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Database: PDB
Entry: 4Y85
LinkDB: 4Y85
Original site: 4Y85 
HEADER    TRANSFERASE                             16-FEB-15   4Y85              
TITLE     CRYSTAL STRUCTURE OF COT KINASE DOMAIN IN COMPLEX WITH 5-(5-(1H-INDOL-
TITLE    2 3-YL)-1H-PYRROLO[2,3-B]PYRIDIN-3-YL)-1,3,4-OXADIAZOL-2-AMINE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 8;          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESDIUES 36-395;                                       
COMPND   5 SYNONYM: CANCER OSAKA THYROID ONCOGENE,PROTO-ONCOGENE C-COT,         
COMPND   6 SERINE/THREONINE-PROTEIN KINASE COT,TUMOR PROGRESSION LOCUS 2,TPL-2; 
COMPND   7 EC: 2.7.11.25;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAP3K8, COT, ESTF;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF21;                                   
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PFASTBAC1-HM                               
KEYWDS    COT, TPL-2, MAP3K8, KINASE, INHIBITOR, COMPLEX, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.GUTMANN,A.HINNIGER                                                  
REVDAT   6   29-MAY-19 4Y85    1       SSBOND                                   
REVDAT   5   24-APR-19 4Y85    1       SOURCE                                   
REVDAT   4   27-JUN-18 4Y85    1       SSBOND                                   
REVDAT   3   24-JUN-15 4Y85    1       JRNL                                     
REVDAT   2   13-MAY-15 4Y85    1       JRNL                                     
REVDAT   1   06-MAY-15 4Y85    0                                                
JRNL        AUTH   S.GUTMANN,A.HINNIGER,G.FENDRICH,P.DRUCKES,S.ANTZ,H.MATTES,   
JRNL        AUTH 2 H.MOBITZ,S.OFNER,N.SCHMIEDEBERG,A.STOJANOVIC,S.RIEFFEL,      
JRNL        AUTH 3 A.STRAUSS,T.TROXLER,R.GLATTHAR,H.SPARRER                     
JRNL        TITL   THE CRYSTAL STRUCTURE OF CANCER OSAKA THYROID KINASE REVEALS 
JRNL        TITL 2 AN UNEXPECTED KINASE DOMAIN FOLD.                            
JRNL        REF    J.BIOL.CHEM.                  V. 290 15210 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25918157                                                     
JRNL        DOI    10.1074/JBC.M115.648097                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 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) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 45305                          
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)  : 0.179                          
REMARK   3   R VALUE            (WORKING SET)  : 0.177                          
REMARK   3   FREE R VALUE                      : 0.207                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2265                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.33                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.39                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.04                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3143                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2063                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2986                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2038                   
REMARK   3   BIN FREE R VALUE                        : 0.2525                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.00                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 157                      
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            : 6939                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 361                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.49                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.61720                                              
REMARK   3    B22 (A**2) : 3.89530                                              
REMARK   3    B33 (A**2) : -8.51250                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.92780                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.268               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.280               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.192               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.282               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.195               
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      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 7198   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9813   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2311   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 125    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1171   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 7198   ; 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   : 958    ; 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   : 8212   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.98                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.81                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.51                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   20.3224    4.3193  194.1522           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1307 T22:   -0.1163                                    
REMARK   3     T33:   -0.0466 T12:   -0.0020                                    
REMARK   3     T13:   -0.0059 T23:   -0.0019                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7629 L22:    2.1085                                    
REMARK   3     L33:    0.5390 L12:    0.2248                                    
REMARK   3     L13:    0.1189 L23:    0.2053                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0121 S12:   -0.0341 S13:    0.0960                     
REMARK   3     S21:    0.0328 S22:    0.0016 S23:   -0.1148                     
REMARK   3     S31:   -0.0183 S32:   -0.0458 S33:    0.0105                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.8751   46.6846  194.8587           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1447 T22:   -0.1502                                    
REMARK   3     T33:   -0.0232 T12:    0.0068                                    
REMARK   3     T13:   -0.0142 T23:   -0.0103                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6479 L22:    1.0721                                    
REMARK   3     L33:    0.3214 L12:    0.6370                                    
REMARK   3     L13:   -0.4314 L23:   -0.0703                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0431 S12:    0.0184 S13:    0.1023                     
REMARK   3     S21:   -0.0088 S22:   -0.0084 S23:    0.2528                     
REMARK   3     S31:    0.0335 S32:   -0.0236 S33:   -0.0347                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   20.9907    4.8519  234.4064           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1530 T22:   -0.1739                                    
REMARK   3     T33:   -0.0460 T12:    0.0181                                    
REMARK   3     T13:   -0.0071 T23:   -0.0014                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.6450 L22:    1.6759                                    
REMARK   3     L33:    0.4288 L12:    0.7001                                    
REMARK   3     L13:    0.3711 L23:    0.3745                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0540 S12:    0.0588 S13:   -0.4460                     
REMARK   3     S21:    0.0111 S22:   -0.0304 S23:    0.0721                     
REMARK   3     S31:   -0.0470 S32:   -0.0495 S33:   -0.0236                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y85 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000207030.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 73.770                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.720                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.10400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.19                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.270                              
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   (%): 48.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.2, 24% PEGMME 550,      
REMARK 280  0.05 M MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K       
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       73.98900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.55650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.98900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.55650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 465     GLY A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     TRP A    72                                                      
REMARK 465     ALA A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     HIS A    97                                                      
REMARK 465     PHE A    98                                                      
REMARK 465     TYR A    99                                                      
REMARK 465     GLY A   100                                                      
REMARK 465     GLN A   101                                                      
REMARK 465     ARG A   102                                                      
REMARK 465     GLY A   140                                                      
REMARK 465     SER A   141                                                      
REMARK 465     ASP A   142                                                      
REMARK 465     PRO A   391                                                      
REMARK 465     ARG A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     ASP A   394                                                      
REMARK 465     GLN A   395                                                      
REMARK 465     GLY B    64                                                      
REMARK 465     PRO B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     GLN B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     PRO B    71                                                      
REMARK 465     TRP B    72                                                      
REMARK 465     THR B    94                                                      
REMARK 465     ALA B    95                                                      
REMARK 465     LYS B    96                                                      
REMARK 465     HIS B    97                                                      
REMARK 465     PHE B    98                                                      
REMARK 465     TYR B    99                                                      
REMARK 465     GLY B   100                                                      
REMARK 465     GLN B   101                                                      
REMARK 465     ARG B   102                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     SER B   141                                                      
REMARK 465     ASP B   142                                                      
REMARK 465     PRO B   391                                                      
REMARK 465     ARG B   392                                                      
REMARK 465     GLU B   393                                                      
REMARK 465     ASP B   394                                                      
REMARK 465     GLN B   395                                                      
REMARK 465     GLY C    64                                                      
REMARK 465     PRO C    65                                                      
REMARK 465     SER C    66                                                      
REMARK 465     GLY C    67                                                      
REMARK 465     GLN C    68                                                      
REMARK 465     GLU C    69                                                      
REMARK 465     VAL C    70                                                      
REMARK 465     PRO C    71                                                      
REMARK 465     TRP C    72                                                      
REMARK 465     ASN C    93                                                      
REMARK 465     THR C    94                                                      
REMARK 465     ALA C    95                                                      
REMARK 465     LYS C    96                                                      
REMARK 465     HIS C    97                                                      
REMARK 465     PHE C    98                                                      
REMARK 465     TYR C    99                                                      
REMARK 465     GLY C   100                                                      
REMARK 465     GLN C   101                                                      
REMARK 465     ARG C   102                                                      
REMARK 465     ASN C   138                                                      
REMARK 465     ILE C   139                                                      
REMARK 465     GLY C   140                                                      
REMARK 465     SER C   141                                                      
REMARK 465     ASP C   142                                                      
REMARK 465     PRO C   391                                                      
REMARK 465     ARG C   392                                                      
REMARK 465     GLU C   393                                                      
REMARK 465     ASP C   394                                                      
REMARK 465     GLN C   395                                                      
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     SER A  74    OG                                                  
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     HIS A  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 104    CG   CD   OE1  NE2                                  
REMARK 470     MET A 112    CE                                                  
REMARK 470     VAL A 113    CG1  CG2                                            
REMARK 470     ILE A 114    CG1  CG2  CD1                                       
REMARK 470     ILE A 123    CG1  CG2  CD1                                       
REMARK 470     SER A 125    OG                                                  
REMARK 470     LYS A 133    CG   CD   CE   NZ                                   
REMARK 470     LEU A 134    CG   CD1  CD2                                       
REMARK 470     ASN A 138    CG   OD1  ND2                                       
REMARK 470     ILE A 139    CG1  CG2  CD1                                       
REMARK 470     LYS A 161    CG   CD   CE   NZ                                   
REMARK 470     ARG A 163    NE   CZ   NH1  NH2                                  
REMARK 470     ASP A 172    CG   OD1  OD2                                       
REMARK 470     LYS A 175    CG   CD   CE   NZ                                   
REMARK 470     GLU A 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     SER A 221    OG                                                  
REMARK 470     LYS A 235    CG   CD   CE   NZ                                   
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     SER A 263    OG                                                  
REMARK 470     THR A 264    OG1  CG2                                            
REMARK 470     GLU A 279    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 280    CG   OD1  OD2                                       
REMARK 470     LYS A 285    CG   CD   CE   NZ                                   
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 321    CG   CD   OE1  NE2                                  
REMARK 470     THR A 322    CG2                                                 
REMARK 470     LYS A 329    CG   CD   CE   NZ                                   
REMARK 470     ILE A 343    CG1  CG2  CD1                                       
REMARK 470     LYS A 345    CG   CD   CE   NZ                                   
REMARK 470     GLU A 351    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 355    CG   OD1  OD2                                       
REMARK 470     ASP A 356    CG   OD1  OD2                                       
REMARK 470     GLU A 363    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 366    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 375    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A 386    CG   CD   OE1  OE2                                  
REMARK 470     SER B  74    OG                                                  
REMARK 470     GLU B  82    CG   CD   OE1  OE2                                  
REMARK 470     HIS B  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PRO B 103    CG   CD                                             
REMARK 470     VAL B 113    CG1  CG2                                            
REMARK 470     ILE B 114    CG1  CG2  CD1                                       
REMARK 470     LYS B 133    CG   CD   CE   NZ                                   
REMARK 470     LEU B 134    CG   CD1  CD2                                       
REMARK 470     ASN B 138    CG   OD1  ND2                                       
REMARK 470     ILE B 139    CG1  CG2  CD1                                       
REMARK 470     LYS B 161    CG   CD   CE   NZ                                   
REMARK 470     ARG B 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 175    CG   CD   CE   NZ                                   
REMARK 470     GLU B 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 201    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 235    CG   CD   CE   NZ                                   
REMARK 470     LYS B 248    CG   CD   CE   NZ                                   
REMARK 470     SER B 263    OG                                                  
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 280    CG   OD1  OD2                                       
REMARK 470     VAL B 281    CG1  CG2                                            
REMARK 470     LYS B 285    CG   CD   CE   NZ                                   
REMARK 470     ARG B 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 321    CG   CD   OE1  NE2                                  
REMARK 470     THR B 322    CG2                                                 
REMARK 470     VAL B 328    CG1  CG2                                            
REMARK 470     LYS B 329    CG   CD   CE   NZ                                   
REMARK 470     ILE B 343    CG1  CG2  CD1                                       
REMARK 470     LYS B 345    CG   CD   CE   NZ                                   
REMARK 470     ASP B 356    CG   OD1  OD2                                       
REMARK 470     GLU B 363    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 366    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 386    CG   CD   OE1  OE2                                  
REMARK 470     SER C  74    OG                                                  
REMARK 470     GLU C  82    CG   CD   OE1  OE2                                  
REMARK 470     HIS C  90    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL C 113    CG1  CG2                                            
REMARK 470     ILE C 114    CG1  CG2  CD1                                       
REMARK 470     SER C 125    OG                                                  
REMARK 470     LYS C 133    CG   CD   CE   NZ                                   
REMARK 470     LEU C 134    CG   CD1  CD2                                       
REMARK 470     LYS C 161    CG   CD   CE   NZ                                   
REMARK 470     ASP C 172    CG   OD1  OD2                                       
REMARK 470     LYS C 175    CG   CD   CE   NZ                                   
REMARK 470     GLU C 188    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 201    CG   CD   OE1  OE2                                  
REMARK 470     SER C 221    OG                                                  
REMARK 470     LYS C 235    CG   CD   CE   NZ                                   
REMARK 470     VAL C 237    CG1  CG2                                            
REMARK 470     LYS C 248    CG   CD   CE   NZ                                   
REMARK 470     SER C 263    OG                                                  
REMARK 470     THR C 264    OG1  CG2                                            
REMARK 470     GLU C 279    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 280    CG   OD1  OD2                                       
REMARK 470     VAL C 281    CG1  CG2                                            
REMARK 470     LYS C 285    CG   CD   CE   NZ                                   
REMARK 470     LEU C 300    CG   CD1  CD2                                       
REMARK 470     ARG C 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C 306    OG1  CG2                                            
REMARK 470     GLN C 321    CG   CD   OE1  NE2                                  
REMARK 470     THR C 322    CG2                                                 
REMARK 470     VAL C 328    CG1  CG2                                            
REMARK 470     LYS C 329    CG   CD   CE   NZ                                   
REMARK 470     LYS C 345    CG   CD   CE   NZ                                   
REMARK 470     GLN C 346    CG   CD   OE1  NE2                                  
REMARK 470     ASP C 355    CG   OD1  OD2                                       
REMARK 470     ASP C 356    CG   OD1  OD2                                       
REMARK 470     GLU C 363    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 364    CD1  CD2                                            
REMARK 470     LYS C 384    CG   CD   CE   NZ                                   
REMARK 470     GLU C 386    CG   CD   OE1  OE2                                  
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    TYR A 121       80.60   -157.42                                   
REMARK 500    ASP A 124       -6.34     76.35                                   
REMARK 500    HIS A 252       -7.97     78.32                                   
REMARK 500    ASP A 253       53.26   -147.16                                   
REMARK 500    ASP A 270       98.71     64.84                                   
REMARK 500    SER A 305     -157.54   -143.05                                   
REMARK 500    TRP A 327      -31.77     73.90                                   
REMARK 500    SER A 334      -92.84   -135.35                                   
REMARK 500    GLU A 370      123.01    -38.36                                   
REMARK 500    ASP B 124       -2.35     77.65                                   
REMARK 500    SER B 125      -42.54   -130.31                                   
REMARK 500    HIS B 252       -7.37     78.49                                   
REMARK 500    ASP B 253       52.90   -148.13                                   
REMARK 500    ASP B 270       98.82     64.00                                   
REMARK 500    SER B 305     -156.66   -142.49                                   
REMARK 500    TRP B 327      -32.82     75.18                                   
REMARK 500    SER B 334      -92.59   -129.96                                   
REMARK 500    TYR C 121       82.01   -153.48                                   
REMARK 500    ASP C 124       -3.35     77.75                                   
REMARK 500    SER C 125      -55.17   -121.84                                   
REMARK 500    HIS C 252       -6.53     77.82                                   
REMARK 500    ASP C 253       52.24   -147.46                                   
REMARK 500    ASP C 270       99.76     64.27                                   
REMARK 500    SER C 305     -157.80   -141.68                                   
REMARK 500    TRP C 327      -32.84     74.27                                   
REMARK 500    SER C 334      -94.44   -125.34                                   
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 C 606        DISTANCE =  6.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 499 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 499 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 499 C 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Y83   RELATED DB: PDB                                   
REMARK 900 4Y83 CONTAINS THE SAME PROTEIN WITH A DIFFERENT INHIBITOR            
DBREF  4Y85 A   66   395  UNP    P41279   M3K8_HUMAN      66    395             
DBREF  4Y85 B   66   395  UNP    P41279   M3K8_HUMAN      66    395             
DBREF  4Y85 C   66   395  UNP    P41279   M3K8_HUMAN      66    395             
SEQADV 4Y85 GLY A   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y85 PRO A   65  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y85 GLY B   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y85 PRO B   65  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y85 GLY C   64  UNP  P41279              EXPRESSION TAG                 
SEQADV 4Y85 PRO C   65  UNP  P41279              EXPRESSION TAG                 
SEQRES   1 A  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 A  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 A  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 A  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 A  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 A  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 A  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 A  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 A  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 A  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 A  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 A  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 A  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 A  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 A  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 A  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 A  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 A  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 A  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 A  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 A  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 A  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 A  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 A  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 A  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 A  332  ASN PRO PRO ARG GLU ASP GLN                                  
SEQRES   1 B  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 B  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 B  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 B  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 B  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 B  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 B  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 B  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 B  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 B  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 B  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 B  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 B  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 B  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 B  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 B  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 B  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 B  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 B  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 B  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 B  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 B  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 B  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 B  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 B  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 B  332  ASN PRO PRO ARG GLU ASP GLN                                  
SEQRES   1 C  332  GLY PRO SER GLY GLN GLU VAL PRO TRP LEU SER SER VAL          
SEQRES   2 C  332  ARG TYR GLY THR VAL GLU ASP LEU LEU ALA PHE ALA ASN          
SEQRES   3 C  332  HIS ILE SER ASN THR ALA LYS HIS PHE TYR GLY GLN ARG          
SEQRES   4 C  332  PRO GLN GLU SER GLY ILE LEU LEU ASN MET VAL ILE THR          
SEQRES   5 C  332  PRO GLN ASN GLY ARG TYR GLN ILE ASP SER ASP VAL LEU          
SEQRES   6 C  332  LEU ILE PRO TRP LYS LEU THR TYR ARG ASN ILE GLY SER          
SEQRES   7 C  332  ASP PHE ILE PRO ARG GLY ALA PHE GLY LYS VAL TYR LEU          
SEQRES   8 C  332  ALA GLN ASP ILE LYS THR LYS LYS ARG MET ALA CYS LYS          
SEQRES   9 C  332  LEU ILE PRO VAL ASP GLN PHE LYS PRO SER ASP VAL GLU          
SEQRES  10 C  332  ILE GLN ALA CYS PHE ARG HIS GLU ASN ILE ALA GLU LEU          
SEQRES  11 C  332  TYR GLY ALA VAL LEU TRP GLY GLU THR VAL HIS LEU PHE          
SEQRES  12 C  332  MET GLU ALA GLY GLU GLY GLY SER VAL LEU GLU LYS LEU          
SEQRES  13 C  332  GLU SER CYS GLY PRO MET ARG GLU PHE GLU ILE ILE TRP          
SEQRES  14 C  332  VAL THR LYS HIS VAL LEU LYS GLY LEU ASP PHE LEU HIS          
SEQRES  15 C  332  SER LYS LYS VAL ILE HIS HIS ASP ILE LYS PRO SER ASN          
SEQRES  16 C  332  ILE VAL PHE MET SER THR LYS ALA VAL LEU VAL ASP PHE          
SEQRES  17 C  332  GLY LEU SER VAL GLN MET THR GLU ASP VAL TYR PHE PRO          
SEQRES  18 C  332  LYS ASP LEU ARG GLY THR GLU ILE TYR MET SER PRO GLU          
SEQRES  19 C  332  VAL ILE LEU CYS ARG GLY HIS SER THR LYS ALA ASP ILE          
SEQRES  20 C  332  TYR SER LEU GLY ALA THR LEU ILE HIS MET GLN THR GLY          
SEQRES  21 C  332  THR PRO PRO TRP VAL LYS ARG TYR PRO ARG SER ALA TYR          
SEQRES  22 C  332  PRO SER TYR LEU TYR ILE ILE HIS LYS GLN ALA PRO PRO          
SEQRES  23 C  332  LEU GLU ASP ILE ALA ASP ASP CYS SER PRO GLY MET ARG          
SEQRES  24 C  332  GLU LEU ILE GLU ALA SER LEU GLU ARG ASN PRO ASN HIS          
SEQRES  25 C  332  ARG PRO ARG ALA ALA ASP LEU LEU LYS HIS GLU ALA LEU          
SEQRES  26 C  332  ASN PRO PRO ARG GLU ASP GLN                                  
HET    499  A 401      24                                                       
HET    499  B 401      24                                                       
HET    499  C 401      24                                                       
HETNAM     499 5-[5-(1H-INDOL-3-YL)-1H-PYRROLO[2,3-B]PYRIDIN-3-YL]-1,           
HETNAM   2 499  3,4-OXADIAZOL-2-AMINE                                           
FORMUL   4  499    3(C17 H12 N6 O)                                              
FORMUL   7  HOH   *361(H2 O)                                                    
HELIX    1 AA1 THR A   80  ASN A   93  1                                  14    
HELIX    2 AA2 ASP A  172  LYS A  175  5                                   4    
HELIX    3 AA3 PRO A  176  PHE A  185  1                                  10    
HELIX    4 AA4 SER A  214  GLY A  223  1                                  10    
HELIX    5 AA5 ARG A  226  LYS A  247  1                                  22    
HELIX    6 AA6 LYS A  255  SER A  257  5                                   3    
HELIX    7 AA7 THR A  290  MET A  294  5                                   5    
HELIX    8 AA8 SER A  295  CYS A  301  1                                   7    
HELIX    9 AA9 THR A  306  GLY A  323  1                                  18    
HELIX   10 AB1 TYR A  339  ALA A  347  1                                   9    
HELIX   11 AB2 PRO A  349  ILE A  353  5                                   5    
HELIX   12 AB3 SER A  358  LEU A  369  1                                  12    
HELIX   13 AB4 ARG A  378  LEU A  383  1                                   6    
HELIX   14 AB5 LYS A  384  ASN A  389  5                                   6    
HELIX   15 AB6 THR B   80  ASN B   93  1                                  14    
HELIX   16 AB7 ASP B  172  LYS B  175  5                                   4    
HELIX   17 AB8 PRO B  176  PHE B  185  1                                  10    
HELIX   18 AB9 SER B  214  GLY B  223  1                                  10    
HELIX   19 AC1 ARG B  226  LYS B  247  1                                  22    
HELIX   20 AC2 LYS B  255  SER B  257  5                                   3    
HELIX   21 AC3 THR B  290  MET B  294  5                                   5    
HELIX   22 AC4 SER B  295  CYS B  301  1                                   7    
HELIX   23 AC5 THR B  306  GLY B  323  1                                  18    
HELIX   24 AC6 TYR B  339  ALA B  347  1                                   9    
HELIX   25 AC7 PRO B  349  ILE B  353  5                                   5    
HELIX   26 AC8 SER B  358  LEU B  369  1                                  12    
HELIX   27 AC9 ASN B  372  ARG B  376  5                                   5    
HELIX   28 AD1 ARG B  378  LEU B  383  1                                   6    
HELIX   29 AD2 LYS B  384  ASN B  389  5                                   6    
HELIX   30 AD3 THR C   80  SER C   92  1                                  13    
HELIX   31 AD4 ASP C  172  LYS C  175  5                                   4    
HELIX   32 AD5 PRO C  176  PHE C  185  1                                  10    
HELIX   33 AD6 SER C  214  GLY C  223  1                                  10    
HELIX   34 AD7 ARG C  226  LYS C  247  1                                  22    
HELIX   35 AD8 LYS C  255  SER C  257  5                                   3    
HELIX   36 AD9 THR C  290  MET C  294  5                                   5    
HELIX   37 AE1 SER C  295  CYS C  301  1                                   7    
HELIX   38 AE2 THR C  306  GLY C  323  1                                  18    
HELIX   39 AE3 TYR C  339  ALA C  347  1                                   9    
HELIX   40 AE4 PRO C  349  ILE C  353  5                                   5    
HELIX   41 AE5 SER C  358  LEU C  369  1                                  12    
HELIX   42 AE6 ARG C  378  LEU C  383  1                                   6    
HELIX   43 AE7 LYS C  384  ASN C  389  5                                   6    
SHEET    1 AA1 7 VAL A  76  TYR A  78  0                                        
SHEET    2 AA1 7 SER A 106  LEU A 109  1  O  LEU A 109   N  ARG A  77           
SHEET    3 AA1 7 LEU A 193  TRP A 199 -1  O  LEU A 198   N  SER A 106           
SHEET    4 AA1 7 THR A 202  MET A 207 -1  O  HIS A 204   N  VAL A 197           
SHEET    5 AA1 7 ARG A 163  PRO A 170 -1  N  ILE A 169   O  VAL A 203           
SHEET    6 AA1 7 LYS A 151  ASP A 157 -1  N  TYR A 153   O  CYS A 166           
SHEET    7 AA1 7 VAL A 127  ILE A 130 -1  N  LEU A 128   O  GLN A 156           
SHEET    1 AA2 2 VAL A 249  ILE A 250  0                                        
SHEET    2 AA2 2 VAL A 275  GLN A 276 -1  O  VAL A 275   N  ILE A 250           
SHEET    1 AA3 2 ILE A 259  PHE A 261  0                                        
SHEET    2 AA3 2 ALA A 266  LEU A 268 -1  O  VAL A 267   N  VAL A 260           
SHEET    1 AA4 7 VAL B  76  TYR B  78  0                                        
SHEET    2 AA4 7 SER B 106  LEU B 109  1  O  LEU B 109   N  ARG B  77           
SHEET    3 AA4 7 LEU B 193  TRP B 199 -1  O  LEU B 198   N  SER B 106           
SHEET    4 AA4 7 THR B 202  MET B 207 -1  O  HIS B 204   N  VAL B 197           
SHEET    5 AA4 7 ARG B 163  PRO B 170 -1  N  ILE B 169   O  VAL B 203           
SHEET    6 AA4 7 LYS B 151  ASP B 157 -1  N  ALA B 155   O  MET B 164           
SHEET    7 AA4 7 VAL B 127  ILE B 130 -1  N  ILE B 130   O  LEU B 154           
SHEET    1 AA5 2 VAL B 249  ILE B 250  0                                        
SHEET    2 AA5 2 VAL B 275  GLN B 276 -1  O  VAL B 275   N  ILE B 250           
SHEET    1 AA6 2 ILE B 259  PHE B 261  0                                        
SHEET    2 AA6 2 ALA B 266  LEU B 268 -1  O  VAL B 267   N  VAL B 260           
SHEET    1 AA7 7 VAL C  76  TYR C  78  0                                        
SHEET    2 AA7 7 SER C 106  LEU C 109  1  O  LEU C 109   N  ARG C  77           
SHEET    3 AA7 7 LEU C 193  TRP C 199 -1  O  LEU C 198   N  SER C 106           
SHEET    4 AA7 7 THR C 202  MET C 207 -1  O  HIS C 204   N  VAL C 197           
SHEET    5 AA7 7 ARG C 163  PRO C 170 -1  N  ILE C 169   O  VAL C 203           
SHEET    6 AA7 7 LYS C 151  ASP C 157 -1  N  TYR C 153   O  CYS C 166           
SHEET    7 AA7 7 VAL C 127  ILE C 130 -1  N  LEU C 128   O  GLN C 156           
SHEET    1 AA8 2 VAL C 249  ILE C 250  0                                        
SHEET    2 AA8 2 VAL C 275  GLN C 276 -1  O  VAL C 275   N  ILE C 250           
SHEET    1 AA9 2 ILE C 259  PHE C 261  0                                        
SHEET    2 AA9 2 ALA C 266  LEU C 268 -1  O  VAL C 267   N  VAL C 260           
CISPEP   1 ALA A  347    PRO A  348          0         4.14                     
CISPEP   2 ALA B  347    PRO B  348          0         4.21                     
CISPEP   3 ALA C  347    PRO C  348          0         3.01                     
SITE     1 AC1 16 TRP A 132  PRO A 145  GLY A 147  VAL A 152                    
SITE     2 AC1 16 ALA A 165  LYS A 167  GLU A 208  GLY A 210                    
SITE     3 AC1 16 GLY A 213  SER A 214  GLU A 217  VAL A 260                    
SITE     4 AC1 16 VAL A 269  ASP A 270  HOH A 554  HOH A 567                    
SITE     1 AC2 16 TRP B 132  PHE B 143  PRO B 145  GLY B 147                    
SITE     2 AC2 16 VAL B 152  ALA B 165  LYS B 167  GLU B 208                    
SITE     3 AC2 16 GLY B 210  GLY B 213  SER B 214  GLU B 217                    
SITE     4 AC2 16 VAL B 260  VAL B 269  ASP B 270  HOH B 539                    
SITE     1 AC3 17 TRP C 132  PRO C 145  GLY C 147  VAL C 152                    
SITE     2 AC3 17 ALA C 165  LYS C 167  GLU C 208  GLY C 210                    
SITE     3 AC3 17 GLY C 213  SER C 214  GLU C 217  VAL C 260                    
SITE     4 AC3 17 VAL C 269  ASP C 270  HOH C 529  HOH C 533                    
SITE     5 AC3 17 HOH C 543                                                     
CRYST1  147.978   85.113   85.964  90.00  91.06  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006758  0.000000  0.000125        0.00000                         
SCALE2      0.000000  0.011749  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011635        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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