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Database: PDB
Entry: 6ELR
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Original site: 6ELR 
HEADER    TRANSFERASE                             29-SEP-17   6ELR              
TITLE     HUMAN JAK1 KINASE DOMAIN IN COMPLEX WITH COMPOUND 7                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.7.10.2;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: Y182, Y183 ARE PHOSPHORYLATED                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: JAK1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    JANUS KINASE 1 KINASE DOMAIN (JAK1), TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.READ                                                              
REVDAT   1   10-OCT-18 6ELR    0                                                
JRNL        AUTH   N.P.GRIMSTER,J.A.READ                                        
JRNL        TITL   HUMAN JAK1 KINASE DOMAIN IN COMPLEX WITH COMPOUND 7          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 57849                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.181                          
REMARK   3   FREE R VALUE                      : 0.205                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 3.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1774                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.85                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 91.21                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4037                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2260                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3906                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2250                   
REMARK   3   BIN FREE R VALUE                        : 0.2340                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 3.24                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 131                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4490                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 511                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.94                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.54850                                              
REMARK   3    B22 (A**2) : -0.20750                                             
REMARK   3    B33 (A**2) : -1.34100                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.32980                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.230               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.126               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.113               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.122               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.111               
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      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4680   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6345   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1619   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 109    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 670    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4680   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 591    ; 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   : 5626   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.26                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.21                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    6.6471   23.2008    9.7840           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0770 T22:   -0.1031                                    
REMARK   3     T33:    0.0342 T12:   -0.0298                                    
REMARK   3     T13:    0.0227 T23:   -0.0147                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.0745 L22:    0.8415                                    
REMARK   3     L33:    1.2392 L12:   -0.3847                                    
REMARK   3     L13:    1.2134 L23:   -0.3836                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0951 S12:   -0.0775 S13:   -0.5680                     
REMARK   3     S21:    0.0210 S22:    0.0767 S23:    0.1055                     
REMARK   3     S31:    0.0587 S32:   -0.0449 S33:   -0.1719                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   13.4439  -23.4316   10.1789           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0879 T22:   -0.0686                                    
REMARK   3     T33:   -0.0589 T12:   -0.0205                                    
REMARK   3     T13:    0.0014 T23:   -0.0441                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.9043 L22:    1.4261                                    
REMARK   3     L33:    1.2738 L12:    0.6022                                    
REMARK   3     L13:   -1.1978 L23:   -0.0146                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1647 S12:   -0.3658 S13:    0.5811                     
REMARK   3     S21:    0.0622 S22:   -0.0030 S23:    0.1271                     
REMARK   3     S31:   -0.1017 S32:    0.1193 S33:   -0.1617                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ELR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006804.                                   
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                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999                              
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2MM LIGAND, 27% (M/V) PEG6000, 0.1 M     
REMARK 280  MES/NAOH PH 6.0, 5 MM DTT, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 282K                                                    
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       87.04650            
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 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 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   884                                                      
REMARK 465     HIS A   885                                                      
REMARK 465     PHE A   886                                                      
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     ASN A   917                                                      
REMARK 465     ASP A   947                                                      
REMARK 465     GLY A   948                                                      
REMARK 465     GLY A   949                                                      
REMARK 465     ASP B   854                                                      
REMARK 465     ILE B   855                                                      
REMARK 465     VAL B   856                                                      
REMARK 465     SER B   857                                                      
REMARK 465     GLU B   858                                                      
REMARK 465     LYS B   859                                                      
REMARK 465     LYS B   860                                                      
REMARK 465     PRO B   861                                                      
REMARK 465     ALA B   862                                                      
REMARK 465     THR B   863                                                      
REMARK 465     GLU B   864                                                      
REMARK 465     GLU B   913                                                      
REMARK 465     SER B   914                                                      
REMARK 465     GLY B   915                                                      
REMARK 465     GLY B   916                                                      
REMARK 465     ASN B   917                                                      
REMARK 465     ASP B   947                                                      
REMARK 465     GLY B   948                                                      
REMARK 465     GLY B   949                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 860    CG   CD   CE   NZ                                   
REMARK 470     THR A 863    OG1  CG2                                            
REMARK 470     GLU A 864    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 865    CG1  CG2                                            
REMARK 470     GLU A 883    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 888    CE   NZ                                             
REMARK 470     LYS A 911    CG   CD   CE   NZ                                   
REMARK 470     ILE A 919    CD1                                                 
REMARK 470     LYS A 939    CE   NZ                                             
REMARK 470     ASN A 950    CG   OD1  ND2                                       
REMARK 470     LYS A 970    CD   CE   NZ                                        
REMARK 470     LYS A1032    CE   NZ                                             
REMARK 470     GLU A1033    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1039    CG   OD1  OD2                                       
REMARK 470     ARG A1041    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A1042    CG   OD1  OD2                                       
REMARK 470     GLN A1055    CD   OE1  NE2                                       
REMARK 470     LYS A1090    CD   CE   NZ                                        
REMARK 470     GLN A1098    CG   CD   OE1  NE2                                  
REMARK 470     LYS A1109    CE   NZ                                             
REMARK 470     LYS A1130    CE   NZ                                             
REMARK 470     SER A1137    OG                                                  
REMARK 470     GLU A1147    CD   OE1  OE2                                       
REMARK 470     LYS A1154    CG   CD   CE   NZ                                   
REMARK 470     VAL B 865    CG1  CG2                                            
REMARK 470     LYS B 872    CD   CE   NZ                                        
REMARK 470     LYS B 876    CE   NZ                                             
REMARK 470     HIS B 885    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 888    CE   NZ                                             
REMARK 470     LYS B 911    CG   CD   CE   NZ                                   
REMARK 470     ILE B 919    CD1                                                 
REMARK 470     TYR B 933    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 946    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 965    CD   CE   NZ                                        
REMARK 470     LYS B 970    CE   NZ                                             
REMARK 470     LYS B 974    NZ                                                  
REMARK 470     ARG B 997    CZ   NH1  NH2                                       
REMARK 470     GLN B 998    CD   OE1  NE2                                       
REMARK 470     GLU B1029    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1031    CG   OD1  OD2                                       
REMARK 470     LYS B1032    CD   CE   NZ                                        
REMARK 470     VAL B1037    CB   CG1  CG2                                       
REMARK 470     ASP B1039    CG   OD1  OD2                                       
REMARK 470     ARG B1041    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1042    CG   OD1  OD2                                       
REMARK 470     SER B1056    OG                                                  
REMARK 470     LYS B1057    CE   NZ                                             
REMARK 470     LYS B1090    CD   CE   NZ                                        
REMARK 470     GLN B1098    CG   CD   OE1  NE2                                  
REMARK 470     LYS B1109    CG   CD   CE   NZ                                   
REMARK 470     LYS B1112    CG   CD   CE   NZ                                   
REMARK 470     LYS B1154    CG   CD   CE   NZ                                   
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       66.41   -118.90                                   
REMARK 500    ASP A1003       33.43   -144.49                                   
REMARK 500    THR A1095       55.37   -114.39                                   
REMARK 500    ILE B 878      -60.39   -103.53                                   
REMARK 500    ASP B 895       67.84   -119.85                                   
REMARK 500    ASP B1003       33.54   -144.31                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 976   OD1                                                    
REMARK 620 2 HOH B1304   O    57.3                                              
REMARK 620 3 HOH B1444   O    85.9 105.8                                        
REMARK 620 4 HOH B1379   O   137.3 105.7 136.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BFK A 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BFK B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 1202                 
DBREF  6ELR A  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
DBREF  6ELR B  854  1154  UNP    P23458   JAK1_HUMAN     854   1154             
SEQRES   1 A  301  ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL ASP          
SEQRES   2 A  301  PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE ARG          
SEQRES   3 A  301  ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU CYS          
SEQRES   4 A  301  ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN VAL          
SEQRES   5 A  301  ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN HIS          
SEQRES   6 A  301  ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG ASN          
SEQRES   7 A  301  LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE CYS          
SEQRES   8 A  301  THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET GLU          
SEQRES   9 A  301  PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO LYS          
SEQRES  10 A  301  ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS TYR          
SEQRES  11 A  301  ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY SER          
SEQRES  12 A  301  ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL          
SEQRES  13 A  301  LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP PHE          
SEQRES  14 A  301  GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR PTR          
SEQRES  15 A  301  THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP TYR          
SEQRES  16 A  301  ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE ALA          
SEQRES  17 A  301  SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU LEU          
SEQRES  18 A  301  LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA LEU          
SEQRES  19 A  301  PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET THR          
SEQRES  20 A  301  VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS ARG          
SEQRES  21 A  301  LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR GLN          
SEQRES  22 A  301  LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN ARG          
SEQRES  23 A  301  THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA LEU          
SEQRES  24 A  301  LEU LYS                                                      
SEQRES   1 B  301  ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL ASP          
SEQRES   2 B  301  PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE ARG          
SEQRES   3 B  301  ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU CYS          
SEQRES   4 B  301  ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN VAL          
SEQRES   5 B  301  ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN HIS          
SEQRES   6 B  301  ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG ASN          
SEQRES   7 B  301  LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE CYS          
SEQRES   8 B  301  THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET GLU          
SEQRES   9 B  301  PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO LYS          
SEQRES  10 B  301  ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS TYR          
SEQRES  11 B  301  ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY SER          
SEQRES  12 B  301  ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL          
SEQRES  13 B  301  LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP PHE          
SEQRES  14 B  301  GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR PTR          
SEQRES  15 B  301  THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP TYR          
SEQRES  16 B  301  ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE ALA          
SEQRES  17 B  301  SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU LEU          
SEQRES  18 B  301  LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA LEU          
SEQRES  19 B  301  PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET THR          
SEQRES  20 B  301  VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS ARG          
SEQRES  21 B  301  LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR GLN          
SEQRES  22 B  301  LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN ARG          
SEQRES  23 B  301  THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA LEU          
SEQRES  24 B  301  LEU LYS                                                      
MODRES 6ELR PTR A 1034  TYR  MODIFIED RESIDUE                                   
MODRES 6ELR PTR A 1035  TYR  MODIFIED RESIDUE                                   
MODRES 6ELR PTR B 1034  TYR  MODIFIED RESIDUE                                   
MODRES 6ELR PTR B 1035  TYR  MODIFIED RESIDUE                                   
HET    PTR  A1034      16                                                       
HET    PTR  A1035      16                                                       
HET    PTR  B1034      16                                                       
HET    PTR  B1035      16                                                       
HET    BFK  A1201      34                                                       
HET    BFK  B1201      34                                                       
HET     NA  B1202       1                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     BFK [3-[[5-METHYL-2-[[3-(4-METHYLPIPERAZIN-1-YL)-5-                  
HETNAM   2 BFK  METHYLSULFONYL-PHENYL]AMINO]PYRIMIDIN-4-                        
HETNAM   3 BFK  YL]AMINO]PHENYL]METHANOL                                        
HETNAM      NA SODIUM ION                                                       
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    4(C9 H12 N O6 P)                                             
FORMUL   3  BFK    2(C24 H30 N6 O3 S)                                           
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *511(H2 O)                                                    
HELIX    1 AA1 GLU A  871  ARG A  873  5                                   3    
HELIX    2 AA2 ILE A  919  ASN A  931  1                                  13    
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  SER A 1056  1                                   8    
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  CYS A 1131  1                                  11    
HELIX   14 AB5 GLN A 1135  ARG A 1139  5                                   5    
HELIX   15 AB6 SER A 1141  LYS A 1154  1                                  14    
HELIX   16 AB7 GLU B  871  ARG B  873  5                                   3    
HELIX   17 AB8 ILE B  919  ASN B  931  1                                  13    
HELIX   18 AB9 SER B  963  ASN B  971  1                                   9    
HELIX   19 AC1 ASN B  976  ARG B  997  1                                  22    
HELIX   20 AC2 ALA B 1005  ARG B 1007  5                                   3    
HELIX   21 AC3 PRO B 1044  TYR B 1048  5                                   5    
HELIX   22 AC4 ALA B 1049  SER B 1056  1                                   8    
HELIX   23 AC5 ILE B 1060  THR B 1076  1                                  17    
HELIX   24 AC6 ASP B 1079  SER B 1082  5                                   4    
HELIX   25 AC7 SER B 1083  GLY B 1093  1                                  11    
HELIX   26 AC8 HIS B 1096  GLN B 1098  5                                   3    
HELIX   27 AC9 MET B 1099  GLU B 1110  1                                  12    
HELIX   28 AD1 PRO B 1121  CYS B 1131  1                                  11    
HELIX   29 AD2 GLN B 1135  ARG B 1139  5                                   5    
HELIX   30 AD3 SER B 1141  LYS B 1154  1                                  14    
SHEET    1 AA1 5 LEU A 875  GLY A 882  0                                        
SHEET    2 AA1 5 LYS A 888  TYR A 894 -1  O  LEU A 891   N  ARG A 879           
SHEET    3 AA1 5 GLU A 903  SER A 909 -1  O  GLU A 903   N  TYR A 894           
SHEET    4 AA1 5 ILE A 952  GLU A 957 -1  O  MET A 956   N  ALA A 906           
SHEET    5 AA1 5 TYR A 940  THR A 945 -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  GLU B 903   N  TYR B 894           
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  GLY B 942   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  1.34  
LINK         C   PTR A1034                 N   PTR A1035     1555   1555  1.35  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.35  
LINK         OD1 ASN B 976                NA    NA B1202     1555   1555  2.84  
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  
LINK        NA    NA B1202                 O   HOH B1304     1555   1555  3.06  
LINK        NA    NA B1202                 O   HOH B1444     1555   1555  2.92  
LINK        NA    NA B1202                 O   HOH B1379     1555   1555  2.27  
SITE     1 AC1 17 ARG A 879  LEU A 881  VAL A 889  ALA A 906                    
SITE     2 AC1 17 MET A 956  GLU A 957  PHE A 958  LEU A 959                    
SITE     3 AC1 17 PRO A 960  GLY A 962  SER A 963  GLU A 966                    
SITE     4 AC1 17 ARG A1007  ASN A1008  LEU A1010  GLY A1020                    
SITE     5 AC1 17 HOH A1386                                                     
SITE     1 AC2 17 ARG B 879  LEU B 881  VAL B 889  ALA B 906                    
SITE     2 AC2 17 MET B 956  GLU B 957  PHE B 958  LEU B 959                    
SITE     3 AC2 17 PRO B 960  GLY B 962  GLU B 966  ARG B1007                    
SITE     4 AC2 17 ASN B1008  LEU B1010  GLY B1020  HOH B1337                    
SITE     5 AC2 17 HOH B1354                                                     
SITE     1 AC3  5 ASN B 976  LYS B 978  HOH B1304  HOH B1379                    
SITE     2 AC3  5 HOH B1444                                                     
CRYST1   42.991  174.093   44.968  90.00  94.37  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      0.023261  0.000000  0.001778        0.00000                         
SCALE2      0.000000  0.005744  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022303        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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