GenomeNet

Database: PDB
Entry: 2QD9
LinkDB: 2QD9
Original site: 2QD9 
HEADER    TRANSFERASE                             20-JUN-07   2QD9              
TITLE     P38 ALPHA MAP KINASE INHIBITOR BASED ON HETEROBICYCLIC SCAFFOLDS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE P38 ALPHA;                                       
COMPND   5 EC: 2.7.11.24;                                                       
COMPND   6 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: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21 DE3;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, KINASE, TRANSFERASE, P38 MAP KINASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.SACK                                                              
REVDAT   4   12-DEC-18 2QD9    1       COMPND REMARK HETNAM                     
REVDAT   3   24-FEB-09 2QD9    1       VERSN                                    
REVDAT   2   29-JAN-08 2QD9    1       JRNL                                     
REVDAT   1   21-AUG-07 2QD9    0                                                
JRNL        AUTH   T.G.MURALI DHAR,S.T.WROBLESKI,S.LIN,J.A.FURCH,D.S.NIRSCHL,   
JRNL        AUTH 2 Y.FAN,G.TODDERUD,S.PITT,A.M.DOWEYKO,J.S.SACK,A.MATHUR,       
JRNL        AUTH 3 M.MCKINNON,J.C.BARRISH,J.H.DODD,G.L.SCHIEVEN,K.LEFTHERIS     
JRNL        TITL   SYNTHESIS AND SAR OF P38ALPHA MAP KINASE INHIBITORS BASED ON 
JRNL        TITL 2 HETEROBICYCLIC SCAFFOLDS.                                    
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  17  5019 2007              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   17664068                                                     
JRNL        DOI    10.1016/J.BMCL.2007.07.029                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 39579                          
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) : 0.252                           
REMARK   3   R VALUE            (WORKING SET) : 0.251                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2102                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2805                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2671                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.95000                                             
REMARK   3    B22 (A**2) : -0.61000                                             
REMARK   3    B33 (A**2) : 1.56000                                              
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): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.100         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.009         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2778 ; 0.024 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3775 ; 2.134 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   326 ; 6.176 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   419 ; 0.152 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2115 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1279 ; 0.235 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   177 ; 0.186 ; 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):    28 ; 0.125 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.292 ; 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):  1651 ; 1.654 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2676 ; 2.603 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1127 ; 3.513 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1099 ; 5.223 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2QD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000043452.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41971                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 46.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: REMARK: NONE                                                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       32.82500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.49000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.49000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.82500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.18000            
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: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     LYS A   118                                                      
REMARK 465     CYS A   119                                                      
REMARK 465     GLN A   120                                                      
REMARK 465     ARG A   173                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     MET A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     TYR A   182                                                      
REMARK 465     VAL A   183                                                      
REMARK 465     ALA A   184                                                      
REMARK 465     THR A   185                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  71   CD    GLU A  71   OE1     0.071                       
REMARK 500    GLU A  71   CD    GLU A  71   OE2     0.087                       
REMARK 500    CYS A 162   CB    CYS A 162   SG     -0.302                       
REMARK 500    MET A 288   SD    MET A 288   CE     -0.397                       
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    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LEU A 138   CB  -  CG  -  CD1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    LEU A 156   CB  -  CG  -  CD2 ANGL. DEV. = -14.1 DEGREES          
REMARK 500    LEU A 164   CB  -  CG  -  CD1 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ASP A 283   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    MET A 288   CG  -  SD  -  CE  ANGL. DEV. = -12.2 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    LYS A  15       -0.62     68.07                                   
REMARK 500    ARG A 149      -20.76     78.80                                   
REMARK 500    TRP A 197     -145.23    -69.58                                   
REMARK 500    HIS A 199       91.53    -43.46                                   
REMARK 500    ASN A 201     -169.67   -117.23                                   
REMARK 500    LEU A 289       42.13    -99.48                                   
REMARK 500    PRO A 350      158.05    -49.99                                   
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 A 482        DISTANCE =  7.15 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LGF A 361                 
DBREF  2QD9 A    2   360  UNP    Q16539   MK14_HUMAN       2    360             
SEQADV 2QD9 MET A   -5  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2QD9 ALA A   -4  UNP  Q16539              CLONING ARTIFACT               
SEQADV 2QD9 HIS A   -3  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2QD9 HIS A   -2  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2QD9 HIS A   -1  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2QD9 HIS A    0  UNP  Q16539              EXPRESSION TAG                 
SEQADV 2QD9 HIS A    1  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  366  MET ALA HIS HIS HIS HIS HIS SER GLN GLU ARG PRO THR          
SEQRES   2 A  366  PHE TYR ARG GLN GLU LEU ASN LYS THR ILE TRP GLU VAL          
SEQRES   3 A  366  PRO GLU ARG TYR GLN ASN LEU SER PRO VAL GLY SER GLY          
SEQRES   4 A  366  ALA TYR GLY SER VAL CYS ALA ALA PHE ASP THR LYS THR          
SEQRES   5 A  366  GLY LEU ARG VAL ALA VAL LYS LYS LEU SER ARG PRO PHE          
SEQRES   6 A  366  GLN SER ILE ILE HIS ALA LYS ARG THR TYR ARG GLU LEU          
SEQRES   7 A  366  ARG LEU LEU LYS HIS MET LYS HIS GLU ASN VAL ILE GLY          
SEQRES   8 A  366  LEU LEU ASP VAL PHE THR PRO ALA ARG SER LEU GLU GLU          
SEQRES   9 A  366  PHE ASN ASP VAL TYR LEU VAL THR HIS LEU MET GLY ALA          
SEQRES  10 A  366  ASP LEU ASN ASN ILE VAL LYS CYS GLN LYS LEU THR ASP          
SEQRES  11 A  366  ASP HIS VAL GLN PHE LEU ILE TYR GLN ILE LEU ARG GLY          
SEQRES  12 A  366  LEU LYS TYR ILE HIS SER ALA ASP ILE ILE HIS ARG ASP          
SEQRES  13 A  366  LEU LYS PRO SER ASN LEU ALA VAL ASN GLU ASP CYS GLU          
SEQRES  14 A  366  LEU LYS ILE LEU ASP PHE GLY LEU ALA ARG HIS THR ASP          
SEQRES  15 A  366  ASP GLU MET THR GLY TYR VAL ALA THR ARG TRP TYR ARG          
SEQRES  16 A  366  ALA PRO GLU ILE MET LEU ASN TRP MET HIS TYR ASN GLN          
SEQRES  17 A  366  THR VAL ASP ILE TRP SER VAL GLY CYS ILE MET ALA GLU          
SEQRES  18 A  366  LEU LEU THR GLY ARG THR LEU PHE PRO GLY THR ASP HIS          
SEQRES  19 A  366  ILE ASP GLN LEU LYS LEU ILE LEU ARG LEU VAL GLY THR          
SEQRES  20 A  366  PRO GLY ALA GLU LEU LEU LYS LYS ILE SER SER GLU SER          
SEQRES  21 A  366  ALA ARG ASN TYR ILE GLN SER LEU THR GLN MET PRO LYS          
SEQRES  22 A  366  MET ASN PHE ALA ASN VAL PHE ILE GLY ALA ASN PRO LEU          
SEQRES  23 A  366  ALA VAL ASP LEU LEU GLU LYS MET LEU VAL LEU ASP SER          
SEQRES  24 A  366  ASP LYS ARG ILE THR ALA ALA GLN ALA LEU ALA HIS ALA          
SEQRES  25 A  366  TYR PHE ALA GLN TYR HIS ASP PRO ASP ASP GLU PRO VAL          
SEQRES  26 A  366  ALA ASP PRO TYR ASP GLN SER PHE GLU SER ARG ASP LEU          
SEQRES  27 A  366  LEU ILE ASP GLU TRP LYS SER LEU THR TYR ASP GLU VAL          
SEQRES  28 A  366  ILE SER PHE VAL PRO PRO PRO LEU ASP GLN GLU GLU MET          
SEQRES  29 A  366  GLU SER                                                      
HET    LGF  A 361      40                                                       
HETNAM     LGF 1-[5-[[3-[2,4-BIS(FLUORANYL)PHENYL]-6,8-DIHYDRO-5~{H}-           
HETNAM   2 LGF  IMIDAZO[1,5-A]PYRAZIN-7-YL]CARBONYL]-6-METHOXY-1~{H}-           
HETNAM   3 LGF  PYRROLO[2,3-B]PYRIDIN-3-YL]-2-[(3~{R})-3-                       
HETNAM   4 LGF  OXIDANYLPYRROLIDIN-1-YL]ETHANE-1,2-DIONE                        
HETSYN     LGF 3,11-DIFLUORO-6,8,13-TRIMETHYL-8H-QUINO[4,3,2-                   
HETSYN   2 LGF  KL]ACRIDIN-13-IUM                                               
FORMUL   2  LGF    C27 H24 F2 N6 O5                                             
FORMUL   3  HOH   *139(H2 O)                                                    
HELIX    1   1 SER A   61  MET A   78  1                                  18    
HELIX    2   2 LEU A  113  VAL A  117  1                                   5    
HELIX    3   3 THR A  123  ALA A  144  1                                  22    
HELIX    4   4 LYS A  152  SER A  154  5                                   3    
HELIX    5   5 ALA A  190  LEU A  195  1                                   6    
HELIX    6   6 THR A  203  GLY A  219  1                                  17    
HELIX    7   7 ASP A  227  GLY A  240  1                                  14    
HELIX    8   8 GLY A  243  LYS A  248  1                                   6    
HELIX    9   9 SER A  252  SER A  261  1                                  10    
HELIX   10  10 ASN A  269  PHE A  274  1                                   6    
HELIX   11  11 ASN A  278  LEU A  289  1                                  12    
HELIX   12  12 ASP A  292  ARG A  296  5                                   5    
HELIX   13  13 THR A  298  ALA A  304  1                                   7    
HELIX   14  14 HIS A  305  ALA A  309  5                                   5    
HELIX   15  15 ASP A  313  GLU A  317  5                                   5    
HELIX   16  16 GLN A  325  ARG A  330  5                                   6    
HELIX   17  17 LEU A  333  SER A  347  1                                  15    
SHEET    1   A 2 PHE A   8  LEU A  13  0                                        
SHEET    2   A 2 THR A  16  PRO A  21 -1  O  TRP A  18   N  GLN A  11           
SHEET    1   B 5 TYR A  24  PRO A  29  0                                        
SHEET    2   B 5 GLY A  36  ASP A  43 -1  O  ALA A  40   N  SER A  28           
SHEET    3   B 5 ARG A  49  LEU A  55 -1  O  VAL A  52   N  CYS A  39           
SHEET    4   B 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53           
SHEET    5   B 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105           
SHEET    1   C 3 ALA A 111  ASP A 112  0                                        
SHEET    2   C 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111           
SHEET    3   C 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SITE     1 AC1 15 VAL A  30  VAL A  38  ALA A  51  LYS A  53                    
SITE     2 AC1 15 LEU A 104  THR A 106  MET A 109  GLY A 110                    
SITE     3 AC1 15 ALA A 111  ASP A 112  ASN A 115  SER A 154                    
SITE     4 AC1 15 ALA A 157  LEU A 167  HOH A 365                               
CRYST1   65.650   74.360   78.980  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      0.015232  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013448  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012661        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system