GenomeNet

Database: PDB
Entry: 1FQ9
LinkDB: 1FQ9
Original site: 1FQ9 
HEADER    GROWTH FACTOR/GROWTH FACTOR RECEPTOR    04-SEP-00   1FQ9              
TITLE     CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 2;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 (FGF2);   
COMPND   5 SYNONYM: FGF2;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 1;                       
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 FRAGMENT: EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 1      
COMPND  12 (FGFR1) CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II (D2) AND III    
COMPND  13 (D3);                                                                
COMPND  14 SYNONYM: FGFR1;                                                      
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: 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;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    I-SET SUBGROUP WITHIN THE IMMUNOGLOBULIN SUPERFAMILY, B-TREFOIL FOLD, 
KEYWDS   2 GROWTH FACTOR-GROWTH FACTOR RECEPTOR COMPLEX                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHLESSINGER,A.N.PLOTNIKOV,O.A.IBRAHIMI,A.V.ELISEENKOVA,B.K.YEH,    
AUTHOR   2 A.YAYON,R.J.LINHARDT,M.MOHAMMADI                                     
REVDAT   3   13-JUL-11 1FQ9    1       VERSN                                    
REVDAT   2   24-FEB-09 1FQ9    1       VERSN                                    
REVDAT   1   27-SEP-00 1FQ9    0                                                
JRNL        AUTH   J.SCHLESSINGER,A.N.PLOTNIKOV,O.A.IBRAHIMI,A.V.ELISEENKOVA,   
JRNL        AUTH 2 B.K.YEH,A.YAYON,R.J.LINHARDT,M.MOHAMMADI                     
JRNL        TITL   CRYSTAL STRUCTURE OF A TERNARY FGF-FGFR-HEPARIN COMPLEX      
JRNL        TITL 2 REVEALS A DUAL ROLE FOR HEPARIN IN FGFR BINDING AND          
JRNL        TITL 3 DIMERIZATION.                                                
JRNL        REF    MOL.CELL                      V.   6   743 2000              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   11030354                                                     
JRNL        DOI    10.1016/S1097-2765(00)00073-3                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 18305                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 886                             
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            : 5251                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 245                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
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) : 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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FQ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011812.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97669                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.940                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GLYCEROL, TRIS-HCL,    
REMARK 280  PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       98.14600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       49.44400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       49.44400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.07300            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       49.44400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       49.44400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      147.21900            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       49.44400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       49.44400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       49.07300            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       49.44400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       49.44400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      147.21900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       98.14600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    15                                                      
REMARK 465     LYS A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     LYS B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     THR C   141                                                      
REMARK 465     ASP C   142                                                      
REMARK 465     ASN C   143                                                      
REMARK 465     THR C   144                                                      
REMARK 465     LYS C   145                                                      
REMARK 465     PRO C   146                                                      
REMARK 465     ASN C   147                                                      
REMARK 465     ARG C   148                                                      
REMARK 465     GLU C   360                                                      
REMARK 465     ALA C   361                                                      
REMARK 465     LEU C   362                                                      
REMARK 465     GLU C   363                                                      
REMARK 465     GLU C   364                                                      
REMARK 465     ARG C   365                                                      
REMARK 465     THR D   141                                                      
REMARK 465     ASP D   142                                                      
REMARK 465     ASN D   143                                                      
REMARK 465     THR D   144                                                      
REMARK 465     LYS D   145                                                      
REMARK 465     PRO D   146                                                      
REMARK 465     ASN D   147                                                      
REMARK 465     ARG D   148                                                      
REMARK 465     ILE D   293                                                      
REMARK 465     GLU D   294                                                      
REMARK 465     VAL D   295                                                      
REMARK 465     ASN D   296                                                      
REMARK 465     GLY D   297                                                      
REMARK 465     SER D   298                                                      
REMARK 465     LYS D   299                                                      
REMARK 465     ILE D   300                                                      
REMARK 465     GLY D   301                                                      
REMARK 465     PRO D   302                                                      
REMARK 465     ASP D   303                                                      
REMARK 465     ASN D   304                                                      
REMARK 465     LEU D   305                                                      
REMARK 465     PRO D   306                                                      
REMARK 465     TYR D   307                                                      
REMARK 465     GLU D   360                                                      
REMARK 465     ALA D   361                                                      
REMARK 465     LEU D   362                                                      
REMARK 465     GLU D   363                                                      
REMARK 465     GLU D   364                                                      
REMARK 465     ARG D   365                                                      
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  18    CG   CD   CE   NZ                                   
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     LYS C 195    CG   CD   CE   NZ                                   
REMARK 470     GLN C 258    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 278    CG   CD   CE   NZ                                   
REMARK 470     GLU C 294    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 329    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 198    CG   CD   CE   NZ                                   
REMARK 470     GLN D 258    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 329    CG   CD   NE   CZ   NH1  NH2                        
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  41     -160.24   -163.56                                   
REMARK 500    GLU A  59      162.78    169.42                                   
REMARK 500    ARG A  60      117.20    -33.99                                   
REMARK 500    ASP A  90       -5.06    -58.57                                   
REMARK 500    TYR A 111       58.55    -94.35                                   
REMARK 500    THR A 112       -7.36    -28.19                                   
REMARK 500    SER A 128       -9.62    -58.44                                   
REMARK 500    ASP B  41     -160.54   -162.80                                   
REMARK 500    GLU B  59      162.73    169.41                                   
REMARK 500    ARG B  60      118.62    -33.74                                   
REMARK 500    LEU B  83      163.98    179.61                                   
REMARK 500    THR B 112       -6.26    -30.64                                   
REMARK 500    TYR B 124     -179.99    -67.00                                   
REMARK 500    LYS C 160       32.11    -83.35                                   
REMARK 500    ALA C 171      -23.41     76.98                                   
REMARK 500    GLN C 185      121.57    -37.72                                   
REMARK 500    SER C 219       68.94     38.57                                   
REMARK 500    ASN C 234     -166.23   -128.57                                   
REMARK 500    SER C 271     -175.78    -58.86                                   
REMARK 500    SER C 281      124.62    177.82                                   
REMARK 500    ASN C 296     -148.47   -177.61                                   
REMARK 500    ASN C 330       76.98     36.59                                   
REMARK 500    ASN C 345     -167.13   -119.72                                   
REMARK 500    ALA C 354      149.94   -174.96                                   
REMARK 500    ALA D 171      -27.34     77.80                                   
REMARK 500    SER D 219       76.32     33.31                                   
REMARK 500    ASN D 234     -166.24   -129.47                                   
REMARK 500    SER D 271     -174.23    -62.50                                   
REMARK 500    SER D 281      127.80    178.69                                   
REMARK 500    ASP D 282      -70.32    -64.60                                   
REMARK 500    ASN D 330       77.99     35.79                                   
REMARK 500    ASN D 345     -167.67   -122.91                                   
REMARK 500    ALA D 354      148.88   -173.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B 112        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UAP A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDS A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDS A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDU A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UAP B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDS B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDS B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN B 306                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1CVS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FGF2-FGFR1 COMPLEX                              
DBREF  1FQ9 A   15   146  UNP    P09038   FGF2_HUMAN      24    155             
DBREF  1FQ9 B   15   146  UNP    P09038   FGF2_HUMAN      24    155             
DBREF  1FQ9 C  141   365  UNP    P11362   FGR1_HUMAN     141    365             
DBREF  1FQ9 D  141   365  UNP    P11362   FGR1_HUMAN     141    365             
SEQADV 1FQ9 SER A   69  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1FQ9 SER A   87  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1FQ9 SER B   69  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1FQ9 SER B   87  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1FQ9 GLN C  185  UNP  P11362    ASN   185 ENGINEERED                     
SEQADV 1FQ9 GLN D  185  UNP  P11362    ASN   185 ENGINEERED                     
SEQRES   1 A  132  GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN          
SEQRES   2 A  132  GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL          
SEQRES   3 A  132  ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU          
SEQRES   4 A  132  GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS          
SEQRES   5 A  132  GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP          
SEQRES   6 A  132  GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS          
SEQRES   7 A  132  PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR          
SEQRES   8 A  132  TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU          
SEQRES   9 A  132  LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY          
SEQRES  10 A  132  PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA          
SEQRES  11 A  132  LYS SER                                                      
SEQRES   1 B  132  GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN          
SEQRES   2 B  132  GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL          
SEQRES   3 B  132  ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU          
SEQRES   4 B  132  GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS          
SEQRES   5 B  132  GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP          
SEQRES   6 B  132  GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS          
SEQRES   7 B  132  PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR          
SEQRES   8 B  132  TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU          
SEQRES   9 B  132  LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY          
SEQRES  10 B  132  PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA          
SEQRES  11 B  132  LYS SER                                                      
SEQRES   1 C  225  THR ASP ASN THR LYS PRO ASN ARG MET PRO VAL ALA PRO          
SEQRES   2 C  225  TYR TRP THR SER PRO GLU LYS MET GLU LYS LYS LEU HIS          
SEQRES   3 C  225  ALA VAL PRO ALA ALA LYS THR VAL LYS PHE LYS CYS PRO          
SEQRES   4 C  225  SER SER GLY THR PRO GLN PRO THR LEU ARG TRP LEU LYS          
SEQRES   5 C  225  ASN GLY LYS GLU PHE LYS PRO ASP HIS ARG ILE GLY GLY          
SEQRES   6 C  225  TYR LYS VAL ARG TYR ALA THR TRP SER ILE ILE MET ASP          
SEQRES   7 C  225  SER VAL VAL PRO SER ASP LYS GLY ASN TYR THR CYS ILE          
SEQRES   8 C  225  VAL GLU ASN GLU TYR GLY SER ILE ASN HIS THR TYR GLN          
SEQRES   9 C  225  LEU ASP VAL VAL GLU ARG SER PRO HIS ARG PRO ILE LEU          
SEQRES  10 C  225  GLN ALA GLY LEU PRO ALA ASN LYS THR VAL ALA LEU GLY          
SEQRES  11 C  225  SER ASN VAL GLU PHE MET CYS LYS VAL TYR SER ASP PRO          
SEQRES  12 C  225  GLN PRO HIS ILE GLN TRP LEU LYS HIS ILE GLU VAL ASN          
SEQRES  13 C  225  GLY SER LYS ILE GLY PRO ASP ASN LEU PRO TYR VAL GLN          
SEQRES  14 C  225  ILE LEU LYS THR ALA GLY VAL ASN THR THR ASP LYS GLU          
SEQRES  15 C  225  MET GLU VAL LEU HIS LEU ARG ASN VAL SER PHE GLU ASP          
SEQRES  16 C  225  ALA GLY GLU TYR THR CYS LEU ALA GLY ASN SER ILE GLY          
SEQRES  17 C  225  LEU SER HIS HIS SER ALA TRP LEU THR VAL LEU GLU ALA          
SEQRES  18 C  225  LEU GLU GLU ARG                                              
SEQRES   1 D  225  THR ASP ASN THR LYS PRO ASN ARG MET PRO VAL ALA PRO          
SEQRES   2 D  225  TYR TRP THR SER PRO GLU LYS MET GLU LYS LYS LEU HIS          
SEQRES   3 D  225  ALA VAL PRO ALA ALA LYS THR VAL LYS PHE LYS CYS PRO          
SEQRES   4 D  225  SER SER GLY THR PRO GLN PRO THR LEU ARG TRP LEU LYS          
SEQRES   5 D  225  ASN GLY LYS GLU PHE LYS PRO ASP HIS ARG ILE GLY GLY          
SEQRES   6 D  225  TYR LYS VAL ARG TYR ALA THR TRP SER ILE ILE MET ASP          
SEQRES   7 D  225  SER VAL VAL PRO SER ASP LYS GLY ASN TYR THR CYS ILE          
SEQRES   8 D  225  VAL GLU ASN GLU TYR GLY SER ILE ASN HIS THR TYR GLN          
SEQRES   9 D  225  LEU ASP VAL VAL GLU ARG SER PRO HIS ARG PRO ILE LEU          
SEQRES  10 D  225  GLN ALA GLY LEU PRO ALA ASN LYS THR VAL ALA LEU GLY          
SEQRES  11 D  225  SER ASN VAL GLU PHE MET CYS LYS VAL TYR SER ASP PRO          
SEQRES  12 D  225  GLN PRO HIS ILE GLN TRP LEU LYS HIS ILE GLU VAL ASN          
SEQRES  13 D  225  GLY SER LYS ILE GLY PRO ASP ASN LEU PRO TYR VAL GLN          
SEQRES  14 D  225  ILE LEU LYS THR ALA GLY VAL ASN THR THR ASP LYS GLU          
SEQRES  15 D  225  MET GLU VAL LEU HIS LEU ARG ASN VAL SER PHE GLU ASP          
SEQRES  16 D  225  ALA GLY GLU TYR THR CYS LEU ALA GLY ASN SER ILE GLY          
SEQRES  17 D  225  LEU SER HIS HIS SER ALA TRP LEU THR VAL LEU GLU ALA          
SEQRES  18 D  225  LEU GLU GLU ARG                                              
HET    UAP  A 301      15                                                       
HET    SGN  A 302      20                                                       
HET    IDS  A 303      15                                                       
HET    SGN  A 304      20                                                       
HET    IDS  A 305      15                                                       
HET    SGN  A 306      20                                                       
HET    IDU  A 307      15                                                       
HET    SGN  A 308      20                                                       
HET    UAP  B 301      15                                                       
HET    SGN  B 302      20                                                       
HET    IDS  B 303      15                                                       
HET    SGN  B 304      20                                                       
HET    IDS  B 305      15                                                       
HET    SGN  B 306      20                                                       
HETNAM     UAP 1,4-DIDEOXY-5-DEHYDRO-O2-SULFO-GLUCURONIC ACID                   
HETNAM     SGN N,O6-DISULFO-GLUCOSAMINE                                         
HETNAM     IDS 2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID                            
HETNAM     IDU 2-O-SULFO-BETA-L-ALTROPYRANURONIC ACID                           
HETSYN     IDS O2-SULFO-GLUCURONIC ACID                                         
FORMUL   5  UAP    2(C6 H8 O8 S)                                                
FORMUL   5  SGN    7(C6 H13 N O11 S2)                                           
FORMUL   5  IDS    4(C6 H10 O10 S)                                              
FORMUL   5  IDU    C6 H10 O10 S                                                 
HELIX    1   1 LEU A  126  THR A  130  5                                   5    
HELIX    2   2 LEU B  126  THR B  130  5                                   5    
HELIX    3   3 SER C  157  GLU C  162  5                                   6    
HELIX    4   4 LYS C  198  ARG C  202  5                                   5    
HELIX    5   5 TYR C  210  THR C  212  5                                   3    
HELIX    6   6 VAL C  221  LYS C  225  5                                   5    
HELIX    7   7 THR C  319  GLU C  324  1                                   6    
HELIX    8   8 SER D  157  GLU D  162  5                                   6    
HELIX    9   9 LYS D  198  ARG D  202  5                                   5    
HELIX   10  10 TYR D  210  THR D  212  5                                   3    
HELIX   11  11 VAL D  221  LYS D  225  5                                   5    
HELIX   12  12 THR D  319  GLU D  324  1                                   6    
SHEET    1   A 4 VAL A  40  VAL A  43  0                                        
SHEET    2   A 4 PHE A  30  ILE A  34 -1  N  PHE A  31   O  VAL A  43           
SHEET    3   A 4 LYS A  21  CYS A  25 -1  O  LEU A  23   N  LEU A  32           
SHEET    4   A 4 PHE A 139  SER A 143 -1  N  LEU A 140   O  TYR A  24           
SHEET    1   B 4 LEU A  53  GLU A  59  0                                        
SHEET    2   B 4 VAL A  62  GLY A  67 -1  N  VAL A  62   O  GLU A  59           
SHEET    3   B 4 ARG A  72  MET A  76 -1  O  ARG A  72   N  GLY A  67           
SHEET    4   B 4 LEU A  82  SER A  85 -1  O  LEU A  83   N  ALA A  75           
SHEET    1   C 4 LEU A  53  GLU A  59  0                                        
SHEET    2   C 4 VAL A  62  GLY A  67 -1  N  VAL A  62   O  GLU A  59           
SHEET    3   C 4 PHE A  94  LEU A  98 -1  O  PHE A  94   N  VAL A  63           
SHEET    4   C 4 ASN A 104  SER A 108 -1  O  THR A 105   N  ARG A  97           
SHEET    1   D 4 VAL B  40  VAL B  43  0                                        
SHEET    2   D 4 PHE B  30  ILE B  34 -1  N  PHE B  31   O  VAL B  43           
SHEET    3   D 4 LYS B  21  CYS B  25 -1  O  LEU B  23   N  LEU B  32           
SHEET    4   D 4 PHE B 139  SER B 143 -1  N  LEU B 140   O  TYR B  24           
SHEET    1   E 4 LEU B  53  GLU B  59  0                                        
SHEET    2   E 4 VAL B  62  GLY B  67 -1  N  VAL B  62   O  GLU B  59           
SHEET    3   E 4 ARG B  72  MET B  76 -1  O  ARG B  72   N  GLY B  67           
SHEET    4   E 4 LEU B  82  SER B  85 -1  O  LEU B  83   N  ALA B  75           
SHEET    1   F 4 LEU B  53  GLU B  59  0                                        
SHEET    2   F 4 VAL B  62  GLY B  67 -1  N  VAL B  62   O  GLU B  59           
SHEET    3   F 4 PHE B  94  LEU B  98 -1  O  PHE B  94   N  VAL B  63           
SHEET    4   F 4 ASN B 104  SER B 108 -1  N  THR B 105   O  ARG B  97           
SHEET    1   G 2 TYR C 154  TRP C 155  0                                        
SHEET    2   G 2 SER C 180  SER C 181 -1  O  SER C 181   N  TYR C 154           
SHEET    1   H 5 LEU C 165  PRO C 169  0                                        
SHEET    2   H 5 GLY C 237  VAL C 248  1  O  GLN C 244   N  HIS C 166           
SHEET    3   H 5 GLY C 226  ASN C 234 -1  O  GLY C 226   N  LEU C 245           
SHEET    4   H 5 THR C 187  LYS C 192 -1  N  THR C 187   O  GLU C 233           
SHEET    5   H 5 LYS C 195  GLU C 196 -1  O  LYS C 195   N  LYS C 192           
SHEET    1   I 3 VAL C 174  LYS C 177  0                                        
SHEET    2   I 3 SER C 214  MET C 217 -1  N  ILE C 215   O  PHE C 176           
SHEET    3   I 3 LYS C 207  ARG C 209 -1  O  LYS C 207   N  ILE C 216           
SHEET    1   J 2 ILE C 256  LEU C 257  0                                        
SHEET    2   J 2 VAL C 279  TYR C 280 -1  O  TYR C 280   N  ILE C 256           
SHEET    1   K 5 LYS C 265  VAL C 267  0                                        
SHEET    2   K 5 LEU C 349  VAL C 358  1  O  TRP C 355   N  LYS C 265           
SHEET    3   K 5 GLY C 337  GLY C 344 -1  O  GLY C 337   N  LEU C 356           
SHEET    4   K 5 HIS C 286  HIS C 292 -1  N  HIS C 286   O  GLY C 344           
SHEET    5   K 5 VAL C 308  THR C 313 -1  N  GLN C 309   O  LYS C 291           
SHEET    1   L 2 VAL C 273  MET C 276  0                                        
SHEET    2   L 2 VAL C 325  LEU C 328 -1  O  LEU C 326   N  PHE C 275           
SHEET    1   M 2 TYR D 154  TRP D 155  0                                        
SHEET    2   M 2 SER D 180  SER D 181 -1  O  SER D 181   N  TYR D 154           
SHEET    1   N 5 LEU D 165  PRO D 169  0                                        
SHEET    2   N 5 GLY D 237  VAL D 248  1  O  GLN D 244   N  HIS D 166           
SHEET    3   N 5 GLY D 226  ASN D 234 -1  O  GLY D 226   N  LEU D 245           
SHEET    4   N 5 THR D 187  LYS D 192 -1  N  THR D 187   O  GLU D 233           
SHEET    5   N 5 LYS D 195  GLU D 196 -1  O  LYS D 195   N  LYS D 192           
SHEET    1   O 3 VAL D 174  LYS D 177  0                                        
SHEET    2   O 3 SER D 214  MET D 217 -1  N  ILE D 215   O  PHE D 176           
SHEET    3   O 3 TYR D 206  ARG D 209 -1  O  LYS D 207   N  ILE D 216           
SHEET    1   P 2 ILE D 256  LEU D 257  0                                        
SHEET    2   P 2 VAL D 279  TYR D 280 -1  O  TYR D 280   N  ILE D 256           
SHEET    1   Q 5 LYS D 265  VAL D 267  0                                        
SHEET    2   Q 5 LEU D 349  VAL D 358  1  O  TRP D 355   N  LYS D 265           
SHEET    3   Q 5 GLY D 337  GLY D 344 -1  O  GLY D 337   N  LEU D 356           
SHEET    4   Q 5 HIS D 286  LYS D 291 -1  N  HIS D 286   O  GLY D 344           
SHEET    5   Q 5 GLN D 309  THR D 313 -1  N  GLN D 309   O  LYS D 291           
SHEET    1   R 2 VAL D 273  MET D 276  0                                        
SHEET    2   R 2 VAL D 325  LEU D 328 -1  N  LEU D 326   O  PHE D 275           
SSBOND   1 CYS C  178    CYS C  230                          1555   1555  2.04  
SSBOND   2 CYS C  277    CYS C  341                          1555   1555  2.01  
SSBOND   3 CYS D  178    CYS D  230                          1555   1555  2.02  
SSBOND   4 CYS D  277    CYS D  341                          1555   1555  2.03  
LINK         C1  UAP B 301                 O4  SGN B 302     1555   1555  1.40  
LINK         O4  SGN A 302                 C1  UAP A 301     1555   1555  1.43  
LINK         C4  IDU A 307                 O1  SGN A 306     1555   1555  1.45  
LINK         C1  IDU A 307                 O4  SGN A 308     1555   1555  1.45  
LINK         O1  SGN A 302                 C4  IDS A 303     1555   1555  1.42  
LINK         C1  IDS A 303                 O4  SGN A 304     1555   1555  1.40  
LINK         O1  SGN A 304                 C4  IDS A 305     1555   1555  1.42  
LINK         C1  IDS A 305                 O4  SGN A 306     1555   1555  1.40  
LINK         O1  SGN B 302                 C4  IDS B 303     1555   1555  1.43  
LINK         C1  IDS B 303                 O4  SGN B 304     1555   1555  1.42  
LINK         O1  SGN B 304                 C4  IDS B 305     1555   1555  1.43  
LINK         C1  IDS B 305                 O4  SGN B 306     1555   1555  1.43  
CISPEP   1 THR C  183    PRO C  184          0        -0.23                     
CISPEP   2 LEU C  261    PRO C  262          0         0.11                     
CISPEP   3 THR D  183    PRO D  184          0        -0.20                     
CISPEP   4 LEU D  261    PRO D  262          0         0.23                     
SITE     1 AC1  8 SGN A 302  THR C 173  LYS C 175  LYS C 177                    
SITE     2 AC1  8 THR D 173  LYS D 207  ILE D 216  ASP D 218                    
SITE     1 AC2  6 UAP A 301  IDS A 303  LYS C 160  LYS C 163                    
SITE     2 AC2  6 LYS C 177  LYS D 207                                          
SITE     1 AC3  6 ASN A  27  ARG A 120  LYS A 135  SGN A 302                    
SITE     2 AC3  6 SGN A 304  LYS D 207                                          
SITE     1 AC4 10 ASN A  27  ARG A 120  LYS A 125  GLN A 134                    
SITE     2 AC4 10 LYS A 135  ALA A 136  IDS A 303  IDS A 305                    
SITE     3 AC4 10 TYR D 206  LYS D 207                                          
SITE     1 AC5  6 ASN A  27  LYS A 119  ARG A 120  LYS A 125                    
SITE     2 AC5  6 SGN A 304  SGN A 306                                          
SITE     1 AC6  6 LYS A 119  LYS A 129  IDS A 305  IDU A 307                    
SITE     2 AC6  6 LYS B  77  SER B  87                                          
SITE     1 AC7  5 SGN A 306  SGN A 308  ARG B  72  SER B  85                    
SITE     2 AC7  5 LYS B  86                                                     
SITE     1 AC8  1 IDU A 307                                                     
SITE     1 AC9  6 SGN B 302  LYS C 207  ILE C 216  LYS D 172                    
SITE     2 AC9  6 THR D 173  LYS D 175                                          
SITE     1 BC1  8 LYS B 135  UAP B 301  IDS B 303  LYS C 207                    
SITE     2 BC1  8 LYS D 160  LYS D 163  LYS D 172  LYS D 177                    
SITE     1 BC2  6 ARG B 120  LYS B 135  SGN B 302  SGN B 304                    
SITE     2 BC2  6 LYS C 207  ARG C 209                                          
SITE     1 BC3  8 ASN B  27  ARG B 120  GLN B 134  LYS B 135                    
SITE     2 BC3  8 ALA B 136  IDS B 303  IDS B 305  ARG C 209                    
SITE     1 BC4  5 LYS B 119  ARG B 120  LYS B 125  SGN B 304                    
SITE     2 BC4  5 SGN B 306                                                     
SITE     1 BC5  4 LYS B 119  THR B 121  LYS B 129  IDS B 305                    
CRYST1   98.888   98.888  196.292  90.00  90.00  90.00 P 41 21 2    16          
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      0.010112  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005094        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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