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Database: PDB
Entry: 2IVS
LinkDB: 2IVS
Original site: 2IVS 
HEADER    TRANSFERASE                             16-JUN-06   2IVS              
TITLE     CRYSTAL STRUCTURE OF NON-PHOSPHORYLATED RET TYROSINE KINASE DOMAIN    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE RECEPTOR RET;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TYROSINE KINASE DOMAIN, UNP RESIDUES 705-1013;             
COMPND   5 SYNONYM: RET RECEPTOR, C-RET;                                        
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: 5 N-TERMINAL VECTOR-DERIVED RESIDUES GPLSL            
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_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PBACPAK-HIS3                              
KEYWDS    NUCLEOTIDE-BINDING, HIRSCHSPRUNG DISEASE, PHOSPHORYLATION, DISEASE    
KEYWDS   2 MUTATION, PHOSPHOTRANSFERASE, TYROSINE-PROTEIN KINASE, CHROMOSOMAL   
KEYWDS   3 TRANSLOCATION, POLYMORPHISM, GDNF RECEPTOR, TRANSMEMBRANE, PROTO-    
KEYWDS   4 ONCOGENE, TYROSINE KINASE, RET, KINASE, MEMBRANE, ATP-BINDING,       
KEYWDS   5 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.P.KNOWLES,J.MURRAY-RUST,N.Q.MCDONALD                                
REVDAT   6   08-MAY-19 2IVS    1       REMARK                                   
REVDAT   5   30-JAN-19 2IVS    1       REMARK                                   
REVDAT   4   20-DEC-17 2IVS    1       COMPND JRNL   REMARK HETNAM              
REVDAT   4 2                   1       ATOM                                     
REVDAT   3   24-FEB-09 2IVS    1       VERSN                                    
REVDAT   2   01-NOV-06 2IVS    1       JRNL                                     
REVDAT   1   14-AUG-06 2IVS    0                                                
JRNL        AUTH   P.P.KNOWLES,J.MURRAY-RUST,S.KJAER,R.P.SCOTT,S.HANRAHAN,      
JRNL        AUTH 2 M.SANTORO,C.F.IBANEZ,N.Q.MCDONALD                            
JRNL        TITL   STRUCTURE AND CHEMICAL INHIBITION OF THE RET TYROSINE KINASE 
JRNL        TITL 2 DOMAIN.                                                      
JRNL        REF    J.BIOL.CHEM.                  V. 281 33577 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16928683                                                     
JRNL        DOI    10.1074/JBC.M605604200                                       
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) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 39256                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2087                            
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) : 2394                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4311                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.66000                                              
REMARK   3    B22 (A**2) : -0.32000                                             
REMARK   3    B33 (A**2) : -1.27000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.21000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.175         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.640         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4485 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6074 ; 1.520 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   559 ; 5.321 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   175 ;34.637 ;23.086       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   738 ;13.161 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;18.987 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   674 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3319 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2061 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3073 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   291 ; 0.177 ; 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):    54 ; 0.166 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.195 ; 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):  2873 ; 1.015 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4447 ; 1.661 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1875 ; 2.609 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1625 ; 3.979 ; 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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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.                                                          
REMARK   4                                                                      
REMARK   4 2IVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1290029132.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.939                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
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   : 41522                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.00                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GJO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 3 MG/ML IN 20 MM TRIS-HCL PH     
REMARK 280  8.0, 10MM NACL, 1MM DTT RESERVOIR 2.0 M SODIUM FORMATE, 0.1M        
REMARK 280  SODIUM CITRATE PH 5.5 VAPOUR DIFFUSION, SITTING DROP,295 K,         
REMARK 280  VAPOR DIFFUSION, SITTING DROP                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.10850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   700                                                      
REMARK 465     PRO A   701                                                      
REMARK 465     LEU A   702                                                      
REMARK 465     SER A   703                                                      
REMARK 465     LEU 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     LYS A   710                                                      
REMARK 465     ILE A   711                                                      
REMARK 465     LEU A   712                                                      
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  1013                                                      
REMARK 465     LEU B   712                                                      
REMARK 465     GLU B   713                                                      
REMARK 465     ASP B   714                                                      
REMARK 465     VAL B   822                                                      
REMARK 465     GLY B   823                                                      
REMARK 465     PRO B   824                                                      
REMARK 465     GLY B   825                                                      
REMARK 465     TYR B   826                                                      
REMARK 465     LEU B   827                                                      
REMARK 465     GLY B   828                                                      
REMARK 465     SER B   829                                                      
REMARK 465     GLY B   830                                                      
REMARK 465     GLY B   831                                                      
REMARK 465     SER B   832                                                      
REMARK 465     ARG B   833                                                      
REMARK 465     ASN B   834                                                      
REMARK 465     SER B   835                                                      
REMARK 465     SER B   836                                                      
REMARK 465     SER B   837                                                      
REMARK 465     LEU B   838                                                      
REMARK 465     ASP B   839                                                      
REMARK 465     HIS B   840                                                      
REMARK 465     PRO B   841                                                      
REMARK 465     ASP B   842                                                      
REMARK 465     GLU B   843                                                      
REMARK 465     TYR B   900                                                      
REMARK 465     GLU B   901                                                      
REMARK 465     GLU B   902                                                      
REMARK 465     ASP B   903                                                      
REMARK 465     SER B   904                                                      
REMARK 465     TYR B   905                                                      
REMARK 465     VAL B   906                                                      
REMARK 465     LYS B   907                                                      
REMARK 465     ARG B   908                                                      
REMARK 465     SER B   909                                                      
REMARK 465     GLN B   910                                                      
REMARK 465     ARG B  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     GLU A 713    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 716    CG   CD   CE   NZ                                   
REMARK 470     LYS A 737    NZ                                                  
REMARK 470     LYS A 747    NZ                                                  
REMARK 470     ARG A 749    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 761    NZ                                                  
REMARK 470     LYS A 780    CE   NZ                                             
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 821    CG   CD   CE   NZ                                   
REMARK 470     LEU A 827    CG   CD1  CD2                                       
REMARK 470     LYS A 869    CD   CE   NZ                                        
REMARK 470     GLU A 884    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 900    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 902    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 907    CG   CD   CE   NZ                                   
REMARK 470     ARG A 959    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 965    CG   CD   CE   NZ                                   
REMARK 470     GLU A 971    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 978    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 979    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 982    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 989    CD   CE   NZ                                        
REMARK 470     GLU A 991    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 994    CD   CE   NZ                                        
REMARK 470     ARG A1012    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 710    CE   NZ                                             
REMARK 470     ILE B 711    CG1  CG2  CD1                                       
REMARK 470     LYS B 716    CD   CE   NZ                                        
REMARK 470     LYS B 737    CD   CE   NZ                                        
REMARK 470     LYS B 761    CG   CD   CE   NZ                                   
REMARK 470     GLU B 762    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 770    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 789    CE   NZ                                             
REMARK 470     GLU B 818    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 820    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 821    CG   CD   CE   NZ                                   
REMARK 470     GLU B 867    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 869    CG   CD   CE   NZ                                   
REMARK 470     LYS B 887    NZ                                                  
REMARK 470     ASP B 898    CG   OD1  OD2                                       
REMARK 470     VAL B 899    CG1  CG2                                            
REMARK 470     ARG B 959    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B 962    CG   OD1  ND2                                       
REMARK 470     LYS B 965    CG   CD   CE   NZ                                   
REMARK 470     ASN B 975    CG   OD1  ND2                                       
REMARK 470     GLU B 978    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 979    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 982    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 989    CE   NZ                                             
REMARK 470     GLU B 991    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 994    CE   NZ                                             
REMARK 470     LYS B1011    CG   CD   CE   NZ                                   
REMARK 470     ARG B1012    CG   CD   NE   CZ   NH1  NH2                        
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A  863   NE2                                                 
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   OD2  ASP A  1000     O    HOH A  2137              1.93            
REMARK 500   NE2  GLN A   931     O    HOH A  2100              1.97            
REMARK 500   O    HOH A  2091     O    HOH A  2098              2.15            
REMARK 500   O    HOH A  2041     O    HOH A  2077              2.16            
REMARK 500   NH2  ARG B   749     O    HOH B  2020              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    GLN A 863   CD    GLN A 863   NE2     1.186                       
REMARK 500    GLN A 863   CD    GLN A 863   NE2     1.528                       
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    GLN A 863   OE1 -  CD  -  NE2 ANGL. DEV. =  33.1 DEGREES          
REMARK 500    GLN A 863   OE1 -  CD  -  NE2 ANGL. DEV. =  15.4 DEGREES          
REMARK 500    GLN A 863   CG  -  CD  -  NE2 ANGL. DEV. = -63.8 DEGREES          
REMARK 500    GLN A 863   CG  -  CD  -  NE2 ANGL. DEV. = -40.8 DEGREES          
REMARK 500    ARG A 912   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 912   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 873      -26.26     77.78                                   
REMARK 500    ASP A 892       73.30     61.37                                   
REMARK 500    ARG B 873      -25.74     73.93                                   
REMARK 500    ASP B 892       66.85     63.60                                   
REMARK 500    ASN B 975       59.28   -105.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLN A 863         0.18    SIDE CHAIN                              
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 ACK A3016                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACK B3016                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A3013                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A3014                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B3013                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B3014                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B3015                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IVT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN       
REMARK 900 RELATED ENTRIES                                                      
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: 2IVV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN       
REMARK 900 COMPLEXED WITH THE INHIBITOR PP1                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 705-1013 CORRESPOND WITH P07949, 700-704 ARE VECTOR-                 
REMARK 999 DERIVED                                                              
DBREF  2IVS A  700   704  PDB    2IVS     2IVS           700    704             
DBREF  2IVS A  705  1013  UNP    P07949   RET_HUMAN      705   1013             
DBREF  2IVS B  700   704  PDB    2IVS     2IVS           700    704             
DBREF  2IVS B  705  1013  UNP    P07949   RET_HUMAN      705   1013             
SEQRES   1 A  314  GLY PRO LEU SER LEU SER VAL ASP ALA PHE LYS ILE LEU          
SEQRES   2 A  314  GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN LEU VAL          
SEQRES   3 A  314  LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY LYS VAL          
SEQRES   4 A  314  VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG ALA GLY          
SEQRES   5 A  314  TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU ASN ALA          
SEQRES   6 A  314  SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU PHE ASN          
SEQRES   7 A  314  VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE LYS LEU          
SEQRES   8 A  314  TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU LEU ILE          
SEQRES   9 A  314  VAL GLU TYR ALA LYS TYR GLY SER LEU ARG GLY PHE LEU          
SEQRES  10 A  314  ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU GLY SER          
SEQRES  11 A  314  GLY GLY SER ARG ASN SER SER SER LEU ASP HIS PRO ASP          
SEQRES  12 A  314  GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER PHE ALA          
SEQRES  13 A  314  TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA GLU MET          
SEQRES  14 A  314  LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU          
SEQRES  15 A  314  VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP PHE GLY          
SEQRES  16 A  314  LEU SER ARG ASP VAL TYR GLU GLU ASP SER TYR VAL LYS          
SEQRES  17 A  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP MET ALA ILE          
SEQRES  18 A  314  GLU SER LEU PHE ASP HIS ILE TYR THR THR GLN SER ASP          
SEQRES  19 A  314  VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE VAL THR          
SEQRES  20 A  314  LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO GLU ARG          
SEQRES  21 A  314  LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET GLU ARG          
SEQRES  22 A  314  PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU MET LEU          
SEQRES  23 A  314  GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO VAL PHE          
SEQRES  24 A  314  ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET VAL LYS          
SEQRES  25 A  314  ARG ARG                                                      
SEQRES   1 B  314  GLY PRO LEU SER LEU SER VAL ASP ALA PHE LYS ILE LEU          
SEQRES   2 B  314  GLU ASP PRO LYS TRP GLU PHE PRO ARG LYS ASN LEU VAL          
SEQRES   3 B  314  LEU GLY LYS THR LEU GLY GLU GLY GLU PHE GLY LYS VAL          
SEQRES   4 B  314  VAL LYS ALA THR ALA PHE HIS LEU LYS GLY ARG ALA GLY          
SEQRES   5 B  314  TYR THR THR VAL ALA VAL LYS MET LEU LYS GLU ASN ALA          
SEQRES   6 B  314  SER PRO SER GLU LEU ARG ASP LEU LEU SER GLU PHE ASN          
SEQRES   7 B  314  VAL LEU LYS GLN VAL ASN HIS PRO HIS VAL ILE LYS LEU          
SEQRES   8 B  314  TYR GLY ALA CYS SER GLN ASP GLY PRO LEU LEU LEU ILE          
SEQRES   9 B  314  VAL GLU TYR ALA LYS TYR GLY SER LEU ARG GLY PHE LEU          
SEQRES  10 B  314  ARG GLU SER ARG LYS VAL GLY PRO GLY TYR LEU GLY SER          
SEQRES  11 B  314  GLY GLY SER ARG ASN SER SER SER LEU ASP HIS PRO ASP          
SEQRES  12 B  314  GLU ARG ALA LEU THR MET GLY ASP LEU ILE SER PHE ALA          
SEQRES  13 B  314  TRP GLN ILE SER GLN GLY MET GLN TYR LEU ALA GLU MET          
SEQRES  14 B  314  LYS LEU VAL HIS ARG ASP LEU ALA ALA ARG ASN ILE LEU          
SEQRES  15 B  314  VAL ALA GLU GLY ARG LYS MET LYS ILE SER ASP PHE GLY          
SEQRES  16 B  314  LEU SER ARG ASP VAL TYR GLU GLU ASP SER TYR VAL LYS          
SEQRES  17 B  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP MET ALA ILE          
SEQRES  18 B  314  GLU SER LEU PHE ASP HIS ILE TYR THR THR GLN SER ASP          
SEQRES  19 B  314  VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE VAL THR          
SEQRES  20 B  314  LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO GLU ARG          
SEQRES  21 B  314  LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET GLU ARG          
SEQRES  22 B  314  PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU MET LEU          
SEQRES  23 B  314  GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO VAL PHE          
SEQRES  24 B  314  ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET VAL LYS          
SEQRES  25 B  314  ARG ARG                                                      
HET    FMT  A3013       3                                                       
HET    FMT  A3014       3                                                       
HET    FMT  A3015       3                                                       
HET    ACK  A3016      22                                                       
HET    FMT  B3013       3                                                       
HET    FMT  B3014       3                                                       
HET    FMT  B3015       3                                                       
HET    ACK  B3016      22                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM     ACK 2',3'- CYCLIC AMP                                                
FORMUL   3  FMT    6(C H2 O2)                                                   
FORMUL   6  ACK    2(C10 H12 N5 O6 P)                                           
FORMUL  11  HOH   *262(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  LYS A  780  1                                  16    
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 ALA A  876  ARG A  878  5                                   3    
HELIX    7   7 PRO A  914  MET A  918  5                                   5    
HELIX    8   8 ALA A  919  HIS A  926  1                                   8    
HELIX    9   9 THR A  929  THR A  946  1                                  18    
HELIX   10  10 PRO A  956  GLU A  958  5                                   3    
HELIX   11  11 ARG A  959  THR A  966  1                                   8    
HELIX   12  12 SER A  977  TRP A  988  1                                  12    
HELIX   13  13 GLU A  991  ARG A  995  5                                   5    
HELIX   14  14 VAL A  997  LYS A 1011  1                                  15    
HELIX   15  15 GLY B  700  ILE B  711  1                                  12    
HELIX   16  16 PRO B  720  LYS B  722  5                                   3    
HELIX   17  17 LEU B  746  ARG B  749  5                                   4    
HELIX   18  18 SER B  765  LYS B  780  1                                  16    
HELIX   19  19 SER B  811  GLU B  818  1                                   8    
HELIX   20  20 THR B  847  MET B  868  1                                  22    
HELIX   21  21 ALA B  876  ARG B  878  5                                   3    
HELIX   22  22 ASP B  892  SER B  896  5                                   5    
HELIX   23  23 PRO B  914  MET B  918  5                                   5    
HELIX   24  24 ALA B  919  HIS B  926  1                                   8    
HELIX   25  25 THR B  929  THR B  946  1                                  18    
HELIX   26  26 PRO B  956  GLU B  958  5                                   3    
HELIX   27  27 ARG B  959  THR B  966  1                                   8    
HELIX   28  28 SER B  977  TRP B  988  1                                  12    
HELIX   29  29 GLU B  991  ARG B  995  5                                   5    
HELIX   30  30 VAL B  997  ARG B 1012  1                                  16    
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  GLU A 805 -1  O  LEU A 802   N  LYS A 758           
SHEET    5  AA 5 LEU A 790  CYS A 794 -1  N  TYR A 791   O  ILE A 803           
SHEET    1  AB 2 GLY A 825  TYR A 826  0                                        
SHEET    2  AB 2 ALA A 845  LEU A 846  1  N  LEU A 846   O  GLY A 825           
SHEET    1  AC 2 LEU A 870  VAL A 871  0                                        
SHEET    2  AC 2 ARG A 897  ASP A 898 -1  O  ARG A 897   N  VAL A 871           
SHEET    1  AD 2 ILE A 880  ALA A 883  0                                        
SHEET    2  AD 2 LYS A 887  ILE A 890 -1  O  LYS A 887   N  ALA A 883           
SHEET    1  AE 2 TYR A 905  VAL A 906  0                                        
SHEET    2  AE 2 ILE A 927  TYR A 928 -1  O  TYR A 928   N  TYR A 905           
SHEET    1  BA 5 LEU B 724  GLU B 732  0                                        
SHEET    2  BA 5 LYS B 737  PHE B 744 -1  O  VAL B 738   N  LEU B 730           
SHEET    3  BA 5 TYR B 752  MET B 759 -1  O  THR B 753   N  ALA B 743           
SHEET    4  BA 5 LEU B 801  GLU B 805 -1  O  LEU B 802   N  LYS B 758           
SHEET    5  BA 5 LEU B 790  CYS B 794 -1  N  TYR B 791   O  ILE B 803           
SHEET    1  BB 2 ILE B 880  ALA B 883  0                                        
SHEET    2  BB 2 LYS B 887  ILE B 890 -1  O  LYS B 887   N  ALA B 883           
CISPEP   1 GLY A  823    PRO A  824          0         0.70                     
SITE     1 AC1 16 LEU A 730  GLU A 732  VAL A 738  ALA A 756                    
SITE     2 AC1 16 VAL A 804  GLU A 805  ALA A 807  GLY A 810                    
SITE     3 AC1 16 SER A 811  LEU A 881  HOH A2014  HOH A2079                    
SITE     4 AC1 16 HOH A2143  HOH A2146  HOH A2147  FMT A3015                    
SITE     1 AC2 15 LEU B 730  GLU B 732  GLY B 733  VAL B 738                    
SITE     2 AC2 15 ALA B 756  VAL B 804  GLU B 805  ALA B 807                    
SITE     3 AC2 15 GLY B 810  SER B 811  LEU B 881  HOH B2064                    
SITE     4 AC2 15 HOH B2112  HOH B2113  HOH B2114                               
SITE     1 AC3  6 ARG A 873  LEU A 895  ARG A 897  GLY A 911                    
SITE     2 AC3  6 ARG A 912  ILE A 913                                          
SITE     1 AC4  7 GLY A 733  GLU A 734  PHE A 735  GLY A 736                    
SITE     2 AC4  7 LYS A 758  HOH A2082  HOH A2143                               
SITE     1 AC5  6 ARG A 878  ASN A 879  ASP A 892  HOH A2144                    
SITE     2 AC5  6 HOH A2145  ACK A3016                                          
SITE     1 AC6  8 GLN A 910  LEU A 923  PHE A 924  HIS A 926                    
SITE     2 AC6  8 GLY B 700  PRO B 701  LEU B 702  SER B 703                    
SITE     1 AC7  5 ARG B 873  LEU B 895  ARG B 897  GLY B 911                    
SITE     2 AC7  5 ARG B 912                                                     
SITE     1 AC8  7 GLY B 733  GLU B 734  PHE B 735  GLY B 736                    
SITE     2 AC8  7 LYS B 758  HOH B2111  HOH B2112                               
CRYST1   50.399   80.217   79.684  90.00 100.09  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019842  0.000000  0.003531        0.00000                         
SCALE2      0.000000  0.012466  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012747        0.00000                         
MTRIX1   1 -0.104840 -0.982570  0.153490       27.00879    1                    
MTRIX2   1 -0.980940  0.076790 -0.178500       20.02734    1                    
MTRIX3   1  0.163600 -0.169280 -0.971900      -29.55180    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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