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Database: PDB
Entry: 3MJG
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HEADER    HORMONE/TRANSFERASE                     12-APR-10   3MJG              
TITLE     THE STRUCTURE OF A PLATELET DERIVED GROWTH FACTOR RECEPTOR COMPLEX    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-DERIVED GROWTH FACTOR SUBUNIT B;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 21-185;                                       
COMPND   5 SYNONYM: PDGF SUBUNIT B, PLATELET-DERIVED GROWTH FACTOR B CHAIN,     
COMPND   6 PLATELET-DERIVED GROWTH FACTOR BETA POLYPEPTIDE, PDGF-2, PROTO-      
COMPND   7 ONCOGENE C-SIS;                                                      
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BETA-TYPE PLATELET-DERIVED GROWTH FACTOR RECEPTOR;         
COMPND  11 CHAIN: X, Y;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 33-314;                                       
COMPND  13 SYNONYM: PDGF-R-BETA, CD140 ANTIGEN-LIKE FAMILY MEMBER B;            
COMPND  14 EC: 2.7.10.1;                                                        
COMPND  15 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: PDGF2, PDGFB, SIS;                                             
SOURCE   6 EXPRESSION_SYSTEM:  HOMO SAPIENS;                                    
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: EMBRYONIC KIDNEY-293 CELLS;             
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: PDGFRB;                                                        
SOURCE  14 EXPRESSION_SYSTEM:  HOMO SAPIENS;                                    
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: EMBRYONIC KIDNEY-293 CELLS              
KEYWDS    PROTEIN-PROTEIN COMPLEX, GROWTH FACTOR-RECEPTOR COMPLEX, TRANSFERASE- 
KEYWDS   2 HORMONE COMPLEX, HORMONE-TRANSFERASE COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.R.SHIM,X.HE                                                       
REVDAT   3   08-NOV-17 3MJG    1       SOURCE                                   
REVDAT   2   18-AUG-10 3MJG    1       JRNL                                     
REVDAT   1   16-JUN-10 3MJG    0                                                
JRNL        AUTH   A.H.SHIM,H.LIU,P.J.FOCIA,X.CHEN,P.C.LIN,X.HE                 
JRNL        TITL   STRUCTURES OF A PLATELET-DERIVED GROWTH FACTOR/PROPEPTIDE    
JRNL        TITL 2 COMPLEX AND A PLATELET-DERIVED GROWTH FACTOR/RECEPTOR        
JRNL        TITL 3 COMPLEX.                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 11307 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20534510                                                     
JRNL        DOI    10.1073/PNAS.1000806107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.24                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2835260.480                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 54642                          
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) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2764                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8466                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 439                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5888                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 196                                     
REMARK   3   SOLVENT ATOMS            : 1170                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.52000                                             
REMARK   3    B22 (A**2) : 11.67000                                             
REMARK   3    B33 (A**2) : -6.14000                                             
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) : 0.33                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.43                            
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) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.46                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 27.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.190                           
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        : 0.27                                                 
REMARK   3   BSOL        : 61.54                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 3MJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUN-08                          
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               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9786                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54767                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
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 ENTRIES 1PDG, 1FLT                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.84 M (NH4)2HPO4, 0.1 M IMIDAZOLE, PH   
REMARK 280  8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       39.23500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.07500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       58.41000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.07500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       58.41000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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, X, Y                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Y                                     
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       39.23500            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000     -116.82000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000       67.07500            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X                               
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   -60                                                      
REMARK 465     GLY A   -59                                                      
REMARK 465     ASP A   -58                                                      
REMARK 465     PRO A   -57                                                      
REMARK 465     ILE A   -56                                                      
REMARK 465     PRO A   -55                                                      
REMARK 465     GLU A   -54                                                      
REMARK 465     GLU A   -53                                                      
REMARK 465     LEU A   -52                                                      
REMARK 465     TYR A   -51                                                      
REMARK 465     GLU A   -50                                                      
REMARK 465     MET A   -49                                                      
REMARK 465     LEU A   -48                                                      
REMARK 465     SER A   -47                                                      
REMARK 465     ASP A   -46                                                      
REMARK 465     HIS A   -45                                                      
REMARK 465     SER A   -44                                                      
REMARK 465     ILE A   -43                                                      
REMARK 465     ARG A   -42                                                      
REMARK 465     SER A   -41                                                      
REMARK 465     PHE A   -40                                                      
REMARK 465     ASP A   -39                                                      
REMARK 465     ASP A   -38                                                      
REMARK 465     LEU A   -37                                                      
REMARK 465     GLN A   -36                                                      
REMARK 465     ARG A   -35                                                      
REMARK 465     LEU A   -34                                                      
REMARK 465     LEU A   -33                                                      
REMARK 465     HIS A   -32                                                      
REMARK 465     GLY A   -31                                                      
REMARK 465     ASP A   -30                                                      
REMARK 465     PRO A   -29                                                      
REMARK 465     GLY A   -28                                                      
REMARK 465     GLU A   -27                                                      
REMARK 465     GLU A   -26                                                      
REMARK 465     ASP A   -25                                                      
REMARK 465     GLY A   -24                                                      
REMARK 465     ALA A   -23                                                      
REMARK 465     GLU A   -22                                                      
REMARK 465     LEU A   -21                                                      
REMARK 465     ASP A   -20                                                      
REMARK 465     LEU A   -19                                                      
REMARK 465     ASN A   -18                                                      
REMARK 465     MET A   -17                                                      
REMARK 465     THR A   -16                                                      
REMARK 465     ARG A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     GLU A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     SER A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ARG A    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ALA A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     HIS A   106                                                      
REMARK 465     HIS A   107                                                      
REMARK 465     HIS A   108                                                      
REMARK 465     HIS A   109                                                      
REMARK 465     HIS A   110                                                      
REMARK 465     HIS A   111                                                      
REMARK 465     GLU B   -60                                                      
REMARK 465     GLY B   -59                                                      
REMARK 465     ASP B   -58                                                      
REMARK 465     PRO B   -57                                                      
REMARK 465     ILE B   -56                                                      
REMARK 465     PRO B   -55                                                      
REMARK 465     GLU B   -54                                                      
REMARK 465     GLU B   -53                                                      
REMARK 465     LEU B   -52                                                      
REMARK 465     TYR B   -51                                                      
REMARK 465     GLU B   -50                                                      
REMARK 465     MET B   -49                                                      
REMARK 465     LEU B   -48                                                      
REMARK 465     SER B   -47                                                      
REMARK 465     ASP B   -46                                                      
REMARK 465     HIS B   -45                                                      
REMARK 465     SER B   -44                                                      
REMARK 465     ILE B   -43                                                      
REMARK 465     ARG B   -42                                                      
REMARK 465     SER B   -41                                                      
REMARK 465     PHE B   -40                                                      
REMARK 465     ASP B   -39                                                      
REMARK 465     ASP B   -38                                                      
REMARK 465     LEU B   -37                                                      
REMARK 465     GLN B   -36                                                      
REMARK 465     ARG B   -35                                                      
REMARK 465     LEU B   -34                                                      
REMARK 465     LEU B   -33                                                      
REMARK 465     HIS B   -32                                                      
REMARK 465     GLY B   -31                                                      
REMARK 465     ASP B   -30                                                      
REMARK 465     PRO B   -29                                                      
REMARK 465     GLY B   -28                                                      
REMARK 465     GLU B   -27                                                      
REMARK 465     GLU B   -26                                                      
REMARK 465     ASP B   -25                                                      
REMARK 465     GLY B   -24                                                      
REMARK 465     ALA B   -23                                                      
REMARK 465     GLU B   -22                                                      
REMARK 465     LEU B   -21                                                      
REMARK 465     ASP B   -20                                                      
REMARK 465     LEU B   -19                                                      
REMARK 465     ASN B   -18                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     THR B   -16                                                      
REMARK 465     ARG B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     SER B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     GLU B    -9                                                      
REMARK 465     LEU B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     SER B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     ALA B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     ARG B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ALA B   103                                                      
REMARK 465     ALA B   104                                                      
REMARK 465     HIS B   105                                                      
REMARK 465     HIS B   106                                                      
REMARK 465     HIS B   107                                                      
REMARK 465     HIS B   108                                                      
REMARK 465     HIS B   109                                                      
REMARK 465     HIS B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     SER X   105                                                      
REMARK 465     ARG X   106                                                      
REMARK 465     GLY X   107                                                      
REMARK 465     LEU X   108                                                      
REMARK 465     GLU X   109                                                      
REMARK 465     THR X   110                                                      
REMARK 465     SER X   313                                                      
REMARK 465     GLY X   314                                                      
REMARK 465     HIS X   315                                                      
REMARK 465     HIS X   316                                                      
REMARK 465     HIS X   317                                                      
REMARK 465     HIS X   318                                                      
REMARK 465     HIS X   319                                                      
REMARK 465     HIS X   320                                                      
REMARK 465     HIS X   321                                                      
REMARK 465     LEU Y    33                                                      
REMARK 465     SER Y   105                                                      
REMARK 465     ARG Y   106                                                      
REMARK 465     GLY Y   107                                                      
REMARK 465     LEU Y   108                                                      
REMARK 465     GLU Y   109                                                      
REMARK 465     THR Y   110                                                      
REMARK 465     SER Y   313                                                      
REMARK 465     GLY Y   314                                                      
REMARK 465     HIS Y   315                                                      
REMARK 465     HIS Y   316                                                      
REMARK 465     HIS Y   317                                                      
REMARK 465     HIS Y   318                                                      
REMARK 465     HIS Y   319                                                      
REMARK 465     HIS Y   320                                                      
REMARK 465     HIS Y   321                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN X    45     C1   NDG X     1              1.45            
REMARK 500   OE2  GLU X    97     NH1  ARG X   115              2.14            
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    ASP A  31      109.73   -167.98                                   
REMARK 500    ASN A  36       47.48    -85.57                                   
REMARK 500    VAL A  78       95.88   -161.35                                   
REMARK 500    ARG A  79       70.12     64.40                                   
REMARK 500    LYS A  80      -23.93     62.08                                   
REMARK 500    ASP B  31       98.24   -167.44                                   
REMARK 500    ALA B  35       38.50   -141.89                                   
REMARK 500    ASN B  54       -8.20    -56.08                                   
REMARK 500    SER X  47       -3.68     62.96                                   
REMARK 500    PRO X  59      159.62    -43.10                                   
REMARK 500    SER X  66      -13.03     67.51                                   
REMARK 500    PRO X  70      105.39    -50.49                                   
REMARK 500    PRO X 148       47.26    -74.44                                   
REMARK 500    LYS X 163      -73.72    -23.65                                   
REMARK 500    SER X 212     -176.65   -178.38                                   
REMARK 500    GLN X 222      129.44   -175.24                                   
REMARK 500    ARG X 251        0.13    -51.35                                   
REMARK 500    LYS X 252      -80.20    -76.20                                   
REMARK 500    SER X 254       87.11     54.86                                   
REMARK 500    ARG X 256      130.67    -34.91                                   
REMARK 500    MET X 268      -97.19    -69.16                                   
REMARK 500    LEU X 283     -165.76    -79.58                                   
REMARK 500    GLU X 284      -29.20     65.60                                   
REMARK 500    SER Y  47        5.52     53.01                                   
REMARK 500    CYS Y  54      112.49   -170.13                                   
REMARK 500    MET Y  65       38.24     78.59                                   
REMARK 500    GLN Y  71     -167.98   -105.33                                   
REMARK 500    GLU Y  72       79.17   -160.54                                   
REMARK 500    ASN Y  89       76.14     56.44                                   
REMARK 500    THR Y 101     -151.14   -102.68                                   
REMARK 500    VAL Y 120       79.16   -111.90                                   
REMARK 500    PRO Y 121       91.13    -46.23                                   
REMARK 500    ASP Y 131      157.28    -49.80                                   
REMARK 500    PRO Y 148       48.17    -55.89                                   
REMARK 500    HIS Y 175      -15.53    -48.25                                   
REMARK 500    ASP Y 185       87.42    -68.55                                   
REMARK 500    ASP Y 196        5.48   -160.05                                   
REMARK 500    SER Y 201     -174.10    -67.40                                   
REMARK 500    ASP Y 202     -171.41    -69.62                                   
REMARK 500    SER Y 212     -172.12   -177.22                                   
REMARK 500    GLN Y 222      126.22   -173.54                                   
REMARK 500    ARG Y 251       23.98    -76.08                                   
REMARK 500    LYS Y 252      -73.50    -91.08                                   
REMARK 500    LEU Y 265      -77.82    -67.54                                   
REMARK 500    MET Y 268      -73.82    -78.13                                   
REMARK 500    TYR Y 270      112.95    -38.99                                   
REMARK 500    ALA Y 281      105.89    -56.56                                   
REMARK 500    LEU Y 283     -159.99    -82.11                                   
REMARK 500    GLU Y 284      -26.78     59.93                                   
REMARK 500    ASN Y 298      -85.33   -106.11                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      52 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NDG X    1                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NDG X 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG X 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG Y 7                   
DBREF  3MJG A  -60   104  UNP    P01127   PDGFB_HUMAN     21    185             
DBREF  3MJG B  -60   104  UNP    P01127   PDGFB_HUMAN     21    185             
DBREF  3MJG X   33   314  UNP    P09619   PGFRB_HUMAN     33    314             
DBREF  3MJG Y   33   314  UNP    P09619   PGFRB_HUMAN     33    314             
SEQADV 3MJG HIS A  105  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  106  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  107  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  108  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  109  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  110  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS A  111  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  105  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  106  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  107  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  108  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  109  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  110  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS B  111  UNP  P01127              EXPRESSION TAG                 
SEQADV 3MJG HIS X  315  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  316  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  317  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  318  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  319  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  320  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS X  321  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  315  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  316  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  317  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  318  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  319  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  320  UNP  P09619              EXPRESSION TAG                 
SEQADV 3MJG HIS Y  321  UNP  P09619              EXPRESSION TAG                 
SEQRES   1 A  172  GLU GLY ASP PRO ILE PRO GLU GLU LEU TYR GLU MET LEU          
SEQRES   2 A  172  SER ASP HIS SER ILE ARG SER PHE ASP ASP LEU GLN ARG          
SEQRES   3 A  172  LEU LEU HIS GLY ASP PRO GLY GLU GLU ASP GLY ALA GLU          
SEQRES   4 A  172  LEU ASP LEU ASN MET THR ARG SER HIS SER GLY GLY GLU          
SEQRES   5 A  172  LEU GLU SER LEU ALA ARG GLY ARG ARG SER LEU GLY SER          
SEQRES   6 A  172  LEU THR ILE ALA GLU PRO ALA MET ILE ALA GLU CYS LYS          
SEQRES   7 A  172  THR ARG THR GLU VAL PHE GLU ILE SER ARG ARG LEU ILE          
SEQRES   8 A  172  ASP ARG THR ASN ALA ASN PHE LEU VAL TRP PRO PRO CYS          
SEQRES   9 A  172  VAL GLU VAL GLN ARG CYS SER GLY CYS CYS ASN ASN ARG          
SEQRES  10 A  172  ASN VAL GLN CYS ARG PRO THR GLN VAL GLN LEU ARG PRO          
SEQRES  11 A  172  VAL GLN VAL ARG LYS ILE GLU ILE VAL ARG LYS LYS PRO          
SEQRES  12 A  172  ILE PHE LYS LYS ALA THR VAL THR LEU GLU ASP HIS LEU          
SEQRES  13 A  172  ALA CYS LYS CYS GLU THR VAL ALA ALA HIS HIS HIS HIS          
SEQRES  14 A  172  HIS HIS HIS                                                  
SEQRES   1 B  172  GLU GLY ASP PRO ILE PRO GLU GLU LEU TYR GLU MET LEU          
SEQRES   2 B  172  SER ASP HIS SER ILE ARG SER PHE ASP ASP LEU GLN ARG          
SEQRES   3 B  172  LEU LEU HIS GLY ASP PRO GLY GLU GLU ASP GLY ALA GLU          
SEQRES   4 B  172  LEU ASP LEU ASN MET THR ARG SER HIS SER GLY GLY GLU          
SEQRES   5 B  172  LEU GLU SER LEU ALA ARG GLY ARG ARG SER LEU GLY SER          
SEQRES   6 B  172  LEU THR ILE ALA GLU PRO ALA MET ILE ALA GLU CYS LYS          
SEQRES   7 B  172  THR ARG THR GLU VAL PHE GLU ILE SER ARG ARG LEU ILE          
SEQRES   8 B  172  ASP ARG THR ASN ALA ASN PHE LEU VAL TRP PRO PRO CYS          
SEQRES   9 B  172  VAL GLU VAL GLN ARG CYS SER GLY CYS CYS ASN ASN ARG          
SEQRES  10 B  172  ASN VAL GLN CYS ARG PRO THR GLN VAL GLN LEU ARG PRO          
SEQRES  11 B  172  VAL GLN VAL ARG LYS ILE GLU ILE VAL ARG LYS LYS PRO          
SEQRES  12 B  172  ILE PHE LYS LYS ALA THR VAL THR LEU GLU ASP HIS LEU          
SEQRES  13 B  172  ALA CYS LYS CYS GLU THR VAL ALA ALA HIS HIS HIS HIS          
SEQRES  14 B  172  HIS HIS HIS                                                  
SEQRES   1 X  289  LEU VAL VAL THR PRO PRO GLY PRO GLU LEU VAL LEU ASN          
SEQRES   2 X  289  VAL SER SER THR PHE VAL LEU THR CYS SER GLY SER ALA          
SEQRES   3 X  289  PRO VAL VAL TRP GLU ARG MET SER GLN GLU PRO PRO GLN          
SEQRES   4 X  289  GLU MET ALA LYS ALA GLN ASP GLY THR PHE SER SER VAL          
SEQRES   5 X  289  LEU THR LEU THR ASN LEU THR GLY LEU ASP THR GLY GLU          
SEQRES   6 X  289  TYR PHE CYS THR HIS ASN ASP SER ARG GLY LEU GLU THR          
SEQRES   7 X  289  ASP GLU ARG LYS ARG LEU TYR ILE PHE VAL PRO ASP PRO          
SEQRES   8 X  289  THR VAL GLY PHE LEU PRO ASN ASP ALA GLU GLU LEU PHE          
SEQRES   9 X  289  ILE PHE LEU THR GLU ILE THR GLU ILE THR ILE PRO CYS          
SEQRES  10 X  289  ARG VAL THR ASP PRO GLN LEU VAL VAL THR LEU HIS GLU          
SEQRES  11 X  289  LYS LYS GLY ASP VAL ALA LEU PRO VAL PRO TYR ASP HIS          
SEQRES  12 X  289  GLN ARG GLY PHE SER GLY ILE PHE GLU ASP ARG SER TYR          
SEQRES  13 X  289  ILE CYS LYS THR THR ILE GLY ASP ARG GLU VAL ASP SER          
SEQRES  14 X  289  ASP ALA TYR TYR VAL TYR ARG LEU GLN VAL SER SER ILE          
SEQRES  15 X  289  ASN VAL SER VAL ASN ALA VAL GLN THR VAL VAL ARG GLN          
SEQRES  16 X  289  GLY GLU ASN ILE THR LEU MET CYS ILE VAL ILE GLY ASN          
SEQRES  17 X  289  GLU VAL VAL ASN PHE GLU TRP THR TYR PRO ARG LYS GLU          
SEQRES  18 X  289  SER GLY ARG LEU VAL GLU PRO VAL THR ASP PHE LEU LEU          
SEQRES  19 X  289  ASP MET PRO TYR HIS ILE ARG SER ILE LEU HIS ILE PRO          
SEQRES  20 X  289  SER ALA GLU LEU GLU ASP SER GLY THR TYR THR CYS ASN          
SEQRES  21 X  289  VAL THR GLU SER VAL ASN ASP HIS GLN ASP GLU LYS ALA          
SEQRES  22 X  289  ILE ASN ILE THR VAL VAL GLU SER GLY HIS HIS HIS HIS          
SEQRES  23 X  289  HIS HIS HIS                                                  
SEQRES   1 Y  289  LEU VAL VAL THR PRO PRO GLY PRO GLU LEU VAL LEU ASN          
SEQRES   2 Y  289  VAL SER SER THR PHE VAL LEU THR CYS SER GLY SER ALA          
SEQRES   3 Y  289  PRO VAL VAL TRP GLU ARG MET SER GLN GLU PRO PRO GLN          
SEQRES   4 Y  289  GLU MET ALA LYS ALA GLN ASP GLY THR PHE SER SER VAL          
SEQRES   5 Y  289  LEU THR LEU THR ASN LEU THR GLY LEU ASP THR GLY GLU          
SEQRES   6 Y  289  TYR PHE CYS THR HIS ASN ASP SER ARG GLY LEU GLU THR          
SEQRES   7 Y  289  ASP GLU ARG LYS ARG LEU TYR ILE PHE VAL PRO ASP PRO          
SEQRES   8 Y  289  THR VAL GLY PHE LEU PRO ASN ASP ALA GLU GLU LEU PHE          
SEQRES   9 Y  289  ILE PHE LEU THR GLU ILE THR GLU ILE THR ILE PRO CYS          
SEQRES  10 Y  289  ARG VAL THR ASP PRO GLN LEU VAL VAL THR LEU HIS GLU          
SEQRES  11 Y  289  LYS LYS GLY ASP VAL ALA LEU PRO VAL PRO TYR ASP HIS          
SEQRES  12 Y  289  GLN ARG GLY PHE SER GLY ILE PHE GLU ASP ARG SER TYR          
SEQRES  13 Y  289  ILE CYS LYS THR THR ILE GLY ASP ARG GLU VAL ASP SER          
SEQRES  14 Y  289  ASP ALA TYR TYR VAL TYR ARG LEU GLN VAL SER SER ILE          
SEQRES  15 Y  289  ASN VAL SER VAL ASN ALA VAL GLN THR VAL VAL ARG GLN          
SEQRES  16 Y  289  GLY GLU ASN ILE THR LEU MET CYS ILE VAL ILE GLY ASN          
SEQRES  17 Y  289  GLU VAL VAL ASN PHE GLU TRP THR TYR PRO ARG LYS GLU          
SEQRES  18 Y  289  SER GLY ARG LEU VAL GLU PRO VAL THR ASP PHE LEU LEU          
SEQRES  19 Y  289  ASP MET PRO TYR HIS ILE ARG SER ILE LEU HIS ILE PRO          
SEQRES  20 Y  289  SER ALA GLU LEU GLU ASP SER GLY THR TYR THR CYS ASN          
SEQRES  21 Y  289  VAL THR GLU SER VAL ASN ASP HIS GLN ASP GLU LYS ALA          
SEQRES  22 Y  289  ILE ASN ILE THR VAL VAL GLU SER GLY HIS HIS HIS HIS          
SEQRES  23 Y  289  HIS HIS HIS                                                  
MODRES 3MJG ASN X   89  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN X  292  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y   89  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y  230  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y   45  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y  103  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y  307  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y  292  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN X  230  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN Y  215  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN X  307  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN X  103  ASN  GLYCOSYLATION SITE                                 
MODRES 3MJG ASN X  215  ASN  GLYCOSYLATION SITE                                 
HET    NDG  X   1      14                                                       
HET    NAG  X   2      14                                                       
HET    NAG  X   3      14                                                       
HET    NAG  X   4      14                                                       
HET    NAG  X   5      14                                                       
HET    NAG  X   6      14                                                       
HET    NAG  X   7      14                                                       
HET    NAG  Y   1      14                                                       
HET    NAG  Y   2      14                                                       
HET    NAG  Y   3      14                                                       
HET    NAG  Y   4      14                                                       
HET    NAG  Y   5      14                                                       
HET    NAG  Y   6      14                                                       
HET    NAG  Y   7      14                                                       
HETNAM     NDG 2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE                        
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   5  NDG    C8 H15 N O6                                                  
FORMUL   6  NAG    13(C8 H15 N O6)                                              
FORMUL  19  HOH   *1170(H2 O)                                                   
HELIX    1   1 SER A   26  ILE A   30  5                                   5    
HELIX    2   2 SER B   26  ASP B   31  1                                   6    
HELIX    3   3 THR X   91  THR X   95  5                                   5    
HELIX    4   4 ASP X  131  LEU X  135  1                                   5    
HELIX    5   5 THR Y   91  THR Y   95  5                                   5    
HELIX    6   6 ASP Y  131  LEU Y  135  1                                   5    
SHEET    1   A 3 GLU A   9  PRO A  10  0                                        
SHEET    2   A 3 VAL B  58  VAL B  78  1  O  GLN B  71   N  GLU A   9           
SHEET    3   A 3 PHE B  37  TRP B  40 -1  N  LEU B  38   O  ILE B  75           
SHEET    1   B 3 GLU A   9  PRO A  10  0                                        
SHEET    2   B 3 VAL B  58  VAL B  78  1  O  GLN B  71   N  GLU A   9           
SHEET    3   B 3 LYS B  81  THR B 101 -1  O  LEU B  91   N  ARG B  68           
SHEET    1   C 2 LYS A  17  GLU A  24  0                                        
SHEET    2   C 2 CYS A  43  SER A  50 -1  O  VAL A  44   N  PHE A  23           
SHEET    1   D 3 LEU A  38  TRP A  40  0                                        
SHEET    2   D 3 VAL A  58  VAL A  78 -1  O  ILE A  75   N  LEU A  38           
SHEET    3   D 3 LYS A  81  THR A 101 -1  O  ILE A  83   N  GLU A  76           
SHEET    1   E 2 LYS B  17  GLU B  24  0                                        
SHEET    2   E 2 CYS B  43  SER B  50 -1  O  VAL B  44   N  PHE B  23           
SHEET    1   F 4 GLU X  41  VAL X  43  0                                        
SHEET    2   F 4 LYS X 114  PHE X 119  1  O  PHE X 119   N  LEU X  42           
SHEET    3   F 4 GLY X  96  THR X 101 -1  N  GLY X  96   O  ILE X 118           
SHEET    4   F 4 VAL X  61  GLU X  63 -1  N  VAL X  61   O  THR X 101           
SHEET    1   G 3 PHE X  50  GLY X  56  0                                        
SHEET    2   G 3 PHE X  81  LEU X  87 -1  O  PHE X  81   N  GLY X  56           
SHEET    3   G 3 GLN X  71  LYS X  75 -1  N  ALA X  74   O  SER X  82           
SHEET    1   H 4 PHE X 136  LEU X 139  0                                        
SHEET    2   H 4 TYR X 204  ARG X 208  1  O  TYR X 205   N  ILE X 137           
SHEET    3   H 4 SER X 187  ILE X 194 -1  N  TYR X 188   O  TYR X 204           
SHEET    4   H 4 VAL X 158  GLU X 162 -1  N  THR X 159   O  LYS X 191           
SHEET    1   I 4 PHE X 136  LEU X 139  0                                        
SHEET    2   I 4 TYR X 204  ARG X 208  1  O  TYR X 205   N  ILE X 137           
SHEET    3   I 4 SER X 187  ILE X 194 -1  N  TYR X 188   O  TYR X 204           
SHEET    4   I 4 ARG X 197  ASP X 200 -1  O  VAL X 199   N  THR X 192           
SHEET    1   J 3 ILE X 145  ILE X 147  0                                        
SHEET    2   J 3 GLY X 178  GLY X 181 -1  O  PHE X 179   N  ILE X 147           
SHEET    3   J 3 TYR X 173  ASP X 174 -1  N  ASP X 174   O  GLY X 178           
SHEET    1   K 4 SER X 217  ALA X 220  0                                        
SHEET    2   K 4 ILE X 231  ILE X 238 -1  O  MET X 234   N  ASN X 219           
SHEET    3   K 4 HIS X 271  ILE X 278 -1  O  ILE X 278   N  ILE X 231           
SHEET    4   K 4 VAL X 261  PHE X 264 -1  N  ASP X 263   O  ARG X 273           
SHEET    1   L 4 VAL X 224  ARG X 226  0                                        
SHEET    2   L 4 HIS X 300  VAL X 311  1  O  VAL X 311   N  VAL X 225           
SHEET    3   L 4 GLY X 287  GLU X 295 -1  N  VAL X 293   O  ASP X 302           
SHEET    4   L 4 ASN X 244  THR X 248 -1  N  ASN X 244   O  THR X 294           
SHEET    1   M 4 GLU Y  41  VAL Y  43  0                                        
SHEET    2   M 4 LEU Y 116  PHE Y 119  1  O  PHE Y 119   N  LEU Y  42           
SHEET    3   M 4 GLY Y  96  CYS Y 100 -1  N  TYR Y  98   O  LEU Y 116           
SHEET    4   M 4 TRP Y  62  GLU Y  63 -1  N  GLU Y  63   O  PHE Y  99           
SHEET    1   N 3 PHE Y  50  GLY Y  56  0                                        
SHEET    2   N 3 THR Y  80  LEU Y  87 -1  O  PHE Y  81   N  GLY Y  56           
SHEET    3   N 3 GLU Y  72  ALA Y  76 -1  N  ALA Y  76   O  THR Y  80           
SHEET    1   O 4 PHE Y 136  LEU Y 139  0                                        
SHEET    2   O 4 TYR Y 204  ARG Y 208  1  O  TYR Y 205   N  ILE Y 137           
SHEET    3   O 4 SER Y 187  ILE Y 194 -1  N  TYR Y 188   O  TYR Y 204           
SHEET    4   O 4 THR Y 159  GLU Y 162 -1  N  HIS Y 161   O  ILE Y 189           
SHEET    1   P 4 PHE Y 136  LEU Y 139  0                                        
SHEET    2   P 4 TYR Y 204  ARG Y 208  1  O  TYR Y 205   N  ILE Y 137           
SHEET    3   P 4 SER Y 187  ILE Y 194 -1  N  TYR Y 188   O  TYR Y 204           
SHEET    4   P 4 ARG Y 197  ASP Y 200 -1  O  VAL Y 199   N  THR Y 192           
SHEET    1   Q 3 ILE Y 145  ILE Y 147  0                                        
SHEET    2   Q 3 GLY Y 178  GLY Y 181 -1  O  GLY Y 181   N  ILE Y 145           
SHEET    3   Q 3 TYR Y 173  ASP Y 174 -1  N  ASP Y 174   O  GLY Y 178           
SHEET    1   R 4 SER Y 217  ALA Y 220  0                                        
SHEET    2   R 4 ILE Y 231  ILE Y 238 -1  O  MET Y 234   N  ASN Y 219           
SHEET    3   R 4 HIS Y 271  ILE Y 278 -1  O  SER Y 274   N  CYS Y 235           
SHEET    4   R 4 VAL Y 261  PHE Y 264 -1  N  ASP Y 263   O  ARG Y 273           
SHEET    1   S 4 VAL Y 224  ARG Y 226  0                                        
SHEET    2   S 4 GLN Y 301  VAL Y 311  1  O  VAL Y 311   N  VAL Y 225           
SHEET    3   S 4 GLY Y 287  THR Y 294 -1  N  TYR Y 289   O  ILE Y 306           
SHEET    4   S 4 ASN Y 244  THR Y 248 -1  N  ASN Y 244   O  THR Y 294           
SSBOND   1 CYS A   16    CYS A   60                          1555   1555  2.05  
SSBOND   2 CYS A   43    CYS B   52                          1555   1555  2.05  
SSBOND   3 CYS A   49    CYS A   97                          1555   1555  2.04  
SSBOND   4 CYS A   52    CYS B   43                          1555   1555  2.04  
SSBOND   5 CYS A   53    CYS A   99                          1555   1555  2.06  
SSBOND   6 CYS B   16    CYS B   60                          1555   1555  2.05  
SSBOND   7 CYS B   49    CYS B   97                          1555   1555  2.04  
SSBOND   8 CYS B   53    CYS B   99                          1555   1555  2.06  
SSBOND   9 CYS X   54    CYS X  100                          1555   1555  2.01  
SSBOND  10 CYS X  149    CYS X  190                          1555   1555  2.04  
SSBOND  11 CYS X  235    CYS X  291                          1555   1555  2.05  
SSBOND  12 CYS Y   54    CYS Y  100                          1555   1555  2.03  
SSBOND  13 CYS Y  149    CYS Y  190                          1555   1555  2.04  
SSBOND  14 CYS Y  235    CYS Y  291                          1555   1555  2.03  
LINK         ND2 ASN X  89                 C1  NAG X   2     1555   1555  1.45  
LINK         ND2 ASN X 292                 C1  NAG X   6     1555   1555  1.45  
LINK         ND2 ASN Y  89                 C1  NAG Y   2     1555   1555  1.45  
LINK         ND2 ASN Y 230                 C1  NAG Y   5     1555   1555  1.45  
LINK         ND2 ASN Y  45                 C1  NAG Y   1     1555   1555  1.45  
LINK         ND2 ASN Y 103                 C1  NAG Y   3     1555   1555  1.45  
LINK         ND2 ASN Y 307                 C1  NAG Y   7     1555   1555  1.45  
LINK         ND2 ASN Y 292                 C1  NAG Y   6     1555   1555  1.45  
LINK         ND2 ASN X 230                 C1  NAG X   5     1555   1555  1.45  
LINK         ND2 ASN Y 215                 C1  NAG Y   4     1555   1555  1.46  
LINK         ND2 ASN X 307                 C1  NAG X   7     1555   1555  1.46  
LINK         ND2 ASN X 103                 C1  NAG X   3     1555   1555  1.46  
LINK         ND2 ASN X 215                 C1  NAG X   4     1555   1555  1.46  
CISPEP   1 TRP A   40    PRO A   41          0        -0.28                     
CISPEP   2 TRP B   40    PRO B   41          0        -0.51                     
CISPEP   3 PRO X   37    PRO X   38          0         0.51                     
CISPEP   4 GLY X   39    PRO X   40          0        -0.41                     
CISPEP   5 PRO Y   37    PRO Y   38          0        -0.95                     
CISPEP   6 GLY Y   39    PRO Y   40          0        -0.61                     
SITE     1 AC1  5 ASN X  45  THR X 223  ILE X 306  ASN X 307                    
SITE     2 AC1  5 HOH X 377                                                     
SITE     1 AC2  2 ASN X  89  HOH X 402                                          
SITE     1 AC3  4 HIS X 102  ASN X 103  HOH X1394  ARG Y 273                    
SITE     1 AC4  2 ASN X 215  HOH X 399                                          
SITE     1 AC5  5 PRO X  40  ASN X 230  HIS X 277  HOH X 611                    
SITE     2 AC5  5 HOH X1232                                                     
SITE     1 AC6  6 GLU X 246  ASN X 292  GLN X 301  GLU X 303                    
SITE     2 AC6  6 HOH X 615  NAG Y   7                                          
SITE     1 AC7  3 THR X 288  ALA X 305  ASN X 307                               
SITE     1 AC8  4 ASN Y  45  SER Y  48  HOH Y 888  HOH Y1003                    
SITE     1 AC9  4 GLU X 253  SER X 254  ASN Y  89  HOH Y1204                    
SITE     1 BC1  4 HIS Y 102  ASN Y 103  HOH Y 700  HOH Y 943                    
SITE     1 BC2  4 ILE Y 214  ASN Y 215  ASP Y 302  HOH Y 504                    
SITE     1 BC3  2 ASN Y 230  HOH Y 809                                          
SITE     1 BC4  5 GLU Y 246  ASN Y 292  THR Y 294  GLN Y 301                    
SITE     2 BC4  5 HOH Y 755                                                     
SITE     1 BC5  4 NAG X   6  THR Y 288  ASN Y 307  HOH Y 525                    
CRYST1   78.470  116.820  134.150  90.00  90.00  90.00 P 21 21 21    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      0.012744  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007454        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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