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Database: PDB
Entry: 4IPF
LinkDB: 4IPF
Original site: 4IPF 
HEADER    LIGASE/ANTAGONIST                       09-JAN-13   4IPF              
TITLE     THE 1.7A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH RO5045337   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 21-105;                                       
COMPND   5 SYNONYM: DOUBLE MINUTE 2 PROTEIN, XDM2, P53-BINDING PROTEIN MDM2;    
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;                                 
SOURCE   3 ORGANISM_COMMON: CLAWED FROG,COMMON PLATANNA,PLATANNA;               
SOURCE   4 ORGANISM_TAXID: 8355;                                                
SOURCE   5 GENE: MDM2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PUBS 520                                  
KEYWDS    MDM2, P53, PROTEIN-PROTEIN INTERACTION, IMIDAZOLINE, E3 UBIQUITIN     
KEYWDS   2 LIGASE, NUCLEUS, LIGASE-ANTAGONIST COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.GRAVES,C.LUKACS,R.U.KAMMLOTT,R.CROWTHER                           
REVDAT   2   24-APR-13 4IPF    1       JRNL                                     
REVDAT   1   20-FEB-13 4IPF    0                                                
JRNL        AUTH   C.TOVAR,B.GRAVES,K.PACKMAN,Z.FILIPOVIC,B.H.XIA,C.TARDELL,    
JRNL        AUTH 2 R.GARRIDO,E.LEE,K.KOLINSKY,K.H.TO,M.LINN,F.PODLASKI,         
JRNL        AUTH 3 P.WOVKULICH,B.VU,L.T.VASSILEV                                
JRNL        TITL   MDM2 SMALL-MOLECULE ANTAGONIST RG7112 ACTIVATES P53          
JRNL        TITL 2 SIGNALING AND REGRESSES HUMAN TUMORS IN PRECLINICAL CANCER   
JRNL        TITL 3 MODELS.                                                      
JRNL        REF    CANCER RES.                   V.  73  2587 2013              
JRNL        REFN                   ISSN 0008-5472                               
JRNL        PMID   23400593                                                     
JRNL        DOI    10.1158/0008-5472.CAN-12-2807                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.T.VASSILEV,B.T.VU,B.GRAVES,D.CARVAJAL,F.PODLASKI,          
REMARK   1  AUTH 2 Z.FILIPOVIC,N.KONG,U.KAMMLOTT,C.LUKACS,C.KLEIN,N.FOTOUHI,    
REMARK   1  AUTH 3 E.A.LIU                                                      
REMARK   1  TITL   IN VIVO ACTIVATION OF THE P53 PATHWAY BY SMALL-MOLECULE      
REMARK   1  TITL 2 ANTAGONISTS OF MDM2                                          
REMARK   1  REF    SCIENCE                       V. 303   844 2004              
REMARK   1  REFN                   ISSN 0036-8075                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2005                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 850326.780                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 10703                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 548                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2130               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2120               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.231                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.100                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 548                  
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0100               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 10703                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1417                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 78                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.044                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 690                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 137                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.64000                                             
REMARK   3    B22 (A**2) : 2.63000                                              
REMARK   3    B33 (A**2) : -1.99000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.09                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.94                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.100 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.670 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.970 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.830 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 48.57                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARA                               
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : RO5045337.PRX                                  
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : RO5045337.TPX                                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IPF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077042.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JAN-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
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 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11957                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 82.6                               
REMARK 200  DATA REDUNDANCY                : 3.580                              
REMARK 200  R MERGE                    (I) : 0.03700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 20.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.99                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50% SATURATED AMMONIUM SULFATE, 100 MM   
REMARK 280  BIS-TRIS, PH 6.5, 5% (V/V) PEG200, 5 MM DTT, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 278.0K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       33.36200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       33.36200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       21.54150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       33.74650            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       21.54150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       33.74650            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       33.36200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       21.54150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       33.74650            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       33.36200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       21.54150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       33.74650            
REMARK 290   SMTRY3   8  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 300 REMARK: THE FULL-LENGTH PROTEIN WOULD FORM A DIMER THROUGH ITS C-    
REMARK 300 TERMINAL DOMAIN BUT THIS N-TERMINAL DOMAIN FORMS ONLY MONOMERS.      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 383  LIES ON A SPECIAL POSITION.                          
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1F0 A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1RV1   RELATED DB: PDB                                   
REMARK 900 EARLIER STRUCTURE WITH A RELATED CIS-IMIDAZOLINE COMPOUND            
DBREF  4IPF A   21   105  UNP    P56273   MDM2_XENLA      21    105             
SEQADV 4IPF LEU A   50  UNP  P56273    ILE    50 ENGINEERED MUTATION            
SEQADV 4IPF HIS A   92  UNP  P56273    PRO    92 ENGINEERED MUTATION            
SEQADV 4IPF ILE A   95  UNP  P56273    LEU    95 ENGINEERED MUTATION            
SEQRES   1 A   85  GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU          
SEQRES   2 A   85  LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET          
SEQRES   3 A   85  LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA          
SEQRES   4 A   85  LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS          
SEQRES   5 A   85  CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN          
SEQRES   6 A   85  GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET          
SEQRES   7 A   85  ILE SER ARG ASN LEU VAL SER                                  
HET    1F0  A 201      49                                                       
HET    SO4  A 202       5                                                       
HET    SO4  A 203       5                                                       
HETNAM     1F0 [(4S,5R)-2-(4-TERT-BUTYL-2-ETHOXYPHENYL)-4,5-BIS(4-              
HETNAM   2 1F0  CHLOROPHENYL)-4,5-DIMETHYL-4,5-DIHYDRO-1H-IMIDAZOL-1-           
HETNAM   3 1F0  YL]{4-[3-(METHYLSULFONYL)PROPYL]PIPERAZIN-1-                    
HETNAM   4 1F0  YL}METHANONE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETSYN     1F0 RO5045337, RG7112                                                
FORMUL   2  1F0    C38 H48 CL2 N4 O4 S                                          
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *137(H2 O)                                                    
HELIX    1   1 THR A   27  ALA A   37  1                                  11    
HELIX    2   2 THR A   45  LYS A   60  1                                  16    
HELIX    3   3 ASP A   76  PHE A   82  5                                   7    
HELIX    4   4 GLU A   91  ARG A  101  1                                  11    
SHEET    1   A 2 ILE A  70  HIS A  72  0                                        
SHEET    2   A 2 GLU A  86  SER A  88 -1  O  PHE A  87   N  VAL A  71           
SITE     1 AC1 17 LYS A  35  SER A  36  GLY A  38  LEU A  50                    
SITE     2 AC1 17 LEU A  53  GLY A  54  ILE A  57  MET A  58                    
SITE     3 AC1 17 GLN A  68  HIS A  69  GLN A  85  VAL A  89                    
SITE     4 AC1 17 HIS A  92  TYR A  96  HOH A 316  HOH A 341                    
SITE     5 AC1 17 HOH A 366                                                     
SITE     1 AC2  8 ASN A  75  GLU A  91  HIS A  92  ARG A  93                    
SITE     2 AC2  8 ARG A  94  HOH A 356  HOH A 379  HOH A 387                    
SITE     1 AC3  8 PHE A  82  GLY A  83  VAL A  84  ARG A  94                    
SITE     2 AC3  8 ARG A 101  HOH A 378  HOH A 416  HOH A 417                    
CRYST1   43.083   67.493   66.724  90.00  90.00  90.00 C 2 2 21      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      0.023211  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014987        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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