GenomeNet

Database: PDB
Entry: 3FLZ
LinkDB: 3FLZ
Original site: 3FLZ 
HEADER    SIGNALING PROTEIN, TRANSFERASE          19-DEC-08   3FLZ              
TITLE     P38 KINASE CRYSTAL STRUCTURE IN COMPLEX WITH 8-METHYL-6-PHENOXY-2-    
TITLE    2 (TETRAHYDRO-PYRAN-4-YLAMINO)-8H-PYRIDO[2,3-D]PYRIMIDIN-7-ONE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MITOGEN-ACTIVATED PROTEIN KINASE P38 ALPHA, MAP KINASE P38  
COMPND   5 ALPHA, CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY DRUG-BINDING PROTEIN,  
COMPND   6 CSAID-BINDING PROTEIN, CSBP, MAX-INTERACTING PROTEIN 2, MAP KINASE   
COMPND   7 MXI2, SAPK2A;                                                        
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: CSBP, CSBP1, CSBP2, CSPB1, MAPK14, MXI2;                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P38; MAP KINASE; SERINE/THREONINE KINASE, ATP-BINDING, KINASE,        
KEYWDS   2 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, SERINE/THREONINE-       
KEYWDS   3 PROTEIN KINASE, TRANSFERASE, SIGNALING PROTEIN                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,M.GHATE                                                 
REVDAT   2   13-JUL-11 3FLZ    1       VERSN                                    
REVDAT   1   22-DEC-09 3FLZ    0                                                
JRNL        AUTH   M.SOTH,A.KUGLSTATTER,D.GOLDSTEIN                             
JRNL        TITL   THE DISCOVERY OF PAMAPIMOD AND R1487 AS ORALLY BIOAVAILABLE  
JRNL        TITL 2 AND HIGHLY SELECTIVE INHIBITORS OF P38 MAP KINASE            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23265                          
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) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1255                            
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) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1608                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.56                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2801                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 207                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 41.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : -1.18000                                             
REMARK   3    B33 (A**2) : 1.40000                                              
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): 0.253         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.207         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.157         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.142        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2897 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3935 ; 1.054 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   345 ; 5.063 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;35.581 ;24.044       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   499 ;13.365 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.839 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   438 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2192 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1197 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1986 ; 0.300 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   180 ; 0.137 ; 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):    36 ; 0.141 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.080 ; 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):  1795 ; 0.652 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2819 ; 1.172 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1287 ; 1.215 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1116 ; 2.030 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1001        A  2173                          
REMARK   3    RESIDUE RANGE :   A   361        A   361                          
REMARK   3    RESIDUE RANGE :   A     4        A   352                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4160  17.2954  21.7519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0205 T22:  -0.0083                                     
REMARK   3      T33:  -0.0345 T12:   0.0211                                     
REMARK   3      T13:  -0.0131 T23:   0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3151 L22:   0.3018                                     
REMARK   3      L33:   0.3226 L12:   0.2401                                     
REMARK   3      L13:  -0.2409 L23:  -0.0911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0332 S12:   0.0094 S13:  -0.0498                       
REMARK   3      S21:  -0.0206 S22:   0.0283 S23:   0.0037                       
REMARK   3      S31:   0.0029 S32:  -0.0091 S33:   0.0049                       
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   : 1.20                                          
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 3FLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050753.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
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   : 24691                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.230                              
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     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
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) : 2.23                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.61700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1P38                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.6, 50 MM CACL2, 17%     
REMARK 280  PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K           
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       22.91450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.02850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.98900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.02850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.91450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.98900            
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 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     MET A   -11                                                      
REMARK 465     ARG A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ARG A   173                                                      
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: 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    ASN A  14     -102.21     59.09                                   
REMARK 500    ARG A  57       72.39     31.45                                   
REMARK 500    LYS A 118       59.34     38.99                                   
REMARK 500    CYS A 119       -3.03     60.73                                   
REMARK 500    ARG A 149      -16.74     81.59                                   
REMARK 500    ASP A 150       40.58   -148.03                                   
REMARK 500    ASN A 201     -166.19   -114.70                                   
REMARK 500    PHE A 274       66.44   -105.68                                   
REMARK 500    LEU A 289       57.73    -96.55                                   
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 FLZ A 361                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FLN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FLQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FLS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FLW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FLY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FMH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FMJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FMK   RELATED DB: PDB                                   
DBREF  3FLZ A    1   360  UNP    Q16539   MK14_HUMAN       1    360             
SEQADV 3FLZ MET A  -11  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ ARG A  -10  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ GLY A   -9  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ SER A   -8  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -7  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -6  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -5  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -4  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -3  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ HIS A   -2  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ GLY A   -1  UNP  Q16539              EXPRESSION TAG                 
SEQADV 3FLZ SER A    0  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  372  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER MET          
SEQRES   2 A  372  SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU ASN          
SEQRES   3 A  372  LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN LEU          
SEQRES   4 A  372  SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS ALA          
SEQRES   5 A  372  ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL LYS          
SEQRES   6 A  372  LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA LYS          
SEQRES   7 A  372  ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET LYS          
SEQRES   8 A  372  HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR PRO          
SEQRES   9 A  372  ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU VAL          
SEQRES  10 A  372  THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL LYS          
SEQRES  11 A  372  CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU ILE          
SEQRES  12 A  372  TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA          
SEQRES  13 A  372  ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU ALA          
SEQRES  14 A  372  VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE GLY          
SEQRES  15 A  372  LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR VAL          
SEQRES  16 A  372  ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN          
SEQRES  17 A  372  TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER VAL          
SEQRES  18 A  372  GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR LEU          
SEQRES  19 A  372  PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU ILE          
SEQRES  20 A  372  LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU LYS          
SEQRES  21 A  372  LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN SER          
SEQRES  22 A  372  LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL PHE          
SEQRES  23 A  372  ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU LYS          
SEQRES  24 A  372  MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA ALA          
SEQRES  25 A  372  GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS ASP          
SEQRES  26 A  372  PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN SER          
SEQRES  27 A  372  PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS SER          
SEQRES  28 A  372  LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO PRO          
SEQRES  29 A  372  LEU ASP GLN GLU GLU MET GLU SER                              
HET    FLZ  A 361      26                                                       
HETNAM     FLZ 8-METHYL-6-PHENOXY-2-(TETRAHYDRO-2H-PYRAN-4-YLAMINO)             
HETNAM   2 FLZ  PYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE                                
FORMUL   2  FLZ    C19 H20 N4 O3                                                
FORMUL   3  HOH   *207(H2 O)                                                    
HELIX    1   1 SER A   61  MET A   78  1                                  18    
HELIX    2   2 SER A   95  PHE A   99  5                                   5    
HELIX    3   3 LEU A  113  LYS A  118  1                                   6    
HELIX    4   4 THR A  123  ALA A  144  1                                  22    
HELIX    5   5 LYS A  152  SER A  154  5                                   3    
HELIX    6   6 THR A  175  THR A  180  5                                   6    
HELIX    7   7 ALA A  190  LEU A  195  1                                   6    
HELIX    8   8 THR A  203  GLY A  219  1                                  17    
HELIX    9   9 ASP A  227  GLY A  240  1                                  14    
HELIX   10  10 GLY A  243  ILE A  250  1                                   8    
HELIX   11  11 SER A  252  SER A  261  1                                  10    
HELIX   12  12 ASN A  269  PHE A  274  1                                   6    
HELIX   13  13 ASN A  278  LEU A  289  1                                  12    
HELIX   14  14 ASP A  292  ARG A  296  5                                   5    
HELIX   15  15 THR A  298  ALA A  304  1                                   7    
HELIX   16  16 HIS A  305  ALA A  309  5                                   5    
HELIX   17  17 ASP A  313  GLU A  317  5                                   5    
HELIX   18  18 GLN A  325  ARG A  330  5                                   6    
HELIX   19  19 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  GLY A  33  0                                        
SHEET    2   B 5 GLY A  36  ASP A  43 -1  O  PHE A  42   N  GLN A  25           
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  THR A 106   N  ALA A  51           
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 11 GLY A  33  ALA A  51  LYS A  53  LEU A 104                    
SITE     2 AC1 11 THR A 106  HIS A 107  MET A 109  GLY A 110                    
SITE     3 AC1 11 ALA A 111  ASP A 112  HOH A2021                               
CRYST1   45.829   85.978  126.057  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      0.021820  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007933        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system