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Database: PDB
Entry: 3PGV
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HEADER    HYDROLASE                               02-NOV-10   3PGV              
TITLE     CRYSTAL STRUCTURE OF A HALOACID DEHALOGENASE-LIKE HYDROLASE           
TITLE    2 (KPN_04322) FROM KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 78578 AT
TITLE    3 2.39 A RESOLUTION                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOACID DEHALOGENASE-LIKE HYDROLASE;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CONSERVED PROTEIN, PHOSPHATASE-LIKE DOMAIN;                 
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE;        
SOURCE   3 ORGANISM_TAXID: 272620;                                              
SOURCE   4 STRAIN: MGH 78578;                                                   
SOURCE   5 GENE: YIGL, KPN78578_42660, KPN_04322;                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,      
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   2   20-JUL-11 3PGV    1       KEYWDS                                   
REVDAT   1   15-DEC-10 3PGV    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A HALOACID DEHALOGENASE-LIKE HYDROLASE  
JRNL        TITL 2 (KPN_04322) FROM KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 
JRNL        TITL 3 78578 AT 2.39 A RESOLUTION                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.78                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 48579                          
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)  : 0.169                          
REMARK   3   R VALUE            (WORKING SET)  : 0.167                          
REMARK   3   FREE R VALUE                      : 0.211                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.040                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2450                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.39                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.45                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3529                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2158                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3324                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2133                   
REMARK   3   BIN FREE R VALUE                        : 0.2573                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.81                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 205                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8111                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 428                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.56                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.61790                                              
REMARK   3    B22 (A**2) : -11.18320                                            
REMARK   3    B33 (A**2) : 2.56530                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.96990                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : NULL                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8491   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11463  ; 6.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3029   ; 8.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 224    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1244   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8491   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1063   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 10001  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.57                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.12                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.18                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A    2    A  265                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.1552   45.4313   20.0200           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1964 T22:    0.0371                                    
REMARK   3     T33:   -0.1007 T12:   -0.0352                                    
REMARK   3     T13:    0.0230 T23:    0.0565                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5708 L22:    1.5798                                    
REMARK   3     L33:    0.9512 L12:    0.9589                                    
REMARK   3     L13:    0.5576 L23:   -0.0617                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0299 S12:   -0.0908 S13:   -0.3537                     
REMARK   3     S21:    0.0500 S22:   -0.0226 S23:   -0.0350                     
REMARK   3     S31:   -0.0316 S32:    0.0601 S33:   -0.0073                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   B    1    B  266                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.4982   50.7601   62.5212           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0748 T22:   -0.0224                                    
REMARK   3     T33:   -0.1067 T12:    0.0799                                    
REMARK   3     T13:   -0.0019 T23:    0.0075                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5983 L22:    0.3873                                    
REMARK   3     L33:    1.6030 L12:   -0.4763                                    
REMARK   3     L13:   -0.3165 L23:    0.0286                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0215 S12:   -0.0845 S13:    0.1342                     
REMARK   3     S21:    0.0422 S22:    0.0629 S23:   -0.0619                     
REMARK   3     S31:   -0.0230 S32:   -0.0168 S33:   -0.0414                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   C    1    C  266                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -42.3040   31.1927   19.1177           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2425 T22:    0.0226                                    
REMARK   3     T33:   -0.1783 T12:   -0.0764                                    
REMARK   3     T13:   -0.0220 T23:    0.0008                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.7162 L22:    1.6150                                    
REMARK   3     L33:    0.8790 L12:    1.8777                                    
REMARK   3     L13:   -0.3245 L23:   -0.4224                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1942 S12:   -0.5152 S13:   -0.2602                     
REMARK   3     S21:    0.0943 S22:   -0.2502 S23:   -0.1482                     
REMARK   3     S31:   -0.0398 S32:    0.0199 S33:    0.0560                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   D    1    D  266                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.0154   34.6430   61.0768           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1445 T22:    0.0816                                    
REMARK   3     T33:   -0.1183 T12:    0.0602                                    
REMARK   3     T13:   -0.0109 T23:    0.0057                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7325 L22:    1.3038                                    
REMARK   3     L33:    1.0848 L12:   -1.1648                                    
REMARK   3     L13:   -0.4064 L23:    0.4707                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0131 S12:    0.0911 S13:    0.1854                     
REMARK   3     S21:    0.0285 S22:    0.0000 S23:   -0.1440                     
REMARK   3     S31:    0.0176 S32:    0.0401 S33:   -0.0131                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1.A MET-INHIBITION PROTOCOL WAS USED      
REMARK   3  FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE   
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75   
REMARK   3  FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET               
REMARK   3  INCORPORATION. 2.PROTEIN ATOM RECORD CONTAINS SUM OF TLS AND        
REMARK   3  RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND           
REMARK   3  RESIDUAL U FACTORS.3.4-(2-HYDROXYETHYL)-1-PIPERAZINE                
REMARK   3  ETHANESULFONIC ACID (EPE), GLYCEROL (GOL), AND 1,2 ETHANEDIOL       
REMARK   3  (EDO) FROM THE CRYSTALLIZATION AND CRYOGENIC CONDITIONS HAVE BEEN   
REMARK   3  MODELED INTO THE STRUCTURE. 4.A METAL ION WITHIN COORDINATION       
REMARK   3  DISTANCE OF THE SIDECHAINS OF ASP 8, ASP 214, THE CARBONYL OXYGEN   
REMARK   3  OF ASP 10, AND OXYGEN ATOMS OF GLYCEROL, AND 4-(2-HYDROXYETHYL)-    
REMARK   3  1-PIPERAZINE ETHANESULFONIC ACID. IN SOME RELATED STRUCTURES,       
REMARK   3  THIS METAL ION IS MODELED AS CALCIUM, AND IN OTHER RELATED          
REMARK   3  STRUCTURES, IT IS MODELED AS MAGNESIUM. HERE THE METAL ION IS       
REMARK   3  MODELD AS CALCIUM BASED ON A BETTER FIT TO ELECTRON DENSITY MAPS    
REMARK   3  THAN THAT FOR MAGNESIUM. 5. NCS RESTRAINTS WERE APPLIED USING       
REMARK   3  BUSTER'S LSSR RESTRAINT REPRESENTATION. 6. THE REFINEMENT WAS       
REMARK   3  RESTRAINED AGAINST THE SAD PHASES.                                  
REMARK   4                                                                      
REMARK   4 3PGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-NOV-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB062357.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97849                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48581                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.778                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.0400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: DATA WERE SCALED USING XSCALE WITH FRIEDEL PAIRS KEPT AS     
REMARK 200  SEPARATE WHEN COMPUTING R-SYM, COMPLETENESS AND <I/SIGMA(I)>        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.0% GLYCEROL, 8.50% ISO-PROPANOL,      
REMARK 280  17.0% PEG-4000, 0.1M HEPES PH 7.5, NANODROP, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       59.28450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.98050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       59.28450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.98050            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: CRYSTAL PACKING SUGGESTS THE ASSIGNMENT OF A MONOMER AS THE  
REMARK 300 POSSIBLE OLIGOMERIZATION STATE IN SOLUTION.                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MSE A   -18                                                      
REMARK 465     GLY A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     ASP A   -15                                                      
REMARK 465     LYS A   -14                                                      
REMARK 465     ILE A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     GLU A   120                                                      
REMARK 465     MSE A   121                                                      
REMARK 465     ARG A   122                                                      
REMARK 465     ASP A   266                                                      
REMARK 465     MSE B   -18                                                      
REMARK 465     GLY B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     ASP B   -15                                                      
REMARK 465     LYS B   -14                                                      
REMARK 465     ILE B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PHE B    -2                                                      
REMARK 465     GLN B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLU B   119                                                      
REMARK 465     GLU B   120                                                      
REMARK 465     MSE B   121                                                      
REMARK 465     ARG B   122                                                      
REMARK 465     PHE B   123                                                      
REMARK 465     PHE B   124                                                      
REMARK 465     LYS B   125                                                      
REMARK 465     GLU B   126                                                      
REMARK 465     ALA B   127                                                      
REMARK 465     MSE C   -18                                                      
REMARK 465     GLY C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     ASP C   -15                                                      
REMARK 465     LYS C   -14                                                      
REMARK 465     ILE C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     ASN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     TYR C    -3                                                      
REMARK 465     PHE C    -2                                                      
REMARK 465     GLN C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     GLU C   119                                                      
REMARK 465     GLU C   120                                                      
REMARK 465     MSE C   121                                                      
REMARK 465     ARG C   122                                                      
REMARK 465     PHE C   123                                                      
REMARK 465     PHE C   124                                                      
REMARK 465     LYS C   125                                                      
REMARK 465     GLU C   126                                                      
REMARK 465     MSE D   -18                                                      
REMARK 465     GLY D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     ASP D   -15                                                      
REMARK 465     LYS D   -14                                                      
REMARK 465     ILE D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     ASN D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     TYR D    -3                                                      
REMARK 465     PHE D    -2                                                      
REMARK 465     GLN D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     GLU D   119                                                      
REMARK 465     GLU D   120                                                      
REMARK 465     MSE D   121                                                      
REMARK 465     ARG D   122                                                      
REMARK 465     PHE D   123                                                      
REMARK 465     PHE D   124                                                      
REMARK 465     LYS D   125                                                      
REMARK 465     GLU D   126                                                      
REMARK 465     ALA D   127                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  29    CE   NZ                                             
REMARK 470     LYS A 262    CE   NZ                                             
REMARK 470     GLN B 162    CG   CD   OE1  NE2                                  
REMARK 470     MSE C   1    CG  SE    CE                                        
REMARK 470     LYS C 132    CE   NZ                                             
REMARK 470     GLU C 138    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 152    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 162    CD   OE1  NE2                                       
REMARK 470     LEU C 265    CG   CD1  CD2                                       
REMARK 470     ASP C 266    CG   OD1  OD2                                       
REMARK 470     LYS D  29    CD   CE   NZ                                        
REMARK 470     LYS D 132    CE   NZ                                             
REMARK 470     GLU D 152    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A   9      -71.42   -101.43                                   
REMARK 500    THR A  12      -84.85   -122.23                                   
REMARK 500    GLU A 108     -120.07     52.72                                   
REMARK 500    SER A 177      -72.34   -104.12                                   
REMARK 500    LEU B   9      -72.22   -101.21                                   
REMARK 500    THR B  12      -84.81   -122.25                                   
REMARK 500    GLU B 108     -120.31     52.47                                   
REMARK 500    SER B 177      -72.75   -102.35                                   
REMARK 500    LEU C   9      -71.54   -101.84                                   
REMARK 500    THR C  12      -85.24   -123.88                                   
REMARK 500    GLU C 108     -120.85     52.58                                   
REMARK 500    SER C 177      -71.82   -103.15                                   
REMARK 500    LEU D   9      -72.71   -101.35                                   
REMARK 500    THR D  12      -84.91   -124.11                                   
REMARK 500    GLU D 108     -119.59     52.02                                   
REMARK 500    SER D 177      -71.99   -103.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     EPE A  268                                                       
REMARK 610     EPE C  270                                                       
REMARK 610     EPE D  271                                                       
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 C 267  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C   8   OD2                                                    
REMARK 620 2 ASP C 214   OD1  80.2                                              
REMARK 620 3 EPE C 270   O1S 114.1 165.7                                        
REMARK 620 4 ASP C  10   O    80.8  89.5  92.8                                  
REMARK 620 5 GOL C 274   O2  142.2  75.0  92.4  71.0                            
REMARK 620 6 HOH C 644   O    81.6  96.9  85.7 159.9 129.1                      
REMARK 620 7 GOL C 274   O1  145.1  81.9  85.7 128.7  57.9  71.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 267  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   8   OD2                                                    
REMARK 620 2 ASP A 214   OD1  80.1                                              
REMARK 620 3 ASP A  10   O    80.7  91.4                                        
REMARK 620 4 EPE A 268   O1S 112.4 167.4  89.9                                  
REMARK 620 5 HOH A 645   O    81.3  99.2 157.2  84.1                            
REMARK 620 6 GOL A 272   O1  142.5  91.8 136.3  78.7  63.9                      
REMARK 620 7 GOL A 272   O2  153.9  87.6  76.7  80.5 123.6  60.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 267  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B   8   OD2                                                    
REMARK 620 2 ASP B  10   O    81.5                                              
REMARK 620 3 EPE B 269   O1S 117.9 100.9                                        
REMARK 620 4 ASP B 214   OD1  76.6  91.2 162.1                                  
REMARK 620 5 GOL B 273   O2  151.5  75.2  82.8  87.7                            
REMARK 620 6 HOH B 648   O    79.5 160.2  83.4  89.7 124.7                      
REMARK 620 7 GOL B 273   O3  131.5 140.1  83.7  78.5  66.0  59.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 267  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 EPE D 271   O1S                                                    
REMARK 620 2 ASP D   8   OD2 112.8                                              
REMARK 620 3 ASP D  10   O    96.3  79.3                                        
REMARK 620 4 HOH D 463   O    84.4  74.3 151.4                                  
REMARK 620 5 ASP D 214   OD1 171.7  74.7  88.5  94.6                            
REMARK 620 6 GOL D 275   O2   97.8 140.4  72.6 135.8  77.2                      
REMARK 620 7 GOL D 275   O3   86.9 134.6 141.4  67.2  85.2  68.8                
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 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 268                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 272                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 276                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 277                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 293                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE B 269                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 273                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 289                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 290                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE C 270                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 274                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 288                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 267                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE D 271                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 275                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 281                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 282                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 283                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 284                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 285                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 291                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 292                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 388334   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT (RESIDUES 1-266) WAS EXPRESSED WITH AND CONTAINS A     
REMARK 999 PURIFICATION TAG MGSDKIHHHHHHENLYFQG.                                
DBREF  3PGV A    1   266  UNP    A6TGK6   A6TGK6_KLEP7     1    266             
DBREF  3PGV B    1   266  UNP    A6TGK6   A6TGK6_KLEP7     1    266             
DBREF  3PGV C    1   266  UNP    A6TGK6   A6TGK6_KLEP7     1    266             
DBREF  3PGV D    1   266  UNP    A6TGK6   A6TGK6_KLEP7     1    266             
SEQADV 3PGV MSE A  -18  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY A  -17  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV SER A  -16  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASP A  -15  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LYS A  -14  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ILE A  -13  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A  -12  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A  -11  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A  -10  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A   -9  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A   -8  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS A   -7  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLU A   -6  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASN A   -5  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LEU A   -4  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV TYR A   -3  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV PHE A   -2  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLN A   -1  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY A    0  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV MSE B  -18  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY B  -17  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV SER B  -16  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASP B  -15  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LYS B  -14  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ILE B  -13  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B  -12  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B  -11  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B  -10  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B   -9  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B   -8  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS B   -7  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLU B   -6  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASN B   -5  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LEU B   -4  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV TYR B   -3  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV PHE B   -2  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLN B   -1  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY B    0  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV MSE C  -18  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY C  -17  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV SER C  -16  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASP C  -15  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LYS C  -14  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ILE C  -13  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C  -12  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C  -11  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C  -10  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C   -9  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C   -8  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS C   -7  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLU C   -6  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASN C   -5  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LEU C   -4  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV TYR C   -3  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV PHE C   -2  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLN C   -1  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY C    0  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV MSE D  -18  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY D  -17  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV SER D  -16  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASP D  -15  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LYS D  -14  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ILE D  -13  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D  -12  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D  -11  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D  -10  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D   -9  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D   -8  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV HIS D   -7  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLU D   -6  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV ASN D   -5  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV LEU D   -4  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV TYR D   -3  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV PHE D   -2  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLN D   -1  UNP  A6TGK6              LEADER SEQUENCE                
SEQADV 3PGV GLY D    0  UNP  A6TGK6              LEADER SEQUENCE                
SEQRES   1 A  285  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 A  285  ASN LEU TYR PHE GLN GLY MSE TYR GLN VAL VAL ALA SER          
SEQRES   3 A  285  ASP LEU ASP GLY THR LEU LEU SER PRO ASP HIS PHE LEU          
SEQRES   4 A  285  THR PRO TYR ALA LYS GLU THR LEU LYS LEU LEU THR ALA          
SEQRES   5 A  285  ARG GLY ILE ASN PHE VAL PHE ALA THR GLY ARG HIS TYR          
SEQRES   6 A  285  ILE ASP VAL GLY GLN ILE ARG ASP ASN LEU GLY ILE ARG          
SEQRES   7 A  285  SER TYR MSE ILE THR SER ASN GLY ALA ARG VAL HIS ASP          
SEQRES   8 A  285  SER ASP GLY GLN GLN ILE PHE ALA HIS ASN LEU ASP ARG          
SEQRES   9 A  285  ASP ILE ALA ALA ASP LEU PHE GLU ILE VAL ARG ASN ASP          
SEQRES  10 A  285  PRO LYS ILE VAL THR ASN VAL TYR ARG GLU ASP GLU TRP          
SEQRES  11 A  285  TYR MSE ASN ARG HIS ARG PRO GLU GLU MSE ARG PHE PHE          
SEQRES  12 A  285  LYS GLU ALA VAL PHE ASN TYR LYS LEU TYR GLU PRO GLY          
SEQRES  13 A  285  GLU LEU ASP PRO GLN GLY ILE SER LYS VAL PHE PHE THR          
SEQRES  14 A  285  CYS GLU ASP HIS GLU HIS LEU LEU PRO LEU GLU GLN ALA          
SEQRES  15 A  285  MSE ASN ALA ARG TRP GLY ASP ARG VAL ASN VAL SER PHE          
SEQRES  16 A  285  SER THR LEU THR CYS LEU GLU VAL MSE ALA GLY GLY VAL          
SEQRES  17 A  285  SER LYS GLY HIS ALA LEU GLU ALA VAL ALA LYS MSE LEU          
SEQRES  18 A  285  GLY TYR THR LEU SER ASP CYS ILE ALA PHE GLY ASP GLY          
SEQRES  19 A  285  MSE ASN ASP ALA GLU MSE LEU SER MSE ALA GLY LYS GLY          
SEQRES  20 A  285  CYS ILE MSE ALA ASN ALA HIS GLN ARG LEU LYS ASP LEU          
SEQRES  21 A  285  HIS PRO GLU LEU GLU VAL ILE GLY SER ASN ALA ASP ASP          
SEQRES  22 A  285  ALA VAL PRO ARG TYR LEU ARG LYS LEU TYR LEU ASP              
SEQRES   1 B  285  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 B  285  ASN LEU TYR PHE GLN GLY MSE TYR GLN VAL VAL ALA SER          
SEQRES   3 B  285  ASP LEU ASP GLY THR LEU LEU SER PRO ASP HIS PHE LEU          
SEQRES   4 B  285  THR PRO TYR ALA LYS GLU THR LEU LYS LEU LEU THR ALA          
SEQRES   5 B  285  ARG GLY ILE ASN PHE VAL PHE ALA THR GLY ARG HIS TYR          
SEQRES   6 B  285  ILE ASP VAL GLY GLN ILE ARG ASP ASN LEU GLY ILE ARG          
SEQRES   7 B  285  SER TYR MSE ILE THR SER ASN GLY ALA ARG VAL HIS ASP          
SEQRES   8 B  285  SER ASP GLY GLN GLN ILE PHE ALA HIS ASN LEU ASP ARG          
SEQRES   9 B  285  ASP ILE ALA ALA ASP LEU PHE GLU ILE VAL ARG ASN ASP          
SEQRES  10 B  285  PRO LYS ILE VAL THR ASN VAL TYR ARG GLU ASP GLU TRP          
SEQRES  11 B  285  TYR MSE ASN ARG HIS ARG PRO GLU GLU MSE ARG PHE PHE          
SEQRES  12 B  285  LYS GLU ALA VAL PHE ASN TYR LYS LEU TYR GLU PRO GLY          
SEQRES  13 B  285  GLU LEU ASP PRO GLN GLY ILE SER LYS VAL PHE PHE THR          
SEQRES  14 B  285  CYS GLU ASP HIS GLU HIS LEU LEU PRO LEU GLU GLN ALA          
SEQRES  15 B  285  MSE ASN ALA ARG TRP GLY ASP ARG VAL ASN VAL SER PHE          
SEQRES  16 B  285  SER THR LEU THR CYS LEU GLU VAL MSE ALA GLY GLY VAL          
SEQRES  17 B  285  SER LYS GLY HIS ALA LEU GLU ALA VAL ALA LYS MSE LEU          
SEQRES  18 B  285  GLY TYR THR LEU SER ASP CYS ILE ALA PHE GLY ASP GLY          
SEQRES  19 B  285  MSE ASN ASP ALA GLU MSE LEU SER MSE ALA GLY LYS GLY          
SEQRES  20 B  285  CYS ILE MSE ALA ASN ALA HIS GLN ARG LEU LYS ASP LEU          
SEQRES  21 B  285  HIS PRO GLU LEU GLU VAL ILE GLY SER ASN ALA ASP ASP          
SEQRES  22 B  285  ALA VAL PRO ARG TYR LEU ARG LYS LEU TYR LEU ASP              
SEQRES   1 C  285  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 C  285  ASN LEU TYR PHE GLN GLY MSE TYR GLN VAL VAL ALA SER          
SEQRES   3 C  285  ASP LEU ASP GLY THR LEU LEU SER PRO ASP HIS PHE LEU          
SEQRES   4 C  285  THR PRO TYR ALA LYS GLU THR LEU LYS LEU LEU THR ALA          
SEQRES   5 C  285  ARG GLY ILE ASN PHE VAL PHE ALA THR GLY ARG HIS TYR          
SEQRES   6 C  285  ILE ASP VAL GLY GLN ILE ARG ASP ASN LEU GLY ILE ARG          
SEQRES   7 C  285  SER TYR MSE ILE THR SER ASN GLY ALA ARG VAL HIS ASP          
SEQRES   8 C  285  SER ASP GLY GLN GLN ILE PHE ALA HIS ASN LEU ASP ARG          
SEQRES   9 C  285  ASP ILE ALA ALA ASP LEU PHE GLU ILE VAL ARG ASN ASP          
SEQRES  10 C  285  PRO LYS ILE VAL THR ASN VAL TYR ARG GLU ASP GLU TRP          
SEQRES  11 C  285  TYR MSE ASN ARG HIS ARG PRO GLU GLU MSE ARG PHE PHE          
SEQRES  12 C  285  LYS GLU ALA VAL PHE ASN TYR LYS LEU TYR GLU PRO GLY          
SEQRES  13 C  285  GLU LEU ASP PRO GLN GLY ILE SER LYS VAL PHE PHE THR          
SEQRES  14 C  285  CYS GLU ASP HIS GLU HIS LEU LEU PRO LEU GLU GLN ALA          
SEQRES  15 C  285  MSE ASN ALA ARG TRP GLY ASP ARG VAL ASN VAL SER PHE          
SEQRES  16 C  285  SER THR LEU THR CYS LEU GLU VAL MSE ALA GLY GLY VAL          
SEQRES  17 C  285  SER LYS GLY HIS ALA LEU GLU ALA VAL ALA LYS MSE LEU          
SEQRES  18 C  285  GLY TYR THR LEU SER ASP CYS ILE ALA PHE GLY ASP GLY          
SEQRES  19 C  285  MSE ASN ASP ALA GLU MSE LEU SER MSE ALA GLY LYS GLY          
SEQRES  20 C  285  CYS ILE MSE ALA ASN ALA HIS GLN ARG LEU LYS ASP LEU          
SEQRES  21 C  285  HIS PRO GLU LEU GLU VAL ILE GLY SER ASN ALA ASP ASP          
SEQRES  22 C  285  ALA VAL PRO ARG TYR LEU ARG LYS LEU TYR LEU ASP              
SEQRES   1 D  285  MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS GLU          
SEQRES   2 D  285  ASN LEU TYR PHE GLN GLY MSE TYR GLN VAL VAL ALA SER          
SEQRES   3 D  285  ASP LEU ASP GLY THR LEU LEU SER PRO ASP HIS PHE LEU          
SEQRES   4 D  285  THR PRO TYR ALA LYS GLU THR LEU LYS LEU LEU THR ALA          
SEQRES   5 D  285  ARG GLY ILE ASN PHE VAL PHE ALA THR GLY ARG HIS TYR          
SEQRES   6 D  285  ILE ASP VAL GLY GLN ILE ARG ASP ASN LEU GLY ILE ARG          
SEQRES   7 D  285  SER TYR MSE ILE THR SER ASN GLY ALA ARG VAL HIS ASP          
SEQRES   8 D  285  SER ASP GLY GLN GLN ILE PHE ALA HIS ASN LEU ASP ARG          
SEQRES   9 D  285  ASP ILE ALA ALA ASP LEU PHE GLU ILE VAL ARG ASN ASP          
SEQRES  10 D  285  PRO LYS ILE VAL THR ASN VAL TYR ARG GLU ASP GLU TRP          
SEQRES  11 D  285  TYR MSE ASN ARG HIS ARG PRO GLU GLU MSE ARG PHE PHE          
SEQRES  12 D  285  LYS GLU ALA VAL PHE ASN TYR LYS LEU TYR GLU PRO GLY          
SEQRES  13 D  285  GLU LEU ASP PRO GLN GLY ILE SER LYS VAL PHE PHE THR          
SEQRES  14 D  285  CYS GLU ASP HIS GLU HIS LEU LEU PRO LEU GLU GLN ALA          
SEQRES  15 D  285  MSE ASN ALA ARG TRP GLY ASP ARG VAL ASN VAL SER PHE          
SEQRES  16 D  285  SER THR LEU THR CYS LEU GLU VAL MSE ALA GLY GLY VAL          
SEQRES  17 D  285  SER LYS GLY HIS ALA LEU GLU ALA VAL ALA LYS MSE LEU          
SEQRES  18 D  285  GLY TYR THR LEU SER ASP CYS ILE ALA PHE GLY ASP GLY          
SEQRES  19 D  285  MSE ASN ASP ALA GLU MSE LEU SER MSE ALA GLY LYS GLY          
SEQRES  20 D  285  CYS ILE MSE ALA ASN ALA HIS GLN ARG LEU LYS ASP LEU          
SEQRES  21 D  285  HIS PRO GLU LEU GLU VAL ILE GLY SER ASN ALA ASP ASP          
SEQRES  22 D  285  ALA VAL PRO ARG TYR LEU ARG LYS LEU TYR LEU ASP              
MODRES 3PGV MSE A   62  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  113  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  164  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  201  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  221  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  224  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE A  231  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B   62  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  113  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  164  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  185  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  201  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  216  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  221  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  224  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE B  231  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C   62  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  113  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  164  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  185  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  201  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  216  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  221  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  224  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE C  231  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D   62  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  113  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  164  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  185  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  201  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  216  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  221  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  224  MET  SELENOMETHIONINE                                   
MODRES 3PGV MSE D  231  MET  SELENOMETHIONINE                                   
HET    MSE  A  62       8                                                       
HET    MSE  A 113       8                                                       
HET    MSE  A 164       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 201       8                                                       
HET    MSE  A 216       8                                                       
HET    MSE  A 221       8                                                       
HET    MSE  A 224       8                                                       
HET    MSE  A 231       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  62       8                                                       
HET    MSE  B 113       8                                                       
HET    MSE  B 164       8                                                       
HET    MSE  B 185       8                                                       
HET    MSE  B 201       8                                                       
HET    MSE  B 216       8                                                       
HET    MSE  B 221       8                                                       
HET    MSE  B 224       8                                                       
HET    MSE  B 231       8                                                       
HET    MSE  C   1       5                                                       
HET    MSE  C  62       8                                                       
HET    MSE  C 113       8                                                       
HET    MSE  C 164       8                                                       
HET    MSE  C 185       8                                                       
HET    MSE  C 201       8                                                       
HET    MSE  C 216       8                                                       
HET    MSE  C 221       8                                                       
HET    MSE  C 224       8                                                       
HET    MSE  C 231       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D  62       8                                                       
HET    MSE  D 113       8                                                       
HET    MSE  D 164       8                                                       
HET    MSE  D 185       8                                                       
HET    MSE  D 201       8                                                       
HET    MSE  D 216       8                                                       
HET    MSE  D 221       8                                                       
HET    MSE  D 224       8                                                       
HET    MSE  D 231       8                                                       
HET     CA  A 267       1                                                       
HET    EPE  A 268      13                                                       
HET    GOL  A 272       6                                                       
HET    EDO  A 276       4                                                       
HET    EDO  A 277       4                                                       
HET    EDO  A 278       4                                                       
HET    EDO  A 287       4                                                       
HET    EDO  A 293       4                                                       
HET     CA  B 267       1                                                       
HET    EPE  B 269      15                                                       
HET    GOL  B 273       6                                                       
HET    EDO  B 289       4                                                       
HET    EDO  B 290       4                                                       
HET     CA  C 267       1                                                       
HET    EPE  C 270      14                                                       
HET    GOL  C 274       6                                                       
HET    EDO  C 286       4                                                       
HET    EDO  C 288       4                                                       
HET     CA  D 267       1                                                       
HET    EPE  D 271      14                                                       
HET    GOL  D 275       6                                                       
HET    EDO  D 279       4                                                       
HET    EDO  D 280       4                                                       
HET    EDO  D 281       4                                                       
HET    EDO  D 282       4                                                       
HET    EDO  D 283       4                                                       
HET    EDO  D 284       4                                                       
HET    EDO  D 285       4                                                       
HET    EDO  D 291       4                                                       
HET    EDO  D 292       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CA CALCIUM ION                                                      
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EPE HEPES                                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    39(C5 H11 N O2 SE)                                           
FORMUL   5   CA    4(CA 2+)                                                     
FORMUL   6  EPE    4(C8 H18 N2 O4 S)                                            
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   8  EDO    18(C2 H6 O2)                                                 
FORMUL  35  HOH   *428(H2 O)                                                    
HELIX    1   1 THR A   21  ALA A   33  1                                  13    
HELIX    2   2 HIS A   45  ASP A   48  5                                   4    
HELIX    3   3 VAL A   49  GLY A   57  1                                   9    
HELIX    4   4 SER A   65  GLY A   67  5                                   3    
HELIX    5   5 ASP A   84  PHE A   92  1                                   9    
HELIX    6   6 ASP A  153  GLY A  169  1                                  17    
HELIX    7   7 SER A  190  LEU A  202  1                                  13    
HELIX    8   8 THR A  205  SER A  207  5                                   3    
HELIX    9   9 GLY A  215  ASN A  217  5                                   3    
HELIX   10  10 ASP A  218  ALA A  225  1                                   8    
HELIX   11  11 HIS A  235  HIS A  242  1                                   8    
HELIX   12  12 SER A  250  ASP A  253  5                                   4    
HELIX   13  13 ASP A  254  LEU A  265  1                                  12    
HELIX   14  14 THR B   21  ARG B   34  1                                  14    
HELIX   15  15 HIS B   45  ASP B   48  5                                   4    
HELIX   16  16 VAL B   49  LEU B   56  1                                   8    
HELIX   17  17 SER B   65  GLY B   67  5                                   3    
HELIX   18  18 ASP B   84  PHE B   92  1                                   9    
HELIX   19  19 ASP B  153  GLY B  169  1                                  17    
HELIX   20  20 SER B  190  LEU B  202  1                                  13    
HELIX   21  21 THR B  205  SER B  207  5                                   3    
HELIX   22  22 GLY B  215  ASN B  217  5                                   3    
HELIX   23  23 ASP B  218  ALA B  225  1                                   8    
HELIX   24  24 HIS B  235  HIS B  242  1                                   8    
HELIX   25  25 SER B  250  ASP B  253  5                                   4    
HELIX   26  26 ASP B  254  LEU B  265  1                                  12    
HELIX   27  27 THR C   21  ALA C   33  1                                  13    
HELIX   28  28 HIS C   45  ASP C   48  5                                   4    
HELIX   29  29 VAL C   49  LEU C   56  1                                   8    
HELIX   30  30 SER C   65  GLY C   67  5                                   3    
HELIX   31  31 ASP C   84  PHE C   92  1                                   9    
HELIX   32  32 ASP C  153  GLY C  169  1                                  17    
HELIX   33  33 SER C  190  LEU C  202  1                                  13    
HELIX   34  34 THR C  205  SER C  207  5                                   3    
HELIX   35  35 GLY C  215  ASN C  217  5                                   3    
HELIX   36  36 ASP C  218  ALA C  225  1                                   8    
HELIX   37  37 HIS C  235  HIS C  242  1                                   8    
HELIX   38  38 SER C  250  ASP C  253  5                                   4    
HELIX   39  39 ASP C  254  LEU C  265  1                                  12    
HELIX   40  40 THR D   21  ARG D   34  1                                  14    
HELIX   41  41 HIS D   45  ASP D   48  5                                   4    
HELIX   42  42 VAL D   49  LEU D   56  1                                   8    
HELIX   43  43 SER D   65  GLY D   67  5                                   3    
HELIX   44  44 ASP D   84  PHE D   92  1                                   9    
HELIX   45  45 ASP D  153  GLY D  169  1                                  17    
HELIX   46  46 SER D  190  LEU D  202  1                                  13    
HELIX   47  47 THR D  205  SER D  207  5                                   3    
HELIX   48  48 GLY D  215  ASN D  217  5                                   3    
HELIX   49  49 ASP D  218  ALA D  225  1                                   8    
HELIX   50  50 HIS D  235  HIS D  242  1                                   8    
HELIX   51  51 SER D  250  ASP D  253  5                                   4    
HELIX   52  52 ASP D  254  LEU D  265  1                                  12    
SHEET    1   A 8 GLN A  77  ALA A  80  0                                        
SHEET    2   A 8 ARG A  69  HIS A  71 -1  N  VAL A  70   O  ILE A  78           
SHEET    3   A 8 TYR A  61  THR A  64 -1  N  MSE A  62   O  HIS A  71           
SHEET    4   A 8 ASN A  37  ALA A  41  1  N  PHE A  40   O  ILE A  63           
SHEET    5   A 8 VAL A   4  ASP A   8  1  N  VAL A   5   O  ASN A  37           
SHEET    6   A 8 CYS A 209  GLY A 213  1  O  ILE A 210   N  ALA A   6           
SHEET    7   A 8 LYS A 227  ILE A 230  1  O  LYS A 227   N  ALA A 211           
SHEET    8   A 8 GLU A 246  VAL A 247  1  O  GLU A 246   N  ILE A 230           
SHEET    1   B 6 TYR A 131  LEU A 133  0                                        
SHEET    2   B 6 GLU A 110  MSE A 113  1  N  MSE A 113   O  LYS A 132           
SHEET    3   B 6 VAL A 102  ARG A 107 -1  N  VAL A 105   O  TYR A 112           
SHEET    4   B 6 ILE A 144  THR A 150 -1  O  PHE A 148   N  ASN A 104           
SHEET    5   B 6 CYS A 181  ALA A 186 -1  O  LEU A 182   N  PHE A 149           
SHEET    6   B 6 VAL A 172  PHE A 176 -1  N  ASN A 173   O  MSE A 185           
SHEET    1   C 8 GLN B  77  ALA B  80  0                                        
SHEET    2   C 8 ARG B  69  HIS B  71 -1  N  VAL B  70   O  ILE B  78           
SHEET    3   C 8 TYR B  61  THR B  64 -1  N  MSE B  62   O  HIS B  71           
SHEET    4   C 8 ASN B  37  ALA B  41  1  N  PHE B  40   O  ILE B  63           
SHEET    5   C 8 VAL B   4  ASP B   8  1  N  VAL B   5   O  ASN B  37           
SHEET    6   C 8 CYS B 209  GLY B 213  1  O  ILE B 210   N  ALA B   6           
SHEET    7   C 8 LYS B 227  ILE B 230  1  O  LYS B 227   N  ALA B 211           
SHEET    8   C 8 GLU B 246  VAL B 247  1  O  GLU B 246   N  ILE B 230           
SHEET    1   D 6 TYR B 131  LEU B 133  0                                        
SHEET    2   D 6 GLU B 110  MSE B 113  1  N  MSE B 113   O  LYS B 132           
SHEET    3   D 6 VAL B 102  ARG B 107 -1  N  VAL B 105   O  TYR B 112           
SHEET    4   D 6 ILE B 144  THR B 150 -1  O  PHE B 148   N  ASN B 104           
SHEET    5   D 6 CYS B 181  ALA B 186 -1  O  LEU B 182   N  PHE B 149           
SHEET    6   D 6 VAL B 172  PHE B 176 -1  N  SER B 175   O  GLU B 183           
SHEET    1   E 8 GLN C  77  ALA C  80  0                                        
SHEET    2   E 8 ARG C  69  HIS C  71 -1  N  VAL C  70   O  ILE C  78           
SHEET    3   E 8 TYR C  61  THR C  64 -1  N  MSE C  62   O  HIS C  71           
SHEET    4   E 8 ASN C  37  ALA C  41  1  N  PHE C  40   O  ILE C  63           
SHEET    5   E 8 VAL C   4  ASP C   8  1  N  VAL C   5   O  ASN C  37           
SHEET    6   E 8 CYS C 209  GLY C 213  1  O  ILE C 210   N  ALA C   6           
SHEET    7   E 8 LYS C 227  ILE C 230  1  O  LYS C 227   N  ALA C 211           
SHEET    8   E 8 GLU C 246  VAL C 247  1  O  GLU C 246   N  ILE C 230           
SHEET    1   F 6 TYR C 131  LEU C 133  0                                        
SHEET    2   F 6 GLU C 110  MSE C 113  1  N  TRP C 111   O  LYS C 132           
SHEET    3   F 6 VAL C 102  ARG C 107 -1  N  VAL C 105   O  TYR C 112           
SHEET    4   F 6 ILE C 144  THR C 150 -1  O  PHE C 148   N  ASN C 104           
SHEET    5   F 6 CYS C 181  ALA C 186 -1  O  LEU C 182   N  PHE C 149           
SHEET    6   F 6 VAL C 172  PHE C 176 -1  N  ASN C 173   O  MSE C 185           
SHEET    1   G 8 GLN D  77  ALA D  80  0                                        
SHEET    2   G 8 ARG D  69  HIS D  71 -1  N  VAL D  70   O  ILE D  78           
SHEET    3   G 8 TYR D  61  THR D  64 -1  N  MSE D  62   O  HIS D  71           
SHEET    4   G 8 ASN D  37  ALA D  41  1  N  PHE D  40   O  ILE D  63           
SHEET    5   G 8 VAL D   4  ASP D   8  1  N  VAL D   5   O  ASN D  37           
SHEET    6   G 8 CYS D 209  GLY D 213  1  O  ILE D 210   N  ALA D   6           
SHEET    7   G 8 LYS D 227  ILE D 230  1  O  LYS D 227   N  ALA D 211           
SHEET    8   G 8 GLU D 246  VAL D 247  1  O  GLU D 246   N  ILE D 230           
SHEET    1   H 6 TYR D 131  LEU D 133  0                                        
SHEET    2   H 6 GLU D 110  MSE D 113  1  N  MSE D 113   O  LYS D 132           
SHEET    3   H 6 VAL D 102  ARG D 107 -1  N  VAL D 105   O  TYR D 112           
SHEET    4   H 6 ILE D 144  THR D 150 -1  O  PHE D 148   N  ASN D 104           
SHEET    5   H 6 CYS D 181  ALA D 186 -1  O  LEU D 182   N  PHE D 149           
SHEET    6   H 6 VAL D 172  PHE D 176 -1  N  ASN D 173   O  MSE D 185           
LINK         C   TYR A  61                 N   MSE A  62     1555   1555  1.33  
LINK         C   MSE A  62                 N   ILE A  63     1555   1555  1.35  
LINK         C   TYR A 112                 N   MSE A 113     1555   1555  1.32  
LINK         C   MSE A 113                 N   ASN A 114     1555   1555  1.35  
LINK         C   ALA A 163                 N   MSE A 164     1555   1555  1.35  
LINK         C   MSE A 164                 N   ASN A 165     1555   1555  1.36  
LINK         C   VAL A 184                 N   MSE A 185     1555   1555  1.34  
LINK         C   MSE A 185                 N   ALA A 186     1555   1555  1.35  
LINK         C   LYS A 200                 N   MSE A 201     1555   1555  1.37  
LINK         C   MSE A 201                 N   LEU A 202     1555   1555  1.36  
LINK         C   GLY A 215                 N   MSE A 216     1555   1555  1.34  
LINK         C   MSE A 216                 N   ASN A 217     1555   1555  1.36  
LINK         C   GLU A 220                 N   MSE A 221     1555   1555  1.34  
LINK         C   MSE A 221                 N   LEU A 222     1555   1555  1.34  
LINK         C   SER A 223                 N   MSE A 224     1555   1555  1.35  
LINK         C   MSE A 224                 N   ALA A 225     1555   1555  1.34  
LINK         C   ILE A 230                 N   MSE A 231     1555   1555  1.34  
LINK         C   MSE A 231                 N   ALA A 232     1555   1555  1.35  
LINK         C   MSE B   1                 N   TYR B   2     1555   1555  1.35  
LINK         C   TYR B  61                 N   MSE B  62     1555   1555  1.33  
LINK         C   MSE B  62                 N   ILE B  63     1555   1555  1.34  
LINK         C   TYR B 112                 N   MSE B 113     1555   1555  1.32  
LINK         C   MSE B 113                 N   ASN B 114     1555   1555  1.36  
LINK         C   ALA B 163                 N   MSE B 164     1555   1555  1.34  
LINK         C   MSE B 164                 N   ASN B 165     1555   1555  1.33  
LINK         C   VAL B 184                 N   MSE B 185     1555   1555  1.35  
LINK         C   MSE B 185                 N   ALA B 186     1555   1555  1.35  
LINK         C   LYS B 200                 N   MSE B 201     1555   1555  1.37  
LINK         C   MSE B 201                 N   LEU B 202     1555   1555  1.36  
LINK         C   GLY B 215                 N   MSE B 216     1555   1555  1.35  
LINK         C   MSE B 216                 N   ASN B 217     1555   1555  1.35  
LINK         C   GLU B 220                 N   MSE B 221     1555   1555  1.36  
LINK         C   MSE B 221                 N   LEU B 222     1555   1555  1.34  
LINK         C   SER B 223                 N   MSE B 224     1555   1555  1.36  
LINK         C   MSE B 224                 N   ALA B 225     1555   1555  1.35  
LINK         C   ILE B 230                 N   MSE B 231     1555   1555  1.35  
LINK         C   MSE B 231                 N   ALA B 232     1555   1555  1.35  
LINK         C   MSE C   1                 N   TYR C   2     1555   1555  1.34  
LINK         C   TYR C  61                 N   MSE C  62     1555   1555  1.33  
LINK         C   MSE C  62                 N   ILE C  63     1555   1555  1.34  
LINK         C   TYR C 112                 N   MSE C 113     1555   1555  1.32  
LINK         C   MSE C 113                 N   ASN C 114     1555   1555  1.35  
LINK         C   ALA C 163                 N   MSE C 164     1555   1555  1.34  
LINK         C   MSE C 164                 N   ASN C 165     1555   1555  1.35  
LINK         C   VAL C 184                 N   MSE C 185     1555   1555  1.34  
LINK         C   MSE C 185                 N   ALA C 186     1555   1555  1.35  
LINK         C   LYS C 200                 N   MSE C 201     1555   1555  1.37  
LINK         C   MSE C 201                 N   LEU C 202     1555   1555  1.36  
LINK         C   GLY C 215                 N   MSE C 216     1555   1555  1.34  
LINK         C   MSE C 216                 N   ASN C 217     1555   1555  1.35  
LINK         C   GLU C 220                 N   MSE C 221     1555   1555  1.34  
LINK         C   MSE C 221                 N   LEU C 222     1555   1555  1.35  
LINK         C   SER C 223                 N   MSE C 224     1555   1555  1.35  
LINK         C   MSE C 224                 N   ALA C 225     1555   1555  1.36  
LINK         C   ILE C 230                 N   MSE C 231     1555   1555  1.34  
LINK         C   MSE C 231                 N   ALA C 232     1555   1555  1.36  
LINK         C   MSE D   1                 N   TYR D   2     1555   1555  1.35  
LINK         C   TYR D  61                 N   MSE D  62     1555   1555  1.33  
LINK         C   MSE D  62                 N   ILE D  63     1555   1555  1.34  
LINK         C   TYR D 112                 N   MSE D 113     1555   1555  1.32  
LINK         C   MSE D 113                 N   ASN D 114     1555   1555  1.35  
LINK         C   ALA D 163                 N   MSE D 164     1555   1555  1.36  
LINK         C   MSE D 164                 N   ASN D 165     1555   1555  1.34  
LINK         C   VAL D 184                 N   MSE D 185     1555   1555  1.34  
LINK         C   MSE D 185                 N   ALA D 186     1555   1555  1.34  
LINK         C   LYS D 200                 N   MSE D 201     1555   1555  1.37  
LINK         C   MSE D 201                 N   LEU D 202     1555   1555  1.35  
LINK         C   GLY D 215                 N   MSE D 216     1555   1555  1.35  
LINK         C   MSE D 216                 N   ASN D 217     1555   1555  1.35  
LINK         C   GLU D 220                 N   MSE D 221     1555   1555  1.35  
LINK         C   MSE D 221                 N   LEU D 222     1555   1555  1.33  
LINK         C   SER D 223                 N   MSE D 224     1555   1555  1.35  
LINK         C   MSE D 224                 N   ALA D 225     1555   1555  1.34  
LINK         C   ILE D 230                 N   MSE D 231     1555   1555  1.35  
LINK         C   MSE D 231                 N   ALA D 232     1555   1555  1.35  
LINK         OD2 ASP C   8                CA    CA C 267     1555   1555  2.14  
LINK         OD2 ASP A   8                CA    CA A 267     1555   1555  2.19  
LINK         OD2 ASP B   8                CA    CA B 267     1555   1555  2.22  
LINK        CA    CA D 267                 O1S EPE D 271     1555   1555  2.23  
LINK         OD1 ASP A 214                CA    CA A 267     1555   1555  2.23  
LINK         O   ASP B  10                CA    CA B 267     1555   1555  2.27  
LINK         OD1 ASP C 214                CA    CA C 267     1555   1555  2.30  
LINK        CA    CA B 267                 O1S EPE B 269     1555   1555  2.31  
LINK         OD2 ASP D   8                CA    CA D 267     1555   1555  2.31  
LINK        CA    CA C 267                 O1S EPE C 270     1555   1555  2.31  
LINK         O   ASP D  10                CA    CA D 267     1555   1555  2.36  
LINK         OD1 ASP B 214                CA    CA B 267     1555   1555  2.36  
LINK        CA    CA D 267                 O   HOH D 463     1555   1555  2.37  
LINK        CA    CA B 267                 O2  GOL B 273     1555   1555  2.39  
LINK         O   ASP A  10                CA    CA A 267     1555   1555  2.39  
LINK         OD1 ASP D 214                CA    CA D 267     1555   1555  2.40  
LINK         O   ASP C  10                CA    CA C 267     1555   1555  2.41  
LINK        CA    CA A 267                 O1S EPE A 268     1555   1555  2.44  
LINK        CA    CA D 267                 O2  GOL D 275     1555   1555  2.53  
LINK        CA    CA B 267                 O   HOH B 648     1555   1555  2.61  
LINK        CA    CA A 267                 O   HOH A 645     1555   1555  2.62  
LINK        CA    CA A 267                 O1  GOL A 272     1555   1555  2.62  
LINK        CA    CA C 267                 O2  GOL C 274     1555   1555  2.63  
LINK        CA    CA C 267                 O   HOH C 644     1555   1555  2.66  
LINK        CA    CA D 267                 O3  GOL D 275     1555   1555  2.75  
LINK        CA    CA A 267                 O2  GOL A 272     1555   1555  2.82  
LINK        CA    CA B 267                 O3  GOL B 273     1555   1555  2.83  
LINK        CA    CA C 267                 O1  GOL C 274     1555   1555  2.84  
SITE     1 AC1  6 ASP A   8  ASP A  10  ASP A 214  EPE A 268                    
SITE     2 AC1  6 GOL A 272  HOH A 645                                          
SITE     1 AC2  8 ASP A   8  ASP A  10  GLY A  43  SER A 177                    
SITE     2 AC2  8 LYS A 191  ASN A 217   CA A 267  GOL A 272                    
SITE     1 AC3  9 ASP A  10  SER A 177  THR A 178  ASP A 214                    
SITE     2 AC3  9 HIS A 235   CA A 267  EPE A 268  HOH A 354                    
SITE     3 AC3  9 HOH A 645                                                     
SITE     1 AC4  3 ASP A  84  ALA A 186  HOH A 451                               
SITE     1 AC5  5 GLU A 110  TRP A 111  PHE A 129  ASN A 130                    
SITE     2 AC5  5 LYS A 132                                                     
SITE     1 AC6  6 HIS A 154  PHE A 176  HIS A 235  ARG A 237                    
SITE     2 AC6  6 HOH A 399  HOH A 456                                          
SITE     1 AC7  3 ARG A  59  TYR A  61  SER A  73                               
SITE     1 AC8  2 PHE A 123  ALA B 163                                          
SITE     1 AC9  6 ASP B   8  ASP B  10  ASP B 214  EPE B 269                    
SITE     2 AC9  6 GOL B 273  HOH B 648                                          
SITE     1 BC1 13 ASP B   8  ASP B  10  HIS B  18  THR B  42                    
SITE     2 BC1 13 GLY B  43  SER B 177  THR B 178  LYS B 191                    
SITE     3 BC1 13 ASN B 217   CA B 267  GOL B 273  HOH B 629                    
SITE     4 BC1 13 ASP D  17                                                     
SITE     1 BC2 10 ASP B  10  SER B 177  THR B 178  ASP B 214                    
SITE     2 BC2 10 GLY B 215  HIS B 235   CA B 267  EPE B 269                    
SITE     3 BC2 10 HOH B 648  HOH D 435                                          
SITE     1 BC3  3 TYR B  61  ASP B  72  SER B  73                               
SITE     1 BC4  2 MSE B 224  HOH B 556                                          
SITE     1 BC5  6 ASP C   8  ASP C  10  ASP C 214  EPE C 270                    
SITE     2 BC5  6 GOL C 274  HOH C 644                                          
SITE     1 BC6 11 ASP A  17  ASP C   8  ASP C  10  HIS C  18                    
SITE     2 BC6 11 THR C  42  GLY C  43  SER C 177  LYS C 191                    
SITE     3 BC6 11 ASN C 217   CA C 267  GOL C 274                               
SITE     1 BC7  8 ASP C  10  SER C 177  THR C 178  ASP C 214                    
SITE     2 BC7  8 GLY C 215  HIS C 235   CA C 267  EPE C 270                    
SITE     1 BC8  2 HOH A 456  HOH C 312                                          
SITE     1 BC9  3 ASN C 165  ASN C 173  VAL C 174                               
SITE     1 CC1  6 ASP D   8  ASP D  10  ASP D 214  EPE D 271                    
SITE     2 CC1  6 GOL D 275  HOH D 463                                          
SITE     1 CC2 11 ASP D   8  ASP D  10  HIS D  18  GLY D  43                    
SITE     2 CC2 11 SER D 177  LYS D 191  ASN D 217   CA D 267                    
SITE     3 CC2 11 GOL D 275  EDO D 280  HOH D 463                               
SITE     1 CC3 11 ASP D  10  SER D 177  THR D 178  ASP D 214                    
SITE     2 CC3 11 GLY D 215  ASN D 217  HIS D 235   CA D 267                    
SITE     3 CC3 11 EPE D 271  HOH D 463  HOH D 704                               
SITE     1 CC4  4 VAL B 247  ILE B 248  GLN D 236  EDO D 283                    
SITE     1 CC5  5 TYR D 106  LYS D 146  PHE D 148  GLU D 183                    
SITE     2 CC5  5 EPE D 271                                                     
SITE     1 CC6  7 VAL D  95  ASP D  98  HIS D 156  PRO D 159                    
SITE     2 CC6  7 LEU D 160  ALA D 163  ALA D 166                               
SITE     1 CC7  7 GLY D  67  PHE D  79  HIS D  81  GLY D 188                    
SITE     2 CC7  7 VAL D 189  HIS D 193  ALA D 194                               
SITE     1 CC8  4 LYS B 239  LYS D 239  EDO D 279  EDO D 292                    
SITE     1 CC9  3 TYR D  61  ASP D  72  SER D  73                               
SITE     1 DC1  2 ALA B 197  ASP D  84                                          
SITE     1 DC2  3 ARG D 237  ASP D 240  LEU D 241                               
SITE     1 DC3  4 GLN B 236  VAL D 247  ILE D 248  EDO D 283                    
CRYST1  118.569   61.961  169.407  90.00  94.19  90.00 C 1 2 1      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      0.008434  0.000000  0.000618        0.00000                         
SCALE2      0.000000  0.016139  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005919        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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