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Database: PDB
Entry: 5FM2
LinkDB: 5FM2
Original site: 5FM2 
HEADER    TRANSFERASE                             30-OCT-15   5FM2              
TITLE     CRYSTAL STRUCTURE OF HYPER-PHOSPHORYLATED RET KINASE DOMAIN WITH      
TITLE    2 (PROXIMAL) JUXTAMEMBRANE SEGMENT                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 659-1013;                                     
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_CELL_LINE: SF21                                    
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.PLAZA-MENACHO,K.BARNOUIN,R.BARRY,A.BORG,M.ORME,S.MOUILLERON,        
AUTHOR   2 R.J.MARTINEZ-TORRES,P.MEIER,N.Q.MCDONALD                             
REVDAT   3   24-APR-19 5FM2    1       SOURCE LINK                              
REVDAT   2   01-MAR-17 5FM2    1       JRNL                                     
REVDAT   1   28-DEC-16 5FM2    0                                                
JRNL        AUTH   I.PLAZA-MENACHO,K.BARNOUIN,R.BARRY,A.BORG,M.ORME,R.CHAUHAN,  
JRNL        AUTH 2 S.MOUILLERON,R.J.MARTINEZ-TORRES,P.MEIER,N.Q.MCDONALD        
JRNL        TITL   RET FUNCTIONS AS A DUAL-SPECIFICITY KINASE THAT REQUIRES     
JRNL        TITL 2 ALLOSTERIC INPUTS FROM JUXTAMEMBRANE ELEMENTS.               
JRNL        REF    CELL REP                      V.  17  3319 2016              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   28009299                                                     
JRNL        DOI    10.1016/J.CELREP.2016.11.061                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.380                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 6686                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.235                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 315                             
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 55.1347 -  4.1574    1.00     3292   157  0.2230 0.2321        
REMARK   3     2  4.1574 -  3.3000    1.00     3079   158  0.2572 0.2941        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.85                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.002           2151                                  
REMARK   3   ANGLE     :  0.647           2937                                  
REMARK   3   CHIRALITY :  0.039            328                                  
REMARK   3   PLANARITY :  0.003            368                                  
REMARK   3   DIHEDRAL  : 16.152           1247                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 713:737)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1642  13.4489   0.2081              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5378 T22:   0.5325                                     
REMARK   3      T33:   0.8739 T12:   0.0843                                     
REMARK   3      T13:  -0.0586 T23:   0.0821                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0160 L22:   3.7570                                     
REMARK   3      L33:   5.8614 L12:   2.6723                                     
REMARK   3      L13:   0.6666 L23:  -0.2271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5473 S12:  -0.4206 S13:   1.0045                       
REMARK   3      S21:   0.0916 S22:  -0.1293 S23:   0.4488                       
REMARK   3      S31:   0.1327 S32:  -0.5395 S33:  -0.3833                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 738:890)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -26.3619  17.0911 -11.4126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4372 T22:   0.6049                                     
REMARK   3      T33:   0.6780 T12:   0.0159                                     
REMARK   3      T13:  -0.1847 T23:  -0.0942                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6255 L22:   3.4028                                     
REMARK   3      L33:   3.9130 L12:   0.4894                                     
REMARK   3      L13:  -2.4321 L23:  -1.0059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1351 S12:   0.2871 S13:  -0.2245                       
REMARK   3      S21:  -0.4754 S22:   0.0508 S23:  -0.0373                       
REMARK   3      S31:   0.3957 S32:   0.0777 S33:   0.0787                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 891:911)                         
REMARK   3    ORIGIN FOR THE GROUP (A): -29.8836  35.3942  -7.7665              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8332 T22:   0.7499                                     
REMARK   3      T33:   0.7643 T12:   0.1697                                     
REMARK   3      T13:   0.0261 T23:   0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6989 L22:   2.2254                                     
REMARK   3      L33:   3.5607 L12:  -1.3453                                     
REMARK   3      L13:  -2.8245 L23:   2.5793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2056 S12:   0.3039 S13:   0.7106                       
REMARK   3      S21:  -0.0022 S22:  -0.2460 S23:   0.1993                       
REMARK   3      S31:  -0.4668 S32:  -0.2442 S33:   0.1416                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESSEQ 912:1012)                        
REMARK   3    ORIGIN FOR THE GROUP (A): -14.3415  31.5242 -23.0069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7243 T22:   0.8370                                     
REMARK   3      T33:   0.4890 T12:  -0.0628                                     
REMARK   3      T13:  -0.1691 T23:   0.1049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3225 L22:   6.0885                                     
REMARK   3      L33:   2.6235 L12:   1.4548                                     
REMARK   3      L13:  -2.6240 L23:   1.3939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1649 S12:   0.3025 S13:   0.3821                       
REMARK   3      S21:  -0.9814 S22:   0.0842 S23:  -0.0271                       
REMARK   3      S31:  -0.8097 S32:   0.0378 S33:   0.1087                       
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 5FM2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290065399.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.9795                             
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   : 6686                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       72.27500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       72.27500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.27500            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       72.27500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       72.27500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       72.27500            
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: 3470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.6 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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  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     CYS A   659                                                      
REMARK 465     TYR A   660                                                      
REMARK 465     HIS A   661                                                      
REMARK 465     LYS A   662                                                      
REMARK 465     PHE A   663                                                      
REMARK 465     ALA A   664                                                      
REMARK 465     HIS A   665                                                      
REMARK 465     LYS A   666                                                      
REMARK 465     PRO A   667                                                      
REMARK 465     PRO A   668                                                      
REMARK 465     ILE A   669                                                      
REMARK 465     SER A   670                                                      
REMARK 465     SER A   671                                                      
REMARK 465     ALA A   672                                                      
REMARK 465     GLU A   673                                                      
REMARK 465     MET A   674                                                      
REMARK 465     THR A   675                                                      
REMARK 465     PHE A   676                                                      
REMARK 465     ARG A   677                                                      
REMARK 465     ARG A   678                                                      
REMARK 465     PRO A   679                                                      
REMARK 465     ALA A   680                                                      
REMARK 465     GLN A   681                                                      
REMARK 465     ALA A   682                                                      
REMARK 465     PHE A   683                                                      
REMARK 465     PRO A   684                                                      
REMARK 465     VAL A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     TYR A   687                                                      
REMARK 465     SER A   688                                                      
REMARK 465     SER A   689                                                      
REMARK 465     SER A   690                                                      
REMARK 465     GLY A   691                                                      
REMARK 465     ALA A   692                                                      
REMARK 465     ARG A   693                                                      
REMARK 465     ARG A   694                                                      
REMARK 465     PRO A   695                                                      
REMARK 465     SER A   696                                                      
REMARK 465     LEU A   697                                                      
REMARK 465     ASP A   698                                                      
REMARK 465     SER A   699                                                      
REMARK 465     MET A   700                                                      
REMARK 465     GLU A   701                                                      
REMARK 465     ASN A   702                                                      
REMARK 465     GLN A   703                                                      
REMARK 465     VAL A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     VAL A   706                                                      
REMARK 465     ASP A   707                                                      
REMARK 465     ALA A   708                                                      
REMARK 465     PHE A   709                                                      
REMARK 465     ARG A   820                                                      
REMARK 465     LYS A   821                                                      
REMARK 465     VAL A   822                                                      
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 465     ARG A   844                                                      
REMARK 465     ARG A  1012                                                      
REMARK 465     ARG A  1013                                                      
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     LYS A 716    CG   CD   CE   NZ                                   
REMARK 470     LYS A 722    CG   CD   CE   NZ                                   
REMARK 470     LYS A 728    CG   CD   CE   NZ                                   
REMARK 470     GLU A 734    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 744    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 747    CG   CD   CE   NZ                                   
REMARK 470     ARG A 749    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 762    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 789    CD   CE   NZ                                        
REMARK 470     GLN A 796    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 797    CG   OD1  OD2                                       
REMARK 470     LYS A 808    CG   CD   CE   NZ                                   
REMARK 470     GLU A 867    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 869    CG   CD   CE   NZ                                   
REMARK 470     ASP A 874    CG   OD1  OD2                                       
REMARK 470     LYS A 887    CG   CD   CE   NZ                                   
REMARK 470     ASP A 892    CG   OD1  OD2                                       
REMARK 470     VAL A 899    CG1  CG2                                            
REMARK 470     TYR A 900    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 901    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
REMARK 470     SER A 904    OG                                                  
REMARK 470     VAL A 906    CG1  CG2                                            
REMARK 470     LYS A 907    CE   NZ                                             
REMARK 470     ARG A 908    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 910    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 925    CG   OD1  OD2                                       
REMARK 470     ARG A 959    NE   CZ   NH1  NH2                                  
REMARK 470     LEU A 963    CG   CD1  CD2                                       
REMARK 470     LYS A 965    CG   CD   CE   NZ                                   
REMARK 470     GLU A 971    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 975    CG   OD1  ND2                                       
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     LYS A 989    CD   CE   NZ                                        
REMARK 470     GLU A 991    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 994    CG   CD   CE   NZ                                   
REMARK 470     LYS A1003    CG   CD   CE   NZ                                   
REMARK 470     LYS A1007    CG   CD   CE   NZ                                   
REMARK 470     VAL A1010    CG1  CG2                                            
REMARK 470     LYS A1011    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 873      -65.75     62.59                                   
REMARK 500    ASP A 892       81.32     58.64                                   
REMARK 500    GLU A 902       51.41   -106.42                                   
REMARK 500    ARG A 969     -165.60   -120.13                                   
REMARK 500    ASN A 975       51.84    -99.66                                   
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 PTR A 809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SEP A 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTR A 928                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PP1 A 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Ligand PTR A 905 bound to SER A   
REMARK 800  904                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FM3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE JM-KD        
DBREF  5FM2 A  659  1013  UNP    P07949   RET_HUMAN      659   1013             
SEQRES   1 A  355  CYS TYR HIS LYS PHE ALA HIS LYS PRO PRO ILE SER SER          
SEQRES   2 A  355  ALA GLU MET THR PHE ARG ARG PRO ALA GLN ALA PHE PRO          
SEQRES   3 A  355  VAL SER TYR SER SER SER GLY ALA ARG ARG PRO SER LEU          
SEQRES   4 A  355  ASP SER MET GLU ASN GLN VAL SER VAL ASP ALA PHE LYS          
SEQRES   5 A  355  ILE LEU GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN          
SEQRES   6 A  355  LEU VAL LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY          
SEQRES   7 A  355  LYS VAL VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG          
SEQRES   8 A  355  ALA GLY TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU          
SEQRES   9 A  355  ASN ALA SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU          
SEQRES  10 A  355  PHE ASN VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE          
SEQRES  11 A  355  LYS LEU TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU          
SEQRES  12 A  355  LEU ILE VAL GLU TYR ALA LYS PTR GLY SER LEU ARG GLY          
SEQRES  13 A  355  PHE LEU ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU          
SEQRES  14 A  355  GLY SER GLY GLY SER ARG ASN SER SER SER LEU ASP HIS          
SEQRES  15 A  355  PRO ASP GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER          
SEQRES  16 A  355  PHE ALA TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA          
SEQRES  17 A  355  GLU MET LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN          
SEQRES  18 A  355  ILE LEU VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP          
SEQRES  19 A  355  PHE GLY LEU SER ARG ASP VAL TYR GLU GLU ASP SER PTR          
SEQRES  20 A  355  VAL LYS ARG SEP GLN GLY ARG ILE PRO VAL LYS TRP MET          
SEQRES  21 A  355  ALA ILE GLU SER LEU PHE ASP HIS ILE PTR THR THR GLN          
SEQRES  22 A  355  SER ASP VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE          
SEQRES  23 A  355  VAL THR LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO          
SEQRES  24 A  355  GLU ARG LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET          
SEQRES  25 A  355  GLU ARG PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU          
SEQRES  26 A  355  MET LEU GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO          
SEQRES  27 A  355  VAL PHE ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET          
SEQRES  28 A  355  VAL LYS ARG ARG                                              
MODRES 5FM2 PTR A  809  TYR  O-PHOSPHOTYROSINE                                  
MODRES 5FM2 PTR A  905  TYR  O-PHOSPHOTYROSINE                                  
MODRES 5FM2 SEP A  909  SER  PHOSPHOSERINE                                      
MODRES 5FM2 PTR A  928  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 809      16                                                       
HET    PTR  A 905      16                                                       
HET    SEP  A 909      10                                                       
HET    PTR  A 928      16                                                       
HET    PP1  A2012      21                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PP1 1-TER-BUTYL-3-P-TOLYL-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-             
HETNAM   2 PP1  YLAMINE                                                         
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  PTR    3(C9 H12 N O6 P)                                             
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2  PP1    C16 H19 N5                                                   
FORMUL   3  HOH   *3(H2 O)                                                      
HELIX    1   1 PRO A  720  LYS A  722  5                                   3    
HELIX    2   2 LEU A  746  ARG A  749  5                                   4    
HELIX    3   3 SER A  765  VAL A  782  1                                  18    
HELIX    4   4 SER A  811  SER A  819  1                                   9    
HELIX    5   5 THR A  847  MET A  868  1                                  22    
HELIX    6   6 PRO A  914  MET A  918  5                                   5    
HELIX    7   7 ALA A  919  HIS A  926  1                                   8    
HELIX    8   8 THR A  929  THR A  946  1                                  18    
HELIX    9   9 PRO A  956  GLU A  958  5                                   3    
HELIX   10  10 ARG A  959  THR A  966  1                                   8    
HELIX   11  11 SER A  977  TRP A  988  1                                  12    
HELIX   12  12 GLU A  991  ARG A  995  5                                   5    
HELIX   13  13 VAL A  997  LYS A 1011  1                                  15    
SHEET    1  AA 5 LEU A 724  GLU A 732  0                                        
SHEET    2  AA 5 LYS A 737  PHE A 744 -1  O  VAL A 738   N  LEU A 730           
SHEET    3  AA 5 TYR A 752  MET A 759 -1  O  THR A 753   N  ALA A 743           
SHEET    4  AA 5 LEU A 801  VAL A 804 -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 LEU A 870  VAL A 871  0                                        
SHEET    2  AB 2 ARG A 897  ASP A 898 -1  O  ARG A 897   N  VAL A 871           
SHEET    1  AC 2 ILE A 880  ALA A 883  0                                        
SHEET    2  AC 2 LYS A 887  ILE A 890 -1  O  LYS A 887   N  ALA A 883           
LINK         C   LYS A 808                 N   PTR A 809     1555   1555  1.33  
LINK         C   PTR A 809                 N   GLY A 810     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  
LINK         C   ARG A 908                 N   SEP A 909     1555   1555  1.33  
LINK         C   SEP A 909                 N   GLN A 910     1555   1555  1.33  
LINK         C   ILE A 927                 N   PTR A 928     1555   1555  1.33  
LINK         C   PTR A 928                 N   THR A 929     1555   1555  1.33  
SITE     1 AC1  7 ALA A 807  LYS A 808  GLY A 810  VAL A 882                    
SITE     2 AC1  7 ALA A 883  GLU A 884  GLY A 885                               
SITE     1 AC2  8 ARG A 873  GLY A 894  LEU A 895  ARG A 897                    
SITE     2 AC2  8 LYS A 907  ARG A 908  GLN A 910  PTR A 928                    
SITE     1 AC3 10 ARG A 873  ARG A 897  SEP A 909  GLY A 911                    
SITE     2 AC3 10 MET A 918  SER A 922  HIS A 926  ILE A 927                    
SITE     3 AC3 10 THR A 929  SER A 932                                          
SITE     1 AC4 11 LEU A 730  PHE A 735  VAL A 738  ALA A 756                    
SITE     2 AC4 11 LYS A 758  GLU A 775  VAL A 804  GLU A 805                    
SITE     3 AC4 11 ALA A 807  LEU A 881  SER A 891                               
SITE     1 AC5  7 PRO A 720  ASN A 723  HIS A 745  ASP A 903                    
SITE     2 AC5  7 SER A 904  VAL A 906  LYS A 907                               
CRYST1   98.430   98.430  144.550  90.00  90.00 120.00 P 63 2 2     12          
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      0.010160  0.005866  0.000000        0.00000                         
SCALE2      0.000000  0.011731  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006918        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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