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Database: PDB
Entry: 4FJ6
LinkDB: 4FJ6
Original site: 4FJ6 
HEADER    HYDROLASE                               11-JUN-12   4FJ6              
TITLE     CRYSTAL STRUCTURE OF A GLYCOSIDE HYDROLASE FAMILY 33, CANDIDATE       
TITLE    2 SIALIDASE (BDI_2946) FROM PARABACTEROIDES DISTASONIS ATCC 8503 AT    
TITLE    3 1.90 A RESOLUTION                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOSIDE HYDROLASE FAMILY 33, CANDIDATE SIALIDASE;        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARABACTEROIDES DISTASONIS;                     
SOURCE   3 ORGANISM_TAXID: 435591;                                              
SOURCE   4 STRAIN: ATCC 8503;                                                   
SOURCE   5 GENE: BDI_2946;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PB1;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    BACTERIAL NEURAMINIDASE REPEAT, INTRAMOLECULAR TRANS-SIALIDASE, A     
KEYWDS   2 CARBOHYDRATE BINDING DOMAIN, STRUCTURAL GENOMICS, JOINT CENTER FOR   
KEYWDS   3 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-        
KEYWDS   4 BIOLOGY, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   2   01-AUG-12 4FJ6    1       AUTHOR                                   
REVDAT   1   25-JUL-12 4FJ6    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF A GLYCOSIDE HYDROLASE FAMILY 33,        
JRNL        TITL 2 CANDIDATE SIALIDASE (BDI_2946) FROM PARABACTEROIDES          
JRNL        TITL 3 DISTASONIS ATCC 8503 AT 1.90 A RESOLUTION                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 209495                         
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10526                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 14788                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 785                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16160                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 178                                     
REMARK   3   SOLVENT ATOMS            : 2000                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.77                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.21000                                              
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : 0.10000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.155         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.144         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.394         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16905 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A): 11325 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23016 ; 1.531 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 27804 ; 0.999 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2155 ; 4.873 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   733 ;35.349 ;24.748       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2928 ;10.521 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;10.873 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2612 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 18667 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3221 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     22       A     539      6                      
REMARK   3           1     B     22       B     539      6                      
REMARK   3           1     C     22       C     539      6                      
REMARK   3           1     D     22       D     539      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   6506 ; 0.200 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   6506 ; 0.220 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   6506 ; 0.240 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   6506 ; 0.200 ; 5.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   6506 ; 1.720 ;10.000           
REMARK   3   LOOSE THERMAL      1    B (A**2):   6506 ; 1.850 ;10.000           
REMARK   3   LOOSE THERMAL      1    C (A**2):   6506 ; 1.800 ;10.000           
REMARK   3   LOOSE THERMAL      1    D (A**2):   6506 ; 2.070 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    22        A   540                          
REMARK   3    ORIGIN FOR THE GROUP (A):  99.6640  24.2080 275.7830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1073 T22:   0.0458                                     
REMARK   3      T33:   0.0664 T12:   0.0349                                     
REMARK   3      T13:  -0.0388 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4293 L22:   0.1685                                     
REMARK   3      L33:   0.3873 L12:  -0.0865                                     
REMARK   3      L13:   0.1786 L23:  -0.0981                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0269 S12:  -0.0622 S13:   0.0009                       
REMARK   3      S21:   0.0292 S22:   0.0637 S23:   0.0224                       
REMARK   3      S31:   0.0156 S32:  -0.0427 S33:  -0.0368                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    21        B   540                          
REMARK   3    ORIGIN FOR THE GROUP (A): 120.5090  27.8030 238.1000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1092 T22:   0.0705                                     
REMARK   3      T33:   0.0651 T12:   0.0260                                     
REMARK   3      T13:  -0.0197 T23:  -0.0300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1987 L22:   0.1324                                     
REMARK   3      L33:   0.4798 L12:   0.1244                                     
REMARK   3      L13:  -0.0876 L23:  -0.0024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:  -0.0123 S13:   0.0329                       
REMARK   3      S21:  -0.0730 S22:   0.0189 S23:   0.0040                       
REMARK   3      S31:   0.0374 S32:   0.1091 S33:   0.0120                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    21        C   539                          
REMARK   3    ORIGIN FOR THE GROUP (A): 135.4930 -20.5910 277.8870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0833 T22:   0.0447                                     
REMARK   3      T33:   0.0971 T12:   0.0272                                     
REMARK   3      T13:  -0.0205 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1242 L22:   0.5615                                     
REMARK   3      L33:   0.6711 L12:   0.1516                                     
REMARK   3      L13:   0.2352 L23:   0.0634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0321 S12:   0.0111 S13:  -0.0462                       
REMARK   3      S21:  -0.0868 S22:   0.0096 S23:  -0.0555                       
REMARK   3      S31:   0.0843 S32:  -0.0019 S33:  -0.0416                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    20        D   540                          
REMARK   3    ORIGIN FOR THE GROUP (A): 142.8180  -0.8550 315.6580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0442 T22:   0.1037                                     
REMARK   3      T33:   0.0676 T12:  -0.0101                                     
REMARK   3      T13:  -0.0005 T23:   0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1639 L22:   0.4549                                     
REMARK   3      L33:   0.3712 L12:   0.1951                                     
REMARK   3      L13:   0.0657 L23:   0.0256                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:  -0.0553 S13:  -0.0168                       
REMARK   3      S21:   0.0047 S22:  -0.0617 S23:  -0.0108                       
REMARK   3      S31:  -0.0041 S32:  -0.0078 S33:   0.0143                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL   
REMARK   3  B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U      
REMARK   3  FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.     
REMARK   3  5. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE          
REMARK   3  INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE    
REMARK   3  ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED       
REMARK   3  SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 6. PHOSPHATE   
REMARK   3  IONS (PO4) AND GLYCEROL (GOL) MOLECULES FROM THE CRYSTALLIZATION/   
REMARK   3  CRYOPROTECTION SOLUTION ARE MODELED. 7. CHLORIDE (CL) IONS FROM     
REMARK   3  PROTEIN BUFFER HAVE BEEN MODELED.                                   
REMARK   4                                                                      
REMARK   4 4FJ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072964.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.5                               
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) : 0.97922,0.91837,0.97871            
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT        
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING);   
REMARK 200                                   SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HORIZONTAL          
REMARK 200                                   FOCUSING)                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 209534                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.773                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.10500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD,SHARP                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 1.2M SODIUM        
REMARK 280  DIHYDROGEN PHOSPHATE, 0.8M DI-POTASSIUM HYDROGEN PHOSPHATE, 0.1M    
REMARK 280  GLYCINE PH 10.5, VAPOR DIFFUSION,SITTING DROP,NANODROP,             
REMARK 280  TEMPERATURE 277K, VAPOR DIFFUSION, SITTING DROP                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       85.86900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.57649            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       81.26200            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       85.86900            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.57649            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       81.26200            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       85.86900            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.57649            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       81.26200            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.15298            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000      162.52400            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.15298            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000      162.52400            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.15298            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      162.52400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A DIMER  
REMARK 300 AS THE SIGNIFICANT OLIGOMERIZATION STATE.                            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     GLN A   541                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     GLN B   541                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     HIS C   540                                                      
REMARK 465     GLN C   541                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     GLN D   541                                                      
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 455    CG   CD   CE   NZ                                   
REMARK 470     LYS A 473    CD   CE   NZ                                        
REMARK 470     HIS A 540    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 136    CG   CD   CE   NZ                                   
REMARK 470     LYS B 381    CD   CE   NZ                                        
REMARK 470     LYS B 473    CG   CD   CE   NZ                                   
REMARK 470     LYS C  86    CD   CE   NZ                                        
REMARK 470     ASN C 172    CG   OD1  ND2                                       
REMARK 470     LYS C 381    CG   CD   CE   NZ                                   
REMARK 470     LYS C 455    CD   CE   NZ                                        
REMARK 470     LYS C 473    CG   CD   CE   NZ                                   
REMARK 470     GLU C 493    CD   OE1  OE2                                       
REMARK 470     LYS D 473    CG   CD   CE   NZ                                   
REMARK 470     GLN D 536    CD   OE1  NE2                                       
REMARK 470     HIS D 540    CG   ND1  CD2  CE1  NE2                             
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    ILE A 201       74.49     68.98                                   
REMARK 500    GLU A 228      177.31    179.43                                   
REMARK 500    LYS A 254     -112.91     31.03                                   
REMARK 500    ASN A 264       29.93   -150.67                                   
REMARK 500    HIS A 386     -107.67    -99.52                                   
REMARK 500    THR A 394     -103.08   -125.80                                   
REMARK 500    SER A 438      -56.01   -163.77                                   
REMARK 500    VAL A 444       81.73     75.67                                   
REMARK 500    HIS A 494       41.85   -101.41                                   
REMARK 500    ILE B 201       74.48     69.18                                   
REMARK 500    GLU B 228      168.50    178.96                                   
REMARK 500    LYS B 229       97.35    -68.50                                   
REMARK 500    LYS B 254     -118.91     36.88                                   
REMARK 500    GLN B 255       50.00   -109.00                                   
REMARK 500    ASN B 264       35.66   -148.48                                   
REMARK 500    HIS B 386     -107.25    -99.96                                   
REMARK 500    THR B 394     -101.74   -127.44                                   
REMARK 500    SER B 438      -48.84   -162.24                                   
REMARK 500    VAL B 444       83.06     70.51                                   
REMARK 500    HIS B 494       41.90    -99.29                                   
REMARK 500    ASP B 513     -158.36   -150.05                                   
REMARK 500    ILE C 201       73.21     71.29                                   
REMARK 500    GLU C 228     -179.91   -177.35                                   
REMARK 500    LYS C 254     -114.11     29.76                                   
REMARK 500    GLN C 255       57.74   -112.82                                   
REMARK 500    ASN C 264       31.57   -145.29                                   
REMARK 500    HIS C 386     -107.74   -103.25                                   
REMARK 500    THR C 394      -99.31   -127.64                                   
REMARK 500    SER C 438      -54.35   -165.82                                   
REMARK 500    VAL C 444       81.64     76.78                                   
REMARK 500    HIS C 494       43.22   -100.23                                   
REMARK 500    ILE D 201       74.81     70.90                                   
REMARK 500    LYS D 254     -116.67     31.98                                   
REMARK 500    GLN D 255       52.45   -109.28                                   
REMARK 500    ASN D 264       34.58   -147.60                                   
REMARK 500    HIS D 386     -105.33   -103.52                                   
REMARK 500    THR D 394     -101.16   -125.87                                   
REMARK 500    SER D 438      -56.35   -170.32                                   
REMARK 500    VAL D 444       82.10     76.11                                   
REMARK 500    HIS D 494       47.51   -102.39                                   
REMARK 500    ALA D 526      143.42   -170.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 610                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 419091   RELATED DB: TARGETTRACK                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG                 
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING   
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 20-541 OF THE TARGET         
REMARK 999 SEQUENCE.                                                            
DBREF  4FJ6 A   20   541  UNP    A6LG40   A6LG40_PARD8    20    541             
DBREF  4FJ6 B   20   541  UNP    A6LG40   A6LG40_PARD8    20    541             
DBREF  4FJ6 C   20   541  UNP    A6LG40   A6LG40_PARD8    20    541             
DBREF  4FJ6 D   20   541  UNP    A6LG40   A6LG40_PARD8    20    541             
SEQADV 4FJ6 GLY A    0  UNP  A6LG40              LEADER SEQUENCE                
SEQADV 4FJ6 GLY B    0  UNP  A6LG40              LEADER SEQUENCE                
SEQADV 4FJ6 GLY C    0  UNP  A6LG40              LEADER SEQUENCE                
SEQADV 4FJ6 GLY D    0  UNP  A6LG40              LEADER SEQUENCE                
SEQRES   1 A  523  GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO          
SEQRES   2 A  523  ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE          
SEQRES   3 A  523  ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE          
SEQRES   4 A  523  THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE          
SEQRES   5 A  523  GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO          
SEQRES   6 A  523  SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE          
SEQRES   7 A  523  SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU          
SEQRES   8 A  523  SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU          
SEQRES   9 A  523  SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU          
SEQRES  10 A  523  LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS          
SEQRES  11 A  523  PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE          
SEQRES  12 A  523  PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR          
SEQRES  13 A  523  TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY          
SEQRES  14 A  523  VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG          
SEQRES  15 A  523  ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU          
SEQRES  16 A  523  GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU          
SEQRES  17 A  523  GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP          
SEQRES  18 A  523  LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR          
SEQRES  19 A  523  PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY          
SEQRES  20 A  523  VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN          
SEQRES  21 A  523  THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY          
SEQRES  22 A  523  ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR          
SEQRES  23 A  523  PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU          
SEQRES  24 A  523  ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR          
SEQRES  25 A  523  SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN          
SEQRES  26 A  523  GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU          
SEQRES  27 A  523  VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO          
SEQRES  28 A  523  ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR          
SEQRES  29 A  523  TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU          
SEQRES  30 A  523  ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU          
SEQRES  31 A  523  ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA          
SEQRES  32 A  523  THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO          
SEQRES  33 A  523  SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA          
SEQRES  34 A  523  SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY          
SEQRES  35 A  523  LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS          
SEQRES  36 A  523  GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY          
SEQRES  37 A  523  GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP          
SEQRES  38 A  523  GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE          
SEQRES  39 A  523  ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL          
SEQRES  40 A  523  ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU          
SEQRES  41 A  523  ILE HIS GLN                                                  
SEQRES   1 B  523  GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO          
SEQRES   2 B  523  ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE          
SEQRES   3 B  523  ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE          
SEQRES   4 B  523  THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE          
SEQRES   5 B  523  GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO          
SEQRES   6 B  523  SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE          
SEQRES   7 B  523  SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU          
SEQRES   8 B  523  SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU          
SEQRES   9 B  523  SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU          
SEQRES  10 B  523  LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS          
SEQRES  11 B  523  PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE          
SEQRES  12 B  523  PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR          
SEQRES  13 B  523  TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY          
SEQRES  14 B  523  VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG          
SEQRES  15 B  523  ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU          
SEQRES  16 B  523  GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU          
SEQRES  17 B  523  GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP          
SEQRES  18 B  523  LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR          
SEQRES  19 B  523  PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY          
SEQRES  20 B  523  VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN          
SEQRES  21 B  523  THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY          
SEQRES  22 B  523  ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR          
SEQRES  23 B  523  PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU          
SEQRES  24 B  523  ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR          
SEQRES  25 B  523  SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN          
SEQRES  26 B  523  GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU          
SEQRES  27 B  523  VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO          
SEQRES  28 B  523  ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR          
SEQRES  29 B  523  TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU          
SEQRES  30 B  523  ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU          
SEQRES  31 B  523  ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA          
SEQRES  32 B  523  THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO          
SEQRES  33 B  523  SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA          
SEQRES  34 B  523  SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY          
SEQRES  35 B  523  LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS          
SEQRES  36 B  523  GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY          
SEQRES  37 B  523  GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP          
SEQRES  38 B  523  GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE          
SEQRES  39 B  523  ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL          
SEQRES  40 B  523  ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU          
SEQRES  41 B  523  ILE HIS GLN                                                  
SEQRES   1 C  523  GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO          
SEQRES   2 C  523  ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE          
SEQRES   3 C  523  ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE          
SEQRES   4 C  523  THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE          
SEQRES   5 C  523  GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO          
SEQRES   6 C  523  SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE          
SEQRES   7 C  523  SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU          
SEQRES   8 C  523  SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU          
SEQRES   9 C  523  SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU          
SEQRES  10 C  523  LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS          
SEQRES  11 C  523  PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE          
SEQRES  12 C  523  PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR          
SEQRES  13 C  523  TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY          
SEQRES  14 C  523  VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG          
SEQRES  15 C  523  ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU          
SEQRES  16 C  523  GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU          
SEQRES  17 C  523  GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP          
SEQRES  18 C  523  LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR          
SEQRES  19 C  523  PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY          
SEQRES  20 C  523  VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN          
SEQRES  21 C  523  THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY          
SEQRES  22 C  523  ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR          
SEQRES  23 C  523  PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU          
SEQRES  24 C  523  ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR          
SEQRES  25 C  523  SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN          
SEQRES  26 C  523  GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU          
SEQRES  27 C  523  VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO          
SEQRES  28 C  523  ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR          
SEQRES  29 C  523  TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU          
SEQRES  30 C  523  ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU          
SEQRES  31 C  523  ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA          
SEQRES  32 C  523  THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO          
SEQRES  33 C  523  SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA          
SEQRES  34 C  523  SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY          
SEQRES  35 C  523  LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS          
SEQRES  36 C  523  GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY          
SEQRES  37 C  523  GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP          
SEQRES  38 C  523  GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE          
SEQRES  39 C  523  ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL          
SEQRES  40 C  523  ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU          
SEQRES  41 C  523  ILE HIS GLN                                                  
SEQRES   1 D  523  GLY ALA ASP SER ILE TYR VAL ARG GLU GLN GLN ILE PRO          
SEQRES   2 D  523  ILE LEU ILE ASP ARG ILE ASP ASN VAL LEU TYR GLU MSE          
SEQRES   3 D  523  ARG ILE PRO ALA GLN LYS GLY ASP VAL LEU ASN GLU ILE          
SEQRES   4 D  523  THR ILE GLN ILE GLY ASP ASN VAL ASP LEU SER ASP ILE          
SEQRES   5 D  523  GLN ALA ILE ARG LEU PHE TYR SER GLY VAL GLU ALA PRO          
SEQRES   6 D  523  SER ARG LYS GLY GLU HIS PHE SER PRO VAL THR TYR ILE          
SEQRES   7 D  523  SER SER HIS ILE PRO GLY ASN THR ARG LYS ALA LEU GLU          
SEQRES   8 D  523  SER TYR SER VAL ARG GLN ASP GLU VAL THR ALA PRO LEU          
SEQRES   9 D  523  SER ARG THR VAL LYS LEU THR SER LYS GLN PRO MSE LEU          
SEQRES  10 D  523  LYS GLY ILE ASN TYR PHE TRP VAL SER ILE GLN MSE LYS          
SEQRES  11 D  523  PRO GLU THR SER LEU LEU ALA LYS VAL ALA THR THR MSE          
SEQRES  12 D  523  PRO ASN ALA GLN ILE ASN ASN LYS PRO ILE ASN ILE THR          
SEQRES  13 D  523  TRP LYS GLY LYS VAL ASP GLU ARG HIS VAL GLY ILE GLY          
SEQRES  14 D  523  VAL ARG GLN ALA GLY ASP ASP GLY SER ALA ALA PHE ARG          
SEQRES  15 D  523  ILE PRO GLY LEU VAL THR THR ASN ASN GLY THR LEU LEU          
SEQRES  16 D  523  GLY VAL TYR ASP ILE ARG TYR ASN SER SER VAL ASP LEU          
SEQRES  17 D  523  GLN GLU LYS ILE ASP ILE GLY VAL SER ARG SER THR ASP          
SEQRES  18 D  523  LYS GLY GLN THR TRP GLU PRO MSE ARG VAL ALA MSE THR          
SEQRES  19 D  523  PHE LYS GLN THR ASP GLY LEU PRO HIS GLY GLN ASN GLY          
SEQRES  20 D  523  VAL GLY ASP PRO SER ILE LEU VAL ASP GLU LYS THR ASN          
SEQRES  21 D  523  THR ILE TRP VAL VAL ALA ALA TRP THR HIS GLY MSE GLY          
SEQRES  22 D  523  ASN GLU ARG ALA TRP TRP ASN SER MSE PRO GLY MSE THR          
SEQRES  23 D  523  PRO ASP GLU THR ALA GLN LEU MSE LEU VAL LYS SER GLU          
SEQRES  24 D  523  ASP ASP GLY LYS THR TRP SER GLU PRO ILE ASN ILE THR          
SEQRES  25 D  523  SER GLN VAL LYS ASP PRO SER TRP TYR PHE LEU LEU GLN          
SEQRES  26 D  523  GLY PRO GLY ARG GLY ILE THR MSE GLN ASP GLY THR LEU          
SEQRES  27 D  523  VAL PHE PRO ILE GLN PHE ILE ASP ALA THR ARG VAL PRO          
SEQRES  28 D  523  ASN ALA GLY ILE MSE TYR SER LYS ASP ARG GLY LYS THR          
SEQRES  29 D  523  TRP HIS LEU HIS ASN LEU ALA ARG THR ASN THR THR GLU          
SEQRES  30 D  523  ALA GLN VAL ALA GLU VAL GLU PRO GLY VAL LEU MSE LEU          
SEQRES  31 D  523  ASN MSE ARG ASP ASN ARG GLY GLY SER ARG ALA VAL ALA          
SEQRES  32 D  523  THR THR LYS ASP LEU GLY LYS THR TRP THR GLU HIS PRO          
SEQRES  33 D  523  SER SER ARG SER ALA LEU GLN GLU SER VAL CYS MSE ALA          
SEQRES  34 D  523  SER LEU ILE LYS VAL ASN ALA LYS ASP ASN ILE THR GLY          
SEQRES  35 D  523  LYS ASP LEU LEU LEU PHE SER ASN PRO ASN THR THR LYS          
SEQRES  36 D  523  GLY ARG ASN HIS ILE THR ILE LYS ALA SER LEU ASP GLY          
SEQRES  37 D  523  GLY LEU THR TRP PRO THR GLU HIS GLN VAL LEU LEU ASP          
SEQRES  38 D  523  GLU ALA GLU GLY TRP GLY TYR SER CYS LEU SER MSE ILE          
SEQRES  39 D  523  ASP LYS GLU THR VAL GLY ILE PHE TYR GLU SER SER VAL          
SEQRES  40 D  523  ALA HIS MSE THR PHE GLN ALA VAL LYS LEU GLN ASP LEU          
SEQRES  41 D  523  ILE HIS GLN                                                  
MODRES 4FJ6 MSE A   44  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  134  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  147  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  161  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  247  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  251  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  290  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  300  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  303  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  312  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  351  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  374  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  407  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  410  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  446  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  511  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE A  528  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B   44  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  134  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  147  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  161  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  247  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  251  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  290  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  300  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  303  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  312  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  351  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  374  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  407  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  410  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  446  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  511  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE B  528  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C   44  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  134  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  147  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  161  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  247  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  251  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  290  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  300  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  303  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  312  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  351  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  374  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  407  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  410  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  446  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  511  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE C  528  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D   44  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  134  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  147  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  161  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  247  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  251  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  290  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  300  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  303  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  312  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  351  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  374  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  407  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  410  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  446  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  511  MET  SELENOMETHIONINE                                   
MODRES 4FJ6 MSE D  528  MET  SELENOMETHIONINE                                   
HET    MSE  A  44       8                                                       
HET    MSE  A 134       8                                                       
HET    MSE  A 147       8                                                       
HET    MSE  A 161       8                                                       
HET    MSE  A 247       8                                                       
HET    MSE  A 251       8                                                       
HET    MSE  A 290       8                                                       
HET    MSE  A 300       8                                                       
HET    MSE  A 303      13                                                       
HET    MSE  A 312       8                                                       
HET    MSE  A 351       8                                                       
HET    MSE  A 374       8                                                       
HET    MSE  A 407       8                                                       
HET    MSE  A 410       8                                                       
HET    MSE  A 446       8                                                       
HET    MSE  A 511       8                                                       
HET    MSE  A 528       8                                                       
HET    MSE  B  44       8                                                       
HET    MSE  B 134       8                                                       
HET    MSE  B 147       8                                                       
HET    MSE  B 161       8                                                       
HET    MSE  B 247       8                                                       
HET    MSE  B 251       8                                                       
HET    MSE  B 290      13                                                       
HET    MSE  B 300       8                                                       
HET    MSE  B 303      13                                                       
HET    MSE  B 312       8                                                       
HET    MSE  B 351       8                                                       
HET    MSE  B 374       8                                                       
HET    MSE  B 407       8                                                       
HET    MSE  B 410       8                                                       
HET    MSE  B 446       8                                                       
HET    MSE  B 511       8                                                       
HET    MSE  B 528       8                                                       
HET    MSE  C  44       8                                                       
HET    MSE  C 134       8                                                       
HET    MSE  C 147       8                                                       
HET    MSE  C 161       8                                                       
HET    MSE  C 247       8                                                       
HET    MSE  C 251       8                                                       
HET    MSE  C 290       8                                                       
HET    MSE  C 300       8                                                       
HET    MSE  C 303       8                                                       
HET    MSE  C 312       8                                                       
HET    MSE  C 351       8                                                       
HET    MSE  C 374       8                                                       
HET    MSE  C 407       8                                                       
HET    MSE  C 410      13                                                       
HET    MSE  C 446       8                                                       
HET    MSE  C 511       8                                                       
HET    MSE  C 528       8                                                       
HET    MSE  D  44       8                                                       
HET    MSE  D 134       8                                                       
HET    MSE  D 147       8                                                       
HET    MSE  D 161       8                                                       
HET    MSE  D 247       8                                                       
HET    MSE  D 251       8                                                       
HET    MSE  D 290       8                                                       
HET    MSE  D 300       8                                                       
HET    MSE  D 303       8                                                       
HET    MSE  D 312       8                                                       
HET    MSE  D 351       8                                                       
HET    MSE  D 374       8                                                       
HET    MSE  D 407       8                                                       
HET    MSE  D 410       8                                                       
HET    MSE  D 446       8                                                       
HET    MSE  D 511       8                                                       
HET    MSE  D 528      13                                                       
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HET    GOL  A 604       6                                                       
HET    PO4  A 605       5                                                       
HET    PO4  A 606       5                                                       
HET    PO4  A 607       5                                                       
HET    PO4  A 608       5                                                       
HET    PO4  A 609       5                                                       
HET     CL  B 601       1                                                       
HET     CL  B 602       1                                                       
HET    GOL  B 603       6                                                       
HET    GOL  B 604       6                                                       
HET    GOL  B 605      12                                                       
HET    PO4  B 606       5                                                       
HET    PO4  B 607       5                                                       
HET    PO4  B 608       5                                                       
HET    GOL  C 601       6                                                       
HET    GOL  C 602       6                                                       
HET    GOL  C 603       6                                                       
HET    PO4  C 604       5                                                       
HET    PO4  C 605       5                                                       
HET    PO4  C 606       5                                                       
HET    PO4  C 607       5                                                       
HET    PO4  C 608       5                                                       
HET     CL  D 601       1                                                       
HET    GOL  D 602       6                                                       
HET    GOL  D 603       6                                                       
HET    GOL  D 604       6                                                       
HET    GOL  D 605       6                                                       
HET    GOL  D 606       6                                                       
HET    PO4  D 607       5                                                       
HET    PO4  D 608       5                                                       
HET    PO4  D 609       5                                                       
HET    PO4  D 610       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    68(C5 H11 N O2 SE)                                           
FORMUL   5  GOL    15(C3 H8 O3)                                                 
FORMUL   9  PO4    17(O4 P 3-)                                                  
FORMUL  14   CL    3(CL 1-)                                                     
FORMUL  40  HOH   *2000(H2 O)                                                   
HELIX    1   1 ASP A   66  SER A   68  5                                   3    
HELIX    2   2 GLY A  192  SER A  196  5                                   5    
HELIX    3   3 GLN A  255  LEU A  259  5                                   5    
HELIX    4   4 PRO A  260  ASN A  264  5                                   5    
HELIX    5   5 ARG A  294  ASN A  298  5                                   5    
HELIX    6   6 ILE A  329  LYS A  334  1                                   6    
HELIX    7   7 ASN A  453  ASN A  457  5                                   5    
HELIX    8   8 PRO A  491  GLU A  493  5                                   3    
HELIX    9   9 LEU A  535  ILE A  539  1                                   5    
HELIX   10  10 ASP B   66  SER B   68  5                                   3    
HELIX   11  11 GLY B  192  SER B  196  5                                   5    
HELIX   12  12 GLN B  255  LEU B  259  5                                   5    
HELIX   13  13 PRO B  260  ASN B  264  5                                   5    
HELIX   14  14 ARG B  294  ASN B  298  5                                   5    
HELIX   15  15 ILE B  329  LYS B  334  1                                   6    
HELIX   16  16 ASN B  453  ASN B  457  5                                   5    
HELIX   17  17 PRO B  491  GLU B  493  5                                   3    
HELIX   18  18 LEU B  535  ILE B  539  1                                   5    
HELIX   19  19 ASP C   66  SER C   68  5                                   3    
HELIX   20  20 GLY C  192  SER C  196  5                                   5    
HELIX   21  21 GLN C  255  LEU C  259  5                                   5    
HELIX   22  22 PRO C  260  ASN C  264  5                                   5    
HELIX   23  23 ARG C  294  SER C  299  1                                   6    
HELIX   24  24 ILE C  329  LYS C  334  1                                   6    
HELIX   25  25 ASN C  453  ASN C  457  5                                   5    
HELIX   26  26 PRO C  491  GLU C  493  5                                   3    
HELIX   27  27 LEU C  535  ILE C  539  1                                   5    
HELIX   28  28 ASP D   66  SER D   68  5                                   3    
HELIX   29  29 GLY D  192  SER D  196  5                                   5    
HELIX   30  30 GLN D  255  LEU D  259  5                                   5    
HELIX   31  31 PRO D  260  ASN D  264  5                                   5    
HELIX   32  32 ARG D  294  SER D  299  1                                   6    
HELIX   33  33 ILE D  329  LYS D  334  1                                   6    
HELIX   34  34 ASN D  453  ASN D  457  5                                   5    
HELIX   35  35 PRO D  491  GLU D  493  5                                   3    
HELIX   36  36 LEU D  535  ILE D  539  1                                   5    
SHEET    1   A 6 VAL A 113  THR A 119  0                                        
SHEET    2   A 6 ILE A  70  VAL A  80 -1  N  LEU A  75   O  GLN A 115           
SHEET    3   A 6 GLY A 137  MSE A 147 -1  O  GLN A 146   N  ALA A  72           
SHEET    4   A 6 VAL A  40  ALA A  48 -1  N  ILE A  46   O  ASN A 139           
SHEET    5   A 6 ILE A  23  ARG A  26 -1  N  TYR A  24   O  ARG A  45           
SHEET    6   A 6 ILE A 173  TRP A 175  1  O  THR A 174   N  ILE A  23           
SHEET    1   B 3 ILE A  32  LEU A  33  0                                        
SHEET    2   B 3 ARG A 182  ARG A 189  1  O  HIS A 183   N  ILE A  32           
SHEET    3   B 3 LYS A 156  VAL A 157 -1  N  VAL A 157   O  ARG A 182           
SHEET    1   C 5 ILE A  32  LEU A  33  0                                        
SHEET    2   C 5 ARG A 182  ARG A 189  1  O  HIS A 183   N  ILE A  32           
SHEET    3   C 5 MSE A 528  LYS A 534 -1  O  PHE A 530   N  ILE A 186           
SHEET    4   C 5 THR A 516  TYR A 521 -1  N  TYR A 521   O  THR A 529           
SHEET    5   C 5 SER A 507  MSE A 511 -1  N  SER A 510   O  GLY A 518           
SHEET    1   D 4 THR A 125  LEU A 128  0                                        
SHEET    2   D 4 GLU A  56  ILE A  61 -1  N  ILE A  59   O  VAL A 126           
SHEET    3   D 4 THR A 159  ILE A 166 -1  O  GLN A 165   N  GLU A  56           
SHEET    4   D 4 LYS A 169  PRO A 170 -1  O  LYS A 169   N  ILE A 166           
SHEET    1   E 4 ALA A 198  THR A 206  0                                        
SHEET    2   E 4 LEU A 212  ARG A 219 -1  O  ASP A 217   N  ARG A 200           
SHEET    3   E 4 ILE A 230  SER A 237 -1  O  ASP A 231   N  ILE A 218           
SHEET    4   E 4 ARG A 248  MSE A 251 -1  O  ARG A 248   N  VAL A 234           
SHEET    1   F 5 ILE A 327  ASN A 328  0                                        
SHEET    2   F 5 GLN A 310  SER A 316 -1  N  LEU A 313   O  ILE A 327           
SHEET    3   F 5 ILE A 280  TRP A 286 -1  N  TRP A 286   O  GLN A 310           
SHEET    4   F 5 VAL A 266  VAL A 273 -1  N  SER A 270   O  VAL A 283           
SHEET    5   F 5 GLY A 346  ARG A 347  1  O  GLY A 346   N  PRO A 269           
SHEET    1   G 4 PHE A 340  GLN A 343  0                                        
SHEET    2   G 4 LEU A 356  ILE A 363 -1  O  GLN A 361   N  LEU A 342           
SHEET    3   G 4 PRO A 369  SER A 376 -1  O  MSE A 374   N  PHE A 358           
SHEET    4   G 4 HIS A 384  LEU A 385 -1  O  HIS A 384   N  TYR A 375           
SHEET    1   H 4 ILE A 349  THR A 350  0                                        
SHEET    2   H 4 LEU A 356  ILE A 363 -1  O  VAL A 357   N  ILE A 349           
SHEET    3   H 4 PRO A 369  SER A 376 -1  O  MSE A 374   N  PHE A 358           
SHEET    4   H 4 ARG A 390  THR A 391 -1  O  ARG A 390   N  ALA A 371           
SHEET    1   I 4 THR A 393  GLU A 402  0                                        
SHEET    2   I 4 VAL A 405  ASP A 412 -1  O  ARG A 411   N  GLU A 395           
SHEET    3   I 4 ALA A 419  THR A 423 -1  O  ALA A 419   N  MSE A 410           
SHEET    4   I 4 THR A 431  GLU A 432 -1  O  THR A 431   N  THR A 422           
SHEET    1   J 4 SER A 448  VAL A 452  0                                        
SHEET    2   J 4 LEU A 463  PRO A 469 -1  O  LEU A 463   N  VAL A 452           
SHEET    3   J 4 ILE A 478  SER A 483 -1  O  LYS A 481   N  PHE A 466           
SHEET    4   J 4 GLN A 495  ASP A 499 -1  O  LEU A 498   N  ILE A 478           
SHEET    1   K 6 VAL B 113  THR B 119  0                                        
SHEET    2   K 6 ILE B  70  VAL B  80 -1  N  LEU B  75   O  GLN B 115           
SHEET    3   K 6 GLY B 137  MSE B 147 -1  O  GLN B 146   N  ALA B  72           
SHEET    4   K 6 VAL B  40  ALA B  48 -1  N  ALA B  48   O  GLY B 137           
SHEET    5   K 6 ILE B  23  ARG B  26 -1  N  TYR B  24   O  ARG B  45           
SHEET    6   K 6 ILE B 173  TRP B 175  1  O  THR B 174   N  ILE B  23           
SHEET    1   L 3 ILE B  32  LEU B  33  0                                        
SHEET    2   L 3 ARG B 182  ARG B 189  1  O  HIS B 183   N  ILE B  32           
SHEET    3   L 3 LYS B 156  VAL B 157 -1  N  VAL B 157   O  ARG B 182           
SHEET    1   M 5 ILE B  32  LEU B  33  0                                        
SHEET    2   M 5 ARG B 182  ARG B 189  1  O  HIS B 183   N  ILE B  32           
SHEET    3   M 5 MSE B 528  LYS B 534 -1  O  PHE B 530   N  ILE B 186           
SHEET    4   M 5 THR B 516  TYR B 521 -1  N  TYR B 521   O  THR B 529           
SHEET    5   M 5 SER B 507  MSE B 511 -1  N  SER B 510   O  GLY B 518           
SHEET    1   N 4 THR B 125  THR B 129  0                                        
SHEET    2   N 4 GLU B  56  ILE B  61 -1  N  ILE B  59   O  VAL B 126           
SHEET    3   N 4 THR B 159  ILE B 166 -1  O  GLN B 165   N  GLU B  56           
SHEET    4   N 4 LYS B 169  PRO B 170 -1  O  LYS B 169   N  ILE B 166           
SHEET    1   O 4 ALA B 198  THR B 206  0                                        
SHEET    2   O 4 LEU B 212  ARG B 219 -1  O  ASP B 217   N  ARG B 200           
SHEET    3   O 4 ILE B 230  SER B 237 -1  O  ASP B 231   N  ILE B 218           
SHEET    4   O 4 ARG B 248  MSE B 251 -1  O  MSE B 251   N  ILE B 232           
SHEET    1   P 5 ILE B 327  ASN B 328  0                                        
SHEET    2   P 5 GLN B 310  SER B 316 -1  N  LEU B 313   O  ILE B 327           
SHEET    3   P 5 ILE B 280  TRP B 286 -1  N  TRP B 286   O  GLN B 310           
SHEET    4   P 5 VAL B 266  VAL B 273 -1  N  LEU B 272   O  TRP B 281           
SHEET    5   P 5 GLY B 346  ARG B 347  1  O  GLY B 346   N  ILE B 271           
SHEET    1   Q 4 PHE B 340  GLN B 343  0                                        
SHEET    2   Q 4 LEU B 356  ILE B 363 -1  O  GLN B 361   N  LEU B 342           
SHEET    3   Q 4 PRO B 369  SER B 376 -1  O  MSE B 374   N  PHE B 358           
SHEET    4   Q 4 HIS B 384  LEU B 385 -1  O  HIS B 384   N  TYR B 375           
SHEET    1   R 4 ILE B 349  THR B 350  0                                        
SHEET    2   R 4 LEU B 356  ILE B 363 -1  O  VAL B 357   N  ILE B 349           
SHEET    3   R 4 PRO B 369  SER B 376 -1  O  MSE B 374   N  PHE B 358           
SHEET    4   R 4 ARG B 390  THR B 391 -1  O  ARG B 390   N  ALA B 371           
SHEET    1   S 4 THR B 393  GLU B 402  0                                        
SHEET    2   S 4 VAL B 405  ASP B 412 -1  O  MSE B 407   N  ALA B 399           
SHEET    3   S 4 ALA B 419  THR B 423 -1  O  ALA B 419   N  MSE B 410           
SHEET    4   S 4 THR B 431  GLU B 432 -1  O  THR B 431   N  THR B 422           
SHEET    1   T 2 GLY B 416  SER B 417  0                                        
SHEET    2   T 2 GLN B 441  GLU B 442 -1  O  GLU B 442   N  GLY B 416           
SHEET    1   U 4 SER B 448  VAL B 452  0                                        
SHEET    2   U 4 LEU B 463  PRO B 469 -1  O  LEU B 463   N  VAL B 452           
SHEET    3   U 4 ILE B 478  SER B 483 -1  O  LYS B 481   N  PHE B 466           
SHEET    4   U 4 GLN B 495  ASP B 499 -1  O  LEU B 498   N  ILE B 478           
SHEET    1   V 6 VAL C 113  THR C 119  0                                        
SHEET    2   V 6 ILE C  70  VAL C  80 -1  N  LEU C  75   O  GLN C 115           
SHEET    3   V 6 GLY C 137  MSE C 147 -1  O  GLN C 146   N  ALA C  72           
SHEET    4   V 6 VAL C  40  ALA C  48 -1  N  LEU C  41   O  VAL C 143           
SHEET    5   V 6 TYR C  24  ARG C  26 -1  N  TYR C  24   O  ARG C  45           
SHEET    6   V 6 THR C 174  TRP C 175  1  O  THR C 174   N  VAL C  25           
SHEET    1   W 3 ILE C  32  LEU C  33  0                                        
SHEET    2   W 3 ARG C 182  ARG C 189  1  O  HIS C 183   N  ILE C  32           
SHEET    3   W 3 LYS C 156  VAL C 157 -1  N  VAL C 157   O  ARG C 182           
SHEET    1   X 5 ILE C  32  LEU C  33  0                                        
SHEET    2   X 5 ARG C 182  ARG C 189  1  O  HIS C 183   N  ILE C  32           
SHEET    3   X 5 MSE C 528  LYS C 534 -1  O  MSE C 528   N  ARG C 189           
SHEET    4   X 5 THR C 516  TYR C 521 -1  N  TYR C 521   O  THR C 529           
SHEET    5   X 5 SER C 507  MSE C 511 -1  N  SER C 510   O  GLY C 518           
SHEET    1   Y 4 THR C 125  THR C 129  0                                        
SHEET    2   Y 4 GLU C  56  ILE C  61 -1  N  ILE C  59   O  VAL C 126           
SHEET    3   Y 4 THR C 159  ILE C 166 -1  O  THR C 160   N  GLN C  60           
SHEET    4   Y 4 LYS C 169  PRO C 170 -1  O  LYS C 169   N  ILE C 166           
SHEET    1   Z 4 ALA C 198  THR C 206  0                                        
SHEET    2   Z 4 LEU C 212  ARG C 219 -1  O  ASP C 217   N  ARG C 200           
SHEET    3   Z 4 ILE C 230  SER C 237 -1  O  ASP C 231   N  ILE C 218           
SHEET    4   Z 4 ARG C 248  MSE C 251 -1  O  MSE C 251   N  ILE C 232           
SHEET    1  AA 5 ILE C 327  ASN C 328  0                                        
SHEET    2  AA 5 GLN C 310  SER C 316 -1  N  LEU C 313   O  ILE C 327           
SHEET    3  AA 5 ILE C 280  TRP C 286 -1  N  ALA C 284   O  MSE C 312           
SHEET    4  AA 5 VAL C 266  VAL C 273 -1  N  LEU C 272   O  TRP C 281           
SHEET    5  AA 5 GLY C 346  ARG C 347  1  O  GLY C 346   N  ILE C 271           
SHEET    1  AB 4 PHE C 340  GLN C 343  0                                        
SHEET    2  AB 4 LEU C 356  ILE C 363 -1  O  GLN C 361   N  LEU C 342           
SHEET    3  AB 4 PRO C 369  SER C 376 -1  O  MSE C 374   N  PHE C 358           
SHEET    4  AB 4 HIS C 384  LEU C 385 -1  O  HIS C 384   N  TYR C 375           
SHEET    1  AC 4 ILE C 349  THR C 350  0                                        
SHEET    2  AC 4 LEU C 356  ILE C 363 -1  O  VAL C 357   N  ILE C 349           
SHEET    3  AC 4 PRO C 369  SER C 376 -1  O  MSE C 374   N  PHE C 358           
SHEET    4  AC 4 ARG C 390  THR C 391 -1  O  ARG C 390   N  ALA C 371           
SHEET    1  AD 4 THR C 393  GLU C 402  0                                        
SHEET    2  AD 4 VAL C 405  ASP C 412 -1  O  MSE C 407   N  ALA C 399           
SHEET    3  AD 4 ALA C 419  THR C 423 -1  O  ALA C 419   N  MSE C 410           
SHEET    4  AD 4 THR C 431  GLU C 432 -1  O  THR C 431   N  THR C 422           
SHEET    1  AE 4 SER C 448  VAL C 452  0                                        
SHEET    2  AE 4 LEU C 463  PRO C 469 -1  O  LEU C 463   N  VAL C 452           
SHEET    3  AE 4 ILE C 478  SER C 483 -1  O  LYS C 481   N  PHE C 466           
SHEET    4  AE 4 GLN C 495  ASP C 499 -1  O  LEU C 498   N  ILE C 478           
SHEET    1  AF 6 VAL D 113  THR D 119  0                                        
SHEET    2  AF 6 ILE D  70  VAL D  80 -1  N  LEU D  75   O  GLN D 115           
SHEET    3  AF 6 GLY D 137  MSE D 147 -1  O  GLN D 146   N  ALA D  72           
SHEET    4  AF 6 VAL D  40  ALA D  48 -1  N  ILE D  46   O  ASN D 139           
SHEET    5  AF 6 ILE D  23  ARG D  26 -1  N  TYR D  24   O  ARG D  45           
SHEET    6  AF 6 ILE D 173  TRP D 175  1  O  THR D 174   N  ILE D  23           
SHEET    1  AG 3 ILE D  32  LEU D  33  0                                        
SHEET    2  AG 3 ARG D 182  ARG D 189  1  O  HIS D 183   N  ILE D  32           
SHEET    3  AG 3 LYS D 156  VAL D 157 -1  N  VAL D 157   O  ARG D 182           
SHEET    1  AH 5 ILE D  32  LEU D  33  0                                        
SHEET    2  AH 5 ARG D 182  ARG D 189  1  O  HIS D 183   N  ILE D  32           
SHEET    3  AH 5 MSE D 528  LYS D 534 -1  O  PHE D 530   N  ILE D 186           
SHEET    4  AH 5 THR D 516  TYR D 521 -1  N  TYR D 521   O  THR D 529           
SHEET    5  AH 5 SER D 507  ASP D 513 -1  N  SER D 510   O  GLY D 518           
SHEET    1  AI 4 THR D 125  THR D 129  0                                        
SHEET    2  AI 4 GLU D  56  ILE D  61 -1  N  ILE D  59   O  VAL D 126           
SHEET    3  AI 4 THR D 159  ILE D 166 -1  O  GLN D 165   N  GLU D  56           
SHEET    4  AI 4 LYS D 169  PRO D 170 -1  O  LYS D 169   N  ILE D 166           
SHEET    1  AJ 4 ALA D 198  THR D 206  0                                        
SHEET    2  AJ 4 LEU D 212  ARG D 219 -1  O  ASP D 217   N  ARG D 200           
SHEET    3  AJ 4 ILE D 230  SER D 237 -1  O  ASP D 231   N  ILE D 218           
SHEET    4  AJ 4 ARG D 248  MSE D 251 -1  O  MSE D 251   N  ILE D 232           
SHEET    1  AK 5 ILE D 327  ASN D 328  0                                        
SHEET    2  AK 5 GLN D 310  SER D 316 -1  N  LEU D 313   O  ILE D 327           
SHEET    3  AK 5 ILE D 280  TRP D 286 -1  N  TRP D 286   O  GLN D 310           
SHEET    4  AK 5 VAL D 266  VAL D 273 -1  N  LEU D 272   O  TRP D 281           
SHEET    5  AK 5 GLY D 346  ARG D 347  1  O  GLY D 346   N  ILE D 271           
SHEET    1  AL 4 PHE D 340  GLN D 343  0                                        
SHEET    2  AL 4 LEU D 356  ILE D 363 -1  O  GLN D 361   N  LEU D 342           
SHEET    3  AL 4 PRO D 369  SER D 376 -1  O  MSE D 374   N  PHE D 358           
SHEET    4  AL 4 HIS D 384  LEU D 385 -1  O  HIS D 384   N  TYR D 375           
SHEET    1  AM 4 ILE D 349  THR D 350  0                                        
SHEET    2  AM 4 LEU D 356  ILE D 363 -1  O  VAL D 357   N  ILE D 349           
SHEET    3  AM 4 PRO D 369  SER D 376 -1  O  MSE D 374   N  PHE D 358           
SHEET    4  AM 4 ARG D 390  THR D 391 -1  O  ARG D 390   N  ALA D 371           
SHEET    1  AN 4 THR D 393  GLU D 402  0                                        
SHEET    2  AN 4 VAL D 405  ASP D 412 -1  O  MSE D 407   N  ALA D 399           
SHEET    3  AN 4 ALA D 419  THR D 423 -1  O  ALA D 419   N  MSE D 410           
SHEET    4  AN 4 THR D 431  GLU D 432 -1  O  THR D 431   N  THR D 422           
SHEET    1  AO 2 GLY D 416  SER D 417  0                                        
SHEET    2  AO 2 GLN D 441  GLU D 442 -1  O  GLU D 442   N  GLY D 416           
SHEET    1  AP 4 SER D 448  VAL D 452  0                                        
SHEET    2  AP 4 LEU D 463  PRO D 469 -1  O  LEU D 463   N  VAL D 452           
SHEET    3  AP 4 ILE D 478  SER D 483 -1  O  LYS D 481   N  PHE D 466           
SHEET    4  AP 4 GLN D 495  ASP D 499 -1  O  LEU D 498   N  ILE D 478           
LINK         C   GLU A  43                 N   MSE A  44     1555   1555  1.33  
LINK         C   MSE A  44                 N   ARG A  45     1555   1555  1.33  
LINK         C   PRO A 133                 N   MSE A 134     1555   1555  1.33  
LINK         C   MSE A 134                 N   LEU A 135     1555   1555  1.33  
LINK         C   GLN A 146                 N   MSE A 147     1555   1555  1.33  
LINK         C   MSE A 147                 N   LYS A 148     1555   1555  1.33  
LINK         C   THR A 160                 N   MSE A 161     1555   1555  1.33  
LINK         C   MSE A 161                 N   PRO A 162     1555   1555  1.35  
LINK         C   PRO A 246                 N   MSE A 247     1555   1555  1.33  
LINK         C   MSE A 247                 N   ARG A 248     1555   1555  1.33  
LINK         C   ALA A 250                 N   MSE A 251     1555   1555  1.34  
LINK         C   MSE A 251                 N   THR A 252     1555   1555  1.33  
LINK         C   GLY A 289                 N   MSE A 290     1555   1555  1.34  
LINK         C   MSE A 290                 N   GLY A 291     1555   1555  1.33  
LINK         C   SER A 299                 N   MSE A 300     1555   1555  1.33  
LINK         C   MSE A 300                 N   PRO A 301     1555   1555  1.36  
LINK         C   GLY A 302                 N   MSE A 303     1555   1555  1.34  
LINK         C   MSE A 303                 N   THR A 304     1555   1555  1.33  
LINK         C   LEU A 311                 N   MSE A 312     1555   1555  1.34  
LINK         C   MSE A 312                 N   LEU A 313     1555   1555  1.34  
LINK         C   THR A 350                 N   MSE A 351     1555   1555  1.33  
LINK         C   MSE A 351                 N   GLN A 352     1555   1555  1.33  
LINK         C   ILE A 373                 N   MSE A 374     1555   1555  1.33  
LINK         C   MSE A 374                 N   TYR A 375     1555   1555  1.33  
LINK         C   LEU A 406                 N   MSE A 407     1555   1555  1.33  
LINK         C   MSE A 407                 N   LEU A 408     1555   1555  1.33  
LINK         C   ASN A 409                 N   MSE A 410     1555   1555  1.33  
LINK         C   MSE A 410                 N   ARG A 411     1555   1555  1.33  
LINK         C   CYS A 445                 N   MSE A 446     1555   1555  1.33  
LINK         C   MSE A 446                 N   ALA A 447     1555   1555  1.33  
LINK         C   SER A 510                 N   MSE A 511     1555   1555  1.33  
LINK         C   MSE A 511                 N   ILE A 512     1555   1555  1.33  
LINK         C   HIS A 527                 N   MSE A 528     1555   1555  1.34  
LINK         C   MSE A 528                 N   THR A 529     1555   1555  1.33  
LINK         C   GLU B  43                 N   MSE B  44     1555   1555  1.33  
LINK         C   MSE B  44                 N   ARG B  45     1555   1555  1.33  
LINK         C   PRO B 133                 N   MSE B 134     1555   1555  1.33  
LINK         C   MSE B 134                 N   LEU B 135     1555   1555  1.33  
LINK         C   GLN B 146                 N   MSE B 147     1555   1555  1.33  
LINK         C   MSE B 147                 N   LYS B 148     1555   1555  1.33  
LINK         C   THR B 160                 N   MSE B 161     1555   1555  1.33  
LINK         C   MSE B 161                 N   PRO B 162     1555   1555  1.35  
LINK         C   PRO B 246                 N   MSE B 247     1555   1555  1.33  
LINK         C   MSE B 247                 N   ARG B 248     1555   1555  1.33  
LINK         C   ALA B 250                 N   MSE B 251     1555   1555  1.33  
LINK         C   MSE B 251                 N   THR B 252     1555   1555  1.33  
LINK         C   GLY B 289                 N   MSE B 290     1555   1555  1.34  
LINK         C   MSE B 290                 N   GLY B 291     1555   1555  1.34  
LINK         C   SER B 299                 N   MSE B 300     1555   1555  1.33  
LINK         C   MSE B 300                 N   PRO B 301     1555   1555  1.36  
LINK         C   GLY B 302                 N   MSE B 303     1555   1555  1.34  
LINK         C   MSE B 303                 N   THR B 304     1555   1555  1.34  
LINK         C   LEU B 311                 N   MSE B 312     1555   1555  1.33  
LINK         C   MSE B 312                 N   LEU B 313     1555   1555  1.34  
LINK         C   THR B 350                 N   MSE B 351     1555   1555  1.33  
LINK         C   MSE B 351                 N   GLN B 352     1555   1555  1.33  
LINK         C   ILE B 373                 N   MSE B 374     1555   1555  1.33  
LINK         C   MSE B 374                 N   TYR B 375     1555   1555  1.33  
LINK         C   LEU B 406                 N   MSE B 407     1555   1555  1.33  
LINK         C   MSE B 407                 N   LEU B 408     1555   1555  1.34  
LINK         C   ASN B 409                 N   MSE B 410     1555   1555  1.33  
LINK         C   MSE B 410                 N   ARG B 411     1555   1555  1.33  
LINK         C   CYS B 445                 N   MSE B 446     1555   1555  1.33  
LINK         C   MSE B 446                 N   ALA B 447     1555   1555  1.33  
LINK         C   SER B 510                 N   MSE B 511     1555   1555  1.33  
LINK         C   MSE B 511                 N   ILE B 512     1555   1555  1.33  
LINK         C   HIS B 527                 N   MSE B 528     1555   1555  1.33  
LINK         C   MSE B 528                 N   THR B 529     1555   1555  1.33  
LINK         C   GLU C  43                 N   MSE C  44     1555   1555  1.33  
LINK         C   MSE C  44                 N   ARG C  45     1555   1555  1.33  
LINK         C   PRO C 133                 N   MSE C 134     1555   1555  1.33  
LINK         C   MSE C 134                 N   LEU C 135     1555   1555  1.33  
LINK         C   GLN C 146                 N   MSE C 147     1555   1555  1.33  
LINK         C   MSE C 147                 N   LYS C 148     1555   1555  1.33  
LINK         C   THR C 160                 N   MSE C 161     1555   1555  1.33  
LINK         C   MSE C 161                 N   PRO C 162     1555   1555  1.35  
LINK         C   PRO C 246                 N   MSE C 247     1555   1555  1.33  
LINK         C   MSE C 247                 N   ARG C 248     1555   1555  1.33  
LINK         C   ALA C 250                 N   MSE C 251     1555   1555  1.34  
LINK         C   MSE C 251                 N   THR C 252     1555   1555  1.33  
LINK         C   GLY C 289                 N   MSE C 290     1555   1555  1.33  
LINK         C   MSE C 290                 N   GLY C 291     1555   1555  1.33  
LINK         C   SER C 299                 N   MSE C 300     1555   1555  1.33  
LINK         C   MSE C 300                 N   PRO C 301     1555   1555  1.36  
LINK         C   GLY C 302                 N   MSE C 303     1555   1555  1.33  
LINK         C   MSE C 303                 N   THR C 304     1555   1555  1.34  
LINK         C   LEU C 311                 N   MSE C 312     1555   1555  1.34  
LINK         C   MSE C 312                 N   LEU C 313     1555   1555  1.34  
LINK         C   THR C 350                 N   MSE C 351     1555   1555  1.33  
LINK         C   MSE C 351                 N   GLN C 352     1555   1555  1.33  
LINK         C   ILE C 373                 N   MSE C 374     1555   1555  1.33  
LINK         C   MSE C 374                 N   TYR C 375     1555   1555  1.33  
LINK         C   LEU C 406                 N   MSE C 407     1555   1555  1.33  
LINK         C   MSE C 407                 N   LEU C 408     1555   1555  1.33  
LINK         C   ASN C 409                 N   MSE C 410     1555   1555  1.34  
LINK         C   MSE C 410                 N   ARG C 411     1555   1555  1.34  
LINK         C   CYS C 445                 N   MSE C 446     1555   1555  1.33  
LINK         C   MSE C 446                 N   ALA C 447     1555   1555  1.33  
LINK         C   SER C 510                 N   MSE C 511     1555   1555  1.33  
LINK         C   MSE C 511                 N   ILE C 512     1555   1555  1.33  
LINK         C   HIS C 527                 N   MSE C 528     1555   1555  1.33  
LINK         C   MSE C 528                 N   THR C 529     1555   1555  1.33  
LINK         C   GLU D  43                 N   MSE D  44     1555   1555  1.33  
LINK         C   MSE D  44                 N   ARG D  45     1555   1555  1.34  
LINK         C   PRO D 133                 N   MSE D 134     1555   1555  1.33  
LINK         C   MSE D 134                 N   LEU D 135     1555   1555  1.33  
LINK         C   GLN D 146                 N   MSE D 147     1555   1555  1.33  
LINK         C   MSE D 147                 N   LYS D 148     1555   1555  1.32  
LINK         C   THR D 160                 N   MSE D 161     1555   1555  1.33  
LINK         C   MSE D 161                 N   PRO D 162     1555   1555  1.35  
LINK         C   PRO D 246                 N   MSE D 247     1555   1555  1.33  
LINK         C   MSE D 247                 N   ARG D 248     1555   1555  1.33  
LINK         C   ALA D 250                 N   MSE D 251     1555   1555  1.34  
LINK         C   MSE D 251                 N   THR D 252     1555   1555  1.34  
LINK         C   GLY D 289                 N   MSE D 290     1555   1555  1.34  
LINK         C   MSE D 290                 N   GLY D 291     1555   1555  1.33  
LINK         C   SER D 299                 N   MSE D 300     1555   1555  1.33  
LINK         C   MSE D 300                 N   PRO D 301     1555   1555  1.35  
LINK         C   GLY D 302                 N   MSE D 303     1555   1555  1.34  
LINK         C   MSE D 303                 N   THR D 304     1555   1555  1.33  
LINK         C   LEU D 311                 N   MSE D 312     1555   1555  1.34  
LINK         C   MSE D 312                 N   LEU D 313     1555   1555  1.34  
LINK         C   THR D 350                 N   MSE D 351     1555   1555  1.33  
LINK         C   MSE D 351                 N   GLN D 352     1555   1555  1.33  
LINK         C   ILE D 373                 N   MSE D 374     1555   1555  1.33  
LINK         C   MSE D 374                 N   TYR D 375     1555   1555  1.33  
LINK         C   LEU D 406                 N   MSE D 407     1555   1555  1.33  
LINK         C   MSE D 407                 N   LEU D 408     1555   1555  1.33  
LINK         C   ASN D 409                 N   MSE D 410     1555   1555  1.33  
LINK         C   MSE D 410                 N   ARG D 411     1555   1555  1.34  
LINK         C   CYS D 445                 N   MSE D 446     1555   1555  1.32  
LINK         C   MSE D 446                 N   ALA D 447     1555   1555  1.33  
LINK         C   SER D 510                 N   MSE D 511     1555   1555  1.33  
LINK         C   MSE D 511                 N   ILE D 512     1555   1555  1.33  
LINK         C   HIS D 527                 N   MSE D 528     1555   1555  1.34  
LINK         C   MSE D 528                 N   THR D 529     1555   1555  1.33  
CISPEP   1 ALA A  120    PRO A  121          0        -1.61                     
CISPEP   2 LEU A  226    GLN A  227          0         2.54                     
CISPEP   3 ALA B  120    PRO B  121          0        -0.74                     
CISPEP   4 LEU B  226    GLN B  227          0         2.37                     
CISPEP   5 ALA C  120    PRO C  121          0        -1.78                     
CISPEP   6 LEU C  226    GLN C  227          0         1.76                     
CISPEP   7 ALA D  120    PRO D  121          0         0.22                     
CISPEP   8 LEU D  226    GLN D  227          0         1.35                     
SITE     1 AC1  7 SER A  98  HIS A  99  GLY A 503  TRP A 504                    
SITE     2 AC1  7 GLU A 522  SER A 523  HIS A 527                               
SITE     1 AC2  9 GLU A 275  ARG A 347  ILE A 349  ILE A 450                    
SITE     2 AC2  9 LYS A 451  HOH A 752  HOH A 861  HOH A 871                    
SITE     3 AC2  9 HOH A 900                                                     
SITE     1 AC3  9 ASP A  35  ARG A 105  GLY A 187  VAL A 188                    
SITE     2 AC3  9 GLN A 190  HOH A 725  HOH A 859  HOH A 885                    
SITE     3 AC3  9 HOH A1165                                                     
SITE     1 AC4  5 ARG A 200  SER A 223  VAL A 224  TRP A 504                    
SITE     2 AC4  5 HOH A 902                                                     
SITE     1 AC5  5 LYS A 229  LYS A 254  HIS A 261  HOH A 983                    
SITE     2 AC5  5 HOH A1065                                                     
SITE     1 AC6  7 ARG A  26  HIS A  89  PHE A  90  SER A  91                    
SITE     2 AC6  7 HOH A 727  HOH A 960  HOH A1167                               
SITE     1 AC7  5 ARG A 200  ARG A 411  ARG A 475  TYR A 506                    
SITE     2 AC7  5 HOH A 902                                                     
SITE     1 AC8  5 HIS A 384  HIS A 386  HOH A1016  HOH A1103                    
SITE     2 AC8  5 HOH A1155                                                     
SITE     1 AC9  6 ARG A 236  GLU A 245  LYS A 321  HOH A1097                    
SITE     2 AC9  6 HOH A1119  HOH A1159                                          
SITE     1 BC1  3 LYS B  50  GLN D  49  LYS D  50                               
SITE     1 BC2  1 GLU B 109                                                     
SITE     1 BC3  8 GLU A 109  SER A 110  LYS B 229  LYS B 254                    
SITE     2 BC3  8 HIS B 261  HOH B1062  HOH B1173  HOH B1174                    
SITE     1 BC4  7 GLU B 275  ILE B 450  LYS B 451  HOH B 737                    
SITE     2 BC4  7 HOH B 741  HOH B1017  HOH B1026                               
SITE     1 BC5 10 ASN A 168  ASP B  35  ARG B 105  ILE B 186                    
SITE     2 BC5 10 GLY B 187  VAL B 188  GLN B 190  HOH B 789                    
SITE     3 BC5 10 HOH B 905  HOH B 962                                          
SITE     1 BC6  5 ARG B 200  ARG B 411  ARG B 475  TYR B 506                    
SITE     2 BC6  5 HOH B 835                                                     
SITE     1 BC7  9 ARG B  26  HIS B  89  PHE B  90  SER B  91                    
SITE     2 BC7  9 HOH B 780  HOH B 850  HOH B 920  HOH B 936                    
SITE     3 BC7  9 HOH B1127                                                     
SITE     1 BC8  4 ARG B 236  THR B 238  GLU B 245  LYS B 321                    
SITE     1 BC9  6 ASN C 103  GLU C 109  SER C 110  HOH C 759                    
SITE     2 BC9  6 HOH C1069  HOH C1070                                          
SITE     1 CC1  8 GLU C 275  ILE C 349  ILE C 450  LYS C 451                    
SITE     2 CC1  8 HOH C 792  HOH C 910  HOH C 988  HOH C1065                    
SITE     1 CC2  7 VAL C  93  THR C  94  LEU C 108  TYR C 111                    
SITE     2 CC2  7 HOH C 962  HOH C1179  ASN D 292                               
SITE     1 CC3  3 HIS C 261  HOH C 768  HOH C1128                               
SITE     1 CC4  7 ARG C 200  ASP C 225  ARG C 411  ARG C 475                    
SITE     2 CC4  7 TYR C 506  HOH C 779  HOH C 975                               
SITE     1 CC5  8 ARG C  26  HIS C  89  PHE C  90  SER C  91                    
SITE     2 CC5  8 HOH C 744  HOH C 790  HOH C1002  HOH C1059                    
SITE     1 CC6  5 HIS C 384  HIS C 386  HOH C 832  HOH C 871                    
SITE     2 CC6  5 HOH C1110                                                     
SITE     1 CC7  4 ARG C 390  ARG C 414  ARG C 437  HOH C1190                    
SITE     1 CC8  1 ARG D 236                                                     
SITE     1 CC9  8 GLU D 275  ILE D 349  ILE D 450  LYS D 451                    
SITE     2 CC9  8 HOH D 735  HOH D 843  HOH D 844  HOH D1008                    
SITE     1 DC1  6 ASN C 292  VAL D  93  THR D  94  LEU D 108                    
SITE     2 DC1  6 TYR D 111  HOH D 834                                          
SITE     1 DC2  9 ASP D  35  ARG D 105  GLY D 187  VAL D 188                    
SITE     2 DC2  9 ARG D 189  ASP D 193  HOH D 756  HOH D 870                    
SITE     3 DC2  9 HOH D 927                                                     
SITE     1 DC3  9 SER D  98  HIS D  99  GLY D 503  TRP D 504                    
SITE     2 DC3  9 GLU D 522  SER D 523  SER D 524  ALA D 526                    
SITE     3 DC3  9 HOH D1162                                                     
SITE     1 DC4  7 HOH C1068  ASN D 103  ALA D 107  LEU D 108                    
SITE     2 DC4  7 GLU D 109  SER D 110  HOH D 732                               
SITE     1 DC5  6 HOH C 718  LYS D 229  LYS D 254  HIS D 261                    
SITE     2 DC5  6 HOH D 709  HOH D 712                                          
SITE     1 DC6 10 ARG D  26  HIS D  89  PHE D  90  SER D  91                    
SITE     2 DC6 10 HOH D 771  HOH D 880  HOH D1005  HOH D1056                    
SITE     3 DC6 10 HOH D1109  HOH D1129                                          
SITE     1 DC7  5 ARG D 200  ARG D 411  ARG D 475  TYR D 506                    
SITE     2 DC7  5 HOH D1153                                                     
SITE     1 DC8  5 HIS D 384  HIS D 386  HOH D 818  HOH D 937                    
SITE     2 DC8  5 HOH D1155                                                     
CRYST1  171.738  171.738  243.786  90.00  90.00 120.00 H 3          36          
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      0.005823  0.003362  0.000000        0.00000                         
SCALE2      0.000000  0.006724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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