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Database: PDB
Entry: 2E9W
LinkDB: 2E9W
Original site: 2E9W 
HEADER    TRANSFERASE/HORMONE                     27-JAN-07   2E9W              
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF KIT IN COMPLEX WITH  
TITLE    2 STEM CELL FACTOR (SCF)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAST/STEM CELL GROWTH FACTOR RECEPTOR;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAINS, D1 - D5;                            
COMPND   5 SYNONYM: SCFR, PROTO-ONCOGENE TYROSINE-PROTEIN KINASE KIT, C-KIT,    
COMPND   6 CD117 ANTIGEN;                                                       
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: KIT LIGAND;                                                
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 FRAGMENT: SOLUBLE FORM, RESIDUES 26 - 166;                           
COMPND  14 SYNONYM: C-KIT LIGAND, STEM CELL FACTOR, SCF, MAST CELL GROWTH       
COMPND  15 FACTOR, MGF;                                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KIT;                                                           
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PBLUEBAC III;                              
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: SCF;                                                           
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: MGT7;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    GLYCOPROTEIN, RECEPTOR TYROSINE KINASE, GROWTH FACTOR CYTOKINE,       
KEYWDS   2 DIMERIZATION, TRANSFERASE-HORMONE COMPLEX                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YUZAWA,Y.OPATOWSKY,Z.ZHANG,V.MANDIYAN,I.LAX,J.SCHLESSINGER          
REVDAT   4   29-JUL-20 2E9W    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 2E9W    1       VERSN                                    
REVDAT   2   24-FEB-09 2E9W    1       VERSN                                    
REVDAT   1   07-AUG-07 2E9W    0                                                
JRNL        AUTH   S.YUZAWA,Y.OPATOWSKY,Z.ZHANG,V.MANDIYAN,I.LAX,J.SCHLESSINGER 
JRNL        TITL   STRUCTURAL BASIS FOR ACTIVATION OF THE RECEPTOR TYROSINE     
JRNL        TITL 2 KINASE KIT BY STEM CELL FACTOR                               
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 130   323 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17662946                                                     
JRNL        DOI    10.1016/J.CELL.2007.05.055                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 4329206.640                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 31945                          
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 SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.294                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1594                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4770                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 241                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.024                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9084                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 84                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 78.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.15000                                             
REMARK   3    B22 (A**2) : 23.73000                                             
REMARK   3    B33 (A**2) : -16.58000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 28.76000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.63                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.75                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.700                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.020                           
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) : 7.410 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 11.800; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 11.630; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 16.820; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.43                                                 
REMARK   3   BSOL        : 243.0                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2E9W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000026408.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.249999                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31962                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.550                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.17600                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EXZ AND 2EC8                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-12% PEG 8000, 5-8% ETHYLENE GLYCOL,    
REMARK 280  0.2M AMMONIUM SULFATE, PH 8.0, VAPOR DIFFUSION, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      134.73850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.03600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      134.73850            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       26.03600            
REMARK 290   SMTRY3   4  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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     GLN A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     THR A   446                                                      
REMARK 465     GLU A   447                                                      
REMARK 465     GLN A   448                                                      
REMARK 465     ARG A   449                                                      
REMARK 465     GLY A   466                                                      
REMARK 465     PRO A   467                                                      
REMARK 465     PRO A   468                                                      
REMARK 465     PHE A   508                                                      
REMARK 465     LYS A   509                                                      
REMARK 465     GLY A   510                                                      
REMARK 465     ASN A   511                                                      
REMARK 465     ASN A   512                                                      
REMARK 465     LYS A   513                                                      
REMARK 465     GLU A   514                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     VAL B    29                                                      
REMARK 465     SER B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     MET B   318                                                      
REMARK 465     ILE B   319                                                      
REMARK 465     THR B   446                                                      
REMARK 465     GLU B   447                                                      
REMARK 465     GLN B   448                                                      
REMARK 465     ARG B   449                                                      
REMARK 465     PHE B   508                                                      
REMARK 465     LYS B   509                                                      
REMARK 465     GLY B   510                                                      
REMARK 465     ASN B   511                                                      
REMARK 465     ASN B   512                                                      
REMARK 465     LYS B   513                                                      
REMARK 465     GLU B   514                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     LYS C    96                                                      
REMARK 465     ASP C    97                                                      
REMARK 465     LEU C    98                                                      
REMARK 465     LYS C    99                                                      
REMARK 465     ALA C   132                                                      
REMARK 465     SER C   133                                                      
REMARK 465     GLU C   134                                                      
REMARK 465     SER C   141                                                      
REMARK 465     GLU D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     VAL D   131                                                      
REMARK 465     ALA D   132                                                      
REMARK 465     SER D   133                                                      
REMARK 465     GLU D   134                                                      
REMARK 465     THR D   135                                                      
REMARK 465     SER D   136                                                      
REMARK 465     ASP D   137                                                      
REMARK 465     CYS D   138                                                      
REMARK 465     VAL D   139                                                      
REMARK 465     VAL D   140                                                      
REMARK 465     SER D   141                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  33    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 117    CG   CD1  CD2                                       
REMARK 470     LYS A 154    CG   CD   CE   NZ                                   
REMARK 470     LYS A 158    CG   CD   CE   NZ                                   
REMARK 470     ARG A 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 173    CG   CD   CE   NZ                                   
REMARK 470     LYS A 218    CG   CD   CE   NZ                                   
REMARK 470     SER A 278    OG                                                  
REMARK 470     LYS A 310    CG   CD   CE   NZ                                   
REMARK 470     MET A 318    CG   SD   CE                                        
REMARK 470     GLU A 344    CG   CD   OE1  OE2                                  
REMARK 470     THR A 356    OG1  CG2                                            
REMARK 470     ASP A 357    CG   OD1  OD2                                       
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     LYS A 383    CG   CD   CE   NZ                                   
REMARK 470     VAL A 399    CG1  CG2                                            
REMARK 470     ASN A 423    CG   OD1  ND2                                       
REMARK 470     ASP A 439    CG   OD1  OD2                                       
REMARK 470     TYR A 441    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE A 442    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS A 443    SG                                                  
REMARK 470     PRO A 444    CG   CD                                             
REMARK 470     CYS A 450    SG                                                  
REMARK 470     SER A 451    OG                                                  
REMARK 470     SER A 453    OG                                                  
REMARK 470     VAL A 454    CG1  CG2                                            
REMARK 470     LEU A 455    CG   CD1  CD2                                       
REMARK 470     PRO A 456    CG   CD                                             
REMARK 470     VAL A 457    CG1  CG2                                            
REMARK 470     ASP A 458    CG   OD1  OD2                                       
REMARK 470     VAL A 459    CG1  CG2                                            
REMARK 470     GLN A 460    CG   CD   OE1  NE2                                  
REMARK 470     THR A 461    OG1  CG2                                            
REMARK 470     LEU A 462    CG   CD1  CD2                                       
REMARK 470     ASN A 463    CG   OD1  ND2                                       
REMARK 470     SER A 464    OG                                                  
REMARK 470     SER A 465    OG                                                  
REMARK 470     PHE A 469    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A 483    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 484    CG   CD   CE   NZ                                   
REMARK 470     HIS A 485    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN A 486    CG   OD1  ND2                                       
REMARK 470     LYS A 492    CG   CD   CE   NZ                                   
REMARK 470     TYR A 494    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 496    CG   OD1  OD2                                       
REMARK 470     VAL A 497    CG1  CG2                                            
REMARK 470     LYS A 499    CG   CD   CE   NZ                                   
REMARK 470     TYR A 503    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  33    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 117    CG   CD1  CD2                                       
REMARK 470     LYS B 154    CG   CD   CE   NZ                                   
REMARK 470     ARG B 161    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 173    CG   CD   CE   NZ                                   
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     TYR B 243    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 244    OG                                                  
REMARK 470     GLU B 249    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 252    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 254    CG   CD   CE   NZ                                   
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     TYR B 259    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER B 278    OG                                                  
REMARK 470     LYS B 310    CG   CD   CE   NZ                                   
REMARK 470     GLU B 344    CG   CD   OE1  OE2                                  
REMARK 470     MET B 351    CG   SD   CE                                        
REMARK 470     THR B 356    OG1  CG2                                            
REMARK 470     ASP B 357    CG   OD1  OD2                                       
REMARK 470     LYS B 358    CG   CD   CE   NZ                                   
REMARK 470     HIS B 378    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 383    CG   CD   CE   NZ                                   
REMARK 470     VAL B 399    CG1  CG2                                            
REMARK 470     ASN B 423    CG   OD1  ND2                                       
REMARK 470     ASP B 439    CG   OD1  OD2                                       
REMARK 470     TYR B 441    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE B 442    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS B 443    SG                                                  
REMARK 470     PRO B 444    CG   CD                                             
REMARK 470     CYS B 450    SG                                                  
REMARK 470     SER B 451    OG                                                  
REMARK 470     SER B 453    OG                                                  
REMARK 470     VAL B 454    CG1  CG2                                            
REMARK 470     LEU B 455    CG   CD1  CD2                                       
REMARK 470     PRO B 456    CG   CD                                             
REMARK 470     VAL B 457    CG1  CG2                                            
REMARK 470     ASP B 458    CG   OD1  OD2                                       
REMARK 470     VAL B 459    CG1  CG2                                            
REMARK 470     GLN B 460    CG   CD   OE1  NE2                                  
REMARK 470     THR B 461    OG1  CG2                                            
REMARK 470     LEU B 462    CG   CD1  CD2                                       
REMARK 470     ASN B 463    CG   OD1  ND2                                       
REMARK 470     SER B 464    OG                                                  
REMARK 470     SER B 465    OG                                                  
REMARK 470     PHE B 469    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 471    CG   CD   CE   NZ                                   
REMARK 470     PHE B 483    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 484    CG   CD   CE   NZ                                   
REMARK 470     HIS B 485    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 486    CG   OD1  ND2                                       
REMARK 470     LYS B 492    CG   CD   CE   NZ                                   
REMARK 470     TYR B 494    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 496    CG   OD1  OD2                                       
REMARK 470     VAL B 497    CG1  CG2                                            
REMARK 470     LYS B 499    CG   CD   CE   NZ                                   
REMARK 470     TYR B 503    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG C   5    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C  41    OG                                                  
REMARK 470     SER C  67    OG                                                  
REMARK 470     GLU C  68    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  91    CG   CD   CE   NZ                                   
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     PHE C 102    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP C 128    CG   OD1  OD2                                       
REMARK 470     THR C 135    OG1  CG2                                            
REMARK 470     VAL C 139    CG1  CG2                                            
REMARK 470     ARG D   5    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D  41    OG                                                  
REMARK 470     SER D  67    OG                                                  
REMARK 470     GLU D  68    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  91    CG   CD   CE   NZ                                   
REMARK 470     LYS D 100    CG   CD   CE   NZ                                   
REMARK 470     PHE D 102    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP D 128    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 151   CA  -  CB  -  SG  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    CYS A 183   CA  -  CB  -  SG  ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP B 121   N   -  CA  -  C   ANGL. DEV. = -16.3 DEGREES          
REMARK 500    PRO B 137   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    CYS B 151   CA  -  CB  -  SG  ANGL. DEV. =   8.9 DEGREES          
REMARK 500    PRO B 456   N   -  CA  -  CB  ANGL. DEV. =   7.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  64      -35.57   -132.63                                   
REMARK 500    LYS A  65      157.45    175.72                                   
REMARK 500    ILE A  70      -78.81   -114.38                                   
REMARK 500    LEU A  71      -61.39   -103.76                                   
REMARK 500    GLU A  73      155.82    -46.16                                   
REMARK 500    GLN A  79      117.04   -167.68                                   
REMARK 500    ALA A  89      -12.87    -45.55                                   
REMARK 500    SER A 106      133.27    173.59                                   
REMARK 500    ARG A 122        4.57    -52.90                                   
REMARK 500    LEU A 124      108.22   -162.64                                   
REMARK 500    ASP A 129      -21.76     69.71                                   
REMARK 500    ARG A 135       68.89    -64.91                                   
REMARK 500    LYS A 154     -174.94    -54.09                                   
REMARK 500    ASP A 165       99.08   -170.63                                   
REMARK 500    PRO A 166      -19.38    -42.47                                   
REMARK 500    ALA A 168      -92.01   -137.81                                   
REMARK 500    VAL A 175      113.84    -21.59                                   
REMARK 500    ALA A 178        2.35    -57.97                                   
REMARK 500    LEU A 202      134.21    -37.71                                   
REMARK 500    ALA A 210      151.96    177.70                                   
REMARK 500    LEU A 222      112.06   -160.76                                   
REMARK 500    VAL A 238       -8.84    -56.18                                   
REMARK 500    SER A 241       -9.84    -53.01                                   
REMARK 500    VAL A 242      179.34    -50.29                                   
REMARK 500    GLU A 249      128.90    -33.57                                   
REMARK 500    ASN A 250       75.95     46.21                                   
REMARK 500    SER A 251      139.87    175.38                                   
REMARK 500    GLN A 256      101.18    -56.79                                   
REMARK 500    HIS A 264       52.42   -103.54                                   
REMARK 500    SER A 279       87.68     54.36                                   
REMARK 500    ASN A 283        0.30    -66.09                                   
REMARK 500    SER A 285     -176.13    -59.61                                   
REMARK 500    PHE A 296      -31.05   -179.03                                   
REMARK 500    PRO A 317     -167.64    -79.33                                   
REMARK 500    MET A 318      -72.63    -90.49                                   
REMARK 500    THR A 321       38.50    -76.86                                   
REMARK 500    ASP A 327      123.28    -39.43                                   
REMARK 500    VAL A 331      137.77   -173.68                                   
REMARK 500    PRO A 341     -176.58    -68.75                                   
REMARK 500    GLU A 344     -100.50   -123.24                                   
REMARK 500    MET A 351       75.68     43.23                                   
REMARK 500    ASN A 352       14.62     39.13                                   
REMARK 500    PHE A 355      -76.31   -144.20                                   
REMARK 500    GLU A 366       -8.63     61.23                                   
REMARK 500    ASN A 367      170.93    -55.75                                   
REMARK 500    SER A 369       15.61   -149.63                                   
REMARK 500    ARG A 381       64.64     65.29                                   
REMARK 500    SER A 397      -19.34    -47.68                                   
REMARK 500    ASP A 398      -92.52   -115.90                                   
REMARK 500    PRO A 413      158.28    -40.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     166 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EXZ   RELATED DB: PDB                                   
REMARK 900 THE FREE FORM OF SCF                                                 
REMARK 900 RELATED ID: 2EC8   RELATED DB: PDB                                   
REMARK 900 THE FREE FORM OF THE SAME PROTEIN                                    
DBREF  2E9W A   26   514  UNP    P10721   KIT_HUMAN       26    514             
DBREF  2E9W B   26   514  UNP    P10721   KIT_HUMAN       26    514             
DBREF  2E9W C    1   141  UNP    P21583   SCF_HUMAN       26    166             
DBREF  2E9W D    1   141  UNP    P21583   SCF_HUMAN       26    166             
SEQADV 2E9W SER A  130  UNP  P10721    ASN   130 ENGINEERED                     
SEQADV 2E9W SER A  145  UNP  P10721    ASN   145 ENGINEERED                     
SEQADV 2E9W SER B  130  UNP  P10721    ASN   130 ENGINEERED                     
SEQADV 2E9W SER B  145  UNP  P10721    ASN   145 ENGINEERED                     
SEQRES   1 A  489  GLN PRO SER VAL SER PRO GLY GLU PRO SER PRO PRO SER          
SEQRES   2 A  489  ILE HIS PRO GLY LYS SER ASP LEU ILE VAL ARG VAL GLY          
SEQRES   3 A  489  ASP GLU ILE ARG LEU LEU CYS THR ASP PRO GLY PHE VAL          
SEQRES   4 A  489  LYS TRP THR PHE GLU ILE LEU ASP GLU THR ASN GLU ASN          
SEQRES   5 A  489  LYS GLN ASN GLU TRP ILE THR GLU LYS ALA GLU ALA THR          
SEQRES   6 A  489  ASN THR GLY LYS TYR THR CYS THR ASN LYS HIS GLY LEU          
SEQRES   7 A  489  SER ASN SER ILE TYR VAL PHE VAL ARG ASP PRO ALA LYS          
SEQRES   8 A  489  LEU PHE LEU VAL ASP ARG SER LEU TYR GLY LYS GLU ASP          
SEQRES   9 A  489  SER ASP THR LEU VAL ARG CYS PRO LEU THR ASP PRO GLU          
SEQRES  10 A  489  VAL THR SER TYR SER LEU LYS GLY CYS GLN GLY LYS PRO          
SEQRES  11 A  489  LEU PRO LYS ASP LEU ARG PHE ILE PRO ASP PRO LYS ALA          
SEQRES  12 A  489  GLY ILE MET ILE LYS SER VAL LYS ARG ALA TYR HIS ARG          
SEQRES  13 A  489  LEU CYS LEU HIS CYS SER VAL ASP GLN GLU GLY LYS SER          
SEQRES  14 A  489  VAL LEU SER GLU LYS PHE ILE LEU LYS VAL ARG PRO ALA          
SEQRES  15 A  489  PHE LYS ALA VAL PRO VAL VAL SER VAL SER LYS ALA SER          
SEQRES  16 A  489  TYR LEU LEU ARG GLU GLY GLU GLU PHE THR VAL THR CYS          
SEQRES  17 A  489  THR ILE LYS ASP VAL SER SER SER VAL TYR SER THR TRP          
SEQRES  18 A  489  LYS ARG GLU ASN SER GLN THR LYS LEU GLN GLU LYS TYR          
SEQRES  19 A  489  ASN SER TRP HIS HIS GLY ASP PHE ASN TYR GLU ARG GLN          
SEQRES  20 A  489  ALA THR LEU THR ILE SER SER ALA ARG VAL ASN ASP SER          
SEQRES  21 A  489  GLY VAL PHE MET CYS TYR ALA ASN ASN THR PHE GLY SER          
SEQRES  22 A  489  ALA ASN VAL THR THR THR LEU GLU VAL VAL ASP LYS GLY          
SEQRES  23 A  489  PHE ILE ASN ILE PHE PRO MET ILE ASN THR THR VAL PHE          
SEQRES  24 A  489  VAL ASN ASP GLY GLU ASN VAL ASP LEU ILE VAL GLU TYR          
SEQRES  25 A  489  GLU ALA PHE PRO LYS PRO GLU HIS GLN GLN TRP ILE TYR          
SEQRES  26 A  489  MET ASN ARG THR PHE THR ASP LYS TRP GLU ASP TYR PRO          
SEQRES  27 A  489  LYS SER GLU ASN GLU SER ASN ILE ARG TYR VAL SER GLU          
SEQRES  28 A  489  LEU HIS LEU THR ARG LEU LYS GLY THR GLU GLY GLY THR          
SEQRES  29 A  489  TYR THR PHE LEU VAL SER ASN SER ASP VAL ASN ALA ALA          
SEQRES  30 A  489  ILE ALA PHE ASN VAL TYR VAL ASN THR LYS PRO GLU ILE          
SEQRES  31 A  489  LEU THR TYR ASP ARG LEU VAL ASN GLY MET LEU GLN CYS          
SEQRES  32 A  489  VAL ALA ALA GLY PHE PRO GLU PRO THR ILE ASP TRP TYR          
SEQRES  33 A  489  PHE CYS PRO GLY THR GLU GLN ARG CYS SER ALA SER VAL          
SEQRES  34 A  489  LEU PRO VAL ASP VAL GLN THR LEU ASN SER SER GLY PRO          
SEQRES  35 A  489  PRO PHE GLY LYS LEU VAL VAL GLN SER SER ILE ASP SER          
SEQRES  36 A  489  SER ALA PHE LYS HIS ASN GLY THR VAL GLU CYS LYS ALA          
SEQRES  37 A  489  TYR ASN ASP VAL GLY LYS THR SER ALA TYR PHE ASN PHE          
SEQRES  38 A  489  ALA PHE LYS GLY ASN ASN LYS GLU                              
SEQRES   1 B  489  GLN PRO SER VAL SER PRO GLY GLU PRO SER PRO PRO SER          
SEQRES   2 B  489  ILE HIS PRO GLY LYS SER ASP LEU ILE VAL ARG VAL GLY          
SEQRES   3 B  489  ASP GLU ILE ARG LEU LEU CYS THR ASP PRO GLY PHE VAL          
SEQRES   4 B  489  LYS TRP THR PHE GLU ILE LEU ASP GLU THR ASN GLU ASN          
SEQRES   5 B  489  LYS GLN ASN GLU TRP ILE THR GLU LYS ALA GLU ALA THR          
SEQRES   6 B  489  ASN THR GLY LYS TYR THR CYS THR ASN LYS HIS GLY LEU          
SEQRES   7 B  489  SER ASN SER ILE TYR VAL PHE VAL ARG ASP PRO ALA LYS          
SEQRES   8 B  489  LEU PHE LEU VAL ASP ARG SER LEU TYR GLY LYS GLU ASP          
SEQRES   9 B  489  SER ASP THR LEU VAL ARG CYS PRO LEU THR ASP PRO GLU          
SEQRES  10 B  489  VAL THR SER TYR SER LEU LYS GLY CYS GLN GLY LYS PRO          
SEQRES  11 B  489  LEU PRO LYS ASP LEU ARG PHE ILE PRO ASP PRO LYS ALA          
SEQRES  12 B  489  GLY ILE MET ILE LYS SER VAL LYS ARG ALA TYR HIS ARG          
SEQRES  13 B  489  LEU CYS LEU HIS CYS SER VAL ASP GLN GLU GLY LYS SER          
SEQRES  14 B  489  VAL LEU SER GLU LYS PHE ILE LEU LYS VAL ARG PRO ALA          
SEQRES  15 B  489  PHE LYS ALA VAL PRO VAL VAL SER VAL SER LYS ALA SER          
SEQRES  16 B  489  TYR LEU LEU ARG GLU GLY GLU GLU PHE THR VAL THR CYS          
SEQRES  17 B  489  THR ILE LYS ASP VAL SER SER SER VAL TYR SER THR TRP          
SEQRES  18 B  489  LYS ARG GLU ASN SER GLN THR LYS LEU GLN GLU LYS TYR          
SEQRES  19 B  489  ASN SER TRP HIS HIS GLY ASP PHE ASN TYR GLU ARG GLN          
SEQRES  20 B  489  ALA THR LEU THR ILE SER SER ALA ARG VAL ASN ASP SER          
SEQRES  21 B  489  GLY VAL PHE MET CYS TYR ALA ASN ASN THR PHE GLY SER          
SEQRES  22 B  489  ALA ASN VAL THR THR THR LEU GLU VAL VAL ASP LYS GLY          
SEQRES  23 B  489  PHE ILE ASN ILE PHE PRO MET ILE ASN THR THR VAL PHE          
SEQRES  24 B  489  VAL ASN ASP GLY GLU ASN VAL ASP LEU ILE VAL GLU TYR          
SEQRES  25 B  489  GLU ALA PHE PRO LYS PRO GLU HIS GLN GLN TRP ILE TYR          
SEQRES  26 B  489  MET ASN ARG THR PHE THR ASP LYS TRP GLU ASP TYR PRO          
SEQRES  27 B  489  LYS SER GLU ASN GLU SER ASN ILE ARG TYR VAL SER GLU          
SEQRES  28 B  489  LEU HIS LEU THR ARG LEU LYS GLY THR GLU GLY GLY THR          
SEQRES  29 B  489  TYR THR PHE LEU VAL SER ASN SER ASP VAL ASN ALA ALA          
SEQRES  30 B  489  ILE ALA PHE ASN VAL TYR VAL ASN THR LYS PRO GLU ILE          
SEQRES  31 B  489  LEU THR TYR ASP ARG LEU VAL ASN GLY MET LEU GLN CYS          
SEQRES  32 B  489  VAL ALA ALA GLY PHE PRO GLU PRO THR ILE ASP TRP TYR          
SEQRES  33 B  489  PHE CYS PRO GLY THR GLU GLN ARG CYS SER ALA SER VAL          
SEQRES  34 B  489  LEU PRO VAL ASP VAL GLN THR LEU ASN SER SER GLY PRO          
SEQRES  35 B  489  PRO PHE GLY LYS LEU VAL VAL GLN SER SER ILE ASP SER          
SEQRES  36 B  489  SER ALA PHE LYS HIS ASN GLY THR VAL GLU CYS LYS ALA          
SEQRES  37 B  489  TYR ASN ASP VAL GLY LYS THR SER ALA TYR PHE ASN PHE          
SEQRES  38 B  489  ALA PHE LYS GLY ASN ASN LYS GLU                              
SEQRES   1 C  141  GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS          
SEQRES   2 C  141  ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR          
SEQRES   3 C  141  MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU          
SEQRES   4 C  141  PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU          
SEQRES   5 C  141  SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN          
SEQRES   6 C  141  ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS          
SEQRES   7 C  141  LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS          
SEQRES   8 C  141  GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER          
SEQRES   9 C  141  PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG          
SEQRES  10 C  141  ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL          
SEQRES  11 C  141  VAL ALA SER GLU THR SER ASP CYS VAL VAL SER                  
SEQRES   1 D  141  GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS          
SEQRES   2 D  141  ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR          
SEQRES   3 D  141  MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU          
SEQRES   4 D  141  PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU          
SEQRES   5 D  141  SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN          
SEQRES   6 D  141  ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS          
SEQRES   7 D  141  LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS          
SEQRES   8 D  141  GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER          
SEQRES   9 D  141  PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG          
SEQRES  10 D  141  ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL          
SEQRES  11 D  141  VAL ALA SER GLU THR SER ASP CYS VAL VAL SER                  
MODRES 2E9W ASN A  283  ASN  GLYCOSYLATION SITE                                 
MODRES 2E9W ASN A  300  ASN  GLYCOSYLATION SITE                                 
MODRES 2E9W ASN A  352  ASN  GLYCOSYLATION SITE                                 
MODRES 2E9W ASN B  293  ASN  GLYCOSYLATION SITE                                 
MODRES 2E9W ASN B  300  ASN  GLYCOSYLATION SITE                                 
MODRES 2E9W ASN B  352  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 700      14                                                       
HET    NAG  A 750      14                                                       
HET    NAG  A 800      14                                                       
HET    NAG  B 850      14                                                       
HET    NAG  B 900      14                                                       
HET    NAG  B 950      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   5  NAG    6(C8 H15 N O6)                                               
HELIX    1   1 GLU A   88  THR A   92  5                                   5    
HELIX    2   2 LYS A  176  HIS A  180  5                                   5    
HELIX    3   3 ARG A  281  SER A  285  5                                   5    
HELIX    4   4 LYS B  176  HIS B  180  5                                   5    
HELIX    5   5 ARG B  281  SER B  285  5                                   5    
HELIX    6   6 CYS C    4  VAL C    8  5                                   5    
HELIX    7   7 THR C    9  LYS C   13  5                                   5    
HELIX    8   8 ASP C   14  ASN C   21  1                                   8    
HELIX    9   9 TRP C   44  LEU C   60  1                                  17    
HELIX   10  10 ASP C   61  PHE C   63  5                                   3    
HELIX   11  11 SER C   71  SER C   94  1                                  24    
HELIX   12  12 THR C  111  ALA C  125  1                                  15    
HELIX   13  13 CYS D    4  VAL D    8  5                                   5    
HELIX   14  14 ASP D   14  ASN D   21  1                                   8    
HELIX   15  15 TRP D   44  LEU D   60  1                                  17    
HELIX   16  16 ASP D   61  PHE D   63  5                                   3    
HELIX   17  17 SER D   71  SER D   94  1                                  24    
HELIX   18  18 THR D  111  ALA D  125  1                                  15    
SHEET    1   A 3 SER A  38  HIS A  40  0                                        
SHEET    2   A 3 ILE A  54  THR A  59 -1  O  THR A  59   N  SER A  38           
SHEET    3   A 3 GLU A  81  THR A  84 -1  O  TRP A  82   N  LEU A  56           
SHEET    1   B 5 ASP A  45  ARG A  49  0                                        
SHEET    2   B 5 SER A 104  ARG A 112  1  O  PHE A 110   N  VAL A  48           
SHEET    3   B 5 GLY A  93  THR A  98 -1  N  CYS A  97   O  ASN A 105           
SHEET    4   B 5 LYS A  65  GLU A  69 -1  N  THR A  67   O  THR A  96           
SHEET    5   B 5 THR A  74  ASN A  77 -1  O  ASN A  77   N  TRP A  66           
SHEET    1   C 2 TYR A 125  LYS A 127  0                                        
SHEET    2   C 2 LYS A 203  ARG A 205  1  O  ARG A 205   N  GLY A 126           
SHEET    1   D 3 SER A 147  GLY A 150  0                                        
SHEET    2   D 3 LEU A 184  GLN A 190 -1  O  SER A 187   N  SER A 147           
SHEET    3   D 3 LYS A 193  PHE A 200 -1  O  VAL A 195   N  VAL A 188           
SHEET    1   E 4 VAL A 213  VAL A 216  0                                        
SHEET    2   E 4 PHE A 229  LYS A 236 -1  O  LYS A 236   N  VAL A 213           
SHEET    3   E 4 GLU A 270  ILE A 277 -1  O  ILE A 277   N  PHE A 229           
SHEET    4   E 4 GLU A 257  TRP A 262 -1  N  LYS A 258   O  THR A 274           
SHEET    1   F 2 LEU A 223  ARG A 224  0                                        
SHEET    2   F 2 VAL A 307  VAL A 308  1  O  VAL A 308   N  LEU A 223           
SHEET    1   G 3 SER A 244  ARG A 248  0                                        
SHEET    2   G 3 GLY A 286  ASN A 294 -1  O  MET A 289   N  LYS A 247           
SHEET    3   G 3 GLY A 297  LEU A 305 -1  O  VAL A 301   N  CYS A 290           
SHEET    1   H 4 PHE A 312  PHE A 316  0                                        
SHEET    2   H 4 VAL A 331  PHE A 340 -1  O  GLU A 336   N  PHE A 316           
SHEET    3   H 4 ARG A 372  LEU A 379 -1  O  TYR A 373   N  TYR A 337           
SHEET    4   H 4 TRP A 359  PRO A 363 -1  N  GLU A 360   O  GLU A 376           
SHEET    1   I 5 THR A 322  ASN A 326  0                                        
SHEET    2   I 5 ASN A 400  ASP A 419  1  O  TYR A 408   N  VAL A 323           
SHEET    3   I 5 GLY A 388  SER A 395 -1  N  TYR A 390   O  PHE A 405           
SHEET    4   I 5 GLN A 347  TYR A 350 -1  N  ILE A 349   O  THR A 391           
SHEET    5   I 5 ARG A 353  THR A 354 -1  O  ARG A 353   N  TYR A 350           
SHEET    1   J 4 THR A 322  ASN A 326  0                                        
SHEET    2   J 4 ASN A 400  ASP A 419  1  O  TYR A 408   N  VAL A 323           
SHEET    3   J 4 MET A 425  PHE A 433 -1  O  VAL A 429   N  THR A 417           
SHEET    4   J 4 LEU A 472  ASP A 479 -1  O  VAL A 474   N  ALA A 430           
SHEET    1   K 3 THR A 437  TRP A 440  0                                        
SHEET    2   K 3 GLU A 490  ASN A 495 -1  O  TYR A 494   N  THR A 437           
SHEET    3   K 3 GLY A 498  TYR A 503 -1  O  ALA A 502   N  CYS A 491           
SHEET    1   L 3 ILE B  39  HIS B  40  0                                        
SHEET    2   L 3 ILE B  54  CYS B  58 -1  O  LEU B  57   N  HIS B  40           
SHEET    3   L 3 GLU B  81  THR B  84 -1  O  TRP B  82   N  LEU B  56           
SHEET    1   M 5 ASP B  45  ARG B  49  0                                        
SHEET    2   M 5 SER B 104  ARG B 112  1  O  PHE B 110   N  VAL B  48           
SHEET    3   M 5 GLY B  93  THR B  98 -1  N  CYS B  97   O  ASN B 105           
SHEET    4   M 5 LYS B  65  PHE B  68 -1  N  THR B  67   O  THR B  96           
SHEET    5   M 5 ASN B  75  ASN B  77 -1  O  ASN B  75   N  PHE B  68           
SHEET    1   N 2 TYR B 125  LYS B 127  0                                        
SHEET    2   N 2 LYS B 203  ARG B 205  1  O  ARG B 205   N  GLY B 126           
SHEET    1   O 3 SER B 130  VAL B 134  0                                        
SHEET    2   O 3 ILE B 170  VAL B 175 -1  O  ILE B 170   N  VAL B 134           
SHEET    3   O 3 PHE B 162  PRO B 164 -1  N  ILE B 163   O  MET B 171           
SHEET    1   P 3 SER B 147  LYS B 149  0                                        
SHEET    2   P 3 LEU B 184  GLN B 190 -1  O  SER B 187   N  SER B 147           
SHEET    3   P 3 LYS B 193  PHE B 200 -1  O  VAL B 195   N  VAL B 188           
SHEET    1   Q 4 VAL B 213  VAL B 216  0                                        
SHEET    2   Q 4 PHE B 229  LYS B 236 -1  O  THR B 234   N  SER B 215           
SHEET    3   Q 4 GLU B 270  ILE B 277 -1  O  ILE B 277   N  PHE B 229           
SHEET    4   Q 4 GLU B 257  TRP B 262 -1  N  ASN B 260   O  GLN B 272           
SHEET    1   R 2 SER B 220  ARG B 224  0                                        
SHEET    2   R 2 THR B 304  VAL B 308  1  O  THR B 304   N  TYR B 221           
SHEET    1   S 3 TYR B 243  ARG B 248  0                                        
SHEET    2   S 3 PHE B 288  ASN B 294 -1  O  ASN B 293   N  TYR B 243           
SHEET    3   S 3 GLY B 297  ALA B 299 -1  O  GLY B 297   N  ASN B 294           
SHEET    1   T 4 PHE B 312  PHE B 316  0                                        
SHEET    2   T 4 VAL B 331  PHE B 340 -1  O  PHE B 340   N  PHE B 312           
SHEET    3   T 4 ARG B 372  LEU B 379 -1  O  TYR B 373   N  TYR B 337           
SHEET    4   T 4 ASP B 361  PRO B 363 -1  N  TYR B 362   O  VAL B 374           
SHEET    1   U 2 THR B 322  PHE B 324  0                                        
SHEET    2   U 2 ASN B 406  TYR B 408  1  O  ASN B 406   N  VAL B 323           
SHEET    1   V 4 ARG B 353  THR B 354  0                                        
SHEET    2   V 4 GLN B 346  TYR B 350 -1  N  TYR B 350   O  ARG B 353           
SHEET    3   V 4 TYR B 390  SER B 395 -1  O  THR B 391   N  ILE B 349           
SHEET    4   V 4 ASN B 400  ALA B 404 -1  O  ILE B 403   N  PHE B 392           
SHEET    1   W 4 THR B 411  THR B 417  0                                        
SHEET    2   W 4 MET B 425  PHE B 433 -1  O  PHE B 433   N  THR B 411           
SHEET    3   W 4 LEU B 472  ASP B 479 -1  O  VAL B 474   N  ALA B 430           
SHEET    4   W 4 GLN B 460  THR B 461 -1  N  THR B 461   O  GLN B 475           
SHEET    1   X 3 THR B 437  TYR B 441  0                                        
SHEET    2   X 3 GLU B 490  TYR B 494 -1  O  TYR B 494   N  THR B 437           
SHEET    3   X 3 LYS B 499  TYR B 503 -1  O  ALA B 502   N  CYS B 491           
SHEET    1   Y 2 ILE C  28  LEU C  30  0                                        
SHEET    2   Y 2 ARG C 108  PHE C 110 -1  O  PHE C 110   N  ILE C  28           
SHEET    1   Z 2 ILE D  28  LEU D  30  0                                        
SHEET    2   Z 2 ARG D 108  PHE D 110 -1  O  ARG D 108   N  LEU D  30           
SSBOND   1 CYS A   58    CYS A   97                          1555   1555  2.03  
SSBOND   2 CYS A  136    CYS A  186                          1555   1555  2.02  
SSBOND   3 CYS A  151    CYS A  183                          1555   1555  2.03  
SSBOND   4 CYS A  233    CYS A  290                          1555   1555  2.03  
SSBOND   5 CYS A  428    CYS A  491                          1555   1555  2.03  
SSBOND   6 CYS B   58    CYS B   97                          1555   1555  2.03  
SSBOND   7 CYS B  136    CYS B  186                          1555   1555  2.01  
SSBOND   8 CYS B  151    CYS B  183                          1555   1555  2.03  
SSBOND   9 CYS B  233    CYS B  290                          1555   1555  2.03  
SSBOND  10 CYS B  428    CYS B  491                          1555   1555  2.03  
SSBOND  11 CYS C    4    CYS C   89                          1555   1555  2.03  
SSBOND  12 CYS C   43    CYS C  138                          1555   1555  2.03  
SSBOND  13 CYS D    4    CYS D   89                          1555   1555  2.03  
LINK         ND2 ASN A 283                 C1  NAG A 700     1555   1555  1.45  
LINK         ND2 ASN A 300                 C1  NAG A 750     1555   1555  1.46  
LINK         ND2 ASN A 352                 C1  NAG A 800     1555   1555  1.46  
LINK         ND2 ASN B 293                 C1  NAG B 850     1555   1555  1.46  
LINK         ND2 ASN B 300                 C1  NAG B 900     1555   1555  1.45  
LINK         ND2 ASN B 352                 C1  NAG B 950     1555   1555  1.45  
CISPEP   1 HIS A   40    PRO A   41          0        -0.19                     
CISPEP   2 PHE A  340    PRO A  341          0        -0.41                     
CISPEP   3 PHE A  433    PRO A  434          0        -0.17                     
CISPEP   4 HIS B   40    PRO B   41          0         0.53                     
CISPEP   5 PHE B  340    PRO B  341          0        -0.07                     
CISPEP   6 PHE B  433    PRO B  434          0        -0.18                     
CISPEP   7 LEU C   39    PRO C   40          0        -0.13                     
CISPEP   8 LEU D   39    PRO D   40          0         0.03                     
CRYST1  269.477   52.072  189.791  90.00 108.00  90.00 C 1 2 1       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      0.003711  0.000000  0.001206        0.00000                         
SCALE2      0.000000  0.019204  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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