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Database: PDB
Entry: 4LXO
LinkDB: 4LXO
Original site: 4LXO 
HEADER    CELL ADHESION                           30-JUL-13   4LXO              
TITLE     CRYSTAL STRUCTURE OF 9,10FN3-ELEGANTIN CHIMERA                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRONECTIN;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: FN, COLD-INSOLUBLE GLOBULIN, CIG, ANASTELLIN, UGL-Y1, UGL-  
COMPND   5 Y2, UGL-Y3;                                                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: FN1, FN;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-21A                                   
KEYWDS    FIBRONECTIN TYPE III DOMAIN, CELL BINDING, INTEGRIN ALPHA5BETA1, CELL 
KEYWDS   2 ADHESION                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.S.CHANG,J.H.SHIU,W.J.CHUANG                                         
REVDAT   1   06-AUG-14 4LXO    0                                                
JRNL        AUTH   Y.S.CHANG,J.H.SHIU,W.J.CHUANG                                
JRNL        TITL   DESIGN, STRUCTURE DETERMINATION, AND BIOLOGICAL EVALUATION   
JRNL        TITL 2 OF POTENT INTEGRIN ALPHA5BETA1-SPECIFIC ANTAGONIST USING THE 
JRNL        TITL 3 NINTH AND TENTH MODULE OF FIBRONECTIN TYPE III DOMAIN        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.42 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) : 1.42                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 90292                          
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4767                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.42                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13014                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 657                          
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2828                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 504                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.74000                                              
REMARK   3    B22 (A**2) : 0.74000                                              
REMARK   3    B33 (A**2) : -1.48000                                             
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): 0.055         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.054         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.028         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.560         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2902 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3980 ; 1.653 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   366 ; 7.384 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   122 ;35.130 ;22.295       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   428 ;12.345 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;22.327 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   458 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2248 ; 0.011 ; 0.022       
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):  1844 ; 2.456 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3032 ; 3.746 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1058 ; 4.795 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   948 ; 6.888 ; 4.500       
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):  2902 ; 2.479 ; 3.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1326        A  1509                          
REMARK   3    RESIDUE RANGE :   A  1601        A  1601                          
REMARK   3    RESIDUE RANGE :   A  1701        A  1980                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.486    3.058  -26.678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0784 T22:   0.0061                                     
REMARK   3      T33:   0.0359 T12:   0.0119                                     
REMARK   3      T13:  -0.0049 T23:   0.0069                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6462 L22:   0.1403                                     
REMARK   3      L33:   1.2987 L12:   0.1441                                     
REMARK   3      L13:   0.4504 L23:   0.0927                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0493 S12:   0.0039 S13:   0.0704                       
REMARK   3      S21:   0.0070 S22:   0.0099 S23:   0.0179                       
REMARK   3      S31:  -0.1946 S32:   0.0145 S33:   0.0394                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1326        B  1509                          
REMARK   3    RESIDUE RANGE :   B  1601        B  1601                          
REMARK   3    RESIDUE RANGE :   B  1701        B  1924                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.136  -13.270  -24.867              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0423 T22:   0.0125                                     
REMARK   3      T33:   0.0295 T12:   0.0153                                     
REMARK   3      T13:   0.0190 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9229 L22:   0.5488                                     
REMARK   3      L33:   0.8433 L12:   0.1514                                     
REMARK   3      L13:   0.2899 L23:  -0.1163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:   0.0650 S13:  -0.0906                       
REMARK   3      S21:   0.0139 S22:   0.0003 S23:  -0.0506                       
REMARK   3      S31:   0.0301 S32:   0.0762 S33:  -0.0129                       
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 4LXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-AUG-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB081215.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
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) : 1,0000                             
REMARK 200  MONOCHROMATOR                  : LN2-COOLED FIXED-EXIT DOUBLE       
REMARK 200                                   CRYSTAL SI(111) MONOCHROMATOR      
REMARK 200  OPTICS                         : VERTICALLY COLLIMATING             
REMARK 200                                   PREMIRROR, TOROIDAL FOCUSING       
REMARK 200                                   MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95355                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.420                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 49.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.42                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1FNF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CALCIUM ACETATE, 7%(W/V)            
REMARK 280  PEG10000, PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       87.94000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       37.55750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       37.55750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      131.91000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       37.55750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       37.55750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.97000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       37.55750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       37.55750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      131.91000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       37.55750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       37.55750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.97000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       87.94000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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  1319                                                      
REMARK 465     HIS A  1320                                                      
REMARK 465     HIS A  1321                                                      
REMARK 465     HIS A  1322                                                      
REMARK 465     HIS A  1323                                                      
REMARK 465     HIS A  1324                                                      
REMARK 465     HIS A  1325                                                      
REMARK 465     MET B  1319                                                      
REMARK 465     HIS B  1320                                                      
REMARK 465     HIS B  1321                                                      
REMARK 465     HIS B  1322                                                      
REMARK 465     HIS B  1323                                                      
REMARK 465     HIS B  1324                                                      
REMARK 465     HIS B  1325                                                      
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    HOH A  1735     O    HOH A  1951              1.45            
REMARK 500   O    HOH A  1757     O    HOH A  1972              1.56            
REMARK 500   O    HOH A  1925     O    HOH A  1968              1.60            
REMARK 500   O    HOH B  1702     O    HOH B  1901              1.74            
REMARK 500   O    HOH A  1707     O    HOH A  1953              1.78            
REMARK 500   O    HOH B  1714     O    HOH B  1924              1.78            
REMARK 500   O    SER A  1458     O    HOH A  1855              1.79            
REMARK 500   NH1  ARG A  1421     O    HOH A  1943              1.83            
REMARK 500   O    HOH B  1904     O    HOH B  1917              1.92            
REMARK 500   O    HOH A  1705     O    HOH B  1912              1.94            
REMARK 500   O    ASN A  1496     O    HOH A  1915              1.95            
REMARK 500   OG   SER B  1458     O    HOH B  1769              1.95            
REMARK 500   O    HOH B  1894     O    HOH B  1897              1.96            
REMARK 500   O    HOH A  1774     O    HOH A  1957              1.98            
REMARK 500   O    HOH A  1929     O    HOH B  1911              1.99            
REMARK 500   O    HOH A  1965     O    HOH B  1787              2.01            
REMARK 500   O    HOH A  1723     O    HOH A  1913              2.02            
REMARK 500   O    HOH A  1977     O    HOH B  1899              2.04            
REMARK 500   O    HOH A  1939     O    HOH A  1954              2.04            
REMARK 500   O    HOH A  1960     O    HOH A  1970              2.07            
REMARK 500   O    HOH A  1891     O    HOH A  1944              2.08            
REMARK 500   O    HOH A  1767     O    HOH A  1803              2.09            
REMARK 500   O    HOH B  1867     O    HOH B  1872              2.11            
REMARK 500   NH1  ARG A  1421     O    HOH A  1941              2.11            
REMARK 500   O    HOH A  1806     O    HOH B  1902              2.15            
REMARK 500   C    ASN A  1496     O    HOH A  1915              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1970     O    HOH B  1917     5454     1.92            
REMARK 500   O    HOH A  1956     O    HOH B  1896     5454     1.93            
REMARK 500   O    HOH A  1959     O    HOH B  1851     5454     1.94            
REMARK 500   O    HOH A  1723     O    HOH B  1860     5454     2.14            
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    LEU A1434   CB  -  CG  -  CD2 ANGL. DEV. =  20.8 DEGREES          
REMARK 500    ARG B1421   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 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    HIS A1365      -10.36     75.79                                   
REMARK 500    ALA A1441       49.74    -85.35                                   
REMARK 500    ASN A1457        5.26    -65.59                                   
REMARK 500    PRO A1497      144.99    -13.57                                   
REMARK 500    HIS B1365      -13.25     76.97                                   
REMARK 500    ALA B1441       48.01    -83.54                                   
REMARK 500    SER B1470       52.11    -93.21                                   
REMARK 500    ALA B1492       50.37     36.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A 1496     PRO A 1497                  149.70                    
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    ALA A1492        22.6      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 A1932        DISTANCE =  5.96 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B1601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A1438   OD1                                                    
REMARK 620 2 GLU B1392   OE1  91.2                                              
REMARK 620 3 HOH A1705   O    87.7 175.3                                        
REMARK 620 4 GLU B1364   OE1  80.1  82.9  92.4                                  
REMARK 620 5 HOH A1708   O   151.7  94.5  88.7 128.0                            
REMARK 620 6 TRP A1437   O    78.3  99.4  84.8 158.4  73.4                      
REMARK 620 7 GLU B1364   OE2 132.6  86.8  90.6  52.6  75.5 148.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1392   OE1                                                    
REMARK 620 2 ASP B1438   OD1  91.3                                              
REMARK 620 3 GLU A1364   OE1  82.8  79.9                                        
REMARK 620 4 TRP B1437   O   100.1  79.0 158.8                                  
REMARK 620 5 HOH B1848   O   175.0  88.5  92.3  84.8                            
REMARK 620 6 HOH B1718   O    95.5 151.4 128.5  72.4  87.0                      
REMARK 620 7 GLU A1364   OE2  85.0 133.2  53.3 147.6  91.5  75.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LXN   RELATED DB: PDB                                   
DBREF  4LXO A 1326  1509  UNP    P02751   FINC_HUMAN    1357   1540             
DBREF  4LXO B 1326  1509  UNP    P02751   FINC_HUMAN    1357   1540             
SEQADV 4LXO MET A 1319  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1320  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1321  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1322  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1323  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1324  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS A 1325  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO PRO A 1408  UNP  P02751    LEU  1439 ENGINEERED MUTATION            
SEQADV 4LXO CYS A 1490  UNP  P02751    VAL  1521 ENGINEERED MUTATION            
SEQADV 4LXO ARG A 1491  UNP  P02751    THR  1522 ENGINEERED MUTATION            
SEQADV 4LXO ALA A 1492  UNP  P02751    GLY  1523 ENGINEERED MUTATION            
SEQADV 4LXO ASN A 1496  UNP  P02751    SER  1527 ENGINEERED MUTATION            
SEQADV 4LXO ASP A 1498  UNP  P02751    ALA  1529 ENGINEERED MUTATION            
SEQADV 4LXO CYS A 1499  UNP  P02751    SER  1530 ENGINEERED MUTATION            
SEQADV 4LXO MET B 1319  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1320  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1321  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1322  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1323  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1324  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO HIS B 1325  UNP  P02751              EXPRESSION TAG                 
SEQADV 4LXO PRO B 1408  UNP  P02751    LEU  1439 ENGINEERED MUTATION            
SEQADV 4LXO CYS B 1490  UNP  P02751    VAL  1521 ENGINEERED MUTATION            
SEQADV 4LXO ARG B 1491  UNP  P02751    THR  1522 ENGINEERED MUTATION            
SEQADV 4LXO ALA B 1492  UNP  P02751    GLY  1523 ENGINEERED MUTATION            
SEQADV 4LXO ASN B 1496  UNP  P02751    SER  1527 ENGINEERED MUTATION            
SEQADV 4LXO ASP B 1498  UNP  P02751    ALA  1529 ENGINEERED MUTATION            
SEQADV 4LXO CYS B 1499  UNP  P02751    SER  1530 ENGINEERED MUTATION            
SEQRES   1 A  191  MET HIS HIS HIS HIS HIS HIS GLY LEU ASP SER PRO THR          
SEQRES   2 A  191  GLY ILE ASP PHE SER ASP ILE THR ALA ASN SER PHE THR          
SEQRES   3 A  191  VAL HIS TRP ILE ALA PRO ARG ALA THR ILE THR GLY TYR          
SEQRES   4 A  191  ARG ILE ARG HIS HIS PRO GLU HIS PHE SER GLY ARG PRO          
SEQRES   5 A  191  ARG GLU ASP ARG VAL PRO HIS SER ARG ASN SER ILE THR          
SEQRES   6 A  191  LEU THR ASN LEU THR PRO GLY THR GLU TYR VAL VAL SER          
SEQRES   7 A  191  ILE VAL ALA LEU ASN GLY ARG GLU GLU SER PRO PRO LEU          
SEQRES   8 A  191  ILE GLY GLN GLN SER THR VAL SER ASP VAL PRO ARG ASP          
SEQRES   9 A  191  LEU GLU VAL VAL ALA ALA THR PRO THR SER LEU LEU ILE          
SEQRES  10 A  191  SER TRP ASP ALA PRO ALA VAL THR VAL ARG TYR TYR ARG          
SEQRES  11 A  191  ILE THR TYR GLY GLU THR GLY GLY ASN SER PRO VAL GLN          
SEQRES  12 A  191  GLU PHE THR VAL PRO GLY SER LYS SER THR ALA THR ILE          
SEQRES  13 A  191  SER GLY LEU LYS PRO GLY VAL ASP TYR THR ILE THR VAL          
SEQRES  14 A  191  TYR ALA CYS ARG ALA ARG GLY ASP ASN PRO ASP CYS SER          
SEQRES  15 A  191  LYS PRO ILE SER ILE ASN TYR ARG THR                          
SEQRES   1 B  191  MET HIS HIS HIS HIS HIS HIS GLY LEU ASP SER PRO THR          
SEQRES   2 B  191  GLY ILE ASP PHE SER ASP ILE THR ALA ASN SER PHE THR          
SEQRES   3 B  191  VAL HIS TRP ILE ALA PRO ARG ALA THR ILE THR GLY TYR          
SEQRES   4 B  191  ARG ILE ARG HIS HIS PRO GLU HIS PHE SER GLY ARG PRO          
SEQRES   5 B  191  ARG GLU ASP ARG VAL PRO HIS SER ARG ASN SER ILE THR          
SEQRES   6 B  191  LEU THR ASN LEU THR PRO GLY THR GLU TYR VAL VAL SER          
SEQRES   7 B  191  ILE VAL ALA LEU ASN GLY ARG GLU GLU SER PRO PRO LEU          
SEQRES   8 B  191  ILE GLY GLN GLN SER THR VAL SER ASP VAL PRO ARG ASP          
SEQRES   9 B  191  LEU GLU VAL VAL ALA ALA THR PRO THR SER LEU LEU ILE          
SEQRES  10 B  191  SER TRP ASP ALA PRO ALA VAL THR VAL ARG TYR TYR ARG          
SEQRES  11 B  191  ILE THR TYR GLY GLU THR GLY GLY ASN SER PRO VAL GLN          
SEQRES  12 B  191  GLU PHE THR VAL PRO GLY SER LYS SER THR ALA THR ILE          
SEQRES  13 B  191  SER GLY LEU LYS PRO GLY VAL ASP TYR THR ILE THR VAL          
SEQRES  14 B  191  TYR ALA CYS ARG ALA ARG GLY ASP ASN PRO ASP CYS SER          
SEQRES  15 B  191  LYS PRO ILE SER ILE ASN TYR ARG THR                          
HET     CA  A1601       1                                                       
HET     CA  B1601       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *504(H2 O)                                                    
SHEET    1   A 3 THR A1331  SER A1336  0                                        
SHEET    2   A 3 PHE A1343  ILE A1348 -1  O  THR A1344   N  SER A1336           
SHEET    3   A 3 SER A1381  LEU A1384 -1  O  ILE A1382   N  VAL A1345           
SHEET    1   B 4 ARG A1371  VAL A1375  0                                        
SHEET    2   B 4 GLY A1356  PRO A1363 -1  N  ILE A1359   O  ASP A1373           
SHEET    3   B 4 GLU A1392  ASN A1401 -1  O  VAL A1394   N  HIS A1362           
SHEET    4   B 4 GLU A1404  GLU A1405 -1  O  GLU A1404   N  ASN A1401           
SHEET    1   C 4 ARG A1371  VAL A1375  0                                        
SHEET    2   C 4 GLY A1356  PRO A1363 -1  N  ILE A1359   O  ASP A1373           
SHEET    3   C 4 GLU A1392  ASN A1401 -1  O  VAL A1394   N  HIS A1362           
SHEET    4   C 4 LEU A1409  SER A1414 -1  O  GLY A1411   N  VAL A1395           
SHEET    1   D 3 ARG A1421  THR A1429  0                                        
SHEET    2   D 3 SER A1432  ASP A1438 -1  O  LEU A1434   N  ALA A1427           
SHEET    3   D 3 THR A1471  ILE A1474 -1  O  ILE A1474   N  LEU A1433           
SHEET    1   E 4 GLN A1461  PRO A1466  0                                        
SHEET    2   E 4 TYR A1446  GLU A1453 -1  N  ILE A1449   O  PHE A1463           
SHEET    3   E 4 ASP A1482  ARG A1491 -1  O  CYS A1490   N  TYR A1446           
SHEET    4   E 4 ASP A1498  CYS A1499 -1  O  ASP A1498   N  ARG A1491           
SHEET    1   F 4 GLN A1461  PRO A1466  0                                        
SHEET    2   F 4 TYR A1446  GLU A1453 -1  N  ILE A1449   O  PHE A1463           
SHEET    3   F 4 ASP A1482  ARG A1491 -1  O  CYS A1490   N  TYR A1446           
SHEET    4   F 4 ILE A1503  ARG A1508 -1  O  TYR A1507   N  TYR A1483           
SHEET    1   G 3 THR B1331  SER B1336  0                                        
SHEET    2   G 3 PHE B1343  ILE B1348 -1  O  THR B1344   N  SER B1336           
SHEET    3   G 3 SER B1381  LEU B1384 -1  O  ILE B1382   N  VAL B1345           
SHEET    1   H 4 ARG B1371  PRO B1376  0                                        
SHEET    2   H 4 GLY B1356  PRO B1363 -1  N  ILE B1359   O  ASP B1373           
SHEET    3   H 4 GLU B1392  ASN B1401 -1  O  LEU B1400   N  GLY B1356           
SHEET    4   H 4 GLU B1404  GLU B1405 -1  O  GLU B1404   N  ASN B1401           
SHEET    1   I 4 ARG B1371  PRO B1376  0                                        
SHEET    2   I 4 GLY B1356  PRO B1363 -1  N  ILE B1359   O  ASP B1373           
SHEET    3   I 4 GLU B1392  ASN B1401 -1  O  LEU B1400   N  GLY B1356           
SHEET    4   I 4 LEU B1409  SER B1414 -1  O  GLN B1413   N  TYR B1393           
SHEET    1   J 3 ARG B1421  THR B1429  0                                        
SHEET    2   J 3 SER B1432  ASP B1438 -1  O  LEU B1434   N  ALA B1427           
SHEET    3   J 3 THR B1471  ILE B1474 -1  O  ILE B1474   N  LEU B1433           
SHEET    1   K 4 GLN B1461  PRO B1466  0                                        
SHEET    2   K 4 TYR B1446  GLU B1453 -1  N  ILE B1449   O  PHE B1463           
SHEET    3   K 4 TYR B1483  CYS B1490 -1  O  THR B1484   N  GLY B1452           
SHEET    4   K 4 ILE B1503  TYR B1507 -1  O  TYR B1507   N  TYR B1483           
SSBOND   1 CYS A 1490    CYS A 1499                          1555   1555  2.13  
SSBOND   2 CYS B 1490    CYS B 1499                          1555   1555  2.08  
LINK         OD1 ASP A1438                CA    CA B1601     1555   1555  2.30  
LINK         OE1 GLU A1392                CA    CA A1601     1555   1555  2.30  
LINK         OE1 GLU B1392                CA    CA B1601     1555   1555  2.30  
LINK         OD1 ASP B1438                CA    CA A1601     1555   1555  2.33  
LINK         OE1 GLU A1364                CA    CA A1601     1555   1555  2.36  
LINK         O   TRP B1437                CA    CA A1601     1555   1555  2.39  
LINK        CA    CA A1601                 O   HOH B1848     1555   1555  2.40  
LINK        CA    CA B1601                 O   HOH A1705     1555   1555  2.40  
LINK         OE1 GLU B1364                CA    CA B1601     1555   1555  2.42  
LINK        CA    CA B1601                 O   HOH A1708     1555   1555  2.42  
LINK         O   TRP A1437                CA    CA B1601     1555   1555  2.43  
LINK        CA    CA A1601                 O   HOH B1718     1555   1555  2.44  
LINK         OE2 GLU A1364                CA    CA A1601     1555   1555  2.45  
LINK         OE2 GLU B1364                CA    CA B1601     1555   1555  2.48  
SITE     1 AC1  6 GLU A1364  GLU A1392  TRP B1437  ASP B1438                    
SITE     2 AC1  6 HOH B1718  HOH B1848                                          
SITE     1 AC2  6 TRP A1437  ASP A1438  HOH A1705  HOH A1708                    
SITE     2 AC2  6 GLU B1364  GLU B1392                                          
CRYST1   75.115   75.115  175.880  90.00  90.00  90.00 P 43 21 2    16          
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      0.013313  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005686        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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