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Database: PDB
Entry: 3CCT
LinkDB: 3CCT
Original site: 3CCT 
HEADER    OXIDOREDUCTASE                          26-FEB-08   3CCT              
TITLE     THERMODYNAMIC AND STRUCTURE GUIDED DESIGN OF STATIN HMG-COA REDUCTASE 
TITLE    2 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 GENE: HMGCR;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 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    A.PAVLOVSKY,R.W.SARVER,M.S.HARRIS,B.C.FINZEL                          
REVDAT   4   25-OCT-17 3CCT    1       REMARK                                   
REVDAT   3   24-FEB-09 3CCT    1       VERSN                                    
REVDAT   2   12-AUG-08 3CCT    1       JRNL                                     
REVDAT   1   17-JUN-08 3CCT    0                                                
JRNL        AUTH   R.W.SARVER,E.BILLS,G.BOLTON,L.D.BRATTON,N.L.CASPERS,         
JRNL        AUTH 2 J.B.DUNBAR,M.S.HARRIS,R.H.HUTCHINGS,R.M.KENNEDY,S.D.LARSEN,  
JRNL        AUTH 3 A.PAVLOVSKY,J.A.PFEFFERKORN,G.BAINBRIDGE                     
JRNL        TITL   THERMODYNAMIC AND STRUCTURE GUIDED DESIGN OF STATIN BASED    
JRNL        TITL 2 INHIBITORS OF 3-HYDROXY-3-METHYLGLUTARYL COENZYME A          
JRNL        TITL 3 REDUCTASE.                                                   
JRNL        REF    J.MED.CHEM.                   V.  51  3804 2008              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   18540668                                                     
JRNL        DOI    10.1021/JM7015057                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 84267                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8471                            
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) : 2.12                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3935                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2770                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 447                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12282                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 168                                     
REMARK   3   SOLVENT ATOMS            : 395                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.36000                                              
REMARK   3    B22 (A**2) : -0.54000                                             
REMARK   3    B33 (A**2) : -0.26000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.57000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.325         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.222         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.056         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12642 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A): 11703 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17095 ; 1.251 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 27258 ; 0.771 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1648 ; 5.391 ; 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):  1957 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 14137 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2357 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2762 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A): 13966 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  7501 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   469 ; 0.147 ; 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):    16 ; 0.120 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    61 ; 0.191 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.190 ; 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):  8174 ; 0.570 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13065 ; 1.097 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4468 ; 1.527 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4030 ; 2.697 ; 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 3CCT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86863                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 45.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24800                            
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   (%): 45.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 15-20 MG/ML, LIGAND              
REMARK 280  (SATURATED),PEG 4000, MGCL2 0.2M, TRIS-HCL PH8 0.1M, 7-10 DAYS,     
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
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       86.75500            
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: 25100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -171.8 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     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     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     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     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     LEU D   481                                                      
REMARK 465     GLU D   482                                                      
REMARK 465     THR D   483                                                      
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   OD1  ASN C   771     OG   SER C   775              2.03            
REMARK 500   OE2  GLU A   700     OE2  GLU D   700              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 547   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 623   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 464   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C 547   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
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      -78.61   -114.03                                   
REMARK 500    LYS A 474      176.39     56.64                                   
REMARK 500    HIS A 475      -43.63    120.74                                   
REMARK 500    ALA A 478      -38.11    150.10                                   
REMARK 500    LEU A 484      -37.30    169.05                                   
REMARK 500    TYR A 514      -18.42   -161.31                                   
REMARK 500    ALA A 525      -52.28   -126.24                                   
REMARK 500    CYS A 561      -12.29     80.60                                   
REMARK 500    ALA A 629       99.20    -68.13                                   
REMARK 500    SER A 651       37.74   -158.97                                   
REMARK 500    LYS A 735      -62.66    -95.04                                   
REMARK 500    LEU A 737      -66.72   -103.23                                   
REMARK 500    TYR A 749       55.42    -90.17                                   
REMARK 500    HIS A 752       43.97   -159.99                                   
REMARK 500    ASN A 830       75.54   -156.15                                   
REMARK 500    LYS B 457      -94.61   -114.09                                   
REMARK 500    TYR B 514      -28.96   -144.52                                   
REMARK 500    ALA B 525      -46.70   -158.98                                   
REMARK 500    CYS B 561       -9.26     73.88                                   
REMARK 500    ARG B 630       81.00   -150.14                                   
REMARK 500    SER B 651       37.16   -147.26                                   
REMARK 500    LYS B 735      -62.75    -97.12                                   
REMARK 500    LEU B 737      -67.02   -101.75                                   
REMARK 500    HIS B 752       41.96   -152.31                                   
REMARK 500    SER B 799       52.63   -143.51                                   
REMARK 500    LYS C 457      -77.65    -74.84                                   
REMARK 500    TYR C 514      -15.40   -145.67                                   
REMARK 500    ALA C 525      -44.75   -149.52                                   
REMARK 500    CYS C 561       -4.61     81.87                                   
REMARK 500    ALA C 629       97.81    -67.60                                   
REMARK 500    SER C 651       39.78   -154.21                                   
REMARK 500    LYS C 735      -62.02   -104.30                                   
REMARK 500    LEU C 737      -69.80   -101.66                                   
REMARK 500    TYR C 749       53.74    -95.95                                   
REMARK 500    HIS C 752       41.95   -156.73                                   
REMARK 500    ASN C 830       84.72   -151.05                                   
REMARK 500    TYR D 514      -20.39   -161.38                                   
REMARK 500    ALA D 525      -47.30   -154.90                                   
REMARK 500    CYS D 561      -11.71     75.57                                   
REMARK 500    SER D 651       38.28   -152.80                                   
REMARK 500    ALA D 710      145.25   -170.07                                   
REMARK 500    LYS D 735      -64.78   -100.18                                   
REMARK 500    LEU D 737      -67.53   -106.69                                   
REMARK 500    TYR D 749       58.07    -96.18                                   
REMARK 500    HIS D 752       42.11   -159.45                                   
REMARK 500    SER D 799       52.43   -145.31                                   
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 3HI B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3HI B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3HI D 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3HI C 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CCW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CCZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CD0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CD5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CD7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CDA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3CDB   RELATED DB: PDB                                   
DBREF  3CCT A  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3CCT B  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3CCT C  441   875  UNP    P04035   HMDH_HUMAN     441    875             
DBREF  3CCT D  441   875  UNP    P04035   HMDH_HUMAN     441    875             
SEQADV 3CCT HIS A  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS A  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS A  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS A  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS A  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS A  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT ILE A  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3CCT HIS B  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS B  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS B  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS B  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS B  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS B  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT ILE B  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3CCT HIS C  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS C  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS C  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS C  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS C  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS C  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT ILE C  485  UNP  P04035    MET   485 ENGINEERED                     
SEQADV 3CCT HIS D  435  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS D  436  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS D  437  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS D  438  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS D  439  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT HIS D  440  UNP  P04035              EXPRESSION TAG                 
SEQADV 3CCT 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    3HI  B   1      42                                                       
HET    3HI  B   2      42                                                       
HET    3HI  C   4      42                                                       
HET    3HI  D   3      42                                                       
HETNAM     3HI (3R,5R)-7-[2-(4-FLUOROPHENYL)-4-[(2-HYDROXYPHENYL)               
HETNAM   2 3HI  CARBAMOYL]-5-(1-METHYLETHYL)-3-PHENYL-1H-PYRROL-1-YL]-          
HETNAM   3 3HI  3,5-DIHYDROXYHEPTANOIC ACID                                     
FORMUL   5  3HI    4(C33 H35 F N2 O6)                                           
FORMUL   9  HOH   *395(H2 O)                                                    
HELIX    1   1 PRO A  444  ASN A  454  1                                  11    
HELIX    2   2 GLY A  458  LEU A  462  5                                   5    
HELIX    3   3 SER A  463  ASN A  472  1                                  10    
HELIX    4   4 THR A  487  LEU A  503  1                                  17    
HELIX    5   5 SER A  507  LEU A  512  5                                   6    
HELIX    6   6 ASN A  518  VAL A  522  5                                   5    
HELIX    7   7 CYS A  561  GLY A  576  1                                  16    
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  LEU A  737  1                                  14    
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  LEU A  821  1                                  11    
HELIX   20  20 GLY A  832  GLY A  860  1                                  29    
HELIX   21  21 PRO B  444  ASN B  454  1                                  11    
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 LYS B  480  ILE B  485  1                                   6    
HELIX   25  25 THR B  487  LEU B  503  1                                  17    
HELIX   26  26 ASN B  518  VAL B  522  5                                   5    
HELIX   27  27 CYS B  561  GLY B  576  1                                  16    
HELIX   28  28 ARG B  598  GLU B  610  1                                  13    
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  LEU B  737  1                                  14    
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  GLY B  822  1                                  12    
HELIX   40  40 GLY B  832  GLY B  860  1                                  29    
HELIX   41  41 PRO C  444  ASN C  454  1                                  11    
HELIX   42  42 GLY C  458  LEU C  462  5                                   5    
HELIX   43  43 SER C  463  ALA C  473  1                                  11    
HELIX   44  44 PRO C  477  TYR C  479  5                                   3    
HELIX   45  45 LYS C  480  ILE C  485  1                                   6    
HELIX   46  46 THR C  487  LYS C  501  1                                  15    
HELIX   47  47 SER C  507  LEU C  512  5                                   6    
HELIX   48  48 CYS C  561  LEU C  575  1                                  15    
HELIX   49  49 ARG C  598  THR C  611  1                                  14    
HELIX   50  50 THR C  611  SER C  624  1                                  14    
HELIX   51  51 GLY C  656  PHE C  675  1                                  20    
HELIX   52  52 ALA C  694  GLY C  701  1                                   8    
HELIX   53  53 PRO C  713  VAL C  720  1                                   8    
HELIX   54  54 THR C  724  LEU C  737  1                                  14    
HELIX   55  55 LEU C  737  ALA C  743  1                                   7    
HELIX   56  56 HIS C  752  CYS C  764  1                                  13    
HELIX   57  57 ASP C  767  ALA C  769  5                                   3    
HELIX   58  58 GLN C  770  SER C  775  1                                   6    
HELIX   59  59 GLY C  806  ASN C  810  5                                   5    
HELIX   60  60 LEU C  811  GLY C  822  1                                  12    
HELIX   61  61 GLY C  832  GLY C  860  1                                  29    
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 THR D  487  LYS D  501  1                                  15    
HELIX   65  65 GLU D  505  LEU D  512  5                                   8    
HELIX   66  66 CYS D  561  GLY D  576  1                                  16    
HELIX   67  67 ARG D  598  THR D  611  1                                  14    
HELIX   68  68 THR D  611  SER D  624  1                                  14    
HELIX   69  69 GLY D  656  PHE D  675  1                                  20    
HELIX   70  70 ALA D  694  GLY D  701  1                                   8    
HELIX   71  71 PRO D  713  VAL D  720  1                                   8    
HELIX   72  72 THR D  724  LEU D  737  1                                  14    
HELIX   73  73 LEU D  737  ALA D  743  1                                   7    
HELIX   74  74 HIS D  752  CYS D  764  1                                  13    
HELIX   75  75 ASP D  767  ALA D  769  5                                   3    
HELIX   76  76 GLN D  770  SER D  775  1                                   6    
HELIX   77  77 GLY D  806  ASN D  810  5                                   5    
HELIX   78  78 LEU D  811  LEU D  821  1                                  11    
HELIX   79  79 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  GLY A 539   O  MET A 555           
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  MET B 555   N  GLY B 539           
SHEET    1   B 4 HIS A 635  ALA A 639  0                                        
SHEET    2   B 4 ASN A 642  SER A 649 -1  O  TYR A 644   N  SER A 637           
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  TYR A 644   N  SER A 637           
SHEET    3   C 7 SER A 580  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  LEU A 791   N  ILE A 712           
SHEET    6   C 7 CYS A 777  SER A 784 -1  N  GLU A 782   O  TYR A 792           
SHEET    7   C 7 GLY A 748  TYR A 749  1  N  TYR A 749   O  THR A 779           
SHEET    1   D 4 HIS B 635  ALA B 639  0                                        
SHEET    2   D 4 ASN B 642  SER B 649 -1  O  TYR B 644   N  SER B 637           
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  SER B 649 -1  O  TYR B 644   N  SER B 637           
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  SER B 705   N  LEU B 584           
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  LEU B 780   O  SER B 794           
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  ILE D 531   N  VAL C 538           
SHEET    4   F 4 LYS D 549  ALA D 556 -1  O  VAL D 553   N  ALA D 541           
SHEET    1   G 4 HIS C 635  ALA C 639  0                                        
SHEET    2   G 4 ASN C 642  SER C 649 -1  O  ARG C 646   N  HIS C 635           
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  SER C 649 -1  O  ARG C 646   N  HIS C 635           
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  GLU C 709   N  SER C 580           
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  ILE D 793   N  ALA D 710           
SHEET    6   J 7 CYS D 777  SER D 784 -1  N  GLU D 782   O  TYR D 792           
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         5.24                     
CISPEP   2 CYS A  688    THR A  689          0       -12.91                     
CISPEP   3 GLY B  542    PRO B  543          0         1.73                     
CISPEP   4 CYS B  688    THR B  689          0        -2.88                     
CISPEP   5 GLY C  542    PRO C  543          0         3.50                     
CISPEP   6 CYS C  688    THR C  689          0        -9.41                     
CISPEP   7 GLY D  542    PRO D  543          0        -0.53                     
CISPEP   8 CYS D  688    THR D  689          0       -12.18                     
SITE     1 AC1 20 GLU A 559  GLY A 560  LEU A 562  SER A 565                    
SITE     2 AC1 20 ARG A 568  LYS A 735  ALA A 751  HIS A 752                    
SITE     3 AC1 20 ASN A 755  LEU A 853  ALA A 856  LEU A 857                    
SITE     4 AC1 20 ARG B 590  MET B 657  SER B 661  SER B 684                    
SITE     5 AC1 20 ASP B 690  LYS B 691  LYS B 692  HOH B 905                    
SITE     1 AC2 19 ARG A 590  MET A 657  SER A 661  SER A 684                    
SITE     2 AC2 19 ASP A 690  LYS A 691  LYS A 692  GLU B 559                    
SITE     3 AC2 19 CYS B 561  LEU B 562  SER B 565  ARG B 568                    
SITE     4 AC2 19 LYS B 735  ALA B 751  HIS B 752  ASN B 755                    
SITE     5 AC2 19 LEU B 853  ALA B 856  HOH B 879                               
SITE     1 AC3 19 GLU C 559  GLY C 560  CYS C 561  SER C 565                    
SITE     2 AC3 19 ARG C 568  LYS C 735  ALA C 751  HIS C 752                    
SITE     3 AC3 19 ASN C 755  LEU C 853  ALA C 856  HOH D  45                    
SITE     4 AC3 19 ARG D 590  SER D 661  SER D 684  ASN D 686                    
SITE     5 AC3 19 ASP D 690  LYS D 691  LYS D 692                               
SITE     1 AC4 20 HOH C  25  ARG C 590  SER C 661  SER C 684                    
SITE     2 AC4 20 ASN C 686  ASP C 690  LYS C 691  LYS C 692                    
SITE     3 AC4 20 GLU D 559  GLY D 560  CYS D 561  LEU D 562                    
SITE     4 AC4 20 SER D 565  ARG D 568  LYS D 735  ALA D 751                    
SITE     5 AC4 20 HIS D 752  ASN D 755  LEU D 853  ALA D 856                    
CRYST1   73.940  173.510   76.400  90.00 119.18  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      0.013524  0.000000  0.007552        0.00000                         
SCALE2      0.000000  0.005763  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014992        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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