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Database: PDB
Entry: 3PTG
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Original site: 3PTG 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       02-DEC-10   3PTG              
TITLE     DESIGN AND SYNTHESIS OF A NOVEL, ORALLY EFFICACIOUS TRI-SUBSTITUTED   
TITLE    2 THIOPHENE BASED JNK INHIBITOR                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 40-401;                                       
COMPND   5 SYNONYM: MAP KINASE 10, MAPK 10, MAP KINASE P49 3F12, STRESS-        
COMPND   6 ACTIVATED PROTEIN KINASE JNK3, C-JUN N-TERMINAL KINASE 3;            
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;         
COMPND  11 CHAIN: J;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 157-167;                                      
COMPND  13 SYNONYM: JIP-1, JNK-INTERACTING PROTEIN 1, ISLET-BRAIN 1, IB-1, JNK  
COMPND  14 MAP KINASE SCAFFOLD PROTEIN 1, MITOGEN-ACTIVATED PROTEIN KINASE 8-   
COMPND  15 INTERACTING PROTEIN 1;                                               
COMPND  16 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: MAPK10, JNK3, JNK3A, PRKM10;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    JNK INHIBITOR, THIOPHENE, NEURODEGENERATION, TRANSFERASE-TRANSFERASE  
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BOWERS,A.P.TRUONG,J.NEITZ,M.NEITZEL,G.D.PROBST,R.K.HOM,A.W.KONRADI, 
AUTHOR   2 H.L.SHAM,G.TOTH,H.PAN,N.YAO,D.R.ARTIS,E.F.BRIGHAM,K.P.QUINN,J.SAUER, 
AUTHOR   3 K.POWELL,L.RUSLIM,F.BARD,T.A.YEDNOCK,I.GRISWOLD-PRENNER              
REVDAT   2   23-MAR-11 3PTG    1       JRNL                                     
REVDAT   1   02-MAR-11 3PTG    0                                                
JRNL        AUTH   S.BOWERS,A.P.TRUONG,R.J.NEITZ,M.NEITZEL,G.D.PROBST,R.K.HOM,  
JRNL        AUTH 2 B.PETERSON,R.A.GALEMMO,A.W.KONRADI,H.L.SHAM,G.TOTH,H.PAN,    
JRNL        AUTH 3 N.YAO,D.R.ARTIS,E.F.BRIGHAM,K.P.QUINN,J.M.SAUER,K.POWELL,    
JRNL        AUTH 4 L.RUSLIM,Z.REN,F.BARD,T.A.YEDNOCK,I.GRISWOLD-PRENNER         
JRNL        TITL   DESIGN AND SYNTHESIS OF A NOVEL, ORALLY ACTIVE, BRAIN        
JRNL        TITL 2 PENETRANT, TRI-SUBSTITUTED THIOPHENE BASED JNK INHIBITOR.    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  1838 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21316234                                                     
JRNL        DOI    10.1016/J.BMCL.2011.01.046                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 13169                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.316                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 701                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.43                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 993                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.4520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2841                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 28                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.12000                                              
REMARK   3    B22 (A**2) : -0.61000                                             
REMARK   3    B33 (A**2) : -0.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.382         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.284         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.196        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2934 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3973 ; 2.025 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   346 ; 8.045 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   135 ;34.717 ;24.296       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   527 ;20.881 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;17.510 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   435 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2211 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1405 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1949 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   104 ; 0.193 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    37 ; 0.243 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.250 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1812 ; 0.960 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2854 ; 1.650 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1289 ; 1.943 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1119 ; 2.950 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3PTG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062792.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13169                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
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) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
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: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3000, 0.1 M SODIUM CITRATE, 15%   
REMARK 280  GLYCEROL, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.88600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.72500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.21700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       41.72500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.88600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.21700            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, J                                  
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     ALA A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     VAL A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     THR A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     THR A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     MET A   219                                                      
REMARK 465     MET A   220                                                      
REMARK 465     THR A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     TYR A   223                                                      
REMARK 465     VAL A   224                                                      
REMARK 465     ASP A   321                                                      
REMARK 465     SER A   322                                                      
REMARK 465     GLU A   323                                                      
REMARK 465     ARG J   153                                                      
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     LYS A 326    CG   CD   CE   NZ                                   
REMARK 470     LEU A 327    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A    52     O    SER A    56              1.93            
REMARK 500   OH   TYR A   229     OE1  GLU A   255              2.16            
REMARK 500   O    LEU A   206     O    HOH A     7              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 153   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    LEU A 236   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LYS A 328   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A  52      -71.75    -58.57                                   
REMARK 500    VAL A  53       70.00     68.16                                   
REMARK 500    GLN A 140      -46.84   -142.82                                   
REMARK 500    MET A 159     -157.58    -69.09                                   
REMARK 500    ARG A 188      -16.55     67.19                                   
REMARK 500    LEU A 206      -95.65    -76.50                                   
REMARK 500    ASP A 207     -153.00    -85.65                                   
REMARK 500    PHE A 208       83.60   -174.62                                   
REMARK 500    THR A 226       -0.43    167.39                                   
REMARK 500    LYS A 241     -152.38   -132.55                                   
REMARK 500    ASN A 243        3.28    -69.57                                   
REMARK 500    PRO A 264     -160.53    -62.50                                   
REMARK 500    ARG A 266       86.29     62.20                                   
REMARK 500    ASP A 267      139.74     62.66                                   
REMARK 500    PRO A 282      176.52    -56.73                                   
REMARK 500    PRO A 292       98.80    -54.83                                   
REMARK 500    THR A 293      -54.98    155.38                                   
REMARK 500    THR A 308      155.84     78.17                                   
REMARK 500    SER A 316      -17.51    -49.00                                   
REMARK 500    PRO A 319      -24.24    -33.63                                   
REMARK 500    ASN A 325       17.38     54.64                                   
REMARK 500    LYS A 326       79.06    173.63                                   
REMARK 500    LEU A 327     -141.19     20.82                                   
REMARK 500    LYS A 328      -57.20    154.72                                   
REMARK 500    ALA A 370      111.16    -38.87                                   
REMARK 500    ASP A 377       94.39    -57.76                                   
REMARK 500    LYS A 378      -45.46    -27.45                                   
REMARK 500    LEU A 380      121.60    -25.35                                   
REMARK 500    ASP A 381      -17.27   -177.89                                   
REMARK 500    GLU A 382      124.75     65.27                                   
REMARK 500    ARG A 383      118.86     89.13                                   
REMARK 500    VAL A 398       37.98    -86.81                                   
REMARK 500    MET A 399       20.02    175.10                                   
REMARK 500    ASN A 400       33.88    -68.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  265     ARG A  266                   37.26                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  52        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ILE A  77        23.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 327        23.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 932 A 1                   
DBREF  3PTG A   40   401  UNP    P53779   MK10_HUMAN      40    401             
DBREF  3PTG J  153   163  UNP    Q9UQF2   JIP1_HUMAN     157    167             
SEQADV 3PTG ALA A   39  UNP  P53779              EXPRESSION TAG                 
SEQRES   1 A  363  ALA SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER VAL          
SEQRES   2 A  363  GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR          
SEQRES   3 A  363  GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE          
SEQRES   4 A  363  VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN VAL          
SEQRES   5 A  363  ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR          
SEQRES   6 A  363  HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS          
SEQRES   7 A  363  CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN VAL          
SEQRES   8 A  363  PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP VAL          
SEQRES   9 A  363  TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU CYS GLN          
SEQRES  10 A  363  VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR          
SEQRES  11 A  363  LEU LEU TYR GLN MET LEU CYS GLY ILE LYS HIS LEU HIS          
SEQRES  12 A  363  SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN          
SEQRES  13 A  363  ILE VAL VAL LYS SER ASP CYS THR LEU LYS ILE LEU ASP          
SEQRES  14 A  363  PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET          
SEQRES  15 A  363  THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU          
SEQRES  16 A  363  VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE          
SEQRES  17 A  363  TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG HIS          
SEQRES  18 A  363  LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP          
SEQRES  19 A  363  ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU          
SEQRES  20 A  363  PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL          
SEQRES  21 A  363  GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO LYS          
SEQRES  22 A  363  LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU HIS          
SEQRES  23 A  363  ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER          
SEQRES  24 A  363  LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER VAL          
SEQRES  25 A  363  ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR          
SEQRES  26 A  363  ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE TYR          
SEQRES  27 A  363  ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU          
SEQRES  28 A  363  TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER              
SEQRES   1 J   11  ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE                  
HET    932  A   1      26                                                       
HETNAM     932 N-[4-METHYL-3-(1H-1,2,4-TRIAZOL-5-YL)THIOPHEN-2-YL]-2-           
HETNAM   2 932  (2-OXO-3,4-DIHYDROQUINOLIN-1(2H)-YL)ACETAMIDE                   
FORMUL   3  932    C18 H17 N5 O2 S                                              
FORMUL   4  HOH   *28(H2 O)                                                     
HELIX    1   1 ASN A  101  LYS A  116  1                                  16    
HELIX    2   2 LEU A  153  MET A  159  1                                   7    
HELIX    3   3 ASP A  162  ALA A  183  1                                  22    
HELIX    4   4 LYS A  191  SER A  193  5                                   3    
HELIX    5   5 THR A  226  ARG A  230  5                                   5    
HELIX    6   6 ALA A  231  LEU A  236  1                                   6    
HELIX    7   7 ASN A  243  HIS A  259  1                                  17    
HELIX    8   8 ASP A  267  GLY A  280  1                                  14    
HELIX    9   9 CYS A  283  LYS A  289  1                                   7    
HELIX   10  10 THR A  293  ASN A  300  1                                   8    
HELIX   11  11 THR A  308  PHE A  313  1                                   6    
HELIX   12  12 PRO A  314  PHE A  318  5                                   5    
HELIX   13  13 LYS A  328  LEU A  340  1                                  13    
HELIX   14  14 ASP A  343  ARG A  347  5                                   5    
HELIX   15  15 SER A  349  HIS A  356  1                                   8    
HELIX   16  16 HIS A  356  VAL A  361  1                                   6    
HELIX   17  17 ASP A  364  GLU A  369  1                                   6    
HELIX   18  18 THR A  386  VAL A  398  1                                  13    
SHEET    1   A 2 PHE A  48  VAL A  51  0                                        
SHEET    2   A 2 PHE A  58  LEU A  61 -1  O  PHE A  58   N  VAL A  51           
SHEET    1   B 5 TYR A  64  GLY A  71  0                                        
SHEET    2   B 5 GLY A  76  ASP A  83 -1  O  TYR A  82   N  GLN A  65           
SHEET    3   B 5 ASN A  89  LEU A  95 -1  O  LYS A  94   N  ILE A  77           
SHEET    4   B 5 TYR A 143  GLU A 147 -1  O  LEU A 144   N  LYS A  93           
SHEET    5   B 5 LEU A 126  PHE A 130 -1  N  LEU A 127   O  VAL A 145           
SHEET    1   C 3 ALA A 151  ASN A 152  0                                        
SHEET    2   C 3 ILE A 195  VAL A 197 -1  O  VAL A 197   N  ALA A 151           
SHEET    3   C 3 LEU A 203  ILE A 205 -1  O  LYS A 204   N  VAL A 196           
CISPEP   1 PHE A  208    GLY A  209          0        -2.10                     
CISPEP   2 GLY A  209    LEU A  210          0        22.84                     
CISPEP   3 LEU A  210    ALA A  211          0         1.47                     
CISPEP   4 HIS A  324    ASN A  325          0        17.82                     
CISPEP   5 LYS A  326    LEU A  327          0        15.33                     
CISPEP   6 LEU A  327    LYS A  328          0        25.95                     
CISPEP   7 GLN A  379    LEU A  380          0         3.72                     
CISPEP   8 ASP A  381    GLU A  382          0        13.01                     
SITE     1 AC1 11 ILE A  70  VAL A  78  ALA A  91  MET A 146                    
SITE     2 AC1 11 GLU A 147  MET A 149  ASP A 150  ALA A 151                    
SITE     3 AC1 11 ASN A 152  VAL A 196  HOH A 405                               
CRYST1   59.772   80.434   83.450  90.00  90.00  90.00 P 21 21 21    4          
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      0.016730  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012433  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011983        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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