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Database: PDB
Entry: 1IIL
LinkDB: 1IIL
Original site: 1IIL 
HEADER    GROWTH FACTOR/GROWTH FACTOR RECEPTOR    23-APR-01   1IIL              
TITLE     CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2            
TITLE    2 (FGFR2) IN COMPLEX WITH FGF2                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 2;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: FGF2, HBGF-2, BASIC FIBROBLAST GROWTH FACTOR,               
COMPND   5 BFGF;                                                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;                       
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: EXTRACELLULAR LIGAND BINDING DOMAIN CONSISTING             
COMPND  12 OF IG-LIKE DOMAINS II (D2) AND III (D3), RESIDUES 147-366;           
COMPND  13 SYNONYM: FGFR2, KERATINOCYTE GROWTH FACTOR RECEPTOR;                 
COMPND  14 EC: 2.7.1.112;                                                       
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 BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET-28A;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET-28A                                   
KEYWDS    IMMUNOGLOBULIN LIKE DOMAIN, B-TREFOIL, GROWTH FACTOR/GROWTH           
KEYWDS   2 FACTOR RECEPTOR COMPLEX                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.A.IBRAHIMI,A.V.ELISEENKOVA,A.N.PLOTNIKOV,D.M.ORNITZ,                
AUTHOR   2 M.MOHAMMADI                                                          
REVDAT   3   24-FEB-09 1IIL    1       VERSN                                    
REVDAT   2   20-JUN-01 1IIL    1       JRNL                                     
REVDAT   1   09-MAY-01 1IIL    0                                                
JRNL        AUTH   O.A.IBRAHIMI,A.V.ELISEENKOVA,A.N.PLOTNIKOV,K.YU,             
JRNL        AUTH 2 D.M.ORNITZ,M.MOHAMMADI                                       
JRNL        TITL   STRUCTURAL BASIS FOR FIBROBLAST GROWTH FACTOR                
JRNL        TITL 2 RECEPTOR 2 ACTIVATION IN APERT SYNDROME.                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  98  7182 2001              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   11390973                                                     
JRNL        DOI    10.1073/PNAS.121183798                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
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)   (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 75473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3824                            
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            : 10600                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 77                                      
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) : 1.44700                                              
REMARK   3    B22 (A**2) : -18.14300                                            
REMARK   3    B33 (A**2) : 16.69500                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.65000                                              
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.41                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
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) : 1.140 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.550 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.390 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS                                                  
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 32.50                                                
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 1IIL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB013302.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.5                                
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) : 0.97624                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 321836                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.770                              
REMARK 200  R MERGE                    (I) : 0.04100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.13700                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1EV2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, HEPES-NAOH,       
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 3050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 2920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
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     ALA A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ILE A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     GLY A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     GLY A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ILE B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     THR B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ASP B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     GLY B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     PHE B    21                                                      
REMARK 465     SER B   155                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ILE C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     THR C     8                                                      
REMARK 465     LEU C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     LEU C    12                                                      
REMARK 465     PRO C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     ASP C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     GLY C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     PHE C    21                                                      
REMARK 465     PRO C    22                                                      
REMARK 465     PRO C    23                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ILE D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     THR D     8                                                      
REMARK 465     LEU D     9                                                      
REMARK 465     PRO D    10                                                      
REMARK 465     ALA D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     PRO D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     ASP D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     GLY D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 465     GLY D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     PHE D    21                                                      
REMARK 465     PRO D    22                                                      
REMARK 465     SER D   155                                                      
REMARK 465     ASN E   147                                                      
REMARK 465     SER E   148                                                      
REMARK 465     ASN E   149                                                      
REMARK 465     GLU E   295                                                      
REMARK 465     LYS E   296                                                      
REMARK 465     ASN E   297                                                      
REMARK 465     GLY E   298                                                      
REMARK 465     SER E   299                                                      
REMARK 465     LYS E   300                                                      
REMARK 465     TYR E   301                                                      
REMARK 465     GLY E   302                                                      
REMARK 465     PRO E   303                                                      
REMARK 465     ASP E   304                                                      
REMARK 465     GLY E   305                                                      
REMARK 465     LEU E   306                                                      
REMARK 465     ALA E   362                                                      
REMARK 465     PRO E   363                                                      
REMARK 465     GLY E   364                                                      
REMARK 465     ARG E   365                                                      
REMARK 465     GLU E   366                                                      
REMARK 465     ASN F   147                                                      
REMARK 465     SER F   148                                                      
REMARK 465     ASN F   149                                                      
REMARK 465     GLU F   295                                                      
REMARK 465     LYS F   296                                                      
REMARK 465     ASN F   297                                                      
REMARK 465     GLY F   298                                                      
REMARK 465     SER F   299                                                      
REMARK 465     LYS F   300                                                      
REMARK 465     TYR F   301                                                      
REMARK 465     GLY F   302                                                      
REMARK 465     PRO F   303                                                      
REMARK 465     ASP F   304                                                      
REMARK 465     GLY F   305                                                      
REMARK 465     LEU F   306                                                      
REMARK 465     ALA F   362                                                      
REMARK 465     PRO F   363                                                      
REMARK 465     GLY F   364                                                      
REMARK 465     ARG F   365                                                      
REMARK 465     GLU F   366                                                      
REMARK 465     ASN G   147                                                      
REMARK 465     SER G   148                                                      
REMARK 465     ASN G   149                                                      
REMARK 465     ARG G   365                                                      
REMARK 465     GLU G   366                                                      
REMARK 465     ASN H   147                                                      
REMARK 465     SER H   148                                                      
REMARK 465     ASN H   149                                                      
REMARK 465     ARG H   365                                                      
REMARK 465     GLU H   366                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  86    CG   CD   CE   NZ                                   
REMARK 470     GLU A  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  95    CG   CD   CE   NZ                                   
REMARK 470     ARG A 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 155    OG                                                  
REMARK 470     LYS B  86    CG   CD   CE   NZ                                   
REMARK 470     GLU B  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  95    CG   CD   CE   NZ                                   
REMARK 470     ARG B 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  55    CG   CD   CE   NZ                                   
REMARK 470     GLU C  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  95    CG   CD   CE   NZ                                   
REMARK 470     LYS C 128    CG   CD   CE   NZ                                   
REMARK 470     ARG C 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C 155    OG                                                  
REMARK 470     LYS D  55    CG   CD   CE   NZ                                   
REMARK 470     LYS D  86    CG   CD   CE   NZ                                   
REMARK 470     GLU D  87    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  95    CG   CD   CE   NZ                                   
REMARK 470     LYS D 128    CG   CD   CE   NZ                                   
REMARK 470     ARG D 129    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN E 150    CG   OD1  ND2                                       
REMARK 470     GLU E 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS E 161    CG   CD   CE   NZ                                   
REMARK 470     GLU E 163    CG   CD   OE1  OE2                                  
REMARK 470     VAL E 269    CG1  CG2                                            
REMARK 470     TYR E 308    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS E 322    CG   CD   CE   NZ                                   
REMARK 470     ARG E 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN E 331    CG   OD1  ND2                                       
REMARK 470     GLU E 335    CG   CD   OE1  OE2                                  
REMARK 470     ASN F 150    CG   OD1  ND2                                       
REMARK 470     GLU F 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS F 161    CG   CD   CE   NZ                                   
REMARK 470     GLU F 163    CG   CD   OE1  OE2                                  
REMARK 470     VAL F 269    CG1  CG2                                            
REMARK 470     TYR F 308    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS F 322    CG   CD   CE   NZ                                   
REMARK 470     ARG F 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN F 331    CG   OD1  ND2                                       
REMARK 470     GLU F 335    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 151    CG   CD   CE   NZ                                   
REMARK 470     GLU G 160    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 269    CG1  CG2                                            
REMARK 470     GLU G 295    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 296    CG   CD   CE   NZ                                   
REMARK 470     LYS G 322    CG   CD   CE   NZ                                   
REMARK 470     GLU G 335    CG   CD   OE1  OE2                                  
REMARK 470     ASN H 150    CG   OD1  ND2                                       
REMARK 470     LYS H 151    CG   CD   CE   NZ                                   
REMARK 470     GLU H 160    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 196    CG   CD   CE   NZ                                   
REMARK 470     VAL H 269    CG1  CG2                                            
REMARK 470     GLU H 295    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 296    CG   CD   CE   NZ                                   
REMARK 470     LYS H 322    CG   CD   CE   NZ                                   
REMARK 470     GLU H 335    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  50     -159.72   -151.78                                   
REMARK 500    TYR A 120       79.92   -107.29                                   
REMARK 500    THR A 121       -1.49    -53.80                                   
REMARK 500    TYR B 120       79.24   -108.18                                   
REMARK 500    THR B 121       -1.82    -53.08                                   
REMARK 500    TYR C 120       79.82   -108.67                                   
REMARK 500    THR C 121        3.05    -57.38                                   
REMARK 500    THR D 121        1.79    -56.61                                   
REMARK 500    ASN E 158       83.05   -152.21                                   
REMARK 500    ALA E 172       -6.43     86.03                                   
REMARK 500    ARG E 253       41.77   -105.62                                   
REMARK 500    TYR E 308      107.55    -51.45                                   
REMARK 500    THR E 320      152.49    -48.42                                   
REMARK 500    ASN F 158       81.67   -152.74                                   
REMARK 500    ALA F 172       -7.24     87.68                                   
REMARK 500    ARG F 253       44.00   -104.62                                   
REMARK 500    TYR F 308      107.63    -51.64                                   
REMARK 500    THR F 320      152.59    -48.60                                   
REMARK 500    ASN G 158       82.43   -151.63                                   
REMARK 500    ALA G 172       -9.69     88.94                                   
REMARK 500    ARG G 253       55.36   -104.00                                   
REMARK 500    ASN G 297     -146.96    142.93                                   
REMARK 500    PRO G 361      173.40    -58.78                                   
REMARK 500    ALA G 362      -95.89    -93.18                                   
REMARK 500    PRO G 363      -97.99   -101.31                                   
REMARK 500    ASN H 158       82.69   -152.08                                   
REMARK 500    ALA H 172       -9.85     89.18                                   
REMARK 500    ARG H 253       57.21   -104.01                                   
REMARK 500    ASN H 297     -146.41    137.96                                   
REMARK 500    THR H 320      152.33    -48.97                                   
REMARK 500    PRO H 361      174.51    -59.26                                   
REMARK 500    ALA H 362     -152.22    -93.03                                   
REMARK 500    PRO H 363     -116.43    -47.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EV2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR          
REMARK 900 LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2)                      
REMARK 900 RELATED ID: 1II4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2           
REMARK 900 (FGFR2) IN COMPLEX WITH FGF2                                         
DBREF  1IIL A    1   155  UNP    P09038   FGF2_HUMAN       1    155             
DBREF  1IIL B    1   155  UNP    P09038   FGF2_HUMAN       1    155             
DBREF  1IIL C    1   155  UNP    P09038   FGF2_HUMAN       1    155             
DBREF  1IIL D    1   155  UNP    P09038   FGF2_HUMAN       1    155             
DBREF  1IIL E  147   366  UNP    P21802   FGR2_HUMAN     147    366             
DBREF  1IIL F  147   366  UNP    P21802   FGR2_HUMAN     147    366             
DBREF  1IIL G  147   366  UNP    P21802   FGR2_HUMAN     147    366             
DBREF  1IIL H  147   366  UNP    P21802   FGR2_HUMAN     147    366             
SEQADV 1IIL SER A   78  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1IIL SER A   96  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1IIL SER B   78  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1IIL SER B   96  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1IIL SER C   78  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1IIL SER C   96  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1IIL SER D   78  UNP  P09038    CYS    78 ENGINEERED                     
SEQADV 1IIL SER D   96  UNP  P09038    CYS    96 ENGINEERED                     
SEQADV 1IIL ARG E  253  UNP  P21802    PRO   253 ENGINEERED                     
SEQADV 1IIL ARG F  253  UNP  P21802    PRO   253 ENGINEERED                     
SEQADV 1IIL ARG G  253  UNP  P21802    PRO   253 ENGINEERED                     
SEQADV 1IIL ARG H  253  UNP  P21802    PRO   253 ENGINEERED                     
SEQRES   1 A  155  MET ALA ALA GLY SER ILE THR THR LEU PRO ALA LEU PRO          
SEQRES   2 A  155  GLU ASP GLY GLY SER GLY ALA PHE PRO PRO GLY HIS PHE          
SEQRES   3 A  155  LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN GLY GLY PHE          
SEQRES   4 A  155  PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL ASP GLY VAL          
SEQRES   5 A  155  ARG GLU LYS SER ASP PRO HIS ILE LYS LEU GLN LEU GLN          
SEQRES   6 A  155  ALA GLU GLU ARG GLY VAL VAL SER ILE LYS GLY VAL SER          
SEQRES   7 A  155  ALA ASN ARG TYR LEU ALA MET LYS GLU ASP GLY ARG LEU          
SEQRES   8 A  155  LEU ALA SER LYS SER VAL THR ASP GLU CYS PHE PHE PHE          
SEQRES   9 A  155  GLU ARG LEU GLU SER ASN ASN TYR ASN THR TYR ARG SER          
SEQRES  10 A  155  ARG LYS TYR THR SER TRP TYR VAL ALA LEU LYS ARG THR          
SEQRES  11 A  155  GLY GLN TYR LYS LEU GLY SER LYS THR GLY PRO GLY GLN          
SEQRES  12 A  155  LYS ALA ILE LEU PHE LEU PRO MET SER ALA LYS SER              
SEQRES   1 B  155  MET ALA ALA GLY SER ILE THR THR LEU PRO ALA LEU PRO          
SEQRES   2 B  155  GLU ASP GLY GLY SER GLY ALA PHE PRO PRO GLY HIS PHE          
SEQRES   3 B  155  LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN GLY GLY PHE          
SEQRES   4 B  155  PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL ASP GLY VAL          
SEQRES   5 B  155  ARG GLU LYS SER ASP PRO HIS ILE LYS LEU GLN LEU GLN          
SEQRES   6 B  155  ALA GLU GLU ARG GLY VAL VAL SER ILE LYS GLY VAL SER          
SEQRES   7 B  155  ALA ASN ARG TYR LEU ALA MET LYS GLU ASP GLY ARG LEU          
SEQRES   8 B  155  LEU ALA SER LYS SER VAL THR ASP GLU CYS PHE PHE PHE          
SEQRES   9 B  155  GLU ARG LEU GLU SER ASN ASN TYR ASN THR TYR ARG SER          
SEQRES  10 B  155  ARG LYS TYR THR SER TRP TYR VAL ALA LEU LYS ARG THR          
SEQRES  11 B  155  GLY GLN TYR LYS LEU GLY SER LYS THR GLY PRO GLY GLN          
SEQRES  12 B  155  LYS ALA ILE LEU PHE LEU PRO MET SER ALA LYS SER              
SEQRES   1 C  155  MET ALA ALA GLY SER ILE THR THR LEU PRO ALA LEU PRO          
SEQRES   2 C  155  GLU ASP GLY GLY SER GLY ALA PHE PRO PRO GLY HIS PHE          
SEQRES   3 C  155  LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN GLY GLY PHE          
SEQRES   4 C  155  PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL ASP GLY VAL          
SEQRES   5 C  155  ARG GLU LYS SER ASP PRO HIS ILE LYS LEU GLN LEU GLN          
SEQRES   6 C  155  ALA GLU GLU ARG GLY VAL VAL SER ILE LYS GLY VAL SER          
SEQRES   7 C  155  ALA ASN ARG TYR LEU ALA MET LYS GLU ASP GLY ARG LEU          
SEQRES   8 C  155  LEU ALA SER LYS SER VAL THR ASP GLU CYS PHE PHE PHE          
SEQRES   9 C  155  GLU ARG LEU GLU SER ASN ASN TYR ASN THR TYR ARG SER          
SEQRES  10 C  155  ARG LYS TYR THR SER TRP TYR VAL ALA LEU LYS ARG THR          
SEQRES  11 C  155  GLY GLN TYR LYS LEU GLY SER LYS THR GLY PRO GLY GLN          
SEQRES  12 C  155  LYS ALA ILE LEU PHE LEU PRO MET SER ALA LYS SER              
SEQRES   1 D  155  MET ALA ALA GLY SER ILE THR THR LEU PRO ALA LEU PRO          
SEQRES   2 D  155  GLU ASP GLY GLY SER GLY ALA PHE PRO PRO GLY HIS PHE          
SEQRES   3 D  155  LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN GLY GLY PHE          
SEQRES   4 D  155  PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL ASP GLY VAL          
SEQRES   5 D  155  ARG GLU LYS SER ASP PRO HIS ILE LYS LEU GLN LEU GLN          
SEQRES   6 D  155  ALA GLU GLU ARG GLY VAL VAL SER ILE LYS GLY VAL SER          
SEQRES   7 D  155  ALA ASN ARG TYR LEU ALA MET LYS GLU ASP GLY ARG LEU          
SEQRES   8 D  155  LEU ALA SER LYS SER VAL THR ASP GLU CYS PHE PHE PHE          
SEQRES   9 D  155  GLU ARG LEU GLU SER ASN ASN TYR ASN THR TYR ARG SER          
SEQRES  10 D  155  ARG LYS TYR THR SER TRP TYR VAL ALA LEU LYS ARG THR          
SEQRES  11 D  155  GLY GLN TYR LYS LEU GLY SER LYS THR GLY PRO GLY GLN          
SEQRES  12 D  155  LYS ALA ILE LEU PHE LEU PRO MET SER ALA LYS SER              
SEQRES   1 E  220  ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR          
SEQRES   2 E  220  GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA          
SEQRES   3 E  220  ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO          
SEQRES   4 E  220  MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE          
SEQRES   5 E  220  LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN          
SEQRES   6 E  220  GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER          
SEQRES   7 E  220  ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR          
SEQRES   8 E  220  GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU          
SEQRES   9 E  220  ARG SER ARG HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO          
SEQRES  10 E  220  ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE          
SEQRES  11 E  220  VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN          
SEQRES  12 E  220  TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY          
SEQRES  13 E  220  PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA          
SEQRES  14 E  220  GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR          
SEQRES  15 E  220  ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR          
SEQRES  16 E  220  CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER          
SEQRES  17 E  220  ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU              
SEQRES   1 F  220  ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR          
SEQRES   2 F  220  GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA          
SEQRES   3 F  220  ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO          
SEQRES   4 F  220  MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE          
SEQRES   5 F  220  LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN          
SEQRES   6 F  220  GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER          
SEQRES   7 F  220  ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR          
SEQRES   8 F  220  GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU          
SEQRES   9 F  220  ARG SER ARG HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO          
SEQRES  10 F  220  ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE          
SEQRES  11 F  220  VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN          
SEQRES  12 F  220  TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY          
SEQRES  13 F  220  PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA          
SEQRES  14 F  220  GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR          
SEQRES  15 F  220  ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR          
SEQRES  16 F  220  CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER          
SEQRES  17 F  220  ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU              
SEQRES   1 G  220  ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR          
SEQRES   2 G  220  GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA          
SEQRES   3 G  220  ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO          
SEQRES   4 G  220  MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE          
SEQRES   5 G  220  LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN          
SEQRES   6 G  220  GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER          
SEQRES   7 G  220  ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR          
SEQRES   8 G  220  GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU          
SEQRES   9 G  220  ARG SER ARG HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO          
SEQRES  10 G  220  ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE          
SEQRES  11 G  220  VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN          
SEQRES  12 G  220  TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY          
SEQRES  13 G  220  PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA          
SEQRES  14 G  220  GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR          
SEQRES  15 G  220  ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR          
SEQRES  16 G  220  CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER          
SEQRES  17 G  220  ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU              
SEQRES   1 H  220  ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR          
SEQRES   2 H  220  GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA          
SEQRES   3 H  220  ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO          
SEQRES   4 H  220  MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE          
SEQRES   5 H  220  LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN          
SEQRES   6 H  220  GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER          
SEQRES   7 H  220  ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR          
SEQRES   8 H  220  GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU          
SEQRES   9 H  220  ARG SER ARG HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO          
SEQRES  10 H  220  ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE          
SEQRES  11 H  220  VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN          
SEQRES  12 H  220  TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY          
SEQRES  13 H  220  PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA          
SEQRES  14 H  220  GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR          
SEQRES  15 H  220  ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR          
SEQRES  16 H  220  CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER          
SEQRES  17 H  220  ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU              
FORMUL   9  HOH   *77(H2 O)                                                     
HELIX    1   1 ASP A   57  ILE A   60  5                                   4    
HELIX    2   2 LEU A  135  THR A  139  5                                   5    
HELIX    3   3 GLN A  143  ILE A  146  5                                   4    
HELIX    4   4 ASP B   57  ILE B   60  5                                   4    
HELIX    5   5 LEU B  135  THR B  139  5                                   5    
HELIX    6   6 GLN B  143  ILE B  146  5                                   4    
HELIX    7   7 ASP C   57  ILE C   60  5                                   4    
HELIX    8   8 THR C   98  CYS C  101  5                                   4    
HELIX    9   9 LEU C  135  THR C  139  5                                   5    
HELIX   10  10 GLN C  143  ILE C  146  5                                   4    
HELIX   11  11 ASP D   57  ILE D   60  5                                   4    
HELIX   12  12 THR D   98  CYS D  101  5                                   4    
HELIX   13  13 LEU D  135  THR D  139  5                                   5    
HELIX   14  14 GLN D  143  ILE D  146  5                                   4    
HELIX   15  15 ASN E  158  GLU E  163  5                                   6    
HELIX   16  16 LYS E  199  ARG E  203  5                                   5    
HELIX   17  17 ASN E  211  HIS E  213  5                                   3    
HELIX   18  18 VAL E  222  LYS E  226  5                                   5    
HELIX   19  19 THR E  320  ILE E  324  5                                   5    
HELIX   20  20 THR E  333  ALA E  337  5                                   5    
HELIX   21  21 ASN F  158  GLU F  163  5                                   6    
HELIX   22  22 LYS F  199  ARG F  203  5                                   5    
HELIX   23  23 ASN F  211  HIS F  213  5                                   3    
HELIX   24  24 VAL F  222  LYS F  226  5                                   5    
HELIX   25  25 THR F  320  ILE F  324  5                                   5    
HELIX   26  26 THR F  333  ALA F  337  5                                   5    
HELIX   27  27 ASN G  158  GLU G  163  5                                   6    
HELIX   28  28 LYS G  199  ARG G  203  5                                   5    
HELIX   29  29 ASN G  211  HIS G  213  5                                   3    
HELIX   30  30 VAL G  222  LYS G  226  5                                   5    
HELIX   31  31 THR G  320  ILE G  324  5                                   5    
HELIX   32  32 THR G  333  ALA G  337  5                                   5    
HELIX   33  33 ASN H  158  GLU H  163  5                                   6    
HELIX   34  34 LYS H  199  ARG H  203  5                                   5    
HELIX   35  35 ASN H  211  HIS H  213  5                                   3    
HELIX   36  36 VAL H  222  LYS H  226  5                                   5    
HELIX   37  37 THR H  320  ILE H  324  5                                   5    
HELIX   38  38 THR H  333  ALA H  337  5                                   5    
SHEET    1   A 4 VAL A  49  VAL A  52  0                                        
SHEET    2   A 4 PHE A  39  ILE A  43 -1  N  PHE A  40   O  VAL A  52           
SHEET    3   A 4 LYS A  30  CYS A  34 -1  O  LEU A  32   N  LEU A  41           
SHEET    4   A 4 PHE A 148  SER A 152 -1  N  LEU A 149   O  TYR A  33           
SHEET    1   B 4 LEU A  62  GLU A  68  0                                        
SHEET    2   B 4 VAL A  71  GLY A  76 -1  N  VAL A  71   O  GLU A  68           
SHEET    3   B 4 ARG A  81  MET A  85 -1  O  ARG A  81   N  GLY A  76           
SHEET    4   B 4 LEU A  91  SER A  94 -1  O  LEU A  92   N  ALA A  84           
SHEET    1   C 4 LEU A  62  GLU A  68  0                                        
SHEET    2   C 4 VAL A  71  GLY A  76 -1  N  VAL A  71   O  GLU A  68           
SHEET    3   C 4 PHE A 103  LEU A 107 -1  O  PHE A 103   N  VAL A  72           
SHEET    4   C 4 ASN A 113  SER A 117 -1  O  THR A 114   N  ARG A 106           
SHEET    1   D 4 VAL B  49  VAL B  52  0                                        
SHEET    2   D 4 PHE B  39  ILE B  43 -1  N  PHE B  40   O  VAL B  52           
SHEET    3   D 4 LYS B  30  CYS B  34 -1  O  LEU B  32   N  LEU B  41           
SHEET    4   D 4 PHE B 148  SER B 152 -1  N  LEU B 149   O  TYR B  33           
SHEET    1   E 4 LEU B  62  GLU B  68  0                                        
SHEET    2   E 4 VAL B  71  GLY B  76 -1  N  VAL B  71   O  GLU B  68           
SHEET    3   E 4 ARG B  81  MET B  85 -1  O  ARG B  81   N  GLY B  76           
SHEET    4   E 4 LEU B  91  SER B  94 -1  O  LEU B  92   N  ALA B  84           
SHEET    1   F 4 LEU B  62  GLU B  68  0                                        
SHEET    2   F 4 VAL B  71  GLY B  76 -1  N  VAL B  71   O  GLU B  68           
SHEET    3   F 4 PHE B 103  LEU B 107 -1  O  PHE B 103   N  VAL B  72           
SHEET    4   F 4 ASN B 113  SER B 117 -1  O  THR B 114   N  ARG B 106           
SHEET    1   G 4 VAL C  49  VAL C  52  0                                        
SHEET    2   G 4 PHE C  39  ILE C  43 -1  N  PHE C  40   O  VAL C  52           
SHEET    3   G 4 LYS C  30  CYS C  34 -1  O  LEU C  32   N  LEU C  41           
SHEET    4   G 4 PHE C 148  SER C 152 -1  N  LEU C 149   O  TYR C  33           
SHEET    1   H 4 LEU C  62  GLU C  68  0                                        
SHEET    2   H 4 VAL C  71  GLY C  76 -1  O  VAL C  71   N  GLU C  67           
SHEET    3   H 4 ARG C  81  MET C  85 -1  O  ARG C  81   N  GLY C  76           
SHEET    4   H 4 LEU C  91  SER C  94 -1  O  LEU C  92   N  ALA C  84           
SHEET    1   I 4 LEU C  62  GLU C  68  0                                        
SHEET    2   I 4 VAL C  71  GLY C  76 -1  O  VAL C  71   N  GLU C  67           
SHEET    3   I 4 PHE C 103  LEU C 107 -1  O  PHE C 103   N  VAL C  72           
SHEET    4   I 4 ASN C 113  SER C 117 -1  O  THR C 114   N  ARG C 106           
SHEET    1   J 4 VAL D  49  VAL D  52  0                                        
SHEET    2   J 4 PHE D  39  ILE D  43 -1  N  PHE D  40   O  VAL D  52           
SHEET    3   J 4 LYS D  30  CYS D  34 -1  O  LEU D  32   N  LEU D  41           
SHEET    4   J 4 PHE D 148  SER D 152 -1  N  LEU D 149   O  TYR D  33           
SHEET    1   K 4 LEU D  62  GLU D  68  0                                        
SHEET    2   K 4 VAL D  71  GLY D  76 -1  N  VAL D  71   O  GLU D  68           
SHEET    3   K 4 ARG D  81  MET D  85 -1  O  ARG D  81   N  GLY D  76           
SHEET    4   K 4 LEU D  91  SER D  94 -1  O  LEU D  92   N  ALA D  84           
SHEET    1   L 4 LEU D  62  GLU D  68  0                                        
SHEET    2   L 4 VAL D  71  GLY D  76 -1  N  VAL D  71   O  GLU D  68           
SHEET    3   L 4 PHE D 103  LEU D 107 -1  O  PHE D 103   N  VAL D  72           
SHEET    4   L 4 ASN D 113  SER D 117 -1  O  THR D 114   N  ARG D 106           
SHEET    1   M 2 ARG E 152  TRP E 156  0                                        
SHEET    2   M 2 ALA E 181  ASN E 184 -1  N  GLY E 182   O  TYR E 155           
SHEET    1   N 5 LEU E 166  PRO E 170  0                                        
SHEET    2   N 5 GLY E 238  VAL E 249  1  O  HIS E 245   N  HIS E 167           
SHEET    3   N 5 GLY E 227  ASN E 235 -1  O  GLY E 227   N  LEU E 246           
SHEET    4   N 5 THR E 188  LYS E 193 -1  N  THR E 188   O  GLU E 234           
SHEET    5   N 5 LYS E 196  GLU E 197 -1  O  LYS E 196   N  LYS E 193           
SHEET    1   O 3 VAL E 175  ARG E 178  0                                        
SHEET    2   O 3 SER E 215  MET E 218 -1  N  LEU E 216   O  PHE E 177           
SHEET    3   O 3 LYS E 208  ARG E 210 -1  O  LYS E 208   N  ILE E 217           
SHEET    1   P 2 ILE E 257  LEU E 258  0                                        
SHEET    2   P 2 VAL E 280  TYR E 281 -1  O  TYR E 281   N  ILE E 257           
SHEET    1   Q 5 ALA E 266  VAL E 269  0                                        
SHEET    2   Q 5 ILE E 350  LEU E 360  1  O  TRP E 356   N  ALA E 266           
SHEET    3   Q 5 GLY E 338  GLY E 345 -1  O  GLY E 338   N  LEU E 357           
SHEET    4   Q 5 HIS E 287  HIS E 293 -1  N  HIS E 287   O  GLY E 345           
SHEET    5   Q 5 LEU E 309  ALA E 314 -1  O  LYS E 310   N  LYS E 292           
SHEET    1   R 2 VAL E 274  VAL E 277  0                                        
SHEET    2   R 2 VAL E 326  ILE E 329 -1  N  LEU E 327   O  PHE E 276           
SHEET    1   S 2 ARG F 152  TRP F 156  0                                        
SHEET    2   S 2 ALA F 181  ASN F 184 -1  N  GLY F 182   O  TYR F 155           
SHEET    1   T 5 LEU F 166  PRO F 170  0                                        
SHEET    2   T 5 GLY F 238  VAL F 249  1  O  HIS F 245   N  HIS F 167           
SHEET    3   T 5 GLY F 227  ASN F 235 -1  O  GLY F 227   N  LEU F 246           
SHEET    4   T 5 THR F 188  LYS F 193 -1  N  THR F 188   O  GLU F 234           
SHEET    5   T 5 LYS F 196  GLU F 197 -1  O  LYS F 196   N  LYS F 193           
SHEET    1   U 3 VAL F 175  ARG F 178  0                                        
SHEET    2   U 3 SER F 215  MET F 218 -1  O  LEU F 216   N  PHE F 177           
SHEET    3   U 3 LYS F 208  ARG F 210 -1  O  LYS F 208   N  ILE F 217           
SHEET    1   V 2 ILE F 257  LEU F 258  0                                        
SHEET    2   V 2 VAL F 280  TYR F 281 -1  O  TYR F 281   N  ILE F 257           
SHEET    1   W 5 ALA F 266  VAL F 269  0                                        
SHEET    2   W 5 ILE F 350  LEU F 360  1  O  TRP F 356   N  ALA F 266           
SHEET    3   W 5 GLY F 338  GLY F 345 -1  O  GLY F 338   N  LEU F 357           
SHEET    4   W 5 HIS F 287  HIS F 293 -1  N  HIS F 287   O  GLY F 345           
SHEET    5   W 5 LEU F 309  ALA F 314 -1  O  LYS F 310   N  LYS F 292           
SHEET    1   X 2 VAL F 274  VAL F 277  0                                        
SHEET    2   X 2 VAL F 326  ILE F 329 -1  N  LEU F 327   O  PHE F 276           
SHEET    1   Y 2 ARG G 152  TRP G 156  0                                        
SHEET    2   Y 2 ALA G 181  ASN G 184 -1  N  GLY G 182   O  TYR G 155           
SHEET    1   Z 5 LEU G 166  PRO G 170  0                                        
SHEET    2   Z 5 GLY G 238  VAL G 249  1  O  HIS G 245   N  HIS G 167           
SHEET    3   Z 5 GLY G 227  ASN G 235 -1  O  GLY G 227   N  LEU G 246           
SHEET    4   Z 5 THR G 188  LYS G 193 -1  N  THR G 188   O  GLU G 234           
SHEET    5   Z 5 LYS G 196  GLU G 197 -1  O  LYS G 196   N  LYS G 193           
SHEET    1  AA 3 VAL G 175  ARG G 178  0                                        
SHEET    2  AA 3 SER G 215  MET G 218 -1  O  LEU G 216   N  PHE G 177           
SHEET    3  AA 3 LYS G 208  ARG G 210 -1  O  LYS G 208   N  ILE G 217           
SHEET    1  AB 2 ILE G 257  LEU G 258  0                                        
SHEET    2  AB 2 VAL G 280  TYR G 281 -1  N  TYR G 281   O  ILE G 257           
SHEET    1  AC 5 ALA G 266  VAL G 269  0                                        
SHEET    2  AC 5 ILE G 350  LEU G 360  1  O  TRP G 356   N  ALA G 266           
SHEET    3  AC 5 GLY G 338  GLY G 345 -1  O  GLY G 338   N  LEU G 357           
SHEET    4  AC 5 HIS G 287  HIS G 293 -1  N  HIS G 287   O  GLY G 345           
SHEET    5  AC 5 LEU G 309  ALA G 314 -1  O  LYS G 310   N  LYS G 292           
SHEET    1  AD 2 VAL G 274  VAL G 277  0                                        
SHEET    2  AD 2 VAL G 326  ILE G 329 -1  N  LEU G 327   O  PHE G 276           
SHEET    1  AE 2 ARG H 152  TRP H 156  0                                        
SHEET    2  AE 2 ALA H 181  ASN H 184 -1  N  GLY H 182   O  TYR H 155           
SHEET    1  AF 5 LEU H 166  PRO H 170  0                                        
SHEET    2  AF 5 GLY H 238  VAL H 249  1  O  HIS H 245   N  HIS H 167           
SHEET    3  AF 5 GLY H 227  ASN H 235 -1  O  GLY H 227   N  LEU H 246           
SHEET    4  AF 5 THR H 188  LYS H 193 -1  N  THR H 188   O  GLU H 234           
SHEET    5  AF 5 LYS H 196  GLU H 197 -1  O  LYS H 196   N  LYS H 193           
SHEET    1  AG 3 VAL H 175  ARG H 178  0                                        
SHEET    2  AG 3 SER H 215  MET H 218 -1  O  LEU H 216   N  PHE H 177           
SHEET    3  AG 3 LYS H 208  ARG H 210 -1  O  LYS H 208   N  ILE H 217           
SHEET    1  AH 2 ILE H 257  LEU H 258  0                                        
SHEET    2  AH 2 VAL H 280  TYR H 281 -1  N  TYR H 281   O  ILE H 257           
SHEET    1  AI 5 ALA H 266  VAL H 269  0                                        
SHEET    2  AI 5 ILE H 350  LEU H 360  1  O  TRP H 356   N  ALA H 266           
SHEET    3  AI 5 GLY H 338  GLY H 345 -1  O  GLY H 338   N  LEU H 357           
SHEET    4  AI 5 HIS H 287  HIS H 293 -1  N  HIS H 287   O  GLY H 345           
SHEET    5  AI 5 LEU H 309  ALA H 314 -1  O  LYS H 310   N  LYS H 292           
SHEET    1  AJ 2 VAL H 274  VAL H 277  0                                        
SHEET    2  AJ 2 VAL H 326  ILE H 329 -1  N  LEU H 327   O  PHE H 276           
SSBOND   1 CYS E  179    CYS E  231                          1555   1555  2.54  
SSBOND   2 CYS E  278    CYS E  342                          1555   1555  2.53  
SSBOND   3 CYS F  179    CYS F  231                          1555   1555  2.56  
SSBOND   4 CYS F  278    CYS F  342                          1555   1555  2.59  
SSBOND   5 CYS G  179    CYS G  231                          1555   1555  2.47  
SSBOND   6 CYS G  278    CYS G  342                          1555   1555  2.55  
SSBOND   7 CYS H  179    CYS H  231                          1555   1555  2.50  
SSBOND   8 CYS H  278    CYS H  342                          1555   1555  2.52  
CISPEP   1 ASN E  184    PRO E  185          0         0.28                     
CISPEP   2 LEU E  262    PRO E  263          0        -0.04                     
CISPEP   3 ASN F  184    PRO F  185          0         0.04                     
CISPEP   4 LEU F  262    PRO F  263          0        -0.03                     
CISPEP   5 ASN G  184    PRO G  185          0         0.02                     
CISPEP   6 LEU G  262    PRO G  263          0        -0.11                     
CISPEP   7 ASN H  184    PRO H  185          0        -0.01                     
CISPEP   8 LEU H  262    PRO H  263          0        -0.14                     
CRYST1   70.796   72.490   89.919  90.01  89.82  90.00 P 1           4          
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      0.014125  0.000000 -0.000044        0.00000                         
SCALE2      0.000000  0.013795  0.000002        0.00000                         
SCALE3      0.000000  0.000000  0.011121        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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