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Database: PDB
Entry: 5E1E
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HEADER    TRANSFERASE                             29-SEP-15   5E1E              
TITLE     HUMAN JAK1 KINASE IN COMPLEX WITH COMPOUND 30 AT 2.30 ANGSTROMS       
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROTEIN KINASE 2 DOMAIN RESIDUES 865-1154;                 
COMPND   5 SYNONYM: JANUS KINASE 1,JAK-1;                                       
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAK1, JAK1A, JAK1B;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    KINASE, TRANSFERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.D.FERGUSON                                                          
REVDAT   3   30-DEC-15 5E1E    1       JRNL                                     
REVDAT   2   16-DEC-15 5E1E    1       JRNL                                     
REVDAT   1   25-NOV-15 5E1E    0                                                
JRNL        AUTH   M.M.VASBINDER,M.ALIMZHANOV,M.AUGUSTIN,G.BEBERNITZ,K.BELL,    
JRNL        AUTH 2 C.CHUAQUI,T.DEEGAN,A.D.FERGUSON,K.GOODWIN,D.HUSZAR,          
JRNL        AUTH 3 A.KAWATKAR,S.KAWATKAR,J.READ,J.SHI,S.STEINBACHER,H.STEUBER,  
JRNL        AUTH 4 Q.SU,D.TOADER,H.WANG,R.WOESSNER,A.WU,M.YE,M.ZINDA            
JRNL        TITL   IDENTIFICATION OF AZABENZIMIDAZOLES AS POTENT JAK1 SELECTIVE 
JRNL        TITL 2 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  26    60 2016              
JRNL        REFN                   ESSN 1464-3405                               
JRNL        PMID   26614408                                                     
JRNL        DOI    10.1016/J.BMCL.2015.11.031                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30693                          
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)  : 0.227                          
REMARK   3   R VALUE            (WORKING SET)  : 0.225                          
REMARK   3   FREE R VALUE                      : 0.268                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.270                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1312                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 15                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.38                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.23                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2950                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2384                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2823                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2355                   
REMARK   3   BIN FREE R VALUE                        : 0.3053                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.31                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 127                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4591                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.99270                                              
REMARK   3    B22 (A**2) : -0.31510                                             
REMARK   3    B33 (A**2) : -2.67760                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.325               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.370               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.250               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.347               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.247               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4827   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6513   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1745   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 123    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 728    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4827   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 587    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 5524   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.57                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|867 - A|959 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.9740  -19.4140   15.0570           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0313 T22:    0.0868                                    
REMARK   3     T33:   -0.0313 T12:   -0.0170                                    
REMARK   3     T13:   -0.0288 T23:   -0.0201                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7456 L22:    3.8336                                    
REMARK   3     L33:    1.2851 L12:    0.9631                                    
REMARK   3     L13:   -0.6017 L23:   -0.8177                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0861 S12:   -0.3458 S13:    0.1309                     
REMARK   3     S21:    0.2585 S22:   -0.1475 S23:   -0.0875                     
REMARK   3     S31:   -0.2010 S32:    0.1450 S33:    0.0614                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { A|961 - A|1154 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.2400  -37.7960   23.4880           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0013 T22:    0.1495                                    
REMARK   3     T33:    0.0134 T12:   -0.0212                                    
REMARK   3     T13:   -0.0265 T23:    0.0681                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3834 L22:    0.7403                                    
REMARK   3     L33:    1.5177 L12:    0.0979                                    
REMARK   3     L13:    0.6399 L23:   -0.3185                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0772 S12:   -0.5779 S13:   -0.4077                     
REMARK   3     S21:    0.0837 S22:   -0.0755 S23:   -0.0274                     
REMARK   3     S31:    0.1179 S32:   -0.1654 S33:   -0.0016                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { B|867 - B|959 }                                      
REMARK   3    ORIGIN FOR THE GROUP (A):   -9.4120   24.5780   15.2320           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0168 T22:    0.1036                                    
REMARK   3     T33:   -0.0437 T12:   -0.0157                                    
REMARK   3     T13:   -0.0254 T23:   -0.0096                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7162 L22:    3.1789                                    
REMARK   3     L33:    1.0996 L12:    0.4941                                    
REMARK   3     L13:   -0.7192 L23:   -0.7138                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0581 S12:   -0.1811 S13:    0.1468                     
REMARK   3     S21:    0.1491 S22:   -0.0570 S23:   -0.1515                     
REMARK   3     S31:   -0.2519 S32:    0.2717 S33:   -0.0011                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { B|961 - B|1154 }                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -25.9230    6.3090   23.3770           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0403 T22:    0.1110                                    
REMARK   3     T33:   -0.0122 T12:   -0.0092                                    
REMARK   3     T13:   -0.0249 T23:    0.0260                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1254 L22:    0.8529                                    
REMARK   3     L33:    1.1440 L12:    0.0792                                    
REMARK   3     L13:    0.4627 L23:   -0.1817                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0319 S12:   -0.4217 S13:   -0.2304                     
REMARK   3     S21:    0.0684 S22:   -0.0830 S23:   -0.0198                     
REMARK   3     S31:    0.1499 S32:   -0.1608 S33:    0.0511                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214170.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30744                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.460                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% (M/V) PEG6000, 0.1 M MES/NAOH PH     
REMARK 280  6.0 AND 5 MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
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       21.54750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.46400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.35400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       87.46400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.54750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.35400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   912                                                      
REMARK 465     GLU A   913                                                      
REMARK 465     SER A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLY A   916                                                      
REMARK 465     GLU A   946                                                      
REMARK 465     ASP A   947                                                      
REMARK 465     GLY A   948                                                      
REMARK 465     GLY A   949                                                      
REMARK 465     PRO B   912                                                      
REMARK 465     GLU B   913                                                      
REMARK 465     SER B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLY B   916                                                      
REMARK 465     ASP B   947                                                      
REMARK 465     GLY B   948                                                      
REMARK 465     GLY B   949                                                      
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 895       71.26   -118.90                                   
REMARK 500    GLN A 998       46.93     70.31                                   
REMARK 500    ARG A1002       -0.01     64.83                                   
REMARK 500    ASP A1003       34.11   -140.69                                   
REMARK 500    ASP A1021       87.79     50.16                                   
REMARK 500    ASP A1042       41.30   -107.99                                   
REMARK 500    ILE B 878      -62.38   -103.38                                   
REMARK 500    ILE B 878      -67.91   -103.38                                   
REMARK 500    ASP B 895       71.62   -118.70                                   
REMARK 500    ASP B1003       33.88   -141.01                                   
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 PEG A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5JG A 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5JG B 1201                
DBREF  5E1E A  865  1154  UNP    P23458   JAK1_HUMAN     865   1154             
DBREF  5E1E B  865  1154  UNP    P23458   JAK1_HUMAN     865   1154             
SEQRES   1 A  290  VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG          
SEQRES   2 A  290  ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU          
SEQRES   3 A  290  LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU          
SEQRES   4 A  290  GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY          
SEQRES   5 A  290  ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU          
SEQRES   6 A  290  ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY          
SEQRES   7 A  290  ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE          
SEQRES   8 A  290  MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU          
SEQRES   9 A  290  PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU          
SEQRES  10 A  290  LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU          
SEQRES  11 A  290  GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG          
SEQRES  12 A  290  ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY          
SEQRES  13 A  290  ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU          
SEQRES  14 A  290  PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE          
SEQRES  15 A  290  TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR          
SEQRES  16 A  290  ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS          
SEQRES  17 A  290  GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET          
SEQRES  18 A  290  ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN          
SEQRES  19 A  290  MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY          
SEQRES  20 A  290  LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL          
SEQRES  21 A  290  TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER          
SEQRES  22 A  290  ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU          
SEQRES  23 A  290  ALA LEU LEU LYS                                              
SEQRES   1 B  290  VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG          
SEQRES   2 B  290  ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU          
SEQRES   3 B  290  LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU          
SEQRES   4 B  290  GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY          
SEQRES   5 B  290  ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU          
SEQRES   6 B  290  ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY          
SEQRES   7 B  290  ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE          
SEQRES   8 B  290  MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU          
SEQRES   9 B  290  PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU          
SEQRES  10 B  290  LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU          
SEQRES  11 B  290  GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG          
SEQRES  12 B  290  ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY          
SEQRES  13 B  290  ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU          
SEQRES  14 B  290  PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE          
SEQRES  15 B  290  TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR          
SEQRES  16 B  290  ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS          
SEQRES  17 B  290  GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET          
SEQRES  18 B  290  ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN          
SEQRES  19 B  290  MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY          
SEQRES  20 B  290  LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL          
SEQRES  21 B  290  TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER          
SEQRES  22 B  290  ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU          
SEQRES  23 B  290  ALA LEU LEU LYS                                              
MODRES 5E1E PTR A 1034  TYR  MODIFIED RESIDUE                                   
MODRES 5E1E PTR A 1035  TYR  MODIFIED RESIDUE                                   
MODRES 5E1E PTR B 1034  TYR  MODIFIED RESIDUE                                   
MODRES 5E1E PTR B 1035  TYR  MODIFIED RESIDUE                                   
HET    PTR  A1034      16                                                       
HET    PTR  A1035      16                                                       
HET    PTR  B1034      16                                                       
HET    PTR  B1035      16                                                       
HET    PEG  A1201       7                                                       
HET    5JG  A1202      29                                                       
HET    5JG  B1201      29                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     5JG 6-CHLORO-2-(2-FLUORO-4,5-DIMETHOXYPHENYL)-N-(PIPERIDIN-          
HETNAM   2 5JG  4-YLMETHYL)-3H-IMIDAZO[4,5-B]PYRIDIN-7-AMINE                    
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   3  PEG    C4 H10 O3                                                    
FORMUL   4  5JG    2(C20 H23 CL F N5 O2)                                        
FORMUL   6  HOH   *227(H2 O)                                                    
HELIX    1 AA1 GLU A  871  ARG A  873  5                                   3    
HELIX    2 AA2 HIS A  918  ASN A  931  1                                  14    
HELIX    3 AA3 SER A  963  ASN A  971  1                                   9    
HELIX    4 AA4 ASN A  976  ARG A  997  1                                  22    
HELIX    5 AA5 ALA A 1005  ARG A 1007  5                                   3    
HELIX    6 AA6 PRO A 1044  TYR A 1048  5                                   5    
HELIX    7 AA7 ALA A 1049  GLN A 1055  1                                   7    
HELIX    8 AA8 ILE A 1060  THR A 1076  1                                  17    
HELIX    9 AA9 ASP A 1079  SER A 1082  5                                   4    
HELIX   10 AB1 SER A 1083  GLY A 1093  1                                  11    
HELIX   11 AB2 HIS A 1096  GLN A 1098  5                                   3    
HELIX   12 AB3 MET A 1099  GLU A 1110  1                                  12    
HELIX   13 AB4 PRO A 1121  LYS A 1130  1                                  10    
HELIX   14 AB5 CYS A 1131  GLU A 1133  5                                   3    
HELIX   15 AB6 GLN A 1135  ARG A 1139  5                                   5    
HELIX   16 AB7 SER A 1141  LYS A 1154  1                                  14    
HELIX   17 AB8 GLU B  871  ARG B  873  5                                   3    
HELIX   18 AB9 HIS B  918  ASN B  931  1                                  14    
HELIX   19 AC1 SER B  963  LEU B  968  1                                   6    
HELIX   20 AC2 PRO B  969  ASN B  971  5                                   3    
HELIX   21 AC3 ASN B  976  ARG B  997  1                                  22    
HELIX   22 AC4 ALA B 1005  ARG B 1007  5                                   3    
HELIX   23 AC5 PRO B 1044  TYR B 1048  5                                   5    
HELIX   24 AC6 ALA B 1049  GLN B 1055  1                                   7    
HELIX   25 AC7 ILE B 1060  THR B 1076  1                                  17    
HELIX   26 AC8 ASP B 1079  SER B 1082  5                                   4    
HELIX   27 AC9 SER B 1083  GLY B 1093  1                                  11    
HELIX   28 AD1 HIS B 1096  GLN B 1098  5                                   3    
HELIX   29 AD2 MET B 1099  GLU B 1110  1                                  12    
HELIX   30 AD3 PRO B 1121  LYS B 1130  1                                  10    
HELIX   31 AD4 CYS B 1131  GLU B 1133  5                                   3    
HELIX   32 AD5 GLN B 1135  ARG B 1139  5                                   5    
HELIX   33 AD6 SER B 1141  LYS B 1154  1                                  14    
SHEET    1 AA1 5 LEU A 875  GLU A 883  0                                        
SHEET    2 AA1 5 GLY A 887  TYR A 894 -1  O  LEU A 891   N  ILE A 878           
SHEET    3 AA1 5 GLU A 903  LEU A 910 -1  O  VAL A 907   N  GLU A 890           
SHEET    4 AA1 5 LYS A 953  GLU A 957 -1  O  MET A 956   N  ALA A 906           
SHEET    5 AA1 5 TYR A 940  CYS A 944 -1  N  LYS A 941   O  ILE A 955           
SHEET    1 AA2 2 TYR A 999  VAL A1000  0                                        
SHEET    2 AA2 2 LYS A1026  ALA A1027 -1  O  LYS A1026   N  VAL A1000           
SHEET    1 AA3 2 VAL A1009  SER A1013  0                                        
SHEET    2 AA3 2 GLN A1016  ILE A1019 -1  O  LYS A1018   N  LEU A1010           
SHEET    1 AA4 2 PTR A1034  THR A1036  0                                        
SHEET    2 AA4 2 LYS A1057  TYR A1059 -1  O  PHE A1058   N  PTR A1035           
SHEET    1 AA5 5 LEU B 875  GLY B 884  0                                        
SHEET    2 AA5 5 GLY B 887  TYR B 894 -1  O  LEU B 891   N  ARG B 879           
SHEET    3 AA5 5 GLU B 903  LEU B 910 -1  O  VAL B 907   N  GLU B 890           
SHEET    4 AA5 5 ILE B 952  GLU B 957 -1  O  MET B 956   N  ALA B 906           
SHEET    5 AA5 5 TYR B 940  THR B 945 -1  N  LYS B 941   O  ILE B 955           
SHEET    1 AA6 2 TYR B 999  VAL B1000  0                                        
SHEET    2 AA6 2 LYS B1026  ALA B1027 -1  O  LYS B1026   N  VAL B1000           
SHEET    1 AA7 2 VAL B1009  SER B1013  0                                        
SHEET    2 AA7 2 GLN B1016  ILE B1019 -1  O  LYS B1018   N  LEU B1010           
SHEET    1 AA8 2 PTR B1034  THR B1036  0                                        
SHEET    2 AA8 2 LYS B1057  TYR B1059 -1  O  PHE B1058   N  PTR B1035           
LINK         C   GLU A1033                 N   PTR A1034     1555   1555  1.35  
LINK         C   PTR A1034                 N   PTR A1035     1555   1555  1.35  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.35  
LINK         C   GLU B1033                 N   PTR B1034     1555   1555  1.34  
LINK         C   PTR B1034                 N   PTR B1035     1555   1555  1.35  
LINK         C   PTR B1035                 N   THR B1036     1555   1555  1.36  
SITE     1 AC1  4 ARG A 879  ARG A 893  GLN A 904  HOH A1329                    
SITE     1 AC2 14 LEU A 881  ALA A 906  MET A 956  GLU A 957                    
SITE     2 AC2 14 PHE A 958  LEU A 959  PRO A 960  GLY A 962                    
SITE     3 AC2 14 GLU A 966  ARG A1007  ASN A1008  LEU A1010                    
SITE     4 AC2 14 ASP A1021  HOH A1391                                          
SITE     1 AC3 14 LEU B 881  ALA B 906  MET B 956  GLU B 957                    
SITE     2 AC3 14 PHE B 958  LEU B 959  PRO B 960  GLY B 962                    
SITE     3 AC3 14 GLU B 966  ARG B1007  ASN B1008  LEU B1010                    
SITE     4 AC3 14 GLY B1020  ASP B1021                                          
CRYST1   43.095   88.708  174.928  90.00  90.00  90.00 P 21 21 21    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      0.023205  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005717        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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