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Database: PDB
Entry: 3F1R
LinkDB: 3F1R
Original site: 3F1R 
HEADER    HORMONE                                 28-OCT-08   3F1R              
TITLE     CRYSTAL STRUCTURE OF FGF20 DIMER                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR 20;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FGF-20;                                                     
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FGF20;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BLR (DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24A                                
KEYWDS    BETA-TREFOIL FOLD, GROWTH FACTOR, POLYMORPHISM, SECRETED,             
KEYWDS   2 HORMONE                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KALININA,M.MOHAMMADI                                                
REVDAT   2   01-SEP-09 3F1R    1       JRNL                                     
REVDAT   1   28-JUL-09 3F1R    0                                                
JRNL        AUTH   J.KALININA,S.A.BYRON,H.P.MAKARENKOVA,S.K.OLSEN,              
JRNL        AUTH 2 A.V.ELISEENKOVA,W.J.LAROCHELLE,M.DHANABAL,S.BLAIS,           
JRNL        AUTH 3 D.M.ORNITZ,L.A.DAY,T.A.NEUBERT,P.M.POLLOCK,                  
JRNL        AUTH 4 M.MOHAMMADI                                                  
JRNL        TITL   HOMODIMERIZATION CONTROLS THE FIBROBLAST GROWTH              
JRNL        TITL 2 FACTOR 9 SUBFAMILY'S RECEPTOR BINDING AND HEPARAN            
JRNL        TITL 3 SULFATE-DEPENDENT DIFFUSION IN THE EXTRACELLULAR             
JRNL        TITL 4 MATRIX                                                       
JRNL        REF    MOL.CELL.BIOL.                V.  29  4663 2009              
JRNL        REFN                   ISSN 0270-7306                               
JRNL        PMID   19564416                                                     
JRNL        DOI    10.1128/MCB.01780-08                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.58                          
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)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 14309                          
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) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 680                             
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            : 2510                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 9                                       
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) : 40.82300                                             
REMARK   3    B22 (A**2) : 40.82300                                             
REMARK   3    B33 (A**2) : -81.64700                                            
REMARK   3    B12 (A**2) : 14.19500                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.43                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.77                            
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 3F1R COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050037.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : KOHZU DOUBLE CRYSTAL               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16050                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1IHK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.2M LI2SO4, 15%          
REMARK 280  GLYCEROL, 13% PEG 2000, PH 8.5, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.07200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       29.48643            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.93333            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       51.07200            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       29.48643            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       39.93333            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       51.07200            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       29.48643            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.93333            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       58.97287            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       79.86667            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       58.97287            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       79.86667            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       58.97287            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       79.86667            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     GLN A    20                                                      
REMARK 465     VAL A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     HIS A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     LEU A    36                                                      
REMARK 465     LEU A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     ARG A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     GLU A    45                                                      
REMARK 465     ARG A    46                                                      
REMARK 465     SER A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ARG A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     MET A   209                                                      
REMARK 465     TYR A   210                                                      
REMARK 465     THR A   211                                                      
REMARK 465     MET B  1001                                                      
REMARK 465     ALA B  1002                                                      
REMARK 465     PRO B  1003                                                      
REMARK 465     LEU B  1004                                                      
REMARK 465     ALA B  1005                                                      
REMARK 465     GLU B  1006                                                      
REMARK 465     VAL B  1007                                                      
REMARK 465     GLY B  1008                                                      
REMARK 465     GLY B  1009                                                      
REMARK 465     PHE B  1010                                                      
REMARK 465     LEU B  1011                                                      
REMARK 465     GLY B  1012                                                      
REMARK 465     GLY B  1013                                                      
REMARK 465     LEU B  1014                                                      
REMARK 465     GLU B  1015                                                      
REMARK 465     GLY B  1016                                                      
REMARK 465     LEU B  1017                                                      
REMARK 465     GLY B  1018                                                      
REMARK 465     GLN B  1019                                                      
REMARK 465     GLN B  1020                                                      
REMARK 465     VAL B  1021                                                      
REMARK 465     GLY B  1022                                                      
REMARK 465     SER B  1023                                                      
REMARK 465     HIS B  1024                                                      
REMARK 465     PHE B  1025                                                      
REMARK 465     LEU B  1026                                                      
REMARK 465     LEU B  1027                                                      
REMARK 465     PRO B  1028                                                      
REMARK 465     PRO B  1029                                                      
REMARK 465     ALA B  1030                                                      
REMARK 465     GLY B  1031                                                      
REMARK 465     GLU B  1032                                                      
REMARK 465     ARG B  1033                                                      
REMARK 465     PRO B  1034                                                      
REMARK 465     PRO B  1035                                                      
REMARK 465     LEU B  1036                                                      
REMARK 465     LEU B  1037                                                      
REMARK 465     GLY B  1038                                                      
REMARK 465     GLU B  1039                                                      
REMARK 465     ARG B  1040                                                      
REMARK 465     ARG B  1041                                                      
REMARK 465     SER B  1042                                                      
REMARK 465     ALA B  1043                                                      
REMARK 465     ALA B  1044                                                      
REMARK 465     GLU B  1045                                                      
REMARK 465     ARG B  1046                                                      
REMARK 465     SER B  1047                                                      
REMARK 465     ALA B  1048                                                      
REMARK 465     ARG B  1049                                                      
REMARK 465     GLY B  1050                                                      
REMARK 465     GLY B  1051                                                      
REMARK 465     MET B  1209                                                      
REMARK 465     TYR B  1210                                                      
REMARK 465     THR B  1211                                                      
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     PRO A  52    CG   CD                                             
REMARK 470     GLN A  56    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B1052    CG   CD                                             
REMARK 470     GLN B1056    CG   CD   OE1  NE2                                  
REMARK 470     GLU B1145    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1163    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    ALA A  54      -94.88     76.69                                   
REMARK 500    ARG A  72       -7.91    -54.58                                   
REMARK 500    GLU A 144      -47.26   -130.02                                   
REMARK 500    GLU A 145      119.77    167.26                                   
REMARK 500    ASN A 146       35.22     71.54                                   
REMARK 500    ASN A 170     -178.85    -67.55                                   
REMARK 500    VAL A 200       56.02   -145.24                                   
REMARK 500    ALA B1054      -86.66     83.17                                   
REMARK 500    GLU B1145      122.04    167.72                                   
REMARK 500    ASN B1146       35.14     71.25                                   
REMARK 500    ASN B1170     -178.65    -69.29                                   
REMARK 500    VAL B1200       55.60   -146.13                                   
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 SO4 A 301                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 300                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IHK   RELATED DB: PDB                                   
REMARK 900 FGF9 CRYSTAL STRUCTURE                                               
REMARK 900 RELATED ID: 1G82   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF FIBROBLAST GROWTH FACTOR 9                              
DBREF  3F1R A    1   211  UNP    Q9NP95   FGF20_HUMAN      1    211             
DBREF  3F1R B 1001  1211  UNP    Q9NP95   FGF20_HUMAN      1    211             
SEQRES   1 A  211  MET ALA PRO LEU ALA GLU VAL GLY GLY PHE LEU GLY GLY          
SEQRES   2 A  211  LEU GLU GLY LEU GLY GLN GLN VAL GLY SER HIS PHE LEU          
SEQRES   3 A  211  LEU PRO PRO ALA GLY GLU ARG PRO PRO LEU LEU GLY GLU          
SEQRES   4 A  211  ARG ARG SER ALA ALA GLU ARG SER ALA ARG GLY GLY PRO          
SEQRES   5 A  211  GLY ALA ALA GLN LEU ALA HIS LEU HIS GLY ILE LEU ARG          
SEQRES   6 A  211  ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU GLN          
SEQRES   7 A  211  ILE LEU PRO ASP GLY SER VAL GLN GLY THR ARG GLN ASP          
SEQRES   8 A  211  HIS SER LEU PHE GLY ILE LEU GLU PHE ILE SER VAL ALA          
SEQRES   9 A  211  VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY LEU          
SEQRES  10 A  211  TYR LEU GLY MET ASN ASP LYS GLY GLU LEU TYR GLY SER          
SEQRES  11 A  211  GLU LYS LEU THR SER GLU CYS ILE PHE ARG GLU GLN PHE          
SEQRES  12 A  211  GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN ILE TYR          
SEQRES  13 A  211  LYS HIS GLY ASP THR GLY ARG ARG TYR PHE VAL ALA LEU          
SEQRES  14 A  211  ASN LYS ASP GLY THR PRO ARG ASP GLY ALA ARG SER LYS          
SEQRES  15 A  211  ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO VAL          
SEQRES  16 A  211  ASP PRO GLU ARG VAL PRO GLU LEU TYR LYS ASP LEU LEU          
SEQRES  17 A  211  MET TYR THR                                                  
SEQRES   1 B  211  MET ALA PRO LEU ALA GLU VAL GLY GLY PHE LEU GLY GLY          
SEQRES   2 B  211  LEU GLU GLY LEU GLY GLN GLN VAL GLY SER HIS PHE LEU          
SEQRES   3 B  211  LEU PRO PRO ALA GLY GLU ARG PRO PRO LEU LEU GLY GLU          
SEQRES   4 B  211  ARG ARG SER ALA ALA GLU ARG SER ALA ARG GLY GLY PRO          
SEQRES   5 B  211  GLY ALA ALA GLN LEU ALA HIS LEU HIS GLY ILE LEU ARG          
SEQRES   6 B  211  ARG ARG GLN LEU TYR CYS ARG THR GLY PHE HIS LEU GLN          
SEQRES   7 B  211  ILE LEU PRO ASP GLY SER VAL GLN GLY THR ARG GLN ASP          
SEQRES   8 B  211  HIS SER LEU PHE GLY ILE LEU GLU PHE ILE SER VAL ALA          
SEQRES   9 B  211  VAL GLY LEU VAL SER ILE ARG GLY VAL ASP SER GLY LEU          
SEQRES  10 B  211  TYR LEU GLY MET ASN ASP LYS GLY GLU LEU TYR GLY SER          
SEQRES  11 B  211  GLU LYS LEU THR SER GLU CYS ILE PHE ARG GLU GLN PHE          
SEQRES  12 B  211  GLU GLU ASN TRP TYR ASN THR TYR SER SER ASN ILE TYR          
SEQRES  13 B  211  LYS HIS GLY ASP THR GLY ARG ARG TYR PHE VAL ALA LEU          
SEQRES  14 B  211  ASN LYS ASP GLY THR PRO ARG ASP GLY ALA ARG SER LYS          
SEQRES  15 B  211  ARG HIS GLN LYS PHE THR HIS PHE LEU PRO ARG PRO VAL          
SEQRES  16 B  211  ASP PRO GLU ARG VAL PRO GLU LEU TYR LYS ASP LEU LEU          
SEQRES  17 B  211  MET TYR THR                                                  
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    SO4  B 300       5                                                       
HET    SO4  B 304       5                                                       
HET    SO4  B 305       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    6(O4 S 2-)                                                   
FORMUL   9  HOH   *9(H2 O)                                                      
HELIX    1   1 ALA A   55  ARG A   65  1                                  11    
HELIX    2   2 THR A  134  CYS A  137  5                                   4    
HELIX    3   3 ASP A  177  SER A  181  5                                   5    
HELIX    4   4 GLN A  185  THR A  188  5                                   4    
HELIX    5   5 ASP A  196  TYR A  204  5                                   9    
HELIX    6   6 ALA B 1055  ARG B 1065  1                                  11    
HELIX    7   7 THR B 1134  CYS B 1137  5                                   4    
HELIX    8   8 ASP B 1177  SER B 1181  5                                   5    
HELIX    9   9 GLN B 1185  THR B 1188  5                                   4    
HELIX   10  10 ASP B 1196  TYR B 1204  5                                   9    
SHEET    1   A 8 VAL A  85  THR A  88  0                                        
SHEET    2   A 8 PHE A  75  ILE A  79 -1  N  HIS A  76   O  THR A  88           
SHEET    3   A 8 ARG A  66  CYS A  71 -1  N  CYS A  71   O  PHE A  75           
SHEET    4   A 8 ILE A  97  ALA A 104 -1  O  LEU A  98   N  ARG A  67           
SHEET    5   A 8 LEU A 107  GLY A 112 -1  O  ARG A 111   N  GLU A  99           
SHEET    6   A 8 PHE A 139  GLU A 145 -1  O  PHE A 139   N  VAL A 108           
SHEET    7   A 8 TYR A 148  LYS A 157 -1  O  THR A 150   N  GLN A 142           
SHEET    8   A 8 ARG A 164  PHE A 166 -1  O  TYR A 165   N  SER A 153           
SHEET    1   B 6 VAL A  85  THR A  88  0                                        
SHEET    2   B 6 PHE A  75  ILE A  79 -1  N  HIS A  76   O  THR A  88           
SHEET    3   B 6 ARG A  66  CYS A  71 -1  N  CYS A  71   O  PHE A  75           
SHEET    4   B 6 PHE A 190  ARG A 193 -1  O  ARG A 193   N  GLN A  68           
SHEET    5   B 6 TYR A 148  LYS A 157 -1  N  ASN A 149   O  PHE A 190           
SHEET    6   B 6 ARG A 164  PHE A 166 -1  O  TYR A 165   N  SER A 153           
SHEET    1   C 2 TYR A 118  MET A 121  0                                        
SHEET    2   C 2 LEU A 127  SER A 130 -1  O  SER A 130   N  TYR A 118           
SHEET    1   D 8 VAL B1085  THR B1088  0                                        
SHEET    2   D 8 PHE B1075  ILE B1079 -1  N  HIS B1076   O  THR B1088           
SHEET    3   D 8 ARG B1066  CYS B1071 -1  N  CYS B1071   O  PHE B1075           
SHEET    4   D 8 ILE B1097  ALA B1104 -1  O  LEU B1098   N  ARG B1067           
SHEET    5   D 8 LEU B1107  GLY B1112 -1  O  ARG B1111   N  GLU B1099           
SHEET    6   D 8 PHE B1139  GLU B1145 -1  O  PHE B1139   N  VAL B1108           
SHEET    7   D 8 TYR B1148  LYS B1157 -1  O  SER B1152   N  ARG B1140           
SHEET    8   D 8 ARG B1164  PHE B1166 -1  O  TYR B1165   N  SER B1153           
SHEET    1   E 6 VAL B1085  THR B1088  0                                        
SHEET    2   E 6 PHE B1075  ILE B1079 -1  N  HIS B1076   O  THR B1088           
SHEET    3   E 6 ARG B1066  CYS B1071 -1  N  CYS B1071   O  PHE B1075           
SHEET    4   E 6 PHE B1190  ARG B1193 -1  O  ARG B1193   N  GLN B1068           
SHEET    5   E 6 TYR B1148  LYS B1157 -1  N  ASN B1149   O  PHE B1190           
SHEET    6   E 6 ARG B1164  PHE B1166 -1  O  TYR B1165   N  SER B1153           
SHEET    1   F 2 TYR B1118  MET B1121  0                                        
SHEET    2   F 2 LEU B1127  SER B1130 -1  O  SER B1130   N  TYR B1118           
SITE     1 AC1  3 ARG A 140  LYS A 157  ARG A 164                               
SITE     1 AC2  4 ARG A 163  ARG A 164  ARG A 180  ARG A 183                    
SITE     1 AC3  2 ARG A 180  LYS A 182                                          
SITE     1 AC4  4 ARG B1163  ARG B1164  ARG B1180  ARG B1183                    
SITE     1 AC5  3 ARG B1176  ARG B1180  LYS B1182                               
SITE     1 AC6  3 ARG B1140  LYS B1157  ARG B1164                               
CRYST1  102.144  102.144  119.800  90.00  90.00 120.00 H 3          18          
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      0.009790  0.005652  0.000000        0.00000                         
SCALE2      0.000000  0.011305  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008347        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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