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Database: PDB
Entry: 3ZEP
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HEADER    TRANSFERASE                             06-DEC-12   3ZEP              
TITLE     CRYSTAL STRUCTURE OF JAK3 KINASE DOMAIN IN COMPLEX WITH A             
TITLE    2 PYRROLOPYRAZINE-2-PHENYL ETHER INHIBITOR                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 813-1100;                          
COMPND   5 SYNONYM: JANUS KINASE 3, JAK-3, LEUKOCYTE JANUS KINASE, L-JAK;       
COMPND   6 EC: 2.7.10.2, 2.7.1.112;                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSFERASE, STAT5, STAT6, INTERLEUKIN-2, COMMON-GAMMA CHAIN, ATP     
KEYWDS   2 SITE KINASE INHIBITOR, CANCER, SCID, SEVERE COMBINED                 
KEYWDS   3 IMMUNODEFICIENCY                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,A.JESTEL,S.NAGEL,J.BOETTCHER,M.BLAESSE                  
REVDAT   2   14-SEP-16 3ZEP    1       SEQADV                                   
REVDAT   1   11-DEC-13 3ZEP    0                                                
JRNL        AUTH   S.JAIME-FIGUEROA,J.DE VICENTE,J.HERMANN,A.JAHANGIR,S.JIN,    
JRNL        AUTH 2 A.KUGLSTATTER,S.M.LYNCH,J.MENKE,L.NIU,V.PATEL,A.SHAO,M.SOTH, 
JRNL        AUTH 3 M.D.VU,C.YEE                                                 
JRNL        TITL   DISCOVERY OF A SERIES OF NOVEL 5H-PYRROLO[2,3-B]PYRAZINE-2-  
JRNL        TITL 2 PHENYL ETHERS, AS POTENT JAK3 KINASE INHIBITORS.             
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  23  2522 2013              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23541670                                                     
JRNL        DOI    10.1016/J.BMCL.2013.03.015                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 103.70                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.83                          
REMARK   3   NUMBER OF REFLECTIONS             : 52795                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.22627                         
REMARK   3   R VALUE            (WORKING SET) : 0.22559                         
REMARK   3   FREE R VALUE                     : 0.26484                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 924                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.353                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.414                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3527                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.290                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 64                           
REMARK   3   BIN FREE R VALUE                    : 0.382                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8850                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 130                                     
REMARK   3   SOLVENT ATOMS            : 279                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.076                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.55                                                
REMARK   3    B22 (A**2) : -2.15                                                
REMARK   3    B33 (A**2) : 4.85                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.66                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.400         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.263         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.219         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.145        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.920                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9000 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6345 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12201 ; 1.098 ; 2.013       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15267 ; 0.981 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1084 ; 5.078 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   382 ;33.631 ;22.853       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1467 ;11.645 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    75 ;12.959 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1318 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9885 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1902 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   814        A   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.281   -8.343   -0.117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0842 T22:  -0.0446                                     
REMARK   3      T33:  -0.1062 T12:  -0.0172                                     
REMARK   3      T13:   0.0127 T23:   0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2597 L22:   5.1879                                     
REMARK   3      L33:   2.4571 L12:  -0.3515                                     
REMARK   3      L13:  -0.6432 L23:   1.3075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0139 S12:   0.0397 S13:   0.5239                       
REMARK   3      S21:  -0.3375 S22:   0.1291 S23:  -0.5781                       
REMARK   3      S31:  -0.1131 S32:   0.1524 S33:  -0.1153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   905        A  1098                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -15.012  -25.295   14.428              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0936 T22:  -0.0449                                     
REMARK   3      T33:  -0.1937 T12:  -0.0252                                     
REMARK   3      T13:  -0.0192 T23:  -0.0062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8693 L22:   2.9489                                     
REMARK   3      L33:   3.0824 L12:  -0.1513                                     
REMARK   3      L13:  -0.1212 L23:  -0.5443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0111 S12:  -0.1723 S13:  -0.0121                       
REMARK   3      S21:   0.2546 S22:   0.0498 S23:  -0.1512                       
REMARK   3      S31:   0.0716 S32:   0.0075 S33:  -0.0608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   814        B   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   19.837   27.604   56.575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0830 T22:  -0.0732                                     
REMARK   3      T33:  -0.0378 T12:  -0.0025                                     
REMARK   3      T13:  -0.0439 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8568 L22:   8.7727                                     
REMARK   3      L33:   0.9865 L12:   1.9583                                     
REMARK   3      L13:   0.7244 L23:  -0.1391                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0420 S12:  -0.0445 S13:  -0.3578                       
REMARK   3      S21:   0.2499 S22:   0.0218 S23:  -0.9276                       
REMARK   3      S31:  -0.0284 S32:   0.2063 S33:   0.0201                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   905        B  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):    6.416   40.243   38.771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0927 T22:  -0.0476                                     
REMARK   3      T33:  -0.0989 T12:   0.0233                                     
REMARK   3      T13:   0.0024 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4342 L22:   3.3973                                     
REMARK   3      L33:   3.1237 L12:  -0.0114                                     
REMARK   3      L13:   0.9912 L23:  -0.1433                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:   0.2850 S13:  -0.0109                       
REMARK   3      S21:  -0.2855 S22:  -0.0462 S23:  -0.1859                       
REMARK   3      S31:  -0.0361 S32:   0.1937 S33:   0.0069                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   814        C   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.372    8.564   56.496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0828 T22:  -0.0350                                     
REMARK   3      T33:  -0.0252 T12:  -0.0024                                     
REMARK   3      T13:   0.0393 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2733 L22:   6.2837                                     
REMARK   3      L33:   1.2317 L12:   0.9323                                     
REMARK   3      L13:  -0.2022 L23:   0.9003                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0301 S12:  -0.1690 S13:   0.3942                       
REMARK   3      S21:   0.2058 S22:  -0.1043 S23:   0.8691                       
REMARK   3      S31:   0.0772 S32:  -0.3241 S33:   0.0742                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   905        C  1100                          
REMARK   3    ORIGIN FOR THE GROUP (A):    9.799   -3.559   37.865              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0568 T22:  -0.0339                                     
REMARK   3      T33:  -0.1144 T12:   0.0488                                     
REMARK   3      T13:  -0.0326 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2912 L22:   2.6876                                     
REMARK   3      L33:   3.0223 L12:  -0.4014                                     
REMARK   3      L13:   0.3693 L23:   0.6885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0287 S12:   0.2986 S13:  -0.0869                       
REMARK   3      S21:  -0.3328 S22:  -0.0202 S23:   0.2150                       
REMARK   3      S31:   0.0056 S32:  -0.0075 S33:  -0.0084                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   814        D   904                          
REMARK   3    ORIGIN FOR THE GROUP (A):   25.680  -47.164    0.287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0607 T22:  -0.0319                                     
REMARK   3      T33:  -0.0991 T12:  -0.0056                                     
REMARK   3      T13:  -0.0322 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3059 L22:   7.6710                                     
REMARK   3      L33:   2.1033 L12:   0.0707                                     
REMARK   3      L13:   0.6709 L23:   1.4897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0977 S12:  -0.0036 S13:  -0.5233                       
REMARK   3      S21:   0.3969 S22:   0.1286 S23:  -0.8526                       
REMARK   3      S31:   0.0605 S32:   0.2128 S33:  -0.0309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   905        D  1099                          
REMARK   3    ORIGIN FOR THE GROUP (A):   13.415  -30.323  -13.828              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0496 T22:  -0.0257                                     
REMARK   3      T33:  -0.1906 T12:   0.0306                                     
REMARK   3      T13:   0.0139 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9701 L22:   3.3074                                     
REMARK   3      L33:   2.4520 L12:   0.1125                                     
REMARK   3      L13:   0.5730 L23:   0.2072                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0379 S12:   0.2006 S13:   0.1353                       
REMARK   3      S21:  -0.3834 S22:   0.0376 S23:  -0.2859                       
REMARK   3      S31:  -0.1042 S32:   0.1196 S33:  -0.0754                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS. U VALUES WITH TLS ADDED.                         
REMARK   3   DISORDERED SIDE CHAINS HAVE OCCUPANCY 0.00                         
REMARK   4                                                                      
REMARK   4 3ZEP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-DEC-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-55017.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55677                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 103.69                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 2.9                                
REMARK 200  R MERGE                    (I) : 0.10                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.70                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC5 RIGID BODY                                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       57.03800            
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     ASP A   813                                                      
REMARK 465     GLY A   892                                                      
REMARK 465     PRO A   893                                                      
REMARK 465     GLY A   894                                                      
REMARK 465     ARG A   895                                                      
REMARK 465     GLN A   896                                                      
REMARK 465     GLU A  1041                                                      
REMARK 465     ARG A  1042                                                      
REMARK 465     ASP A  1043                                                      
REMARK 465     VAL A  1044                                                      
REMARK 465     TRP A  1099                                                      
REMARK 465     SER A  1100                                                      
REMARK 465     ASP B   813                                                      
REMARK 465     GLY B   831                                                      
REMARK 465     ASN B   832                                                      
REMARK 465     PHE B   833                                                      
REMARK 465     GLY B   892                                                      
REMARK 465     PRO B   893                                                      
REMARK 465     GLY B   894                                                      
REMARK 465     ARG B   895                                                      
REMARK 465     GLN B   896                                                      
REMARK 465     GLU B   985                                                      
REMARK 465     PRO B   986                                                      
REMARK 465     GLY B   987                                                      
REMARK 465     GLN B   988                                                      
REMARK 465     SER B  1040                                                      
REMARK 465     GLU B  1041                                                      
REMARK 465     ARG B  1042                                                      
REMARK 465     ASP B  1043                                                      
REMARK 465     VAL B  1044                                                      
REMARK 465     ASP C   813                                                      
REMARK 465     GLY C   831                                                      
REMARK 465     ASN C   832                                                      
REMARK 465     PHE C   833                                                      
REMARK 465     PRO C   893                                                      
REMARK 465     GLY C   894                                                      
REMARK 465     ARG C   895                                                      
REMARK 465     GLN C   896                                                      
REMARK 465     PRO C   986                                                      
REMARK 465     GLY C   987                                                      
REMARK 465     ASP D   813                                                      
REMARK 465     PRO D   893                                                      
REMARK 465     GLY D   894                                                      
REMARK 465     ARG D   895                                                      
REMARK 465     GLN D   896                                                      
REMARK 465     PRO D   986                                                      
REMARK 465     GLY D   987                                                      
REMARK 465     GLN D   988                                                      
REMARK 465     SER D  1040                                                      
REMARK 465     GLU D  1041                                                      
REMARK 465     ARG D  1042                                                      
REMARK 465     ASP D  1043                                                      
REMARK 465     VAL D  1044                                                      
REMARK 465     SER D  1100                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  819   CD   OE1  OE2                                       
REMARK 480     LYS A  823   CE   NZ                                             
REMARK 480     GLN A  858   CG   CD   OE1  NE2                                  
REMARK 480     HIS A  859   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS A  876   CE   NZ                                             
REMARK 480     ARG A  916   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU A  960   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  978   CE   NZ                                             
REMARK 480     ARG A  984   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A  988   CG   CD   OE1  NE2                                  
REMARK 480     LYS A 1026   CG   CD   CE   NZ                                   
REMARK 480     GLN B  858   CG   CD   OE1  NE2                                  
REMARK 480     HIS B  859   CG   ND1  CD2  CE1  NE2                             
REMARK 480     ARG B  870   CZ   NH1  NH2                                       
REMARK 480     LYS B  972   CG   CD   CE   NZ                                   
REMARK 480     LYS B  978   CD   CE   NZ                                        
REMARK 480     ARG B  984   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG B 1049   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU B 1052   CG   CD   OE1  OE2                                  
REMARK 480     LEU B 1053   CG   CD1  CD2                                       
REMARK 480     GLU B 1055   CG   CD   OE1  OE2                                  
REMARK 480     GLN B 1083   CG   CD   OE1  NE2                                  
REMARK 480     TRP B 1099   CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3  CH2         
REMARK 480     GLU C  818   CD   OE1  OE2                                       
REMARK 480     LYS C  830   CG   CD   CE   NZ                                   
REMARK 480     HIS C  859   CG   ND1  CD2  CE1  NE2                             
REMARK 480     ARG C  870   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C  972   CE   NZ                                             
REMARK 480     LYS C  978   CE   NZ                                             
REMARK 480     ARG C  984   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN C  988   CG   CD   OE1  NE2                                  
REMARK 480     ARG C 1036   NE   CZ   NH1  NH2                                  
REMARK 480     LEU C 1047   CG   CD1  CD2                                       
REMARK 480     ARG C 1049   CZ   NH1  NH2                                       
REMARK 480     GLU C 1052   CG   CD   OE1  OE2                                  
REMARK 480     GLU C 1056   CG   CD   OE1  OE2                                  
REMARK 480     GLU C 1069   CG   CD   OE1  OE2                                  
REMARK 480     GLN C 1083   CG   CD   OE1  NE2                                  
REMARK 480     GLU D  819   CD   OE1  OE2                                       
REMARK 480     LYS D  823   CD   CE   NZ                                        
REMARK 480     GLN D  858   CG   CD   OE1  NE2                                  
REMARK 480     HIS D  859   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLN D  865   CD   OE1  NE2                                       
REMARK 480     ARG D  887   CZ   NH1  NH2                                       
REMARK 480     LYS D  978   CE   NZ                                             
REMARK 480     ARG D  984   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS D 1026   CD   CE   NZ                                        
REMARK 480     TRP D 1099   CG   CD1  CD2  NE1  CE2  CE3  CZ2  CZ3  CH2         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY D 892   CA  -  C   -  N   ANGL. DEV. = -71.9 DEGREES          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 846       32.73   -142.00                                   
REMARK 500    ASN A 847       55.85     26.66                                   
REMARK 500    GLN A 858      -63.67    -94.35                                   
REMARK 500    ARG A 948       -0.01     72.81                                   
REMARK 500    ASP A 949       52.12   -157.59                                   
REMARK 500    HIS A 962      118.92   -161.17                                   
REMARK 500    ASP A 967       83.63     58.57                                   
REMARK 500    TRP A1078       33.17    -96.00                                   
REMARK 500    ILE B 825      -66.16   -100.05                                   
REMARK 500    ASN B 847       19.29     59.05                                   
REMARK 500    SER B 860      -70.11    -46.56                                   
REMARK 500    HIS B 917       39.42    -99.06                                   
REMARK 500    ARG B 948       -5.89     73.98                                   
REMARK 500    ASP B 949       38.79   -147.05                                   
REMARK 500    ASP B 967       84.45     62.39                                   
REMARK 500    TRP B1078       35.10    -94.52                                   
REMARK 500    TRP B1099       77.98     63.83                                   
REMARK 500    ILE C 825      -61.07   -105.46                                   
REMARK 500    ASN C 847       16.87     57.60                                   
REMARK 500    ARG C 948      -21.16     76.34                                   
REMARK 500    ASP C 967       86.35     63.59                                   
REMARK 500    ARG C 984       56.62   -100.70                                   
REMARK 500    TRP C1078       31.88    -98.63                                   
REMARK 500    TRP C1099       69.60     63.43                                   
REMARK 500    LEU D 828      -62.83    -90.08                                   
REMARK 500    ASP D 846       27.16   -142.76                                   
REMARK 500    SER D 897     -169.85   -100.47                                   
REMARK 500    ARG D 948      -13.88     79.20                                   
REMARK 500    ASP D 949       51.08   -149.54                                   
REMARK 500    ASP D 967       80.73     59.25                                   
REMARK 500    ARG D 984       74.19   -107.08                                   
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 1NX A2099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NX B2101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NX C2101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1NX D2100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C2102                 
DBREF  3ZEP A  813  1100  UNP    P52333   JAK3_HUMAN     813   1100             
DBREF  3ZEP B  813  1100  UNP    P52333   JAK3_HUMAN     813   1100             
DBREF  3ZEP C  813  1100  UNP    P52333   JAK3_HUMAN     813   1100             
DBREF  3ZEP D  813  1100  UNP    P52333   JAK3_HUMAN     813   1100             
SEQADV 3ZEP SER A 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 3ZEP SER A 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQADV 3ZEP SER B 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 3ZEP SER B 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQADV 3ZEP SER C 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 3ZEP SER C 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQADV 3ZEP SER D 1040  UNP  P52333    CYS  1040 ENGINEERED MUTATION            
SEQADV 3ZEP SER D 1048  UNP  P52333    CYS  1048 ENGINEERED MUTATION            
SEQRES   1 A  288  ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS TYR ILE          
SEQRES   2 A  288  SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL GLU LEU          
SEQRES   3 A  288  CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY ALA LEU          
SEQRES   4 A  288  VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO ASP GLN          
SEQRES   5 A  288  GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU LYS ALA          
SEQRES   6 A  288  LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY VAL SER          
SEQRES   7 A  288  TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL MET GLU          
SEQRES   8 A  288  TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU GLN ARG          
SEQRES   9 A  288  HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU LEU TYR          
SEQRES  10 A  288  SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU GLY SER          
SEQRES  11 A  288  ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE          
SEQRES  12 A  288  LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA ASP PHE          
SEQRES  13 A  288  GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP PTR PTR          
SEQRES  14 A  288  VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE TRP TYR          
SEQRES  15 A  288  ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER ARG GLN          
SEQRES  16 A  288  SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR GLU LEU          
SEQRES  17 A  288  PHE THR TYR CYS ASP LYS SER CYS SER PRO SER ALA GLU          
SEQRES  18 A  288  PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL PRO ALA          
SEQRES  19 A  288  LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY GLN ARG          
SEQRES  20 A  288  LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL HIS GLU          
SEQRES  21 A  288  LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN ASP ARG          
SEQRES  22 A  288  PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP MET LEU          
SEQRES  23 A  288  TRP SER                                                      
SEQRES   1 B  288  ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS TYR ILE          
SEQRES   2 B  288  SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL GLU LEU          
SEQRES   3 B  288  CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY ALA LEU          
SEQRES   4 B  288  VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO ASP GLN          
SEQRES   5 B  288  GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU LYS ALA          
SEQRES   6 B  288  LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY VAL SER          
SEQRES   7 B  288  TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL MET GLU          
SEQRES   8 B  288  TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU GLN ARG          
SEQRES   9 B  288  HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU LEU TYR          
SEQRES  10 B  288  SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU GLY SER          
SEQRES  11 B  288  ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE          
SEQRES  12 B  288  LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA ASP PHE          
SEQRES  13 B  288  GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP PTR PTR          
SEQRES  14 B  288  VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE TRP TYR          
SEQRES  15 B  288  ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER ARG GLN          
SEQRES  16 B  288  SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR GLU LEU          
SEQRES  17 B  288  PHE THR TYR CYS ASP LYS SER CYS SER PRO SER ALA GLU          
SEQRES  18 B  288  PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL PRO ALA          
SEQRES  19 B  288  LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY GLN ARG          
SEQRES  20 B  288  LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL HIS GLU          
SEQRES  21 B  288  LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN ASP ARG          
SEQRES  22 B  288  PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP MET LEU          
SEQRES  23 B  288  TRP SER                                                      
SEQRES   1 C  288  ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS TYR ILE          
SEQRES   2 C  288  SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL GLU LEU          
SEQRES   3 C  288  CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY ALA LEU          
SEQRES   4 C  288  VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO ASP GLN          
SEQRES   5 C  288  GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU LYS ALA          
SEQRES   6 C  288  LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY VAL SER          
SEQRES   7 C  288  TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL MET GLU          
SEQRES   8 C  288  TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU GLN ARG          
SEQRES   9 C  288  HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU LEU TYR          
SEQRES  10 C  288  SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU GLY SER          
SEQRES  11 C  288  ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE          
SEQRES  12 C  288  LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA ASP PHE          
SEQRES  13 C  288  GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP PTR PTR          
SEQRES  14 C  288  VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE TRP TYR          
SEQRES  15 C  288  ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER ARG GLN          
SEQRES  16 C  288  SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR GLU LEU          
SEQRES  17 C  288  PHE THR TYR CYS ASP LYS SER CYS SER PRO SER ALA GLU          
SEQRES  18 C  288  PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL PRO ALA          
SEQRES  19 C  288  LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY GLN ARG          
SEQRES  20 C  288  LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL HIS GLU          
SEQRES  21 C  288  LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN ASP ARG          
SEQRES  22 C  288  PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP MET LEU          
SEQRES  23 C  288  TRP SER                                                      
SEQRES   1 D  288  ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS TYR ILE          
SEQRES   2 D  288  SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL GLU LEU          
SEQRES   3 D  288  CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY ALA LEU          
SEQRES   4 D  288  VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO ASP GLN          
SEQRES   5 D  288  GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU LYS ALA          
SEQRES   6 D  288  LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY VAL SER          
SEQRES   7 D  288  TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL MET GLU          
SEQRES   8 D  288  TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU GLN ARG          
SEQRES   9 D  288  HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU LEU TYR          
SEQRES  10 D  288  SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU GLY SER          
SEQRES  11 D  288  ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE          
SEQRES  12 D  288  LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA ASP PHE          
SEQRES  13 D  288  GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP PTR PTR          
SEQRES  14 D  288  VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE TRP TYR          
SEQRES  15 D  288  ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER ARG GLN          
SEQRES  16 D  288  SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR GLU LEU          
SEQRES  17 D  288  PHE THR TYR CYS ASP LYS SER CYS SER PRO SER ALA GLU          
SEQRES  18 D  288  PHE LEU ARG MET MET GLY SER GLU ARG ASP VAL PRO ALA          
SEQRES  19 D  288  LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY GLN ARG          
SEQRES  20 D  288  LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL HIS GLU          
SEQRES  21 D  288  LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN ASP ARG          
SEQRES  22 D  288  PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP MET LEU          
SEQRES  23 D  288  TRP SER                                                      
MODRES 3ZEP PTR A  980  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR A  981  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR B  980  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR B  981  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR C  980  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR C  981  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR D  980  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3ZEP PTR D  981  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 980      16                                                       
HET    PTR  A 981      16                                                       
HET    PTR  B 980      16                                                       
HET    PTR  B 981      16                                                       
HET    PTR  C 980      16                                                       
HET    PTR  C 981      16                                                       
HET    PTR  D 980      16                                                       
HET    PTR  D 981      16                                                       
HET    1NX  A2099      31                                                       
HET    1NX  B2101      31                                                       
HET    1NX  C2101      31                                                       
HET    1NX  D2100      31                                                       
HET    GOL  C2102       6                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     1NX 2-[[(3R)-3-ACETAMIDO-2,3-DIHYDRO-1H-INDEN-5-                     
HETNAM   2 1NX  YL]OXY]-N-[(1S)-1-CYCLOPROPYLETHYL]-5H-                         
HETNAM   3 1NX  PYRROLO[2,3-B]PYRAZINE-7-CARBOXAMIDE                            
HETNAM     GOL GLYCEROL                                                         
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  PTR    8(C9 H12 N O6 P)                                             
FORMUL   6  1NX    4(C23 H25 N5 O3)                                             
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  HOH   *279(H2 O)                                                    
HELIX    1   1 GLU A  818  ARG A  820  5                                   3    
HELIX    2   2 GLY A  861  LEU A  878  1                                  18    
HELIX    3   3 CYS A  909  HIS A  917  1                                   9    
HELIX    4   4 ASP A  922  ARG A  943  1                                  22    
HELIX    5   5 ALA A  951  ARG A  953  5                                   3    
HELIX    6   6 PRO A  990  TYR A  994  5                                   5    
HELIX    7   7 ALA A  995  ASN A 1002  1                                   8    
HELIX    8   8 SER A 1005  THR A 1022  1                                  18    
HELIX    9   9 SER A 1029  GLY A 1039  1                                  11    
HELIX   10  10 PRO A 1045  GLY A 1057  1                                  13    
HELIX   11  11 PRO A 1067  TRP A 1078  1                                  12    
HELIX   12  12 SER A 1081  ARG A 1085  5                                   5    
HELIX   13  13 SER A 1087  MET A 1097  1                                  11    
HELIX   14  14 GLU B  818  ARG B  820  5                                   3    
HELIX   15  15 GLY B  861  LEU B  878  1                                  18    
HELIX   16  16 CYS B  909  HIS B  917  1                                   9    
HELIX   17  17 ASP B  922  ARG B  943  1                                  22    
HELIX   18  18 ALA B  951  ARG B  953  5                                   3    
HELIX   19  19 PRO B  990  TYR B  994  5                                   5    
HELIX   20  20 ALA B  995  ASN B 1002  1                                   8    
HELIX   21  21 SER B 1005  THR B 1022  1                                  18    
HELIX   22  22 ASP B 1025  CYS B 1028  5                                   4    
HELIX   23  23 SER B 1029  GLY B 1039  1                                  11    
HELIX   24  24 PRO B 1045  GLY B 1057  1                                  13    
HELIX   25  25 PRO B 1067  TRP B 1078  1                                  12    
HELIX   26  26 SER B 1081  ARG B 1085  5                                   5    
HELIX   27  27 SER B 1087  MET B 1097  1                                  11    
HELIX   28  28 GLU C  818  ARG C  820  5                                   3    
HELIX   29  29 GLY C  861  LEU C  878  1                                  18    
HELIX   30  30 CYS C  909  HIS C  917  1                                   9    
HELIX   31  31 ARG C  918  LEU C  921  5                                   4    
HELIX   32  32 ASP C  922  ARG C  943  1                                  22    
HELIX   33  33 ALA C  951  ARG C  953  5                                   3    
HELIX   34  34 PRO C  990  TYR C  994  5                                   5    
HELIX   35  35 ALA C  995  ASN C 1002  1                                   8    
HELIX   36  36 SER C 1005  THR C 1022  1                                  18    
HELIX   37  37 ASP C 1025  CYS C 1028  5                                   4    
HELIX   38  38 SER C 1029  GLY C 1039  1                                  11    
HELIX   39  39 LEU C 1047  GLU C 1056  1                                  10    
HELIX   40  40 PRO C 1067  TRP C 1078  1                                  12    
HELIX   41  41 SER C 1081  ARG C 1085  5                                   5    
HELIX   42  42 SER C 1087  MET C 1097  1                                  11    
HELIX   43  43 GLU D  818  ARG D  820  5                                   3    
HELIX   44  44 GLY D  861  LEU D  878  1                                  18    
HELIX   45  45 CYS D  909  HIS D  917  1                                   9    
HELIX   46  46 ASP D  922  ARG D  943  1                                  22    
HELIX   47  47 ALA D  951  ARG D  953  5                                   3    
HELIX   48  48 PRO D  990  TYR D  994  5                                   5    
HELIX   49  49 ALA D  995  ASN D 1002  1                                   8    
HELIX   50  50 SER D 1005  PHE D 1021  1                                  17    
HELIX   51  51 ASP D 1025  CYS D 1028  5                                   4    
HELIX   52  52 SER D 1029  GLY D 1039  1                                  11    
HELIX   53  53 PRO D 1045  GLU D 1056  1                                  12    
HELIX   54  54 PRO D 1067  TRP D 1078  1                                  12    
HELIX   55  55 SER D 1081  ARG D 1085  5                                   5    
HELIX   56  56 SER D 1087  MET D 1097  1                                  11    
SHEET    1  AA 5 LEU A 822  GLY A 829  0                                        
SHEET    2  AA 5 SER A 835  TYR A 841 -1  O  VAL A 836   N  LEU A 828           
SHEET    3  AA 5 ALA A 850  GLN A 856 -1  O  ALA A 850   N  TYR A 841           
SHEET    4  AA 5 ARG A 899  GLU A 903 -1  O  LEU A 900   N  LYS A 855           
SHEET    5  AA 5 TYR A 886  SER A 890 -1  N  ARG A 887   O  VAL A 901           
SHEET    1  AB 2 CYS A 945  VAL A 946  0                                        
SHEET    2  AB 2 LYS A 972  LEU A 973 -1  O  LYS A 972   N  VAL A 946           
SHEET    1  AC 2 ILE A 955  SER A 959  0                                        
SHEET    2  AC 2 HIS A 962  ILE A 965 -1  O  HIS A 962   N  GLU A 958           
SHEET    1  AD 2 PTR A 981  VAL A 982  0                                        
SHEET    2  AD 2 ILE A1003  PHE A1004 -1  O  PHE A1004   N  PTR A 981           
SHEET    1  BA 5 LEU B 822  GLY B 829  0                                        
SHEET    2  BA 5 SER B 835  TYR B 841 -1  O  VAL B 836   N  LEU B 828           
SHEET    3  BA 5 ALA B 850  GLN B 856 -1  O  ALA B 850   N  TYR B 841           
SHEET    4  BA 5 ARG B 899  GLU B 903 -1  O  LEU B 900   N  LYS B 855           
SHEET    5  BA 5 TYR B 886  SER B 890 -1  N  ARG B 887   O  VAL B 901           
SHEET    1  BB 2 CYS B 945  VAL B 946  0                                        
SHEET    2  BB 2 LYS B 972  LEU B 973 -1  O  LYS B 972   N  VAL B 946           
SHEET    1  BC 2 ILE B 955  SER B 959  0                                        
SHEET    2  BC 2 HIS B 962  ILE B 965 -1  O  HIS B 962   N  GLU B 958           
SHEET    1  BD 2 PTR B 981  VAL B 982  0                                        
SHEET    2  BD 2 ILE B1003  PHE B1004 -1  O  PHE B1004   N  PTR B 981           
SHEET    1  CA 5 LEU C 822  GLY C 829  0                                        
SHEET    2  CA 5 SER C 835  TYR C 841 -1  O  VAL C 836   N  LEU C 828           
SHEET    3  CA 5 LEU C 851  GLN C 856 -1  O  VAL C 852   N  CYS C 839           
SHEET    4  CA 5 ARG C 899  GLU C 903 -1  O  LEU C 900   N  LYS C 855           
SHEET    5  CA 5 TYR C 886  SER C 890 -1  N  ARG C 887   O  VAL C 901           
SHEET    1  CB 2 CYS C 945  VAL C 946  0                                        
SHEET    2  CB 2 LYS C 972  LEU C 973 -1  O  LYS C 972   N  VAL C 946           
SHEET    1  CC 2 ILE C 955  SER C 959  0                                        
SHEET    2  CC 2 HIS C 962  ILE C 965 -1  O  HIS C 962   N  SER C 959           
SHEET    1  CD 2 PTR C 981  VAL C 982  0                                        
SHEET    2  CD 2 ILE C1003  PHE C1004 -1  O  PHE C1004   N  PTR C 981           
SHEET    1  DA 5 LEU D 822  GLY D 829  0                                        
SHEET    2  DA 5 SER D 835  TYR D 841 -1  O  VAL D 836   N  LEU D 828           
SHEET    3  DA 5 ALA D 850  GLN D 856 -1  O  ALA D 850   N  TYR D 841           
SHEET    4  DA 5 ARG D 899  GLU D 903 -1  O  LEU D 900   N  LYS D 855           
SHEET    5  DA 5 TYR D 886  SER D 890 -1  N  ARG D 887   O  VAL D 901           
SHEET    1  DB 2 CYS D 945  VAL D 946  0                                        
SHEET    2  DB 2 LYS D 972  LEU D 973 -1  O  LYS D 972   N  VAL D 946           
SHEET    1  DC 2 ILE D 955  SER D 959  0                                        
SHEET    2  DC 2 HIS D 962  ILE D 965 -1  O  HIS D 962   N  GLU D 958           
SHEET    1  DD 2 PTR D 981  VAL D 982  0                                        
SHEET    2  DD 2 ILE D1003  PHE D1004 -1  O  PHE D1004   N  PTR D 981           
LINK         N   PTR A 980                 C   ASP A 979     1555   1555  1.33  
LINK         C   PTR A 980                 N   PTR A 981     1555   1555  1.33  
LINK         C   PTR A 981                 N   VAL A 982     1555   1555  1.33  
LINK         N   PTR B 980                 C   ASP B 979     1555   1555  1.34  
LINK         C   PTR B 980                 N   PTR B 981     1555   1555  1.33  
LINK         C   PTR B 981                 N   VAL B 982     1555   1555  1.33  
LINK         C   PTR C 980                 N   PTR C 981     1555   1555  1.33  
LINK         N   PTR C 980                 C   ASP C 979     1555   1555  1.33  
LINK         C   PTR C 981                 N   VAL C 982     1555   1555  1.33  
LINK         C   PTR D 980                 N   PTR D 981     1555   1555  1.33  
LINK         N   PTR D 980                 C   ASP D 979     1555   1555  1.33  
LINK         C   PTR D 981                 N   VAL D 982     1555   1555  1.34  
SITE     1 AC1 13 LEU A 828  GLY A 829  LYS A 830  VAL A 836                    
SITE     2 AC1 13 ALA A 853  GLU A 903  TYR A 904  LEU A 905                    
SITE     3 AC1 13 GLY A 908  ASN A 954  LEU A 956  ASP A 967                    
SITE     4 AC1 13 HOH A2025                                                     
SITE     1 AC2 13 GLN B 827  LEU B 828  ALA B 853  MET B 902                    
SITE     2 AC2 13 GLU B 903  TYR B 904  LEU B 905  GLY B 908                    
SITE     3 AC2 13 CYS B 909  ARG B 953  LEU B 956  HOH B2030                    
SITE     4 AC2 13 ARG C 916                                                     
SITE     1 AC3 16 ARG B 916  GLN C 827  LEU C 828  VAL C 836                    
SITE     2 AC3 16 ALA C 853  MET C 902  GLU C 903  TYR C 904                    
SITE     3 AC3 16 LEU C 905  GLY C 908  CYS C 909  ASN C 954                    
SITE     4 AC3 16 LEU C 956  ASP C 967  HOH C2023  HOH C2073                    
SITE     1 AC4 11 LEU D 828  GLY D 829  LYS D 830  VAL D 836                    
SITE     2 AC4 11 ALA D 853  GLU D 903  TYR D 904  LEU D 905                    
SITE     3 AC4 11 CYS D 909  ASN D 954  LEU D 956                               
SITE     1 AC5  2 ARG B 920  GLU C 837                                          
CRYST1   57.554  114.076  104.196  90.00  96.82  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      0.017375  0.000000  0.002078        0.00000                         
SCALE2      0.000000  0.008766  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009666        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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