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Database: PDB
Entry: 3EYG
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HEADER    TRANSFERASE                             20-OCT-08   3EYG              
TITLE     CRYSTAL STRUCTURES OF JAK1 AND JAK2 INHIBITOR COMPLEXES               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.10.2;                                                        
COMPND   5 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, HCG_22179;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    JAK KINASE, ATP-BINDING, KINASE, NUCLEOTIDE-BINDING,                  
KEYWDS   2 PHOSPHOPROTEIN, SH2 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN            
KEYWDS   3 KINASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.K.WILLIAMS,R.S.BAMERT,O.PATELL,C.WANG,P.M.WALDEN,E.FANTINO          
REVDAT   4   29-DEC-09 3EYG    1       REMARK                                   
REVDAT   3   05-MAY-09 3EYG    1       JRNL                                     
REVDAT   2   10-FEB-09 3EYG    1       TITLE                                    
REVDAT   1   03-FEB-09 3EYG    0                                                
JRNL        AUTH   N.K.WILLIAMS,R.S.BAMERT,O.PATEL,C.WANG,P.M.WALDEN,           
JRNL        AUTH 2 A.F.WILKS,E.FANTINO,J.ROSSJOHN,I.S.LUCET                     
JRNL        TITL   DISSECTING SPECIFICITY IN THE JANUS KINASES: THE             
JRNL        TITL 2 STRUCTURES OF JAK-SPECIFIC INHIBITORS COMPLEXED TO           
JRNL        TITL 3 THE JAK1 AND JAK2 PROTEIN TYROSINE KINASE DOMAINS.           
JRNL        REF    J.MOL.BIOL.                   V. 387   219 2009              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   19361440                                                     
JRNL        DOI    10.1016/J.JMB.2009.01.041                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 23336                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1188                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1603                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 265                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : 0.65000                                              
REMARK   3    B33 (A**2) : -0.72000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.153         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.096         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.289         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2373 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3202 ; 1.535 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   281 ; 6.017 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;40.932 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   436 ;14.149 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;13.819 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   343 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1764 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1175 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1626 ; 0.314 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   233 ; 0.174 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    65 ; 0.182 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.225 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1457 ; 2.318 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2277 ; 3.516 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1059 ; 5.791 ; 7.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   925 ; 8.533 ;10.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3EYG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049924.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26544                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.91700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.91700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       22.51250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.10900            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       22.51250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.10900            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.91700            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       22.51250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.10900            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.91700            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       22.51250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.10900            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1229  LIES ON A SPECIAL POSITION.                          
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     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 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     PRO A 912    CG   CD                                             
REMARK 470     GLU A 946    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 950    CG   OD1  ND2                                       
REMARK 470     GLU A1029    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PRO A  1118     O    HOH A  1318              2.09            
REMARK 500   O    GLU A  1012     O    HOH A  1331              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1369     O    HOH A  1392     4555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A 885      -76.65    -73.28                                   
REMARK 500    ASP A1003       37.53   -153.23                                   
REMARK 500    PHE A1022       28.09   -141.71                                   
REMARK 500    ASP A1031       -8.96     74.04                                   
REMARK 500    ASN A1119       -4.35     79.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL A  865     ASP A  866                  146.20                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1373        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A1411        DISTANCE =  5.21 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MI1 A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3EYH   RELATED DB: PDB                                   
DBREF  3EYG A  865  1154  UNP    Q59GQ2   Q59GQ2_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                                              
MODRES 3EYG PTR A 1034  TYR  O-PHOSPHOTYROSINE                                  
MODRES 3EYG PTR A 1035  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A1034      16                                                       
HET    PTR  A1035      16                                                       
HET    MI1  A   1      23                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     MI1 3-{(3R,4R)-4-METHYL-3-[METHYL(7H-PYRROLO[2,3-                    
HETNAM   2 MI1  D]PYRIMIDIN-4-YL)AMINO]PIPERIDIN-1-YL}-3-                       
HETNAM   3 MI1  OXOPROPANENITRILE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     MI1 CP-690,550                                                       
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   2  MI1    C16 H20 N6 O                                                 
FORMUL   3  HOH   *265(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  LEU A  968  1                                   6    
HELIX    4   4 PRO A  969  LYS A  972  5                                   4    
HELIX    5   5 ASN A  976  ARG A  997  1                                  22    
HELIX    6   6 ALA A 1005  ARG A 1007  5                                   3    
HELIX    7   7 PRO A 1044  TYR A 1048  5                                   5    
HELIX    8   8 ALA A 1049  SER A 1056  1                                   8    
HELIX    9   9 ILE A 1060  THR A 1076  1                                  17    
HELIX   10  10 ASP A 1079  SER A 1082  5                                   4    
HELIX   11  11 SER A 1083  GLY A 1093  1                                  11    
HELIX   12  12 HIS A 1096  GLN A 1098  5                                   3    
HELIX   13  13 MET A 1099  GLU A 1110  1                                  12    
HELIX   14  14 PRO A 1121  CYS A 1131  1                                  11    
HELIX   15  15 GLN A 1135  ARG A 1139  5                                   5    
HELIX   16  16 SER A 1141  ALA A 1151  1                                  11    
SHEET    1   A 5 LEU A 875  GLU A 883  0                                        
SHEET    2   A 5 GLY A 887  TYR A 894 -1  O  VAL A 889   N  LEU A 881           
SHEET    3   A 5 GLN A 904  LEU A 910 -1  O  VAL A 905   N  CYS A 892           
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 A1034  THR A1036  0                                        
SHEET    2   D 2 LYS A1057  TYR A1059 -1  O  PHE A1058   N  PTR A1035           
LINK         C   GLU A1033                 N   PTR A1034     1555   1555  1.33  
LINK         C   PTR A1034                 N   PTR A1035     1555   1555  1.33  
LINK         C   PTR A1035                 N   THR A1036     1555   1555  1.33  
SITE     1 AC1 17 LEU A 881  GLY A 882  GLU A 883  GLY A 884                    
SITE     2 AC1 17 GLY A 887  VAL A 889  ALA A 906  LYS A 908                    
SITE     3 AC1 17 GLU A 957  PHE A 958  LEU A 959  ARG A1007                    
SITE     4 AC1 17 ASN A1008  LEU A1010  GLY A1020  ASP A1021                    
SITE     5 AC1 17 HOH A1157                                                     
CRYST1   45.025   88.218  145.834  90.00  90.00  90.00 C 2 2 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      0.022210  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011336  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006857        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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