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Database: PDB
Entry: 4LWV
LinkDB: 4LWV
Original site: 4LWV 
HEADER    LIGASE/LIGASE INHIBITOR                 28-JUL-13   4LWV              
TITLE     THE 2.3A CRYSTAL STRUCTURE OF HUMANIZED XENOPUS MDM2 WITH RO5545353   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE MDM2;                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (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: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PUBS 520                                  
KEYWDS    MDM2, E3 UBIQUITIN LIGASE, P53, NUCLEUS, LIGASE-LIGASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.GRAVES,C.LUKACS,C.A.JANSON                                        
REVDAT   1   02-JUL-14 4LWV    0                                                
JRNL        AUTH   Z.ZHANG,X.J.CHU,J.J.LIU,Q.DING,J.ZHANG,D.BARTKOVITZ,N.JIANG, 
JRNL        AUTH 2 P.KARNACHI,S.S.SO,C.TOVAR,Z.M.FILIPOVIC,B.HIGGINS,K.GLENN,   
JRNL        AUTH 3 K.PACKMAN,L.VASSILEV,B.GRAVES                                
JRNL        TITL   DISCOVERY OF POTENT AND ORALLY ACTIVE P53-MDM2 INHIBITORS    
JRNL        TITL 2 RO5353 AND RO2468 FOR POTENTIAL CLINICAL DEVELOPMENT.        
JRNL        REF    ACS MED.CHEM.LETT.            V.   5   124 2014              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   24900784                                                     
JRNL        DOI    10.1021/ML400359Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.32 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) : 2.32                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1115147.730                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19022                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 541                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.012                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2330               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2300               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.284                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.000                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 541                  
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0120               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 10923                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.32                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1694                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 87                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.037                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2070                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.40                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.300                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.700                           
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) : 1.610 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.870 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.240 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 24.94                                                
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  : RO5545353.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   : RO5545353.TPX                                  
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4LWV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081186.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99990                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR                       
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.320                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.12200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.32                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: 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   (%): 65.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40-50% SATURATED AMMONIUM SULFATE,       
REMARK 280  0.1M MES, PH 6.5, 5% PEG200, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 278K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       44.37100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       66.04650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.37100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       66.04650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 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  66     -140.96     63.51                                   
REMARK 500    GLN A  67      -86.51     58.28                                   
REMARK 500    GLN A  68       25.19    143.12                                   
REMARK 500    HIS A  69       56.19     71.74                                   
REMARK 500    LYS B  66      -81.47     95.36                                   
REMARK 500    GLN B  68      -10.83   -158.32                                   
REMARK 500    CYS B  73       31.86   -158.28                                   
REMARK 500    VAL B 104      -72.35    -96.62                                   
REMARK 500    ALA C  59      -73.21    -55.78                                   
REMARK 500    LYS C  60      -19.78    -46.81                                   
REMARK 500    LYS C  66      -84.09    119.70                                   
REMARK 500    GLN C  67      -64.91    -24.22                                   
REMARK 500    GLN C  68       27.12    161.64                                   
REMARK 500    HIS C  69       61.29     72.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A   65     LYS A   66                 -148.40                    
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 20W 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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20W B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20W C 201                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LWT   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4LWU   RELATED DB: PDB                                   
DBREF  4LWV A   21   105  UNP    P56273   MDM2_XENLA      21    105             
DBREF  4LWV B   21   105  UNP    P56273   MDM2_XENLA      21    105             
DBREF  4LWV C   21   105  UNP    P56273   MDM2_XENLA      21    105             
SEQADV 4LWV LEU A   50  UNP  P56273    ILE    50 ENGINEERED MUTATION            
SEQADV 4LWV HIS A   92  UNP  P56273    PRO    92 ENGINEERED MUTATION            
SEQADV 4LWV ILE A   95  UNP  P56273    LEU    95 ENGINEERED MUTATION            
SEQADV 4LWV LEU B   50  UNP  P56273    ILE    50 ENGINEERED MUTATION            
SEQADV 4LWV HIS B   92  UNP  P56273    PRO    92 ENGINEERED MUTATION            
SEQADV 4LWV ILE B   95  UNP  P56273    LEU    95 ENGINEERED MUTATION            
SEQADV 4LWV LEU C   50  UNP  P56273    ILE    50 ENGINEERED MUTATION            
SEQADV 4LWV HIS C   92  UNP  P56273    PRO    92 ENGINEERED MUTATION            
SEQADV 4LWV ILE C   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                                  
SEQRES   1 B   85  GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU          
SEQRES   2 B   85  LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET          
SEQRES   3 B   85  LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA          
SEQRES   4 B   85  LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS          
SEQRES   5 B   85  CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN          
SEQRES   6 B   85  GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET          
SEQRES   7 B   85  ILE SER ARG ASN LEU VAL SER                                  
SEQRES   1 C   85  GLU LYS LEU VAL GLN PRO THR PRO LEU LEU LEU SER LEU          
SEQRES   2 C   85  LEU LYS SER ALA GLY ALA GLN LYS GLU THR PHE THR MET          
SEQRES   3 C   85  LYS GLU VAL LEU TYR HIS LEU GLY GLN TYR ILE MET ALA          
SEQRES   4 C   85  LYS GLN LEU TYR ASP GLU LYS GLN GLN HIS ILE VAL HIS          
SEQRES   5 C   85  CYS SER ASN ASP PRO LEU GLY GLU LEU PHE GLY VAL GLN          
SEQRES   6 C   85  GLU PHE SER VAL LYS GLU HIS ARG ARG ILE TYR ALA MET          
SEQRES   7 C   85  ILE SER ARG ASN LEU VAL SER                                  
HET    20W  A 201      41                                                       
HET    SO4  A 202       5                                                       
HET    SO4  A 203       5                                                       
HET    SO4  A 204       5                                                       
HET    20W  B 201      41                                                       
HET    20W  C 201      41                                                       
HETNAM     20W (2S,3R,4R,5R)-N-(4-CARBAMOYL-2-METHOXYPHENYL)-2'-                
HETNAM   2 20W  CHLORO-4-(3-CHLORO-2-FLUOROPHENYL)-2-(2,2-                      
HETNAM   3 20W  DIMETHYLPROPYL)-5'-OXO-4',5'-DIHYDROSPIRO[PYRROLIDINE-          
HETNAM   4 20W  3,6'-THIENO[3,2-B]PYRROLE]-5-CARBOXAMIDE                        
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  20W    3(C29 H29 CL2 F N4 O4 S)                                     
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL  10  HOH   *48(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  GLY A   83  1                                   8    
HELIX    4   4 GLU A   91  ARG A  101  1                                  11    
HELIX    5   5 THR B   27  ALA B   37  1                                  11    
HELIX    6   6 MET B   46  GLN B   61  1                                  16    
HELIX    7   7 ASP B   76  GLY B   83  1                                   8    
HELIX    8   8 GLU B   91  ARG B  101  1                                  11    
HELIX    9   9 THR C   27  ALA C   37  1                                  11    
HELIX   10  10 THR C   45  GLN C   61  1                                  17    
HELIX   11  11 ASP C   76  GLY C   83  1                                   8    
HELIX   12  12 GLU C   91  ARG C  101  1                                  11    
SHEET    1   A 2 GLN A  25  PRO A  26  0                                        
SHEET    2   A 2 LEU A 103  SER A 105 -1  O  VAL A 104   N  GLN A  25           
SHEET    1   B 3 TYR A  63  ASP A  64  0                                        
SHEET    2   B 3 ILE A  70  HIS A  72 -1  O  ILE A  70   N  ASP A  64           
SHEET    3   B 3 GLU A  86  SER A  88 -1  O  PHE A  87   N  VAL A  71           
SHEET    1   C 2 LEU B  23  VAL B  24  0                                        
SHEET    2   C 2 PHE B  44  THR B  45 -1  O  PHE B  44   N  VAL B  24           
SHEET    1   D 2 ILE B  70  HIS B  72  0                                        
SHEET    2   D 2 GLU B  86  SER B  88 -1  O  PHE B  87   N  VAL B  71           
SHEET    1   E 2 ILE C  70  HIS C  72  0                                        
SHEET    2   E 2 GLU C  86  SER C  88 -1  O  PHE C  87   N  VAL C  71           
SITE     1 AC1 12 LEU A  50  HIS A  69  PHE A  82  VAL A  89                    
SITE     2 AC1 12 LYS A  90  HIS A  92  ILE A  95  TYR A  96                    
SITE     3 AC1 12 HOH A 314  LYS C  90  20W C 201  HOH C 308                    
SITE     1 AC2  8 HIS A  92  TYR A  96  HOH A 306  HOH A 317                    
SITE     2 AC2  8 LYS C  90  GLU C  91  HIS C  92  ARG C  93                    
SITE     1 AC3  8 LYS A  90  GLU A  91  HIS A  92  ARG A  93                    
SITE     2 AC3  8 HOH A 307  HOH A 315  HIS C  92  TYR C  96                    
SITE     1 AC4  6 PRO A  28  LEU A  29  PRO B  28  LEU B  29                    
SITE     2 AC4  6 PRO C  28  LEU C  29                                          
SITE     1 AC5 10 LEU B  50  MET B  58  TYR B  63  GLU B  65                    
SITE     2 AC5 10 GLN B  68  VAL B  89  LYS B  90  HIS B  92                    
SITE     3 AC5 10 ILE B  95  TYR B  96                                          
SITE     1 AC6 10 20W A 201  HOH A 314  LEU C  50  MET C  58                    
SITE     2 AC6 10 HIS C  69  VAL C  89  LYS C  90  HIS C  92                    
SITE     3 AC6 10 TYR C  96  HOH C 311                                          
CRYST1   88.742  132.093   35.797  90.00  90.00  90.00 P 21 21 2    12          
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      0.011269  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007570  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027935        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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