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Database: PDB
Entry: 5VLR
LinkDB: 5VLR
Original site: 5VLR 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       26-APR-17   5VLR              
TITLE     CRYSTAL STRUCTURE OF PI3K DELTA IN COMPLEX WITH A TRIFLUORO-ETHYL-    
TITLE    2 PYRAZOL-PYROLOTRIAZINE INHIBITOR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC   
COMPND   3 SUBUNIT DELTA ISOFORM;                                               
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PTDINS-3-KINASE SUBUNIT DELTA,PHOSPHATIDYLINOSITOL 4,5-     
COMPND   6 BISPHOSPHATE 3-KINASE 110 KDA CATALYTIC SUBUNIT DELTA,P110DELTA;     
COMPND   7 EC: 2.7.1.153;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY SUBUNIT ALPHA;    
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: PTDINS-3-KINASE REGULATORY SUBUNIT ALPHA,                   
COMPND  13 PHOSPHATIDYLINOSITOL 3-KINASE 85 KDA REGULATORY SUBUNIT ALPHA,PTDINS-
COMPND  14 3-KINASE REGULATORY SUBUNIT P85-ALPHA;                               
COMPND  15 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: PIK3CD;                                                        
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PIK3R1, GRB1;                                                  
SOURCE  13 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    LIPID KINASE, INHIBITOR, PI3K DELTA, TRANSFERASE-TRANSFERASE          
KEYWDS   2 INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE REGULATOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.SACK                                                              
REVDAT   2   05-JUL-17 5VLR    1       JRNL                                     
REVDAT   1   07-JUN-17 5VLR    0                                                
JRNL        AUTH   Q.LIU,Q.SHI,D.MARCOUX,D.G.BATT,L.CORNELIUS,L.Y.QIN,Z.RUAN,   
JRNL        AUTH 2 J.NEELS,M.BEAUDOIN-BERTRAND,A.S.SRIVASTAVA,L.LI,R.J.CHERNEY, 
JRNL        AUTH 3 H.GONG,S.H.WATTERSON,C.WEIGELT,K.M.GILLOOLY,K.W.MCINTYRE,    
JRNL        AUTH 4 J.H.XIE,M.T.OBERMEIER,A.FURA,B.SLECZKA,K.STEFANSKI,          
JRNL        AUTH 5 R.M.FANCHER,S.PADMANABHAN,T.RP,I.KUNDU,K.RAJAREDDY,R.SMITH,  
JRNL        AUTH 6 J.K.HENNAN,D.XING,J.FAN,P.C.LEVESQUE,Q.RUAN,S.PITT,R.ZHANG,  
JRNL        AUTH 7 D.PEDICORD,J.PAN,M.YARDE,H.LU,J.LIPPY,C.GOLDSTINE,S.SKALA,   
JRNL        AUTH 8 R.A.RAMPULLA,A.MATHUR,A.GUPTA,P.N.ARUNACHALAM,J.S.SACK,      
JRNL        AUTH 9 J.K.MUCKELBAUER,M.E.CVIJIC,L.M.SALTER-CID,R.S.BHIDE,         
JRNL        AUTH10 M.A.POSS,J.HYNES,P.H.CARTER,J.E.MACOR,S.RUEPP,G.L.SCHIEVEN,  
JRNL        AUTH11 J.A.TINO                                                     
JRNL        TITL   IDENTIFICATION OF A POTENT, SELECTIVE, AND EFFICACIOUS       
JRNL        TITL 2 PHOSPHATIDYLINOSITOL 3-KINASE DELTA (PI3K DELTA ) INHIBITOR  
JRNL        TITL 3 FOR THE TREATMENT OF IMMUNOLOGICAL DISORDERS.                
JRNL        REF    J. MED. CHEM.                 V.  60  5193 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28541707                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00618                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 34158                          
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)  : 0.210                          
REMARK   3   R VALUE            (WORKING SET)  : 0.208                          
REMARK   3   FREE R VALUE                      : 0.279                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 2.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 709                            
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               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.89                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.54                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2973                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2526                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2910                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2516                   
REMARK   3   BIN FREE R VALUE                        : 0.3073                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 2.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : NULL                     
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 38                                      
REMARK   3   SOLVENT ATOMS            : 24                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 89.13                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 87.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -14.01350                                            
REMARK   3    B22 (A**2) : -10.34500                                            
REMARK   3    B33 (A**2) : 24.35850                                             
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) : 0.400               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.984               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.384               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 2.823               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.392               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.881                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8599   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11661  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2912   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 203    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1295   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8599   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1120   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 9825   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.15                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.52                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.74                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5VLR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000227635.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-12                          
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               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 1M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34160                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 86.390                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.03400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.2700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL, VAPOR DIFFUSION, TEMPERATURE       
REMARK 280  293K, TEMPERATURE 300K                                              
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       45.42350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.36700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.28950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.36700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.42350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.28950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 49380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   175                                                      
REMARK 465     GLN A   176                                                      
REMARK 465     THR A   177                                                      
REMARK 465     TRP A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     THR A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     ARG A   184                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     PHE A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     PRO A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     VAL A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     GLN A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     GLN A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     ASN A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     ALA A   293                                                      
REMARK 465     PRO A   294                                                      
REMARK 465     GLN A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     LYS A   298                                                      
REMARK 465     PRO A   299                                                      
REMARK 465     ARG A   300                                                      
REMARK 465     ALA A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     PRO A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     ILE A   306                                                      
REMARK 465     PRO A   307                                                      
REMARK 465     ALA A   308                                                      
REMARK 465     LYS A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     VAL A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     LYS A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ALA A   404                                                      
REMARK 465     ARG A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     THR A   407                                                      
REMARK 465     LYS A   408                                                      
REMARK 465     LYS A   409                                                      
REMARK 465     LYS A   410                                                      
REMARK 465     SER A   411                                                      
REMARK 465     LYS A   412                                                      
REMARK 465     SER A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     CYS A   500                                                      
REMARK 465     VAL A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     ARG A   517                                                      
REMARK 465     ARG A   518                                                      
REMARK 465     GLY A   519                                                      
REMARK 465     SER A   520                                                      
REMARK 465     GLY A   769                                                      
REMARK 465     SER A   770                                                      
REMARK 465     GLY A   771                                                      
REMARK 465     GLY A   772                                                      
REMARK 465     LYS A   841                                                      
REMARK 465     SER A   842                                                      
REMARK 465     ASN A   843                                                      
REMARK 465     MET A   844                                                      
REMARK 465     ALA A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     THR A   847                                                      
REMARK 465     ALA A   848                                                      
REMARK 465     ALA A   849                                                      
REMARK 465     LYS A   920                                                      
REMARK 465     THR A   921                                                      
REMARK 465     LYS A   922                                                      
REMARK 465     PHE A   923                                                      
REMARK 465     GLY A   924                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  17    CG   OD1  ND2                                       
REMARK 470     GLN A  18    CG   CD   OE1  NE2                                  
REMARK 470     ARG A  38    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A  42    CD1  CD2                                            
REMARK 470     ILE A  45    CD1                                                 
REMARK 470     GLN A  47    CD   OE1  NE2                                       
REMARK 470     LEU A  48    CD1  CD2                                            
REMARK 470     HIS A  60    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET A  61    SD   CE                                             
REMARK 470     ILE A  73    CD1                                                 
REMARK 470     GLU A  83    CD   OE1  OE2                                       
REMARK 470     ARG A  87    CZ   NH1  NH2                                       
REMARK 470     LEU A  89    CD1  CD2                                            
REMARK 470     ARG A 100    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 105    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 110    CD   CE   NZ                                        
REMARK 470     LYS A 111    CG   CD   CE   NZ                                   
REMARK 470     LEU A 112    CD1  CD2                                            
REMARK 470     LEU A 119    CG   CD1  CD2                                       
REMARK 470     PHE A 146    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 156    CD   OE1  NE2                                       
REMARK 470     LEU A 157    CD1  CD2                                            
REMARK 470     LEU A 163    CD1  CD2                                            
REMARK 470     LEU A 185    CG   CD1  CD2                                       
REMARK 470     ARG A 188    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU A 190    CG   CD1  CD2                                       
REMARK 470     LEU A 191    CG   CD1  CD2                                       
REMARK 470     GLU A 197    CD   OE1  OE2                                       
REMARK 470     GLU A 200    CD   OE1  OE2                                       
REMARK 470     GLU A 201    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 205    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 206    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 207    CG1  CG2                                            
REMARK 470     SER A 208    OG                                                  
REMARK 470     LYS A 210    CD   CE   NZ                                        
REMARK 470     VAL A 212    CG1  CG2                                            
REMARK 470     LEU A 214    CG   CD1  CD2                                       
REMARK 470     LEU A 216    CG   CD1  CD2                                       
REMARK 470     LEU A 221    CG   CD1  CD2                                       
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 470     THR A 226    OG1  CG2                                            
REMARK 470     GLU A 237    CD   OE1  OE2                                       
REMARK 470     TYR A 239    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU A 241    CG   CD1  CD2                                       
REMARK 470     LEU A 250    CD1  CD2                                            
REMARK 470     LEU A 256    CD1  CD2                                            
REMARK 470     ILE A 262    CD1                                                 
REMARK 470     LEU A 266    CD1  CD2                                            
REMARK 470     LEU A 270    CD1  CD2                                            
REMARK 470     LEU A 274    CD1  CD2                                            
REMARK 470     VAL A 277    CG1  CG2                                            
REMARK 470     ILE A 282    CG1  CG2  CD1                                       
REMARK 470     MET A 285    CE                                                  
REMARK 470     LEU A 316    CG   CD1  CD2                                       
REMARK 470     LEU A 319    CD1  CD2                                            
REMARK 470     GLN A 321    CD   OE1  NE2                                       
REMARK 470     ILE A 325    CD1                                                 
REMARK 470     GLU A 326    CD   OE1  OE2                                       
REMARK 470     ILE A 328    CD1                                                 
REMARK 470     GLU A 337    CD   OE1  OE2                                       
REMARK 470     LYS A 340    CE   NZ                                             
REMARK 470     LEU A 341    CD1  CD2                                            
REMARK 470     VAL A 342    CG1  CG2                                            
REMARK 470     VAL A 343    CG1  CG2                                            
REMARK 470     GLN A 344    CD   OE1  NE2                                       
REMARK 470     LEU A 347    CD1  CD2                                            
REMARK 470     LYS A 356    CD   CE   NZ                                        
REMARK 470     VAL A 358    CG1  CG2                                            
REMARK 470     LYS A 372    CE   NZ                                             
REMARK 470     ARG A 374    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 379    CD1                                                 
REMARK 470     ILE A 381    CG1  CG2  CD1                                       
REMARK 470     LEU A 394    CD1  CD2                                            
REMARK 470     LYS A 400    CE   NZ                                             
REMARK 470     LYS A 413    CG   CD   CE   NZ                                   
REMARK 470     ILE A 418    CD1                                                 
REMARK 470     LEU A 425    CD1  CD2                                            
REMARK 470     LYS A 429    CG   CD   CE   NZ                                   
REMARK 470     GLU A 448    CD   OE1  OE2                                       
REMARK 470     LYS A 449    CG   CD   CE   NZ                                   
REMARK 470     LEU A 452    CG   CD1  CD2                                       
REMARK 470     LEU A 471    CD1  CD2                                            
REMARK 470     ILE A 473    CD1                                                 
REMARK 470     LEU A 475    CD1  CD2                                            
REMARK 470     GLU A 477    CD   OE1  OE2                                       
REMARK 470     HIS A 481    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU A 488    CD1  CD2                                            
REMARK 470     GLU A 489    CD   OE1  OE2                                       
REMARK 470     LYS A 490    CG   CD   CE   NZ                                   
REMARK 470     ILE A 491    CD1                                                 
REMARK 470     LEU A 492    CD1  CD2                                            
REMARK 470     GLU A 493    CD   OE1  OE2                                       
REMARK 470     GLU A 506    CD   OE1  OE2                                       
REMARK 470     LEU A 509    CD1  CD2                                            
REMARK 470     GLU A 513    CD   OE1  OE2                                       
REMARK 470     ILE A 514    CD1                                                 
REMARK 470     LEU A 523    CD1  CD2                                            
REMARK 470     LEU A 530    CD1  CD2                                            
REMARK 470     LYS A 533    CD   CE   NZ                                        
REMARK 470     GLU A 537    CD   OE1  OE2                                       
REMARK 470     GLU A 540    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 548    CZ   NH1  NH2                                       
REMARK 470     LYS A 554    CE   NZ                                             
REMARK 470     LYS A 557    CE   NZ                                             
REMARK 470     SER A 623    OG                                                  
REMARK 470     LYS A 631    CD   CE   NZ                                        
REMARK 470     LYS A 642    CD   CE   NZ                                        
REMARK 470     VAL A 657    CG1  CG2                                            
REMARK 470     LYS A 680    CD   CE   NZ                                        
REMARK 470     LYS A 684    CE   NZ                                             
REMARK 470     LYS A 691    CE   NZ                                             
REMARK 470     LEU A 701    CG   CD1  CD2                                       
REMARK 470     GLN A 704    CD   OE1  NE2                                       
REMARK 470     LYS A 705    CD   CE   NZ                                        
REMARK 470     THR A 706    OG1  CG2                                            
REMARK 470     GLN A 710    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 712    CE   NZ                                             
REMARK 470     GLU A 713    CD   OE1  OE2                                       
REMARK 470     LEU A 714    CG   CD1  CD2                                       
REMARK 470     LEU A 717    CG   CD1  CD2                                       
REMARK 470     GLU A 726    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 740    CD1  CD2                                            
REMARK 470     GLU A 747    CD   OE1  OE2                                       
REMARK 470     ASP A 753    CG   OD1  OD2                                       
REMARK 470     LYS A 755    CD   CE   NZ                                        
REMARK 470     LYS A 757    NZ                                                  
REMARK 470     GLU A 766    CD   OE1  OE2                                       
REMARK 470     GLU A 767    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 776    CD1                                                 
REMARK 470     ARG A 830    CZ   NH1  NH2                                       
REMARK 470     ILE A 837    CD1                                                 
REMARK 470     ASN A 840    CG   OD1  ND2                                       
REMARK 470     PHE A 850    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASN A 851    CG   OD1  ND2                                       
REMARK 470     LYS A 852    CG   CD   CE   NZ                                   
REMARK 470     LEU A 855    CG   CD1  CD2                                       
REMARK 470     LEU A 856    CD1  CD2                                            
REMARK 470     LEU A 859    CD1  CD2                                            
REMARK 470     LYS A 860    CD   CE   NZ                                        
REMARK 470     LEU A 868    CD1  CD2                                            
REMARK 470     ARG A 870    NE   CZ   NH1  NH2                                  
REMARK 470     ILE A 872    CD1                                                 
REMARK 470     HIS A 914    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE A 919    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE A 925    CD1                                                 
REMARK 470     ASN A 926    CG   OD1  ND2                                       
REMARK 470     ARG A 927    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 928    CD   OE1  OE2                                       
REMARK 470     ARG A 929    NE   CZ   NH1  NH2                                  
REMARK 470     TYR A 936    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN A 948    CG   OD1  ND2                                       
REMARK 470     GLU A 951    CD   OE1  OE2                                       
REMARK 470     LYS A 952    NZ                                                  
REMARK 470     ARG A 955    CZ   NH1  NH2                                       
REMARK 470     LYS A 993    CE   NZ                                             
REMARK 470     ILE A 995    CD1                                                 
REMARK 470     LEU A1004    CD1  CD2                                            
REMARK 470     LYS A1006    NZ                                                  
REMARK 470     GLU A1010    CD   OE1  OE2                                       
REMARK 470     LYS A1018    CE   NZ                                             
REMARK 470     ARG A1024    NE   CZ   NH1  NH2                                  
REMARK 470     TRP A1027    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1027    CZ3  CH2                                            
REMARK 470     LYS A1028    CD   CE   NZ                                        
REMARK 470     THR A1029    OG1  CG2                                            
REMARK 470     GLN B 432    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 433    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 434    CG   OD1  OD2                                       
REMARK 470     GLN B 435    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 436    CG1  CG2                                            
REMARK 470     LYS B 438    CD   CE   NZ                                        
REMARK 470     ILE B 442    CD1                                                 
REMARK 470     LYS B 447    CD   CE   NZ                                        
REMARK 470     GLN B 457    CD   OE1  NE2                                       
REMARK 470     GLU B 458    CD   OE1  OE2                                       
REMARK 470     LYS B 459    CD   CE   NZ                                        
REMARK 470     ARG B 461    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 462    CD   OE1  OE2                                       
REMARK 470     ARG B 465    CD   NE   CZ   NH1  NH2                             
REMARK 470     MET B 479    CE                                                  
REMARK 470     ARG B 481    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN B 488    CG   OD1  ND2                                       
REMARK 470     LYS B 492    CE   NZ                                             
REMARK 470     ILE B 493    CD1                                                 
REMARK 470     LYS B 506    CE   NZ                                             
REMARK 470     ILE B 509    CD1                                                 
REMARK 470     GLU B 510    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 511    CD   CE   NZ                                        
REMARK 470     LYS B 513    CD   CE   NZ                                        
REMARK 470     ARG B 514    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 515    CD   OE1  OE2                                       
REMARK 470     ASN B 517    CG   OD1  ND2                                       
REMARK 470     ILE B 524    CD1                                                 
REMARK 470     LYS B 530    CE   NZ                                             
REMARK 470     LYS B 532    CE   NZ                                             
REMARK 470     LEU B 545    CD1  CD2                                            
REMARK 470     LYS B 550    NZ                                                  
REMARK 470     LYS B 551    CE   NZ                                             
REMARK 470     LYS B 575    CE   NZ                                             
REMARK 470     LYS B 587    NZ                                                  
REMARK 470     ARG B 590    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 592    CD   CE   NZ                                        
REMARK 470     GLU B 596    CD   OE1  OE2                                       
REMARK 470     ASN B 600    CG   OD1  ND2                                       
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    GLN A  93       71.32     46.87                                   
REMARK 500    ARG A 108       35.38    -74.69                                   
REMARK 500    VAL A 109      -55.82   -122.92                                   
REMARK 500    TRP A 159      -43.25    -22.24                                   
REMARK 500    THR A 204       86.56    -64.26                                   
REMARK 500    LYS A 210       33.28    -92.52                                   
REMARK 500    MET A 217      -94.93    -90.68                                   
REMARK 500    TYR A 239      171.09     66.09                                   
REMARK 500    HIS A 247       50.21   -105.65                                   
REMARK 500    SER A 253       38.40    -65.83                                   
REMARK 500    LEU A 270      143.49    -33.45                                   
REMARK 500    TRP A 317      -79.39     57.09                                   
REMARK 500    SER A 318      -67.01     26.33                                   
REMARK 500    LEU A 319       85.24    -36.30                                   
REMARK 500    ILE A 328      -78.85    -79.71                                   
REMARK 500    LYS A 332       42.22     35.99                                   
REMARK 500    GLU A 368       78.50   -113.98                                   
REMARK 500    LYS A 372       47.82     34.66                                   
REMARK 500    ILE A 381      -47.12     -8.80                                   
REMARK 500    LYS A 400      129.27    -28.59                                   
REMARK 500    ILE A 418      -70.82    -82.09                                   
REMARK 500    ASP A 430       -2.51     75.53                                   
REMARK 500    GLU A 451      122.97     31.87                                   
REMARK 500    ASP A 466      -82.60    -55.44                                   
REMARK 500    LEU A 534       30.49    -87.99                                   
REMARK 500    PHE A 587       67.42   -118.54                                   
REMARK 500    GLN A 704       32.52    -91.10                                   
REMARK 500    LYS A 705     -100.91   -147.26                                   
REMARK 500    HIS A 730       88.08     40.26                                   
REMARK 500    ALA A 742      -93.24    -88.40                                   
REMARK 500    THR A 750     -159.21   -143.77                                   
REMARK 500    GLU A 804       39.73    -95.90                                   
REMARK 500    ARG A 809       55.55     37.09                                   
REMARK 500    ARG A 821       25.87     49.28                                   
REMARK 500    ASP A 911       71.76     40.84                                   
REMARK 500    ARG A 929      105.88    -58.21                                   
REMARK 500    ASN A 949       74.29   -160.11                                   
REMARK 500    GLN B 432       16.22     59.50                                   
REMARK 500    ASP B 434     -164.74   -101.23                                   
REMARK 500    VAL B 436      132.41    -35.47                                   
REMARK 500    LYS B 438      101.04    -51.05                                   
REMARK 500    ARG B 503      -66.59   -100.16                                   
REMARK 500    LYS B 506      -58.92    -29.35                                   
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 9EM A 4001                
DBREF  5VLR A   17  1029  UNP    O00329   PK3CD_HUMAN     17   1029             
DBREF  5VLR B  431   600  UNP    P27986   P85A_HUMAN     431    600             
SEQADV 5VLR ASP B  469  UNP  P27986    GLU   469 ENGINEERED MUTATION            
SEQADV 5VLR THR B  519  UNP  P27986    LYS   519 ENGINEERED MUTATION            
SEQADV 5VLR GLU B  529  UNP  P27986    ASP   529 ENGINEERED MUTATION            
SEQADV 5VLR VAL B  539  UNP  P27986    ILE   539 ENGINEERED MUTATION            
SEQRES   1 A 1013  ASN GLN SER VAL VAL VAL ASP PHE LEU LEU PRO THR GLY          
SEQRES   2 A 1013  VAL TYR LEU ASN PHE PRO VAL SER ARG ASN ALA ASN LEU          
SEQRES   3 A 1013  SER THR ILE LYS GLN LEU LEU TRP HIS ARG ALA GLN TYR          
SEQRES   4 A 1013  GLU PRO LEU PHE HIS MET LEU SER GLY PRO GLU ALA TYR          
SEQRES   5 A 1013  VAL PHE THR CYS ILE ASN GLN THR ALA GLU GLN GLN GLU          
SEQRES   6 A 1013  LEU GLU ASP GLU GLN ARG ARG LEU CYS ASP VAL GLN PRO          
SEQRES   7 A 1013  PHE LEU PRO VAL LEU ARG LEU VAL ALA ARG GLU GLY ASP          
SEQRES   8 A 1013  ARG VAL LYS LYS LEU ILE ASN SER GLN ILE SER LEU LEU          
SEQRES   9 A 1013  ILE GLY LYS GLY LEU HIS GLU PHE ASP SER LEU CYS ASP          
SEQRES  10 A 1013  PRO GLU VAL ASN ASP PHE ARG ALA LYS MET CYS GLN PHE          
SEQRES  11 A 1013  CYS GLU GLU ALA ALA ALA ARG ARG GLN GLN LEU GLY TRP          
SEQRES  12 A 1013  GLU ALA TRP LEU GLN TYR SER PHE PRO LEU GLN LEU GLU          
SEQRES  13 A 1013  PRO SER ALA GLN THR TRP GLY PRO GLY THR LEU ARG LEU          
SEQRES  14 A 1013  PRO ASN ARG ALA LEU LEU VAL ASN VAL LYS PHE GLU GLY          
SEQRES  15 A 1013  SER GLU GLU SER PHE THR PHE GLN VAL SER THR LYS ASP          
SEQRES  16 A 1013  VAL PRO LEU ALA LEU MET ALA CYS ALA LEU ARG LYS LYS          
SEQRES  17 A 1013  ALA THR VAL PHE ARG GLN PRO LEU VAL GLU GLN PRO GLU          
SEQRES  18 A 1013  ASP TYR THR LEU GLN VAL ASN GLY ARG HIS GLU TYR LEU          
SEQRES  19 A 1013  TYR GLY SER TYR PRO LEU CYS GLN PHE GLN TYR ILE CYS          
SEQRES  20 A 1013  SER CYS LEU HIS SER GLY LEU THR PRO HIS LEU THR MET          
SEQRES  21 A 1013  VAL HIS SER SER SER ILE LEU ALA MET ARG ASP GLU GLN          
SEQRES  22 A 1013  SER ASN PRO ALA PRO GLN VAL GLN LYS PRO ARG ALA LYS          
SEQRES  23 A 1013  PRO PRO PRO ILE PRO ALA LYS LYS PRO SER SER VAL SER          
SEQRES  24 A 1013  LEU TRP SER LEU GLU GLN PRO PHE ARG ILE GLU LEU ILE          
SEQRES  25 A 1013  GLN GLY SER LYS VAL ASN ALA ASP GLU ARG MET LYS LEU          
SEQRES  26 A 1013  VAL VAL GLN ALA GLY LEU PHE HIS GLY ASN GLU MET LEU          
SEQRES  27 A 1013  CYS LYS THR VAL SER SER SER GLU VAL SER VAL CYS SER          
SEQRES  28 A 1013  GLU PRO VAL TRP LYS GLN ARG LEU GLU PHE ASP ILE ASN          
SEQRES  29 A 1013  ILE CYS ASP LEU PRO ARG MET ALA ARG LEU CYS PHE ALA          
SEQRES  30 A 1013  LEU TYR ALA VAL ILE GLU LYS ALA LYS LYS ALA ARG SER          
SEQRES  31 A 1013  THR LYS LYS LYS SER LYS LYS ALA ASP CYS PRO ILE ALA          
SEQRES  32 A 1013  TRP ALA ASN LEU MET LEU PHE ASP TYR LYS ASP GLN LEU          
SEQRES  33 A 1013  LYS THR GLY GLU ARG CYS LEU TYR MET TRP PRO SER VAL          
SEQRES  34 A 1013  PRO ASP GLU LYS GLY GLU LEU LEU ASN PRO THR GLY THR          
SEQRES  35 A 1013  VAL ARG SER ASN PRO ASN THR ASP SER ALA ALA ALA LEU          
SEQRES  36 A 1013  LEU ILE CYS LEU PRO GLU VAL ALA PRO HIS PRO VAL TYR          
SEQRES  37 A 1013  TYR PRO ALA LEU GLU LYS ILE LEU GLU LEU GLY ARG HIS          
SEQRES  38 A 1013  SER GLU CYS VAL HIS VAL THR GLU GLU GLU GLN LEU GLN          
SEQRES  39 A 1013  LEU ARG GLU ILE LEU GLU ARG ARG GLY SER GLY GLU LEU          
SEQRES  40 A 1013  TYR GLU HIS GLU LYS ASP LEU VAL TRP LYS LEU ARG HIS          
SEQRES  41 A 1013  GLU VAL GLN GLU HIS PHE PRO GLU ALA LEU ALA ARG LEU          
SEQRES  42 A 1013  LEU LEU VAL THR LYS TRP ASN LYS HIS GLU ASP VAL ALA          
SEQRES  43 A 1013  GLN MET LEU TYR LEU LEU CYS SER TRP PRO GLU LEU PRO          
SEQRES  44 A 1013  VAL LEU SER ALA LEU GLU LEU LEU ASP PHE SER PHE PRO          
SEQRES  45 A 1013  ASP CYS HIS VAL GLY SER PHE ALA ILE LYS SER LEU ARG          
SEQRES  46 A 1013  LYS LEU THR ASP ASP GLU LEU PHE GLN TYR LEU LEU GLN          
SEQRES  47 A 1013  LEU VAL GLN VAL LEU LYS TYR GLU SER TYR LEU ASP CYS          
SEQRES  48 A 1013  GLU LEU THR LYS PHE LEU LEU ASP ARG ALA LEU ALA ASN          
SEQRES  49 A 1013  ARG LYS ILE GLY HIS PHE LEU PHE TRP HIS LEU ARG SER          
SEQRES  50 A 1013  GLU MET HIS VAL PRO SER VAL ALA LEU ARG PHE GLY LEU          
SEQRES  51 A 1013  ILE LEU GLU ALA TYR CYS ARG GLY SER THR HIS HIS MET          
SEQRES  52 A 1013  LYS VAL LEU MET LYS GLN GLY GLU ALA LEU SER LYS LEU          
SEQRES  53 A 1013  LYS ALA LEU ASN ASP PHE VAL LYS LEU SER SER GLN LYS          
SEQRES  54 A 1013  THR PRO LYS PRO GLN THR LYS GLU LEU MET HIS LEU CYS          
SEQRES  55 A 1013  MET ARG GLN GLU ALA TYR LEU GLU ALA LEU SER HIS LEU          
SEQRES  56 A 1013  GLN SER PRO LEU ASP PRO SER THR LEU LEU ALA GLU VAL          
SEQRES  57 A 1013  CYS VAL GLU GLN CYS THR PHE MET ASP SER LYS MET LYS          
SEQRES  58 A 1013  PRO LEU TRP ILE MET TYR SER ASN GLU GLU ALA GLY SER          
SEQRES  59 A 1013  GLY GLY SER VAL GLY ILE ILE PHE LYS ASN GLY ASP ASP          
SEQRES  60 A 1013  LEU ARG GLN ASP MET LEU THR LEU GLN MET ILE GLN LEU          
SEQRES  61 A 1013  MET ASP VAL LEU TRP LYS GLN GLU GLY LEU ASP LEU ARG          
SEQRES  62 A 1013  MET THR PRO TYR GLY CYS LEU PRO THR GLY ASP ARG THR          
SEQRES  63 A 1013  GLY LEU ILE GLU VAL VAL LEU ARG SER ASP THR ILE ALA          
SEQRES  64 A 1013  ASN ILE GLN LEU ASN LYS SER ASN MET ALA ALA THR ALA          
SEQRES  65 A 1013  ALA PHE ASN LYS ASP ALA LEU LEU ASN TRP LEU LYS SER          
SEQRES  66 A 1013  LYS ASN PRO GLY GLU ALA LEU ASP ARG ALA ILE GLU GLU          
SEQRES  67 A 1013  PHE THR LEU SER CYS ALA GLY TYR CYS VAL ALA THR TYR          
SEQRES  68 A 1013  VAL LEU GLY ILE GLY ASP ARG HIS SER ASP ASN ILE MET          
SEQRES  69 A 1013  ILE ARG GLU SER GLY GLN LEU PHE HIS ILE ASP PHE GLY          
SEQRES  70 A 1013  HIS PHE LEU GLY ASN PHE LYS THR LYS PHE GLY ILE ASN          
SEQRES  71 A 1013  ARG GLU ARG VAL PRO PHE ILE LEU THR TYR ASP PHE VAL          
SEQRES  72 A 1013  HIS VAL ILE GLN GLN GLY LYS THR ASN ASN SER GLU LYS          
SEQRES  73 A 1013  PHE GLU ARG PHE ARG GLY TYR CYS GLU ARG ALA TYR THR          
SEQRES  74 A 1013  ILE LEU ARG ARG HIS GLY LEU LEU PHE LEU HIS LEU PHE          
SEQRES  75 A 1013  ALA LEU MET ARG ALA ALA GLY LEU PRO GLU LEU SER CYS          
SEQRES  76 A 1013  SER LYS ASP ILE GLN TYR LEU LYS ASP SER LEU ALA LEU          
SEQRES  77 A 1013  GLY LYS THR GLU GLU GLU ALA LEU LYS HIS PHE ARG VAL          
SEQRES  78 A 1013  LYS PHE ASN GLU ALA LEU ARG GLU SER TRP LYS THR              
SEQRES   1 B  170  TYR GLN GLN ASP GLN VAL VAL LYS GLU ASP ASN ILE GLU          
SEQRES   2 B  170  ALA VAL GLY LYS LYS LEU HIS GLU TYR ASN THR GLN PHE          
SEQRES   3 B  170  GLN GLU LYS SER ARG GLU TYR ASP ARG LEU TYR GLU ASP          
SEQRES   4 B  170  TYR THR ARG THR SER GLN GLU ILE GLN MET LYS ARG THR          
SEQRES   5 B  170  ALA ILE GLU ALA PHE ASN GLU THR ILE LYS ILE PHE GLU          
SEQRES   6 B  170  GLU GLN CYS GLN THR GLN GLU ARG TYR SER LYS GLU TYR          
SEQRES   7 B  170  ILE GLU LYS PHE LYS ARG GLU GLY ASN GLU THR GLU ILE          
SEQRES   8 B  170  GLN ARG ILE MET HIS ASN TYR GLU LYS LEU LYS SER ARG          
SEQRES   9 B  170  ILE SER GLU ILE VAL ASP SER ARG ARG ARG LEU GLU GLU          
SEQRES  10 B  170  ASP LEU LYS LYS GLN ALA ALA GLU TYR ARG GLU ILE ASP          
SEQRES  11 B  170  LYS ARG MET ASN SER ILE LYS PRO ASP LEU ILE GLN LEU          
SEQRES  12 B  170  ARG LYS THR ARG ASP GLN TYR LEU MET TRP LEU THR GLN          
SEQRES  13 B  170  LYS GLY VAL ARG GLN LYS LYS LEU ASN GLU TRP LEU GLY          
SEQRES  14 B  170  ASN                                                          
HET    9EM  A4001      38                                                       
HETNAM     9EM 4-ACETYL-1-(3-{4-AMINO-5-[1-(2,2,2-TRIFLUOROETHYL)-1H-           
HETNAM   2 9EM  PYRAZOL-5-YL]PYRROLO[2,1-F][1,2,4]TRIAZIN-7-                    
HETNAM   3 9EM  YL}PHENYL)-3,3-DIMETHYLPIPERAZIN-2-ONE                          
FORMUL   3  9EM    C25 H25 F3 N8 O2                                             
FORMUL   4  HOH   *24(H2 O)                                                     
HELIX    1 AA1 ASN A   41  GLN A   54  1                                  14    
HELIX    2 AA2 LEU A   58  LEU A   62  5                                   5    
HELIX    3 AA3 GLY A   64  GLU A   66  5                                   3    
HELIX    4 AA4 ARG A   88  GLN A   93  1                                   6    
HELIX    5 AA5 VAL A  109  GLY A  122  1                                  14    
HELIX    6 AA6 GLY A  124  LEU A  131  1                                   8    
HELIX    7 AA7 ASP A  133  LEU A  157  1                                  25    
HELIX    8 AA8 GLY A  158  PHE A  167  1                                  10    
HELIX    9 AA9 VAL A  212  MET A  217  1                                   6    
HELIX   10 AB1 MET A  217  THR A  226  1                                  10    
HELIX   11 AB2 PRO A  255  GLN A  258  5                                   4    
HELIX   12 AB3 PHE A  259  GLY A  269  1                                  11    
HELIX   13 AB4 HIS A  278  ASP A  287  1                                  10    
HELIX   14 AB5 CYS A  382  LEU A  384  5                                   3    
HELIX   15 AB6 ALA A  487  ARG A  496  1                                  10    
HELIX   16 AB7 GLU A  505  GLU A  513  1                                   9    
HELIX   17 AB8 TYR A  524  LEU A  534  1                                  11    
HELIX   18 AB9 LEU A  534  PHE A  542  1                                   9    
HELIX   19 AC1 ALA A  545  THR A  553  1                                   9    
HELIX   20 AC2 LYS A  557  CYS A  569  1                                  13    
HELIX   21 AC3 PRO A  575  LEU A  582  1                                   8    
HELIX   22 AC4 ASP A  589  ARG A  601  1                                  13    
HELIX   23 AC5 THR A  604  LEU A  619  1                                  16    
HELIX   24 AC6 LYS A  620  GLU A  622  5                                   3    
HELIX   25 AC7 CYS A  627  ASN A  640  1                                  14    
HELIX   26 AC8 ASN A  640  SER A  653  1                                  14    
HELIX   27 AC9 VAL A  660  SER A  675  1                                  16    
HELIX   28 AD1 SER A  675  SER A  703  1                                  29    
HELIX   29 AD2 PRO A  707  ARG A  720  1                                  14    
HELIX   30 AD3 GLN A  721  LEU A  728  1                                   8    
HELIX   31 AD4 LEU A  784  GLU A  804  1                                  21    
HELIX   32 AD5 ILE A  834  GLN A  838  1                                   5    
HELIX   33 AD6 ASP A  853  ASN A  863  1                                  11    
HELIX   34 AD7 GLU A  866  LEU A  889  1                                  24    
HELIX   35 AD8 THR A  935  GLN A  943  1                                   9    
HELIX   36 AD9 ASN A  949  HIS A  970  1                                  22    
HELIX   37 AE1 HIS A  970  ARG A  982  1                                  13    
HELIX   38 AE2 ALA A  983  GLY A  985  5                                   3    
HELIX   39 AE3 LEU A  986  SER A  990  5                                   5    
HELIX   40 AE4 CYS A  991  LEU A 1002  1                                  12    
HELIX   41 AE5 THR A 1007  THR A 1029  1                                  23    
HELIX   42 AE6 ASN B  441  SER B  505  1                                  65    
HELIX   43 AE7 SER B  505  ARG B  514  1                                  10    
HELIX   44 AE8 ASN B  517  LYS B  587  1                                  71    
HELIX   45 AE9 ARG B  590  GLY B  599  1                                  10    
SHEET    1 AA1 5 TYR A  31  SER A  37  0                                        
SHEET    2 AA1 5 SER A  19  LEU A  25 -1  N  VAL A  20   O  VAL A  36           
SHEET    3 AA1 5 VAL A  98  ALA A 103  1  O  LEU A  99   N  ASP A  23           
SHEET    4 AA1 5 TYR A  68  ILE A  73 -1  N  VAL A  69   O  VAL A 102           
SHEET    5 AA1 5 GLN A  79  LEU A  82 -1  O  LEU A  82   N  PHE A  70           
SHEET    1 AA2 2 ALA A 189  VAL A 194  0                                        
SHEET    2 AA2 2 PHE A 203  SER A 208 -1  O  PHE A 203   N  VAL A 194           
SHEET    1 AA3 3 TYR A 249  LEU A 250  0                                        
SHEET    2 AA3 3 THR A 240  GLN A 242 -1  N  LEU A 241   O  LEU A 250           
SHEET    3 AA3 3 MET A 276  VAL A 277 -1  O  VAL A 277   N  THR A 240           
SHEET    1 AA4 4 VAL A 370  ASN A 380  0                                        
SHEET    2 AA4 4 PRO A 322  SER A 331 -1  N  ILE A 328   O  TRP A 371           
SHEET    3 AA4 4 ALA A 470  LEU A 475 -1  O  LEU A 472   N  GLN A 329           
SHEET    4 AA4 4 GLY A 435  TYR A 440 -1  N  ARG A 437   O  ILE A 473           
SHEET    1 AA5 3 GLU A 352  MET A 353  0                                        
SHEET    2 AA5 3 LYS A 340  HIS A 349 -1  N  HIS A 349   O  GLU A 352           
SHEET    3 AA5 3 VAL A 363  SER A 364 -1  O  VAL A 363   N  LEU A 341           
SHEET    1 AA6 5 GLU A 352  MET A 353  0                                        
SHEET    2 AA6 5 LYS A 340  HIS A 349 -1  N  HIS A 349   O  GLU A 352           
SHEET    3 AA6 5 ARG A 389  VAL A 397 -1  O  TYR A 395   N  VAL A 342           
SHEET    4 AA6 5 CYS A 416  MET A 424 -1  O  LEU A 423   N  LEU A 390           
SHEET    5 AA6 5 TRP A 442  PRO A 443 -1  O  TRP A 442   N  TRP A 420           
SHEET    1 AA7 2 LEU A 731  GLN A 732  0                                        
SHEET    2 AA7 2 LEU A 740  LEU A 741 -1  O  LEU A 741   N  LEU A 731           
SHEET    1 AA8 3 GLU A 743  VAL A 744  0                                        
SHEET    2 AA8 3 LEU A 759  SER A 764 -1  O  SER A 764   N  GLU A 743           
SHEET    3 AA8 3 THR A 750  PHE A 751 -1  N  THR A 750   O  TRP A 760           
SHEET    1 AA9 5 GLU A 743  VAL A 744  0                                        
SHEET    2 AA9 5 LEU A 759  SER A 764 -1  O  SER A 764   N  GLU A 743           
SHEET    3 AA9 5 VAL A 774  ASN A 780 -1  O  ILE A 776   N  ILE A 761           
SHEET    4 AA9 5 THR A 822  GLU A 826 -1  O  GLY A 823   N  LYS A 779           
SHEET    5 AA9 5 CYS A 815  GLY A 819 -1  N  LEU A 816   O  LEU A 824           
SHEET    1 AB1 3 SER A 831  THR A 833  0                                        
SHEET    2 AB1 3 ILE A 899  ARG A 902 -1  O  ILE A 901   N  ASP A 832           
SHEET    3 AB1 3 LEU A 907  HIS A 909 -1  O  PHE A 908   N  MET A 900           
SITE     1 AC1 15 THR A 750  PHE A 751  MET A 752  PRO A 758                    
SITE     2 AC1 15 TRP A 760  ILE A 777  LYS A 779  TYR A 813                    
SITE     3 AC1 15 ILE A 825  GLU A 826  VAL A 828  THR A 833                    
SITE     4 AC1 15 MET A 900  ILE A 910  ASP A 911                               
CRYST1   90.847  108.579  142.734  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      0.011008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009210  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007006        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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