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Database: PDB
Entry: 4TWP
LinkDB: 4TWP
Original site: 4TWP 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       01-JUL-14   4TWP              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN ABL1 T315I GATEKEEPER MUTANT KINASE    
TITLE    2 DOMAIN IN COMPLEX WITH AXITINIB                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE-PROTEIN KINASE ABL1;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 252-522;                                      
COMPND   5 SYNONYM: ABELSON MURINE LEUKEMIA VIRAL ONCOGENE HOMOLOG 1,ABELSON    
COMPND   6 TYROSINE-PROTEIN KINASE 1,PROTO-ONCOGENE C-ABL,P150;                 
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ABL1, ABL, JTK7;                                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    GATEKEEPER MUTANT KINASE DOMAIN DFGIN, TRANSFERASE-TRANSFERASE        
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.JOHNSON,M.MCTIGUE,C.N.CRONIN                                        
REVDAT   5   22-NOV-17 4TWP    1       SOURCE REMARK                            
REVDAT   4   13-MAY-15 4TWP    1       DBREF                                    
REVDAT   3   18-MAR-15 4TWP    1       JRNL                                     
REVDAT   2   04-MAR-15 4TWP    1       JRNL                                     
REVDAT   1   11-FEB-15 4TWP    0                                                
JRNL        AUTH   T.PEMOVSKA,E.JOHNSON,M.KONTRO,G.A.REPASKY,J.CHEN,P.WELLS,    
JRNL        AUTH 2 C.N.CRONIN,M.MCTIGUE,O.KALLIONIEMI,K.PORKKA,B.W.MURRAY,      
JRNL        AUTH 3 K.WENNERBERG                                                 
JRNL        TITL   AXITINIB EFFECTIVELY INHIBITS BCR-ABL1(T315I) WITH A         
JRNL        TITL 2 DISTINCT BINDING CONFORMATION.                               
JRNL        REF    NATURE                        V. 519   102 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   25686603                                                     
JRNL        DOI    10.1038/NATURE14119                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 52.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33967                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1681                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 52.1488 -  5.4927    0.99     2869   153  0.2067 0.2257        
REMARK   3     2  5.4927 -  4.3604    1.00     2738   140  0.1775 0.1982        
REMARK   3     3  4.3604 -  3.8094    0.99     2700   132  0.1860 0.2054        
REMARK   3     4  3.8094 -  3.4612    0.99     2688   145  0.2089 0.2454        
REMARK   3     5  3.4612 -  3.2131    1.00     2671   138  0.2156 0.2326        
REMARK   3     6  3.2131 -  3.0237    1.00     2682   144  0.2275 0.2778        
REMARK   3     7  3.0237 -  2.8723    1.00     2648   149  0.2290 0.2515        
REMARK   3     8  2.8723 -  2.7473    1.00     2665   143  0.2437 0.3044        
REMARK   3     9  2.7473 -  2.6415    1.00     2650   144  0.2612 0.3152        
REMARK   3    10  2.6415 -  2.5504    1.00     2663   130  0.2661 0.3020        
REMARK   3    11  2.5504 -  2.4706    1.00     2632   129  0.2792 0.3055        
REMARK   3    12  2.4706 -  2.4000    1.00     2680   134  0.2770 0.3586        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 43.95                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.690            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.630           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 49.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.85560                                             
REMARK   3    B22 (A**2) : 5.45750                                              
REMARK   3    B33 (A**2) : 2.39810                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4538                                  
REMARK   3   ANGLE     :  1.126           6141                                  
REMARK   3   CHIRALITY :  0.079            646                                  
REMARK   3   PLANARITY :  0.005            774                                  
REMARK   3   DIHEDRAL  : 16.554           1679                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4TWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202346.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
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 : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.20, XSCALE               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.957                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.200                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES (PH 7.00) 15.0 %W/V PEG      
REMARK 280  3350 0.01 M MAGNESIUM CHLORIDE HEXAHYDRATE 0.0050 M NICKEL(II)      
REMARK 280  CHLORIDE HEXAHYDRATE 5.0 %V/V GLYCEROL, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 286.15K                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.90050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.58200            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.90050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.58200            
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     LYS A   274                                                      
REMARK 465     GLU A   275                                                      
REMARK 465     ASP A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     MET A   278                                                      
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 B 400    CG   CD   CE   NZ                                   
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    HOH A   709     O    HOH A   747              2.02            
REMARK 500   O    HOH A   819     O    HOH A   822              2.04            
REMARK 500   OE2  GLU A   236     OG1  THR A   306              2.13            
REMARK 500   NH2  ARG A   460     O    HOH A   701              2.14            
REMARK 500   O    THR B   389     O    HOH B   701              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   OD2  ASP A   444     OE2  GLU B   459     4855     2.18            
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 295      142.15   -173.14                                   
REMARK 500    ASN A 336     -157.55   -104.06                                   
REMARK 500    ARG A 362       -5.53     83.70                                   
REMARK 500    ALA A 365      163.65    176.52                                   
REMARK 500    ALA A 380     -169.40   -126.10                                   
REMARK 500    ASP A 381       73.68     57.38                                   
REMARK 500    LYS B 262     -111.24     58.96                                   
REMARK 500    ARG B 362      -18.83     78.18                                   
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                              NI A 602  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 352   OE2                                                    
REMARK 620 2 HOH A 738   O    75.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 603  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 490   NE2                                                    
REMARK 620 2 GLU A 494   OE1  65.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 602  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 352   OE1                                                    
REMARK 620 2 GLU B 352   OE2  51.6                                              
REMARK 620 3 HOH B 720   O    69.2 120.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 603  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 490   NE2                                                    
REMARK 620 2 GLU B 494   OE1  69.8                                              
REMARK 620 3 HOH B 705   O    68.3  53.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 605  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 707   O                                                      
REMARK 620 2 HOH A 714   O    86.4                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AXI A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AXI B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NI B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 604                  
DBREF  4TWP A  233   503  UNP    P00519   ABL1_HUMAN     233    503             
DBREF  4TWP B  233   503  UNP    P00519   ABL1_HUMAN     233    503             
SEQADV 4TWP ILE A  315  UNP  P00519    THR   315 ENGINEERED MUTATION            
SEQADV 4TWP ILE B  315  UNP  P00519    THR   315 ENGINEERED MUTATION            
SEQRES   1 A  271  ASP LYS TRP GLU MET GLU ARG THR ASP ILE THR MET LYS          
SEQRES   2 A  271  HIS LYS LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU          
SEQRES   3 A  271  GLY VAL TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS          
SEQRES   4 A  271  THR LEU LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU          
SEQRES   5 A  271  LYS GLU ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN          
SEQRES   6 A  271  LEU VAL GLN LEU LEU GLY VAL CYS THR ARG GLU PRO PRO          
SEQRES   7 A  271  PHE TYR ILE ILE ILE GLU PHE MET THR TYR GLY ASN LEU          
SEQRES   8 A  271  LEU ASP TYR LEU ARG GLU CYS ASN ARG GLN GLU VAL ASN          
SEQRES   9 A  271  ALA VAL VAL LEU LEU TYR MET ALA THR GLN ILE SER SER          
SEQRES  10 A  271  ALA MET GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG          
SEQRES  11 A  271  ASP LEU ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS          
SEQRES  12 A  271  LEU VAL LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET          
SEQRES  13 A  271  THR GLY ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE          
SEQRES  14 A  271  PRO ILE LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN          
SEQRES  15 A  271  LYS PHE SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL          
SEQRES  16 A  271  LEU LEU TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR          
SEQRES  17 A  271  PRO GLY ILE ASP LEU SER GLN VAL TYR GLU LEU LEU GLU          
SEQRES  18 A  271  LYS ASP TYR ARG MET GLU ARG PRO GLU GLY CYS PRO GLU          
SEQRES  19 A  271  LYS VAL TYR GLU LEU MET ARG ALA CYS TRP GLN TRP ASN          
SEQRES  20 A  271  PRO SER ASP ARG PRO SER PHE ALA GLU ILE HIS GLN ALA          
SEQRES  21 A  271  PHE GLU THR MET PHE GLN GLU SER SER ILE SER                  
SEQRES   1 B  271  ASP LYS TRP GLU MET GLU ARG THR ASP ILE THR MET LYS          
SEQRES   2 B  271  HIS LYS LEU GLY GLY GLY GLN TYR GLY GLU VAL TYR GLU          
SEQRES   3 B  271  GLY VAL TRP LYS LYS TYR SER LEU THR VAL ALA VAL LYS          
SEQRES   4 B  271  THR LEU LYS GLU ASP THR MET GLU VAL GLU GLU PHE LEU          
SEQRES   5 B  271  LYS GLU ALA ALA VAL MET LYS GLU ILE LYS HIS PRO ASN          
SEQRES   6 B  271  LEU VAL GLN LEU LEU GLY VAL CYS THR ARG GLU PRO PRO          
SEQRES   7 B  271  PHE TYR ILE ILE ILE GLU PHE MET THR TYR GLY ASN LEU          
SEQRES   8 B  271  LEU ASP TYR LEU ARG GLU CYS ASN ARG GLN GLU VAL ASN          
SEQRES   9 B  271  ALA VAL VAL LEU LEU TYR MET ALA THR GLN ILE SER SER          
SEQRES  10 B  271  ALA MET GLU TYR LEU GLU LYS LYS ASN PHE ILE HIS ARG          
SEQRES  11 B  271  ASP LEU ALA ALA ARG ASN CYS LEU VAL GLY GLU ASN HIS          
SEQRES  12 B  271  LEU VAL LYS VAL ALA ASP PHE GLY LEU SER ARG LEU MET          
SEQRES  13 B  271  THR GLY ASP THR TYR THR ALA HIS ALA GLY ALA LYS PHE          
SEQRES  14 B  271  PRO ILE LYS TRP THR ALA PRO GLU SER LEU ALA TYR ASN          
SEQRES  15 B  271  LYS PHE SER ILE LYS SER ASP VAL TRP ALA PHE GLY VAL          
SEQRES  16 B  271  LEU LEU TRP GLU ILE ALA THR TYR GLY MET SER PRO TYR          
SEQRES  17 B  271  PRO GLY ILE ASP LEU SER GLN VAL TYR GLU LEU LEU GLU          
SEQRES  18 B  271  LYS ASP TYR ARG MET GLU ARG PRO GLU GLY CYS PRO GLU          
SEQRES  19 B  271  LYS VAL TYR GLU LEU MET ARG ALA CYS TRP GLN TRP ASN          
SEQRES  20 B  271  PRO SER ASP ARG PRO SER PHE ALA GLU ILE HIS GLN ALA          
SEQRES  21 B  271  PHE GLU THR MET PHE GLN GLU SER SER ILE SER                  
HET    AXI  A 601      28                                                       
HET     NI  A 602       1                                                       
HET     NI  A 603       1                                                       
HET     NA  A 604       1                                                       
HET     NA  A 605       1                                                       
HET    AXI  B 601      28                                                       
HET     NI  B 602       1                                                       
HET     NI  B 603       1                                                       
HET     NA  B 604       1                                                       
HETNAM     AXI AXITINIB                                                         
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      NA SODIUM ION                                                       
HETSYN     AXI N-METHYL-2-(3-((E)-2-PYRIDIN-2-YL-VINYL)-1H-INDAZOL-6-           
HETSYN   2 AXI  YLSULFANYL)-BENZAMIDE                                           
FORMUL   3  AXI    2(C22 H18 N4 O S)                                            
FORMUL   4   NI    4(NI 2+)                                                     
FORMUL   6   NA    3(NA 1+)                                                     
FORMUL  12  HOH   *189(H2 O)                                                    
HELIX    1 AA1 GLU A  238  THR A  240  5                                   3    
HELIX    2 AA2 GLY A  249  GLN A  252  5                                   4    
HELIX    3 AA3 VAL A  280  ILE A  293  1                                  14    
HELIX    4 AA4 ASN A  322  CYS A  330  1                                   9    
HELIX    5 AA5 ASN A  336  ASN A  358  1                                  23    
HELIX    6 AA6 ALA A  365  ARG A  367  5                                   3    
HELIX    7 AA7 GLU A  373  HIS A  375  5                                   3    
HELIX    8 AA8 PRO A  402  THR A  406  5                                   5    
HELIX    9 AA9 ALA A  407  ASN A  414  1                                   8    
HELIX   10 AB1 SER A  417  THR A  434  1                                  18    
HELIX   11 AB2 ASP A  444  SER A  446  5                                   3    
HELIX   12 AB3 GLN A  447  LYS A  454  1                                   8    
HELIX   13 AB4 PRO A  465  TRP A  476  1                                  12    
HELIX   14 AB5 ASN A  479  ARG A  483  5                                   5    
HELIX   15 AB6 SER A  485  SER A  503  1                                  19    
HELIX   16 AB7 GLU B  238  ILE B  242  5                                   5    
HELIX   17 AB8 GLY B  249  GLN B  252  5                                   4    
HELIX   18 AB9 LYS B  262  SER B  265  5                                   4    
HELIX   19 AC1 GLU B  279  ILE B  293  1                                  15    
HELIX   20 AC2 ASN B  322  CYS B  330  1                                   9    
HELIX   21 AC3 ASN B  336  ASN B  358  1                                  23    
HELIX   22 AC4 ALA B  365  ARG B  367  5                                   3    
HELIX   23 AC5 GLU B  373  HIS B  375  5                                   3    
HELIX   24 AC6 ASP B  381  SER B  385  5                                   5    
HELIX   25 AC7 PRO B  402  THR B  406  5                                   5    
HELIX   26 AC8 ALA B  407  ASN B  414  1                                   8    
HELIX   27 AC9 SER B  417  THR B  434  1                                  18    
HELIX   28 AD1 ASP B  444  SER B  446  5                                   3    
HELIX   29 AD2 GLN B  447  LYS B  454  1                                   8    
HELIX   30 AD3 PRO B  465  TRP B  476  1                                  12    
HELIX   31 AD4 ASN B  479  ARG B  483  5                                   5    
HELIX   32 AD5 SER B  485  SER B  503  1                                  19    
SHEET    1 AA1 5 ILE A 242  LYS A 247  0                                        
SHEET    2 AA1 5 VAL A 256  TRP A 261 -1  O  VAL A 260   N  THR A 243           
SHEET    3 AA1 5 LEU A 266  LYS A 271 -1  O  LEU A 266   N  TRP A 261           
SHEET    4 AA1 5 TYR A 312  GLU A 316 -1  O  ILE A 315   N  ALA A 269           
SHEET    5 AA1 5 LEU A 301  CYS A 305 -1  N  LEU A 302   O  ILE A 314           
SHEET    1 AA2 2 PHE A 359  ILE A 360  0                                        
SHEET    2 AA2 2 ARG A 386  LEU A 387 -1  O  ARG A 386   N  ILE A 360           
SHEET    1 AA3 2 CYS A 369  VAL A 371  0                                        
SHEET    2 AA3 2 VAL A 377  VAL A 379 -1  O  LYS A 378   N  LEU A 370           
SHEET    1 AA4 2 TYR A 393  THR A 394  0                                        
SHEET    2 AA4 2 LYS A 415  PHE A 416 -1  O  PHE A 416   N  TYR A 393           
SHEET    1 AA5 5 THR B 243  LYS B 247  0                                        
SHEET    2 AA5 5 VAL B 256  VAL B 260 -1  O  VAL B 260   N  THR B 243           
SHEET    3 AA5 5 THR B 267  LYS B 271 -1  O  VAL B 268   N  GLY B 259           
SHEET    4 AA5 5 TYR B 312  GLU B 316 -1  O  ILE B 315   N  ALA B 269           
SHEET    5 AA5 5 LEU B 301  CYS B 305 -1  N  GLY B 303   O  ILE B 314           
SHEET    1 AA6 2 PHE B 359  ILE B 360  0                                        
SHEET    2 AA6 2 ARG B 386  LEU B 387 -1  O  ARG B 386   N  ILE B 360           
SHEET    1 AA7 2 CYS B 369  VAL B 371  0                                        
SHEET    2 AA7 2 VAL B 377  VAL B 379 -1  O  LYS B 378   N  LEU B 370           
SHEET    1 AA8 2 TYR B 393  THR B 394  0                                        
SHEET    2 AA8 2 LYS B 415  PHE B 416 -1  O  PHE B 416   N  TYR B 393           
LINK         OE2 GLU A 352                NI    NI A 602     1555   1555  2.42  
LINK         NE2 HIS A 490                NI    NI A 603     1555   1555  2.59  
LINK         OE1 GLU A 494                NI    NI A 603     1555   1555  2.25  
LINK         OE1 GLU B 352                NI    NI B 602     1555   1555  2.41  
LINK         OE2 GLU B 352                NI    NI B 602     1555   1555  2.62  
LINK         OH  TYR B 393                NA    NA B 604     1555   1555  3.15  
LINK         NE2 HIS B 490                NI    NI B 603     1555   1555  2.74  
LINK         OE1 GLU B 494                NI    NI B 603     1555   1555  2.47  
LINK        NI    NI A 602                 O   HOH A 738     1555   1555  2.51  
LINK        NA    NA A 605                 O   HOH A 707     1555   1555  3.08  
LINK        NA    NA A 605                 O   HOH A 714     1555   1555  3.08  
LINK        NI    NI B 602                 O   HOH B 720     1555   1555  2.37  
LINK        NI    NI B 603                 O   HOH B 705     1555   1555  2.79  
CISPEP   1 PRO A  309    PRO A  310          0        -8.63                     
CISPEP   2 PRO B  309    PRO B  310          0        -4.30                     
SITE     1 AC1 12 LEU A 248  TYR A 253  ALA A 269  LYS A 271                    
SITE     2 AC1 12 GLU A 316  PHE A 317  MET A 318  THR A 319                    
SITE     3 AC1 12 GLY A 321  ASN A 368  LEU A 370  ASP A 381                    
SITE     1 AC2  6 GLU A 352  HIS A 490   NI A 603  HOH A 709                    
SITE     2 AC2  6 HOH A 729  HOH A 738                                          
SITE     1 AC3  3 HIS A 490  GLU A 494   NI A 602                               
SITE     1 AC4  2 ARG A 362  HIS A 396                                          
SITE     1 AC5  3 ARG A 362  HOH A 707  HOH A 714                               
SITE     1 AC6 11 TYR B 253  ALA B 269  LYS B 271  GLU B 316                    
SITE     2 AC6 11 PHE B 317  MET B 318  THR B 319  GLY B 321                    
SITE     3 AC6 11 ASN B 368  LEU B 370  ASP B 381                               
SITE     1 AC7  4 GLU B 352  HIS B 490  GLU B 494  HOH B 720                    
SITE     1 AC8  3 HIS B 490  GLU B 494  HOH B 705                               
SITE     1 AC9  3 GLU A 373  ARG B 386  TYR B 393                               
CRYST1   56.818  113.801  131.164  90.00  90.00  90.00 P 2 21 21     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017600  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008787  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007624        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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