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Database: PDB
Entry: 1RW8
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Original site: 1RW8 
HEADER    TRANSFERASE                             16-DEC-03   1RW8              
TITLE     CRYSTAL STRUCTURE OF TGF-BETA RECEPTOR I KINASE WITH ATP              
TITLE    2 SITE INHIBITOR                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE I;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: TRUNCATED KINASE DOMAIN (RESIDUES 200-500);                
COMPND   5 SYNONYM: TGFR-1, TGF-BETA TYPE I RECEPTOR,                           
COMPND   6 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4, SKR4, ACTIVIN           
COMPND   7 RECEPTOR-LIKE KINASE 5, ALK-5;                                       
COMPND   8 EC: 2.7.1.37;                                                        
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: TRU;                                                           
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TGF-BETA RECEPTOR I, PROTEIN KINASE, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.ZHANG,J.S.SAWYER                                                    
REVDAT   2   24-FEB-09 1RW8    1       VERSN                                    
REVDAT   1   01-FEB-05 1RW8    0                                                
JRNL        AUTH   J.S.SAWYER,D.W.BEIGHT,K.S.BRITT,B.D.ANDERSON,                
JRNL        AUTH 2 R.M.CAMPBELL,T.GOODSON JR.,D.K.HERRON,H.Y.LI,                
JRNL        AUTH 3 W.T.MCMILLEN,N.MORT,S.PARSONS,E.C.SMITH,J.R.WAGNER,          
JRNL        AUTH 4 L.YAN,F.ZHANG,J.M.YINGLING                                   
JRNL        TITL   SYNTHESIS AND ACTIVITY OF NEW ARYL- AND                      
JRNL        TITL 2 HETEROARYL-SUBSTITUTED                                       
JRNL        TITL 3 5,6-DIHYDRO-4H-PYRROLO[1,2-B]PYRAZOLE INHIBITORS             
JRNL        TITL 4 OF THE TRANSFORMING GROWTH FACTOR-BETA TYPE I                
JRNL        TITL 5 RECEPTOR KINASE DOMAIN.                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  14  3581 2004              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   15177479                                                     
JRNL        DOI    10.1016/J.BMCL.2004.04.007                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 11890                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHTOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.291                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 607                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.47                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 32                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.035                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2418                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.58000                                              
REMARK   3    B22 (A**2) : 0.08400                                              
REMARK   3    B33 (A**2) : -3.67000                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.04                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.04                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.55                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.550 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : 580.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST           
REMARK   3  SQUARES PROCEDURE                                                   
REMARK   4                                                                      
REMARK   4 1RW8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021085.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JAN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
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                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11890                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1PY5                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, ATP, MGCL2, DTT, HEXANEDIOL,       
REMARK 280  PEG 4000, LISO4, PH 7.5, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 298K                                                    
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       20.98050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.04250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.48050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.04250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.98050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.48050            
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 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 213      -99.08    -86.35                                   
REMARK 500    GLU A 238       35.67    -87.09                                   
REMARK 500    GLN A 250      -64.55   -103.95                                   
REMARK 500    THR A 251       -1.50    -51.04                                   
REMARK 500    LEU A 254       31.72    -85.64                                   
REMARK 500    LYS A 268       83.56    -59.56                                   
REMARK 500    THR A 274      -87.81    -37.35                                   
REMARK 500    GLN A 275      115.14     99.01                                   
REMARK 500    THR A 323      -90.71    -49.07                                   
REMARK 500    GLN A 324       57.09    -94.23                                   
REMARK 500    ARG A 332        4.14     80.12                                   
REMARK 500    ASP A 333       43.87   -159.78                                   
REMARK 500    ASP A 351       78.57     52.01                                   
REMARK 500    ARG A 372      127.66    175.40                                   
REMARK 500    VAL A 373     -151.65    -83.25                                   
REMARK 500    MET A 390       21.04    -70.51                                   
REMARK 500    TRP A 458        7.14    -63.05                                   
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 580 A 501                 
DBREF  1RW8 A  200   500  UNP    P36897   TGFR1_HUMAN    200    500             
SEQRES   1 A  301  THR ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY          
SEQRES   2 A  301  LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG          
SEQRES   3 A  301  GLY GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU          
SEQRES   4 A  301  GLU ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR          
SEQRES   5 A  301  VAL MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA          
SEQRES   6 A  301  ALA ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP          
SEQRES   7 A  301  LEU VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP          
SEQRES   8 A  301  TYR LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE          
SEQRES   9 A  301  LYS LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU          
SEQRES  10 A  301  HIS MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE          
SEQRES  11 A  301  ALA HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS          
SEQRES  12 A  301  LYS ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA          
SEQRES  13 A  301  VAL ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA          
SEQRES  14 A  301  PRO ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO          
SEQRES  15 A  301  GLU VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU          
SEQRES  16 A  301  SER PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL          
SEQRES  17 A  301  PHE TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE          
SEQRES  18 A  301  HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO          
SEQRES  19 A  301  SER ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS          
SEQRES  20 A  301  GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN          
SEQRES  21 A  301  SER CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG          
SEQRES  22 A  301  GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA          
SEQRES  23 A  301  LEU ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN          
SEQRES  24 A  301  GLU GLY                                                      
HET    580  A 501      22                                                       
HETNAM     580 3-(4-FLUOROPHENYL)-2-(6-METHYLPYRIDIN-2-YL)-5,6-                 
HETNAM   2 580  DIHYDRO-4H-PYRROLO[1,2-B]PYRAZOLE                               
FORMUL   2  580    C18 H16 F N3                                                 
FORMUL   3  HOH   *105(H2 O)                                                    
HELIX    1   1 ILE A  201  ILE A  205  5                                   5    
HELIX    2   2 GLU A  238  THR A  251  1                                  14    
HELIX    3   3 SER A  287  TYR A  295  1                                   9    
HELIX    4   4 THR A  298  MET A  318  1                                  21    
HELIX    5   5 THR A  375  MET A  379  5                                   5    
HELIX    6   6 ALA A  380  ASP A  385  1                                   6    
HELIX    7   7 HIS A  392  ARG A  414  1                                  23    
HELIX    8   8 SER A  437  CYS A  446  1                                  10    
HELIX    9   9 PRO A  455  SER A  460  5                                   6    
HELIX   10  10 CYS A  461  GLU A  473  1                                  13    
HELIX   11  11 ASN A  478  ARG A  482  5                                   5    
HELIX   12  12 THR A  484  GLY A  500  1                                  17    
SHEET    1   A 5 VAL A 206  SER A 210  0                                        
SHEET    2   A 5 GLU A 218  TRP A 224 -1  O  ARG A 221   N  GLU A 209           
SHEET    3   A 5 GLU A 227  PHE A 234 -1  O  VAL A 229   N  GLY A 222           
SHEET    4   A 5 LEU A 276  ASP A 281 -1  O  LEU A 276   N  PHE A 234           
SHEET    5   A 5 PHE A 262  ASP A 266 -1  N  ALA A 264   O  VAL A 279           
SHEET    1   B 3 ALA A 328  ALA A 330  0                                        
SHEET    2   B 3 VAL A 356  ASP A 359 -1  O  HIS A 358   N  ALA A 328           
SHEET    3   B 3 THR A 364  ASP A 366 -1  O  THR A 364   N  ASP A 359           
SHEET    1   C 2 ILE A 339  VAL A 341  0                                        
SHEET    2   C 2 CYS A 347  ILE A 349 -1  O  CYS A 348   N  LEU A 340           
SITE     1 AC1 15 HOH A  20  ILE A 211  VAL A 219  ALA A 230                    
SITE     2 AC1 15 LYS A 232  TYR A 249  LEU A 260  LEU A 278                    
SITE     3 AC1 15 SER A 280  ASP A 281  TYR A 282  HIS A 283                    
SITE     4 AC1 15 LYS A 337  ASN A 338  LEU A 340                               
CRYST1   41.961   84.961   84.085  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      0.023832  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011893        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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