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Database: PDB
Entry: 4QPS
LinkDB: 4QPS
Original site: 4QPS 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-JUN-14   4QPS              
TITLE     CRYSTAL STRUCTURE OF JAK3 COMPLEXED TO N-[3-(6-PHENYLAMINO-PYRAZIN-2- 
TITLE    2 YL)-3H-BENZOIMIDAZOL-5-YL]-ACRYLAMIDE                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: JAK3, UNP RESIDUES 811-1103;                               
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 CATALYTIC DOMAIN, TRANSFERASE, TRANSFERASE-TRANSFERASE         
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.ARGIRIADI,E.R.GOEDKEN                                             
REVDAT   2   11-MAR-15 4QPS    1       JRNL                                     
REVDAT   1   14-JAN-15 4QPS    0                                                
JRNL        AUTH   E.R.GOEDKEN,M.A.ARGIRIADI,D.L.BANACH,B.A.FIAMENGO,S.E.FOLEY, 
JRNL        AUTH 2 K.E.FRANK,J.S.GEORGE,C.M.HARRIS,A.D.HOBSON,D.C.IHLE,         
JRNL        AUTH 3 D.MARCOTTE,P.J.MERTA,M.E.MICHALAK,S.E.MURDOCK,M.J.TOMLINSON, 
JRNL        AUTH 4 J.W.VOSS                                                     
JRNL        TITL   TRICYCLIC COVALENT INHIBITORS SELECTIVELY TARGET JAK3        
JRNL        TITL 2 THROUGH AN ACTIVE SITE THIOL.                                
JRNL        REF    J.BIOL.CHEM.                  V. 290  4573 2015              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   25552479                                                     
JRNL        DOI    10.1074/JBC.M114.595181                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.7                                         
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 47010                          
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)  : 0.207                          
REMARK   3   FREE R VALUE                      : 0.251                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2382                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.85                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 98.52                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3375                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2325                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3221                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2316                   
REMARK   3   BIN FREE R VALUE                        : 0.2517                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.56                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 154                      
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            : 4352                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 199                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.21820                                              
REMARK   3    B22 (A**2) : -7.86150                                             
REMARK   3    B33 (A**2) : -0.35680                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.28390                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.223               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.152               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4586   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6209   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1578   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 98     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 689    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4586   ; 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   : 549    ; 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   : 5613   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.04                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.32                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.60                    
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 4QPS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086359.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-3350, 0.2 M AMMONIUM SULFATE     
REMARK 280  AND 0.1 M BISTRIS PH 5.5, VAPOR DIFFUSION, TEMPERATURE 291K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       21.93850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: C                                     
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     PHE A   833                                                      
REMARK 465     GLN A   858                                                      
REMARK 465     HIS A   859                                                      
REMARK 465     SER A   860                                                      
REMARK 465     GLY A   861                                                      
REMARK 465     PRO A   862                                                      
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     ARG A   984                                                      
REMARK 465     GLU A   985                                                      
REMARK 465     PRO A   986                                                      
REMARK 465     GLY A   987                                                      
REMARK 465     GLN A   988                                                      
REMARK 465     SER A   989                                                      
REMARK 465     GLY A  1101                                                      
REMARK 465     SER A  1102                                                      
REMARK 465     ARG A  1103                                                      
REMARK 465     CYS C   811                                                      
REMARK 465     GLN C   812                                                      
REMARK 465     ASP C   813                                                      
REMARK 465     GLN C   858                                                      
REMARK 465     HIS C   859                                                      
REMARK 465     ARG C   984                                                      
REMARK 465     GLU C   985                                                      
REMARK 465     PRO C   986                                                      
REMARK 465     GLY C   987                                                      
REMARK 465     GLN C   988                                                      
REMARK 465     GLU C  1041                                                      
REMARK 465     ARG C  1042                                                      
REMARK 465     ASP C  1043                                                      
REMARK 465     VAL C  1044                                                      
REMARK 465     PRO C  1045                                                      
REMARK 465     ALA C  1046                                                      
REMARK 465     ARG C  1103                                                      
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     ARG A 866    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 866    CG   CD   NE   CZ   NH1  NH2                        
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    ASP A 842       78.32   -118.31                                   
REMARK 500    ARG A 948      -53.21     74.55                                   
REMARK 500    ASP A 967       86.82     64.52                                   
REMARK 500    ARG C 948      -46.68     73.92                                   
REMARK 500    ASP C 967       91.64     60.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A1021        24.2      L          L   OUTSIDE RANGE           
REMARK 500    MET C1038        23.5      L          L   OUTSIDE RANGE           
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 37Q A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 37Q C 1201                
DBREF  4QPS A  811  1103  UNP    P52333   JAK3_HUMAN     811   1103             
DBREF  4QPS C  811  1103  UNP    P52333   JAK3_HUMAN     811   1103             
SEQADV 4QPS ALA A  949  UNP  P52333    ASP   949 ENGINEERED MUTATION            
SEQADV 4QPS SER A 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 4QPS SER A 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQADV 4QPS ALA C  949  UNP  P52333    ASP   949 ENGINEERED MUTATION            
SEQADV 4QPS SER C 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 4QPS SER C 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQRES   1 A  293  CYS GLN ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS          
SEQRES   2 A  293  TYR ILE SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL          
SEQRES   3 A  293  GLU LEU CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY          
SEQRES   4 A  293  ALA LEU VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO          
SEQRES   5 A  293  ASP GLN GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU          
SEQRES   6 A  293  LYS ALA LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY          
SEQRES   7 A  293  VAL SER TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL          
SEQRES   8 A  293  MET GLU TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU          
SEQRES   9 A  293  GLN ARG HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU          
SEQRES  10 A  293  LEU TYR SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU          
SEQRES  11 A  293  GLY SER ARG ARG CYS VAL HIS ARG ALA LEU ALA ALA ARG          
SEQRES  12 A  293  ASN ILE LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA          
SEQRES  13 A  293  ASP PHE GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP          
SEQRES  14 A  293  TYR TYR VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE          
SEQRES  15 A  293  TRP TYR ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER          
SEQRES  16 A  293  ARG GLN SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR          
SEQRES  17 A  293  GLU LEU PHE THR TYR CYS ASP LYS SER CYS SER PRO SER          
SEQRES  18 A  293  ALA GLU PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL          
SEQRES  19 A  293  PRO ALA LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY          
SEQRES  20 A  293  GLN ARG LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL          
SEQRES  21 A  293  HIS GLU LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN          
SEQRES  22 A  293  ASP ARG PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP          
SEQRES  23 A  293  MET LEU TRP SER GLY SER ARG                                  
SEQRES   1 C  293  CYS GLN ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS          
SEQRES   2 C  293  TYR ILE SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL          
SEQRES   3 C  293  GLU LEU CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY          
SEQRES   4 C  293  ALA LEU VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO          
SEQRES   5 C  293  ASP GLN GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU          
SEQRES   6 C  293  LYS ALA LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY          
SEQRES   7 C  293  VAL SER TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL          
SEQRES   8 C  293  MET GLU TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU          
SEQRES   9 C  293  GLN ARG HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU          
SEQRES  10 C  293  LEU TYR SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU          
SEQRES  11 C  293  GLY SER ARG ARG CYS VAL HIS ARG ALA LEU ALA ALA ARG          
SEQRES  12 C  293  ASN ILE LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA          
SEQRES  13 C  293  ASP PHE GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP          
SEQRES  14 C  293  TYR TYR VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE          
SEQRES  15 C  293  TRP TYR ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER          
SEQRES  16 C  293  ARG GLN SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR          
SEQRES  17 C  293  GLU LEU PHE THR TYR CYS ASP LYS SER CYS SER PRO SER          
SEQRES  18 C  293  ALA GLU PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL          
SEQRES  19 C  293  PRO ALA LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY          
SEQRES  20 C  293  GLN ARG LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL          
SEQRES  21 C  293  HIS GLU LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN          
SEQRES  22 C  293  ASP ARG PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP          
SEQRES  23 C  293  MET LEU TRP SER GLY SER ARG                                  
HET    37Q  A1201      27                                                       
HET    37Q  C1201      27                                                       
HETNAM     37Q N-{1-[6-(PHENYLAMINO)PYRAZIN-2-YL]-1H-BENZIMIDAZOL-6-            
HETNAM   2 37Q  YL}PROP-2-ENAMIDE                                               
FORMUL   3  37Q    2(C20 H16 N6 O)                                              
FORMUL   5  HOH   *199(H2 O)                                                    
HELIX    1   1 GLU A  818  ARG A  820  5                                   3    
HELIX    2   2 GLN A  864  ALA A  877  1                                  14    
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 ALA A  995  ASN A 1002  1                                   8    
HELIX    8   8 ARG A 1006  THR A 1022  1                                  17    
HELIX    9   9 ASP A 1025  CYS A 1028  5                                   4    
HELIX   10  10 SER A 1029  MET A 1038  1                                  10    
HELIX   11  11 ALA A 1046  GLU A 1056  1                                  11    
HELIX   12  12 PRO A 1067  TRP A 1078  1                                  12    
HELIX   13  13 SER A 1081  ARG A 1085  5                                   5    
HELIX   14  14 SER A 1087  SER A 1100  1                                  14    
HELIX   15  15 GLU C  818  ARG C  820  5                                   3    
HELIX   16  16 GLY C  861  LEU C  878  1                                  18    
HELIX   17  17 CYS C  909  ARG C  918  1                                  10    
HELIX   18  18 ALA C  919  LEU C  921  5                                   3    
HELIX   19  19 ASP C  922  ARG C  943  1                                  22    
HELIX   20  20 ALA C  951  ARG C  953  5                                   3    
HELIX   21  21 PRO C  990  TYR C  994  5                                   5    
HELIX   22  22 ALA C  995  ASN C 1002  1                                   8    
HELIX   23  23 ARG C 1006  THR C 1022  1                                  17    
HELIX   24  24 ASP C 1025  CYS C 1028  5                                   4    
HELIX   25  25 SER C 1029  GLY C 1039  1                                  11    
HELIX   26  26 SER C 1048  GLY C 1057  1                                  10    
HELIX   27  27 PRO C 1067  TRP C 1078  1                                  12    
HELIX   28  28 SER C 1081  ARG C 1085  5                                   5    
HELIX   29  29 SER C 1087  GLY C 1101  1                                  15    
SHEET    1   A 6 THR A 815  PHE A 817  0                                        
SHEET    2   A 6 TYR A 886  SER A 890  1  O  VAL A 889   N  PHE A 817           
SHEET    3   A 6 ARG A 899  GLU A 903 -1  O  VAL A 901   N  GLY A 888           
SHEET    4   A 6 LEU A 851  GLN A 856 -1  N  ALA A 853   O  MET A 902           
SHEET    5   A 6 SER A 835  TYR A 841 -1  N  CYS A 839   O  VAL A 852           
SHEET    6   A 6 LEU A 822  LYS A 830 -1  N  LYS A 823   O  ARG A 840           
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           
SHEET    1   E 6 THR C 815  ILE C 816  0                                        
SHEET    2   E 6 TYR C 886  TYR C 891  1  O  ARG C 887   N  THR C 815           
SHEET    3   E 6 LEU C 898  GLU C 903 -1  O  VAL C 901   N  GLY C 888           
SHEET    4   E 6 ALA C 850  GLN C 856 -1  N  ALA C 853   O  MET C 902           
SHEET    5   E 6 GLY C 834  TYR C 841 -1  N  GLU C 837   O  VAL C 854           
SHEET    6   E 6 LEU C 822  GLY C 831 -1  N  LYS C 823   O  ARG C 840           
SHEET    1   F 2 CYS C 945  VAL C 946  0                                        
SHEET    2   F 2 LYS C 972  LEU C 973 -1  O  LYS C 972   N  VAL C 946           
SHEET    1   G 2 ILE C 955  SER C 959  0                                        
SHEET    2   G 2 HIS C 962  ILE C 965 -1  O  LYS C 964   N  LEU C 956           
SHEET    1   H 2 TYR C 980  VAL C 982  0                                        
SHEET    2   H 2 ILE C1003  SER C1005 -1  O  PHE C1004   N  TYR C 981           
LINK         SG  CYS A 909                 C1  37Q A1201     1555   1555  1.80  
LINK         SG  CYS C 909                 C1  37Q C1201     1555   1555  1.81  
CISPEP   1 GLY C  892    PRO C  893          0         2.69                     
SITE     1 AC1 13 LEU A 828  VAL A 836  ALA A 853  MET A 902                    
SITE     2 AC1 13 GLU A 903  TYR A 904  LEU A 905  GLY A 908                    
SITE     3 AC1 13 CYS A 909  ASP A 912  ARG A 953  LEU A 956                    
SITE     4 AC1 13 HOH A1385                                                     
SITE     1 AC2 16 LEU C 828  GLY C 829  PHE C 833  VAL C 836                    
SITE     2 AC2 16 ALA C 853  GLU C 903  TYR C 904  LEU C 905                    
SITE     3 AC2 16 GLY C 908  CYS C 909  ARG C 953  LEU C 956                    
SITE     4 AC2 16 ASP C 967  HOH C1301  HOH C1307  HOH C1365                    
CRYST1   79.511   43.877   81.695  90.00 115.26  90.00 P 1 21 1      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      0.012577  0.000000  0.005934        0.00000                         
SCALE2      0.000000  0.022791  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013535        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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