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Database: PDB
Entry: 6OKO
LinkDB: 6OKO
Original site: 6OKO 
HEADER    TRANSFERASE                             14-APR-19   6OKO              
TITLE     CRYSTAL STRUCTURE OF MRIPK3 COMPLEXED WITH N-(3-FLUORO-4-{1H-         
TITLE    2 PYRROLO[2,3-B]PYRIDIN-4-YLOXY}PHENYL)-1-(4-FLUOROPHENYL)-2-OXO-1,2-  
TITLE    3 DIHYDROPYRIDINE-3-CARBOXAMIDE                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 3;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-313;                                        
COMPND   5 SYNONYM: RIP-LIKE PROTEIN KINASE 3, RECEPTOR-INTERACTING PROTEIN 3,  
COMPND   6 MRIP3;                                                               
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: RIPK3, RIP3;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, RIPK3, RIP3, TRANSFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.POKROSS                                                           
REVDAT   2   01-APR-20 6OKO    1       JRNL                                     
REVDAT   1   17-JUL-19 6OKO    0                                                
JRNL        AUTH   A.C.HART,L.ABELL,J.GUO,M.E.MERTZMAN,R.PADMANABHA,J.E.MACOR,  
JRNL        AUTH 2 C.CHAUDHRY,H.LU,K.O'MALLEY,P.J.SHAW,C.WEIGELT,M.POKROSS,     
JRNL        AUTH 3 K.KISH,K.S.KIM,L.CORNELIUS,A.E.DOUGLAS,D.CALAMBUR,P.ZHANG,   
JRNL        AUTH 4 B.CARPENTER,W.J.PITTS                                        
JRNL        TITL   IDENTIFICATION OF RIPK3 TYPE II INHIBITORS USING             
JRNL        TITL 2 HIGH-THROUGHPUT MECHANISTIC STUDIES IN HIT TRIAGE.           
JRNL        REF    ACS MED.CHEM.LETT.            V.  11   266 2020              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   32184955                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.9B00065                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34396                          
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)  : 0.181                          
REMARK   3   R VALUE            (WORKING SET)  : 0.180                          
REMARK   3   FREE R VALUE                      : 0.198                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.250                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1807                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.10                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.17                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.55                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2743                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2148                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2575                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2135                   
REMARK   3   BIN FREE R VALUE                        : 0.2359                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 6.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 168                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3987                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.98                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.87                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.82520                                              
REMARK   3    B22 (A**2) : -9.85670                                             
REMARK   3    B33 (A**2) : 6.03140                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.38300                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.317               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.186               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.145               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.188               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.147               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4197   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 5754   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1362   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 88     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 708    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4197   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 516    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4720   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.57                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.33                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    3.8685    6.8243  -25.0882           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1138 T22:   -0.1103                                    
REMARK   3     T33:   -0.1699 T12:    0.0072                                    
REMARK   3     T13:   -0.0179 T23:   -0.0177                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3744 L22:    0.8876                                    
REMARK   3     L33:    2.4637 L12:    0.6556                                    
REMARK   3     L13:    0.3084 L23:   -0.1341                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0563 S12:    0.0193 S13:   -0.0986                     
REMARK   3     S21:    0.0086 S22:   -0.1894 S23:   -0.0477                     
REMARK   3     S31:    0.0115 S32:   -0.1523 S33:    0.1332                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   31.4665    8.0065  -15.1864           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2803 T22:    0.0829                                    
REMARK   3     T33:   -0.1723 T12:   -0.0340                                    
REMARK   3     T13:   -0.0747 T23:    0.1092                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.7343 L22:    1.8344                                    
REMARK   3     L33:    2.3464 L12:    0.1993                                    
REMARK   3     L13:   -0.5094 L23:   -0.1423                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0550 S12:    0.0422 S13:   -0.0340                     
REMARK   3     S21:    0.1436 S22:   -0.0434 S23:   -0.4775                     
REMARK   3     S31:   -0.0134 S32:    0.6980 S33:    0.0985                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6OKO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240895.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : ???                                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34398                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.530                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.02800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2000                            
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) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-22% W/V PEG3350, 10-15 MM L           
REMARK 280  -PROLINE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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       72.38000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.37500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.38000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.37500            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     TRP A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     GLY A   163                                                      
REMARK 465     LEU A   164                                                      
REMARK 465     SER A   165                                                      
REMARK 465     THR A   166                                                      
REMARK 465     PHE A   167                                                      
REMARK 465     GLN A   168                                                      
REMARK 465     GLY A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     SER A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     GLY A   174                                                      
REMARK 465     SER A   175                                                      
REMARK 465     GLY A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     GLY A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     SER A   181                                                      
REMARK 465     ARG A   182                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     GLY A   185                                                      
REMARK 465     LYS A   230                                                      
REMARK 465     THR A   231                                                      
REMARK 465     SER A   232                                                      
REMARK 465     LEU A   233                                                      
REMARK 465     ILE A   234                                                      
REMARK 465     ARG A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 465     THR A   237                                                      
REMARK 465     VAL A   238                                                      
REMARK 465     CYS A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ARG A   241                                                      
REMARK 465     GLN A   312                                                      
REMARK 465     HIS A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     TRP B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLY B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     SER B   165                                                      
REMARK 465     THR B   166                                                      
REMARK 465     PHE B   167                                                      
REMARK 465     GLN B   168                                                      
REMARK 465     GLY B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     SER B   171                                                      
REMARK 465     GLN B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     SER B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     GLY B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     GLY B   180                                                      
REMARK 465     SER B   181                                                      
REMARK 465     ARG B   182                                                      
REMARK 465     ASP B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     GLY B   185                                                      
REMARK 465     GLY B   186                                                      
REMARK 465     THR B   187                                                      
REMARK 465     VAL B   228                                                      
REMARK 465     ASP B   229                                                      
REMARK 465     LYS B   230                                                      
REMARK 465     THR B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     LEU B   233                                                      
REMARK 465     ILE B   234                                                      
REMARK 465     ARG B   235                                                      
REMARK 465     GLU B   236                                                      
REMARK 465     THR B   237                                                      
REMARK 465     VAL B   238                                                      
REMARK 465     CYS B   239                                                      
REMARK 465     ASP B   240                                                      
REMARK 465     GLN B   312                                                      
REMARK 465     HIS B   313                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     HIS B   317                                                      
REMARK 465     HIS B   318                                                      
REMARK 465     HIS B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  20    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  23    CG   CD   CE   NZ                                   
REMARK 470     LYS A  56    CG   CD   CE   NZ                                   
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     PHE A 197    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 198    CG   CD   CE   NZ                                   
REMARK 470     LEU A 201    CG   CD1  CD2                                       
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     ASP A 229    CG   OD1  OD2                                       
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 298    CG   CD   CE   NZ                                   
REMARK 470     GLU A 305    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 308    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  23    CG   CD   CE   NZ                                   
REMARK 470     LYS B  56    CG   CD   CE   NZ                                   
REMARK 470     LYS B  57    CG   CD   CE   NZ                                   
REMARK 470     LYS B  63    CG   CD   CE   NZ                                   
REMARK 470     GLN B 108    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 191    CG   CD1  CD2                                       
REMARK 470     GLU B 194    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 195    CG   CD1  CD2                                       
REMARK 470     LEU B 196    CG   CD1  CD2                                       
REMARK 470     PHE B 197    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 198    CG   CD   CE   NZ                                   
REMARK 470     VAL B 199    CG1  CG2                                            
REMARK 470     ASN B 200    CG   OD1  ND2                                       
REMARK 470     LEU B 201    CG   CD1  CD2                                       
REMARK 470     LYS B 202    CG   CD   CE   NZ                                   
REMARK 470     GLU B 226    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 248    OG1  CG2                                            
REMARK 470     GLU B 261    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 265    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 269    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER B 273    OG                                                  
REMARK 470     GLN B 274    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 277    CG   OD1  ND2                                       
REMARK 470     LYS B 287    CG   CD   CE   NZ                                   
REMARK 470     GLU B 290    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 297    CG   OD1  OD2                                       
REMARK 470     LYS B 298    CG   CD   CE   NZ                                   
REMARK 470     HIS B 308    CG   ND1  CD2  CE1  NE2                             
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    LEU A 107       34.79    -95.78                                   
REMARK 500    ARG A 142      -14.49     75.17                                   
REMARK 500    LEU A 201      -44.77     66.62                                   
REMARK 500    THR A 257       63.81   -119.27                                   
REMARK 500    VAL B  14      122.71     62.33                                   
REMARK 500    LEU B 107       34.34    -94.11                                   
REMARK 500    ARG B 142      -15.43     75.17                                   
REMARK 500    PRO B 193       -9.89    -57.20                                   
REMARK 500    PHE B 197     -116.14   -145.43                                   
REMARK 500    VAL B 199      -34.32   -148.13                                   
REMARK 500    LYS B 202      122.49     86.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A4240        DISTANCE = 11.14 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1FN A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1FN B 4000                
DBREF  6OKO A    1   313  UNP    Q9QZL0   RIPK3_MOUSE      1    313             
DBREF  6OKO B    1   313  UNP    Q9QZL0   RIPK3_MOUSE      1    313             
SEQADV 6OKO ALA A  111  UNP  Q9QZL0    CYS   111 CONFLICT                       
SEQADV 6OKO ASP A  136  UNP  Q9QZL0    ASN   136 CONFLICT                       
SEQADV 6OKO LYS A  198  UNP  Q9QZL0    ASP   198 CONFLICT                       
SEQADV 6OKO LEU A  314  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO GLU A  315  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  316  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  317  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  318  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  319  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  320  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  321  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  322  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  323  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  324  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS A  325  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO ALA B  111  UNP  Q9QZL0    CYS   111 CONFLICT                       
SEQADV 6OKO ASP B  136  UNP  Q9QZL0    ASN   136 CONFLICT                       
SEQADV 6OKO LYS B  198  UNP  Q9QZL0    ASP   198 CONFLICT                       
SEQADV 6OKO LEU B  314  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO GLU B  315  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  316  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  317  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  318  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  319  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  320  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  321  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  322  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  323  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  324  UNP  Q9QZL0              EXPRESSION TAG                 
SEQADV 6OKO HIS B  325  UNP  Q9QZL0              EXPRESSION TAG                 
SEQRES   1 A  325  MET SER SER VAL LYS LEU TRP PRO THR GLY ALA SER ALA          
SEQRES   2 A  325  VAL PRO LEU VAL SER ARG GLU GLU LEU LYS LYS LEU GLU          
SEQRES   3 A  325  PHE VAL GLY LYS GLY GLY PHE GLY VAL VAL PHE ARG ALA          
SEQRES   4 A  325  HIS HIS ARG THR TRP ASN HIS ASP VAL ALA VAL LYS ILE          
SEQRES   5 A  325  VAL ASN SER LYS LYS ILE SER TRP GLU VAL LYS ALA MET          
SEQRES   6 A  325  VAL ASN LEU ARG ASN GLU ASN VAL LEU LEU LEU LEU GLY          
SEQRES   7 A  325  VAL THR GLU ASP LEU GLN TRP ASP PHE VAL SER GLY GLN          
SEQRES   8 A  325  ALA LEU VAL THR ARG PHE MET GLU ASN GLY SER LEU ALA          
SEQRES   9 A  325  GLY LEU LEU GLN PRO GLU ALA PRO ARG PRO TRP PRO LEU          
SEQRES  10 A  325  LEU CYS ARG LEU LEU GLN GLU VAL VAL LEU GLY MET CYS          
SEQRES  11 A  325  TYR LEU HIS SER LEU ASP PRO PRO LEU LEU HIS ARG ASP          
SEQRES  12 A  325  LEU LYS PRO SER ASN ILE LEU LEU ASP PRO GLU LEU HIS          
SEQRES  13 A  325  ALA LYS LEU ALA ASP PHE GLY LEU SER THR PHE GLN GLY          
SEQRES  14 A  325  GLY SER GLN SER GLY SER GLY SER GLY SER GLY SER ARG          
SEQRES  15 A  325  ASP SER GLY GLY THR LEU ALA TYR LEU ASP PRO GLU LEU          
SEQRES  16 A  325  LEU PHE LYS VAL ASN LEU LYS ALA SER LYS ALA SER ASP          
SEQRES  17 A  325  VAL TYR SER PHE GLY ILE LEU VAL TRP ALA VAL LEU ALA          
SEQRES  18 A  325  GLY ARG GLU ALA GLU LEU VAL ASP LYS THR SER LEU ILE          
SEQRES  19 A  325  ARG GLU THR VAL CYS ASP ARG GLN SER ARG PRO PRO LEU          
SEQRES  20 A  325  THR GLU LEU PRO PRO GLY SER PRO GLU THR PRO GLY LEU          
SEQRES  21 A  325  GLU LYS LEU LYS GLU LEU MET ILE HIS CYS TRP GLY SER          
SEQRES  22 A  325  GLN SER GLU ASN ARG PRO SER PHE GLN ASP CYS GLU PRO          
SEQRES  23 A  325  LYS THR ASN GLU VAL TYR ASN LEU VAL LYS ASP LYS VAL          
SEQRES  24 A  325  ASP ALA ALA VAL SER GLU VAL LYS HIS TYR LEU SER GLN          
SEQRES  25 A  325  HIS LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  325  MET SER SER VAL LYS LEU TRP PRO THR GLY ALA SER ALA          
SEQRES   2 B  325  VAL PRO LEU VAL SER ARG GLU GLU LEU LYS LYS LEU GLU          
SEQRES   3 B  325  PHE VAL GLY LYS GLY GLY PHE GLY VAL VAL PHE ARG ALA          
SEQRES   4 B  325  HIS HIS ARG THR TRP ASN HIS ASP VAL ALA VAL LYS ILE          
SEQRES   5 B  325  VAL ASN SER LYS LYS ILE SER TRP GLU VAL LYS ALA MET          
SEQRES   6 B  325  VAL ASN LEU ARG ASN GLU ASN VAL LEU LEU LEU LEU GLY          
SEQRES   7 B  325  VAL THR GLU ASP LEU GLN TRP ASP PHE VAL SER GLY GLN          
SEQRES   8 B  325  ALA LEU VAL THR ARG PHE MET GLU ASN GLY SER LEU ALA          
SEQRES   9 B  325  GLY LEU LEU GLN PRO GLU ALA PRO ARG PRO TRP PRO LEU          
SEQRES  10 B  325  LEU CYS ARG LEU LEU GLN GLU VAL VAL LEU GLY MET CYS          
SEQRES  11 B  325  TYR LEU HIS SER LEU ASP PRO PRO LEU LEU HIS ARG ASP          
SEQRES  12 B  325  LEU LYS PRO SER ASN ILE LEU LEU ASP PRO GLU LEU HIS          
SEQRES  13 B  325  ALA LYS LEU ALA ASP PHE GLY LEU SER THR PHE GLN GLY          
SEQRES  14 B  325  GLY SER GLN SER GLY SER GLY SER GLY SER GLY SER ARG          
SEQRES  15 B  325  ASP SER GLY GLY THR LEU ALA TYR LEU ASP PRO GLU LEU          
SEQRES  16 B  325  LEU PHE LYS VAL ASN LEU LYS ALA SER LYS ALA SER ASP          
SEQRES  17 B  325  VAL TYR SER PHE GLY ILE LEU VAL TRP ALA VAL LEU ALA          
SEQRES  18 B  325  GLY ARG GLU ALA GLU LEU VAL ASP LYS THR SER LEU ILE          
SEQRES  19 B  325  ARG GLU THR VAL CYS ASP ARG GLN SER ARG PRO PRO LEU          
SEQRES  20 B  325  THR GLU LEU PRO PRO GLY SER PRO GLU THR PRO GLY LEU          
SEQRES  21 B  325  GLU LYS LEU LYS GLU LEU MET ILE HIS CYS TRP GLY SER          
SEQRES  22 B  325  GLN SER GLU ASN ARG PRO SER PHE GLN ASP CYS GLU PRO          
SEQRES  23 B  325  LYS THR ASN GLU VAL TYR ASN LEU VAL LYS ASP LYS VAL          
SEQRES  24 B  325  ASP ALA ALA VAL SER GLU VAL LYS HIS TYR LEU SER GLN          
SEQRES  25 B  325  HIS LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS          
HET    1FN  A4000      50                                                       
HET    1FN  B4000      50                                                       
HETNAM     1FN 1-(4-FLUOROPHENYL)-N-[3-FLUORO-4-(1H-PYRROLO[2,3-                
HETNAM   2 1FN  B]PYRIDIN-4-YLOXY)PHENYL]-2-OXO-1,2-DIHYDROPYRIDINE-3-          
HETNAM   3 1FN  CARBOXAMIDE                                                     
FORMUL   3  1FN    2(C25 H16 F2 N4 O3)                                          
FORMUL   5  HOH   *202(H2 O)                                                    
HELIX    1 AA1 SER A   18  GLU A   20  5                                   3    
HELIX    2 AA2 LYS A   57  VAL A   66  1                                  10    
HELIX    3 AA3 SER A  102  LEU A  107  5                                   6    
HELIX    4 AA4 PRO A  114  SER A  134  1                                  21    
HELIX    5 AA5 LYS A  145  SER A  147  5                                   3    
HELIX    6 AA6 GLY A  186  LEU A  191  5                                   6    
HELIX    7 AA7 ASP A  192  PHE A  197  1                                   6    
HELIX    8 AA8 SER A  204  GLY A  222  1                                  19    
HELIX    9 AA9 PRO A  246  LEU A  250  5                                   5    
HELIX   10 AB1 GLY A  259  TRP A  271  1                                  13    
HELIX   11 AB2 GLN A  274  ARG A  278  5                                   5    
HELIX   12 AB3 SER A  280  LYS A  296  1                                  17    
HELIX   13 AB4 LYS A  298  SER A  311  1                                  14    
HELIX   14 AB5 SER B   18  GLU B   20  5                                   3    
HELIX   15 AB6 LYS B   57  VAL B   66  1                                  10    
HELIX   16 AB7 SER B  102  LEU B  107  5                                   6    
HELIX   17 AB8 PRO B  114  SER B  134  1                                  21    
HELIX   18 AB9 LYS B  145  SER B  147  5                                   3    
HELIX   19 AC1 SER B  204  GLY B  222  1                                  19    
HELIX   20 AC2 PRO B  246  LEU B  250  5                                   5    
HELIX   21 AC3 GLY B  259  TRP B  271  1                                  13    
HELIX   22 AC4 GLN B  274  ARG B  278  5                                   5    
HELIX   23 AC5 SER B  280  LYS B  296  1                                  17    
HELIX   24 AC6 LYS B  298  SER B  311  1                                  14    
SHEET    1 AA1 6 LEU A  16  VAL A  17  0                                        
SHEET    2 AA1 6 GLY A  78  THR A  80  1  O  VAL A  79   N  VAL A  17           
SHEET    3 AA1 6 VAL A  88  ARG A  96 -1  O  ALA A  92   N  THR A  80           
SHEET    4 AA1 6 HIS A  46  VAL A  53 -1  N  LYS A  51   O  LEU A  93           
SHEET    5 AA1 6 VAL A  35  HIS A  41 -1  N  ALA A  39   O  VAL A  48           
SHEET    6 AA1 6 LEU A  22  LYS A  30 -1  N  GLU A  26   O  ARG A  38           
SHEET    1 AA2 4 LEU A  16  VAL A  17  0                                        
SHEET    2 AA2 4 GLY A  78  THR A  80  1  O  VAL A  79   N  VAL A  17           
SHEET    3 AA2 4 VAL A  88  ARG A  96 -1  O  ALA A  92   N  THR A  80           
SHEET    4 AA2 4 LEU A  83  TRP A  85 -1  N  LEU A  83   O  GLY A  90           
SHEET    1 AA3 2 ILE A 149  LEU A 151  0                                        
SHEET    2 AA3 2 ALA A 157  LEU A 159 -1  O  LYS A 158   N  LEU A 150           
SHEET    1 AA4 6 LEU B  16  VAL B  17  0                                        
SHEET    2 AA4 6 GLY B  78  THR B  80  1  O  VAL B  79   N  VAL B  17           
SHEET    3 AA4 6 VAL B  88  ARG B  96 -1  O  ALA B  92   N  THR B  80           
SHEET    4 AA4 6 HIS B  46  VAL B  53 -1  N  VAL B  53   O  GLN B  91           
SHEET    5 AA4 6 VAL B  35  HIS B  41 -1  N  ALA B  39   O  VAL B  48           
SHEET    6 AA4 6 LEU B  22  GLY B  29 -1  N  GLU B  26   O  ARG B  38           
SHEET    1 AA5 4 LEU B  16  VAL B  17  0                                        
SHEET    2 AA5 4 GLY B  78  THR B  80  1  O  VAL B  79   N  VAL B  17           
SHEET    3 AA5 4 VAL B  88  ARG B  96 -1  O  ALA B  92   N  THR B  80           
SHEET    4 AA5 4 LEU B  83  TRP B  85 -1  N  LEU B  83   O  GLY B  90           
SHEET    1 AA6 2 ILE B 149  LEU B 151  0                                        
SHEET    2 AA6 2 ALA B 157  LEU B 159 -1  O  LYS B 158   N  LEU B 150           
CISPEP   1 LYS A   30    GLY A   31          0         5.17                     
CISPEP   2 ASP A  136    PRO A  137          0        -0.07                     
CISPEP   3 GLY B   32    PHE B   33          0         0.14                     
CISPEP   4 ASP B  136    PRO B  137          0         0.09                     
SITE     1 AC1 16 VAL A  36  ALA A  49  LYS A  51  GLU A  61                    
SITE     2 AC1 16 MET A  65  THR A  95  ARG A  96  PHE A  97                    
SITE     3 AC1 16 MET A  98  LEU A 132  HIS A 141  LEU A 150                    
SITE     4 AC1 16 LEU A 159  ALA A 160  ASP A 161  PHE A 162                    
SITE     1 AC2 16 VAL B  36  ALA B  49  LYS B  51  GLU B  61                    
SITE     2 AC2 16 LEU B  68  THR B  95  ARG B  96  PHE B  97                    
SITE     3 AC2 16 MET B  98  LEU B 132  HIS B 141  LEU B 150                    
SITE     4 AC2 16 LEU B 159  ALA B 160  ASP B 161  PHE B 162                    
CRYST1  144.760   52.750  103.750  90.00 130.82  90.00 C 1 2 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      0.006908  0.000000  0.005967        0.00000                         
SCALE2      0.000000  0.018957  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012736        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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