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Database: PDB
Entry: 3LXL
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HEADER    TRANSFERASE                             25-FEB-10   3LXL              
TITLE     STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF THE TYK2 AND JAK3    
TITLE    2 KINASE DOMAINS IN COMPLEX WITH CP-690550 AND CMP-6                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK3;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN;                                             
COMPND   5 SYNONYM: JANUS KINASE 3, JAK-3, LEUKOCYTE JANUS KINASE, L-JAK;       
COMPND   6 EC: 2.7.10.2;                                                        
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 GENE: JAK3;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST9                                    
KEYWDS    TYK2, JAK3, INFLAMMATION, CANCER, PAN INHIBITOR, ATP-BINDING, DISEASE 
KEYWDS   2 MUTATION, KINASE, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,      
KEYWDS   3 SCID, SH2 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.CHRENCIK,T.E.BENSON                                               
REVDAT   2   28-JUL-10 3LXL    1       JRNL                                     
REVDAT   1   02-JUN-10 3LXL    0                                                
JRNL        AUTH   J.E.CHRENCIK,A.PATNY,I.K.LEUNG,B.KORNISKI,T.L.EMMONS,T.HALL, 
JRNL        AUTH 2 R.A.WEINBERG,J.A.GORMLEY,J.M.WILLIAMS,J.E.DAY,J.L.HIRSCH,    
JRNL        AUTH 3 J.R.KIEFER,J.W.LEONE,H.D.FISCHER,C.D.SOMMERS,H.C.HUANG,      
JRNL        AUTH 4 E.J.JACOBSEN,R.E.TENBRINK,A.G.TOMASSELLI,T.E.BENSON          
JRNL        TITL   STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF THE TYK2    
JRNL        TITL 2 AND JAK3 KINASE DOMAINS IN COMPLEX WITH CP-690550 AND CMP-6. 
JRNL        REF    J.MOL.BIOL.                   V. 400   413 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20478313                                                     
JRNL        DOI    10.1016/J.JMB.2010.05.020                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.74 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.74                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31422                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1678                            
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) : 1.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.78                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2260                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.16                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 111                          
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2217                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 289                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.06000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.119         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.115         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.146         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2325 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1619 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3156 ; 1.364 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3917 ; 0.986 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   283 ; 8.240 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   106 ;35.287 ;22.925       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   384 ;12.714 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.748 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   333 ; 0.204 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2618 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   486 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   481 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1733 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1142 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1157 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   182 ; 0.137 ; 0.200       
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):    12 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    59 ; 0.343 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.117 ; 0.200       
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):  1467 ; 0.893 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   568 ; 0.181 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2272 ; 1.340 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1080 ; 1.832 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   883 ; 2.869 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3LXL COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057856.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31422                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.130                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.03000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 47.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.560                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1YVJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-3350, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.02% PHENYLUREA, PH 7.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       23.59600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.53500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.59350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.53500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.59600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.59350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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     MET A   798                                                      
REMARK 465     GLY A   799                                                      
REMARK 465     HIS A   800                                                      
REMARK 465     HIS A   801                                                      
REMARK 465     HIS A   802                                                      
REMARK 465     HIS A   803                                                      
REMARK 465     HIS A   804                                                      
REMARK 465     HIS A   805                                                      
REMARK 465     ALA A   806                                                      
REMARK 465     GLN A   807                                                      
REMARK 465     LEU A   808                                                      
REMARK 465     TYR A   809                                                      
REMARK 465     ALA A   810                                                      
REMARK 465     CYS A   811                                                      
REMARK 465     GLN A   812                                                      
REMARK 465     ASP A   813                                                      
REMARK 465     CYS A  1040                                                      
REMARK 465     GLU A  1041                                                      
REMARK 465     ARG A  1042                                                      
REMARK 465     ASP A  1043                                                      
REMARK 465     TRP A  1099                                                      
REMARK 465     SER A  1100                                                      
REMARK 465     GLY A  1101                                                      
REMARK 465     SER A  1102                                                      
REMARK 465     ARG A  1103                                                      
REMARK 465     GLY A  1104                                                      
REMARK 465     CYS A  1105                                                      
REMARK 465     GLU A  1106                                                      
REMARK 465     THR A  1107                                                      
REMARK 465     HIS A  1108                                                      
REMARK 465     ALA A  1109                                                      
REMARK 465     PHE A  1110                                                      
REMARK 465     THR A  1111                                                      
REMARK 465     ALA A  1112                                                      
REMARK 465     HIS A  1113                                                      
REMARK 465     PRO A  1114                                                      
REMARK 465     GLU A  1115                                                      
REMARK 465     GLY A  1116                                                      
REMARK 465     LYS A  1117                                                      
REMARK 465     HIS A  1118                                                      
REMARK 465     HIS A  1119                                                      
REMARK 465     SER A  1120                                                      
REMARK 465     LEU A  1121                                                      
REMARK 465     SER A  1122                                                      
REMARK 465     PHE A  1123                                                      
REMARK 465     SER A  1124                                                      
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     LYS A 830    NZ                                                  
REMARK 470     ARG A 984    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 985    CD   OE1  OE2                                       
REMARK 470     LYS A1026    CD   CE   NZ                                        
REMARK 470     VAL A1044    CG1  CG2                                            
REMARK 470     ARG A1049    CD   NE   CZ   NH1  NH2                             
REMARK 470     SER A1081    OG                                                  
REMARK 470     GLN A1083    CD   OE1  NE2                                       
REMARK 470     MET A1097    SD   CE                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   938     O    HOH A   102              2.09            
REMARK 500   O    HOH A   103     O    HOH A   340              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 948      -11.64     80.12                                   
REMARK 500    ASP A 967       61.73     63.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  894     ARG A  895                  141.55                    
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 IZA A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LXK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3LXN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3LXP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FUP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EYG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3EYH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2B7A   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1YVJ   RELATED DB: PDB                                   
DBREF  3LXL A  806  1124  UNP    P52333   JAK3_HUMAN     806   1124             
SEQADV 3LXL MET A  798  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL GLY A  799  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  800  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  801  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  802  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  803  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  804  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL HIS A  805  UNP  P52333              EXPRESSION TAG                 
SEQADV 3LXL SER A 1048  UNP  P52333    CYS  1048 ENGINEERED                     
SEQRES   1 A  327  MET GLY HIS HIS HIS HIS HIS HIS ALA GLN LEU TYR ALA          
SEQRES   2 A  327  CYS GLN ASP PRO THR ILE PHE GLU GLU ARG HIS LEU LYS          
SEQRES   3 A  327  TYR ILE SER GLN LEU GLY LYS GLY ASN PHE GLY SER VAL          
SEQRES   4 A  327  GLU LEU CYS ARG TYR ASP PRO LEU GLY ASP ASN THR GLY          
SEQRES   5 A  327  ALA LEU VAL ALA VAL LYS GLN LEU GLN HIS SER GLY PRO          
SEQRES   6 A  327  ASP GLN GLN ARG ASP PHE GLN ARG GLU ILE GLN ILE LEU          
SEQRES   7 A  327  LYS ALA LEU HIS SER ASP PHE ILE VAL LYS TYR ARG GLY          
SEQRES   8 A  327  VAL SER TYR GLY PRO GLY ARG GLN SER LEU ARG LEU VAL          
SEQRES   9 A  327  MET GLU TYR LEU PRO SER GLY CYS LEU ARG ASP PHE LEU          
SEQRES  10 A  327  GLN ARG HIS ARG ALA ARG LEU ASP ALA SER ARG LEU LEU          
SEQRES  11 A  327  LEU TYR SER SER GLN ILE CYS LYS GLY MET GLU TYR LEU          
SEQRES  12 A  327  GLY SER ARG ARG CYS VAL HIS ARG ASP LEU ALA ALA ARG          
SEQRES  13 A  327  ASN ILE LEU VAL GLU SER GLU ALA HIS VAL LYS ILE ALA          
SEQRES  14 A  327  ASP PHE GLY LEU ALA LYS LEU LEU PRO LEU ASP LYS ASP          
SEQRES  15 A  327  TYR TYR VAL VAL ARG GLU PRO GLY GLN SER PRO ILE PHE          
SEQRES  16 A  327  TRP TYR ALA PRO GLU SER LEU SER ASP ASN ILE PHE SER          
SEQRES  17 A  327  ARG GLN SER ASP VAL TRP SER PHE GLY VAL VAL LEU TYR          
SEQRES  18 A  327  GLU LEU PHE THR TYR CYS ASP LYS SER CYS SER PRO SER          
SEQRES  19 A  327  ALA GLU PHE LEU ARG MET MET GLY CYS GLU ARG ASP VAL          
SEQRES  20 A  327  PRO ALA LEU SER ARG LEU LEU GLU LEU LEU GLU GLU GLY          
SEQRES  21 A  327  GLN ARG LEU PRO ALA PRO PRO ALA CYS PRO ALA GLU VAL          
SEQRES  22 A  327  HIS GLU LEU MET LYS LEU CYS TRP ALA PRO SER PRO GLN          
SEQRES  23 A  327  ASP ARG PRO SER PHE SER ALA LEU GLY PRO GLN LEU ASP          
SEQRES  24 A  327  MET LEU TRP SER GLY SER ARG GLY CYS GLU THR HIS ALA          
SEQRES  25 A  327  PHE THR ALA HIS PRO GLU GLY LYS HIS HIS SER LEU SER          
SEQRES  26 A  327  PHE SER                                                      
HET    IZA  A   1      23                                                       
HETNAM     IZA 2-TERT-BUTYL-9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-IMIDAZ[4,           
HETNAM   2 IZA  5-F]ISOQUINOLINE-7-ONE                                          
HETSYN     IZA 2-(1,1-DIMETHYLETHYL)9-FLUORO-3,6-DIHYDRO-7H-BENZ[H]-            
HETSYN   2 IZA  IMIDAZ[4,5-F]ISOQUINOLIN-7-ONE                                  
FORMUL   2  IZA    C18 H16 F N3 O                                               
FORMUL   3  HOH   *289(H2 O)                                                    
HELIX    1   1 GLU A  818  ARG A  820  5                                   3    
HELIX    2   2 GLY A  861  ALA A  877  1                                  17    
HELIX    3   3 CYS A  909  ARG A  918  1                                  10    
HELIX    4   4 ALA A  919  LEU A  921  5                                   3    
HELIX    5   5 ASP A  922  ARG A  943  1                                  22    
HELIX    6   6 ALA A  951  ARG A  953  5                                   3    
HELIX    7   7 ASP A  967  ALA A  971  5                                   5    
HELIX    8   8 PRO A  990  TYR A  994  5                                   5    
HELIX    9   9 ALA A  995  ASN A 1002  1                                   8    
HELIX   10  10 ARG A 1006  THR A 1022  1                                  17    
HELIX   11  11 ASP A 1025  CYS A 1028  5                                   4    
HELIX   12  12 SER A 1029  MET A 1038  1                                  10    
HELIX   13  13 PRO A 1045  GLU A 1056  1                                  12    
HELIX   14  14 PRO A 1067  TRP A 1078  1                                  12    
HELIX   15  15 SER A 1081  ARG A 1085  5                                   5    
HELIX   16  16 SER A 1087  LEU A 1098  1                                  12    
SHEET    1   A 5 LEU A 822  GLY A 831  0                                        
SHEET    2   A 5 GLY A 834  TYR A 841 -1  O  ARG A 840   N  LYS A 823           
SHEET    3   A 5 ALA A 850  LEU A 857 -1  O  ALA A 850   N  TYR A 841           
SHEET    4   A 5 SER A 897  GLU A 903 -1  O  MET A 902   N  ALA A 853           
SHEET    5   A 5 TYR A 886  TYR A 891 -1  N  GLY A 888   O  VAL A 901           
SHEET    1   B 2 CYS A 945  VAL A 946  0                                        
SHEET    2   B 2 LYS A 972  LEU A 973 -1  O  LYS A 972   N  VAL A 946           
SHEET    1   C 2 ILE A 955  SER A 959  0                                        
SHEET    2   C 2 HIS A 962  ILE A 965 -1  O  LYS A 964   N  LEU A 956           
SHEET    1   D 2 TYR A 980  VAL A 982  0                                        
SHEET    2   D 2 ILE A1003  SER A1005 -1  O  PHE A1004   N  TYR A 981           
SITE     1 AC1 13 HOH A   2  HOH A 273  LEU A 828  LYS A 830                    
SITE     2 AC1 13 VAL A 836  ALA A 853  HIS A 859  GLU A 903                    
SITE     3 AC1 13 TYR A 904  LEU A 905  GLY A 908  ASN A 954                    
SITE     4 AC1 13 LEU A 956                                                     
CRYST1   47.192   75.187   89.070  90.00  90.00  90.00 P 21 21 21    4          
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      0.021190  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011227        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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