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Database: PDB
Entry: 4M69
LinkDB: 4M69
Original site: 4M69 
HEADER    TRANSFERASE/SIGNALING PROTEIN           09-AUG-13   4M69              
TITLE     CRYSTAL STRUCTURE OF THE MOUSE RIP3-MLKL COMPLEX                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 3;    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-313;                                        
COMPND   5 SYNONYM: RIP-LIKE PROTEIN KINASE 3, RECEPTOR-INTERACTING PROTEIN 3,  
COMPND   6 RIP-3, MRIP3;                                                        
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: MIXED LINEAGE KINASE DOMAIN-LIKE PROTEIN;                  
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 182-464;                                      
COMPND  13 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;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: MOUSE;                                              
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 GENE: MLKL;                                                          
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    KINASE, PHOSPHORYLATION, TRANSFERASE-SIGNALING PROTEIN COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.XIE,W.PENG,C.YAN,J.WU,Y.SHI                                         
REVDAT   2   06-NOV-13 4M69    1       JRNL                                     
REVDAT   1   16-OCT-13 4M69    0                                                
JRNL        AUTH   T.XIE,W.PENG,C.YAN,J.WU,X.GONG,Y.SHI                         
JRNL        TITL   STRUCTURAL INSIGHTS INTO RIP3-MEDIATED NECROPTOTIC SIGNALING 
JRNL        REF    CELL REP                      V.   5    70 2013              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   24095729                                                     
JRNL        DOI    10.1016/J.CELREP.2013.08.044                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.57                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28464                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.060                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1439                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.5741 -  5.3747    1.00     2857   136  0.2071 0.2376        
REMARK   3     2  5.3747 -  4.2677    1.00     2750   136  0.1753 0.1970        
REMARK   3     3  4.2677 -  3.7287    1.00     2731   142  0.1903 0.1952        
REMARK   3     4  3.7287 -  3.3880    1.00     2688   159  0.2172 0.2530        
REMARK   3     5  3.3880 -  3.1452    1.00     2668   158  0.2375 0.2621        
REMARK   3     6  3.1452 -  2.9599    1.00     2668   143  0.2547 0.2648        
REMARK   3     7  2.9599 -  2.8117    1.00     2696   154  0.2657 0.3019        
REMARK   3     8  2.8117 -  2.6893    1.00     2643   148  0.2828 0.3244        
REMARK   3     9  2.6893 -  2.5858    1.00     2716   123  0.2906 0.3284        
REMARK   3    10  2.5858 -  2.4966    0.98     2608   140  0.2989 0.3607        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 44.68                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.650           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.36090                                              
REMARK   3    B22 (A**2) : 3.08570                                              
REMARK   3    B33 (A**2) : -7.29440                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           4538                                  
REMARK   3   ANGLE     :  1.416           6156                                  
REMARK   3   CHIRALITY :  0.071            685                                  
REMARK   3   PLANARITY :  0.018            780                                  
REMARK   3   DIHEDRAL  : 18.562           1722                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1968 -40.7329   2.0798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2611 T22:   0.2773                                     
REMARK   3      T33:   0.2541 T12:   0.0034                                     
REMARK   3      T13:   0.0172 T23:   0.0274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9818 L22:   1.6509                                     
REMARK   3      L33:   0.7004 L12:   0.7109                                     
REMARK   3      L13:   0.4379 L23:   0.4021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1017 S12:   0.0864 S13:   0.1622                       
REMARK   3      S21:  -0.0811 S22:  -0.0086 S23:   0.0291                       
REMARK   3      S31:  -0.0869 S32:   0.0877 S33:   0.1090                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4M69 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081518.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28489                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.497                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
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: PHASER                                                
REMARK 200 STARTING MODEL: 4M66 AND 4M68                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 0.35M (NH4)2S04, 17%         
REMARK 280  PEG4000, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K    
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       53.56450            
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       53.56450            
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       53.22150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.97550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       53.22150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.97550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       53.56450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       53.22150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       70.97550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       53.56450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       53.22150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       70.97550            
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 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: 3960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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     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     HIS A   313                                                      
REMARK 465     SER B   345                                                      
REMARK 465     ILE B   346                                                      
REMARK 465     SER B   347                                                      
REMARK 465     ARG B   348                                                      
REMARK 465     THR B   349                                                      
REMARK 465     ALA B   350                                                      
REMARK 465     LYS B   351                                                      
REMARK 465     SER B   352                                                      
REMARK 465     THR B   353                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     ALA B   355                                                      
REMARK 465     GLU B   356                                                      
REMARK 465     ARG B   357                                                      
REMARK 465     SER B   459                                                      
REMARK 465     THR B   460                                                      
REMARK 465     ASP B   461                                                      
REMARK 465     LYS B   462                                                      
REMARK 465     LYS B   463                                                      
REMARK 465     VAL B   464                                                      
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    PHE A  33      -33.91   -131.97                                   
REMARK 500    LYS A  56      -17.72     76.81                                   
REMARK 500    ARG A  69      118.00   -169.14                                   
REMARK 500    GLU A  81     -169.96    -76.87                                   
REMARK 500    ASP A  86       52.42     39.05                                   
REMARK 500    LEU A 107       40.43    -88.57                                   
REMARK 500    HIS A 141      -72.10    -64.86                                   
REMARK 500    ARG A 142        0.02     85.35                                   
REMARK 500    ASP A 143       33.64   -150.86                                   
REMARK 500    LEU A 155       15.82     85.02                                   
REMARK 500    ASP A 229       82.86    -65.70                                   
REMARK 500    LYS A 230       91.04   -168.96                                   
REMARK 500    THR A 237      -59.71   -124.72                                   
REMARK 500    CYS A 239      -74.14    -83.52                                   
REMARK 500    THR A 257       55.83   -119.67                                   
REMARK 500    ASP A 297       77.50    -66.82                                   
REMARK 500    LYS A 298        8.38    165.92                                   
REMARK 500    ILE B 183     -146.61    -65.43                                   
REMARK 500    LYS B 184      101.17   -163.88                                   
REMARK 500    CYS B 275       79.51   -118.35                                   
REMARK 500    ARG B 317       -5.40     83.78                                   
REMARK 500    ASN B 318       56.96   -149.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TPO A 231        -21.07                                           
REMARK 500    SEP A 232        -36.73                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP A 401   O1A                                                    
REMARK 620 2 ASN A 148   OD1 168.0                                              
REMARK 620 3 ANP A 401   O1B  86.6 100.3                                        
REMARK 620 4 ASP A 161   OD2  89.9  80.8 164.0                                  
REMARK 620 5 ANP A 401   O2G  82.3  89.2  79.7  84.3                            
REMARK 620 6 HOH A 593   O   108.5  78.5 109.7  86.2 165.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4M66   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M68   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF CHAIN B IS ISOFORM 2 OF Q9D2Y4 (MLKL_MOUSE).         
DBREF  4M69 A    1   313  UNP    Q9QZL0   RIPK3_MOUSE      1    313             
DBREF  4M69 B  182   464  UNP    Q9D2Y4   MLKL_MOUSE     182    464             
SEQRES   1 A  313  MET SER SER VAL LYS LEU TRP PRO THR GLY ALA SER ALA          
SEQRES   2 A  313  VAL PRO LEU VAL SER ARG GLU GLU LEU LYS LYS LEU GLU          
SEQRES   3 A  313  PHE VAL GLY LYS GLY GLY PHE GLY VAL VAL PHE ARG ALA          
SEQRES   4 A  313  HIS HIS ARG THR TRP ASN HIS ASP VAL ALA VAL LYS ILE          
SEQRES   5 A  313  VAL ASN SER LYS LYS ILE SER TRP GLU VAL LYS ALA MET          
SEQRES   6 A  313  VAL ASN LEU ARG ASN GLU ASN VAL LEU LEU LEU LEU GLY          
SEQRES   7 A  313  VAL THR GLU ASP LEU GLN TRP ASP PHE VAL SER GLY GLN          
SEQRES   8 A  313  ALA LEU VAL THR ARG PHE MET GLU ASN GLY SER LEU ALA          
SEQRES   9 A  313  GLY LEU LEU GLN PRO GLU CYS PRO ARG PRO TRP PRO LEU          
SEQRES  10 A  313  LEU CYS ARG LEU LEU GLN GLU VAL VAL LEU GLY MET CYS          
SEQRES  11 A  313  TYR LEU HIS SER LEU ASP PRO PRO LEU LEU HIS ARG ASP          
SEQRES  12 A  313  LEU LYS PRO SER ASN ILE LEU LEU ASP PRO GLU LEU HIS          
SEQRES  13 A  313  ALA LYS LEU ALA ASP PHE GLY LEU SER THR PHE GLN GLY          
SEQRES  14 A  313  GLY SER GLN SER GLY SER GLY SER GLY SER GLY SER ARG          
SEQRES  15 A  313  ASP SEP GLY GLY THR LEU ALA TYR LEU ASP PRO GLU LEU          
SEQRES  16 A  313  LEU PHE LYS VAL ASN LEU LYS ALA SER LYS ALA SER ASP          
SEQRES  17 A  313  VAL TYR SER PHE GLY ILE LEU VAL TRP ALA VAL LEU ALA          
SEQRES  18 A  313  GLY ARG GLU ALA GLU LEU VAL ASP LYS TPO SEP LEU ILE          
SEQRES  19 A  313  ARG GLU THR VAL CYS ASP ARG GLN SER ARG PRO PRO LEU          
SEQRES  20 A  313  THR GLU LEU PRO PRO GLY SER PRO GLU THR PRO GLY LEU          
SEQRES  21 A  313  GLU LYS LEU LYS GLU LEU MET ILE HIS CYS TRP GLY SER          
SEQRES  22 A  313  GLN SER GLU ASN ARG PRO SER PHE GLN ASP CYS GLU PRO          
SEQRES  23 A  313  LYS THR ASN GLU VAL TYR ASN LEU VAL LYS ASP LYS VAL          
SEQRES  24 A  313  ASP ALA ALA VAL SER GLU VAL LYS HIS TYR LEU SER GLN          
SEQRES  25 A  313  HIS                                                          
SEQRES   1 B  283  GLN ILE LYS GLU ILE PRO LYS GLU HIS LEU GLY PRO PRO          
SEQRES   2 B  283  TRP THR LYS LEU LYS THR SER LYS MET SER THR ILE TYR          
SEQRES   3 B  283  ARG GLY GLU TYR HIS ARG SER PRO VAL THR ILE LYS VAL          
SEQRES   4 B  283  PHE ASN ASN PRO GLN ALA GLU SER VAL GLY ILE VAL ARG          
SEQRES   5 B  283  PHE THR PHE ASN ASP GLU ILE LYS THR MET LYS LYS PHE          
SEQRES   6 B  283  ASP SER PRO ASN ILE LEU ARG ILE PHE GLY ILE CYS ILE          
SEQRES   7 B  283  ASP GLN THR VAL LYS PRO PRO GLU PHE SER ILE VAL MET          
SEQRES   8 B  283  GLU TYR CYS GLU LEU GLY THR LEU ARG GLU LEU LEU ASP          
SEQRES   9 B  283  ARG GLU LYS ASP LEU THR MET SER VAL ARG SER LEU LEU          
SEQRES  10 B  283  VAL LEU ARG ALA ALA ARG GLY LEU TYR ARG LEU HIS HIS          
SEQRES  11 B  283  SER GLU THR LEU HIS ARG ASN ILE SER SER SER SER PHE          
SEQRES  12 B  283  LEU VAL ALA GLY GLY TYR GLN VAL LYS LEU ALA GLY PHE          
SEQRES  13 B  283  GLU LEU SER LYS THR GLN ASN SER ILE SER ARG THR ALA          
SEQRES  14 B  283  LYS SER THR LYS ALA GLU ARG SER SER SER THR ILE TYR          
SEQRES  15 B  283  VAL SER PRO GLU ARG LEU LYS ASN PRO PHE CYS LEU TYR          
SEQRES  16 B  283  ASP ILE LYS ALA GLU ILE TYR SER PHE GLY ILE VAL LEU          
SEQRES  17 B  283  TRP GLU ILE ALA THR GLY LYS ILE PRO PHE GLU GLY CYS          
SEQRES  18 B  283  ASP SER LYS LYS ILE ARG GLU LEU VAL ALA GLU ASP LYS          
SEQRES  19 B  283  LYS GLN GLU PRO VAL GLY GLN ASP CYS PRO GLU LEU LEU          
SEQRES  20 B  283  ARG GLU ILE ILE ASN GLU CYS ARG ALA HIS GLU PRO SER          
SEQRES  21 B  283  GLN ARG PRO SER VAL ASP GLY ILE LEU GLU ARG LEU SER          
SEQRES  22 B  283  ALA VAL GLU GLU SER THR ASP LYS LYS VAL                      
MODRES 4M69 SEP A  184  SER  PHOSPHOSERINE                                      
MODRES 4M69 TPO A  231  THR  PHOSPHOTHREONINE                                   
MODRES 4M69 SEP A  232  SER  PHOSPHOSERINE                                      
HET    SEP  A 184      10                                                       
HET    TPO  A 231      11                                                       
HET    SEP  A 232      10                                                       
HET    ANP  A 401      31                                                       
HET    SO4  A 402       5                                                       
HET     MG  A 403       1                                                       
HET     CL  A 404       1                                                       
HET     CL  A 405       1                                                       
HET    SO4  B 501       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3  ANP    C10 H17 N6 O12 P3                                            
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5   MG    MG 2+                                                        
FORMUL   6   CL    2(CL 1-)                                                     
FORMUL   9  HOH   *167(H2 O)                                                    
HELIX    1   1 SER A   18  GLU A   20  5                                   3    
HELIX    2   2 SER A   59  ALA A   64  1                                   6    
HELIX    3   3 MET A   65  LEU A   68  5                                   4    
HELIX    4   4 SER A  102  LEU A  107  5                                   6    
HELIX    5   5 PRO A  114  LEU A  135  1                                  22    
HELIX    6   6 LYS A  145  SER A  147  5                                   3    
HELIX    7   7 GLY A  163  GLN A  168  1                                   6    
HELIX    8   8 SEP A  184  ALA A  189  1                                   6    
HELIX    9   9 ASP A  192  LYS A  198  1                                   7    
HELIX   10  10 SER A  204  GLY A  222  1                                  19    
HELIX   11  11 LYS A  230  VAL A  238  1                                   9    
HELIX   12  12 PRO A  246  LEU A  250  5                                   5    
HELIX   13  13 GLY A  259  TRP A  271  1                                  13    
HELIX   14  14 GLN A  274  ARG A  278  5                                   5    
HELIX   15  15 SER A  280  VAL A  295  1                                  16    
HELIX   16  16 LYS A  298  SER A  311  1                                  14    
HELIX   17  17 PRO B  187  LEU B  191  5                                   5    
HELIX   18  18 SER B  228  PHE B  246  1                                  19    
HELIX   19  19 THR B  279  GLU B  287  1                                   9    
HELIX   20  20 THR B  291  SER B  312  1                                  22    
HELIX   21  21 GLY B  336  THR B  342  1                                   7    
HELIX   22  22 SER B  359  VAL B  364  5                                   6    
HELIX   23  23 SER B  365  ASN B  371  1                                   7    
HELIX   24  24 ASP B  377  GLY B  395  1                                  19    
HELIX   25  25 ASP B  403  GLU B  413  1                                  11    
HELIX   26  26 PRO B  425  ARG B  436  1                                  12    
HELIX   27  27 GLU B  439  ARG B  443  5                                   5    
HELIX   28  28 SER B  445  VAL B  456  1                                  12    
SHEET    1   A 5 LEU A  22  LYS A  30  0                                        
SHEET    2   A 5 GLY A  34  HIS A  41 -1  O  ARG A  38   N  LEU A  25           
SHEET    3   A 5 HIS A  46  VAL A  53 -1  O  VAL A  50   N  PHE A  37           
SHEET    4   A 5 ALA A  92  ARG A  96 -1  O  THR A  95   N  ALA A  49           
SHEET    5   A 5 GLY A  78  VAL A  79 -1  N  GLY A  78   O  VAL A  94           
SHEET    1   B 2 LEU A  83  TRP A  85  0                                        
SHEET    2   B 2 VAL A  88  GLY A  90 -1  O  VAL A  88   N  TRP A  85           
SHEET    1   C 2 ILE A 149  LEU A 151  0                                        
SHEET    2   C 2 ALA A 157  LEU A 159 -1  O  LYS A 158   N  LEU A 150           
SHEET    1   D 5 THR B 196  THR B 200  0                                        
SHEET    2   D 5 SER B 204  TYR B 211 -1  O  ILE B 206   N  LEU B 198           
SHEET    3   D 5 SER B 214  PHE B 221 -1  O  SER B 214   N  TYR B 211           
SHEET    4   D 5 GLU B 267  GLU B 273 -1  O  MET B 272   N  THR B 217           
SHEET    5   D 5 ILE B 254  ASP B 260 -1  N  GLY B 256   O  VAL B 271           
SHEET    1   E 2 PHE B 324  ALA B 327  0                                        
SHEET    2   E 2 GLN B 331  LEU B 334 -1  O  LYS B 333   N  LEU B 325           
LINK         C   ASP A 183                 N   SEP A 184     1555   1555  1.33  
LINK         C   SEP A 184                 N   GLY A 185     1555   1555  1.33  
LINK         C   LYS A 230                 N   TPO A 231     1555   1555  1.33  
LINK         C   TPO A 231                 N   SEP A 232     1555   1555  1.33  
LINK         C   SEP A 232                 N   LEU A 233     1555   1555  1.31  
LINK         O1A ANP A 401                MG    MG A 403     1555   1555  1.80  
LINK         OD1 ASN A 148                MG    MG A 403     1555   1555  1.86  
LINK         O1B ANP A 401                MG    MG A 403     1555   1555  1.92  
LINK         OD2 ASP A 161                MG    MG A 403     1555   1555  2.06  
LINK         O2G ANP A 401                MG    MG A 403     1555   1555  2.06  
LINK        MG    MG A 403                 O   HOH A 593     1555   1555  2.39  
CISPEP   1 ASP A  136    PRO A  137          0         0.44                     
CISPEP   2 PRO B  193    PRO B  194          0         3.57                     
CISPEP   3 LYS B  264    PRO B  265          0         3.29                     
SITE     1 AC1 28 VAL A  28  GLY A  29  LYS A  30  GLY A  31                    
SITE     2 AC1 28 GLY A  32  PHE A  33  GLY A  34  VAL A  36                    
SITE     3 AC1 28 ALA A  49  LYS A  51  THR A  95  ARG A  96                    
SITE     4 AC1 28 PHE A  97  MET A  98  SER A 102  ASP A 143                    
SITE     5 AC1 28 LYS A 145  SER A 147  ASN A 148  LEU A 150                    
SITE     6 AC1 28 ASP A 161   MG A 403  HOH A 526  HOH A 551                    
SITE     7 AC1 28 HOH A 574  HOH A 583  HOH A 584  HOH A 594                    
SITE     1 AC2  8 ARG A  69  ASN A  70  GLU A  71  VAL A  73                    
SITE     2 AC2  8 LEU A  75  ARG A  96  LYS A 158  HOH A 528                    
SITE     1 AC3  4 ASN A 148  ASP A 161  ANP A 401  HOH A 593                    
SITE     1 AC4  1 ASP A  86                                                     
SITE     1 AC5  1 ARG A  42                                                     
SITE     1 AC6  3 PRO B 215  ARG B 301  ARG B 304                               
CRYST1  106.443  141.951  107.129  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      0.009395  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009335        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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