    
SITE     2 AC2 20 SER A 565  LYS A 735  ALA A 751  ASN A 755                    
SITE     3 AC2 20 LEU A 853  ALA A 856  ARG B 590  SER B 661                    
SITE     4 AC2 20 VAL B 683  SER B 684  ASN B 686  ASP B 690                    
SITE     5 AC2 20 LYS B 691  LYS B 692  HOH B 904  HOH B1035                    
SITE     1 AC3 17 ARG C 590  SER C 661  VAL C 683  SER C 684                    
SITE     2 AC3 17 ASP C 690  LYS C 691  LYS C 692  HOH C 880                    
SITE     3 AC3 17 GLU D 559  GLY D 560  CYS D 561  LEU D 562                    
SITE     4 AC3 17 SER D 565  LYS D 735  ALA D 751  ASN D 755                    
SITE     5 AC3 17 ALA D 856                                                     
SITE     1 AC4 20 GLU C 559  GLY C 560  CYS C 561  LEU C 562                    
SITE     2 AC4 20 SER C 565  LYS C 735  ALA C 751  ASN C 755                    
SITE     3 AC4 20 LEU C 853  ALA C 856  ARG D 590  MET D 657                    
SITE     4 AC4 20 SER D 661  VAL D 683  SER D 684  ASP D 690                    
SITE     5 AC4 20 LYS D 691  LYS D 692  HOH D 963  HOH D1114                    
CRYST1   71.588  172.156   75.148  90.00 117.24  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      0.013969  0.000000  0.007191        0.00000                         
SCALE2      0.000000  0.005809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014967        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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