GenomeNet

Database: PDB
Entry: 4L7F
LinkDB: 4L7F
Original site: 4L7F 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JUN-13   4L7F              
TITLE     CO-CRYSTAL STRUCTURE OF JNK1 AND AX13587                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 7-362;                                        
COMPND   5 SYNONYM: MAP KINASE 8, MAPK 8, JNK-46, STRESS-ACTIVATED PROTEIN      
COMPND   6 KINASE 1C, SAPK1C, STRESS-ACTIVATED PROTEIN KINASE JNK1, C-JUN N-    
COMPND   7 TERMINAL KINASE 1;                                                   
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 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: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C                              
KEYWDS    PROTEIN KINASE FOLD, PROTEIN KINASE, JUN-C, PHOSPHORYLATION,          
KEYWDS   2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.L.WALTER,G.M.RANIERI,A.M.RIGGS,H.WEISSIG,B.LI,K.R.SHREDER           
REVDAT   2   09-OCT-13 4L7F    1       JRNL                                     
REVDAT   1   21-AUG-13 4L7F    0                                                
JRNL        AUTH   B.LI,O.M.COCIORVA,T.NOMANBHOY,H.WEISSIG,Q.LI,K.NAKAMURA,     
JRNL        AUTH 2 M.LIYANAGE,M.C.ZHANG,A.Y.SHIH,A.ABAN,Y.HU,J.CAJICA,L.PHAM,   
JRNL        AUTH 3 J.W.KOZARICH,K.R.SHREDER                                     
JRNL        TITL   HIT-TO-LEAD OPTIMIZATION AND KINASE SELECTIVITY OF           
JRNL        TITL 2 IMIDAZO[1,2-A]QUINOXALIN-4-AMINE DERIVED JNK1 INHIBITORS.    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  5217 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23916259                                                     
JRNL        DOI    10.1016/J.BMCL.2013.06.087                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 47049                          
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) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2380                            
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3291                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2871                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 449                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55000                                              
REMARK   3    B22 (A**2) : 0.55000                                              
REMARK   3    B33 (A**2) : -0.83000                                             
REMARK   3    B12 (A**2) : 0.28000                                              
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): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.075         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.581         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3211 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):    26 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4399 ; 1.470 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):    59 ; 3.612 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   423 ; 5.774 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   149 ;36.234 ;24.430       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   624 ;15.152 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;22.028 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   486 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2434 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):    12 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1463 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    37 ; 0.274 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2195 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):     5 ; 0.127 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   357 ; 0.214 ; 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):    76 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    30 ; 0.254 ; 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):  1965 ; 1.068 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3116 ; 1.710 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1475 ; 2.428 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1245 ; 3.865 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 4L7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JUN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB080275.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47064                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       67.90100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       39.20266            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.40267            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       67.90100            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       39.20266            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       31.40267            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       67.90100            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       39.20266            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       31.40267            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       78.40532            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       62.80533            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       78.40532            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       62.80533            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       78.40532            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       62.80533            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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   173                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ALA A   176                                                      
REMARK 465     GLY A   177                                                      
REMARK 465     THR A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     PHE A   180                                                      
REMARK 465     MET A   181                                                      
REMARK 465     MET A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     PRO A   184                                                      
REMARK 465     TYR A   185                                                      
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     VAL A 186    CG1  CG2                                            
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    HOH A   624     O    HOH A   934              1.63            
REMARK 500   O    HOH A   582     O    HOH A   722              1.63            
REMARK 500   O    HOH A   576     O    HOH A   913              1.89            
REMARK 500   O    HOH A   522     O    HOH A   710              2.05            
REMARK 500   NH2  ARG A    72     O    HOH A   934              2.06            
REMARK 500   OE1  GLN A    64     O    HOH A   766              2.08            
REMARK 500   O    HOH A   710     O    HOH A   876              2.10            
REMARK 500   O    HOH A   684     O    HOH A   691              2.13            
REMARK 500   O    HOH A   743     O    HOH A   848              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   640     O    HOH A   938     9554     1.93            
REMARK 500   O    HOH A   553     O    HOH A   938     9554     2.19            
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    SER A  34     -152.16   -137.63                                   
REMARK 500    ALA A  36      -53.35     84.17                                   
REMARK 500    GLN A 102      -52.03   -124.96                                   
REMARK 500    ARG A 150      -18.64     73.90                                   
REMARK 500    CYS A 163        1.36     83.60                                   
REMARK 500    ASP A 339      119.68    -37.23                                   
REMARK 500    LYS A 340        7.61     54.84                                   
REMARK 500    LEU A 342       54.57   -107.04                                   
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    THR A 371        20.7      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 1V5 A 401                 
DBREF  4L7F A    7   362  UNP    P45983   MK08_HUMAN       7    362             
SEQADV 4L7F SER A    5  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F LEU A    6  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F TRP A  363  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F ARG A  364  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F LYS A  365  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F GLY A  366  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F ILE A  367  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F ILE A  368  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F THR A  369  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F ILE A  370  UNP  P45983              EXPRESSION TAG                 
SEQADV 4L7F THR A  371  UNP  P45983              EXPRESSION TAG                 
SEQRES   1 A  367  SER LEU ASP ASN ASN PHE TYR SER VAL GLU ILE GLY ASP          
SEQRES   2 A  367  SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU LYS          
SEQRES   3 A  367  PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA ALA          
SEQRES   4 A  367  TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS LYS          
SEQRES   5 A  367  LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS ARG          
SEQRES   6 A  367  ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN HIS          
SEQRES   7 A  367  LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO GLN          
SEQRES   8 A  367  LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL MET          
SEQRES   9 A  367  GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN MET          
SEQRES  10 A  367  GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR GLN          
SEQRES  11 A  367  MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY ILE          
SEQRES  12 A  367  ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL LYS          
SEQRES  13 A  367  SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU ALA          
SEQRES  14 A  367  ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR VAL          
SEQRES  15 A  367  VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU GLY          
SEQRES  16 A  367  MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL GLY          
SEQRES  17 A  367  CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU PHE          
SEQRES  18 A  367  PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL ILE          
SEQRES  19 A  367  GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS LYS          
SEQRES  20 A  367  LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG PRO          
SEQRES  21 A  367  LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO ASP          
SEQRES  22 A  367  VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU LYS          
SEQRES  23 A  367  ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU VAL          
SEQRES  24 A  367  ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA LEU          
SEQRES  25 A  367  GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER GLU          
SEQRES  26 A  367  ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN LEU          
SEQRES  27 A  367  ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU LEU          
SEQRES  28 A  367  ILE TYR LYS GLU VAL MET ASP TRP ARG LYS GLY ILE ILE          
SEQRES  29 A  367  THR ILE THR                                                  
HET    1V5  A 401      60                                                       
HETNAM     1V5 N-[1-(4-FLUOROPHENYL)CYCLOPROPYL]-4-[(TRANS-4-                   
HETNAM   2 1V5  HYDROXYCYCLOHEXYL)AMINO]IMIDAZO[1,2-A]QUINOXALINE-8-            
HETNAM   3 1V5  CARBOXAMIDE                                                     
FORMUL   2  1V5    C26 H26 F N5 O2                                              
FORMUL   3  HOH   *449(H2 O)                                                    
HELIX    1   1 ASN A   63  VAL A   80  1                                  18    
HELIX    2   2 LEU A  115  GLN A  120  1                                   6    
HELIX    3   3 ASP A  124  SER A  144  1                                  21    
HELIX    4   4 LYS A  153  SER A  155  5                                   3    
HELIX    5   5 ALA A  193  LEU A  198  1                                   6    
HELIX    6   6 ASN A  205  HIS A  221  1                                  17    
HELIX    7   7 ASP A  229  GLY A  242  1                                  14    
HELIX    8   8 CYS A  245  LYS A  250  1                                   6    
HELIX    9   9 GLN A  253  ARG A  263  1                                  11    
HELIX   10  10 SER A  270  PHE A  275  1                                   6    
HELIX   11  11 PRO A  276  PHE A  280  5                                   5    
HELIX   12  12 LYS A  290  LEU A  302  1                                  13    
HELIX   13  13 SER A  311  HIS A  318  1                                   8    
HELIX   14  14 ILE A  321  TYR A  325  5                                   5    
HELIX   15  15 ASP A  326  GLU A  331  1                                   6    
HELIX   16  16 THR A  348  GLY A  366  1                                  19    
SHEET    1   A 2 PHE A  10  ILE A  15  0                                        
SHEET    2   A 2 SER A  18  LEU A  23 -1  O  SER A  18   N  ILE A  15           
SHEET    1   B 5 TYR A  26  GLY A  33  0                                        
SHEET    2   B 5 ILE A  39  ASP A  45 -1  O  VAL A  40   N  ILE A  32           
SHEET    3   B 5 ARG A  50  SER A  58 -1  O  ILE A  54   N  CYS A  41           
SHEET    4   B 5 ASP A 103  GLU A 109 -1  O  VAL A 104   N  LEU A  57           
SHEET    5   B 5 ASN A  90  PHE A  92 -1  N  PHE A  92   O  TYR A 105           
SHEET    1   C 3 ALA A 113  ASN A 114  0                                        
SHEET    2   C 3 ILE A 157  VAL A 159 -1  O  VAL A 159   N  ALA A 113           
SHEET    3   C 3 LEU A 165  ILE A 167 -1  O  LYS A 166   N  VAL A 158           
CISPEP   1 GLY A   33    SER A   34          0        -4.87                     
SITE     1 AC1 19 GLN A  37  GLY A  38  VAL A  40  ALA A  53                    
SITE     2 AC1 19 LYS A  55  LYS A  56  LEU A  57  GLU A 109                    
SITE     3 AC1 19 MET A 111  ASP A 112  ALA A 113  ASN A 114                    
SITE     4 AC1 19 GLN A 117  ASN A 156  LEU A 168  HOH A 554                    
SITE     5 AC1 19 HOH A 569  HOH A 771  HOH A 816                               
CRYST1  135.802  135.802   94.208  90.00  90.00 120.00 H 3           9          
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      0.007364  0.004251  0.000000        0.00000                         
SCALE2      0.000000  0.008503  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010615        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system