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Database: PDB
Entry: 3UD9
LinkDB: 3UD9
Original site: 3UD9 
HEADER    HORMONE                                 27-OCT-11   3UD9              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF FGF1-DISACCHARIDE(NI23) COMPLEX         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;                           
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-        
COMPND   5 ENDOTHELIAL CELL GROWTH FACTOR, ECGF-BETA;                           
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: FGF1;                                                          
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: PET21B                                    
KEYWDS    HEPARIN/HEPARAN SULFATE BINDING, HORMONE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-C.HUNG,Z.SHI                                                       
REVDAT   2   16-JAN-13 3UD9    1       JRNL                                     
REVDAT   1   28-NOV-12 3UD9    0                                                
JRNL        AUTH   Y.-P.HU,Y.-Q.ZHONG,Z.-G.CHEN,C.-Y.CHEN,Z.SHI,M.M.L.ZULUETA,  
JRNL        AUTH 2 C.-C.KU,P.-Y.LEE,C.-C.WANG,S.-C.HUNG                         
JRNL        TITL   DIVERGENT SYNTHESIS OF 48 HEPARAN SULFATE-BASED              
JRNL        TITL 2 DISACCHARIDES AND PROBING THE SPECIFIC SUGAR-FIBROBLAST      
JRNL        TITL 3 GROWTH FACTOR-1 INTERACTION                                  
JRNL        REF    J.AM.CHEM.SOC.                V. 134 20722 2012              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   23240683                                                     
JRNL        DOI    10.1021/JA3090065                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15193                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1714                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 955                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 133                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3056                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 57                                      
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.25000                                             
REMARK   3    B22 (A**2) : 4.19000                                              
REMARK   3    B33 (A**2) : -3.06000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.82000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.283         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.199        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3178 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4293 ; 1.453 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   380 ; 6.837 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;37.132 ;24.200       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   554 ;19.294 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.917 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   457 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2378 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1897 ; 2.419 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3046 ; 3.596 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1281 ; 3.981 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1247 ; 5.563 ; 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 : NULL                              
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    11        A   138                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8479  23.8398  21.3706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1357 T22:   0.1584                                     
REMARK   3      T33:   0.1107 T12:  -0.0130                                     
REMARK   3      T13:  -0.0130 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1566 L22:   1.1837                                     
REMARK   3      L33:   0.4873 L12:   0.4782                                     
REMARK   3      L13:   0.4068 L23:  -0.3019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:  -0.1796 S13:   0.0309                       
REMARK   3      S21:  -0.0189 S22:  -0.0878 S23:   0.0642                       
REMARK   3      S31:  -0.0031 S32:  -0.0124 S33:   0.0534                       
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    10        B   137                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.8222  10.5166   8.4130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1377 T22:   0.1301                                     
REMARK   3      T33:   0.1214 T12:  -0.0135                                     
REMARK   3      T13:  -0.0150 T23:  -0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1284 L22:   0.5810                                     
REMARK   3      L33:   1.6973 L12:  -0.0085                                     
REMARK   3      L13:   0.0534 L23:   0.1012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0173 S12:  -0.0217 S13:  -0.0047                       
REMARK   3      S21:  -0.0140 S22:  -0.0070 S23:  -0.0150                       
REMARK   3      S31:   0.0385 S32:  -0.0943 S33:  -0.0103                       
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 :   C    10        C   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5375  27.7552  48.3020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1291 T22:   0.0996                                     
REMARK   3      T33:   0.0905 T12:  -0.0140                                     
REMARK   3      T13:  -0.0090 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8418 L22:   2.5048                                     
REMARK   3      L33:   2.2649 L12:  -0.1521                                     
REMARK   3      L13:  -0.8866 L23:   0.4416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0274 S12:  -0.1524 S13:  -0.0200                       
REMARK   3      S21:  -0.1065 S22:  -0.1281 S23:   0.1174                       
REMARK   3      S31:   0.0096 S32:  -0.0139 S33:   0.1007                       
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 :   B   141        B   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.4967  -4.1129  18.9742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9544 T22:   0.3439                                     
REMARK   3      T33:   0.8946 T12:  -0.2358                                     
REMARK   3      T13:  -0.6991 T23:   0.1551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.5766 L22:  11.6113                                     
REMARK   3      L33:  30.8734 L12: -14.8522                                     
REMARK   3      L13: -22.6790 L23:  20.9476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:  -1.5177 S13:   0.7255                       
REMARK   3      S21:   0.2597 S22:   1.2374 S23:  -0.8158                       
REMARK   3      S31:   0.1536 S32:   2.1412 S33:  -1.2258                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   143        A   160                          
REMARK   3    RESIDUE RANGE :   C   143        C   152                          
REMARK   3    RESIDUE RANGE :   B   143        B   163                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6908  17.9242  21.8856              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3856 T22:   0.1937                                     
REMARK   3      T33:   0.3413 T12:  -0.0183                                     
REMARK   3      T13:   0.0150 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1477 L22:   0.0306                                     
REMARK   3      L33:   0.0879 L12:  -0.0172                                     
REMARK   3      L13:   0.0897 L23:   0.0070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0345 S12:   0.0349 S13:   0.0431                       
REMARK   3      S21:   0.0485 S22:  -0.0350 S23:   0.0491                       
REMARK   3      S31:   0.0657 S32:   0.0273 S33:   0.0005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   141        A   142                          
REMARK   3    RESIDUE RANGE :   C   141        C   142                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.6677  30.9220  33.1438              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6165 T22:   0.3898                                     
REMARK   3      T33:   0.9565 T12:  -0.1724                                     
REMARK   3      T13:  -0.9633 T23:  -0.4353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.1373 L22:   2.7121                                     
REMARK   3      L33:   0.1975 L12: -10.2549                                     
REMARK   3      L13: -11.2043 L23:   5.0307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0568 S12:  -0.0794 S13:  -0.9625                       
REMARK   3      S21:  -0.2730 S22:  -0.1304 S23:   0.4995                       
REMARK   3      S31:   0.3114 S32:   0.2695 S33:   0.0737                       
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 3UD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-NOV-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068608.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16907                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1RG8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)HPO4, 0.1M SODIUM ACETATE, PH    
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-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   SMTRY1   3  1.000000  0.000000  0.000000       56.78700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       56.78700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.46500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 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     0                                                      
REMARK 465     PHE A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     SER A   139                                                      
REMARK 465     ASP A   140                                                      
REMARK 465     MET B     0                                                      
REMARK 465     PHE B     1                                                      
REMARK 465     ASN B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     SER B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     ASP B   140                                                      
REMARK 465     MET C     0                                                      
REMARK 465     PHE C     1                                                      
REMARK 465     ASN C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     TYR C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     VAL C   137                                                      
REMARK 465     SER C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     ASP C   140                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG C    37     O    HOH C   144              1.32            
REMARK 500   CD2  HIS C    21     O    THR C    34              2.13            
REMARK 500   CD2  LEU A    72     CA   ARG A   119              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    CYS A  83   CB    CYS A  83   SG     -0.098                       
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  32     -163.67   -162.87                                   
REMARK 500    GLU A  49      -82.22    -98.51                                   
REMARK 500    GLU A  91      119.20    -33.30                                   
REMARK 500    ASN A  92       41.76     85.11                                   
REMARK 500    HIS A  93      -23.84     78.19                                   
REMARK 500    TYR A 125      148.95    -38.25                                   
REMARK 500    GLU B  49     -120.04    -97.24                                   
REMARK 500    PRO B  79       95.54    -69.87                                   
REMARK 500    ASN B  80     -169.81   -100.80                                   
REMARK 500    GLU B  82        4.51    -69.87                                   
REMARK 500    ASN B  92        1.52    120.13                                   
REMARK 500    THR C  34     -104.52   -112.63                                   
REMARK 500    ARG C  35        9.89    153.65                                   
REMARK 500    ASP C  36     -100.52   -104.04                                   
REMARK 500    ARG C  37        1.06    125.88                                   
REMARK 500    SER C  50      131.46     81.45                                   
REMARK 500    ASN C  92      -17.24    113.78                                   
REMARK 500    ARG C 119      138.76    -38.37                                   
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    LEU A  72        19.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 150        DISTANCE =  5.52 ANGSTROMS                       
REMARK 525    HOH B 151        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B 152        DISTANCE =  6.75 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGN B 141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IDY B 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 142                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UD7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UD8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UDA   RELATED DB: PDB                                   
DBREF  3UD9 A    1   140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  3UD9 B    1   140  UNP    P05230   FGF1_HUMAN      16    155             
DBREF  3UD9 C    1   140  UNP    P05230   FGF1_HUMAN      16    155             
SEQADV 3UD9 MET A    0  UNP  P05230              EXPRESSION TAG                 
SEQADV 3UD9 MET B    0  UNP  P05230              EXPRESSION TAG                 
SEQADV 3UD9 MET C    0  UNP  P05230              EXPRESSION TAG                 
SEQRES   1 A  141  MET PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS          
SEQRES   2 A  141  LEU LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE          
SEQRES   3 A  141  LEU PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER          
SEQRES   4 A  141  ASP GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL          
SEQRES   5 A  141  GLY GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR          
SEQRES   6 A  141  LEU ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN          
SEQRES   7 A  141  THR PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU          
SEQRES   8 A  141  GLU ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA          
SEQRES   9 A  141  GLU LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER          
SEQRES  10 A  141  CYS LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA          
SEQRES  11 A  141  ILE LEU PHE LEU PRO LEU PRO VAL SER SER ASP                  
SEQRES   1 B  141  MET PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS          
SEQRES   2 B  141  LEU LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE          
SEQRES   3 B  141  LEU PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER          
SEQRES   4 B  141  ASP GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL          
SEQRES   5 B  141  GLY GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR          
SEQRES   6 B  141  LEU ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN          
SEQRES   7 B  141  THR PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU          
SEQRES   8 B  141  GLU ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA          
SEQRES   9 B  141  GLU LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER          
SEQRES  10 B  141  CYS LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA          
SEQRES  11 B  141  ILE LEU PHE LEU PRO LEU PRO VAL SER SER ASP                  
SEQRES   1 C  141  MET PHE ASN LEU PRO PRO GLY ASN TYR LYS LYS PRO LYS          
SEQRES   2 C  141  LEU LEU TYR CYS SER ASN GLY GLY HIS PHE LEU ARG ILE          
SEQRES   3 C  141  LEU PRO ASP GLY THR VAL ASP GLY THR ARG ASP ARG SER          
SEQRES   4 C  141  ASP GLN HIS ILE GLN LEU GLN LEU SER ALA GLU SER VAL          
SEQRES   5 C  141  GLY GLU VAL TYR ILE LYS SER THR GLU THR GLY GLN TYR          
SEQRES   6 C  141  LEU ALA MET ASP THR ASP GLY LEU LEU TYR GLY SER GLN          
SEQRES   7 C  141  THR PRO ASN GLU GLU CYS LEU PHE LEU GLU ARG LEU GLU          
SEQRES   8 C  141  GLU ASN HIS TYR ASN THR TYR ILE SER LYS LYS HIS ALA          
SEQRES   9 C  141  GLU LYS ASN TRP PHE VAL GLY LEU LYS LYS ASN GLY SER          
SEQRES  10 C  141  CYS LYS ARG GLY PRO ARG THR HIS TYR GLY GLN LYS ALA          
SEQRES  11 C  141  ILE LEU PHE LEU PRO LEU PRO VAL SER SER ASP                  
HET    PO4  A 141       5                                                       
HET    PO4  A 142       5                                                       
HET    SGN  B 141      19                                                       
HET    IDY  B 142      18                                                       
HET    PO4  C 141       5                                                       
HET    PO4  C 142       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     SGN N,O6-DISULFO-GLUCOSAMINE                                         
HETNAM     IDY METHYL 2-O-SULFO-ALPHA-L-IDOPYRANOSIDURONIC ACID                 
FORMUL   4  PO4    4(O4 P 3-)                                                   
FORMUL   6  SGN    C6 H13 N O11 S2                                              
FORMUL   6  IDY    C7 H12 O10 S                                                 
FORMUL   9  HOH   *49(H2 O)                                                     
HELIX    1   1 ASN A   80  GLU A   82  5                                   3    
HELIX    2   2 HIS A  102  ASN A  106  5                                   5    
HELIX    3   3 ARG A  119  THR A  123  5                                   5    
HELIX    4   4 GLN A  127  ILE A  130  5                                   4    
HELIX    5   5 ASN B   80  CYS B   83  5                                   4    
HELIX    6   6 HIS B  102  ASN B  106  5                                   5    
HELIX    7   7 ARG B  119  THR B  123  5                                   5    
HELIX    8   8 GLN B  127  ILE B  130  5                                   4    
HELIX    9   9 ASN C   80  CYS C   83  5                                   4    
HELIX   10  10 HIS C  102  ASN C  106  5                                   5    
HELIX   11  11 GLN C  127  ILE C  130  5                                   4    
SHEET    1   A 4 VAL A  31  THR A  34  0                                        
SHEET    2   A 4 HIS A  21  ILE A  25 -1  N  ARG A  24   O  ASP A  32           
SHEET    3   A 4 LYS A  12  CYS A  16 -1  N  CYS A  16   O  HIS A  21           
SHEET    4   A 4 PHE A 132  PRO A 136 -1  O  LEU A 133   N  TYR A  15           
SHEET    1   B 4 LEU A  44  ALA A  48  0                                        
SHEET    2   B 4 GLU A  53  SER A  58 -1  O  TYR A  55   N  SER A  47           
SHEET    3   B 4 LEU A  84  LEU A  89 -1  O  PHE A  85   N  VAL A  54           
SHEET    4   B 4 ASN A  95  SER A  99 -1  O  ILE A  98   N  LEU A  86           
SHEET    1   C 2 TYR A  64  MET A  67  0                                        
SHEET    2   C 2 LEU A  73  SER A  76 -1  O  SER A  76   N  TYR A  64           
SHEET    1   D 2 GLY A 110  LEU A 111  0                                        
SHEET    2   D 2 CYS A 117  LYS A 118 -1  O  LYS A 118   N  GLY A 110           
SHEET    1   E 4 VAL B  31  THR B  34  0                                        
SHEET    2   E 4 HIS B  21  ILE B  25 -1  N  ARG B  24   O  ASP B  32           
SHEET    3   E 4 LEU B  13  CYS B  16 -1  N  CYS B  16   O  HIS B  21           
SHEET    4   E 4 PHE B 132  LEU B 135 -1  O  LEU B 133   N  TYR B  15           
SHEET    1   F 4 LEU B  44  ALA B  48  0                                        
SHEET    2   F 4 GLU B  53  SER B  58 -1  O  TYR B  55   N  SER B  47           
SHEET    3   F 4 PHE B  85  LEU B  89 -1  O  PHE B  85   N  VAL B  54           
SHEET    4   F 4 ASN B  95  SER B  99 -1  O  ILE B  98   N  LEU B  86           
SHEET    1   G 2 TYR B  64  MET B  67  0                                        
SHEET    2   G 2 LEU B  73  SER B  76 -1  O  SER B  76   N  TYR B  64           
SHEET    1   H 2 GLY B 110  LEU B 111  0                                        
SHEET    2   H 2 CYS B 117  LYS B 118 -1  O  LYS B 118   N  GLY B 110           
SHEET    1   I 7 PRO C  11  CYS C  16  0                                        
SHEET    2   I 7 LEU C  44  ALA C  48 -1  O  LEU C  44   N  LYS C  12           
SHEET    3   I 7 GLU C  53  SER C  58 -1  O  LYS C  57   N  GLN C  45           
SHEET    4   I 7 PHE C  85  LEU C  89 -1  O  PHE C  85   N  VAL C  54           
SHEET    5   I 7 ASN C  95  SER C  99 -1  O  ILE C  98   N  LEU C  86           
SHEET    6   I 7 PHE C 132  LEU C 135 -1  O  PHE C 132   N  ASN C  95           
SHEET    7   I 7 PRO C  11  CYS C  16 -1  N  LEU C  13   O  LEU C 135           
SHEET    1   J 2 LEU C  23  ILE C  25  0                                        
SHEET    2   J 2 VAL C  31  GLY C  33 -1  O  ASP C  32   N  ARG C  24           
SHEET    1   K 2 TYR C  64  MET C  67  0                                        
SHEET    2   K 2 LEU C  73  SER C  76 -1  O  SER C  76   N  TYR C  64           
LINK         C1  SGN B 141                 O4  IDY B 142     1555   1555  1.40  
CISPEP   1 LYS B   10    PRO B   11          0       -12.51                     
SITE     1 AC1  9 ASN B  18  LYS B 112  LYS B 113  LYS B 118                    
SITE     2 AC1  9 IDY B 142  THR C  69  LYS C 101  HIS C 102                    
SITE     3 AC1  9 LYS C 105                                                     
SITE     1 AC2  8 ASN B  18  LYS B 113  LYS B 118  GLN B 127                    
SITE     2 AC2  8 LYS B 128  ALA B 129  SGN B 141  THR C  69                    
SITE     1 AC3  8 LYS A 105  ASN A 106  TRP A 107  GLY A 120                    
SITE     2 AC3  8 PRO A 121  THR A 123  PRO C 121  ARG C 122                    
SITE     1 AC4  5 ASN A  18  LYS A 113  LYS A 118  PO4 A 142                    
SITE     2 AC4  5 HOH A 151                                                     
SITE     1 AC5  6 ASN A  18  GLN A 127  LYS A 128  ALA A 129                    
SITE     2 AC5  6 PO4 A 141  HOH A 148                                          
SITE     1 AC6  2 ASN C  18  LYS C 118                                          
CRYST1  113.574   46.930   96.708  90.00 125.71  90.00 C 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      0.008805  0.000000  0.006330        0.00000                         
SCALE2      0.000000  0.021308  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012735        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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