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Database: PDB
Entry: 4CKJ
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HEADER    TRANSFERASE                             06-JAN-14   4CKJ              
TITLE     CRYSTAL STRUCTURE OF RET TYROSINE KINASE DOMAIN BOUND TO 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                                                      
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 4CKJ    1       JRNL                                     
REVDAT   2   19-MAR-14 4CKJ    1       JRNL   REMARK                            
REVDAT   1   05-MAR-14 4CKJ    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 41491                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2090                            
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 49.7582 -  4.0686    0.88     2657   130  0.1570 0.1729        
REMARK   3     2  4.0686 -  3.2295    0.90     2631   159  0.1437 0.1444        
REMARK   3     3  3.2295 -  2.8213    0.90     2645   126  0.1433 0.1941        
REMARK   3     4  2.8213 -  2.5634    0.91     2656   144  0.1541 0.2019        
REMARK   3     5  2.5634 -  2.3797    0.90     2632   141  0.1429 0.1826        
REMARK   3     6  2.3797 -  2.2394    0.87     2568   134  0.1455 0.1547        
REMARK   3     7  2.2394 -  2.1272    0.89     2609   133  0.1370 0.1837        
REMARK   3     8  2.1272 -  2.0346    0.88     2572   126  0.1362 0.1720        
REMARK   3     9  2.0346 -  1.9563    0.90     2630   146  0.1384 0.1936        
REMARK   3    10  1.9563 -  1.8888    0.90     2611   144  0.1537 0.2044        
REMARK   3    11  1.8888 -  1.8297    0.89     2588   130  0.1745 0.2378        
REMARK   3    12  1.8297 -  1.7774    0.92     2691   142  0.1888 0.2293        
REMARK   3    13  1.7774 -  1.7306    0.92     2666   154  0.2141 0.2582        
REMARK   3    14  1.7306 -  1.6884    0.90     2637   131  0.2503 0.2922        
REMARK   3    15  1.6884 -  1.6500    0.89     2608   150  0.2683 0.3306        
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)     : 0.180            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.800           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.19                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.40                          
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      :  0.020           2540                                  
REMARK   3   ANGLE     :  1.838           3437                                  
REMARK   3   CHIRALITY :  0.115            378                                  
REMARK   3   PLANARITY :  0.010            433                                  
REMARK   3   DIHEDRAL  : 15.030            958                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 700 THROUGH 781 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7632   3.4378   2.7365              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1572 T22:   0.1639                                     
REMARK   3      T33:   0.2632 T12:   0.0042                                     
REMARK   3      T13:  -0.0025 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7812 L22:   1.7448                                     
REMARK   3      L33:   0.4238 L12:  -1.0751                                     
REMARK   3      L13:  -0.5677 L23:   0.6981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0430 S12:   0.1811 S13:  -0.0873                       
REMARK   3      S21:  -0.0325 S22:   0.0358 S23:   0.2568                       
REMARK   3      S31:   0.0370 S32:  -0.1170 S33:   0.0136                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 782 THROUGH 847 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0660   9.4253  14.6998              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2446 T22:   0.1636                                     
REMARK   3      T33:   0.2172 T12:   0.0320                                     
REMARK   3      T13:  -0.0040 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4250 L22:   1.0594                                     
REMARK   3      L33:   1.6314 L12:  -0.4316                                     
REMARK   3      L13:   0.1252 L23:  -0.2805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0762 S12:  -0.0787 S13:   0.1893                       
REMARK   3      S21:   0.1374 S22:  -0.0426 S23:   0.1489                       
REMARK   3      S31:  -0.2644 S32:  -0.0331 S33:   0.0406                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 848 THROUGH 1013 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  36.8849  -1.5304  20.8626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2219 T22:   0.2458                                     
REMARK   3      T33:   0.1488 T12:   0.0132                                     
REMARK   3      T13:  -0.0078 T23:   0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6255 L22:   0.9812                                     
REMARK   3      L33:   1.4471 L12:  -0.5368                                     
REMARK   3      L13:  -0.4606 L23:   0.4027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0831 S12:  -0.3991 S13:  -0.1519                       
REMARK   3      S21:   0.1921 S22:   0.0013 S23:  -0.0058                       
REMARK   3      S31:  -0.0682 S32:   0.1194 S33:  -0.0052                       
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 4CKJ 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_1290059341.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-11                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.970                              
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 : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46229                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.200                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
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: PDB ENTRY 2IVT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 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       36.59500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.54500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       36.59500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.54500            
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: 9370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.7 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       73.19000            
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 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 A3000  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     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 465     ASP A   842                                                      
REMARK 465     GLU A   843                                                      
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     ILE A 711    CG1  CG2  CD1                                       
REMARK 470     LEU A 712    CG   CD1  CD2                                       
REMARK 470     LYS A 789    CE   NZ                                             
REMARK 470     ASP A 797    CG   OD1  OD2                                       
REMARK 470     ARG A 820    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 822    CG1  CG2                                            
REMARK 470     GLU A 901    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 959    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 971    CD   OE1  OE2                                       
REMARK 470     GLU A 978    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 979    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 982    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 986    CD   OE1  NE2                                       
REMARK 470     LYS A 994    CD   CE   NZ                                        
REMARK 470     LYS A1003    CE   NZ                                             
REMARK 470     LYS A1007    CD   CE   NZ                                        
REMARK 470     LYS A1011    CE   NZ                                             
REMARK 470     ARG A1012    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1013    CD   NE   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   OE2  GLU A   762     O    HOH A  3038              2.18            
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    ARG A 886   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    GLU A 713       79.64   -119.43                                   
REMARK 500    ARG A 873      -13.67     77.65                                   
REMARK 500    GLU A 884      124.31    -29.26                                   
REMARK 500    ASP A 892       74.35     61.96                                   
REMARK 500    ASP A 974      -71.63    -51.90                                   
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 ADN 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 FMT A 2022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2024                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2025                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2026                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2027                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2030                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4CKI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ONCOGENIC RET TYROSINE KINASE M918T BOUND TO    
REMARK 900 ADENOSINE                                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N TERMINAL RESIDUES GPLSL ARE VECTOR DERIVES RESIDUES.               
DBREF  4CKJ A  705  1013  UNP    P07949   RET_HUMAN      705   1013             
SEQADV 4CKJ GLY A  700  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKJ PRO A  701  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKJ LEU A  702  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKJ SER A  703  UNP  P07949              EXPRESSION TAG                 
SEQADV 4CKJ LEU A  704  UNP  P07949              EXPRESSION TAG                 
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 TYR GLU GLU ASP SER PTR VAL LYS          
SEQRES  17 A  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP MET 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 4CKJ PTR A  905  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 905      16                                                       
HET    ADN  A2014      19                                                       
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    FMT  A2022       3                                                       
HET    FMT  A2023       3                                                       
HET    FMT  A2024       3                                                       
HET    FMT  A2025       3                                                       
HET    FMT  A2026       3                                                       
HET    FMT  A2027       3                                                       
HET    FMT  A2028       3                                                       
HET    FMT  A2029       3                                                       
HET    FMT  A2030       3                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     ADN ADENOSINE                                                        
HETNAM     FMT FORMIC ACID                                                      
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  ADN    C10 H13 N5 O4                                                
FORMUL   3  FMT    16(C H2 O2)                                                  
FORMUL  19  HOH   *107(H2 O)                                                    
HELIX    1   1 GLY A  700  LEU A  712  1                                  13    
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  MET 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 1013  1                                  17    
SHEET    1  AA 5 LEU A 724  GLU A 732  0                                        
SHEET    2  AA 5 GLY A 736  PHE A 744 -1  O  VAL A 738   N  LEU A 730           
SHEET    3  AA 5 TYR A 752  LEU A 760 -1  O  THR A 753   N  ALA A 743           
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 ARG A 820  LYS A 821  0                                        
SHEET    2  AB 2 ALA A 845  LEU A 846  1  N  LEU A 846   O  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   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 11 LEU A 730  GLY A 731  ALA A 756  GLU A 805                    
SITE     2 AC1 11 ALA A 807  SER A 811  LEU A 881  FMT A2016                    
SITE     3 AC1 11 HOH A3053  HOH A3069  HOH A3073                               
SITE     1 AC2  4 LYS A 728  LYS A 740  TYR A 806  FMT A2016                    
SITE     1 AC3  6 LEU A 730  ALA A 807  LYS A 808  GLY A 810                    
SITE     2 AC3  6 ADN A2014  FMT A2015                                          
SITE     1 AC4  4 LYS A 722  ASN A 723  ARG A 908  FMT A2023                    
SITE     1 AC5  3 LYS A 737  LYS A 761  GLU A 762                               
SITE     1 AC6  8 GLY A 700  PRO A 701  LEU A 702  SER A 703                    
SITE     2 AC6  8 GLN A 910  LEU A 923  PHE A 924  HIS A 926                    
SITE     1 AC7  6 ARG A 770  LYS A 907  SER A 909  GLN A 910                    
SITE     2 AC7  6 ARG A 912  HOH A3040                                          
SITE     1 AC8  3 THR A 946  LEU A 947  GLY A 948                               
SITE     1 AC9  5 ARG A 873  LEU A 895  LYS A 907  GLY A 911                    
SITE     2 AC9  5 ARG A 912                                                     
SITE     1 BC1  3 LYS A 722  ARG A 908  FMT A2017                               
SITE     1 BC2  8 PRO A 766  SER A 909  GLN A 910  GLY A 911                    
SITE     2 BC2  8 SER A 922  HIS A 926  TYR A 928  HOH A3080                    
SITE     1 BC3  4 SER A 703  PHE A 961  LYS A 965  HOH A3106                    
SITE     1 BC4  3 ASP A 903  THR A 929  THR A 930                               
SITE     1 BC5  3 ARG A 770  LEU A 773  SER A 774                               
SITE     1 BC6  4 LYS A 808  TYR A 809  GLU A 884  GLY A 885                    
SITE     1 BC7  2 HIS A 786  GLN A 860                                          
SITE     1 BC8  7 LEU A 779  VAL A 782  ILE A 788  LYS A 789                    
SITE     2 BC8  7 LEU A 790  HOH A3044  HOH A3046                               
CRYST1   73.190   69.090   78.640  90.00 101.76  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      0.013663  0.000000  0.002844        0.00000                         
SCALE2      0.000000  0.014474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012989        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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