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Database: PDB
Entry: 4I6Q
LinkDB: 4I6Q
Original site: 4I6Q 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       30-NOV-12   4I6Q              
TITLE     JAK3 KINASE DOMAIN IN COMPLEX WITH 2-PHENOXY-5H-PYRROLO[2,3-          
TITLE    2 B]PYRAZINE-7-CARBOXYLIC ACID ((S)-1-CYCLOPROPYL-ETHYL)-AMIDE         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 811-1124, PROTEIN KINASE DOMAIN;                  
COMPND   5 SYNONYM: JANUS KINASE 3, JAK-3, LEUKOCYTE JANUS KINASE, L-JAK;       
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAK3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE-INHIBITOR COMPLEX, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,A.SHAO                                                  
REVDAT   1   16-OCT-13 4I6Q    0                                                
JRNL        AUTH   S.JAIME-FIGUEROA,J.DE VICENTE,J.HERMANN,A.JAHANGIR,S.JIN,    
JRNL        AUTH 2 A.KUGLSTATTER,S.M.LYNCH,J.MENKE,L.NIU,V.PATEL,A.SHAO,M.SOTH, 
JRNL        AUTH 3 M.D.VU,C.YEE                                                 
JRNL        TITL   DISCOVERY OF A SERIES OF NOVEL                               
JRNL        TITL 2 5H-PYRROLO[2,3-B]PYRAZINE-2-PHENYL ETHERS, AS POTENT JAK3    
JRNL        TITL 3 KINASE INHIBITORS.                                           
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  2522 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23541670                                                     
JRNL        DOI    10.1016/J.BMCL.2013.03.015                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25796                          
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) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1363                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1567                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.3300                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2221                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 92                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.52000                                              
REMARK   3    B22 (A**2) : 0.10000                                              
REMARK   3    B33 (A**2) : -1.62000                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.140         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.140         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.431         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2311 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3124 ; 1.872 ; 1.995       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   274 ; 5.594 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   107 ;34.911 ;22.804       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   393 ;15.704 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;17.759 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   331 ; 0.140 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1776 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   815        A  1102                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0738 -13.7315 -14.9193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0946 T22:   0.0095                                     
REMARK   3      T33:   0.1376 T12:   0.0123                                     
REMARK   3      T13:   0.0178 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3563 L22:   0.4553                                     
REMARK   3      L33:   1.2444 L12:  -0.0376                                     
REMARK   3      L13:  -0.0917 L23:   0.4445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:   0.0061 S13:   0.0154                       
REMARK   3      S21:  -0.0582 S22:  -0.0438 S23:  -0.0365                       
REMARK   3      S31:   0.0424 S32:   0.0112 S33:   0.0199                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4I6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB076373.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25796                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4HVD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.1M MES, 0.2M MGCL, PH     
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
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       23.43700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.63500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.82300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.63500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.43700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.82300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     CYS A   811                                                      
REMARK 465     GLN A   812                                                      
REMARK 465     ASP A   813                                                      
REMARK 465     PRO A   814                                                      
REMARK 465     GLY A   892                                                      
REMARK 465     PRO A   893                                                      
REMARK 465     GLY A   894                                                      
REMARK 465     ARG A   895                                                      
REMARK 465     GLN A   896                                                      
REMARK 465     SER A   897                                                      
REMARK 465     GLY A  1039                                                      
REMARK 465     SER A  1040                                                      
REMARK 465     GLU A  1041                                                      
REMARK 465     ARG A  1042                                                      
REMARK 465     ASP A  1043                                                      
REMARK 465     ARG A  1103                                                      
REMARK 465     GLY A  1104                                                      
REMARK 465     CYS A  1105                                                      
REMARK 465     GLU A  1106                                                      
REMARK 465     THR A  1107                                                      
REMARK 465     HIS A  1108                                                      
REMARK 465     ALA A  1109                                                      
REMARK 465     PHE A  1110                                                      
REMARK 465     THR A  1111                                                      
REMARK 465     ALA A  1112                                                      
REMARK 465     HIS A  1113                                                      
REMARK 465     PRO A  1114                                                      
REMARK 465     GLU A  1115                                                      
REMARK 465     GLY A  1116                                                      
REMARK 465     LYS A  1117                                                      
REMARK 465     HIS A  1118                                                      
REMARK 465     HIS A  1119                                                      
REMARK 465     SER A  1120                                                      
REMARK 465     LEU A  1121                                                      
REMARK 465     SER A  1122                                                      
REMARK 465     PHE A  1123                                                      
REMARK 465     SER A  1124                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1364     O    HOH A  1386              2.11            
REMARK 500   O    HOH A  1322     O    HOH A  1381              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 940   CB  -  CG  -  CD1 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ARG A 953   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 953   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A1006   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 832       54.59     35.40                                   
REMARK 500    ARG A 948      -11.61     80.12                                   
REMARK 500    ALA A 966     -166.37   -122.27                                   
REMARK 500    ASP A 967       80.25     58.65                                   
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 PHU A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1DT A 1202                
DBREF  4I6Q A  811  1124  UNP    P52333   JAK3_HUMAN     811   1124             
SEQADV 4I6Q SER A 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 4I6Q SER A 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQRES   1 A  314  CYS GLN ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS          
SEQRES   2 A  314  TYR ILE SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL          
SEQRES   3 A  314  GLU LEU CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY          
SEQRES   4 A  314  ALA LEU VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO          
SEQRES   5 A  314  ASP GLN GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU          
SEQRES   6 A  314  LYS ALA LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY          
SEQRES   7 A  314  VAL SER TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL          
SEQRES   8 A  314  MET GLU TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU          
SEQRES   9 A  314  GLN ARG HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU          
SEQRES  10 A  314  LEU TYR SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU          
SEQRES  11 A  314  GLY SER ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG          
SEQRES  12 A  314  ASN ILE LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA          
SEQRES  13 A  314  ASP PHE GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP          
SEQRES  14 A  314  TYR TYR VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE          
SEQRES  15 A  314  TRP TYR ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER          
SEQRES  16 A  314  ARG GLN SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR          
SEQRES  17 A  314  GLU LEU PHE THR TYR CYS ASP LYS SER CYS SER PRO SER          
SEQRES  18 A  314  ALA GLU PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL          
SEQRES  19 A  314  PRO ALA LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY          
SEQRES  20 A  314  GLN ARG LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL          
SEQRES  21 A  314  HIS GLU LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN          
SEQRES  22 A  314  ASP ARG PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP          
SEQRES  23 A  314  MET LEU TRP SER GLY SER ARG GLY CYS GLU THR HIS ALA          
SEQRES  24 A  314  PHE THR ALA HIS PRO GLU GLY LYS HIS HIS SER LEU SER          
SEQRES  25 A  314  PHE SER                                                      
HET    PHU  A1201      10                                                       
HET    1DT  A1202      24                                                       
HETNAM     PHU 1-PHENYLUREA                                                     
HETNAM     1DT N-[(1S)-1-CYCLOPROPYLETHYL]-2-PHENOXY-5H-PYRROLO[2,3-            
HETNAM   2 1DT  B]PYRAZINE-7-CARBOXAMIDE                                        
HETSYN     PHU PHENYLUREA                                                       
FORMUL   2  PHU    C7 H8 N2 O                                                   
FORMUL   3  1DT    C18 H18 N4 O2                                                
FORMUL   4  HOH   *92(H2 O)                                                     
HELIX    1   1 GLU A  818  ARG A  820  5                                   3    
HELIX    2   2 GLY A  861  ALA A  877  1                                  17    
HELIX    3   3 CYS A  909  ARG A  918  1                                  10    
HELIX    4   4 ALA A  919  LEU A  921  5                                   3    
HELIX    5   5 ASP A  922  ARG A  943  1                                  22    
HELIX    6   6 ALA A  951  ARG A  953  5                                   3    
HELIX    7   7 PRO A  990  TYR A  994  5                                   5    
HELIX    8   8 ALA A  995  ASN A 1002  1                                   8    
HELIX    9   9 ARG A 1006  THR A 1022  1                                  17    
HELIX   10  10 ASP A 1025  CYS A 1028  5                                   4    
HELIX   11  11 SER A 1029  MET A 1038  1                                  10    
HELIX   12  12 PRO A 1045  GLU A 1056  1                                  12    
HELIX   13  13 PRO A 1067  TRP A 1078  1                                  12    
HELIX   14  14 SER A 1081  ARG A 1085  5                                   5    
HELIX   15  15 SER A 1087  GLY A 1101  1                                  15    
SHEET    1   A 5 LEU A 822  GLY A 831  0                                        
SHEET    2   A 5 GLY A 834  TYR A 841 -1  O  VAL A 836   N  LEU A 828           
SHEET    3   A 5 LEU A 851  LEU A 857 -1  O  VAL A 854   N  GLU A 837           
SHEET    4   A 5 ARG A 899  GLU A 903 -1  O  LEU A 900   N  LYS A 855           
SHEET    5   A 5 TYR A 886  SER A 890 -1  N  ARG A 887   O  VAL A 901           
SHEET    1   B 2 CYS A 945  VAL A 946  0                                        
SHEET    2   B 2 LYS A 972  LEU A 973 -1  O  LYS A 972   N  VAL A 946           
SHEET    1   C 2 ILE A 955  SER A 959  0                                        
SHEET    2   C 2 HIS A 962  ILE A 965 -1  O  LYS A 964   N  LEU A 956           
SHEET    1   D 2 TYR A 980  VAL A 982  0                                        
SHEET    2   D 2 ILE A1003  SER A1005 -1  O  PHE A1004   N  TYR A 981           
SITE     1 AC1  7 PHE A 992  TRP A1011  PRO A1030  MET A1037                    
SITE     2 AC1  7 ARG A1059  LEU A1060  TRP A1078                               
SITE     1 AC2 12 LEU A 828  GLY A 829  VAL A 836  ALA A 853                    
SITE     2 AC2 12 GLU A 903  TYR A 904  LEU A 905  GLY A 908                    
SITE     3 AC2 12 ARG A 953  LEU A 956  ALA A 966  HOH A1347                    
CRYST1   46.874   75.646   89.270  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      0.021334  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013219  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011202        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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