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Database: PDB
Entry: 3CU1
LinkDB: 3CU1
Original site: 3CU1 
HEADER    TRANSFERASE/HORMONE                     15-APR-08   3CU1              
TITLE     CRYSTAL STRUCTURE OF 2:2:2 FGFR2D2:FGF1:SOS COMPLEX                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2;                       
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: IG-LIKE C2-TYPE 2 DOMAIN, UNP RESIDUES 150-249;            
COMPND   5 SYNONYM: FGFR-2, KERATINOCYTE GROWTH FACTOR RECEPTOR 2, CD332        
COMPND   6 ANTIGEN;                                                             
COMPND   7 EC: 2.7.10.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: HEPARIN-BINDING GROWTH FACTOR 1;                           
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 22-152;                                       
COMPND  13 SYNONYM: HBGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, BETA-        
COMPND  14 ENDOTHELIAL CELL GROWTH FACTOR, ECGF- BETA;                          
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: FGFR2, BEK, KGFR, KSAM;                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 GENE: FGF1, FGFA;                                                    
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    FIBROBLAST GROWTH FACTOR 1, FIBROBLAST GROWTH FACTOR RECEPTOR 2, D2   
KEYWDS   2 DOMAIN, SUCROSE OCTA SULFATE, ALTERNATIVE SPLICING, ATP-BINDING,     
KEYWDS   3 DISEASE MUTATION, ECTODERMAL DYSPLASIA, GLYCOPROTEIN, HEPARIN-       
KEYWDS   4 BINDING, IMMUNOGLOBULIN DOMAIN, KINASE, LACRIMO-AURICULO-DENTO-      
KEYWDS   5 DIGITAL SYNDROME, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,      
KEYWDS   6 POLYMORPHISM, SECRETED, TRANSFERASE, TRANSMEMBRANE, TYROSINE-PROTEIN 
KEYWDS   7 KINASE, ACETYLATION, ANGIOGENESIS, DEVELOPMENTAL PROTEIN,            
KEYWDS   8 DIFFERENTIATION, MITOGEN, TRANSFERASE-HORMONE COMPLEX                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GUO,R.DAKSHINAMURTHY,S.K.K.THALLAPURANAM,J.SAKON                    
REVDAT   2   25-OCT-17 3CU1    1       REMARK                                   
REVDAT   1   21-APR-09 3CU1    0                                                
JRNL        AUTH   F.GUO,R.DAKSHINAMURTHY,S.K.K.THALLAPURANAM,J.SAKON           
JRNL        TITL   CRYSTAL STRUCTURE OF 2:2:2 FGFR2D2:FGF1:SOS COMPLEX          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 19219                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1044                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 580                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 37.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 28                           
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3701                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 110                                     
REMARK   3   SOLVENT ATOMS            : 343                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.42000                                              
REMARK   3    B22 (A**2) : -1.49000                                             
REMARK   3    B33 (A**2) : 1.07000                                              
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): 0.641         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.354         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.252         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.260        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3939 ; 0.053 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5355 ; 3.136 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   455 ; 3.368 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   189 ;32.133 ;23.810       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   677 ;16.752 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;15.920 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   572 ; 0.281 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2925 ; 0.013 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2057 ; 0.362 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2612 ; 0.357 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   283 ; 0.303 ; 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):    40 ; 0.319 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.250 ; 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):  2401 ; 0.977 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3687 ; 1.534 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1833 ; 1.158 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1668 ; 1.981 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    150       A     249      2                      
REMARK   3           1     C    150       C     249      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    400 ;  0.08 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    418 ;  0.61 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):    400 ;  0.19 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    418 ;  0.96 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 6                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     10       B      11      6                      
REMARK   3           1     D     10       D      11      6                      
REMARK   3           2     B     12       B      47      2                      
REMARK   3           2     D     12       D      47      2                      
REMARK   3           3     B     48       B      52      6                      
REMARK   3           3     D     48       D      52      6                      
REMARK   3           4     B     53       B      90      2                      
REMARK   3           4     D     53       D      90      2                      
REMARK   3           5     B     91       B      93      3                      
REMARK   3           5     D     91       D      93      3                      
REMARK   3           6     B     94       B     137      2                      
REMARK   3           6     D     94       D     137      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):    484 ;  0.07 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):    476 ;  0.73 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    B    (A):     62 ;  1.19 ;  5.00           
REMARK   3   TIGHT THERMAL      2    B (A**2):    484 ;  0.18 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):    476 ;  0.69 ;  2.00           
REMARK   3   LOOSE THERMAL      2    B (A**2):     62 ;  2.96 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 3CU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047208.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-3000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21046                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG3350, 4% TACSIMATE, PH 7.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       42.96450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.18750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.96450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.18750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     LYS B     9                                                      
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   CB   LEU B    13     O    HOH B   204              1.58            
REMARK 500   O    VAL D   137     O    HOH D   211              1.68            
REMARK 500   CB   THR C   174     O    HOH C   361              1.76            
REMARK 500   O    HOH B   195     O    HOH B   206              1.79            
REMARK 500   CB   ALA C   171     O    HOH C   372              1.80            
REMARK 500   CG   LEU B    13     O    HOH B   204              1.83            
REMARK 500   OE1  GLN C   212     O    HOH C   381              1.87            
REMARK 500   O    HOH C   334     O    HOH C   379              1.87            
REMARK 500   CB   THR A   174     O    HOH A   306              1.88            
REMARK 500   NZ   LYS D   118     O43  SCR D     1              1.91            
REMARK 500   CB   SER B    47     O    HOH B   210              1.93            
REMARK 500   C    LYS D     9     O    HOH D   239              1.99            
REMARK 500   O    HOH D   178     O    HOH D   251              1.99            
REMARK 500   NZ   LYS B   128     O    HOH B   162              2.02            
REMARK 500   O94  SCR D     1     O    HOH D   259              2.02            
REMARK 500   O    HOH B   180     O    HOH B   189              2.03            
REMARK 500   N    ASN C   150     O    HOH C   380              2.04            
REMARK 500   OG1  THR C   174     O    HOH C   361              2.05            
REMARK 500   O    HOH A   302     O    HOH A   325              2.05            
REMARK 500   NH2  ARG D    37     O    HOH D   215              2.07            
REMARK 500   O    VAL B   137     O    HOH B   151              2.07            
REMARK 500   NE2  GLN D    40     O    HOH D   221              2.08            
REMARK 500   O    PRO D   134     O    HOH D   265              2.09            
REMARK 500   O    HOH B   155     O    HOH B   169              2.10            
REMARK 500   CB   SER C   220     O    HOH C   356              2.12            
REMARK 500   N    LYS D   101     O    HOH D   251              2.12            
REMARK 500   N    LYS D    10     O    HOH D   239              2.12            
REMARK 500   O    HOH C   302     O    HOH C   378              2.13            
REMARK 500   OH   TYR A   207     O    HOH A   298              2.14            
REMARK 500   O    HOH A   304     O    HOH A   315              2.15            
REMARK 500   C    VAL A   249     O    HOH A   315              2.18            
REMARK 500   O    PRO A   154     O    HOH A   250              2.18            
REMARK 500   CD2  TYR D   125     O    HOH D   206              2.18            
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    ASN A 150   CB    ASN A 150   CG     -0.148                       
REMARK 500    ARG A 152   CB    ARG A 152   CG     -0.201                       
REMARK 500    ARG A 152   CG    ARG A 152   CD     -0.153                       
REMARK 500    ARG A 152   CZ    ARG A 152   NH2     0.078                       
REMARK 500    TRP A 156   CZ3   TRP A 156   CH2    -0.143                       
REMARK 500    GLU A 160   CG    GLU A 160   CD      0.142                       
REMARK 500    GLU A 160   CD    GLU A 160   OE2     0.115                       
REMARK 500    LYS A 161   CB    LYS A 161   CG      0.181                       
REMARK 500    LYS A 161   CD    LYS A 161   CE      0.168                       
REMARK 500    LYS A 161   CE    LYS A 161   NZ      0.157                       
REMARK 500    GLU A 163   CG    GLU A 163   CD      0.100                       
REMARK 500    GLU A 163   CD    GLU A 163   OE2     0.086                       
REMARK 500    HIS A 167   C     HIS A 167   O       0.118                       
REMARK 500    VAL A 169   CB    VAL A 169   CG1    -0.199                       
REMARK 500    CYS A 179   CA    CYS A 179   CB     -0.104                       
REMARK 500    MET A 189   CG    MET A 189   SD      0.165                       
REMARK 500    ARG A 190   CB    ARG A 190   CG     -0.197                       
REMARK 500    LYS A 196   CD    LYS A 196   CE      0.181                       
REMARK 500    LYS A 196   CE    LYS A 196   NZ      0.238                       
REMARK 500    GLU A 197   CB    GLU A 197   CG     -0.151                       
REMARK 500    GLU A 197   CG    GLU A 197   CD      0.091                       
REMARK 500    GLU A 197   CD    GLU A 197   OE2     0.085                       
REMARK 500    GLU A 201   CD    GLU A 201   OE2     0.072                       
REMARK 500    TYR A 207   CB    TYR A 207   CG     -0.099                       
REMARK 500    TYR A 207   CE2   TYR A 207   CD2    -0.118                       
REMARK 500    LYS A 208   CD    LYS A 208   CE      0.182                       
REMARK 500    GLN A 212   CB    GLN A 212   CG      0.343                       
REMARK 500    GLN A 212   CG    GLN A 212   CD      0.159                       
REMARK 500    GLU A 219   CG    GLU A 219   CD      0.147                       
REMARK 500    GLU A 219   CD    GLU A 219   OE1     0.093                       
REMARK 500    VAL A 221   CB    VAL A 221   CG2    -0.217                       
REMARK 500    VAL A 232   CA    VAL A 232   CB     -0.133                       
REMARK 500    GLU A 234   CG    GLU A 234   CD      0.118                       
REMARK 500    GLU A 234   CD    GLU A 234   OE1     0.101                       
REMARK 500    GLU A 234   CD    GLU A 234   OE2     0.077                       
REMARK 500    GLU A 236   CD    GLU A 236   OE1     0.072                       
REMARK 500    TYR A 237   CD1   TYR A 237   CE1    -0.132                       
REMARK 500    TYR A 237   CE2   TYR A 237   CD2    -0.096                       
REMARK 500    VAL A 248   CB    VAL A 248   CG1     0.144                       
REMARK 500    VAL A 249   CB    VAL A 249   CG1    -0.159                       
REMARK 500    LYS B  10   CD    LYS B  10   CE      0.168                       
REMARK 500    LEU B  14   CG    LEU B  14   CD1    -0.296                       
REMARK 500    TYR B  15   CE2   TYR B  15   CD2    -0.093                       
REMARK 500    PHE B  22   CB    PHE B  22   CG     -0.126                       
REMARK 500    GLU B  49   CG    GLU B  49   CD      0.096                       
REMARK 500    LYS B  57   CE    LYS B  57   NZ      0.219                       
REMARK 500    GLU B  60   CB    GLU B  60   CG     -0.150                       
REMARK 500    TYR B  64   CE1   TYR B  64   CZ      0.083                       
REMARK 500    GLU B  91   CG    GLU B  91   CD      0.124                       
REMARK 500    GLU B  91   C     GLU B  91   O      -0.129                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     124 BOND DEVIATIONS.                              
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    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    LYS A 161   CD  -  CE  -  NZ  ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO A 187   C   -  N   -  CA  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG A 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 210   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    SER A 224   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A 247   CB  -  CG  -  OD1 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ASP A 247   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LEU B  13   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ASP B  36   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASN B  92   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES          
REMARK 500    CYS B 117   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    TYR B 125   CB  -  CA  -  C   ANGL. DEV. =  12.7 DEGREES          
REMARK 500    TYR B 125   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LYS C 151   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG C 165   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG C 190   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG C 203   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ILE C 204   CB  -  CA  -  C   ANGL. DEV. =  12.5 DEGREES          
REMARK 500    GLU C 234   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ASP C 247   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    LEU D  26   CA  -  CB  -  CG  ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP D  32   N   -  CA  -  CB  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    VAL D  51   N   -  CA  -  C   ANGL. DEV. = -23.4 DEGREES          
REMARK 500    VAL D  54   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ASP D  68   CB  -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    GLU D  91   N   -  CA  -  C   ANGL. DEV. =  20.9 DEGREES          
REMARK 500    GLU D  91   CA  -  C   -  N   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    GLU D  91   O   -  C   -  N   ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASN D  92   C   -  N   -  CA  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    ASN D  92   N   -  CA  -  CB  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    CYS D 117   CB  -  CA  -  C   ANGL. DEV. = -15.6 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    ASN A 158       58.14   -146.62                                   
REMARK 500    ASP B  32     -158.41   -159.46                                   
REMARK 500    ALA B  48     -148.33    -97.57                                   
REMARK 500    GLU B  49      102.18    -56.08                                   
REMARK 500    SER B  50     -165.33    -66.11                                   
REMARK 500    GLU B  53      116.10   -169.36                                   
REMARK 500    ASN B  80      167.50    169.79                                   
REMARK 500    GLU B  91       39.09    -71.41                                   
REMARK 500    HIS B  93       70.94   -107.10                                   
REMARK 500    HIS B 102       43.42   -102.86                                   
REMARK 500    LYS C 151      105.63    -48.86                                   
REMARK 500    ASN C 158       58.15   -149.35                                   
REMARK 500    ALA C 172       37.66    -90.20                                   
REMARK 500    ASN C 173     -176.60    -66.94                                   
REMARK 500    CYS C 179       64.95   -153.30                                   
REMARK 500    LYS C 226      143.38    -37.34                                   
REMARK 500    LYS D   9       57.32    -64.01                                   
REMARK 500    LYS D  10     -149.36   -139.78                                   
REMARK 500    LYS D  12      171.23    -51.88                                   
REMARK 500    ASP D  32     -174.43   -173.89                                   
REMARK 500    ALA D  48     -145.58    -89.78                                   
REMARK 500    SER D  50      143.34    164.10                                   
REMARK 500    ASN D  80      164.48    159.58                                   
REMARK 500    GLU D  81      -35.51    -35.33                                   
REMARK 500    ASN D  92      -89.82    157.98                                   
REMARK 500    HIS D  93       67.42   -107.71                                   
REMARK 500    HIS D 102       44.95   -105.80                                   
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 SCR D 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCR B 1                   
DBREF  3CU1 A  150   249  UNP    P21802   FGFR2_HUMAN    150    249             
DBREF  3CU1 B    7   137  UNP    P05230   FGF1_HUMAN      22    152             
DBREF  3CU1 C  150   249  UNP    P21802   FGFR2_HUMAN    150    249             
DBREF  3CU1 D    7   137  UNP    P05230   FGF1_HUMAN      22    152             
SEQRES   1 A  100  ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU LYS MET          
SEQRES   2 A  100  GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN THR VAL          
SEQRES   3 A  100  LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET PRO THR          
SEQRES   4 A  100  MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS GLN GLU          
SEQRES   5 A  100  HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN HIS TRP          
SEQRES   6 A  100  SER LEU ILE MET GLU SER VAL VAL PRO SER ASP LYS GLY          
SEQRES   7 A  100  ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY SER ILE          
SEQRES   8 A  100  ASN HIS THR TYR HIS LEU ASP VAL VAL                          
SEQRES   1 B  131  ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY          
SEQRES   2 B  131  GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP          
SEQRES   3 B  131  GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN          
SEQRES   4 B  131  LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER          
SEQRES   5 B  131  THR GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY          
SEQRES   6 B  131  LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU          
SEQRES   7 B  131  PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR          
SEQRES   8 B  131  ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY          
SEQRES   9 B  131  LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR          
SEQRES  10 B  131  HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO          
SEQRES  11 B  131  VAL                                                          
SEQRES   1 C  100  ASN LYS ARG ALA PRO TYR TRP THR ASN THR GLU LYS MET          
SEQRES   2 C  100  GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA ASN THR VAL          
SEQRES   3 C  100  LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO MET PRO THR          
SEQRES   4 C  100  MET ARG TRP LEU LYS ASN GLY LYS GLU PHE LYS GLN GLU          
SEQRES   5 C  100  HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN GLN HIS TRP          
SEQRES   6 C  100  SER LEU ILE MET GLU SER VAL VAL PRO SER ASP LYS GLY          
SEQRES   7 C  100  ASN TYR THR CYS VAL VAL GLU ASN GLU TYR GLY SER ILE          
SEQRES   8 C  100  ASN HIS THR TYR HIS LEU ASP VAL VAL                          
SEQRES   1 D  131  ASN TYR LYS LYS PRO LYS LEU LEU TYR CYS SER ASN GLY          
SEQRES   2 D  131  GLY HIS PHE LEU ARG ILE LEU PRO ASP GLY THR VAL ASP          
SEQRES   3 D  131  GLY THR ARG ASP ARG SER ASP GLN HIS ILE GLN LEU GLN          
SEQRES   4 D  131  LEU SER ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER          
SEQRES   5 D  131  THR GLU THR GLY GLN TYR LEU ALA MET ASP THR ASP GLY          
SEQRES   6 D  131  LEU LEU TYR GLY SER GLN THR PRO ASN GLU GLU CYS LEU          
SEQRES   7 D  131  PHE LEU GLU ARG LEU GLU GLU ASN HIS TYR ASN THR TYR          
SEQRES   8 D  131  ILE SER LYS LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY          
SEQRES   9 D  131  LEU LYS LYS ASN GLY SER CYS LYS ARG GLY PRO ARG THR          
SEQRES  10 D  131  HIS TYR GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO          
SEQRES  11 D  131  VAL                                                          
HET    SCR  B   1      55                                                       
HET    SCR  D   1      55                                                       
HETNAM     SCR SUCROSE OCTASULFATE                                              
FORMUL   5  SCR    2(C12 H22 O35 S8)                                            
FORMUL   7  HOH   *343(H2 O)                                                    
HELIX    1   1 ASN A  158  GLU A  163  1                                   6    
HELIX    2   2 LYS A  199  ARG A  203  5                                   5    
HELIX    3   3 ASN A  211  HIS A  213  5                                   3    
HELIX    4   4 VAL A  222  LYS A  226  5                                   5    
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  158  GLU C  163  1                                   6    
HELIX   10  10 LYS C  199  ARG C  203  5                                   5    
HELIX   11  11 VAL C  222  LYS C  226  5                                   5    
HELIX   12  12 ASN D   80  CYS D   83  5                                   4    
HELIX   13  13 HIS D  102  ASN D  106  5                                   5    
HELIX   14  14 ARG D  119  THR D  123  5                                   5    
HELIX   15  15 GLN D  127  ILE D  130  5                                   4    
SHEET    1   A 2 ARG A 152  TRP A 156  0                                        
SHEET    2   A 2 ALA A 181  ASN A 184 -1  O  ASN A 184   N  ARG A 152           
SHEET    1   B 5 LEU A 166  PRO A 170  0                                        
SHEET    2   B 5 SER A 239  VAL A 249  1  O  ASP A 247   N  HIS A 167           
SHEET    3   B 5 GLY A 227  GLU A 234 -1  N  TYR A 229   O  TYR A 244           
SHEET    4   B 5 THR A 188  LYS A 193 -1  N  THR A 188   O  GLU A 234           
SHEET    5   B 5 LYS A 196  GLU A 197 -1  O  LYS A 196   N  LYS A 193           
SHEET    1   C 3 VAL A 175  ARG A 178  0                                        
SHEET    2   C 3 SER A 215  MET A 218 -1  O  LEU A 216   N  PHE A 177           
SHEET    3   C 3 LYS A 208  ARG A 210 -1  N  LYS A 208   O  ILE A 217           
SHEET    1   D 4 VAL B  31  THR B  34  0                                        
SHEET    2   D 4 HIS B  21  ILE B  25 -1  N  PHE B  22   O  THR B  34           
SHEET    3   D 4 LYS B  12  CYS B  16 -1  N  CYS B  16   O  HIS B  21           
SHEET    4   D 4 PHE B 132  PRO B 136 -1  O  LEU B 135   N  LEU B  13           
SHEET    1   E 2 LEU B  44  SER B  47  0                                        
SHEET    2   E 2 TYR B  55  SER B  58 -1  O  LYS B  57   N  GLN B  45           
SHEET    1   F 2 TYR B  64  MET B  67  0                                        
SHEET    2   F 2 LEU B  73  SER B  76 -1  O  SER B  76   N  TYR B  64           
SHEET    1   G 2 PHE B  85  LEU B  89  0                                        
SHEET    2   G 2 ASN B  95  SER B  99 -1  O  ILE B  98   N  LEU B  86           
SHEET    1   H 2 ARG C 152  TRP C 156  0                                        
SHEET    2   H 2 ALA C 181  ASN C 184 -1  O  ASN C 184   N  ARG C 152           
SHEET    1   I 5 LEU C 166  PRO C 170  0                                        
SHEET    2   I 5 SER C 239  VAL C 249  1  O  HIS C 245   N  HIS C 167           
SHEET    3   I 5 GLY C 227  GLU C 234 -1  N  TYR C 229   O  TYR C 244           
SHEET    4   I 5 THR C 188  LYS C 193 -1  N  THR C 188   O  GLU C 234           
SHEET    5   I 5 LYS C 196  GLU C 197 -1  O  LYS C 196   N  LYS C 193           
SHEET    1   J 3 VAL C 175  ARG C 178  0                                        
SHEET    2   J 3 SER C 215  MET C 218 -1  O  LEU C 216   N  PHE C 177           
SHEET    3   J 3 LYS C 208  ARG C 210 -1  N  LYS C 208   O  ILE C 217           
SHEET    1   K 4 VAL D  31  THR D  34  0                                        
SHEET    2   K 4 HIS D  21  ILE D  25 -1  N  PHE D  22   O  THR D  34           
SHEET    3   K 4 LEU D  13  CYS D  16 -1  N  CYS D  16   O  HIS D  21           
SHEET    4   K 4 PHE D 132  LEU D 135 -1  O  LEU D 135   N  LEU D  13           
SHEET    1   L 4 LEU D  44  SER D  47  0                                        
SHEET    2   L 4 GLU D  53  SER D  58 -1  O  LYS D  57   N  GLN D  45           
SHEET    3   L 4 PHE D  85  LEU D  89 -1  O  PHE D  85   N  VAL D  54           
SHEET    4   L 4 ASN D  95  SER D  99 -1  O  ILE D  98   N  LEU D  86           
SHEET    1   M 2 TYR D  64  MET D  67  0                                        
SHEET    2   M 2 LEU D  73  SER D  76 -1  O  SER D  76   N  TYR D  64           
SSBOND   1 CYS A  179    CYS A  231                          1555   1555  2.28  
SSBOND   2 CYS C  179    CYS C  231                          1555   1555  2.15  
CISPEP   1 ALA A  171    ALA A  172          0        -1.52                     
CISPEP   2 ASN A  184    PRO A  185          0        -2.28                     
CISPEP   3 ALA B   48    GLU B   49          0         0.42                     
CISPEP   4 SER B   50    VAL B   51          0         1.20                     
CISPEP   5 ASN B   92    HIS B   93          0         0.44                     
CISPEP   6 ALA C  171    ALA C  172          0        -1.79                     
CISPEP   7 ASN C  184    PRO C  185          0        -0.31                     
CISPEP   8 ALA D   48    GLU D   49          0         1.37                     
CISPEP   9 GLU D   49    SER D   50          0         1.01                     
CISPEP  10 SER D   50    VAL D   51          0         1.17                     
CISPEP  11 VAL D   51    GLY D   52          0        -0.96                     
CISPEP  12 GLU D   91    ASN D   92          0        -6.96                     
CISPEP  13 ASN D   92    HIS D   93          0         0.77                     
SITE     1 AC1 15 LYS A 161  LYS A 176  ARG A 178  ARG A 210                    
SITE     2 AC1 15 HIS A 213  SER A 215  ILE A 217  ASN D  18                    
SITE     3 AC1 15 LYS D 112  LYS D 113  ASN D 114  LYS D 118                    
SITE     4 AC1 15 ARG D 122  HIS D 124  GLN D 127                               
SITE     1 AC2 13 ASN B  18  LYS B 112  LYS B 113  LYS B 118                    
SITE     2 AC2 13 ARG B 122  GLN B 127  LYS C 161  LYS C 176                    
SITE     3 AC2 13 ARG C 178  ARG C 210  HIS C 213  SER C 215                    
SITE     4 AC2 13 LYS D 128                                                     
CRYST1   85.929  110.375   74.699  90.00  90.00  90.00 P 21 21 2     8          
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      0.011638  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013387        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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