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Database: PDB
Entry: 2X2U
LinkDB: 2X2U
Original site: 2X2U 
HEADER    TRANSFERASE                             15-JAN-10   2X2U              
TITLE     FIRST TWO CADHERIN-LIKE DOMAINS FROM HUMAN RET                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CADHERIN-LIKE DOMAINS 1 AND 2, RESIDUES 29-270;            
COMPND   5 SYNONYM: C-RET, RET, CADHERIN FAMILY MEMBER 12;                      
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: ASN 151 IS GLYCOSYLATED                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: LEC8;                                   
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: OVARY;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PCDNA3                                     
KEYWDS    HIRSCHSPRUNG DISEASE, EXTRACELLULAR DOMAIN, DISEASE MUTATION,         
KEYWDS   2 TRANSFERASE, GLYCOPROTEIN, TRANSMEMBRANE, KINASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KJAER,S.HANRAHAN,A.G.PURKISS-TREW,N.TOTTY,N.Q.MCDONALD              
REVDAT   6   29-JUL-20 2X2U    1       COMPND REMARK HETNAM LINK                
REVDAT   6 2                   1       SITE   ATOM                              
REVDAT   5   15-MAY-19 2X2U    1       REMARK LINK                              
REVDAT   4   07-MAR-18 2X2U    1       JRNL                                     
REVDAT   3   06-JUL-11 2X2U    1       JRNL   REMARK DBREF  SEQADV              
REVDAT   2   26-MAY-10 2X2U    1       JRNL                                     
REVDAT   1   19-MAY-10 2X2U    0                                                
JRNL        AUTH   S.KJAER,S.HANRAHAN,N.TOTTY,N.Q.MCDONALD                      
JRNL        TITL   MAMMAL-RESTRICTED ELEMENTS PREDISPOSE HUMAN RET TO FOLDING   
JRNL        TITL 2 IMPAIRMENT BY HSCR MUTATIONS.                                
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  17   726 2010              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   20473317                                                     
JRNL        DOI    10.1038/NSMB.1808                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.86                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27156                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1447                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1961                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 104                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1921                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.129         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.133         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.129         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2064 ; 0.032 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2818 ; 2.587 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   235 ; 7.840 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    99 ;31.862 ;22.020       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   301 ;15.522 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.868 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   298 ; 0.198 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1570 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   870 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1337 ; 0.316 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   214 ; 0.196 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    43 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1232 ; 1.773 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1929 ; 2.751 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   970 ; 3.887 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   888 ; 5.362 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. RESIDUES 129-135 ARE DISORDERED                          
REMARK   4                                                                      
REMARK   4 2X2U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290041451.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.946, 1.514                       
REMARK 200  MONOCHROMATOR                  : SI (311) AND SI (111) CRYSTALS     
REMARK 200  OPTICS                         : TOROIDAL MIRRORS                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.60                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.86000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M (NH4)2SO4, 50 MM TRIS PH 7.5, 4%   
REMARK 280  (V/V) 1\,4 BUTANEDIOL AT 15 DEG C., TEMPERATURE 288K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.23750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       43.03700            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.03700            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       82.85625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.03700            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.03700            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       27.61875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.03700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.03700            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       82.85625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.03700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.03700            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       27.61875            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       55.23750            
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: 8800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -219.2 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS  87 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN  98 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 199 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 216 TO SER                        
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     PRO A   129                                                      
REMARK 465     THR A   130                                                      
REMARK 465     SER A   131                                                      
REMARK 465     LEU A   132                                                      
REMARK 465     ARG A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     ALA A   247                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     ALA A   249                                                      
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     GLU A  61    CD   OE1  OE2                                       
REMARK 470     GLU A 107    CD   OE1  OE2                                       
REMARK 470     LYS A 108    NZ                                                  
REMARK 470     SER A 128    OG                                                  
REMARK 470     GLU A 136    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 138    OE1  NE2                                            
REMARK 470     LYS A 161    CD   CE   NZ                                        
REMARK 470     ARG A 215    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 226    CZ   NH1  NH2                                       
REMARK 470     GLU A 232    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 233    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 236    CG   CD   CE   NZ                                   
REMARK 470     ARG A 250    CG   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   NH2  ARG A    87     O    HOH A  2060              1.94            
REMARK 500   O    HOH A  2087     O    HOH A  2090              2.04            
REMARK 500   O    HOH A  2079     O    HOH A  2208              2.12            
REMARK 500   O4   SO4 A  1277     O    HOH A  2203              2.19            
REMARK 500   O    HOH A  2169     O    HOH A  2170              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A 174   CE1   PHE A 174   CZ      0.127                       
REMARK 500    GLN A 187   CB    GLN A 187   CG     -0.170                       
REMARK 500    GLU A 251   CB    GLU A 251   CG     -0.151                       
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  87   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 189   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 205   NE  -  CZ  -  NH2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 230   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 230   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  206     LEU A  207                  149.38                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 SULPHATE (SO4): RESIDUE 8 APPEARS TO HAVE TWO                        
REMARK 600  CONFORMATIONS.                                                      
REMARK 600 DUMMY ATOMS (UNX): THESE DUMMY ATOMS REPRESENT A TRIS                
REMARK 600  MOLECULE WHICH IS PRESENT ON A TWO FOLD CRYSTALLOGRAPHIC            
REMARK 600  AXIS. ATTEMPTS TO REFINE THIS TRIS USING A DICTIONARY FILE          
REMARK 600  FAILED DUE TO THE FLEXIBILITY OF THE MOLECULE, SO THE               
REMARK 600  APPROXIMATE POSITIONS OF ATOMS WERE REFINED USING DUMMY             
REMARK 600  ATOMS.                                                              
REMARK 600 N-ACETYL-D-GLUCOSAMINE (NAG): TWO NAG RESIDUES ATTACHED TO           
REMARK 600  ASN 151 WITH A BETA 1-4 LINK BETWEEN THE NAG RESIDUES.              
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG B    2                                                       
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: PROVIDED BY DEPOSITOR                          
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X2K   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH  
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 2IVU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN       
REMARK 900 COMPLEXED WITH THE INHIBITOR ZD6474                                  
REMARK 900 RELATED ID: 2X2M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH  
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 2IVS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NON-PHOSPHORYLATED RET TYROSINE KINASE DOMAIN   
REMARK 900 RELATED ID: 1XPD   RELATED DB: PDB                                   
REMARK 900 THEORETICAL MODEL OF RET_HUMAN                                       
REMARK 900 RELATED ID: 2IVT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN       
REMARK 900 RELATED ID: 2IVV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN       
REMARK 900 COMPLEXED WITH THE INHIBITOR PP1                                     
REMARK 900 RELATED ID: 2X2L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH  
REMARK 900 INHIBITOR                                                            
DBREF  2X2U A   29   270  UNP    P07949   RET_HUMAN       29    270             
SEQADV 2X2U ARG A   87  UNP  P07949    CYS    87 ENGINEERED MUTATION            
SEQADV 2X2U GLN A   98  UNP  P07949    ASN    98 ENGINEERED MUTATION            
SEQADV 2X2U GLN A  199  UNP  P07949    ASN   199 ENGINEERED MUTATION            
SEQADV 2X2U SER A  216  UNP  P07949    CYS   216 ENGINEERED MUTATION            
SEQADV 2X2U GLU A  271  UNP  P07949              EXPRESSION TAG                 
SEQADV 2X2U PHE A  272  UNP  P07949              EXPRESSION TAG                 
SEQADV 2X2U GLU A  273  UNP  P07949              EXPRESSION TAG                 
SEQADV 2X2U ASN A  274  UNP  P07949              EXPRESSION TAG                 
SEQRES   1 A  246  LEU TYR PHE SER ARG ASP ALA TYR TRP GLU LYS LEU TYR          
SEQRES   2 A  246  VAL ASP GLN ALA ALA GLY THR PRO LEU LEU TYR VAL HIS          
SEQRES   3 A  246  ALA LEU ARG ASP ALA PRO GLU GLU VAL PRO SER PHE ARG          
SEQRES   4 A  246  LEU GLY GLN HIS LEU TYR GLY THR TYR ARG THR ARG LEU          
SEQRES   5 A  246  HIS GLU ASN ASN TRP ILE ARG ILE GLN GLU ASP THR GLY          
SEQRES   6 A  246  LEU LEU TYR LEU GLN ARG SER LEU ASP HIS SER SER TRP          
SEQRES   7 A  246  GLU LYS LEU SER VAL ARG ASN ARG GLY PHE PRO LEU LEU          
SEQRES   8 A  246  THR VAL TYR LEU LYS VAL PHE LEU SER PRO THR SER LEU          
SEQRES   9 A  246  ARG GLU GLY GLU CYS GLN TRP PRO GLY CYS ALA ARG VAL          
SEQRES  10 A  246  TYR PHE SER PHE PHE ASN THR SER PHE PRO ALA CYS SER          
SEQRES  11 A  246  SER LEU LYS PRO ARG GLU LEU CYS PHE PRO GLU THR ARG          
SEQRES  12 A  246  PRO SER PHE ARG ILE ARG GLU ASN ARG PRO PRO GLY THR          
SEQRES  13 A  246  PHE HIS GLN PHE ARG LEU LEU PRO VAL GLN PHE LEU CYS          
SEQRES  14 A  246  PRO GLN ILE SER VAL ALA TYR ARG LEU LEU GLU GLY GLU          
SEQRES  15 A  246  GLY LEU PRO PHE ARG SER ALA PRO ASP SER LEU GLU VAL          
SEQRES  16 A  246  SER THR ARG TRP ALA LEU ASP ARG GLU GLN ARG GLU LYS          
SEQRES  17 A  246  TYR GLU LEU VAL ALA VAL CYS THR VAL HIS ALA GLY ALA          
SEQRES  18 A  246  ARG GLU GLU VAL VAL MET VAL PRO PHE PRO VAL THR VAL          
SEQRES  19 A  246  TYR ASP GLU ASP ASP SER ALA PRO GLU PHE GLU ASN              
MODRES 2X2U ASN A  151  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NAG  B   2      11                                                       
HET    UNX  A1283       1                                                       
HET    UNX  A1284       1                                                       
HET    UNX  A1285       1                                                       
HET    UNX  A1286       1                                                       
HET    UNX  A1287       1                                                       
HET    UNX  A1288       1                                                       
HET    UNX  A1289       1                                                       
HET    UNX  A1290       1                                                       
HET    UNX  A1291       1                                                       
HET    UNX  A1292       1                                                       
HET    UNX  A1297       1                                                       
HET    SO4  A1275       5                                                       
HET    SO4  A1276       5                                                       
HET    SO4  A1277       5                                                       
HET    SO4  A1278       5                                                       
HET    SO4  A1279       5                                                       
HET    SO4  A1280       5                                                       
HET    SO4  A1281       5                                                       
HET    SO4  A1282      10                                                       
HET    BU1  A1293       6                                                       
HET    BU1  A1294       6                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BU1 1,4-BUTANEDIOL                                                   
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   3  UNX    11(X)                                                        
FORMUL  14  SO4    8(O4 S 2-)                                                   
FORMUL  22  BU1    2(C4 H10 O2)                                                 
FORMUL  24  HOH   *216(H2 O)                                                    
HELIX    1   1 THR A   75  ARG A   77  5                                   3    
HELIX    2   2 HIS A  103  ARG A  112  1                                  10    
HELIX    3   3 CYS A  157  SER A  159  5                                   3    
HELIX    4   4 PRO A  162  CYS A  166  1                                   5    
HELIX    5   5 LEU A  191  CYS A  197  1                                   7    
SHEET    1  AA 2 TYR A  30  PHE A  31  0                                        
SHEET    2  AA 2 ALA A  55  LEU A  56 -1  O  LEU A  56   N  TYR A  30           
SHEET    1  AB 4 ALA A  35  TYR A  41  0                                        
SHEET    2  AB 4 CYS A 142  PHE A 150  1  O  ARG A 144   N  TYR A  36           
SHEET    3  AB 4 THR A 120  PHE A 126 -1  O  VAL A 121   N  PHE A 147           
SHEET    4  AB 4 ARG A  67  LEU A  68 -1  O  ARG A  67   N  PHE A 126           
SHEET    1  AC 3 PRO A  49  TYR A  52  0                                        
SHEET    2  AC 3 LEU A  94  LEU A  97 -1  O  LEU A  95   N  LEU A  50           
SHEET    3  AC 3 ILE A  86  ILE A  88 -1  O  ARG A  87   N  TYR A  96           
SHEET    1  AD 2 HIS A  71  TYR A  73  0                                        
SHEET    2  AD 2 ARG A  79  GLU A  82 -1  N  LEU A  80   O  LEU A  72           
SHEET    1  AE 4 PHE A 174  ARG A 177  0                                        
SHEET    2  AE 4 GLU A 252  TYR A 263  1  O  PRO A 259   N  PHE A 174           
SHEET    3  AE 4 LYS A 236  VAL A 245 -1  O  TYR A 237   N  VAL A 260           
SHEET    4  AE 4 VAL A 202  LEU A 207 -1  O  ALA A 203   N  THR A 244           
SHEET    1  AF 3 THR A 184  GLN A 187  0                                        
SHEET    2  AF 3 GLU A 222  THR A 225 -1  O  VAL A 223   N  PHE A 185           
SHEET    3  AF 3 PHE A 214  ARG A 215 -1  O  ARG A 215   N  SER A 224           
SSBOND   1 CYS A  137    CYS A  142                          1555   1555  2.05  
SSBOND   2 CYS A  157    CYS A  197                          1555   1555  2.13  
SSBOND   3 CYS A  166    CYS A  243                          1555   1555  2.02  
LINK         ND2 ASN A 151                 C1  NAG B   1     1555   1555  1.47  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.46  
CISPEP   1 TRP A  139    PRO A  140          0         9.11                     
CRYST1   86.074   86.074  110.475  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011618  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011618  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009052        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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