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Database: PDB
Entry: 4EHZ
LinkDB: 4EHZ
Original site: 4EHZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-APR-12   4EHZ              
TITLE     THE JAK1 KINASE DOMAIN IN COMPLEX WITH INHIBITOR                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 854-1154;                      
COMPND   5 SYNONYM: JANUS KINASE 1, JAK-1;                                      
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: JAK1, JAK1A, JAK1B;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.LUPARDUS,M.STEFFEK                                                
REVDAT   3   23-JAN-13 4EHZ    1       JRNL                                     
REVDAT   2   29-AUG-12 4EHZ    1       JRNL                                     
REVDAT   1   04-JUL-12 4EHZ    0                                                
JRNL        AUTH   M.ZAK,R.MENDONCA,M.BALAZS,K.BARRETT,P.BERGERON,W.S.BLAIR,    
JRNL        AUTH 2 C.CHANG,G.DESHMUKH,J.DEVOSS,P.S.DRAGOVICH,C.EIGENBROT,       
JRNL        AUTH 3 N.GHILARDI,P.GIBBONS,S.GRADL,C.HAMMAN,E.J.HANAN,E.HARSTAD,   
JRNL        AUTH 4 P.R.HEWITT,C.A.HURLEY,T.JIN,A.JOHNSON,T.JOHNSON,J.R.KENNY,   
JRNL        AUTH 5 M.F.KOEHLER,P.BIR KOHLI,J.J.KULAGOWSKI,S.LABADIE,J.LIAO,     
JRNL        AUTH 6 M.LIIMATTA,Z.LIN,P.J.LUPARDUS,R.J.MAXEY,J.M.MURRAY,R.PULK,   
JRNL        AUTH 7 M.RODRIGUEZ,S.SAVAGE,S.SHIA,M.STEFFEK,S.UBHAYAKAR,M.ULTSCH,  
JRNL        AUTH 8 A.VAN ABBEMA,S.I.WARD,L.XIAO,Y.XIAO                          
JRNL        TITL   DISCOVERY AND OPTIMIZATION OF C-2 METHYL                     
JRNL        TITL 2 IMIDAZOPYRROLOPYRIDINES AS POTENT AND ORALLY BIOAVAILABLE    
JRNL        TITL 3 JAK1 INHIBITORS WITH SELECTIVITY OVER JAK2.                  
JRNL        REF    J.MED.CHEM.                   V.  55  6176 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22698084                                                     
JRNL        DOI    10.1021/JM300628C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.17 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_648)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 60351                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3033                            
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 30.0000 -  6.0751    0.98     2843   157  0.1704 0.1839        
REMARK   3     2  6.0751 -  4.8285    0.99     2854   148  0.1784 0.2263        
REMARK   3     3  4.8285 -  4.2200    0.99     2851   152  0.1334 0.1693        
REMARK   3     4  4.2200 -  3.8350    0.98     2824   150  0.1387 0.1754        
REMARK   3     5  3.8350 -  3.5606    0.98     2792   154  0.1550 0.2204        
REMARK   3     6  3.5606 -  3.3510    0.97     2831   156  0.1709 0.2537        
REMARK   3     7  3.3510 -  3.1833    0.96     2764   169  0.1870 0.2402        
REMARK   3     8  3.1833 -  3.0449    0.96     2726   126  0.1827 0.2304        
REMARK   3     9  3.0449 -  2.9278    0.94     2734   134  0.1721 0.2090        
REMARK   3    10  2.9278 -  2.8268    0.95     2695   132  0.1737 0.2366        
REMARK   3    11  2.8268 -  2.7385    0.93     2680   163  0.1718 0.2424        
REMARK   3    12  2.7385 -  2.6603    0.92     2600   137  0.1718 0.2391        
REMARK   3    13  2.6603 -  2.5903    0.91     2654   134  0.1718 0.2253        
REMARK   3    14  2.5903 -  2.5271    0.90     2519   149  0.1871 0.2822        
REMARK   3    15  2.5271 -  2.4697    0.88     2541   132  0.1899 0.2781        
REMARK   3    16  2.4697 -  2.4172    0.87     2499   140  0.1972 0.2839        
REMARK   3    17  2.4172 -  2.3688    0.85     2382   120  0.2010 0.2713        
REMARK   3    18  2.3688 -  2.3241    0.84     2450   130  0.2042 0.2841        
REMARK   3    19  2.3241 -  2.2827    0.82     2336   129  0.2032 0.2980        
REMARK   3    20  2.2827 -  2.2440    0.81     2327   103  0.2051 0.3066        
REMARK   3    21  2.2440 -  2.2078    0.79     2301   111  0.1947 0.3073        
REMARK   3    22  2.2078 -  2.1740    0.73     2115   107  0.1896 0.2421        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 28.23                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.75                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.36680                                             
REMARK   3    B22 (A**2) : 1.57270                                              
REMARK   3    B33 (A**2) : 0.79400                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.69130                                              
REMARK   3    B23 (A**2) : -0.00000                                             
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      :  0.007           9581                                  
REMARK   3   ANGLE     :  1.085          12905                                  
REMARK   3   CHIRALITY :  0.070           1372                                  
REMARK   3   PLANARITY :  0.004           1636                                  
REMARK   3   DIHEDRAL  : 14.839           3641                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 858:871)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -20.8398  67.5665  -6.3064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0352 T22:   0.0760                                     
REMARK   3      T33:   0.0718 T12:  -0.0054                                     
REMARK   3      T13:  -0.0158 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0059 L22:   0.0068                                     
REMARK   3      L33:   0.0221 L12:  -0.0024                                     
REMARK   3      L13:  -0.0055 L23:  -0.0077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0045 S12:  -0.0053 S13:   0.0134                       
REMARK   3      S21:  -0.0055 S22:   0.0134 S23:   0.0114                       
REMARK   3      S31:   0.0052 S32:  -0.0184 S33:  -0.0062                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 872:1033)                        
REMARK   3    ORIGIN FOR THE GROUP (A):   1.6295  58.9266   4.5368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0673 T22:   0.0739                                     
REMARK   3      T33:   0.0673 T12:  -0.0049                                     
REMARK   3      T13:   0.0022 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0992 L22:   0.0446                                     
REMARK   3      L33:   0.0613 L12:  -0.0323                                     
REMARK   3      L13:   0.0618 L23:  -0.0256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0212 S12:   0.0130 S13:  -0.0308                       
REMARK   3      S21:   0.0012 S22:   0.0384 S23:   0.0224                       
REMARK   3      S31:  -0.0133 S32:  -0.0274 S33:  -0.0029                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1036:1154)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4933  47.1504  18.3944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0620 T22:   0.0048                                     
REMARK   3      T33:   0.0451 T12:   0.0200                                     
REMARK   3      T13:  -0.0084 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0377 L22:   0.0030                                     
REMARK   3      L33:   0.0235 L12:   0.0054                                     
REMARK   3      L13:   0.0132 L23:  -0.0035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:  -0.0224 S13:  -0.0581                       
REMARK   3      S21:   0.0388 S22:   0.0316 S23:  -0.0240                       
REMARK   3      S31:  -0.0095 S32:   0.0105 S33:  -0.0102                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 865:1033)                        
REMARK   3    ORIGIN FOR THE GROUP (A):  19.1053   2.9244   4.1403              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0815 T22:   0.0712                                     
REMARK   3      T33:   0.0575 T12:   0.0059                                     
REMARK   3      T13:  -0.0008 T23:  -0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2136 L22:   0.1429                                     
REMARK   3      L33:   0.0312 L12:   0.0245                                     
REMARK   3      L13:  -0.0658 L23:  -0.0489                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:  -0.0639 S13:  -0.0003                       
REMARK   3      S21:  -0.0493 S22:   0.0127 S23:  -0.0170                       
REMARK   3      S31:   0.0334 S32:   0.0259 S33:   0.0059                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 1036:1154)                       
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7060  14.8628  18.2903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0677 T22:  -0.0162                                     
REMARK   3      T33:   0.0024 T12:   0.0149                                     
REMARK   3      T13:   0.0733 T23:  -0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0100 L22:   0.0038                                     
REMARK   3      L33:   0.0109 L12:   0.0030                                     
REMARK   3      L13:  -0.0015 L23:   0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0375 S12:  -0.0146 S13:   0.0543                       
REMARK   3      S21:   0.0194 S22:   0.0162 S23:   0.0278                       
REMARK   3      S31:  -0.0372 S32:   0.0033 S33:  -0.0142                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'C' and (resseq 866:1041)                        
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9487  56.3765 -38.6066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0547 T22:   0.0887                                     
REMARK   3      T33:   0.0766 T12:  -0.0052                                     
REMARK   3      T13:  -0.0078 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0128 L22:   0.0252                                     
REMARK   3      L33:   0.0519 L12:  -0.0184                                     
REMARK   3      L13:   0.0056 L23:  -0.0110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0152 S12:   0.0055 S13:  -0.0143                       
REMARK   3      S21:  -0.0062 S22:   0.0326 S23:   0.0225                       
REMARK   3      S31:   0.0080 S32:  -0.0257 S33:  -0.0265                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'C' and (resseq 1042:1154)                       
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8857  45.8962 -24.9843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0847 T22:   0.0506                                     
REMARK   3      T33:   0.0812 T12:   0.0037                                     
REMARK   3      T13:  -0.0168 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1191 L22:   0.0397                                     
REMARK   3      L33:   0.1195 L12:  -0.0263                                     
REMARK   3      L13:   0.0241 L23:   0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0389 S12:  -0.0199 S13:  -0.0690                       
REMARK   3      S21:  -0.0034 S22:   0.0311 S23:  -0.0033                       
REMARK   3      S31:   0.0067 S32:   0.0057 S33:  -0.0334                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'D' and (resseq 865:1033)                        
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6076   1.6007 -39.7158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0666 T22:   0.0759                                     
REMARK   3      T33:   0.0772 T12:  -0.0065                                     
REMARK   3      T13:  -0.0077 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1528 L22:   0.0647                                     
REMARK   3      L33:   0.1657 L12:  -0.0629                                     
REMARK   3      L13:  -0.0415 L23:  -0.0038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0534 S12:   0.0355 S13:   0.0500                       
REMARK   3      S21:   0.0031 S22:   0.0275 S23:  -0.0393                       
REMARK   3      S31:   0.0265 S32:  -0.0132 S33:   0.0142                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'D' and (resseq 1036:1154)                       
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5644  13.6259 -25.5267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0075 T22:  -0.0992                                     
REMARK   3      T33:   0.0112 T12:   0.0934                                     
REMARK   3      T13:   0.0151 T23:  -0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0321 L22:   0.0022                                     
REMARK   3      L33:   0.0060 L12:   0.0003                                     
REMARK   3      L13:  -0.0040 L23:   0.0066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:  -0.0233 S13:   0.0638                       
REMARK   3      S21:   0.0194 S22:   0.0278 S23:  -0.0003                       
REMARK   3      S31:   0.0007 S32:   0.0049 S33:  -0.0007                       
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 4EHZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071641.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63591                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.170                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 5-6 AND 25-35% PEG 6000,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                     
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       86.08750            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D                                     
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   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     ILE A   855                                                      
REMARK 465     VAL A   856                                                      
REMARK 465     SER A   857                                                      
REMARK 465     GLU A   913                                                      
REMARK 465     SER A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLY A   916                                                      
REMARK 465     ASN A   917                                                      
REMARK 465     GLY B   853                                                      
REMARK 465     ASP B   854                                                      
REMARK 465     ILE B   855                                                      
REMARK 465     VAL B   856                                                      
REMARK 465     SER B   857                                                      
REMARK 465     GLU B   858                                                      
REMARK 465     LYS B   859                                                      
REMARK 465     LYS B   860                                                      
REMARK 465     PRO B   861                                                      
REMARK 465     ALA B   862                                                      
REMARK 465     THR B   863                                                      
REMARK 465     GLU B   864                                                      
REMARK 465     GLU B   913                                                      
REMARK 465     SER B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLY B   916                                                      
REMARK 465     GLU B   946                                                      
REMARK 465     ASP B   947                                                      
REMARK 465     GLY B   948                                                      
REMARK 465     GLY B   949                                                      
REMARK 465     GLY C   853                                                      
REMARK 465     ASP C   854                                                      
REMARK 465     ILE C   855                                                      
REMARK 465     VAL C   856                                                      
REMARK 465     SER C   857                                                      
REMARK 465     GLU C   858                                                      
REMARK 465     LYS C   859                                                      
REMARK 465     LYS C   860                                                      
REMARK 465     PRO C   861                                                      
REMARK 465     ALA C   862                                                      
REMARK 465     THR C   863                                                      
REMARK 465     GLU C   864                                                      
REMARK 465     VAL C   865                                                      
REMARK 465     GLU C   913                                                      
REMARK 465     SER C   914                                                      
REMARK 465     GLY C   915                                                      
REMARK 465     GLY C   916                                                      
REMARK 465     GLU C   946                                                      
REMARK 465     ASP C   947                                                      
REMARK 465     GLY C   948                                                      
REMARK 465     GLY C   949                                                      
REMARK 465     ASN C   950                                                      
REMARK 465     GLY D   853                                                      
REMARK 465     ASP D   854                                                      
REMARK 465     ILE D   855                                                      
REMARK 465     VAL D   856                                                      
REMARK 465     SER D   857                                                      
REMARK 465     GLU D   858                                                      
REMARK 465     LYS D   859                                                      
REMARK 465     LYS D   860                                                      
REMARK 465     PRO D   861                                                      
REMARK 465     ALA D   862                                                      
REMARK 465     THR D   863                                                      
REMARK 465     GLU D   864                                                      
REMARK 465     GLU D   913                                                      
REMARK 465     SER D   914                                                      
REMARK 465     GLY D   915                                                      
REMARK 465     GLY D   916                                                      
REMARK 465     GLU D   946                                                      
REMARK 465     ASP D   947                                                      
REMARK 465     GLY D   948                                                      
REMARK 465     GLY D   949                                                      
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     GLU A 946    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 947    CG   OD1  OD2                                       
REMARK 470     ASN C 917    CG   OD1  ND2                                       
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    LYS A 859       98.32    -64.22                                   
REMARK 500    ASN A 900       36.07     70.20                                   
REMARK 500    ASP A 947      -38.69    -39.38                                   
REMARK 500    ASN A 950      -66.17     61.40                                   
REMARK 500    ARG A1002       -0.30     80.05                                   
REMARK 500    ASP A1003       33.39   -147.70                                   
REMARK 500    ASP A1031      -13.07     75.45                                   
REMARK 500    GLN B 998       32.38     72.79                                   
REMARK 500    ARG B1002       -1.08     70.15                                   
REMARK 500    ASP B1003       32.27   -144.90                                   
REMARK 500    ASP B1031       29.51     43.75                                   
REMARK 500    TYR B1077       29.55     49.94                                   
REMARK 500    ASP C1003       34.74   -153.37                                   
REMARK 500    PHE C1022       25.14   -141.74                                   
REMARK 500    ILE D 878      -60.95   -108.07                                   
REMARK 500    HIS D 885      -50.57     71.46                                   
REMARK 500    ASP D1003       30.23   -151.16                                   
REMARK 500    THR D1140     -177.64    -68.15                                   
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 JAK A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAK B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAK C 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE JAK D 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1203                
DBREF  4EHZ A  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
DBREF  4EHZ B  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
DBREF  4EHZ C  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
DBREF  4EHZ D  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
SEQADV 4EHZ GLY A  853  UNP  P23458              EXPRESSION TAG                 
SEQADV 4EHZ GLY B  853  UNP  P23458              EXPRESSION TAG                 
SEQADV 4EHZ GLY C  853  UNP  P23458              EXPRESSION TAG                 
SEQADV 4EHZ GLY D  853  UNP  P23458              EXPRESSION TAG                 
SEQRES   1 A  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 A  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 A  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 A  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 A  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 A  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 A  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 A  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 A  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 A  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 A  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 A  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 A  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 A  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 A  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 A  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 A  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 A  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 A  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 A  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 A  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 A  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 A  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 A  302  LEU LEU LYS                                                  
SEQRES   1 B  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 B  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 B  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 B  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 B  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 B  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 B  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 B  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 B  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 B  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 B  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 B  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 B  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 B  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 B  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 B  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 B  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 B  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 B  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 B  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 B  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 B  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 B  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 B  302  LEU LEU LYS                                                  
SEQRES   1 C  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 C  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 C  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 C  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 C  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 C  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 C  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 C  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 C  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 C  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 C  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 C  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 C  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 C  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 C  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 C  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 C  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 C  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 C  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 C  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 C  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 C  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 C  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 C  302  LEU LEU LYS                                                  
SEQRES   1 D  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 D  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 D  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 D  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 D  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 D  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 D  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 D  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 D  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 D  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 D  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 D  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 D  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 D  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 D  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 D  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 D  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 D  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 D  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 D  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 D  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 D  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 D  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 D  302  LEU LEU LYS                                                  
MODRES 4EHZ PTR A 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR A 1035  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR B 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR B 1035  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR C 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR C 1035  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR D 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4EHZ PTR D 1035  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1034      16                                                       
HET    PTR  A1035      16                                                       
HET    PTR  B1034      16                                                       
HET    PTR  B1035      16                                                       
HET    PTR  C1034      16                                                       
HET    PTR  C1035      16                                                       
HET    PTR  D1034      16                                                       
HET    PTR  D1035      16                                                       
HET    JAK  A1201      19                                                       
HET    EDO  A1202       4                                                       
HET    EDO  A1203       4                                                       
HET    EDO  A1204       4                                                       
HET    EDO  A1205       4                                                       
HET    EDO  A1206       4                                                       
HET    JAK  B1201      19                                                       
HET    EDO  B1202       4                                                       
HET    JAK  C1201      19                                                       
HET    EDO  C1202       4                                                       
HET    EDO  C1203       4                                                       
HET    EDO  C1204       4                                                       
HET    EDO  C1205       4                                                       
HET    JAK  D1201      19                                                       
HET    EDO  D1202       4                                                       
HET    EDO  D1203       4                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     JAK 2-METHYL-1-(PIPERIDIN-4-YL)-1,6-DIHYDROIMIDAZO[4,5-              
HETNAM   2 JAK  D]PYRROLO[2,3-B]PYRIDINE                                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PTR    8(C9 H12 N O6 P)                                             
FORMUL   5  JAK    4(C14 H17 N5)                                                
FORMUL   6  EDO    12(C2 H6 O2)                                                 
FORMUL  21  HOH   *561(H2 O)                                                    
HELIX    1   1 GLU A  871  ARG A  873  5                                   3    
HELIX    2   2 ILE A  919  ASN A  931  1                                  13    
HELIX    3   3 SER A  963  ASN A  971  1                                   9    
HELIX    4   4 ASN A  976  ARG A  997  1                                  22    
HELIX    5   5 ALA A 1005  ARG A 1007  5                                   3    
HELIX    6   6 PRO A 1044  TYR A 1048  5                                   5    
HELIX    7   7 ALA A 1049  GLN A 1055  1                                   7    
HELIX    8   8 ILE A 1060  THR A 1076  1                                  17    
HELIX    9   9 ASP A 1079  SER A 1082  5                                   4    
HELIX   10  10 SER A 1083  GLY A 1093  1                                  11    
HELIX   11  11 HIS A 1096  GLN A 1098  5                                   3    
HELIX   12  12 MET A 1099  GLU A 1110  1                                  12    
HELIX   13  13 PRO A 1121  TRP A 1132  1                                  12    
HELIX   14  14 GLN A 1135  ARG A 1139  5                                   5    
HELIX   15  15 SER A 1141  LYS A 1154  1                                  14    
HELIX   16  16 GLU B  871  ARG B  873  5                                   3    
HELIX   17  17 HIS B  918  ASN B  931  1                                  14    
HELIX   18  18 SER B  963  LYS B  972  1                                  10    
HELIX   19  19 ASN B  976  ARG B  997  1                                  22    
HELIX   20  20 ALA B 1005  ARG B 1007  5                                   3    
HELIX   21  21 PRO B 1044  TYR B 1048  5                                   5    
HELIX   22  22 ALA B 1049  SER B 1056  1                                   8    
HELIX   23  23 TYR B 1059  THR B 1076  1                                  18    
HELIX   24  24 ASP B 1079  SER B 1082  5                                   4    
HELIX   25  25 SER B 1083  GLY B 1093  1                                  11    
HELIX   26  26 HIS B 1096  GLN B 1098  5                                   3    
HELIX   27  27 MET B 1099  GLU B 1110  1                                  12    
HELIX   28  28 PRO B 1121  TRP B 1132  1                                  12    
HELIX   29  29 GLN B 1135  ARG B 1139  5                                   5    
HELIX   30  30 SER B 1141  LYS B 1154  1                                  14    
HELIX   31  31 GLU C  871  ARG C  873  5                                   3    
HELIX   32  32 HIS C  918  ASN C  931  1                                  14    
HELIX   33  33 SER C  963  LYS C  972  1                                  10    
HELIX   34  34 ASN C  976  ARG C  997  1                                  22    
HELIX   35  35 ALA C 1005  ARG C 1007  5                                   3    
HELIX   36  36 PRO C 1044  TYR C 1048  5                                   5    
HELIX   37  37 ALA C 1049  SER C 1056  1                                   8    
HELIX   38  38 TYR C 1059  THR C 1076  1                                  18    
HELIX   39  39 ASP C 1079  SER C 1082  5                                   4    
HELIX   40  40 SER C 1083  GLY C 1093  1                                  11    
HELIX   41  41 HIS C 1096  GLN C 1098  5                                   3    
HELIX   42  42 MET C 1099  GLU C 1110  1                                  12    
HELIX   43  43 PRO C 1121  CYS C 1131  1                                  11    
HELIX   44  44 GLN C 1135  ARG C 1139  5                                   5    
HELIX   45  45 SER C 1141  LYS C 1154  1                                  14    
HELIX   46  46 GLU D  871  ARG D  873  5                                   3    
HELIX   47  47 HIS D  918  ASN D  931  1                                  14    
HELIX   48  48 SER D  963  LYS D  972  1                                  10    
HELIX   49  49 ASN D  976  ARG D  997  1                                  22    
HELIX   50  50 ALA D 1005  ARG D 1007  5                                   3    
HELIX   51  51 PRO D 1044  TYR D 1048  5                                   5    
HELIX   52  52 ALA D 1049  GLN D 1055  1                                   7    
HELIX   53  53 TYR D 1059  THR D 1076  1                                  18    
HELIX   54  54 ASP D 1079  SER D 1082  5                                   4    
HELIX   55  55 SER D 1083  GLY D 1093  1                                  11    
HELIX   56  56 HIS D 1096  GLN D 1098  5                                   3    
HELIX   57  57 MET D 1099  GLU D 1110  1                                  12    
HELIX   58  58 PRO D 1121  CYS D 1131  1                                  11    
HELIX   59  59 GLN D 1135  ARG D 1139  5                                   5    
HELIX   60  60 SER D 1141  LEU D 1153  1                                  13    
SHEET    1   A 5 LEU A 875  GLU A 883  0                                        
SHEET    2   A 5 GLY A 887  TYR A 894 -1  O  VAL A 889   N  GLY A 882           
SHEET    3   A 5 GLU A 903  LEU A 910 -1  O  VAL A 907   N  GLU A 890           
SHEET    4   A 5 ILE A 952  GLU A 957 -1  O  MET A 956   N  ALA A 906           
SHEET    5   A 5 TYR A 940  THR A 945 -1  N  GLY A 942   O  ILE A 955           
SHEET    1   B 2 TYR A 999  VAL A1000  0                                        
SHEET    2   B 2 LYS A1026  ALA A1027 -1  O  LYS A1026   N  VAL A1000           
SHEET    1   C 2 VAL A1009  SER A1013  0                                        
SHEET    2   C 2 GLN A1016  ILE A1019 -1  O  LYS A1018   N  LEU A1010           
SHEET    1   D 2 PTR A1034  THR A1036  0                                        
SHEET    2   D 2 LYS A1057  TYR A1059 -1  O  PHE A1058   N  PTR A1035           
SHEET    1   E 5 LEU B 875  GLU B 883  0                                        
SHEET    2   E 5 GLY B 887  TYR B 894 -1  O  LEU B 891   N  ILE B 878           
SHEET    3   E 5 GLU B 903  LEU B 910 -1  O  VAL B 905   N  CYS B 892           
SHEET    4   E 5 LYS B 953  GLU B 957 -1  O  MET B 956   N  ALA B 906           
SHEET    5   E 5 TYR B 940  CYS B 944 -1  N  LYS B 941   O  ILE B 955           
SHEET    1   F 2 TYR B 999  VAL B1000  0                                        
SHEET    2   F 2 LYS B1026  ALA B1027 -1  O  LYS B1026   N  VAL B1000           
SHEET    1   G 2 VAL B1009  SER B1013  0                                        
SHEET    2   G 2 GLN B1016  ILE B1019 -1  O  LYS B1018   N  LEU B1010           
SHEET    1   H 2 PTR B1035  THR B1036  0                                        
SHEET    2   H 2 LYS B1057  PHE B1058 -1  O  PHE B1058   N  PTR B1035           
SHEET    1   I 5 LEU C 875  GLU C 883  0                                        
SHEET    2   I 5 GLY C 887  TYR C 894 -1  O  LEU C 891   N  ARG C 879           
SHEET    3   I 5 GLU C 903  LEU C 910 -1  O  VAL C 907   N  GLU C 890           
SHEET    4   I 5 LYS C 953  GLU C 957 -1  O  MET C 956   N  ALA C 906           
SHEET    5   I 5 TYR C 940  CYS C 944 -1  N  GLY C 942   O  ILE C 955           
SHEET    1   J 2 TYR C 999  VAL C1000  0                                        
SHEET    2   J 2 LYS C1026  ALA C1027 -1  O  LYS C1026   N  VAL C1000           
SHEET    1   K 2 VAL C1009  SER C1013  0                                        
SHEET    2   K 2 GLN C1016  ILE C1019 -1  O  LYS C1018   N  LEU C1010           
SHEET    1   L 2 PTR C1035  THR C1036  0                                        
SHEET    2   L 2 LYS C1057  PHE C1058 -1  O  PHE C1058   N  PTR C1035           
SHEET    1   M 6 HIS D 869  PHE D 870  0                                        
SHEET    2   M 6 TYR D 940  CYS D 944  1  O  ILE D 943   N  PHE D 870           
SHEET    3   M 6 LYS D 953  GLU D 957 -1  O  ILE D 955   N  LYS D 941           
SHEET    4   M 6 GLU D 903  LEU D 910 -1  N  ALA D 906   O  MET D 956           
SHEET    5   M 6 GLY D 887  TYR D 894 -1  N  CYS D 892   O  VAL D 905           
SHEET    6   M 6 LEU D 875  GLU D 883 -1  N  ARG D 879   O  LEU D 891           
SHEET    1   N 2 TYR D 999  VAL D1000  0                                        
SHEET    2   N 2 LYS D1026  ALA D1027 -1  O  LYS D1026   N  VAL D1000           
SHEET    1   O 2 VAL D1009  SER D1013  0                                        
SHEET    2   O 2 GLN D1016  ILE D1019 -1  O  LYS D1018   N  LEU D1010           
SHEET    1   P 2 PTR D1035  THR D1036  0                                        
SHEET    2   P 2 LYS D1057  PHE D1058 -1  O  PHE D1058   N  PTR D1035           
LINK         C   GLU A1033                 N   PTR A1034     1555   1555  1.32  
LINK         C   PTR A1034                 N   PTR A1035     1555   1555  1.33  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.33  
LINK         C   GLU B1033                 N   PTR B1034     1555   1555  1.33  
LINK         C   PTR B1034                 N   PTR B1035     1555   1555  1.33  
LINK         C   PTR B1035                 N   THR B1036     1555   1555  1.32  
LINK         C   GLU C1033                 N   PTR C1034     1555   1555  1.32  
LINK         C   PTR C1034                 N   PTR C1035     1555   1555  1.32  
LINK         C   PTR C1035                 N   THR C1036     1555   1555  1.33  
LINK         C   GLU D1033                 N   PTR D1034     1555   1555  1.32  
LINK         C   PTR D1034                 N   PTR D1035     1555   1555  1.32  
LINK         C   PTR D1035                 N   THR D1036     1555   1555  1.32  
SITE     1 AC1 14 LEU A 881  VAL A 889  ALA A 906  GLU A 957                    
SITE     2 AC1 14 PHE A 958  LEU A 959  GLY A 962  GLU A 966                    
SITE     3 AC1 14 ARG A1007  ASN A1008  LEU A1010  EDO A1202                    
SITE     4 AC1 14 HOH A1304  HOH A1336                                          
SITE     1 AC2  5 ARG A 879  PRO A 960  GLY A 962  JAK A1201                    
SITE     2 AC2  5 HOH A1432                                                     
SITE     1 AC3  5 LEU A 977  GLN A 980  LEU A1075  TYR A1077                    
SITE     2 AC3  5 PRO A1118                                                     
SITE     1 AC4  3 PRO A 867  HIS A 869  PHE A 870                               
SITE     1 AC5  3 LEU A 875  GLU A 890  LYS A 953                               
SITE     1 AC6  5 ASN A 976  LYS A 978  GLN A 979  LYS A 982                    
SITE     2 AC6  5 HOH A1414                                                     
SITE     1 AC7 14 LEU B 881  VAL B 889  ALA B 906  GLU B 957                    
SITE     2 AC7 14 PHE B 958  LEU B 959  GLY B 962  GLU B 966                    
SITE     3 AC7 14 ARG B1007  ASN B1008  LEU B1010  HOH B1314                    
SITE     4 AC7 14 HOH B1317  HOH B1424                                          
SITE     1 AC8  4 GLU B 890  VAL B 907  LYS B 953  HOH B1329                    
SITE     1 AC9 14 LEU C 881  VAL C 889  ALA C 906  GLU C 957                    
SITE     2 AC9 14 PHE C 958  LEU C 959  GLY C 962  GLU C 966                    
SITE     3 AC9 14 ARG C1007  ASN C1008  LEU C1010  EDO C1202                    
SITE     4 AC9 14 HOH C1302  HOH C1306                                          
SITE     1 BC1  6 ARG C 879  LEU C 881  PRO C 960  GLY C 962                    
SITE     2 BC1  6 JAK C1201  HOH C1448                                          
SITE     1 BC2  1 GLN C1098                                                     
SITE     1 BC3  5 LEU C 977  GLN C 980  LEU C1075  TYR C1077                    
SITE     2 BC3  5 HOH C1375                                                     
SITE     1 BC4  7 ASP C1040  SER C1043  TYR C1048  CYS C1052                    
SITE     2 BC4  7 SER C1056  PHE C1058  MET D1099                               
SITE     1 BC5 15 LEU D 881  VAL D 889  ALA D 906  GLU D 957                    
SITE     2 BC5 15 PHE D 958  LEU D 959  GLY D 962  GLU D 966                    
SITE     3 BC5 15 ARG D1007  ASN D1008  LEU D1010  GLY D1020                    
SITE     4 BC5 15 EDO D1202  HOH D1302  HOH D1306                               
SITE     1 BC6  5 ARG D 879  PRO D 960  GLY D 962  JAK D1201                    
SITE     2 BC6  5 HOH D1386                                                     
SITE     1 BC7  8 ASP D 866  PRO D 969  LYS D 970  ASN D 971                    
SITE     2 BC7  8 LYS D 972  ASN D 973  HOH D1368  HOH D1392                    
CRYST1   42.712  172.175   88.035  90.00  92.28  90.00 P 1 21 1      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      0.023413  0.000000  0.000932        0.00000                         
SCALE2      0.000000  0.005808  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011368        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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