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Database: PDB
Entry: 2X2M
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Original site: 2X2M 
HEADER    TRANSFERASE                             13-JAN-10   2X2M              
TITLE     CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH   
TITLE    2 INHIBITOR                                                            
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, RESIDUES 705-1013;                 
COMPND   5 SYNONYM: RET TYROSINE KINASE RECEPTOR, C-RET;                        
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBACPAK-HIS3 (CLONTECH) MODIFIED          
KEYWDS    HIRSCHSPRUNG DISEASE, GDNF RECEPTOR, TRANSMEMBRANE, PROTO-ONCOGENE,   
KEYWDS   2 PHOSPHOPROTEIN, DISEASE MUTATION, PHOSPHOTRANSFERASE, RET, KINASE,   
KEYWDS   3 MEMBRANE, TRANSFERASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.P.KNOWLES,J.MURRAY-RUST,S.KJAER,N.Q.MCDONALD                        
REVDAT   7   08-MAY-19 2X2M    1       REMARK LINK                              
REVDAT   6   30-JAN-19 2X2M    1       REMARK                                   
REVDAT   5   28-FEB-18 2X2M    1       JRNL                                     
REVDAT   4   28-JUN-17 2X2M    1       REMARK                                   
REVDAT   3   29-MAR-17 2X2M    1       REMARK                                   
REVDAT   2   02-MAR-10 2X2M    1       JRNL   REMARK                            
REVDAT   1   09-FEB-10 2X2M    0                                                
JRNL        AUTH   L.MOLOGNI,R.ROSTAGNO,S.BRUSSOLO,P.P.KNOWLES,S.KJAER,         
JRNL        AUTH 2 J.MURRAY-RUST,E.ROSSO,A.ZAMBON,L.SCAPOZZA,N.Q.MCDONALD,      
JRNL        AUTH 3 V.LUCCHINI,C.GAMBACORTI-PASSERINI                            
JRNL        TITL   SYNTHESIS, STRUCTURE-ACTIVITY RELATIONSHIP AND               
JRNL        TITL 2 CRYSTALLOGRAPHIC STUDIES OF 3-SUBSTITUTED INDOLIN-2-ONE RET  
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    BIOORG. MED. CHEM.            V.  18  1482 2010              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   20117004                                                     
JRNL        DOI    10.1016/J.BMC.2010.01.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22326                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1197                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1626                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4327                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 45                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.35                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.20000                                              
REMARK   3    B22 (A**2) : 0.70000                                              
REMARK   3    B33 (A**2) : -0.22000                                             
REMARK   3    B12 (A**2) : 0.43000                                              
REMARK   3    B13 (A**2) : 0.63000                                              
REMARK   3    B23 (A**2) : 1.02000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.508         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.278         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.194         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.581         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4471 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6049 ; 1.562 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   559 ; 5.533 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   158 ;37.612 ;22.911       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   742 ;16.289 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;18.952 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   679 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3264 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1951 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3042 ; 0.309 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   169 ; 0.244 ; 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):    32 ; 0.308 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.201 ; 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):  2897 ; 0.790 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4490 ; 1.365 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1844 ; 1.856 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1559 ; 2.928 ; 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.                                                          
REMARK   4                                                                      
REMARK   4 2X2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290036341.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23524                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.21                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.11000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.600                              
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 2IVT, FLEXIBLE LOOPS REMOVED               
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 4.5 MG/ML IN 20 MM TRIS-HCL PH   
REMARK 280  8, 100MM NACL, 1MM DTT, 1MM EDTA RESERVOIR 1.75 M SODIUM FORMATE,   
REMARK 280  0.1 SODIUM CITRATE PH 5.5, 0.15 M POTASSIUM THIOCYANATE VAPOUR      
REMARK 280  DIFFUSION, SITTING DROP, 289 K, VAPOR DIFFUSION, SITTING DROP       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: 3700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.1 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 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     GLU A   713                                                      
REMARK 465     GLY A   733                                                      
REMARK 465     GLU A   734                                                      
REMARK 465     LYS A   821                                                      
REMARK 465     VAL A   822                                                      
REMARK 465     GLY A   823                                                      
REMARK 465     PRO A   824                                                      
REMARK 465     GLY A   825                                                      
REMARK 465     TYR A   826                                                      
REMARK 465     LEU A   827                                                      
REMARK 465     GLY A   828                                                      
REMARK 465     SER A   829                                                      
REMARK 465     GLY A   830                                                      
REMARK 465     GLY A   831                                                      
REMARK 465     SER A   832                                                      
REMARK 465     ARG A   833                                                      
REMARK 465     ASN A   834                                                      
REMARK 465     SER A   835                                                      
REMARK 465     SER A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     HIS A   840                                                      
REMARK 465     PRO A   841                                                      
REMARK 465     ASP A   842                                                      
REMARK 465     GLU A   843                                                      
REMARK 465     ARG A   844                                                      
REMARK 465     LEU B   712                                                      
REMARK 465     GLU B   713                                                      
REMARK 465     ASP B   714                                                      
REMARK 465     GLY B   733                                                      
REMARK 465     GLU B   734                                                      
REMARK 465     PHE B   735                                                      
REMARK 465     GLY B   736                                                      
REMARK 465     ARG B   820                                                      
REMARK 465     LYS B   821                                                      
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     ARG B   844                                                      
REMARK 465     ARG B  1012                                                      
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     ALA A 708    O                                                   
REMARK 470     LYS A 710    CG   CD   CE   NZ                                   
REMARK 470     ILE A 711    CG1  CG2  CD1                                       
REMARK 470     ASP A 714    CG   OD1  OD2                                       
REMARK 470     ARG A 721    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 722    CD   CE   NZ                                        
REMARK 470     GLU A 732    CD   OE1  OE2                                       
REMARK 470     PHE A 735    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 762    CD   OE1  OE2                                       
REMARK 470     GLN A 796    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 797    CG   OD1  OD2                                       
REMARK 470     ARG A 820    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 848    CG   SD   CE                                        
REMARK 470     GLU A 867    CD   OE1  OE2                                       
REMARK 470     GLU A 884    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 892    OD1  OD2                                            
REMARK 470     TYR A 900    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLU A 901    CG   CD   OE2                                       
REMARK 470     ARG A 908    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 959    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 965    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    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 989    CE   NZ                                             
REMARK 470     GLN A 990    CD   OE1  NE2                                       
REMARK 470     GLU A 991    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 993    CG   OD1  OD2                                       
REMARK 470     LYS A 994    CD   CE   NZ                                        
REMARK 470     LYS A1003    CD   CE   NZ                                        
REMARK 470     GLU A1006    CD   OE1  OE2                                       
REMARK 470     LYS A1007    CG   CD   CE   NZ                                   
REMARK 470     LYS A1011    CG   CD   CE   NZ                                   
REMARK 470     ARG A1012    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A1013    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA B 708    O                                                   
REMARK 470     LYS B 710    CG   CD   CE   NZ                                   
REMARK 470     ILE B 711    CG1  CG2  CD1                                       
REMARK 470     LYS B 722    CD   CE   NZ                                        
REMARK 470     GLU B 732    CD   OE1  OE2                                       
REMARK 470     GLU B 762    CD   OE1  OE2                                       
REMARK 470     LYS B 780    NZ                                                  
REMARK 470     GLN B 796    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 797    CG   OD1  OD2                                       
REMARK 470     ARG B 813    CZ   NH1  NH2                                       
REMARK 470     GLU B 867    CD   OE1  OE2                                       
REMARK 470     MET B 868    CG   SD   CE                                        
REMARK 470     LYS B 869    CE   NZ                                             
REMARK 470     GLU B 884    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 900    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     GLU B 901    CG   CD   OE2                                       
REMARK 470     GLU B 902    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 912    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 959    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 965    CE   NZ                                             
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     GLN B 986    CD   OE1  NE2                                       
REMARK 470     LYS B 989    CE   NZ                                             
REMARK 470     GLN B 990    CD   OE1  NE2                                       
REMARK 470     GLU B 991    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 993    CG   OD1  OD2                                       
REMARK 470     LYS B 994    CD   CE   NZ                                        
REMARK 470     ASP B1000    CG   OD1  OD2                                       
REMARK 470     LYS B1003    CG   CD   CE   NZ                                   
REMARK 470     LYS B1007    CE   NZ                                             
REMARK 470     LYS B1011    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 763       44.13     75.44                                   
REMARK 500    ASP A 797       52.05   -143.72                                   
REMARK 500    ARG A 873      -39.82     79.75                                   
REMARK 500    ASP A 892       82.99     64.54                                   
REMARK 500    ASN B 763       43.24     74.08                                   
REMARK 500    ASN B 783       99.36   -162.35                                   
REMARK 500    ASP B 797     -164.13   -120.70                                   
REMARK 500    ARG B 873      -38.31     80.81                                   
REMARK 500    ASP B 892       78.73     54.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X2M A 2016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE X2M B 2015                
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 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: 2IVS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NON-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: 2X2K   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH  
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 2X2L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PHOSPHORYLATED RET TYROSINE KINASE DOMAIN WITH  
REMARK 900 INHIBITOR                                                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 705-1013 CORRESPOND WITH P07949, 700-704 ARE VECTOR-                 
REMARK 999 DERIVED                                                              
DBREF  2X2M A  700   704  PDB    2X2M     2X2M           700    704             
DBREF  2X2M A  705  1013  UNP    P07949   RET_HUMAN      705   1013             
DBREF  2X2M B  700   704  PDB    2X2M     2X2M           700    704             
DBREF  2X2M 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 PTR VAL LYS          
SEQRES  17 A  314  ARG SER GLN GLY ARG ILE PRO VAL LYS TRP MET ALA ILE          
SEQRES  18 A  314  GLU SER LEU PHE ASP HIS ILE TYR THR THR GLN SER ASP          
SEQRES  19 A  314  VAL TRP SER PHE GLY VAL LEU LEU TRP GLU ILE VAL THR          
SEQRES  20 A  314  LEU GLY GLY ASN PRO TYR PRO GLY ILE PRO PRO GLU ARG          
SEQRES  21 A  314  LEU PHE ASN LEU LEU LYS THR GLY HIS ARG MET GLU ARG          
SEQRES  22 A  314  PRO ASP ASN CYS SER GLU GLU MET TYR ARG LEU MET LEU          
SEQRES  23 A  314  GLN CYS TRP LYS GLN GLU PRO ASP LYS ARG PRO VAL PHE          
SEQRES  24 A  314  ALA ASP ILE SER LYS ASP LEU GLU LYS MET MET VAL LYS          
SEQRES  25 A  314  ARG ARG                                                      
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 PTR 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                                                      
MODRES 2X2M PTR A  905  TYR  O-PHOSPHOTYROSINE                                  
MODRES 2X2M PTR B  905  TYR  O-PHOSPHOTYROSINE                                  
HET    PTR  A 905      16                                                       
HET    PTR  B 905      16                                                       
HET    FMT  A2014       3                                                       
HET    FMT  A2015       3                                                       
HET    X2M  A2016      18                                                       
HET    FMT  B2012       3                                                       
HET    FMT  B2013       3                                                       
HET    FMT  B2014       3                                                       
HET    X2M  B2015      18                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     FMT FORMIC ACID                                                      
HETNAM     X2M (3Z)-3-[(3,5-DIMETHYL-1H-PYRROL-2-YL)METHYLIDENE]-1,3-           
HETNAM   2 X2M  DIHYDRO-2H-INDOL-2-ONE                                          
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3  FMT    5(C H2 O2)                                                   
FORMUL   5  X2M    2(C15 H14 N2 O)                                              
FORMUL  10  HOH   *45(H2 O)                                                     
HELIX    1   1 GLY A  700  ASP A  707  1                                   8    
HELIX    2   2 PRO A  720  LYS A  722  5                                   3    
HELIX    3   3 SER A  765  VAL A  782  1                                  18    
HELIX    4   4 SER A  811  GLU A  818  1                                   8    
HELIX    5   5 THR A  847  MET A  868  1                                  22    
HELIX    6   6 ALA A  876  ARG A  878  5                                   3    
HELIX    7   7 PRO A  914  MET A  918  5                                   5    
HELIX    8   8 ALA A  919  HIS A  926  1                                   8    
HELIX    9   9 THR A  929  THR A  946  1                                  18    
HELIX   10  10 PRO A  956  GLU A  958  5                                   3    
HELIX   11  11 ARG A  959  THR A  966  1                                   8    
HELIX   12  12 SER A  977  TRP A  988  1                                  12    
HELIX   13  13 GLU A  991  ARG A  995  5                                   5    
HELIX   14  14 VAL A  997  ARG A 1013  1                                  17    
HELIX   15  15 GLY B  700  ASP B  707  1                                   8    
HELIX   16  16 PRO B  720  LYS B  722  5                                   3    
HELIX   17  17 SER B  765  LYS B  780  1                                  16    
HELIX   18  18 SER B  811  GLU B  818  1                                   8    
HELIX   19  19 THR B  847  MET B  868  1                                  22    
HELIX   20  20 ALA B  876  ARG B  878  5                                   3    
HELIX   21  21 PRO B  914  MET B  918  5                                   5    
HELIX   22  22 ALA B  919  HIS B  926  1                                   8    
HELIX   23  23 THR B  929  THR B  946  1                                  18    
HELIX   24  24 PRO B  956  GLU B  958  5                                   3    
HELIX   25  25 ARG B  959  THR B  966  1                                   8    
HELIX   26  26 SER B  977  TRP B  988  1                                  12    
HELIX   27  27 GLU B  991  ARG B  995  5                                   5    
HELIX   28  28 VAL B  997  LYS B 1011  1                                  15    
SHEET    1  AA 5 LEU A 724  GLY A 731  0                                        
SHEET    2  AA 5 LYS A 737  LEU A 746 -1  O  VAL A 738   N  LEU A 730           
SHEET    3  AA 5 ARG A 749  MET A 759 -1  O  ARG A 749   N  LEU A 746           
SHEET    4  AA 5 LEU A 801  GLU A 805 -1  O  LEU A 802   N  LYS A 758           
SHEET    5  AA 5 LEU A 790  CYS A 794 -1  N  TYR A 791   O  ILE A 803           
SHEET    1  AB 2 LEU A 870  VAL A 871  0                                        
SHEET    2  AB 2 ARG A 897  ASP A 898 -1  O  ARG A 897   N  VAL A 871           
SHEET    1  AC 2 ILE A 880  ALA A 883  0                                        
SHEET    2  AC 2 LYS A 887  ILE A 890 -1  O  LYS A 887   N  ALA A 883           
SHEET    1  AD 2 PTR A 905  VAL A 906  0                                        
SHEET    2  AD 2 ILE A 927  TYR A 928 -1  O  TYR A 928   N  PTR A 905           
SHEET    1  BA 5 LEU B 724  GLY B 731  0                                        
SHEET    2  BA 5 VAL B 738  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  VAL B 804 -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 LEU B 870  VAL B 871  0                                        
SHEET    2  BB 2 ARG B 897  ASP B 898 -1  O  ARG B 897   N  VAL B 871           
SHEET    1  BC 2 ILE B 880  ALA B 883  0                                        
SHEET    2  BC 2 LYS B 887  ILE B 890 -1  O  LYS B 887   N  ALA B 883           
SHEET    1  BD 2 PTR B 905  VAL B 906  0                                        
SHEET    2  BD 2 ILE B 927  TYR B 928 -1  O  TYR B 928   N  PTR B 905           
LINK         C   SER A 904                 N   PTR A 905     1555   1555  1.32  
LINK         C   PTR A 905                 N   VAL A 906     1555   1555  1.32  
LINK         C   SER B 904                 N   PTR B 905     1555   1555  1.33  
LINK         C   PTR B 905                 N   VAL B 906     1555   1555  1.32  
SITE     1 AC1  7 GLN A 910  LEU A 923  HIS A 926  GLY B 700                    
SITE     2 AC1  7 PRO B 701  LEU B 702  SER B 703                               
SITE     1 AC2  6 ARG A 873  LEU A 895  LYS A 907  GLY A 911                    
SITE     2 AC2  6 ARG A 912  ILE A 913                                          
SITE     1 AC3  7 GLY A 700  LEU A 702  SER A 703  GLN B 910                    
SITE     2 AC3  7 LEU B 923  HIS B 926  HOH B3014                               
SITE     1 AC4  6 ARG B 873  LEU B 895  LYS B 907  GLY B 911                    
SITE     2 AC4  6 ARG B 912  ILE B 913                                          
SITE     1 AC5  6 ARG B 721  CYS B 794  ASP B 797  GLY B 798                    
SITE     2 AC5  6 PRO B 799  LEU B 801                                          
SITE     1 AC6 11 LEU A 730  ALA A 756  LYS A 758  VAL A 804                    
SITE     2 AC6 11 GLU A 805  TYR A 806  ALA A 807  LYS A 808                    
SITE     3 AC6 11 GLY A 810  LEU A 881  SER A 891                               
SITE     1 AC7  9 LEU B 730  ALA B 756  VAL B 804  GLU B 805                    
SITE     2 AC7  9 TYR B 806  ALA B 807  GLY B 810  LEU B 881                    
SITE     3 AC7  9 SER B 891                                                     
CRYST1   50.697   50.760   74.588 103.50  99.66  89.92 P 1           2          
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      0.019725 -0.000028  0.003449        0.00000                         
SCALE2      0.000000  0.019701  0.004797        0.00000                         
SCALE3      0.000000  0.000000  0.013997        0.00000                         
MTRIX1   1 -0.001420 -1.000000 -0.002510       -8.12835    1                    
MTRIX2   1 -1.000000  0.001420 -0.000650       -8.14759    1                    
MTRIX3   1  0.000650  0.002510 -1.000000       33.33179    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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