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Database: PDB
Entry: 1E0O
LinkDB: 1E0O
Original site: 1E0O 
HEADER    GROWTH FACTOR                           03-APR-00   1E0O              
TITLE     CRYSTAL STRUCTURE OF A TERNARY FGF1-FGFR2-HEPARIN COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 1;                                
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: ACIDIC FIBROBLAST GROWTH FACTOR;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;                       
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET14A;                                   
SOURCE   8 OTHER_DETAILS: RECOMBINANT;                                          
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PET3A;                                    
SOURCE  16 OTHER_DETAILS: RECOMBINANT                                           
KEYWDS    GROWTH FACTOR, RECEPTOR TYROSINE KINASE, HEPARIN, TERNARY COMPLEX,    
KEYWDS   2 SIGNAL TRANSDUCTION                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.PELLEGRINI,D.F.BURKE,F.VON DELFT,B.MULLOY,T.L.BLUNDELL              
REVDAT   6   29-JUL-20 1E0O    1       COMPND REMARK HETNAM LINK                
REVDAT   6 2                   1       SITE   ATOM                              
REVDAT   5   13-DEC-17 1E0O    1       SOURCE AUTHOR JRNL                       
REVDAT   4   27-APR-11 1E0O    1       VERSN                                    
REVDAT   3   24-FEB-09 1E0O    1       VERSN                                    
REVDAT   2   11-NOV-00 1E0O    1       JRNL                                     
REVDAT   1   23-OCT-00 1E0O    0                                                
JRNL        AUTH   L.PELLEGRINI,D.F.BURKE,F.VON DELFT,B.MULLOY,T.L.BLUNDELL     
JRNL        TITL   CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR RECEPTOR       
JRNL        TITL 2 ECTODOMAIN BOUND TO LIGAND AND HEPARIN                       
JRNL        REF    NATURE                        V. 407  1029 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   11069186                                                     
JRNL        DOI    10.1038/35039551                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 36348                          
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) : 0.274                           
REMARK   3   FREE R VALUE                     : 0.309                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1804                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5001                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 41                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.67                            
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) : 0.55                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.520                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.360 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.110 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.150 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 8.960 ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E0O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-APR-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004815.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36342                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.47400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP, SHELX                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN FROM: 1.0M LI2SO4,   
REMARK 280  0.1M TRISCL PH=8.5, 10MM NISO4, PH 8.50                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.90667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       22.95333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       45.90667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       22.95333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.3 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     PHE A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     SER B   148                                                      
REMARK 465     VAL B   294                                                      
REMARK 465     GLU B   295                                                      
REMARK 465     LYS B   296                                                      
REMARK 465     ASN B   297                                                      
REMARK 465     GLY B   298                                                      
REMARK 465     SER B   299                                                      
REMARK 465     LYS B   300                                                      
REMARK 465     TYR B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     PRO B   303                                                      
REMARK 465     ASP B   304                                                      
REMARK 465     GLY B   305                                                      
REMARK 465     LEU B   306                                                      
REMARK 465     PRO B   307                                                      
REMARK 465     TYR B   308                                                      
REMARK 465     PRO B   361                                                      
REMARK 465     ALA B   362                                                      
REMARK 465     PRO B   363                                                      
REMARK 465     GLY B   364                                                      
REMARK 465     ARG B   365                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     PHE C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     TYR C     8                                                      
REMARK 465     SER C   139                                                      
REMARK 465     ASP C   140                                                      
REMARK 465     SER D   148                                                      
REMARK 465     VAL D   294                                                      
REMARK 465     GLU D   295                                                      
REMARK 465     LYS D   296                                                      
REMARK 465     ASN D   297                                                      
REMARK 465     GLY D   298                                                      
REMARK 465     SER D   299                                                      
REMARK 465     LYS D   300                                                      
REMARK 465     TYR D   301                                                      
REMARK 465     GLY D   302                                                      
REMARK 465     PRO D   303                                                      
REMARK 465     ASP D   304                                                      
REMARK 465     GLY D   305                                                      
REMARK 465     LEU D   306                                                      
REMARK 465     PRO D   307                                                      
REMARK 465     TYR D   308                                                      
REMARK 465     LEU D   309                                                      
REMARK 465     PRO D   361                                                      
REMARK 465     ALA D   362                                                      
REMARK 465     PRO D   363                                                      
REMARK 465     GLY D   364                                                      
REMARK 465     ARG D   365                                                      
REMARK 465     GLU D   366                                                      
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     LYS A  10    CG   CD   CE   NZ                                   
REMARK 470     ASP A  28    CG   OD1  OD2                                       
REMARK 470     ASP A  36    CG   OD1  OD2                                       
REMARK 470     GLN A  40    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  45    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  57    CG   CD   CE   NZ                                   
REMARK 470     ASP A  70    CG   OD1  OD2                                       
REMARK 470     GLN A  77    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  82    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     GLU A 104    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     ASN B 149    CG   OD1  ND2                                       
REMARK 470     LYS B 196    CG   CD   CE   NZ                                   
REMARK 470     LYS B 199    CG   CD   CE   NZ                                   
REMARK 470     GLN B 212    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 226    CG   CD   CE   NZ                                   
REMARK 470     LYS B 279    CG   CD   CE   NZ                                   
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     HIS B 293    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 313    CG   CD   CE   NZ                                   
REMARK 470     LYS B 322    CG   CD   CE   NZ                                   
REMARK 470     GLU B 323    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 325    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 335    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  10    CG   CD   CE   NZ                                   
REMARK 470     GLN C  40    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 100    CG   CD   CE   NZ                                   
REMARK 470     LYS C 101    CG   CD   CE   NZ                                   
REMARK 470     GLU C 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 196    CG   CD   CE   NZ                                   
REMARK 470     LYS D 199    CG   CD   CE   NZ                                   
REMARK 470     GLU D 201    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 226    CG   CD   CE   NZ                                   
REMARK 470     GLN D 285    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 292    CG   CD   CE   NZ                                   
REMARK 470     HIS D 293    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 310    CG   CD   CE   NZ                                   
REMARK 470     LYS D 313    CG   CD   CE   NZ                                   
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     ARG D 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 335    CG   CD   OE1  OE2                                  
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    LEU A  14       65.75   -111.71                                   
REMARK 500    ASP A  28        0.27    -69.57                                   
REMARK 500    ASP A  32     -143.49   -124.80                                   
REMARK 500    THR A  34     -166.63   -117.13                                   
REMARK 500    ARG A  35       -6.32   -141.41                                   
REMARK 500    HIS A  41       35.76    -76.42                                   
REMARK 500    GLN A  43       64.85    -60.56                                   
REMARK 500    GLU A  49      -83.25    -77.71                                   
REMARK 500    THR A  59       14.36    -69.98                                   
REMARK 500    GLU A  60      -68.30   -121.43                                   
REMARK 500    ASP A  68     -171.51    -65.38                                   
REMARK 500    GLU A  81      -34.46    -33.10                                   
REMARK 500    GLU A  91      -39.63    -35.79                                   
REMARK 500    ASN A 106       53.27     95.64                                   
REMARK 500    LEU A 111      137.40   -177.73                                   
REMARK 500    LYS A 113      -16.60    -34.59                                   
REMARK 500    CYS A 117      151.40    -44.05                                   
REMARK 500    ARG A 119      117.50    -24.17                                   
REMARK 500    PRO A 136      174.32    -47.03                                   
REMARK 500    ARG B 152      110.74   -176.24                                   
REMARK 500    PRO B 154      135.26    -35.97                                   
REMARK 500    ASN B 158       66.55   -177.71                                   
REMARK 500    ALA B 172      -13.61     94.97                                   
REMARK 500    SER B 220       62.43     37.01                                   
REMARK 500    ALA B 260      156.11    -48.03                                   
REMARK 500    SER B 267      142.41   -174.93                                   
REMARK 500    VAL B 270      126.52    -36.58                                   
REMARK 500    ALA B 284     -158.60   -134.88                                   
REMARK 500    VAL B 317      -89.01    -60.15                                   
REMARK 500    ILE B 329       77.28   -150.58                                   
REMARK 500    VAL B 332     -176.23    -50.56                                   
REMARK 500    ASP B 336       -8.24    -53.82                                   
REMARK 500    PHE B 352      140.77   -171.72                                   
REMARK 500    ASN C  18      -76.70    -33.82                                   
REMARK 500    HIS C  41       27.96    -66.04                                   
REMARK 500    GLU C  49      -95.46    -74.22                                   
REMARK 500    THR C  59       23.93    -72.48                                   
REMARK 500    GLU C  60      -74.46   -129.45                                   
REMARK 500    ASP C  68     -166.28    -67.20                                   
REMARK 500    HIS C  93       25.11     81.53                                   
REMARK 500    ASN C 106       61.57     69.97                                   
REMARK 500    LYS C 113      -13.78    -44.98                                   
REMARK 500    CYS C 117      148.76    -38.89                                   
REMARK 500    ARG C 122       50.19   -103.62                                   
REMARK 500    PRO C 136      156.50    -46.29                                   
REMARK 500    ASN D 150       32.43    -96.01                                   
REMARK 500    PRO D 154      132.79    -32.44                                   
REMARK 500    LYS D 164       99.19    -66.70                                   
REMARK 500    ALA D 172      -24.65     82.08                                   
REMARK 500    ASN D 194       63.98     36.94                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      59 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  15         0.06    SIDE CHAIN                              
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     IDS E   10                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 201  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  93   NE2                                                    
REMARK 620 2 HOH A 307   O   108.7                                              
REMARK 620 3 HIS B 254   NE2  85.7 122.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 401  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 245   NE2                                                    
REMARK 620 2 ASP B 247   OD1  82.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 402  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 287   NE2                                                    
REMARK 620 2 HOH B 512   O   125.9                                              
REMARK 620 3 HIS D 287   NE2  62.4 154.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI C 203  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  93   NE2                                                    
REMARK 620 2 HIS D 254   NE2  81.3                                              
REMARK 620 3 HOH D 507   O    78.1  74.2                                        
REMARK 620 4 HOH D 515   O   107.4  91.9 164.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI D 404  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 245   NE2                                                    
REMARK 620 2 ASP D 247   OD1  82.3                                              
REMARK 620 3 HOH D 504   O    79.2 105.6                                        
REMARK 620 N                    1     2                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AXM   RELATED DB: PDB                                   
REMARK 900 HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST               
REMARK 900 RELATED ID: 2AXM   RELATED DB: PDB                                   
REMARK 900 HEPARIN-LINKED BIOLOGICALLY-ACTIVE DIMER OF FIBROBLAST               
REMARK 900 RELATED ID: 1DJS   RELATED DB: PDB                                   
REMARK 900 LIGAND-BINDING PORTION OF FIBROBLAST GROWTH FACTOR RECEPTOR          
REMARK 900 RELATED ID: 1CVS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX                    
DBREF  1E0O A    1   140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  1E0O B  148   366  UNP    P21802   FGR2_HUMAN     148    366             
DBREF  1E0O C    1   140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  1E0O D  148   366  UNP    P21802   FGR2_HUMAN     148    366             
SEQRES   1 A  140  PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS LEU          
SEQRES   2 A  140  LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE LEU          
SEQRES   3 A  140  PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER ASP          
SEQRES   4 A  140  GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL GLY          
SEQRES   5 A  140  GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR LEU          
SEQRES   6 A  140  ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR          
SEQRES   7 A  140  PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU          
SEQRES   8 A  140  ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU          
SEQRES   9 A  140  LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER CYS          
SEQRES  10 A  140  LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA ILE          
SEQRES  11 A  140  LEU PHE LEU PRO LEU PRO VAL SER SER ASP                      
SEQRES   1 B  219  SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU          
SEQRES   2 B  219  LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN          
SEQRES   3 B  219  THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET          
SEQRES   4 B  219  PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS          
SEQRES   5 B  219  GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN          
SEQRES   6 B  219  HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER ASP          
SEQRES   7 B  219  LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY          
SEQRES   8 B  219  SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU ARG          
SEQRES   9 B  219  SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO ALA          
SEQRES  10 B  219  ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE VAL          
SEQRES  11 B  219  CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN TRP          
SEQRES  12 B  219  ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY PRO          
SEQRES  13 B  219  ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA GLY          
SEQRES  14 B  219  VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR ILE          
SEQRES  15 B  219  ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR CYS          
SEQRES  16 B  219  LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER ALA          
SEQRES  17 B  219  TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU                  
SEQRES   1 C  140  PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS LEU          
SEQRES   2 C  140  LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE LEU          
SEQRES   3 C  140  PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER ASP          
SEQRES   4 C  140  GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL GLY          
SEQRES   5 C  140  GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR LEU          
SEQRES   6 C  140  ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN THR          
SEQRES   7 C  140  PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU GLU          
SEQRES   8 C  140  ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA GLU          
SEQRES   9 C  140  LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER CYS          
SEQRES  10 C  140  LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA ILE          
SEQRES  11 C  140  LEU PHE LEU PRO LEU PRO VAL SER SER ASP                      
SEQRES   1 D  219  SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU          
SEQRES   2 D  219  LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN          
SEQRES   3 D  219  THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET          
SEQRES   4 D  219  PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS          
SEQRES   5 D  219  GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN          
SEQRES   6 D  219  HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER ASP          
SEQRES   7 D  219  LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY          
SEQRES   8 D  219  SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU ARG          
SEQRES   9 D  219  SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO ALA          
SEQRES  10 D  219  ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE VAL          
SEQRES  11 D  219  CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN TRP          
SEQRES  12 D  219  ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY PRO          
SEQRES  13 D  219  ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA GLY          
SEQRES  14 D  219  VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR ILE          
SEQRES  15 D  219  ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR CYS          
SEQRES  16 D  219  LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER ALA          
SEQRES  17 D  219  TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU                  
HET    SGN  E   1      20                                                       
HET    IDS  E   2      16                                                       
HET    SGN  E   3      19                                                       
HET    IDS  E   4      16                                                       
HET    SGN  E   5      19                                                       
HET    IDS  E   6      16                                                       
HET    SGN  E   7      19                                                       
HET    IDS  E   8      16                                                       
HET    SGN  E   9      19                                                       
HET    IDS  E  10      15                                                       
HET     NI  A 201       1                                                       
HET     NI  B 401       1                                                       
HET     NI  B 402       1                                                       
HET    SO4  C 201       5                                                       
HET    SO4  C 202       5                                                       
HET     NI  C 203       1                                                       
HET    SO4  D 401       5                                                       
HET    SO4  D 402       5                                                       
HET    SO4  D 403       5                                                       
HET     NI  D 404       1                                                       
HETNAM     SGN 2-DEOXY-6-O-SULFO-2-(SULFOAMINO)-ALPHA-D-GLUCOPYRANOSE           
HETNAM     IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID                            
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
HETSYN     IDS O2-SULFO-GLUCURONIC ACID                                         
FORMUL   5  SGN    5(C6 H13 N O11 S2)                                           
FORMUL   5  IDS    5(C6 H10 O10 S)                                              
FORMUL   6   NI    5(NI 2+)                                                     
FORMUL   9  SO4    5(O4 S 2-)                                                   
FORMUL  16  HOH   *41(H2 O)                                                     
HELIX    1 AA1 ASN A   80  CYS A   83  5                                   4    
HELIX    2 AA2 ASN B  158  GLU B  163  5                                   6    
HELIX    3 AA3 LYS B  199  ARG B  203  5                                   5    
HELIX    4 AA4 ASN B  211  HIS B  213  5                                   3    
HELIX    5 AA5 VAL B  222  LYS B  226  5                                   5    
HELIX    6 AA6 THR B  320  GLU B  325  1                                   6    
HELIX    7 AA7 ASN C   80  CYS C   83  5                                   4    
HELIX    8 AA8 HIS C  102  ASN C  106  5                                   5    
HELIX    9 AA9 ARG C  119  THR C  123  5                                   5    
HELIX   10 AB1 LYS D  199  ARG D  203  5                                   5    
HELIX   11 AB2 VAL D  222  LYS D  226  5                                   5    
HELIX   12 AB3 THR D  320  GLU D  325  1                                   6    
SHEET    1 AA1 2 LEU A  13  CYS A  16  0                                        
SHEET    2 AA1 2 PHE A 132  LEU A 135 -1  O  LEU A 135   N  LEU A  13           
SHEET    1 AA2 2 PHE A  22  ILE A  25  0                                        
SHEET    2 AA2 2 VAL A  31  THR A  34 -1  O  THR A  34   N  PHE A  22           
SHEET    1 AA3 4 LEU A  44  ALA A  48  0                                        
SHEET    2 AA3 4 GLU A  53  SER A  58 -1  O  TYR A  55   N  SER A  47           
SHEET    3 AA3 4 PHE A  85  LEU A  89 -1  O  PHE A  85   N  VAL A  54           
SHEET    4 AA3 4 ASN A  95  SER A  99 -1  O  THR A  96   N  ARG A  88           
SHEET    1 AA4 2 TYR A  64  MET A  67  0                                        
SHEET    2 AA4 2 LEU A  73  SER A  76 -1  O  TYR A  74   N  ALA A  66           
SHEET    1 AA5 2 ARG B 152  TRP B 156  0                                        
SHEET    2 AA5 2 ALA B 181  ASN B 184 -1  O  GLY B 182   N  TYR B 155           
SHEET    1 AA6 5 LEU B 166  PRO B 170  0                                        
SHEET    2 AA6 5 GLY B 238  VAL B 249  1  O  HIS B 245   N  HIS B 167           
SHEET    3 AA6 5 GLY B 227  ASN B 235 -1  N  TYR B 229   O  TYR B 244           
SHEET    4 AA6 5 THR B 188  LYS B 193 -1  N  LEU B 192   O  THR B 230           
SHEET    5 AA6 5 LYS B 196  GLU B 197 -1  O  LYS B 196   N  LYS B 193           
SHEET    1 AA7 3 VAL B 175  ARG B 178  0                                        
SHEET    2 AA7 3 SER B 215  MET B 218 -1  O  MET B 218   N  VAL B 175           
SHEET    3 AA7 3 LYS B 208  ARG B 210 -1  N  LYS B 208   O  ILE B 217           
SHEET    1 AA8 2 ILE B 257  LEU B 258  0                                        
SHEET    2 AA8 2 VAL B 280  TYR B 281 -1  O  TYR B 281   N  ILE B 257           
SHEET    1 AA9 5 ALA B 266  VAL B 269  0                                        
SHEET    2 AA9 5 GLY B 349  LEU B 360  1  O  TRP B 356   N  ALA B 266           
SHEET    3 AA9 5 GLY B 338  ASN B 346 -1  N  CYS B 342   O  HIS B 353           
SHEET    4 AA9 5 HIS B 287  LYS B 292 -1  N  HIS B 287   O  GLY B 345           
SHEET    5 AA9 5 LYS B 310  ALA B 314 -1  O  LYS B 310   N  LYS B 292           
SHEET    1 AB1 2 VAL B 274  VAL B 277  0                                        
SHEET    2 AB1 2 VAL B 326  ILE B 329 -1  O  LEU B 327   N  PHE B 276           
SHEET    1 AB2 4 VAL C  31  THR C  34  0                                        
SHEET    2 AB2 4 HIS C  21  ILE C  25 -1  N  PHE C  22   O  THR C  34           
SHEET    3 AB2 4 LEU C  13  CYS C  16 -1  N  CYS C  16   O  HIS C  21           
SHEET    4 AB2 4 PHE C 132  LEU C 135 -1  O  LEU C 135   N  LEU C  13           
SHEET    1 AB3 4 LEU C  44  SER C  47  0                                        
SHEET    2 AB3 4 GLU C  53  SER C  58 -1  O  TYR C  55   N  SER C  47           
SHEET    3 AB3 4 PHE C  85  LEU C  89 -1  O  PHE C  85   N  VAL C  54           
SHEET    4 AB3 4 ASN C  95  SER C  99 -1  O  ILE C  98   N  LEU C  86           
SHEET    1 AB4 2 TYR C  64  MET C  67  0                                        
SHEET    2 AB4 2 LEU C  73  SER C  76 -1  O  TYR C  74   N  ALA C  66           
SHEET    1 AB5 2 LEU C 111  LYS C 112  0                                        
SHEET    2 AB5 2 SER C 116  CYS C 117 -1  O  SER C 116   N  LYS C 112           
SHEET    1 AB6 2 ARG D 152  TRP D 156  0                                        
SHEET    2 AB6 2 ALA D 181  ASN D 184 -1  O  GLY D 182   N  TYR D 155           
SHEET    1 AB7 5 LEU D 166  PRO D 170  0                                        
SHEET    2 AB7 5 GLY D 238  VAL D 249  1  O  HIS D 245   N  HIS D 167           
SHEET    3 AB7 5 GLY D 227  ASN D 235 -1  N  TYR D 229   O  TYR D 244           
SHEET    4 AB7 5 THR D 188  LYS D 193 -1  N  LEU D 192   O  THR D 230           
SHEET    5 AB7 5 LYS D 196  GLU D 197 -1  O  LYS D 196   N  LYS D 193           
SHEET    1 AB8 3 VAL D 175  ARG D 178  0                                        
SHEET    2 AB8 3 SER D 215  MET D 218 -1  O  MET D 218   N  VAL D 175           
SHEET    3 AB8 3 LYS D 208  ARG D 210 -1  N  LYS D 208   O  ILE D 217           
SHEET    1 AB9 2 ILE D 257  LEU D 258  0                                        
SHEET    2 AB9 2 VAL D 280  TYR D 281 -1  O  TYR D 281   N  ILE D 257           
SHEET    1 AC1 5 ALA D 266  VAL D 269  0                                        
SHEET    2 AC1 5 GLY D 349  LEU D 360  1  O  LEU D 360   N  THR D 268           
SHEET    3 AC1 5 GLY D 338  ASN D 346 -1  N  ASN D 346   O  GLY D 349           
SHEET    4 AC1 5 HIS D 287  LYS D 292 -1  N  GLN D 289   O  LEU D 343           
SHEET    5 AC1 5 VAL D 311  ALA D 314 -1  O  LYS D 313   N  TRP D 290           
SHEET    1 AC2 2 VAL D 274  VAL D 277  0                                        
SHEET    2 AC2 2 VAL D 326  ILE D 329 -1  O  LEU D 327   N  PHE D 276           
SSBOND   1 CYS B  179    CYS B  231                          1555   1555  2.04  
SSBOND   2 CYS B  278    CYS B  342                          1555   1555  2.02  
SSBOND   3 CYS D  179    CYS D  231                          1555   1555  2.05  
SSBOND   4 CYS D  278    CYS D  342                          1555   1555  2.03  
LINK         O4  SGN E   1                 C1  IDS E   2     1555   1555  1.43  
LINK         O4  IDS E   2                 C1  SGN E   3     1555   1555  1.44  
LINK         O4  SGN E   3                 C1  IDS E   4     1555   1555  1.44  
LINK         O4  IDS E   4                 C1  SGN E   5     1555   1555  1.42  
LINK         O4  SGN E   5                 C1  IDS E   6     1555   1555  1.38  
LINK         O4  IDS E   6                 C1  SGN E   7     1555   1555  1.37  
LINK         O4  SGN E   7                 C1  IDS E   8     1555   1555  1.38  
LINK         O4  IDS E   8                 C1  SGN E   9     1555   1555  1.42  
LINK         O4  SGN E   9                 C1  IDS E  10     1555   1555  1.40  
LINK         NE2 HIS A  93                NI    NI A 201     1555   1555  2.14  
LINK        NI    NI A 201                 O   HOH A 307     1555   1555  1.96  
LINK        NI    NI A 201                 NE2 HIS B 254     1555   1555  2.41  
LINK         NE2 HIS B 245                NI    NI B 401     1555   1555  2.40  
LINK         OD1 ASP B 247                NI    NI B 401     1555   1555  2.38  
LINK         NE2 HIS B 287                NI    NI B 402     1555   1555  2.06  
LINK        NI    NI B 402                 O   HOH B 512     1555   1555  1.95  
LINK        NI    NI B 402                 NE2 HIS D 287     5564   1555  2.11  
LINK         NE2 HIS C  93                NI    NI C 203     1555   1555  2.37  
LINK        NI    NI C 203                 NE2 HIS D 254     1555   1555  2.35  
LINK        NI    NI C 203                 O   HOH D 507     1555   1555  2.22  
LINK        NI    NI C 203                 O   HOH D 515     1555   1555  2.07  
LINK         NE2 HIS D 245                NI    NI D 404     1555   1555  2.38  
LINK         OD1 ASP D 247                NI    NI D 404     1555   1555  2.14  
LINK        NI    NI D 404                 O   HOH D 504     1555   1555  2.11  
CISPEP   1 ASN B  184    PRO B  185          0         1.68                     
CISPEP   2 SER B  252    PRO B  253          0         3.69                     
CISPEP   3 LEU B  262    PRO B  263          0         0.18                     
CISPEP   4 ASN D  184    PRO D  185          0        -0.08                     
CISPEP   5 SER D  252    PRO D  253          0         0.83                     
CISPEP   6 LEU D  262    PRO D  263          0         0.22                     
CRYST1  195.900  195.900   68.860  90.00  90.00 120.00 P 62         12          
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      0.005105  0.002947  0.000000        0.00000                         
SCALE2      0.000000  0.005894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014522        0.00000                         
MTRIX1   1  0.610700  0.789217 -0.064666      -92.51000    1                    
MTRIX2   1  0.774890 -0.612432 -0.156434      182.22301    1                    
MTRIX3   1 -0.163064  0.045426 -0.985569       33.63400    1                    
MTRIX1   2  0.565035  0.824776  0.021913      -93.16200    1                    
MTRIX2   2  0.799169 -0.540504 -0.263028      173.12801    1                    
MTRIX3   2 -0.205095  0.166132 -0.964539       41.46000    1                    
MTRIX1   3  0.704223  0.669179 -0.237213      -69.99780    1                    
MTRIX2   3  0.551295 -0.725933 -0.411212      197.39650    1                    
MTRIX3   3 -0.447375  0.158811 -0.880133       66.43880    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system