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Database: PDB
Entry: 3TJD
LinkDB: 3TJD
Original site: 3TJD 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       24-AUG-11   3TJD              
TITLE     CO-CRYSTAL STRUCTURE OF JAK2 WITH THIENOPYRIDINE 19                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 837-1132;                                     
COMPND   5 SYNONYM: JANUS KINASE 2, JAK-2;                                      
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 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: JAK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    JAK2, KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.HUANG                                                               
REVDAT   2   28-DEC-11 3TJD    1       JRNL                                     
REVDAT   1   30-NOV-11 3TJD    0                                                
JRNL        AUTH   L.B.SCHENKEL,X.HUANG,A.CHENG,H.L.DEAK,E.DOHERTY,R.EMKEY,     
JRNL        AUTH 2 Y.GU,H.GUNAYDIN,J.L.KIM,J.LEE,R.LOBERG,P.OLIVIERI,           
JRNL        AUTH 3 J.PISTILLO,J.TANG,Q.WAN,H.L.WANG,S.W.WANG,M.C.WELLS,B.WU,    
JRNL        AUTH 4 V.YU,L.LIU,S.GEUNS-MEYER                                     
JRNL        TITL   DISCOVERY OF POTENT AND HIGHLY SELECTIVE THIENOPYRIDINE      
JRNL        TITL 2 JANUS KINASE 2 INHIBITORS.                                   
JRNL        REF    J.MED.CHEM.                   V.  54  8440 2011              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22087750                                                     
JRNL        DOI    10.1021/JM200911R                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18691                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.286                           
REMARK   3   FREE R VALUE                     : 0.312                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
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            : 4768                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3TJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAY-09                          
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 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19812                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.13800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5M OR 1.0 M LICL,  22.5-35% PEG6000,   
REMARK 280  PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.56000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       17.78000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       53.34000            
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: 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     GLY A   835                                                      
REMARK 465     SER A   836                                                      
REMARK 465     GLU A   837                                                      
REMARK 465     ASP A   838                                                      
REMARK 465     ARG A   839                                                      
REMARK 465     ASP A   840                                                      
REMARK 465     PRO A   841                                                      
REMARK 465     THR A   842                                                      
REMARK 465     ALA A   920                                                      
REMARK 465     GLY A   921                                                      
REMARK 465     ARG A   922                                                      
REMARK 465     ARG A   923                                                      
REMARK 465     GLY B   835                                                      
REMARK 465     SER B   836                                                      
REMARK 465     GLU B   837                                                      
REMARK 465     ASP B   838                                                      
REMARK 465     ARG B   839                                                      
REMARK 465     ALA B   920                                                      
REMARK 465     GLY B   921                                                      
REMARK 465     ARG B   922                                                      
REMARK 465     ARG B   923                                                      
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   OH   PTR A  1007     O    HOH A    13              2.15            
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    ARG A 847   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 980   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    PHE A 860       31.80   -153.77                                   
REMARK 500    ASP A 869       78.93   -108.29                                   
REMARK 500    ASN A 874       64.93     32.31                                   
REMARK 500    THR A 875       12.25   -145.73                                   
REMARK 500    HIS A 886       86.19   -152.28                                   
REMARK 500    ARG A 975        2.17     57.24                                   
REMARK 500    ASP A 976       20.42   -145.90                                   
REMARK 500    GLU A 987      -51.28    -26.57                                   
REMARK 500    ASP A1068       40.92    -87.11                                   
REMARK 500    GLN A1070     -132.89    -73.30                                   
REMARK 500    TRP A1106       43.95    -95.13                                   
REMARK 500    ALA A1131      -75.70    -70.36                                   
REMARK 500    GLN B 872       26.77     48.43                                   
REMARK 500    ARG B 975      -21.56     64.72                                   
REMARK 500    ASN B 986      167.12    176.17                                   
REMARK 500    GLU B 987      -19.73    -44.51                                   
REMARK 500    ASP B1068        1.45    -69.25                                   
REMARK 500    GLN B1070     -149.49    -76.44                                   
REMARK 500    ASN B1084       35.31    -87.49                                   
REMARK 500    TRP B1106       43.22    -97.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 847         0.10    SIDE CHAIN                              
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 6TP A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 6TP B 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TJC   RELATED DB: PDB                                   
REMARK 900 CO-CRYSTAL STRUCTURE OF JAK2 WITH THIENOPYRIDINE 8                   
DBREF  3TJD A  837  1132  UNP    O60674   JAK2_HUMAN     837   1132             
DBREF  3TJD B  837  1132  UNP    O60674   JAK2_HUMAN     837   1132             
SEQADV 3TJD GLY A  835  UNP  O60674              EXPRESSION TAG                 
SEQADV 3TJD SER A  836  UNP  O60674              EXPRESSION TAG                 
SEQADV 3TJD GLY B  835  UNP  O60674              EXPRESSION TAG                 
SEQADV 3TJD SER B  836  UNP  O60674              EXPRESSION TAG                 
SEQRES   1 A  298  GLY SER GLU ASP ARG ASP PRO THR GLN PHE GLU GLU ARG          
SEQRES   2 A  298  HIS LEU LYS PHE LEU GLN GLN LEU GLY LYS GLY ASN PHE          
SEQRES   3 A  298  GLY SER VAL GLU MET CYS ARG TYR ASP PRO LEU GLN ASP          
SEQRES   4 A  298  ASN THR GLY GLU VAL VAL ALA VAL LYS LYS LEU GLN HIS          
SEQRES   5 A  298  SER THR GLU GLU HIS LEU ARG ASP PHE GLU ARG GLU ILE          
SEQRES   6 A  298  GLU ILE LEU LYS SER LEU GLN HIS ASP ASN ILE VAL LYS          
SEQRES   7 A  298  TYR LYS GLY VAL CYS TYR SER ALA GLY ARG ARG ASN LEU          
SEQRES   8 A  298  LYS LEU ILE MET GLU TYR LEU PRO TYR GLY SER LEU ARG          
SEQRES   9 A  298  ASP TYR LEU GLN LYS HIS LYS GLU ARG ILE ASP HIS ILE          
SEQRES  10 A  298  LYS LEU LEU GLN TYR THR SER GLN ILE CYS LYS GLY MET          
SEQRES  11 A  298  GLU TYR LEU GLY THR LYS ARG TYR ILE HIS ARG ASP LEU          
SEQRES  12 A  298  ALA THR ARG ASN ILE LEU VAL GLU ASN GLU ASN ARG VAL          
SEQRES  13 A  298  LYS ILE GLY ASP PHE GLY LEU THR LYS VAL LEU PRO GLN          
SEQRES  14 A  298  ASP LYS GLU PTR PTR LYS VAL LYS GLU PRO GLY GLU SER          
SEQRES  15 A  298  PRO ILE PHE TRP TYR ALA PRO GLU SER LEU THR GLU SER          
SEQRES  16 A  298  LYS PHE SER VAL ALA SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  17 A  298  VAL LEU TYR GLU LEU PHE THR TYR ILE GLU LYS SER LYS          
SEQRES  18 A  298  SER PRO PRO ALA GLU PHE MET ARG MET ILE GLY ASN ASP          
SEQRES  19 A  298  LYS GLN GLY GLN MET ILE VAL PHE HIS LEU ILE GLU LEU          
SEQRES  20 A  298  LEU LYS ASN ASN GLY ARG LEU PRO ARG PRO ASP GLY CYS          
SEQRES  21 A  298  PRO ASP GLU ILE TYR MET ILE MET THR GLU CYS TRP ASN          
SEQRES  22 A  298  ASN ASN VAL ASN GLN ARG PRO SER PHE ARG ASP LEU ALA          
SEQRES  23 A  298  LEU ARG VAL ASP GLN ILE ARG ASP ASN MET ALA GLY              
SEQRES   1 B  298  GLY SER GLU ASP ARG ASP PRO THR GLN PHE GLU GLU ARG          
SEQRES   2 B  298  HIS LEU LYS PHE LEU GLN GLN LEU GLY LYS GLY ASN PHE          
SEQRES   3 B  298  GLY SER VAL GLU MET CYS ARG TYR ASP PRO LEU GLN ASP          
SEQRES   4 B  298  ASN THR GLY GLU VAL VAL ALA VAL LYS LYS LEU GLN HIS          
SEQRES   5 B  298  SER THR GLU GLU HIS LEU ARG ASP PHE GLU ARG GLU ILE          
SEQRES   6 B  298  GLU ILE LEU LYS SER LEU GLN HIS ASP ASN ILE VAL LYS          
SEQRES   7 B  298  TYR LYS GLY VAL CYS TYR SER ALA GLY ARG ARG ASN LEU          
SEQRES   8 B  298  LYS LEU ILE MET GLU TYR LEU PRO TYR GLY SER LEU ARG          
SEQRES   9 B  298  ASP TYR LEU GLN LYS HIS LYS GLU ARG ILE ASP HIS ILE          
SEQRES  10 B  298  LYS LEU LEU GLN TYR THR SER GLN ILE CYS LYS GLY MET          
SEQRES  11 B  298  GLU TYR LEU GLY THR LYS ARG TYR ILE HIS ARG ASP LEU          
SEQRES  12 B  298  ALA THR ARG ASN ILE LEU VAL GLU ASN GLU ASN ARG VAL          
SEQRES  13 B  298  LYS ILE GLY ASP PHE GLY LEU THR LYS VAL LEU PRO GLN          
SEQRES  14 B  298  ASP LYS GLU PTR PTR LYS VAL LYS GLU PRO GLY GLU SER          
SEQRES  15 B  298  PRO ILE PHE TRP TYR ALA PRO GLU SER LEU THR GLU SER          
SEQRES  16 B  298  LYS PHE SER VAL ALA SER ASP VAL TRP SER PHE GLY VAL          
SEQRES  17 B  298  VAL LEU TYR GLU LEU PHE THR TYR ILE GLU LYS SER LYS          
SEQRES  18 B  298  SER PRO PRO ALA GLU PHE MET ARG MET ILE GLY ASN ASP          
SEQRES  19 B  298  LYS GLN GLY GLN MET ILE VAL PHE HIS LEU ILE GLU LEU          
SEQRES  20 B  298  LEU LYS ASN ASN GLY ARG LEU PRO ARG PRO ASP GLY CYS          
SEQRES  21 B  298  PRO ASP GLU ILE TYR MET ILE MET THR GLU CYS TRP ASN          
SEQRES  22 B  298  ASN ASN VAL ASN GLN ARG PRO SER PHE ARG ASP LEU ALA          
SEQRES  23 B  298  LEU ARG VAL ASP GLN ILE ARG ASP ASN MET ALA GLY              
MODRES 3TJD PTR A 1007  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3TJD PTR A 1008  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3TJD PTR B 1007  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3TJD PTR B 1008  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1007      16                                                       
HET    PTR  A1008      16                                                       
HET    PTR  B1007      16                                                       
HET    PTR  B1008      16                                                       
HET    6TP  A   1      28                                                       
HET    6TP  B   1      28                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     6TP 4-AMINO-2-[4-(TERT-BUTYLSULFAMOYL)PHENYL]-N-                     
HETNAM   2 6TP  METHYLTHIENO[3,2-C]PYRIDINE-7-CARBOXAMIDE                       
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   3  6TP    2(C19 H22 N4 O3 S2)                                          
FORMUL   5  HOH   *62(H2 O)                                                     
HELIX    1   1 GLU A  845  ARG A  847  5                                   3    
HELIX    2   2 THR A  888  SER A  904  1                                  17    
HELIX    3   3 SER A  936  HIS A  944  1                                   9    
HELIX    4   4 ASP A  949  THR A  969  1                                  21    
HELIX    5   5 ALA A  978  ARG A  980  5                                   3    
HELIX    6   6 PRO A 1017  TYR A 1021  5                                   5    
HELIX    7   7 ALA A 1022  SER A 1029  1                                   8    
HELIX    8   8 SER A 1032  THR A 1049  1                                  18    
HELIX    9   9 GLU A 1052  LYS A 1055  5                                   4    
HELIX   10  10 SER A 1056  GLY A 1066  1                                  11    
HELIX   11  11 GLN A 1072  ASN A 1084  1                                  13    
HELIX   12  12 PRO A 1095  TRP A 1106  1                                  12    
HELIX   13  13 ASN A 1109  ARG A 1113  5                                   5    
HELIX   14  14 SER A 1115  GLY A 1132  1                                  18    
HELIX   15  15 GLU B  845  ARG B  847  5                                   3    
HELIX   16  16 THR B  888  LEU B  905  1                                  18    
HELIX   17  17 SER B  936  HIS B  944  1                                   9    
HELIX   18  18 ASP B  949  LYS B  970  1                                  22    
HELIX   19  19 ALA B 1022  SER B 1029  1                                   8    
HELIX   20  20 SER B 1032  THR B 1049  1                                  18    
HELIX   21  21 GLU B 1052  LYS B 1055  5                                   4    
HELIX   22  22 SER B 1056  GLY B 1066  1                                  11    
HELIX   23  23 MET B 1073  ASN B 1084  1                                  12    
HELIX   24  24 PRO B 1095  TRP B 1106  1                                  12    
HELIX   25  25 ASN B 1109  ARG B 1113  5                                   5    
HELIX   26  26 SER B 1115  GLY B 1132  1                                  18    
SHEET    1   A 5 LEU A 849  LYS A 857  0                                        
SHEET    2   A 5 SER A 862  TYR A 868 -1  O  MET A 865   N  GLN A 853           
SHEET    3   A 5 VAL A 878  LYS A 883 -1  O  VAL A 879   N  CYS A 866           
SHEET    4   A 5 LYS A 926  GLU A 930 -1  O  MET A 929   N  ALA A 880           
SHEET    5   A 5 TYR A 913  CYS A 917 -1  N  GLY A 915   O  ILE A 928           
SHEET    1   B 2 TYR A 972  ILE A 973  0                                        
SHEET    2   B 2 LYS A 999  VAL A1000 -1  O  LYS A 999   N  ILE A 973           
SHEET    1   C 2 ILE A 982  ASN A 986  0                                        
SHEET    2   C 2 ARG A 989  ILE A 992 -1  O  LYS A 991   N  LEU A 983           
SHEET    1   D 2 PTR A1008  LYS A1009  0                                        
SHEET    2   D 2 LYS A1030  PHE A1031 -1  O  PHE A1031   N  PTR A1008           
SHEET    1   E 5 LEU B 849  LYS B 857  0                                        
SHEET    2   E 5 GLY B 861  TYR B 868 -1  O  MET B 865   N  GLN B 853           
SHEET    3   E 5 GLU B 877  LEU B 884 -1  O  VAL B 881   N  GLU B 864           
SHEET    4   E 5 LYS B 926  GLU B 930 -1  O  MET B 929   N  ALA B 880           
SHEET    5   E 5 TYR B 913  CYS B 917 -1  N  LYS B 914   O  ILE B 928           
SHEET    1   F 2 TYR B 972  ILE B 973  0                                        
SHEET    2   F 2 LYS B 999  VAL B1000 -1  O  LYS B 999   N  ILE B 973           
SHEET    1   G 2 ILE B 982  ASN B 986  0                                        
SHEET    2   G 2 ARG B 989  ILE B 992 -1  O  LYS B 991   N  LEU B 983           
SHEET    1   H 2 PTR B1008  LYS B1009  0                                        
SHEET    2   H 2 LYS B1030  PHE B1031 -1  O  PHE B1031   N  PTR B1008           
LINK         C   GLU A1006                 N   PTR A1007     1555   1555  1.32  
LINK         C   PTR A1007                 N   PTR A1008     1555   1555  1.33  
LINK         C   PTR A1008                 N   LYS A1009     1555   1555  1.34  
LINK         C   GLU B1006                 N   PTR B1007     1555   1555  1.33  
LINK         C   PTR B1007                 N   PTR B1008     1555   1555  1.32  
LINK         C   PTR B1008                 N   LYS B1009     1555   1555  1.33  
SITE     1 AC1 13 HOH A  19  LEU A 855  LYS A 857  VAL A 863                    
SITE     2 AC1 13 ALA A 880  GLU A 930  TYR A 931  LEU A 932                    
SITE     3 AC1 13 GLY A 935  ARG A 980  ASN A 981  LEU A 983                    
SITE     4 AC1 13 ASP A 994                                                     
SITE     1 AC2 12 LEU B 855  GLY B 858  ALA B 880  LYS B 882                    
SITE     2 AC2 12 GLU B 930  TYR B 931  LEU B 932  PRO B 933                    
SITE     3 AC2 12 GLY B 935  ARG B 980  ASN B 981  LEU B 983                    
CRYST1  111.820  111.820   71.120  90.00  90.00  90.00 P 41          8          
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      0.008943  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008943  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014061        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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