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Database: PDB
Entry: 5UT1
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Original site: 5UT1 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       14-FEB-17   5UT1              
TITLE     JAK2 JH2 IN COMPLEX WITH BI-D1870                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: JANUS KINASE 2,JAK-2;                                       
COMPND   5 EC: 2.7.10.2;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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: JAK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PSEUDOKINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.PULEO,J.SCHLESSINGER                                              
REVDAT   3   13-SEP-17 5UT1    1       REMARK                                   
REVDAT   2   05-JUL-17 5UT1    1       JRNL                                     
REVDAT   1   07-JUN-17 5UT1    0                                                
JRNL        AUTH   D.E.PULEO,K.KUCERA,H.M.HAMMAREN,D.UNGUREANU,A.S.NEWTON,      
JRNL        AUTH 2 O.SILVENNOINEN,W.L.JORGENSEN,J.SCHLESSINGER                  
JRNL        TITL   IDENTIFICATION AND CHARACTERIZATION OF JAK2 PSEUDOKINASE     
JRNL        TITL 2 DOMAIN SMALL MOLECULE BINDERS.                               
JRNL        REF    ACS MED CHEM LETT             V.   8   618 2017              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   28626521                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.7B00153                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 21059                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1081                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 56.9320 -  3.8997    0.99     2559   135  0.1509 0.1694        
REMARK   3     2  3.8997 -  3.0954    1.00     2482   146  0.1385 0.1757        
REMARK   3     3  3.0954 -  2.7041    1.00     2522   116  0.1557 0.1909        
REMARK   3     4  2.7041 -  2.4569    1.00     2482   131  0.1565 0.1974        
REMARK   3     5  2.4569 -  2.2808    1.00     2480   152  0.1721 0.2212        
REMARK   3     6  2.2808 -  2.1463    1.00     2498   132  0.1779 0.2430        
REMARK   3     7  2.1463 -  2.0388    1.00     2449   138  0.2026 0.2544        
REMARK   3     8  2.0388 -  1.9500    1.00     2506   131  0.2443 0.3184        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.210           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           2192                                  
REMARK   3   ANGLE     :  1.160           2984                                  
REMARK   3   CHIRALITY :  0.065            335                                  
REMARK   3   PLANARITY :  0.007            385                                  
REMARK   3   DIHEDRAL  : 13.789           1294                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 537 THROUGH 556 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8625  21.5435  27.3093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1991 T22:   0.1943                                     
REMARK   3      T33:   0.1022 T12:   0.0035                                     
REMARK   3      T13:  -0.0302 T23:  -0.0599                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3653 L22:   4.7908                                     
REMARK   3      L33:   1.5730 L12:  -1.7533                                     
REMARK   3      L13:  -0.0174 L23:   0.0402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0529 S12:   0.0589 S13:   0.2592                       
REMARK   3      S21:   0.2021 S22:   0.1415 S23:  -0.3087                       
REMARK   3      S31:   0.0149 S32:   0.2610 S33:  -0.0866                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 557 THROUGH 603 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6613  21.8013  23.0047              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1617 T22:   0.1463                                     
REMARK   3      T33:   0.1189 T12:  -0.0320                                     
REMARK   3      T13:  -0.0368 T23:  -0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8946 L22:   6.1225                                     
REMARK   3      L33:   1.8775 L12:  -1.8415                                     
REMARK   3      L13:  -0.2619 L23:  -1.8007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0676 S12:  -0.0586 S13:   0.1450                       
REMARK   3      S21:   0.2421 S22:   0.0684 S23:  -0.1215                       
REMARK   3      S31:  -0.1791 S32:   0.1707 S33:   0.0018                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 604 THROUGH 622 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3230  21.2534  19.0954              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.1423                                     
REMARK   3      T33:   0.1698 T12:  -0.0280                                     
REMARK   3      T13:   0.0247 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6796 L22:   3.4908                                     
REMARK   3      L33:   5.8119 L12:   0.7338                                     
REMARK   3      L13:   4.0897 L23:   2.4049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1657 S12:  -0.2473 S13:   0.0769                       
REMARK   3      S21:   0.2470 S22:  -0.0364 S23:  -0.3087                       
REMARK   3      S31:   0.0419 S32:  -0.1378 S33:  -0.1121                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 623 THROUGH 646 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.2817  11.0375  15.6956              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0934 T22:   0.1796                                     
REMARK   3      T33:   0.2719 T12:   0.0223                                     
REMARK   3      T13:   0.0247 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4640 L22:   1.7132                                     
REMARK   3      L33:   4.1874 L12:  -0.6632                                     
REMARK   3      L13:   0.5080 L23:   1.3154                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0847 S12:  -0.0552 S13:  -0.0690                       
REMARK   3      S21:  -0.1016 S22:  -0.1534 S23:   0.3972                       
REMARK   3      S31:   0.0063 S32:  -0.4936 S33:   0.2170                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 647 THROUGH 697 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.1431  10.3538   6.1272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1281 T22:   0.1165                                     
REMARK   3      T33:   0.1130 T12:   0.0147                                     
REMARK   3      T13:  -0.0214 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1013 L22:   3.0959                                     
REMARK   3      L33:   2.2124 L12:  -0.9898                                     
REMARK   3      L13:  -0.4331 L23:  -0.1754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0809 S12:   0.2093 S13:   0.0498                       
REMARK   3      S21:  -0.2032 S22:  -0.0642 S23:   0.2451                       
REMARK   3      S31:  -0.0459 S32:  -0.2924 S33:   0.0139                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 698 THROUGH 748 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5800  -0.3887  15.4854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1188 T22:   0.1343                                     
REMARK   3      T33:   0.1050 T12:   0.0330                                     
REMARK   3      T13:   0.0008 T23:   0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0229 L22:   2.4822                                     
REMARK   3      L33:   2.1598 L12:  -0.0498                                     
REMARK   3      L13:   0.6905 L23:  -0.0015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0261 S12:  -0.0889 S13:  -0.0210                       
REMARK   3      S21:   0.0839 S22:  -0.0172 S23:  -0.2307                       
REMARK   3      S31:   0.0555 S32:   0.2014 S33:   0.0397                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 749 THROUGH 780 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1153 -10.6659  15.0425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2211 T22:   0.0685                                     
REMARK   3      T33:   0.1936 T12:   0.0026                                     
REMARK   3      T13:   0.0901 T23:   0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7551 L22:   3.6033                                     
REMARK   3      L33:   6.3969 L12:   0.0622                                     
REMARK   3      L13:   0.7393 L23:  -1.2102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1815 S12:  -0.0793 S13:  -0.2647                       
REMARK   3      S21:   0.0768 S22:  -0.1039 S23:   0.0352                       
REMARK   3      S31:   0.4925 S32:   0.0839 S33:   0.2059                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 781 THROUGH 808 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   0.4438  -2.8520   0.5146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1570 T22:   0.1188                                     
REMARK   3      T33:   0.0472 T12:   0.0181                                     
REMARK   3      T13:   0.0351 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9361 L22:   5.9022                                     
REMARK   3      L33:   3.1937 L12:  -1.7845                                     
REMARK   3      L13:   0.4825 L23:  -1.4350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0804 S12:   0.1927 S13:   0.0017                       
REMARK   3      S21:  -0.2616 S22:  -0.1420 S23:   0.0144                       
REMARK   3      S31:   0.0419 S32:   0.1703 S33:   0.0531                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UT1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226415.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5-8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21107                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4FVP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, PH 8.0 0.2M SODIUM ACETATE    
REMARK 280  12-20% PEG 4,000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
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       28.78150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   536                                                      
REMARK 465     PHE A   809                                                      
REMARK 465     THR A   810                                                      
REMARK 465     PRO A   811                                                      
REMARK 465     ASP A   812                                                      
REMARK 465     LEU A   813                                                      
REMARK 465     VAL A   814                                                      
REMARK 465     PRO A   815                                                      
REMARK 465     ARG A   816                                                      
REMARK 465     GLY A   817                                                      
REMARK 465     SER A   818                                                      
REMARK 465     HIS A   819                                                      
REMARK 465     HIS A   820                                                      
REMARK 465     HIS A   821                                                      
REMARK 465     HIS A   822                                                      
REMARK 465     HIS A   823                                                      
REMARK 465     HIS A   824                                                      
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 541    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 543    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 558    CG   CD   CE   NZ                                   
REMARK 470     ARG A 565    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 572    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 585    CG   CD   CE   NZ                                   
REMARK 470     ARG A 588    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 592    CG   CD   OE1  OE2                                  
REMARK 470     MET A 600    CG   SD   CE                                        
REMARK 470     LYS A 603    CG   CD   CE   NZ                                   
REMARK 470     LYS A 630    CG   CD   CE   NZ                                   
REMARK 470     LYS A 639    CG   CD   CE   NZ                                   
REMARK 470     LYS A 640    CG   CD   CE   NZ                                   
REMARK 470     ASN A 643    CG   OD1  ND2                                       
REMARK 470     ARG A 687    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 688    CG   CD   CE   NZ                                   
REMARK 470     LYS A 709    CG   CD   CE   NZ                                   
REMARK 470     GLU A 714    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 728    CG   CD   CE   NZ                                   
REMARK 470     GLN A 760    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 776    CG   CD   CE   NZ                                   
REMARK 470     ARG A 803    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    ASN A 548     -139.29   -115.30                                   
REMARK 500    TYR A 570       17.62     59.14                                   
REMARK 500    ASN A 673       57.78   -149.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     7DZ A  905                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7DZ A 905                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5USY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5USZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UT6   RELATED DB: PDB                                   
DBREF  5UT1 A  536   812  UNP    O60674   JAK2_HUMAN     536    812             
SEQADV 5UT1 ALA A  659  UNP  O60674    TRP   659 ENGINEERED MUTATION            
SEQADV 5UT1 ALA A  777  UNP  O60674    TRP   777 ENGINEERED MUTATION            
SEQADV 5UT1 HIS A  794  UNP  O60674    PHE   794 ENGINEERED MUTATION            
SEQADV 5UT1 LEU A  813  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 VAL A  814  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 PRO A  815  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 ARG A  816  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 GLY A  817  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 SER A  818  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  819  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  820  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  821  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  822  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  823  UNP  O60674              EXPRESSION TAG                 
SEQADV 5UT1 HIS A  824  UNP  O60674              EXPRESSION TAG                 
SEQRES   1 A  289  VAL PHE HIS LYS ILE ARG ASN GLU ASP LEU ILE PHE ASN          
SEQRES   2 A  289  GLU SER LEU GLY GLN GLY THR PHE THR LYS ILE PHE LYS          
SEQRES   3 A  289  GLY VAL ARG ARG GLU VAL GLY ASP TYR GLY GLN LEU HIS          
SEQRES   4 A  289  GLU THR GLU VAL LEU LEU LYS VAL LEU ASP LYS ALA HIS          
SEQRES   5 A  289  ARG ASN TYR SER GLU SER PHE PHE GLU ALA ALA SER MET          
SEQRES   6 A  289  MET SER LYS LEU SER HIS LYS HIS LEU VAL LEU ASN TYR          
SEQRES   7 A  289  GLY VAL CYS VAL CYS GLY ASP GLU ASN ILE LEU VAL GLN          
SEQRES   8 A  289  GLU PHE VAL LYS PHE GLY SER LEU ASP THR TYR LEU LYS          
SEQRES   9 A  289  LYS ASN LYS ASN CYS ILE ASN ILE LEU TRP LYS LEU GLU          
SEQRES  10 A  289  VAL ALA LYS GLN LEU ALA ALA ALA MET HIS PHE LEU GLU          
SEQRES  11 A  289  GLU ASN THR LEU ILE HIS GLY ASN VAL CYS ALA LYS ASN          
SEQRES  12 A  289  ILE LEU LEU ILE ARG GLU GLU ASP ARG LYS THR GLY ASN          
SEQRES  13 A  289  PRO PRO PHE ILE LYS LEU SER ASP PRO GLY ILE SER ILE          
SEQRES  14 A  289  THR VAL LEU PRO LYS ASP ILE LEU GLN GLU ARG ILE PRO          
SEQRES  15 A  289  TRP VAL PRO PRO GLU CYS ILE GLU ASN PRO LYS ASN LEU          
SEQRES  16 A  289  ASN LEU ALA THR ASP LYS TRP SER PHE GLY THR THR LEU          
SEQRES  17 A  289  TRP GLU ILE CYS SER GLY GLY ASP LYS PRO LEU SER ALA          
SEQRES  18 A  289  LEU ASP SER GLN ARG LYS LEU GLN PHE TYR GLU ASP ARG          
SEQRES  19 A  289  HIS GLN LEU PRO ALA PRO LYS ALA ALA GLU LEU ALA ASN          
SEQRES  20 A  289  LEU ILE ASN ASN CYS MET ASP TYR GLU PRO ASP HIS ARG          
SEQRES  21 A  289  PRO SER PHE ARG ALA ILE ILE ARG ASP LEU ASN SER LEU          
SEQRES  22 A  289  PHE THR PRO ASP LEU VAL PRO ARG GLY SER HIS HIS HIS          
SEQRES  23 A  289  HIS HIS HIS                                                  
HET    GOL  A 901       6                                                       
HET    GOL  A 902       6                                                       
HET    GOL  A 903       6                                                       
HET    GOL  A 904       6                                                       
HET    7DZ  A 905      24                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     7DZ (7S)-2-[(3,5-DIFLUORO-4-HYDROXYPHENYL)AMINO]-5,7-                
HETNAM   2 7DZ  DIMETHYL-8-(3-METHYLBUTYL)-7,8-DIHYDROPTERIDIN-6(5H)-           
HETNAM   3 7DZ  ONE                                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     7DZ BI-D1870                                                         
FORMUL   2  GOL    4(C3 H8 O3)                                                  
FORMUL   6  7DZ    C19 H23 F2 N5 O2                                             
FORMUL   7  HOH   *218(H2 O)                                                    
HELIX    1 AA1 ARG A  541  GLU A  543  5                                   3    
HELIX    2 AA2 ASP A  569  GLY A  571  5                                   3    
HELIX    3 AA3 LYS A  585  ASN A  589  5                                   5    
HELIX    4 AA4 TYR A  590  LEU A  604  1                                  15    
HELIX    5 AA5 SER A  633  ASN A  641  1                                   9    
HELIX    6 AA6 LYS A  642  ILE A  645  5                                   4    
HELIX    7 AA7 ASN A  646  ASN A  667  1                                  22    
HELIX    8 AA8 CYS A  675  LYS A  677  5                                   3    
HELIX    9 AA9 ASP A  686  GLY A  690  5                                   5    
HELIX   10 AB1 PRO A  708  ARG A  715  1                                   8    
HELIX   11 AB2 PRO A  720  ASN A  726  1                                   7    
HELIX   12 AB3 PRO A  727  LEU A  730  5                                   4    
HELIX   13 AB4 ASN A  731  SER A  748  1                                  18    
HELIX   14 AB5 ASP A  758  ASP A  768  1                                  11    
HELIX   15 AB6 LEU A  780  MET A  788  1                                   9    
HELIX   16 AB7 GLU A  791  ARG A  795  5                                   5    
HELIX   17 AB8 SER A  797  LEU A  808  1                                  12    
SHEET    1 AA1 5 LEU A 545  GLY A 554  0                                        
SHEET    2 AA1 5 THR A 557  VAL A 567 -1  O  LYS A 561   N  GLU A 549           
SHEET    3 AA1 5 LEU A 573  LEU A 583 -1  O  VAL A 582   N  LYS A 558           
SHEET    4 AA1 5 ILE A 623  GLU A 627 -1  O  GLN A 626   N  LEU A 579           
SHEET    5 AA1 5 ASN A 612  CYS A 616 -1  N  GLY A 614   O  VAL A 625           
SHEET    1 AA2 2 ILE A 679  ARG A 683  0                                        
SHEET    2 AA2 2 PHE A 694  LEU A 697 -1  O  LYS A 696   N  LEU A 680           
CISPEP   1 ILE A  716    PRO A  717          0         8.21                     
SITE     1 AC1  6 ASN A 673  CYS A 675  ARG A 715  TRP A 718                    
SITE     2 AC1  6 GOL A 902  HOH A1067                                          
SITE     1 AC2 10 GLY A 554  THR A 555  ASN A 673  LYS A 677                    
SITE     2 AC2 10 ASN A 678  ARG A 715  GOL A 901  HOH A1005                    
SITE     3 AC2 10 HOH A1018  HOH A1092                                          
SITE     1 AC3  6 ARG A 588  VAL A 617  GLY A 619  ASP A 620                    
SITE     2 AC3  6 GLU A 621  ASN A 622                                          
SITE     1 AC4  4 HIS A 606  HOH A1007  HOH A1020  HOH A1183                    
SITE     1 AC5 15 LEU A 551  LEU A 579  LYS A 581  VAL A 610                    
SITE     2 AC5 15 GLN A 626  GLU A 627  PHE A 628  VAL A 629                    
SITE     3 AC5 15 GLY A 632  LYS A 677  LEU A 680  SER A 698                    
SITE     4 AC5 15 HOH A1049  HOH A1092  HOH A1107                               
CRYST1   44.479   57.563   60.678  90.00 110.30  90.00 P 1 21 1      2          
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      0.022483  0.000000  0.008318        0.00000                         
SCALE2      0.000000  0.017372  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017572        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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