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Database: PDB
Entry: 4CKI
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HEADER    TRANSFERASE                             06-JAN-14   4CKI              
TITLE     CRYSTAL STRUCTURE OF ONCOGENIC RET TYROSINE KINASE M918T BOUND TO     
TITLE    2 ADENOSINE                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 705-1013;                                         
COMPND   5 SYNONYM: CADHERIN FAMILY MEMBER 12, PROTO-ONCOGENE C-RET;            
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.PLAZA-MENACHO,K.BARNOUIN,K.GOODMAN,R.J.MARTINEZ-TORRES,A.BORG,      
AUTHOR   2 J.MURRAY-RUST,S.MOUILLERON,P.KNOWLES,N.Q.MCDONALD                    
REVDAT   3   28-FEB-18 4CKI    1       JRNL                                     
REVDAT   2   19-MAR-14 4CKI    1       TITLE  AUTHOR JRNL                       
REVDAT   1   05-MAR-14 4CKI    0                                                
JRNL        AUTH   I.PLAZA-MENACHO,K.BARNOUIN,K.GOODMAN,R.J.MARTINEZ-TORRES,    
JRNL        AUTH 2 A.BORG,J.MURRAY-RUST,S.MOUILLERON,P.KNOWLES,N.Q.MCDONALD     
JRNL        TITL   ONCOGENIC RET KINASE DOMAIN MUTATIONS PERTURB THE            
JRNL        TITL 2 AUTOPHOSPHORYLATION TRAJECTORY BY ENHANCING SUBSTRATE        
JRNL        TITL 3 PRESENTATION IN TRANS.                                       
JRNL        REF    MOL. CELL                     V.  53   738 2014              
JRNL        REFN                   ISSN 1097-4164                               
JRNL        PMID   24560924                                                     
JRNL        DOI    10.1016/J.MOLCEL.2014.01.015                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.730                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22078                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1107                            
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 39.5654 -  4.2312    1.00     2697   139  0.1433 0.1568        
REMARK   3     2  4.2312 -  3.3590    1.00     2648   132  0.1316 0.1586        
REMARK   3     3  3.3590 -  2.9346    1.00     2641   126  0.1673 0.2072        
REMARK   3     4  2.9346 -  2.6663    1.00     2644   133  0.1742 0.2212        
REMARK   3     5  2.6663 -  2.4753    1.00     2628   142  0.1723 0.2170        
REMARK   3     6  2.4753 -  2.3293    1.00     2590   170  0.1656 0.2113        
REMARK   3     7  2.3293 -  2.2127    1.00     2636   134  0.1696 0.2237        
REMARK   3     8  2.2127 -  2.1164    0.96     2487   131  0.1907 0.2541        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.820           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.005           2558                                  
REMARK   3   ANGLE     :  0.901           3473                                  
REMARK   3   CHIRALITY :  0.062            382                                  
REMARK   3   PLANARITY :  0.004            436                                  
REMARK   3   DIHEDRAL  : 13.215            990                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 700 THROUGH 735 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  51.7698  -1.2907   0.7197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1762 T22:   0.2523                                     
REMARK   3      T33:   0.3161 T12:  -0.0111                                     
REMARK   3      T13:  -0.0219 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4576 L22:   4.2868                                     
REMARK   3      L33:   0.7837 L12:  -2.5064                                     
REMARK   3      L13:  -0.9521 L23:   1.6026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0174 S12:   0.1334 S13:  -0.3244                       
REMARK   3      S21:  -0.0391 S22:  -0.1279 S23:   0.4674                       
REMARK   3      S31:   0.0265 S32:  -0.2617 S33:   0.1092                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 736 THROUGH 781 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  54.5835   1.9391   4.8392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0991 T22:   0.1466                                     
REMARK   3      T33:   0.1970 T12:  -0.0062                                     
REMARK   3      T13:  -0.0186 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3162 L22:   5.3629                                     
REMARK   3      L33:   0.4290 L12:  -3.3762                                     
REMARK   3      L13:  -0.4941 L23:   0.8614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1102 S12:   0.0078 S13:  -0.0147                       
REMARK   3      S21:   0.1089 S22:   0.1617 S23:   0.1355                       
REMARK   3      S31:  -0.0130 S32:  -0.0438 S33:  -0.0725                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 782 THROUGH 890 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  61.8253   3.5519  18.7682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1965 T22:   0.1787                                     
REMARK   3      T33:   0.1611 T12:   0.0601                                     
REMARK   3      T13:   0.0157 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4750 L22:   1.6865                                     
REMARK   3      L33:   3.3061 L12:  -0.2741                                     
REMARK   3      L13:   0.3780 L23:   0.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1939 S12:  -0.3778 S13:   0.1904                       
REMARK   3      S21:   0.2087 S22:   0.0446 S23:   0.0749                       
REMARK   3      S31:  -0.3638 S32:  -0.0852 S33:   0.1351                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 891 THROUGH 1013 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  75.4996  -6.0686  20.8974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1676 T22:   0.2342                                     
REMARK   3      T33:   0.1575 T12:   0.0162                                     
REMARK   3      T13:  -0.0119 T23:   0.0588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7432 L22:   1.9644                                     
REMARK   3      L33:   3.3221 L12:  -0.3243                                     
REMARK   3      L13:  -0.4783 L23:   0.9333                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0773 S12:  -0.3757 S13:  -0.1099                       
REMARK   3      S21:   0.2457 S22:   0.0363 S23:  -0.0751                       
REMARK   3      S31:   0.0358 S32:   0.3084 S33:   0.0072                       
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 4CKI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JAN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290059253.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-FEB-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM16                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22084                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: PDB ENTRY 2IVT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA FORMATE, 0.1M NA CITRATE, PH 5.5   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       35.94650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.28450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.94650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       35.28450            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.4 KCAL/MOL                         
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   BIOMT1   2 -1.000000  0.000000  0.000000      143.78600            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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   823                                                      
REMARK 465     PRO A   824                                                      
REMARK 465     GLY A   825                                                      
REMARK 465     TYR A   826                                                      
REMARK 465     LEU A   827                                                      
REMARK 465     GLY A   828                                                      
REMARK 465     SER A   829                                                      
REMARK 465     GLY A   830                                                      
REMARK 465     GLY A   831                                                      
REMARK 465     SER A   832                                                      
REMARK 465     ARG A   833                                                      
REMARK 465     ASN A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     HIS A   840                                                      
REMARK 465     PRO A   841                                                      
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 710    CG   CD   CE   NZ                                   
REMARK 470     GLU A 713    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 714    CG   OD1  OD2                                       
REMARK 470     GLU A 762    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 789    CE   NZ                                             
REMARK 470     ASP A 797    CG   OD1  OD2                                       
REMARK 470     VAL A 822    CG1  CG2                                            
REMARK 470     ASP A 842    CG   OD1  OD2                                       
REMARK 470     GLU A 843    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 884    CD   OE1  OE2                                       
REMARK 470     GLU A 901    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 959    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 979    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 994    CD   CE   NZ                                        
REMARK 470     ARG A1013    CZ   NH1  NH2                                       
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  3017     O    HOH A  3068              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 712   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
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    ARG A 873      -20.59     75.52                                   
REMARK 500    ASP A 892       75.33     59.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2018                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2019                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2020                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 2022                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CKJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF RET TYROSINE KINASE DOMAIN BOUND TO ADENOSINE   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N TERMINAL RESIDUES GPLSL ARE VECTOR DERIVES RESIDUES.               
DBREF  4CKI A  705  1013  UNP    P07949   RET_HUMAN      705   1013             
SEQADV 4CKI GLY A  700  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKI PRO A  701  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKI LEU A  702  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKI SER A  703  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKI LEU A  704  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKI THR A  918  UNP  P07949    MET   918 ENGINEERED MUTATION            
SEQRES   1 A  314  GLY PRO LEU SER LEU SER VAL ASP ALA PHE LYS ILE LEU          
SEQRES   2 A  314  GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN LEU VAL          
SEQRES   3 A  314  LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY LYS VAL          
SEQRES   4 A  314  VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG ALA GLY          
SEQRES   5 A  314  TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU ASN ALA          
SEQRES   6 A  314  SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU PHE ASN          
SEQRES   7 A  314  VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE LYS LEU          
SEQRES   8 A  314  TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU LEU ILE          
SEQRES   9 A  314  VAL GLU TYR ALA LYS TYR GLY SER LEU ARG GLY PHE LEU          
SEQRES  10 A  314  ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU GLY SER          
SEQRES  11 A  314  GLY GLY SER ARG ASN SER SER SER LEU ASP HIS PRO ASP          
SEQRES  12 A  314  GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER PHE ALA          
SEQRES  13 A  314  TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA GLU MET          
SEQRES  14 A  314  LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU          
SEQRES  15 A  314  VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP PHE GLY          
SEQRES  16 A  314  LEU SER ARG ASP VAL PTR GLU GLU ASP SER PTR VAL LYS          
SEQRES  17 A  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP THR ALA ILE          
SEQRES  18 A  314  GLU SER LEU PHE ASP HIS ILE TYR THR THR GLN SER ASP          
SEQRES  19 A  314  VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE VAL THR          
SEQRES  20 A  314  LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO GLU ARG          
SEQRES  21 A  314  LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET GLU ARG          
SEQRES  22 A  314  PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU MET LEU          
SEQRES  23 A  314  GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO VAL PHE          
SEQRES  24 A  314  ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET VAL LYS          
SEQRES  25 A  314  ARG ARG                                                      
MODRES 4CKI PTR A  900  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4CKI PTR A  905  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 900      16                                                       
HET    PTR  A 905      16                                                       
HET    FMT  A2014       3                                                       
HET    FMT  A2015       3                                                       
HET    FMT  A2016       3                                                       
HET    FMT  A2017       3                                                       
HET    FMT  A2018       3                                                       
HET    FMT  A2019       3                                                       
HET    FMT  A2020       3                                                       
HET    FMT  A2021       3                                                       
HET    ADN  A2022      19                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     FMT FORMIC ACID                                                      
HETNAM     ADN ADENOSINE                                                        
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   2  FMT    8(C H2 O2)                                                   
FORMUL  10  ADN    C10 H13 N5 O4                                                
FORMUL  11  HOH   *218(H2 O)                                                    
HELIX    1   1 GLY A  700  LYS A  710  1                                  11    
HELIX    2   2 PRO A  720  LYS A  722  5                                   3    
HELIX    3   3 SER A  765  LYS A  780  1                                  16    
HELIX    4   4 SER A  811  GLU A  818  1                                   8    
HELIX    5   5 THR A  847  MET A  868  1                                  22    
HELIX    6   6 ALA A  876  ARG A  878  5                                   3    
HELIX    7   7 PRO A  914  THR A  918  5                                   5    
HELIX    8   8 ALA A  919  HIS A  926  1                                   8    
HELIX    9   9 THR A  929  THR A  946  1                                  18    
HELIX   10  10 PRO A  956  GLU A  958  5                                   3    
HELIX   11  11 ARG A  959  THR A  966  1                                   8    
HELIX   12  12 SER A  977  TRP A  988  1                                  12    
HELIX   13  13 GLU A  991  ARG A  995  5                                   5    
HELIX   14  14 VAL A  997  ARG A 1012  1                                  16    
SHEET    1  AA 5 LEU A 724  GLU A 732  0                                        
SHEET    2  AA 5 GLY A 736  LEU A 746 -1  O  VAL A 738   N  LEU A 730           
SHEET    3  AA 5 ARG A 749  LEU A 760 -1  O  ARG A 749   N  LEU A 746           
SHEET    4  AA 5 LEU A 801  GLU A 805 -1  O  LEU A 802   N  LYS A 758           
SHEET    5  AA 5 LEU A 790  CYS A 794 -1  N  TYR A 791   O  ILE A 803           
SHEET    1  AB 2 SER A 819  LYS A 821  0                                        
SHEET    2  AB 2 ARG A 844  LEU A 846  1  O  ARG A 844   N  ARG A 820           
SHEET    1  AC 2 LEU A 870  VAL A 871  0                                        
SHEET    2  AC 2 ARG A 897  ASP A 898 -1  O  ARG A 897   N  VAL A 871           
SHEET    1  AD 2 ILE A 880  ALA A 883  0                                        
SHEET    2  AD 2 LYS A 887  ILE A 890 -1  O  LYS A 887   N  ALA A 883           
SHEET    1  AE 2 PTR A 905  VAL A 906  0                                        
SHEET    2  AE 2 ILE A 927  TYR A 928 -1  O  TYR A 928   N  PTR A 905           
LINK         C   VAL A 899                 N   PTR A 900     1555   1555  1.33  
LINK         C   PTR A 900                 N   GLU A 901     1555   1555  1.33  
LINK         C   SER A 904                 N   PTR A 905     1555   1555  1.33  
LINK         C   PTR A 905                 N   VAL A 906     1555   1555  1.33  
SITE     1 AC1  5 ARG A 873  LYS A 907  GLY A 911  ARG A 912                    
SITE     2 AC1  5 HOH A3070                                                     
SITE     1 AC2  8 GLY A 700  PRO A 701  LEU A 702  SER A 703                    
SITE     2 AC2  8 GLN A 910  LEU A 923  PHE A 924  HIS A 926                    
SITE     1 AC3  2 ARG A 844  ARG A 886                                          
SITE     1 AC4  7 GLY A 733  GLU A 734  PHE A 735  GLY A 736                    
SITE     2 AC4  7 LYS A 758  HOH A3034  HOH A3050                               
SITE     1 AC5  3 THR A 754  PHE A 924  ASP A 925                               
SITE     1 AC6  3 THR A 946  LEU A 947  HOH A3103                               
SITE     1 AC7  4 HIS A 786  TRP A 856  GLN A 860  HOH A3085                    
SITE     1 AC8  4 LYS A 907  SER A 909  ARG A 912  HOH A3066                    
SITE     1 AC9 15 LEU A 730  GLY A 731  GLU A 732  VAL A 738                    
SITE     2 AC9 15 ALA A 756  VAL A 804  GLU A 805  ALA A 807                    
SITE     3 AC9 15 SER A 811  LEU A 881  HOH A2218  HOH A3050                    
SITE     4 AC9 15 HOH A3097  HOH A3123  HOH A3127                               
CRYST1   71.893   70.569   78.997  90.00 101.15  90.00 C 1 2 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      0.013910  0.000000  0.002742        0.00000                         
SCALE2      0.000000  0.014171  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012902        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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