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Database: PDB
Entry: 4JI9
LinkDB: 4JI9
Original site: 4JI9 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       05-MAR-13   4JI9              
TITLE     JAK2 KINASE (JH1 DOMAIN) IN COMPLEX WITH TG101209                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: JH1 DOMAIN, UNP RESIDUES 833-1132;                         
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    PROTEIN KINASE, PHOSPHO-TRANSFER CATALYST, TRANSFERASE-TRANSFERASE    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,M.ULTSCH                                                  
REVDAT   2   21-AUG-13 4JI9    1       JRNL                                     
REVDAT   1   07-AUG-13 4JI9    0                                                
JRNL        AUTH   M.SIU,R.PASTOR,W.LIU,K.BARRETT,M.BERRY,W.S.BLAIR,C.CHANG,    
JRNL        AUTH 2 J.Z.CHEN,C.EIGENBROT,N.GHILARDI,P.GIBBONS,H.HE,C.A.HURLEY,   
JRNL        AUTH 3 J.R.KENNY,S.CYRUS KHOJASTEH,H.LE,L.LEE,J.P.LYSSIKATOS,       
JRNL        AUTH 4 S.MAGNUSON,R.PULK,V.TSUI,M.ULTSCH,Y.XIAO,B.Y.ZHU,D.SAMPATH   
JRNL        TITL   2-AMINO-[1,2,4]TRIAZOLO[1,5-A]PYRIDINES AS JAK2 INHIBITORS.  
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  5014 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23870430                                                     
JRNL        DOI    10.1016/J.BMCL.2013.06.008                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 33915                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 846                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.53                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4601                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4779                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 72                                      
REMARK   3   SOLVENT ATOMS            : 110                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.81000                                              
REMARK   3    B22 (A**2) : 0.81000                                              
REMARK   3    B33 (A**2) : -1.63000                                             
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): 0.300         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.357         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4960 ; 0.006 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6693 ; 1.173 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   572 ; 5.604 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   248 ;37.950 ;24.274       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   915 ;15.073 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;17.165 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   697 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3747 ; 0.004 ; 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4JI9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078079.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33915                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PDB ENTRY 2B7A               
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   (%): 60.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, PEG8000, PH 6, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 300K                           
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       35.23350            
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       17.61675            
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       52.85025            
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     SER A   833                                                      
REMARK 465     GLY A   834                                                      
REMARK 465     ALA A   835                                                      
REMARK 465     PHE 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     SER B   833                                                      
REMARK 465     GLY B   834                                                      
REMARK 465     ALA B   835                                                      
REMARK 465     PHE B   836                                                      
REMARK 465     GLU B   837                                                      
REMARK 465     ASP B   838                                                      
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: 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 859     -115.19     59.21                                   
REMARK 500    GLN A 872       19.93     51.12                                   
REMARK 500    ARG A 975      -32.58     76.43                                   
REMARK 500    TRP A1106       38.09    -89.95                                   
REMARK 500    ASP B 840       98.83     17.29                                   
REMARK 500    ARG B 975      -23.37     75.70                                   
REMARK 500    GLU B1012      107.35     78.19                                   
REMARK 500    TRP B1106       39.70    -95.66                                   
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 1M3 A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1M3 B 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JIA   RELATED DB: PDB                                   
DBREF  4JI9 A  833  1132  UNP    O60674   JAK2_HUMAN     833   1132             
DBREF  4JI9 B  833  1132  UNP    O60674   JAK2_HUMAN     833   1132             
SEQRES   1 A  300  SER GLY ALA PHE GLU ASP ARG ASP PRO THR GLN PHE GLU          
SEQRES   2 A  300  GLU ARG HIS LEU LYS PHE LEU GLN GLN LEU GLY LYS GLY          
SEQRES   3 A  300  ASN PHE GLY SER VAL GLU MET CYS ARG TYR ASP PRO LEU          
SEQRES   4 A  300  GLN ASP ASN THR GLY GLU VAL VAL ALA VAL LYS LYS LEU          
SEQRES   5 A  300  GLN HIS SER THR GLU GLU HIS LEU ARG ASP PHE GLU ARG          
SEQRES   6 A  300  GLU ILE GLU ILE LEU LYS SER LEU GLN HIS ASP ASN ILE          
SEQRES   7 A  300  VAL LYS TYR LYS GLY VAL CYS TYR SER ALA GLY ARG ARG          
SEQRES   8 A  300  ASN LEU LYS LEU ILE MET GLU TYR LEU PRO TYR GLY SER          
SEQRES   9 A  300  LEU ARG ASP TYR LEU GLN LYS HIS LYS GLU ARG ILE ASP          
SEQRES  10 A  300  HIS ILE LYS LEU LEU GLN TYR THR SER GLN ILE CYS LYS          
SEQRES  11 A  300  GLY MET GLU TYR LEU GLY THR LYS ARG TYR ILE HIS ARG          
SEQRES  12 A  300  ASP LEU ALA THR ARG ASN ILE LEU VAL GLU ASN GLU ASN          
SEQRES  13 A  300  ARG VAL LYS ILE GLY ASP PHE GLY LEU THR LYS VAL LEU          
SEQRES  14 A  300  PRO GLN ASP LYS GLU PTR PTR LYS VAL LYS GLU PRO GLY          
SEQRES  15 A  300  GLU SER PRO ILE PHE TRP TYR ALA PRO GLU SER LEU THR          
SEQRES  16 A  300  GLU SER LYS PHE SER VAL ALA SER ASP VAL TRP SER PHE          
SEQRES  17 A  300  GLY VAL VAL LEU TYR GLU LEU PHE THR TYR ILE GLU LYS          
SEQRES  18 A  300  SER LYS SER PRO PRO ALA GLU PHE MET ARG MET ILE GLY          
SEQRES  19 A  300  ASN ASP LYS GLN GLY GLN MET ILE VAL PHE HIS LEU ILE          
SEQRES  20 A  300  GLU LEU LEU LYS ASN ASN GLY ARG LEU PRO ARG PRO ASP          
SEQRES  21 A  300  GLY CYS PRO ASP GLU ILE TYR MET ILE MET THR GLU CYS          
SEQRES  22 A  300  TRP ASN ASN ASN VAL ASN GLN ARG PRO SER PHE ARG ASP          
SEQRES  23 A  300  LEU ALA LEU ARG VAL ASP GLN ILE ARG ASP ASN MET ALA          
SEQRES  24 A  300  GLY                                                          
SEQRES   1 B  300  SER GLY ALA PHE GLU ASP ARG ASP PRO THR GLN PHE GLU          
SEQRES   2 B  300  GLU ARG HIS LEU LYS PHE LEU GLN GLN LEU GLY LYS GLY          
SEQRES   3 B  300  ASN PHE GLY SER VAL GLU MET CYS ARG TYR ASP PRO LEU          
SEQRES   4 B  300  GLN ASP ASN THR GLY GLU VAL VAL ALA VAL LYS LYS LEU          
SEQRES   5 B  300  GLN HIS SER THR GLU GLU HIS LEU ARG ASP PHE GLU ARG          
SEQRES   6 B  300  GLU ILE GLU ILE LEU LYS SER LEU GLN HIS ASP ASN ILE          
SEQRES   7 B  300  VAL LYS TYR LYS GLY VAL CYS TYR SER ALA GLY ARG ARG          
SEQRES   8 B  300  ASN LEU LYS LEU ILE MET GLU TYR LEU PRO TYR GLY SER          
SEQRES   9 B  300  LEU ARG ASP TYR LEU GLN LYS HIS LYS GLU ARG ILE ASP          
SEQRES  10 B  300  HIS ILE LYS LEU LEU GLN TYR THR SER GLN ILE CYS LYS          
SEQRES  11 B  300  GLY MET GLU TYR LEU GLY THR LYS ARG TYR ILE HIS ARG          
SEQRES  12 B  300  ASP LEU ALA THR ARG ASN ILE LEU VAL GLU ASN GLU ASN          
SEQRES  13 B  300  ARG VAL LYS ILE GLY ASP PHE GLY LEU THR LYS VAL LEU          
SEQRES  14 B  300  PRO GLN ASP LYS GLU PTR PTR LYS VAL LYS GLU PRO GLY          
SEQRES  15 B  300  GLU SER PRO ILE PHE TRP TYR ALA PRO GLU SER LEU THR          
SEQRES  16 B  300  GLU SER LYS PHE SER VAL ALA SER ASP VAL TRP SER PHE          
SEQRES  17 B  300  GLY VAL VAL LEU TYR GLU LEU PHE THR TYR ILE GLU LYS          
SEQRES  18 B  300  SER LYS SER PRO PRO ALA GLU PHE MET ARG MET ILE GLY          
SEQRES  19 B  300  ASN ASP LYS GLN GLY GLN MET ILE VAL PHE HIS LEU ILE          
SEQRES  20 B  300  GLU LEU LEU LYS ASN ASN GLY ARG LEU PRO ARG PRO ASP          
SEQRES  21 B  300  GLY CYS PRO ASP GLU ILE TYR MET ILE MET THR GLU CYS          
SEQRES  22 B  300  TRP ASN ASN ASN VAL ASN GLN ARG PRO SER PHE ARG ASP          
SEQRES  23 B  300  LEU ALA LEU ARG VAL ASP GLN ILE ARG ASP ASN MET ALA          
SEQRES  24 B  300  GLY                                                          
MODRES 4JI9 PTR A 1007  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4JI9 PTR A 1008  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4JI9 PTR B 1007  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4JI9 PTR B 1008  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1007      16                                                       
HET    PTR  A1008      16                                                       
HET    PTR  B1007      16                                                       
HET    PTR  B1008      16                                                       
HET    1M3  A1201      36                                                       
HET    1M3  B1201      36                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     1M3 N-TERT-BUTYL-3-[(5-METHYL-2-{[4-(4-METHYLPIPERAZIN-1-            
HETNAM   2 1M3  YL)PHENYL]AMINO}PYRIMIDIN-4-YL)                                 
HETNAM   3 1M3  AMINO]BENZENESULFONAMIDE                                        
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   3  1M3    2(C26 H35 N7 O2 S)                                           
FORMUL   5  HOH   *110(H2 O)                                                    
HELIX    1   1 GLU A  845  ARG A  847  5                                   3    
HELIX    2   2 GLU A  889  SER A  904  1                                  16    
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  GLU A 1028  1                                   7    
HELIX    8   8 VAL A 1033  THR A 1049  1                                  17    
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 1070  ASN A 1084  1                                  15    
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  LYS B  945  1                                  10    
HELIX   18  18 ASP B  949  LYS B  970  1                                  22    
HELIX   19  19 PRO B 1017  TYR B 1021  5                                   5    
HELIX   20  20 ALA B 1022  SER B 1029  1                                   8    
HELIX   21  21 SER B 1032  THR B 1049  1                                  18    
HELIX   22  22 GLU B 1052  LYS B 1055  5                                   4    
HELIX   23  23 SER B 1056  GLY B 1066  1                                  11    
HELIX   24  24 GLN B 1070  ASN B 1084  1                                  15    
HELIX   25  25 PRO B 1095  TRP B 1106  1                                  12    
HELIX   26  26 ASN B 1109  ARG B 1113  5                                   5    
HELIX   27  27 SER B 1115  GLY B 1132  1                                  18    
SHEET    1   A 5 LEU A 849  GLY A 858  0                                        
SHEET    2   A 5 GLY A 861  TYR A 868 -1  O  MET A 865   N  GLN A 853           
SHEET    3   A 5 GLU A 877  LEU A 884 -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 A1007  LYS A1009  0                                        
SHEET    2   D 2 LYS A1030  SER A1032 -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 VAL B 878  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  GLY B 915   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  1.33  
LINK         C   PTR A1007                 N   PTR A1008     1555   1555  1.33  
LINK         C   PTR A1008                 N   LYS A1009     1555   1555  1.33  
LINK         C   GLU B1006                 N   PTR B1007     1555   1555  1.33  
LINK         C   PTR B1007                 N   PTR B1008     1555   1555  1.33  
LINK         C   PTR B1008                 N   LYS B1009     1555   1555  1.33  
SITE     1 AC1 14 LEU A 855  GLY A 856  LYS A 857  GLY A 858                    
SITE     2 AC1 14 ALA A 880  GLU A 930  TYR A 931  LEU A 932                    
SITE     3 AC1 14 GLY A 935  ASN A 981  LEU A 983  GLY A 993                    
SITE     4 AC1 14 ASP A 994  HOH A1301                                          
SITE     1 AC2 13 LEU B 855  GLY B 858  ALA B 880  VAL B 911                    
SITE     2 AC2 13 GLU B 930  TYR B 931  LEU B 932  GLY B 935                    
SITE     3 AC2 13 ASN B 981  LEU B 983  GLY B 993  ASP B 994                    
SITE     4 AC2 13 HOH B1318                                                     
CRYST1  111.992  111.992   70.467  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      0.008929  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014191        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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