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Database: PDB
Entry: 4FK6
LinkDB: 4FK6
Original site: 4FK6 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       12-JUN-12   4FK6              
TITLE     JAK1 KINASE (JH1 DOMAIN) IN COMPLEX WITH COMPOUND 72                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: JH1 (KINASE) DOMAIN, UNP RESIDUES 854-1154;                
COMPND   5 SYNONYM: JANUS KINASE 1, JAK-1;                                      
COMPND   6 EC: 2.7.10.2;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAK1, JAK1A, JAK1B;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PROTEIN KINASE, PHOSPHO TRANSFER, PHOSPHO TYROSINE, TRANSFERASE-      
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.EIGENBROT,M.STEFFEK                                                 
REVDAT   2   12-DEC-12 4FK6    1       JRNL                                     
REVDAT   1   07-NOV-12 4FK6    0                                                
JRNL        AUTH   S.LABADIE,P.S.DRAGOVICH,K.BARRETT,W.S.BLAIR,P.BERGERON,      
JRNL        AUTH 2 C.CHANG,G.DESHMUKH,C.EIGENBROT,N.GHILARDI,P.GIBBONS,         
JRNL        AUTH 3 C.A.HURLEY,A.JOHNSON,J.R.KENNY,P.B.KOHLI,J.J.KULAGOWSKI,     
JRNL        AUTH 4 M.LIIMATTA,P.J.LUPARDUS,R.MENDONCA,J.M.MURRAY,R.PULK,S.SHIA, 
JRNL        AUTH 5 M.STEFFEK,S.UBHAYAKAR,M.ULTSCH,A.VAN ABBEMA,S.WARD,M.ZAK     
JRNL        TITL   STRUCTURE-BASED DISCOVERY OF C-2 SUBSTITUTED                 
JRNL        TITL 2 IMIDAZO-PYRROLOPYRIDINE JAK1 INHIBITORS WITH IMPROVED        
JRNL        TITL 3 SELECTIVITY OVER JAK2.                                       
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  7627 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   23107482                                                     
JRNL        DOI    10.1016/J.BMCL.2012.10.008                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 31252                          
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)  : 0.211                          
REMARK   3   R VALUE            (WORKING SET)  : 0.209                          
REMARK   3   FREE R VALUE                      : 0.251                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.770                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1490                           
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               : 16                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.27                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.80                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2426                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2340                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2304                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2343                   
REMARK   3   BIN FREE R VALUE                        : 0.2284                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.03                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 122                      
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            : 4663                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 50                                      
REMARK   3   SOLVENT ATOMS            : 138                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.97710                                             
REMARK   3    B22 (A**2) : 10.59140                                             
REMARK   3    B33 (A**2) : -5.61430                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.35730                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.35                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.30                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4858   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6565   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1723   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 129    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 679    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4858   ; 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   : 599    ; 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   : 5448   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.05                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.82                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.45                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|863 - 959}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.9286   58.2786   -2.2774           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0407 T22:   -0.0088                                    
REMARK   3     T33:    0.0859 T12:   -0.0055                                    
REMARK   3     T13:   -0.0897 T23:    0.0040                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1550 L22:    3.2615                                    
REMARK   3     L33:    4.2499 L12:   -0.5793                                    
REMARK   3     L13:    0.6994 L23:   -1.0282                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0043 S12:    0.0877 S13:   -0.1441                     
REMARK   3     S21:   -0.5491 S22:    0.0393 S23:    0.5394                     
REMARK   3     S31:    0.0969 S32:   -0.2396 S33:   -0.0350                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|960 - 1154}                                         
REMARK   3    ORIGIN FOR THE GROUP (A):   12.3396   51.3381   16.8743           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0630 T22:   -0.1010                                    
REMARK   3     T33:   -0.0233 T12:   -0.0111                                    
REMARK   3     T13:   -0.0735 T23:    0.0068                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9540 L22:    3.9066                                    
REMARK   3     L33:    1.4106 L12:   -0.1008                                    
REMARK   3     L13:    0.2568 L23:   -0.7722                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0659 S12:   -0.0898 S13:   -0.1486                     
REMARK   3     S21:    0.5483 S22:    0.0490 S23:   -0.4495                     
REMARK   3     S31:   -0.0196 S32:    0.0875 S33:    0.0169                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {B|864 - 959}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   25.8555    3.8943   -1.7435           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1338 T22:   -0.0047                                    
REMARK   3     T33:    0.0457 T12:    0.0238                                    
REMARK   3     T13:    0.0722 T23:   -0.0038                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7484 L22:    3.6513                                    
REMARK   3     L33:    4.0917 L12:   -0.0518                                    
REMARK   3     L13:   -0.2821 L23:    0.9831                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0098 S12:    0.1948 S13:    0.1526                     
REMARK   3     S21:   -0.5394 S22:    0.0836 S23:   -0.5491                     
REMARK   3     S31:   -0.1105 S32:    0.1886 S33:   -0.0739                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {B|960 - 1154}                                         
REMARK   3    ORIGIN FOR THE GROUP (A):    9.0946   10.2559   16.9032           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0274 T22:   -0.0740                                    
REMARK   3     T33:   -0.0641 T12:    0.0160                                    
REMARK   3     T13:    0.0460 T23:   -0.0041                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9873 L22:    4.1065                                    
REMARK   3     L33:    1.6495 L12:   -0.1365                                    
REMARK   3     L13:   -0.1872 L23:    0.8917                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1034 S12:   -0.1076 S13:    0.1512                     
REMARK   3     S21:    0.5409 S22:    0.0743 S23:    0.3813                     
REMARK   3     S31:   -0.0158 S32:   -0.1024 S33:    0.0291                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TLS APPLIED USING 4 GROUPS                
REMARK   4                                                                      
REMARK   4 4FK6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073000.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31252                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -2.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2B7A                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES/PEG6000, PH 5.5, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 300K                                      
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       84.98300            
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                                                    
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     GLY A   853                                                      
REMARK 465     ASP A   854                                                      
REMARK 465     ILE A   855                                                      
REMARK 465     VAL A   856                                                      
REMARK 465     SER A   857                                                      
REMARK 465     GLU A   858                                                      
REMARK 465     LYS A   859                                                      
REMARK 465     LYS A   860                                                      
REMARK 465     PRO A   861                                                      
REMARK 465     ALA A   862                                                      
REMARK 465     GLY A   884                                                      
REMARK 465     HIS A   885                                                      
REMARK 465     SER A   914                                                      
REMARK 465     GLY A   915                                                      
REMARK 465     GLY A   916                                                      
REMARK 465     GLY B   853                                                      
REMARK 465     ASP B   854                                                      
REMARK 465     ILE B   855                                                      
REMARK 465     VAL B   856                                                      
REMARK 465     SER B   857                                                      
REMARK 465     GLU B   858                                                      
REMARK 465     LYS B   859                                                      
REMARK 465     LYS B   860                                                      
REMARK 465     PRO B   861                                                      
REMARK 465     ALA B   862                                                      
REMARK 465     THR B   863                                                      
REMARK 465     SER B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLY B   916                                                      
REMARK 465     ASP B   947                                                      
REMARK 465     GLY B   948                                                      
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 A1002       -2.02     70.60                                   
REMARK 500    ASP A1003       39.04   -144.34                                   
REMARK 500    ARG B1002       -1.92     70.80                                   
REMARK 500    ASP B1003       39.32   -144.85                                   
REMARK 500    LYS B1038      -60.08   -108.44                                   
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 0UJ A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0UJ B 1201                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4E4N   RELATED DB: PDB                                   
REMARK 900 JAK1 KINASE INHIBITOR COMPLEX                                        
REMARK 900 RELATED ID: 4E4L   RELATED DB: PDB                                   
REMARK 900 JAK1 KINASE INHIBITOR COMPLEX                                        
DBREF  4FK6 A  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
DBREF  4FK6 B  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
SEQADV 4FK6 GLY A  853  UNP  P23458              EXPRESSION TAG                 
SEQADV 4FK6 GLY B  853  UNP  P23458              EXPRESSION TAG                 
SEQRES   1 A  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 A  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 A  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 A  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 A  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 A  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 A  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 A  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 A  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 A  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 A  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 A  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 A  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 A  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 A  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 A  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 A  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 A  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 A  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 A  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 A  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 A  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 A  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 A  302  LEU LEU LYS                                                  
SEQRES   1 B  302  GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL          
SEQRES   2 B  302  ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE          
SEQRES   3 B  302  ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU          
SEQRES   4 B  302  CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN          
SEQRES   5 B  302  VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN          
SEQRES   6 B  302  HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG          
SEQRES   7 B  302  ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE          
SEQRES   8 B  302  CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET          
SEQRES   9 B  302  GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO          
SEQRES  10 B  302  LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS          
SEQRES  11 B  302  TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY          
SEQRES  12 B  302  SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  13 B  302  VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP          
SEQRES  14 B  302  PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR          
SEQRES  15 B  302  PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP          
SEQRES  16 B  302  TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE          
SEQRES  17 B  302  ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU          
SEQRES  18 B  302  LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA          
SEQRES  19 B  302  LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET          
SEQRES  20 B  302  THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS          
SEQRES  21 B  302  ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR          
SEQRES  22 B  302  GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN          
SEQRES  23 B  302  ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA          
SEQRES  24 B  302  LEU LEU LYS                                                  
MODRES 4FK6 PTR A 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4FK6 PTR A 1035  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4FK6 PTR B 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4FK6 PTR B 1035  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1034      16                                                       
HET    PTR  A1035      16                                                       
HET    PTR  B1034      16                                                       
HET    PTR  B1035      16                                                       
HET    0UJ  A1201      25                                                       
HET    0UJ  B1201      25                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     0UJ N-({1-[(1R,2R,4S)-BICYCLO[2.2.1]HEPT-2-YL]-1,6-                  
HETNAM   2 0UJ  DIHYDROIMIDAZO[4,5-D]PYRROLO[2,3-B]PYRIDIN-2-                   
HETNAM   3 0UJ  YL}METHYL)METHANESULFONAMIDE                                    
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   3  0UJ    2(C17 H21 N5 O2 S)                                           
FORMUL   5  HOH   *138(H2 O)                                                    
HELIX    1   1 GLU A  871  ARG A  873  5                                   3    
HELIX    2   2 HIS A  918  ASN A  931  1                                  14    
HELIX    3   3 SER A  963  ASN A  971  1                                   9    
HELIX    4   4 ASN A  976  ARG A  997  1                                  22    
HELIX    5   5 ALA A 1005  ARG A 1007  5                                   3    
HELIX    6   6 PRO A 1044  TYR A 1048  5                                   5    
HELIX    7   7 ALA A 1049  SER A 1056  1                                   8    
HELIX    8   8 TYR A 1059  THR A 1076  1                                  18    
HELIX    9   9 ASP A 1079  SER A 1082  5                                   4    
HELIX   10  10 SER A 1083  GLY A 1093  1                                  11    
HELIX   11  11 HIS A 1096  GLN A 1098  5                                   3    
HELIX   12  12 MET A 1099  GLU A 1110  1                                  12    
HELIX   13  13 PRO A 1121  TRP A 1132  1                                  12    
HELIX   14  14 GLN A 1135  ARG A 1139  5                                   5    
HELIX   15  15 SER A 1141  LYS A 1154  1                                  14    
HELIX   16  16 GLU B  871  ARG B  873  5                                   3    
HELIX   17  17 HIS B  918  ASN B  931  1                                  14    
HELIX   18  18 SER B  963  LYS B  972  1                                  10    
HELIX   19  19 ASN B  976  ARG B  997  1                                  22    
HELIX   20  20 ALA B 1005  ARG B 1007  5                                   3    
HELIX   21  21 PRO B 1044  TYR B 1048  5                                   5    
HELIX   22  22 ALA B 1049  SER B 1056  1                                   8    
HELIX   23  23 TYR B 1059  THR B 1076  1                                  18    
HELIX   24  24 ASP B 1079  SER B 1082  5                                   4    
HELIX   25  25 SER B 1083  GLY B 1093  1                                  11    
HELIX   26  26 HIS B 1096  GLN B 1098  5                                   3    
HELIX   27  27 MET B 1099  GLU B 1110  1                                  12    
HELIX   28  28 PRO B 1121  TRP B 1132  1                                  12    
HELIX   29  29 GLN B 1135  ARG B 1139  5                                   5    
HELIX   30  30 SER B 1141  LYS B 1154  1                                  14    
SHEET    1   A 5 LEU A 875  GLY A 882  0                                        
SHEET    2   A 5 GLY A 887  TYR A 894 -1  O  VAL A 889   N  GLY A 882           
SHEET    3   A 5 GLU A 903  LEU A 910 -1  O  GLU A 903   N  TYR A 894           
SHEET    4   A 5 ILE A 952  GLU A 957 -1  O  MET A 956   N  ALA A 906           
SHEET    5   A 5 TYR A 940  THR A 945 -1  N  GLY A 942   O  ILE A 955           
SHEET    1   B 2 TYR A 999  VAL A1000  0                                        
SHEET    2   B 2 LYS A1026  ALA A1027 -1  O  LYS A1026   N  VAL A1000           
SHEET    1   C 2 VAL A1009  SER A1013  0                                        
SHEET    2   C 2 GLN A1016  ILE A1019 -1  O  LYS A1018   N  LEU A1010           
SHEET    1   D 2 PTR A1035  THR A1036  0                                        
SHEET    2   D 2 LYS A1057  PHE A1058 -1  O  PHE A1058   N  PTR A1035           
SHEET    1   E 6 HIS B 869  PHE B 870  0                                        
SHEET    2   E 6 TYR B 940  THR B 945  1  O  ILE B 943   N  PHE B 870           
SHEET    3   E 6 ILE B 952  GLU B 957 -1  O  ILE B 955   N  GLY B 942           
SHEET    4   E 6 GLU B 903  LEU B 910 -1  N  ALA B 906   O  MET B 956           
SHEET    5   E 6 GLY B 887  TYR B 894 -1  N  TYR B 894   O  GLU B 903           
SHEET    6   E 6 LEU B 875  GLU B 883 -1  N  GLY B 882   O  VAL B 889           
SHEET    1   F 2 TYR B 999  VAL B1000  0                                        
SHEET    2   F 2 LYS B1026  ALA B1027 -1  O  LYS B1026   N  VAL B1000           
SHEET    1   G 2 VAL B1009  SER B1013  0                                        
SHEET    2   G 2 GLN B1016  ILE B1019 -1  O  LYS B1018   N  LEU B1010           
SHEET    1   H 2 PTR B1035  THR B1036  0                                        
SHEET    2   H 2 LYS B1057  PHE B1058 -1  O  PHE B1058   N  PTR B1035           
LINK         C   GLU A1033                 N   PTR A1034     1555   1555  1.34  
LINK         C   PTR A1034                 N   PTR A1035     1555   1555  1.34  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.34  
LINK         C   GLU B1033                 N   PTR B1034     1555   1555  1.34  
LINK         C   PTR B1034                 N   PTR B1035     1555   1555  1.34  
LINK         C   PTR B1035                 N   THR B1036     1555   1555  1.35  
SITE     1 AC1 12 ARG A 879  LEU A 881  ALA A 906  GLU A 957                    
SITE     2 AC1 12 PHE A 958  LEU A 959  GLY A 962  GLU A 966                    
SITE     3 AC1 12 ARG A1007  ASN A1008  LEU A1010  GLY A1020                    
SITE     1 AC2 12 ARG B 879  LEU B 881  ALA B 906  GLU B 957                    
SITE     2 AC2 12 PHE B 958  LEU B 959  GLY B 962  GLU B 966                    
SITE     3 AC2 12 ARG B1007  ASN B1008  LEU B1010  GLY B1020                    
CRYST1   43.248  169.966   43.805  90.00  90.51  90.00 P 1 21 1      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      0.023122  0.000000  0.000206        0.00000                         
SCALE2      0.000000  0.005884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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