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Database: PDB
Entry: 1RJB
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HEADER    TRANSFERASE                             19-NOV-03   1RJB              
TITLE     CRYSTAL STRUCTURE OF FLT3                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FL CYTOKINE RECEPTOR;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR FLT3, STEM CELL            
COMPND   6 TYROSINE KINASE 1, STK-1, CD135 ANTIGEN;                             
COMPND   7 EC: 2.7.1.112;                                                       
COMPND   8 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: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HIGH-5 INSECT CELLS;                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PBEV10                                     
KEYWDS    KINASE, STRUCTURE, AUTOINHIBITION, JUXTAMEMBRANE DOMAIN,              
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GRIFFITH,J.BLACK,C.FAERMAN,L.SWENSON,M.WYNN,F.LU,J.LIPPKE,          
AUTHOR   2 K.SAXENA                                                             
REVDAT   2   24-FEB-09 1RJB    1       VERSN                                    
REVDAT   1   03-FEB-04 1RJB    0                                                
JRNL        AUTH   J.GRIFFITH,J.BLACK,C.FAERMAN,L.SWENSON,M.WYNN,F.LU,          
JRNL        AUTH 2 J.LIPPKE,K.SAXENA                                            
JRNL        TITL   THE STRUCTURAL BASIS FOR AUTOINHIBITION OF FLT3 BY           
JRNL        TITL 2 THE JUXTAMEMBRANE DOMAIN.                                    
JRNL        REF    MOL.CELL                      V.  13   169 2004              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   14759363                                                     
JRNL        DOI    10.1016/S1097-2765(03)00505-7                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2000                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.26                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 29428                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1482                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 29428                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4568                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2550                       
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 230                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2406                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 310                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.61000                                              
REMARK   3    B22 (A**2) : 1.61000                                              
REMARK   3    B33 (A**2) : -3.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.24                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.27                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.090                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.57                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.85                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.41                                                 
REMARK   3   BSOL        : 81.05                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : MISSING.DAT                                    
REMARK   3  PARAMETER FILE  5  : PARMXRAY.XPL                                   
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : &_1_TOPOLOGY_INFILE_1                          
REMARK   3  TOPOLOGY FILE  2   : &_1_TOPOLOGY_INFILE_2                          
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  3   : &_1_TOPOLOGY_INFILE_3                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RJB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020797.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
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                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CRYSTALCLEAR (MSC/RIGAKU)          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29428                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.820                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, POTASSIUM              
REMARK 280  PHOSPHATE, CAPS, LITHIUM SULFATE, PH 6.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.06000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       40.32550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       40.32550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      112.59000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       40.32550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       40.32550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       37.53000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       40.32550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.32550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      112.59000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       40.32550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.32550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       37.53000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       75.06000            
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 300 REMARK: THERE IS ONE MONOMER IN THE ASYMMETRIC UNIT. THE             
REMARK 300 BIOLOGICAL UNIT OF CONSTRUCT USED IS A MONOMER                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A   564                                                      
REMARK 465     LYS A   565                                                      
REMARK 465     TYR A   566                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     LYS A   568                                                      
REMARK 465     GLN A   569                                                      
REMARK 465     PHE A   570                                                      
REMARK 465     ARG A   571                                                      
REMARK 465     LYS A   649                                                      
REMARK 465     ALA A   650                                                      
REMARK 465     ASP A   651                                                      
REMARK 465     SER A   652                                                      
REMARK 465     SER A   653                                                      
REMARK 465     GLU A   654                                                      
REMARK 465     SER A   762                                                      
REMARK 465     GLU A   763                                                      
REMARK 465     ASP A   764                                                      
REMARK 465     GLU A   765                                                      
REMARK 465     ILE A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     TYR A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     ASN A   770                                                      
REMARK 465     GLN A   771                                                      
REMARK 465     LYS A   772                                                      
REMARK 465     ARG A   773                                                      
REMARK 465     LEU A   774                                                      
REMARK 465     GLU A   775                                                      
REMARK 465     GLU A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     GLU A   778                                                      
REMARK 465     ASP A   779                                                      
REMARK 465     LEU A   780                                                      
REMARK 465     ASN A   781                                                      
REMARK 465     VAL A   782                                                      
REMARK 465     ALA A   948                                                      
REMARK 465     ASP A   949                                                      
REMARK 465     ALA A   950                                                      
REMARK 465     GLU A   951                                                      
REMARK 465     GLU A   952                                                      
REMARK 465     ALA A   953                                                      
REMARK 465     MET A   954                                                      
REMARK 465     TYR A   955                                                      
REMARK 465     GLN A   956                                                      
REMARK 465     ASN A   957                                                      
REMARK 465     VAL A   958                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD2  LEU A   901     CD2  LEU A   901     7555     1.96            
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    LYS A 634      -28.29    -33.53                                   
REMARK 500    ASP A 811       50.56   -144.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 110        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH A 111        DISTANCE =  6.84 ANGSTROMS                       
DBREF  1RJB A  564   907  UNP    P36888   FLT3_HUMAN     564    958             
SEQADV 1RJB     A       UNP  P36888    HIS   711 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ARG   712 DELETION                       
SEQADV 1RJB     A       UNP  P36888    THR   713 DELETION                       
SEQADV 1RJB     A       UNP  P36888    TRP   714 DELETION                       
SEQADV 1RJB     A       UNP  P36888    THR   715 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLU   716 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ILE   717 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PHE   718 DELETION                       
SEQADV 1RJB     A       UNP  P36888    LYS   719 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLU   720 DELETION                       
SEQADV 1RJB     A       UNP  P36888    HIS   721 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ASN   722 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PHE   723 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   724 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PHE   725 DELETION                       
SEQADV 1RJB     A       UNP  P36888    TYR   726 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PRO   727 DELETION                       
SEQADV 1RJB     A       UNP  P36888    THR   728 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PHE   729 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLN   730 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   731 DELETION                       
SEQADV 1RJB     A       UNP  P36888    HIS   732 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PRO   733 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ASN   734 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   735 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   736 DELETION                       
SEQADV 1RJB     A       UNP  P36888    MET   737 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PRO   738 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLY   739 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   740 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ARG   741 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLU   742 DELETION                       
SEQADV 1RJB     A       UNP  P36888    VAL   743 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLN   744 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ILE   745 DELETION                       
SEQADV 1RJB     A       UNP  P36888    HIS   746 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PRO   747 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ASP   748 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   749 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ASP   750 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLN   751 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ILE   752 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   753 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLY   754 DELETION                       
SEQADV 1RJB     A       UNP  P36888    LEU   755 DELETION                       
SEQADV 1RJB     A       UNP  P36888    HIS   756 DELETION                       
SEQADV 1RJB     A       UNP  P36888    GLY   757 DELETION                       
SEQADV 1RJB     A       UNP  P36888    ASN   758 DELETION                       
SEQADV 1RJB     A       UNP  P36888    SER   759 DELETION                       
SEQADV 1RJB     A       UNP  P36888    PHE   760 DELETION                       
SEQADV 1RJB     A       UNP  P36888    HIS   761 DELETION                       
SEQRES   1 A  344  HIS LYS TYR LYS LYS GLN PHE ARG TYR GLU SER GLN LEU          
SEQRES   2 A  344  GLN MET VAL GLN VAL THR GLY SER SER ASP ASN GLU TYR          
SEQRES   3 A  344  PHE TYR VAL ASP PHE ARG GLU TYR GLU TYR ASP LEU LYS          
SEQRES   4 A  344  TRP GLU PHE PRO ARG GLU ASN LEU GLU PHE GLY LYS VAL          
SEQRES   5 A  344  LEU GLY SER GLY ALA PHE GLY LYS VAL MET ASN ALA THR          
SEQRES   6 A  344  ALA TYR GLY ILE SER LYS THR GLY VAL SER ILE GLN VAL          
SEQRES   7 A  344  ALA VAL LYS MET LEU LYS GLU LYS ALA ASP SER SER GLU          
SEQRES   8 A  344  ARG GLU ALA LEU MET SER GLU LEU LYS MET MET THR GLN          
SEQRES   9 A  344  LEU GLY SER HIS GLU ASN ILE VAL ASN LEU LEU GLY ALA          
SEQRES  10 A  344  CYS THR LEU SER GLY PRO ILE TYR LEU ILE PHE GLU TYR          
SEQRES  11 A  344  CYS CYS TYR GLY ASP LEU LEU ASN TYR LEU ARG SER LYS          
SEQRES  12 A  344  ARG GLU LYS PHE SER GLU ASP GLU ILE GLU TYR GLU ASN          
SEQRES  13 A  344  GLN LYS ARG LEU GLU GLU GLU GLU ASP LEU ASN VAL LEU          
SEQRES  14 A  344  THR PHE GLU ASP LEU LEU CYS PHE ALA TYR GLN VAL ALA          
SEQRES  15 A  344  LYS GLY MET GLU PHE LEU GLU PHE LYS SER CYS VAL HIS          
SEQRES  16 A  344  ARG ASP LEU ALA ALA ARG ASN VAL LEU VAL THR HIS GLY          
SEQRES  17 A  344  LYS VAL VAL LYS ILE CYS ASP PHE GLY LEU ALA ARG ASP          
SEQRES  18 A  344  ILE MET SER ASP SER ASN TYR VAL VAL ARG GLY ASN ALA          
SEQRES  19 A  344  ARG LEU PRO VAL LYS TRP MET ALA PRO GLU SER LEU PHE          
SEQRES  20 A  344  GLU GLY ILE TYR THR ILE LYS SER ASP VAL TRP SER TYR          
SEQRES  21 A  344  GLY ILE LEU LEU TRP GLU ILE PHE SER LEU GLY VAL ASN          
SEQRES  22 A  344  PRO TYR PRO GLY ILE PRO VAL ASP ALA ASN PHE TYR LYS          
SEQRES  23 A  344  LEU ILE GLN ASN GLY PHE LYS MET ASP GLN PRO PHE TYR          
SEQRES  24 A  344  ALA THR GLU GLU ILE TYR ILE ILE MET GLN SER CYS TRP          
SEQRES  25 A  344  ALA PHE ASP SER ARG LYS ARG PRO SER PHE PRO ASN LEU          
SEQRES  26 A  344  THR SER PHE LEU GLY CYS GLN LEU ALA ASP ALA GLU GLU          
SEQRES  27 A  344  ALA MET TYR GLN ASN VAL                                      
FORMUL   2  HOH   *310(H2 O)                                                    
HELIX    1   1 ASP A  593  TYR A  597  5                                   5    
HELIX    2   2 ASP A  600  GLU A  604  5                                   5    
HELIX    3   3 PRO A  606  GLU A  608  5                                   3    
HELIX    4   4 ARG A  655  GLY A  669  1                                  15    
HELIX    5   5 ASP A  698  SER A  705  1                                   8    
HELIX    6   6 THR A  784  LYS A  805  1                                  22    
HELIX    7   7 ALA A  813  ARG A  815  5                                   3    
HELIX    8   8 PHE A  830  ARG A  834  5                                   5    
HELIX    9   9 ASP A  835  ASP A  839  5                                   5    
HELIX   10  10 PRO A  851  MET A  855  5                                   5    
HELIX   11  11 ALA A  856  GLY A  863  1                                   8    
HELIX   12  12 THR A  866  PHE A  882  1                                  17    
HELIX   13  13 ASP A  895  ASN A  904  1                                  10    
HELIX   14  14 THR A  915  TRP A  926  1                                  12    
HELIX   15  15 ASP A  929  ARG A  933  5                                   5    
HELIX   16  16 SER A  935  LEU A  947  1                                  13    
SHEET    1   A 3 TYR A 589  TYR A 591  0                                        
SHEET    2   A 3 LEU A 576  VAL A 581 -1  N  GLN A 580   O  PHE A 590           
SHEET    3   A 3 CYS A 807  HIS A 809 -1  O  VAL A 808   N  GLN A 577           
SHEET    1   B 5 LEU A 610  SER A 618  0                                        
SHEET    2   B 5 GLY A 622  TYR A 630 -1  O  THR A 628   N  GLU A 611           
SHEET    3   B 5 SER A 638  LEU A 646 -1  O  ILE A 639   N  ALA A 629           
SHEET    4   B 5 TYR A 688  GLU A 692 -1  O  PHE A 691   N  ALA A 642           
SHEET    5   B 5 LEU A 677  CYS A 681 -1  N  LEU A 678   O  ILE A 690           
SHEET    1   C 2 VAL A 817  THR A 820  0                                        
SHEET    2   C 2 VAL A 824  ILE A 827 -1  O  LYS A 826   N  LEU A 818           
SHEET    1   D 2 VAL A 843  ARG A 845  0                                        
SHEET    2   D 2 ALA A 848  LEU A 850 -1  O  LEU A 850   N  VAL A 843           
CRYST1   80.651   80.651  150.120  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012399  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006661        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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