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Entry: 3JUT
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HEADER    HORMONE                                 15-SEP-09   3JUT              
TITLE     ACIDIC FIBROBLAST GROWTH FACTOR (FGF-1) COMPLEXED WITH GENTISIC ACID  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;                           
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: HEPARIN-BINDING, UNP RESIDUES 24-153;                      
COMPND   5 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-        
COMPND   6 ENDOTHELIAL CELL GROWTH FACTOR, ECGF-BETA;                           
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PRAT-4                                    
KEYWDS    GROWTH FACTOR, FGF-1 INHIBITORS, ANGIOGENESIS, DEVELOPMENTAL PROTEIN, 
KEYWDS   2 DIFFERENTIATION, HEPARIN-BINDING, MITOGEN, HORMONE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.S.FERNANDEZ,G.GIMENEZ-GALLEGO,A.ROMERO                              
REVDAT   3   13-JUL-11 3JUT    1       VERSN                                    
REVDAT   2   12-MAY-10 3JUT    1       JRNL                                     
REVDAT   1   02-FEB-10 3JUT    0                                                
JRNL        AUTH   I.S.FERNANDEZ,P.CUEVAS,J.ANGULO,P.LOPEZ-NAVAJAS,             
JRNL        AUTH 2 A.CANALES-MAYORDOMO,R.GONZALEZ-CORROCHANO,R.M.LOZANO,        
JRNL        AUTH 3 S.VALVERDE,J.JIMENEZ-BARBERO,A.ROMERO,G.GIMENEZ-GALLEGO      
JRNL        TITL   GENTISIC ACID, A COMPOUND ASSOCIATED WITH PLANT DEFENSE AND  
JRNL        TITL 2 A METABOLITE OF ASPIRIN, HEADS A NEW CLASS OF IN VIVO        
JRNL        TITL 3 FIBROBLAST GROWTH FACTOR INHIBITORS.                         
JRNL        REF    J.BIOL.CHEM.                  V. 285 11714 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20145243                                                     
JRNL        DOI    10.1074/JBC.M109.064618                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 38199                          
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 + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2034                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2818                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 132                          
REMARK   3   BIN FREE R VALUE                    : 0.3570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6227                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 31.73                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.346         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.258         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.203         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.715        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6386 ; 0.026 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8611 ; 2.106 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   773 ; 8.314 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   300 ;36.597 ;24.200       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1146 ;20.168 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;22.660 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   912 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4854 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2268 ; 0.222 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4038 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   227 ; 0.164 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   115 ; 0.252 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     9 ; 0.264 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3998 ; 1.002 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6205 ; 1.620 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2751 ; 2.558 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2406 ; 3.698 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B D C E F                     
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     130      6                      
REMARK   3           1     B      1       B     130      6                      
REMARK   3           1     D      1       D     130      6                      
REMARK   3           1     C      1       C     130      6                      
REMARK   3           1     E      1       E     130      6                      
REMARK   3           1     F      1       F     130      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1031 ;  0.63 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1031 ;  0.61 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1031 ;  0.53 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1031 ;  0.53 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    E    (A):   1031 ;  0.63 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    F    (A):   1031 ;  0.72 ;  5.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1031 ;  2.58 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1031 ;  2.74 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1031 ;  2.80 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1031 ;  3.16 ; 10.00           
REMARK   3   LOOSE THERMAL      1    E (A**2):   1031 ;  2.63 ; 10.00           
REMARK   3   LOOSE THERMAL      1    F (A**2):   1031 ;  3.67 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3843 -20.8732  24.3742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1730 T22:  -0.1719                                     
REMARK   3      T33:  -0.1524 T12:  -0.0787                                     
REMARK   3      T13:   0.0030 T23:  -0.0638                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4644 L22:   7.7372                                     
REMARK   3      L33:   5.1230 L12:  -0.3747                                     
REMARK   3      L13:  -0.8415 L23:   3.1597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1372 S12:  -0.3560 S13:   0.0769                       
REMARK   3      S21:   0.5000 S22:  -0.5432 S23:   0.5304                       
REMARK   3      S31:   0.0949 S32:  -0.8154 S33:   0.4060                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.1706   3.0333  23.2038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1719 T22:  -0.2349                                     
REMARK   3      T33:  -0.1806 T12:   0.0010                                     
REMARK   3      T13:  -0.0163 T23:   0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7812 L22:   4.4663                                     
REMARK   3      L33:   3.6973 L12:   0.1156                                     
REMARK   3      L13:  -0.1561 L23:  -2.0838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0132 S12:   0.0850 S13:  -0.1057                       
REMARK   3      S21:  -0.1837 S22:  -0.3111 S23:  -0.1352                       
REMARK   3      S31:   0.1135 S32:   0.5969 S33:   0.3243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7691  -1.1865  43.6125              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2119 T22:  -0.1811                                     
REMARK   3      T33:  -0.2132 T12:   0.0252                                     
REMARK   3      T13:   0.0141 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4001 L22:   4.3264                                     
REMARK   3      L33:   7.1665 L12:   0.9168                                     
REMARK   3      L13:  -0.3143 L23:   0.2627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0340 S12:   0.1368 S13:  -0.0247                       
REMARK   3      S21:  -0.0238 S22:  -0.1494 S23:   0.0849                       
REMARK   3      S31:   0.1027 S32:   0.3769 S33:   0.1834                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.4845  22.9628  -2.5875              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1667 T22:  -0.2030                                     
REMARK   3      T33:  -0.2267 T12:   0.0237                                     
REMARK   3      T13:  -0.0025 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1897 L22:   4.9467                                     
REMARK   3      L33:   5.4862 L12:   2.1846                                     
REMARK   3      L13:  -0.0736 L23:   0.0084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1822 S12:   0.0976 S13:   0.0085                       
REMARK   3      S21:  -0.0629 S22:  -0.1423 S23:  -0.0566                       
REMARK   3      S31:  -0.4100 S32:  -0.1190 S33:  -0.0399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2766 -14.0512  17.3272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1249 T22:  -0.2113                                     
REMARK   3      T33:  -0.1519 T12:   0.0644                                     
REMARK   3      T13:   0.0113 T23:  -0.0827                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2674 L22:   3.1688                                     
REMARK   3      L33:   5.9473 L12:  -1.5479                                     
REMARK   3      L13:   0.0582 L23:  -0.0692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0464 S12:   0.0310 S13:  -0.1126                       
REMARK   3      S21:   0.1365 S22:   0.0630 S23:   0.1710                       
REMARK   3      S31:   0.1252 S32:   0.1117 S33:  -0.0166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.3033   9.8425  28.5983              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1673 T22:   0.0063                                     
REMARK   3      T33:  -0.1405 T12:  -0.1237                                     
REMARK   3      T13:  -0.0264 T23:   0.1240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1795 L22:   4.5202                                     
REMARK   3      L33:   7.1361 L12:   2.5711                                     
REMARK   3      L13:  -2.3414 L23:  -0.6718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3959 S12:  -0.9233 S13:  -0.1634                       
REMARK   3      S21:   0.1484 S22:  -0.3134 S23:  -0.2101                       
REMARK   3      S31:  -0.1936 S32:   0.4373 S33:  -0.0825                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3JUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055186.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM16                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41838                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.210                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
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 1AXM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EQUAL VOLUMES OF PROTEIN AND INHIBITOR   
REMARK 280  SOLUTIONS, 0.75 AND 1.5 MM,RESPECTIVELY WERE MIXED WITH DROPS       
REMARK 280  CONTAINING 60% SODIUM/POTASSIUM TARTRATE BUFFERED WITH 5 MM         
REMARK 280  SODIUM PHOSPHATE [PH 7.8]. THE DROPS WERE EQUILIBRATED AGAINST      
REMARK 280  200 ML OF 1.3M LI2SO4 AND TYPICAL CRYSTALS GREW WITHIN TWO WEEKS    
REMARK 280  , VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS A   1   CD    LYS A   1   CE      0.158                       
REMARK 500    LYS A   2   CE    LYS A   2   NZ      0.218                       
REMARK 500    GLY A  11   N     GLY A  11   CA      0.122                       
REMARK 500    GLU A  41   CD    GLU A  41   OE1     0.093                       
REMARK 500    GLU A  41   CD    GLU A  41   OE2     0.098                       
REMARK 500    GLU A  73   CG    GLU A  73   CD      0.143                       
REMARK 500    GLU A  73   CD    GLU A  73   OE2     0.082                       
REMARK 500    GLU A  82   C     GLU A  82   O       0.169                       
REMARK 500    GLU A  83   CG    GLU A  83   CD      0.129                       
REMARK 500    GLU A  83   CD    GLU A  83   OE1     0.232                       
REMARK 500    GLU A  83   CD    GLU A  83   OE2     0.287                       
REMARK 500    GLU A  96   CG    GLU A  96   CD      0.162                       
REMARK 500    GLU A  96   CD    GLU A  96   OE1     0.106                       
REMARK 500    GLU A  96   CD    GLU A  96   OE2     0.309                       
REMARK 500    LYS A  97   CD    LYS A  97   CE      0.232                       
REMARK 500    GLY F  21   C     GLY F  21   O       0.167                       
REMARK 500    MET F  59   CB    MET F  59   CG      0.247                       
REMARK 500    ASP F  60   CG    ASP F  60   OD2     0.416                       
REMARK 500    TYR F  66   CG    TYR F  66   CD2     0.100                       
REMARK 500    TYR F  66   CG    TYR F  66   CD1     0.125                       
REMARK 500    TYR F  66   CE1   TYR F  66   CZ      0.103                       
REMARK 500    TYR F  66   CZ    TYR F  66   CE2     0.125                       
REMARK 500    GLU F  73   CD    GLU F  73   OE1     0.067                       
REMARK 500    GLU F  74   CD    GLU F  74   OE2     0.136                       
REMARK 500    GLU F  82   CG    GLU F  82   CD      0.102                       
REMARK 500    GLU F  96   CG    GLU F  96   CD      0.091                       
REMARK 500    GLU F  96   C     GLU F  96   O       0.138                       
REMARK 500    GLY F 112   CA    GLY F 112   C       0.101                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  11   C   -  N   -  CA  ANGL. DEV. = -21.3 DEGREES          
REMARK 500    GLU A  96   OE1 -  CD  -  OE2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    GLU A  96   CG  -  CD  -  OE1 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    GLU A  96   CG  -  CD  -  OE2 ANGL. DEV. = -24.9 DEGREES          
REMARK 500    LEU D 127   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ASP F  60   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    THR F  61   CA  -  CB  -  CG2 ANGL. DEV. =  -8.5 DEGREES          
REMARK 500    ASP F  62   OD1 -  CG  -  OD2 ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ASP F  62   CB  -  CG  -  OD1 ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LYS F  92   CD  -  CE  -  NZ  ANGL. DEV. = -16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  24     -143.20   -150.03                                   
REMARK 500    HIS A  85       -5.86     82.06                                   
REMARK 500    HIS A  94       51.48   -140.48                                   
REMARK 500    ASP B  24     -158.49   -156.59                                   
REMARK 500    GLU B  83      -81.23    -41.05                                   
REMARK 500    ASN B  84       42.79    -85.25                                   
REMARK 500    HIS B  85       -0.20     80.66                                   
REMARK 500    ASN B  98       39.52     72.10                                   
REMARK 500    ASP C  24     -159.56   -153.47                                   
REMARK 500    GLU C  41      -86.43    -71.11                                   
REMARK 500    HIS C  85        2.73     86.91                                   
REMARK 500    ASN D  10       95.63    -65.45                                   
REMARK 500    GLU D  41      -75.97    -68.83                                   
REMARK 500    VAL D  43      -77.54    -40.00                                   
REMARK 500    GLU D  83      -37.17    -33.58                                   
REMARK 500    HIS D  85       -1.31     81.68                                   
REMARK 500    VAL D 129      124.03    -38.62                                   
REMARK 500    SER E  42      118.46    115.12                                   
REMARK 500    LYS E 104      171.67    -59.86                                   
REMARK 500    LYS F   2       96.15     70.24                                   
REMARK 500    ASP F  24     -157.78   -164.42                                   
REMARK 500    GLU F  41     -110.99    -70.23                                   
REMARK 500    THR F  61        3.01    -59.71                                   
REMARK 500    LYS F  97       30.06    -83.32                                   
REMARK 500    ASN F  98       77.47     21.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU E   41     SER E   42                  -43.94                    
REMARK 500 VAL E  129     SER E  130                 -145.57                    
REMARK 500 VAL F  129     SER F  130                  -50.85                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER A 130        23.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS C  85        24.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS D  85        24.4      L          L   OUTSIDE RANGE           
REMARK 500    GLU E  41        24.4      L          L   OUTSIDE RANGE           
REMARK 500    SER E  42        20.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU E  83        24.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU F  83        24.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTQ A 131                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTQ B 131                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K1X   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN COMPLEXED WITH DOBESILATE                               
DBREF  3JUT A    1   130  UNP    P05230   FGF1_HUMAN      24    153             
DBREF  3JUT B    1   130  UNP    P05230   FGF1_HUMAN      24    153             
DBREF  3JUT C    1   130  UNP    P05230   FGF1_HUMAN      24    153             
DBREF  3JUT D    1   130  UNP    P05230   FGF1_HUMAN      24    153             
DBREF  3JUT E    1   130  UNP    P05230   FGF1_HUMAN      24    153             
DBREF  3JUT F    1   130  UNP    P05230   FGF1_HUMAN      24    153             
SEQRES   1 A  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 A  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 A  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 A  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 A  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 A  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 A  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 A  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 A  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 A  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
SEQRES   1 B  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 B  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 B  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 B  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 B  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 B  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 B  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 B  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 B  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 B  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
SEQRES   1 C  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 C  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 C  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 C  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 C  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 C  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 C  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 C  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 C  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 C  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
SEQRES   1 D  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 D  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 D  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 D  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 D  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 D  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 D  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 D  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 D  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 D  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
SEQRES   1 E  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 E  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 E  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 E  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 E  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 E  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 E  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 E  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 E  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 E  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
SEQRES   1 F  130  LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY HIS          
SEQRES   2 F  130  PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR          
SEQRES   3 F  130  ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER          
SEQRES   4 F  130  ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU          
SEQRES   5 F  130  THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU          
SEQRES   6 F  130  TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU          
SEQRES   7 F  130  GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER          
SEQRES   8 F  130  LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS          
SEQRES   9 F  130  LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR          
SEQRES  10 F  130  GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER          
HET    GTQ  A 131      11                                                       
HET    GTQ  B 131      11                                                       
HETNAM     GTQ 2,5-DIHYDROXYBENZOIC ACID                                        
FORMUL   7  GTQ    2(C7 H6 O4)                                                  
FORMUL   9  HOH   *23(H2 O)                                                     
HELIX    1   1 ASP A   31  ILE A   34  5                                   4    
HELIX    2   2 ASN A   72  CYS A   75  5                                   4    
HELIX    3   3 LYS A   93  ALA A   95  5                                   3    
HELIX    4   4 ARG A  111  THR A  115  5                                   5    
HELIX    5   5 GLN A  119  ILE A  122  5                                   4    
HELIX    6   6 ASN B   72  CYS B   75  5                                   4    
HELIX    7   7 HIS B   94  ASN B   98  5                                   5    
HELIX    8   8 ARG B  111  THR B  115  5                                   5    
HELIX    9   9 ASN C   72  CYS C   75  5                                   4    
HELIX   10  10 HIS C   94  ASN C   98  5                                   5    
HELIX   11  11 ARG C  111  THR C  115  5                                   5    
HELIX   12  12 GLN C  119  ILE C  122  5                                   4    
HELIX   13  13 ARG D  111  THR D  115  5                                   5    
HELIX   14  14 GLN D  119  ILE D  122  5                                   4    
HELIX   15  15 ASN E   72  CYS E   75  5                                   4    
HELIX   16  16 HIS E   94  ASN E   98  5                                   5    
HELIX   17  17 ARG E  111  THR E  115  5                                   5    
HELIX   18  18 GLN E  119  ILE E  122  5                                   4    
HELIX   19  19 ASP F   31  ILE F   34  5                                   4    
HELIX   20  20 ASN F   72  CYS F   75  5                                   4    
HELIX   21  21 HIS F   94  ASN F   98  5                                   5    
HELIX   22  22 ARG F  111  THR F  115  5                                   5    
HELIX   23  23 GLN F  119  ILE F  122  5                                   4    
SHEET    1   A 4 VAL A  23  THR A  26  0                                        
SHEET    2   A 4 HIS A  13  ILE A  17 -1  N  PHE A  14   O  THR A  26           
SHEET    3   A 4 LYS A   4  CYS A   8 -1  N  CYS A   8   O  HIS A  13           
SHEET    4   A 4 PHE A 124  PRO A 128 -1  O  LEU A 125   N  TYR A   7           
SHEET    1   B 4 LEU A  36  SER A  42  0                                        
SHEET    2   B 4 GLU A  45  SER A  50 -1  O  LYS A  49   N  GLN A  37           
SHEET    3   B 4 PHE A  77  LEU A  81 -1  O  PHE A  77   N  VAL A  46           
SHEET    4   B 4 ASN A  87  SER A  91 -1  O  ILE A  90   N  LEU A  78           
SHEET    1   C 2 TYR A  56  MET A  59  0                                        
SHEET    2   C 2 LEU A  65  SER A  68 -1  O  SER A  68   N  TYR A  56           
SHEET    1   D 4 VAL B  23  THR B  26  0                                        
SHEET    2   D 4 HIS B  13  ILE B  17 -1  N  PHE B  14   O  THR B  26           
SHEET    3   D 4 LYS B   4  CYS B   8 -1  N  CYS B   8   O  HIS B  13           
SHEET    4   D 4 PHE B 124  PRO B 128 -1  O  LEU B 127   N  LEU B   5           
SHEET    1   E 4 LEU B  36  SER B  42  0                                        
SHEET    2   E 4 GLU B  45  SER B  50 -1  O  LYS B  49   N  GLN B  37           
SHEET    3   E 4 PHE B  77  LEU B  81 -1  O  PHE B  77   N  VAL B  46           
SHEET    4   E 4 ASN B  87  SER B  91 -1  O  ILE B  90   N  LEU B  78           
SHEET    1   F 2 TYR B  56  MET B  59  0                                        
SHEET    2   F 2 LEU B  65  SER B  68 -1  O  SER B  68   N  TYR B  56           
SHEET    1   G 4 VAL C  23  THR C  26  0                                        
SHEET    2   G 4 HIS C  13  ILE C  17 -1  N  ARG C  16   O  ASP C  24           
SHEET    3   G 4 LYS C   4  CYS C   8 -1  N  CYS C   8   O  HIS C  13           
SHEET    4   G 4 PHE C 124  PRO C 128 -1  O  LEU C 125   N  TYR C   7           
SHEET    1   H 4 LEU C  36  ALA C  40  0                                        
SHEET    2   H 4 GLU C  45  SER C  50 -1  O  LYS C  49   N  GLN C  37           
SHEET    3   H 4 PHE C  77  LEU C  81 -1  O  PHE C  77   N  VAL C  46           
SHEET    4   H 4 ASN C  87  SER C  91 -1  O  ILE C  90   N  LEU C  78           
SHEET    1   I 2 TYR C  56  MET C  59  0                                        
SHEET    2   I 2 LEU C  65  SER C  68 -1  O  SER C  68   N  TYR C  56           
SHEET    1   J 4 VAL D  23  THR D  26  0                                        
SHEET    2   J 4 HIS D  13  ILE D  17 -1  N  PHE D  14   O  THR D  26           
SHEET    3   J 4 LYS D   4  CYS D   8 -1  N  CYS D   8   O  HIS D  13           
SHEET    4   J 4 PHE D 124  PRO D 128 -1  O  LEU D 127   N  LEU D   5           
SHEET    1   K 4 LEU D  36  ALA D  40  0                                        
SHEET    2   K 4 GLU D  45  SER D  50 -1  O  LYS D  49   N  GLN D  37           
SHEET    3   K 4 LEU D  76  LEU D  81 -1  O  PHE D  77   N  VAL D  46           
SHEET    4   K 4 ASN D  87  SER D  91 -1  O  THR D  88   N  ARG D  80           
SHEET    1   L 2 TYR D  56  MET D  59  0                                        
SHEET    2   L 2 LEU D  65  SER D  68 -1  O  SER D  68   N  TYR D  56           
SHEET    1   M 4 VAL E  23  THR E  26  0                                        
SHEET    2   M 4 HIS E  13  ILE E  17 -1  N  PHE E  14   O  THR E  26           
SHEET    3   M 4 LYS E   4  CYS E   8 -1  N  CYS E   8   O  HIS E  13           
SHEET    4   M 4 PHE E 124  PRO E 128 -1  O  LEU E 125   N  TYR E   7           
SHEET    1   N 4 LEU E  36  ALA E  40  0                                        
SHEET    2   N 4 GLU E  45  SER E  50 -1  O  LYS E  49   N  GLN E  37           
SHEET    3   N 4 PHE E  77  LEU E  81 -1  O  PHE E  77   N  VAL E  46           
SHEET    4   N 4 ASN E  87  SER E  91 -1  O  ILE E  90   N  LEU E  78           
SHEET    1   O 2 TYR E  56  MET E  59  0                                        
SHEET    2   O 2 LEU E  65  SER E  68 -1  O  SER E  68   N  TYR E  56           
SHEET    1   P 4 VAL F  23  THR F  26  0                                        
SHEET    2   P 4 HIS F  13  ILE F  17 -1  N  ARG F  16   O  ASP F  24           
SHEET    3   P 4 LEU F   5  CYS F   8 -1  N  CYS F   8   O  HIS F  13           
SHEET    4   P 4 PHE F 124  LEU F 127 -1  O  LEU F 125   N  TYR F   7           
SHEET    1   Q 4 LEU F  36  ALA F  40  0                                        
SHEET    2   Q 4 GLU F  45  SER F  50 -1  O  LYS F  49   N  GLN F  37           
SHEET    3   Q 4 PHE F  77  LEU F  81 -1  O  PHE F  77   N  VAL F  46           
SHEET    4   Q 4 ASN F  87  SER F  91 -1  O  ILE F  90   N  LEU F  78           
SHEET    1   R 2 TYR F  56  MET F  59  0                                        
SHEET    2   R 2 LEU F  65  SER F  68 -1  O  SER F  68   N  TYR F  56           
CISPEP   1 LYS F    1    LYS F    2          0         3.15                     
SITE     1 AC1  6 ASN A  10  LYS A 105  LYS A 110  GLN A 119                    
SITE     2 AC1  6 LYS A 120  GLU C  74                                          
SITE     1 AC2  5 ASN B  10  LYS B 110  GLN B 119  LYS B 120                    
SITE     2 AC2  5 GLU D  96                                                     
CRYST1   97.658   47.685   98.413  90.00 106.45  90.00 P 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010240  0.000000  0.003023        0.00000                         
SCALE2      0.000000  0.020971  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010595        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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