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Database: PDB
Entry: 3GE1
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HEADER    TRANSFERASE                             24-FEB-09   3GE1              
TITLE     2.7 ANGSTROM CRYSTAL STRUCTURE OF GLYCEROL KINASE (GLPK) FROM         
TITLE    2 STAPHYLOCOCCUS AUREUS IN COMPLEX WITH ADP AND GLYCEROL               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCEROL KINASE;                                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ATP:GLYCEROL 3-PHOSPHOTRANSFERASE, GLYCEROKINASE, GK;       
COMPND   5 EC: 2.7.1.30;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL;        
SOURCE   3 ORGANISM_TAXID: 93062;                                               
SOURCE   4 STRAIN: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS COL;                     
SOURCE   5 GENE: GLPK, SACOL1320;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    GLYCEROL KINASE, GLYCEROL, ADP, IDP00743, ATP-BINDING, GLYCEROL       
KEYWDS   2 METABOLISM, KINASE, NUCLEOTIDE-BINDING, TRANSFERASE, STRUCTURAL      
KEYWDS   3 GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES,     
KEYWDS   4 CSGID                                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.MINASOV,J.BRUNZELLE,T.SKARINA,O.ONOPRIYENKO,S.N.PETERSON,           
AUTHOR   2 A.SAVCHENKO,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF           
AUTHOR   3 INFECTIOUS DISEASES (CSGID)                                          
REVDAT   5   01-NOV-17 3GE1    1       REMARK                                   
REVDAT   4   13-JUL-11 3GE1    1       VERSN                                    
REVDAT   3   27-OCT-09 3GE1    1       AUTHOR                                   
REVDAT   2   21-APR-09 3GE1    1       REMARK                                   
REVDAT   1   24-MAR-09 3GE1    0                                                
JRNL        AUTH   G.MINASOV,J.BRUNZELLE,T.SKARINA,O.ONOPRIYENKO,S.N.PETERSON,  
JRNL        AUTH 2 A.SAVCHENKO,W.F.ANDERSON,                                    
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   2.7 ANGSTROM CRYSTAL STRUCTURE OF GLYCEROL KINASE (GLPK)     
JRNL        TITL 2 FROM STAPHYLOCOCCUS AUREUS IN COMPLEX WITH ADP AND GLYCEROL  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 53455                          
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) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2855                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3193                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 193                          
REMARK   3   BIN FREE R VALUE                    : 0.3860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15660                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 176                                     
REMARK   3   SOLVENT ATOMS            : 274                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 57.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.01000                                             
REMARK   3    B22 (A**2) : -6.79000                                             
REMARK   3    B33 (A**2) : -3.65000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.84000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.386         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.322         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.063        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.915                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 16169 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 10770 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21913 ; 1.011 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 26219 ; 0.691 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1990 ; 2.273 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   771 ;25.653 ;24.812       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2740 ;11.141 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    84 ;14.684 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2376 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 18090 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  3314 ; 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):  9827 ; 0.848 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4112 ; 0.247 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15770 ; 1.593 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6342 ; 2.862 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6143 ; 4.516 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     497      2                      
REMARK   3           1     C      2       C     497      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2909 ;  0.07 ;  0.10           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3634 ;  0.13 ;  2.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2909 ;  0.46 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3634 ;  0.53 ;  5.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      2       B     497      2                      
REMARK   3           1     D      2       D     497      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    B    (A):   2914 ;  0.06 ;  0.10           
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   3640 ;  0.12 ;  2.00           
REMARK   3   TIGHT THERMAL      2    B (A**2):   2914 ;  0.47 ;  2.00           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   3640 ;  0.57 ;  5.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 28                                         
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     0        A    35                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7695 -56.8681   0.3111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1606 T22:   0.2848                                     
REMARK   3      T33:   0.1541 T12:  -0.0319                                     
REMARK   3      T13:  -0.1186 T23:  -0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4649 L22:   4.7660                                     
REMARK   3      L33:   1.0038 L12:   4.5970                                     
REMARK   3      L13:   0.0320 L23:  -0.2188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1827 S12:  -0.4475 S13:  -0.1378                       
REMARK   3      S21:  -0.6868 S22:   0.0161 S23:   0.4090                       
REMARK   3      S31:  -0.0404 S32:  -0.4179 S33:   0.1666                       
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 :   A    36        A   178                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.1766 -50.7619 -10.1259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0660 T22:   0.1387                                     
REMARK   3      T33:   0.1362 T12:   0.0221                                     
REMARK   3      T13:   0.0460 T23:  -0.0673                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3690 L22:   2.1493                                     
REMARK   3      L33:   1.2353 L12:   0.4862                                     
REMARK   3      L13:   0.0549 L23:  -0.6338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1139 S12:   0.1153 S13:  -0.2374                       
REMARK   3      S21:  -0.2112 S22:  -0.0344 S23:  -0.2447                       
REMARK   3      S31:   0.2492 S32:   0.1731 S33:   0.1482                       
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 :   A   179        A   300                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6807 -53.5053 -18.6407              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2906 T22:   0.2000                                     
REMARK   3      T33:   0.1739 T12:  -0.0544                                     
REMARK   3      T13:  -0.0473 T23:  -0.1246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2176 L22:   1.8291                                     
REMARK   3      L33:   2.6856 L12:   0.0562                                     
REMARK   3      L13:  -0.9961 L23:  -0.4240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1185 S12:   0.3179 S13:  -0.2540                       
REMARK   3      S21:  -0.6740 S22:   0.0060 S23:   0.0989                       
REMARK   3      S31:   0.2242 S32:  -0.3527 S33:   0.1125                       
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 :   A   301        A   357                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7770 -30.5601  -2.2746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1114 T22:   0.1631                                     
REMARK   3      T33:   0.0962 T12:  -0.0810                                     
REMARK   3      T13:  -0.0544 T23:   0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5864 L22:   3.3262                                     
REMARK   3      L33:   2.6088 L12:   0.6423                                     
REMARK   3      L13:   0.2924 L23:   2.3415                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0059 S12:  -0.0893 S13:  -0.0307                       
REMARK   3      S21:   0.1915 S22:  -0.0556 S23:   0.2309                       
REMARK   3      S31:   0.4053 S32:  -0.3903 S33:   0.0615                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   358        A   417                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1847 -29.0264  -7.6579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2379 T22:   0.2400                                     
REMARK   3      T33:   0.1870 T12:   0.0019                                     
REMARK   3      T13:  -0.1867 T23:  -0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0424 L22:   3.1482                                     
REMARK   3      L33:   2.7812 L12:   1.6227                                     
REMARK   3      L13:   0.1193 L23:   1.6179                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:   0.0436 S13:  -0.0278                       
REMARK   3      S21:  -0.6777 S22:  -0.2421 S23:   0.6126                       
REMARK   3      S31:  -0.1022 S32:  -0.5827 S33:   0.3369                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   418        A   458                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8237 -48.8215  -9.4661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1098 T22:   0.2827                                     
REMARK   3      T33:   0.1573 T12:  -0.1119                                     
REMARK   3      T13:  -0.0503 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3984 L22:   9.1388                                     
REMARK   3      L33:   0.0877 L12:  -1.2854                                     
REMARK   3      L13:  -0.1041 L23:   0.8226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0464 S12:   0.1295 S13:   0.0253                       
REMARK   3      S21:  -0.2435 S22:  -0.0332 S23:   0.5126                       
REMARK   3      S31:  -0.0066 S32:  -0.0485 S33:   0.0795                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   459        A   498                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.4856 -28.4490 -11.2825              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0911 T22:   0.3953                                     
REMARK   3      T33:   0.2080 T12:   0.0471                                     
REMARK   3      T13:  -0.1231 T23:  -0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3843 L22:   4.1924                                     
REMARK   3      L33:   1.1315 L12:   1.3004                                     
REMARK   3      L13:   0.7343 L23:  -0.3267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1420 S12:   0.3711 S13:   0.1201                       
REMARK   3      S21:  -0.3827 S22:   0.1618 S23:   0.7938                       
REMARK   3      S31:  -0.0619 S32:  -0.3728 S33:  -0.0199                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B    70                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.8725   2.5897  24.0557              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0514 T22:   0.1185                                     
REMARK   3      T33:   0.1327 T12:  -0.0377                                     
REMARK   3      T13:  -0.0177 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2107 L22:   3.4757                                     
REMARK   3      L33:   5.9401 L12:   0.9829                                     
REMARK   3      L13:   2.7565 L23:   1.3583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3860 S12:  -0.3972 S13:   0.1759                       
REMARK   3      S21:  -0.0209 S22:  -0.1770 S23:  -0.0849                       
REMARK   3      S31:   0.2787 S32:   0.0453 S33:  -0.2090                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    71        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4661   7.8871   6.9253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5644 T22:   0.1020                                     
REMARK   3      T33:   0.1988 T12:   0.0669                                     
REMARK   3      T13:  -0.0013 T23:   0.0932                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7304 L22:   1.3567                                     
REMARK   3      L33:   1.8224 L12:  -0.4439                                     
REMARK   3      L13:   0.5992 L23:   0.2090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2780 S12:   0.3088 S13:   0.1374                       
REMARK   3      S21:  -0.7608 S22:   0.0420 S23:   0.1762                       
REMARK   3      S31:  -0.5714 S32:  -0.2095 S33:  -0.3200                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   121        B   195                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5708  13.4119   4.7323              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5814 T22:   0.1548                                     
REMARK   3      T33:   0.2501 T12:   0.0392                                     
REMARK   3      T13:  -0.0966 T23:   0.0944                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9723 L22:   1.5975                                     
REMARK   3      L33:   0.9933 L12:  -0.0999                                     
REMARK   3      L13:  -0.3072 L23:   1.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1038 S12:   0.1727 S13:   0.3429                       
REMARK   3      S21:  -0.9464 S22:  -0.0490 S23:   0.1487                       
REMARK   3      S31:  -0.6479 S32:  -0.1741 S33:  -0.0548                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   196        B   305                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.1853  13.3584   9.5770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4848 T22:   0.0993                                     
REMARK   3      T33:   0.2775 T12:  -0.1222                                     
REMARK   3      T13:   0.1426 T23:  -0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4001 L22:   2.1504                                     
REMARK   3      L33:   1.6895 L12:   0.0921                                     
REMARK   3      L13:   0.0835 L23:   0.8598                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0816 S12:   0.0398 S13:   0.3999                       
REMARK   3      S21:  -0.8677 S22:   0.1523 S23:  -0.3268                       
REMARK   3      S31:  -0.6939 S32:   0.3264 S33:  -0.2339                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   306        B   386                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5082 -17.1580   4.9573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0412 T22:   0.1061                                     
REMARK   3      T33:   0.1028 T12:  -0.0227                                     
REMARK   3      T13:  -0.0040 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9869 L22:   5.7852                                     
REMARK   3      L33:   3.3408 L12:   0.9113                                     
REMARK   3      L13:  -0.3498 L23:   0.4393                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1106 S12:  -0.3075 S13:  -0.0805                       
REMARK   3      S21:  -0.3207 S22:   0.0668 S23:  -0.3694                       
REMARK   3      S31:  -0.0952 S32:   0.0261 S33:  -0.1774                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   387        B   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3704  -5.7920   7.8958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1418 T22:   0.3856                                     
REMARK   3      T33:   0.4157 T12:  -0.1439                                     
REMARK   3      T13:   0.0411 T23:  -0.1009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6713 L22:   4.0138                                     
REMARK   3      L33:   2.5839 L12:  -1.8916                                     
REMARK   3      L13:   1.3942 L23:  -0.0293                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0635 S12:   0.1091 S13:   0.1894                       
REMARK   3      S21:  -0.4567 S22:   0.1374 S23:  -0.7460                       
REMARK   3      S31:  -0.3618 S32:   0.4881 S33:  -0.2010                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   437        B   497                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.0081  -3.4240   8.7246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2701 T22:   0.2300                                     
REMARK   3      T33:   0.4318 T12:  -0.1469                                     
REMARK   3      T13:   0.2476 T23:  -0.1444                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0378 L22:   2.1327                                     
REMARK   3      L33:   2.7413 L12:   0.3566                                     
REMARK   3      L13:   0.0926 L23:   0.8922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0978 S12:  -0.0965 S13:  -0.0124                       
REMARK   3      S21:  -0.6521 S22:   0.3352 S23:  -0.8568                       
REMARK   3      S31:  -0.3408 S32:   0.5783 S33:  -0.4330                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4055 -58.4211  18.1376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0862 T22:   0.0815                                     
REMARK   3      T33:   0.1871 T12:   0.0323                                     
REMARK   3      T13:   0.0346 T23:   0.0652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3953 L22:   3.0829                                     
REMARK   3      L33:   3.9290 L12:  -0.3584                                     
REMARK   3      L13:  -1.9359 L23:   0.5597                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4053 S12:   0.2053 S13:  -0.1050                       
REMARK   3      S21:  -0.4333 S22:  -0.1549 S23:  -0.4182                       
REMARK   3      S31:  -0.1500 S32:   0.1793 S33:  -0.2503                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    67        C    96                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4335 -68.0225  18.5757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4315 T22:   0.0401                                     
REMARK   3      T33:   0.2383 T12:  -0.0099                                     
REMARK   3      T13:   0.0109 T23:   0.0828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3244 L22:   2.2534                                     
REMARK   3      L33:   4.4851 L12:   0.3162                                     
REMARK   3      L13:  -1.9165 L23:   1.8714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1113 S12:   0.1592 S13:  -0.1712                       
REMARK   3      S21:  -0.3723 S22:   0.0453 S23:  -0.1653                       
REMARK   3      S31:   0.5270 S32:  -0.0596 S33:  -0.1566                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    97        C   206                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.3432 -69.7737  34.3559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1972 T22:   0.1883                                     
REMARK   3      T33:   0.2172 T12:  -0.0920                                     
REMARK   3      T13:  -0.0162 T23:   0.1021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9235 L22:   2.5903                                     
REMARK   3      L33:   1.1955 L12:  -0.7854                                     
REMARK   3      L13:  -0.2672 L23:   0.6820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0843 S12:  -0.1808 S13:  -0.2919                       
REMARK   3      S21:   0.4271 S22:   0.0387 S23:   0.1848                       
REMARK   3      S31:   0.4511 S32:  -0.2556 S33:   0.0456                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   207        C   296                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9662 -68.5387  31.6329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1055 T22:   0.2442                                     
REMARK   3      T33:   0.2893 T12:   0.0738                                     
REMARK   3      T13:  -0.0658 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9563 L22:   2.2505                                     
REMARK   3      L33:   1.1015 L12:   0.0328                                     
REMARK   3      L13:  -0.6184 L23:   0.1472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0195 S12:  -0.2900 S13:  -0.2156                       
REMARK   3      S21:   0.0459 S22:   0.0551 S23:  -0.3422                       
REMARK   3      S31:   0.2835 S32:   0.3378 S33:  -0.0356                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   297        C   387                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7045 -41.4974  36.6692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0622 T22:   0.2630                                     
REMARK   3      T33:   0.0984 T12:   0.0043                                     
REMARK   3      T13:   0.0022 T23:   0.0364                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0955 L22:   6.6849                                     
REMARK   3      L33:   0.6234 L12:  -2.0799                                     
REMARK   3      L13:  -0.1628 L23:   0.3407                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2278 S12:   0.0041 S13:   0.0957                       
REMARK   3      S21:  -0.5744 S22:  -0.0404 S23:  -0.3652                       
REMARK   3      S31:   0.0439 S32:   0.1665 S33:  -0.1874                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   388        C   468                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3332 -54.4578  35.2615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0362 T22:   0.5036                                     
REMARK   3      T33:   0.4326 T12:   0.0553                                     
REMARK   3      T13:  -0.0427 T23:   0.0889                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1693 L22:   5.4957                                     
REMARK   3      L33:   3.5324 L12:  -1.5971                                     
REMARK   3      L13:  -1.1336 L23:   4.3813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0049 S12:  -0.3198 S13:   0.0189                       
REMARK   3      S21:   0.2940 S22:   0.3986 S23:  -0.5290                       
REMARK   3      S31:   0.2600 S32:   0.3380 S33:  -0.4035                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   469        C   497                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.0027 -40.6692  48.8466              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0949 T22:   0.3845                                     
REMARK   3      T33:   0.2067 T12:   0.0077                                     
REMARK   3      T13:  -0.0984 T23:   0.0874                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6306 L22:   1.6864                                     
REMARK   3      L33:   3.6642 L12:  -2.5757                                     
REMARK   3      L13:  -3.1137 L23:   0.4195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2218 S12:  -1.1466 S13:   0.4400                       
REMARK   3      S21:   0.3149 S22:   0.2300 S23:  -0.4556                       
REMARK   3      S31:   0.0824 S32:   0.6545 S33:  -0.0082                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D    70                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0919  -3.2566  34.2921              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0251 T22:   0.2396                                     
REMARK   3      T33:   0.1464 T12:   0.0131                                     
REMARK   3      T13:  -0.0119 T23:  -0.0702                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3846 L22:   3.4886                                     
REMARK   3      L33:   4.6606 L12:  -1.8414                                     
REMARK   3      L13:   1.9552 L23:  -1.6448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2249 S12:   0.1767 S13:   0.3266                       
REMARK   3      S21:  -0.2278 S22:  -0.2776 S23:   0.3611                       
REMARK   3      S31:   0.0011 S32:  -0.0180 S33:   0.0528                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    71        D   178                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4165  -6.7709  54.0620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1993 T22:   0.3240                                     
REMARK   3      T33:   0.0822 T12:  -0.0404                                     
REMARK   3      T13:  -0.0162 T23:  -0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9911 L22:   1.4423                                     
REMARK   3      L33:   1.5629 L12:   0.1179                                     
REMARK   3      L13:  -0.1132 L23:   0.3279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0160 S12:  -0.1885 S13:   0.0680                       
REMARK   3      S21:   0.4845 S22:   0.0219 S23:  -0.0375                       
REMARK   3      S31:  -0.1122 S32:   0.2968 S33:  -0.0379                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   179        D   303                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.8303  -5.4023  52.0656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0718 T22:   0.3094                                     
REMARK   3      T33:   0.2303 T12:   0.0110                                     
REMARK   3      T13:   0.0717 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0938 L22:   2.4640                                     
REMARK   3      L33:   1.4604 L12:  -0.0621                                     
REMARK   3      L13:  -0.2142 L23:  -0.3178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0396 S12:  -0.1123 S13:   0.1614                       
REMARK   3      S21:   0.3750 S22:   0.0430 S23:   0.5213                       
REMARK   3      S31:  -0.1637 S32:  -0.2985 S33:  -0.0826                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   304        D   338                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8273 -26.5244  31.0137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4214 T22:   0.2423                                     
REMARK   3      T33:   0.1239 T12:   0.0945                                     
REMARK   3      T13:  -0.1105 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3130 L22:   0.8096                                     
REMARK   3      L33:   2.3545 L12:  -0.5226                                     
REMARK   3      L13:  -0.2154 L23:  -0.9273                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1897 S12:   0.3195 S13:   0.1692                       
REMARK   3      S21:  -0.5409 S22:  -0.1762 S23:   0.0958                       
REMARK   3      S31:   0.4360 S32:   0.0370 S33:  -0.0136                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   339        D   412                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5936 -30.1621  41.6126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0649 T22:   0.2826                                     
REMARK   3      T33:   0.2160 T12:  -0.0490                                     
REMARK   3      T13:  -0.0500 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9173 L22:   5.2074                                     
REMARK   3      L33:   2.8966 L12:  -1.9148                                     
REMARK   3      L13:   0.1404 L23:  -1.0586                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1456 S12:  -0.1106 S13:  -0.0958                       
REMARK   3      S21:  -0.2866 S22:  -0.0810 S23:   0.7781                       
REMARK   3      S31:   0.2665 S32:  -0.3273 S33:   0.2267                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   413        D   468                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5858 -12.7199  35.0272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0892 T22:   0.4596                                     
REMARK   3      T33:   0.5153 T12:  -0.0160                                     
REMARK   3      T13:  -0.1290 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1702 L22:   3.5394                                     
REMARK   3      L33:   2.1476 L12:  -0.6626                                     
REMARK   3      L13:  -0.0214 L23:  -0.0031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0962 S12:   0.0586 S13:  -0.0029                       
REMARK   3      S21:  -0.5442 S22:  -0.0515 S23:   0.6706                       
REMARK   3      S31:   0.0920 S32:  -0.4547 S33:  -0.0447                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   469        D   497                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.9797 -37.0899  42.9379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1635 T22:   0.3062                                     
REMARK   3      T33:   0.3573 T12:  -0.1173                                     
REMARK   3      T13:   0.0192 T23:  -0.0313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9346 L22:   3.4610                                     
REMARK   3      L33:   4.5320 L12:  -4.0687                                     
REMARK   3      L13:   2.6082 L23:  -2.6957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0647 S12:  -0.2432 S13:  -1.0339                       
REMARK   3      S21:  -0.1871 S22:   0.2227 S23:   0.8420                       
REMARK   3      S31:   0.7262 S32:  -0.4936 S33:  -0.2874                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3GE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051743.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97624                            
REMARK 200  MONOCHROMATOR                  : SI{111}                            
REMARK 200  OPTICS                         : BERYLLIUM LENSES                   
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56438                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.11600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3EZW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2% GLYCEROL, PEG3350 20%, 0.2M SODIUM    
REMARK 280  DIHYDROGEN PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       96.82550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: CHAINS A, B, C, D REPRESENT BIOLOGICAL ASSEMBLY (TETRAMER).  
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 63710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -176.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     GLU B   498                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     GLU C   498                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     GLU D   498                                                      
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    MSE A   1        6.29   -169.09                                   
REMARK 500    GLU A  83      -38.40     64.43                                   
REMARK 500    LEU A 129     -132.85   -111.51                                   
REMARK 500    PRO A 133        0.04    -64.85                                   
REMARK 500    PHE A 231       46.40   -153.87                                   
REMARK 500    GLU A 235       73.49   -117.50                                   
REMARK 500    ALA A 242      138.97    174.61                                   
REMARK 500    ALA A 278      106.16    -52.29                                   
REMARK 500    SER A 308      -87.55   -129.64                                   
REMARK 500    ALA A 346       46.74    -83.67                                   
REMARK 500    TRP A 355       70.14     55.67                                   
REMARK 500    GLU A 436       48.42    -87.45                                   
REMARK 500    GLU A 467      137.94   -174.23                                   
REMARK 500    LYS A 472       51.74   -154.84                                   
REMARK 500    MSE B   1       58.45    -95.55                                   
REMARK 500    GLU B  83      -43.20     61.25                                   
REMARK 500    LEU B 129     -129.87   -116.22                                   
REMARK 500    PRO B 133        4.02    -57.15                                   
REMARK 500    ARG B 151      -70.43    -35.74                                   
REMARK 500    LEU B 196       69.42     66.94                                   
REMARK 500    PHE B 231       59.25   -152.83                                   
REMARK 500    GLU B 235       74.12   -113.33                                   
REMARK 500    ALA B 242      146.52   -178.81                                   
REMARK 500    ALA B 253       38.20     76.66                                   
REMARK 500    TYR B 291      152.03    179.17                                   
REMARK 500    SER B 308      -89.13   -121.80                                   
REMARK 500    GLU B 339       59.15     39.70                                   
REMARK 500    TRP B 355       70.58     44.46                                   
REMARK 500    LYS B 372      -64.72    -29.03                                   
REMARK 500    SER B 404       88.30    171.25                                   
REMARK 500    GLU B 467      133.73   -171.14                                   
REMARK 500    LYS B 472       58.99   -146.07                                   
REMARK 500    MSE B 473      111.00   -163.65                                   
REMARK 500    GLU C  83      -34.32     64.50                                   
REMARK 500    LEU C 129     -131.58   -110.22                                   
REMARK 500    LEU C 189        6.74     80.11                                   
REMARK 500    GLU C 221      139.07   -172.14                                   
REMARK 500    PHE C 231       46.81   -155.58                                   
REMARK 500    ALA C 242      138.97    176.93                                   
REMARK 500    ALA C 278      102.18    -56.31                                   
REMARK 500    SER C 308      -91.84   -127.37                                   
REMARK 500    ARG C 320       54.47     38.12                                   
REMARK 500    PRO C 345       46.35    -74.91                                   
REMARK 500    ALA C 346       47.67    -72.41                                   
REMARK 500    LYS C 472       51.89   -151.13                                   
REMARK 500    ALA D  48      -38.08    -38.94                                   
REMARK 500    ASP D  67       74.57     39.28                                   
REMARK 500    GLU D  83      -38.84     61.42                                   
REMARK 500    LEU D 129     -135.27   -114.44                                   
REMARK 500    PRO D 133       -2.98    -57.79                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
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 ADP A 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 504                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 499                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 504                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G25   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF GLYCEROL KINASE (GLPK) IN COMPLEX WITH GLYCEROL     
REMARK 900 RELATED ID: IDP00743   RELATED DB: TARGETDB                          
DBREF  3GE1 A    1   498  UNP    Q5HGD2   GLPK_STAAC       1    498             
DBREF  3GE1 B    1   498  UNP    Q5HGD2   GLPK_STAAC       1    498             
DBREF  3GE1 C    1   498  UNP    Q5HGD2   GLPK_STAAC       1    498             
DBREF  3GE1 D    1   498  UNP    Q5HGD2   GLPK_STAAC       1    498             
SEQADV 3GE1 SER A   -2  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ASN A   -1  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ALA A    0  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 SER B   -2  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ASN B   -1  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ALA B    0  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 SER C   -2  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ASN C   -1  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ALA C    0  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 SER D   -2  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ASN D   -1  UNP  Q5HGD2              EXPRESSION TAG                 
SEQADV 3GE1 ALA D    0  UNP  Q5HGD2              EXPRESSION TAG                 
SEQRES   1 A  501  SER ASN ALA MSE GLU LYS TYR ILE LEU SER ILE ASP GLN          
SEQRES   2 A  501  GLY THR THR SER SER ARG ALA ILE LEU PHE ASN GLN LYS          
SEQRES   3 A  501  GLY GLU ILE ALA GLY VAL ALA GLN ARG GLU PHE LYS GLN          
SEQRES   4 A  501  TYR PHE PRO GLN SER GLY TRP VAL GLU HIS ASP ALA ASN          
SEQRES   5 A  501  GLU ILE TRP THR SER VAL LEU ALA VAL MSE THR GLU VAL          
SEQRES   6 A  501  ILE ASN GLU ASN ASP VAL ARG ALA ASP GLN ILE ALA GLY          
SEQRES   7 A  501  ILE GLY ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP          
SEQRES   8 A  501  ASP LYS HIS THR GLY ARG PRO ILE TYR HIS ALA ILE VAL          
SEQRES   9 A  501  TRP GLN SER ARG GLN THR GLN SER ILE CYS SER GLU LEU          
SEQRES  10 A  501  LYS GLN GLN GLY TYR GLU GLN THR PHE ARG ASP LYS THR          
SEQRES  11 A  501  GLY LEU LEU LEU ASP PRO TYR PHE ALA GLY THR LYS VAL          
SEQRES  12 A  501  LYS TRP ILE LEU ASP ASN VAL GLU GLY ALA ARG GLU LYS          
SEQRES  13 A  501  ALA GLU ASN GLY ASP LEU LEU PHE GLY THR ILE ASP THR          
SEQRES  14 A  501  TRP LEU VAL TRP LYS LEU SER GLY LYS ALA ALA HIS ILE          
SEQRES  15 A  501  THR ASP TYR SER ASN ALA SER ARG THR LEU MSE PHE ASN          
SEQRES  16 A  501  ILE HIS ASP LEU GLU TRP ASP ASP GLU LEU LEU GLU LEU          
SEQRES  17 A  501  LEU THR VAL PRO LYS ASN MSE LEU PRO GLU VAL LYS ALA          
SEQRES  18 A  501  SER SER GLU VAL TYR GLY LYS THR ILE ASP TYR HIS PHE          
SEQRES  19 A  501  TYR GLY GLN GLU VAL PRO ILE ALA GLY VAL ALA GLY ASP          
SEQRES  20 A  501  GLN GLN ALA ALA LEU PHE GLY GLN ALA CYS PHE GLU ARG          
SEQRES  21 A  501  GLY ASP VAL LYS ASN THR TYR GLY THR GLY GLY PHE MSE          
SEQRES  22 A  501  LEU MSE ASN THR GLY ASP LYS ALA VAL LYS SER GLU SER          
SEQRES  23 A  501  GLY LEU LEU THR THR ILE ALA TYR GLY ILE ASP GLY LYS          
SEQRES  24 A  501  VAL ASN TYR ALA LEU GLU GLY SER ILE PHE VAL SER GLY          
SEQRES  25 A  501  SER ALA ILE GLN TRP LEU ARG ASP GLY LEU ARG MSE ILE          
SEQRES  26 A  501  ASN SER ALA PRO GLN SER GLU SER TYR ALA THR ARG VAL          
SEQRES  27 A  501  ASP SER THR GLU GLY VAL TYR VAL VAL PRO ALA PHE VAL          
SEQRES  28 A  501  GLY LEU GLY THR PRO TYR TRP ASP SER GLU ALA ARG GLY          
SEQRES  29 A  501  ALA ILE PHE GLY LEU THR ARG GLY THR GLU LYS GLU HIS          
SEQRES  30 A  501  PHE ILE ARG ALA THR LEU GLU SER LEU CYS TYR GLN THR          
SEQRES  31 A  501  ARG ASP VAL MSE GLU ALA MSE SER LYS ASP SER GLY ILE          
SEQRES  32 A  501  ASP VAL GLN SER LEU ARG VAL ASP GLY GLY ALA VAL LYS          
SEQRES  33 A  501  ASN ASN PHE ILE MSE GLN PHE GLN ALA ASP ILE VAL ASN          
SEQRES  34 A  501  THR SER VAL GLU ARG PRO GLU ILE GLN GLU THR THR ALA          
SEQRES  35 A  501  LEU GLY ALA ALA PHE LEU ALA GLY LEU ALA VAL GLY PHE          
SEQRES  36 A  501  TRP GLU SER LYS ASP ASP ILE ALA LYS ASN TRP LYS LEU          
SEQRES  37 A  501  GLU GLU LYS PHE ASP PRO LYS MSE ASP GLU GLY GLU ARG          
SEQRES  38 A  501  GLU LYS LEU TYR ARG GLY TRP LYS LYS ALA VAL GLU ALA          
SEQRES  39 A  501  THR GLN VAL PHE LYS THR GLU                                  
SEQRES   1 B  501  SER ASN ALA MSE GLU LYS TYR ILE LEU SER ILE ASP GLN          
SEQRES   2 B  501  GLY THR THR SER SER ARG ALA ILE LEU PHE ASN GLN LYS          
SEQRES   3 B  501  GLY GLU ILE ALA GLY VAL ALA GLN ARG GLU PHE LYS GLN          
SEQRES   4 B  501  TYR PHE PRO GLN SER GLY TRP VAL GLU HIS ASP ALA ASN          
SEQRES   5 B  501  GLU ILE TRP THR SER VAL LEU ALA VAL MSE THR GLU VAL          
SEQRES   6 B  501  ILE ASN GLU ASN ASP VAL ARG ALA ASP GLN ILE ALA GLY          
SEQRES   7 B  501  ILE GLY ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP          
SEQRES   8 B  501  ASP LYS HIS THR GLY ARG PRO ILE TYR HIS ALA ILE VAL          
SEQRES   9 B  501  TRP GLN SER ARG GLN THR GLN SER ILE CYS SER GLU LEU          
SEQRES  10 B  501  LYS GLN GLN GLY TYR GLU GLN THR PHE ARG ASP LYS THR          
SEQRES  11 B  501  GLY LEU LEU LEU ASP PRO TYR PHE ALA GLY THR LYS VAL          
SEQRES  12 B  501  LYS TRP ILE LEU ASP ASN VAL GLU GLY ALA ARG GLU LYS          
SEQRES  13 B  501  ALA GLU ASN GLY ASP LEU LEU PHE GLY THR ILE ASP THR          
SEQRES  14 B  501  TRP LEU VAL TRP LYS LEU SER GLY LYS ALA ALA HIS ILE          
SEQRES  15 B  501  THR ASP TYR SER ASN ALA SER ARG THR LEU MSE PHE ASN          
SEQRES  16 B  501  ILE HIS ASP LEU GLU TRP ASP ASP GLU LEU LEU GLU LEU          
SEQRES  17 B  501  LEU THR VAL PRO LYS ASN MSE LEU PRO GLU VAL LYS ALA          
SEQRES  18 B  501  SER SER GLU VAL TYR GLY LYS THR ILE ASP TYR HIS PHE          
SEQRES  19 B  501  TYR GLY GLN GLU VAL PRO ILE ALA GLY VAL ALA GLY ASP          
SEQRES  20 B  501  GLN GLN ALA ALA LEU PHE GLY GLN ALA CYS PHE GLU ARG          
SEQRES  21 B  501  GLY ASP VAL LYS ASN THR TYR GLY THR GLY GLY PHE MSE          
SEQRES  22 B  501  LEU MSE ASN THR GLY ASP LYS ALA VAL LYS SER GLU SER          
SEQRES  23 B  501  GLY LEU LEU THR THR ILE ALA TYR GLY ILE ASP GLY LYS          
SEQRES  24 B  501  VAL ASN TYR ALA LEU GLU GLY SER ILE PHE VAL SER GLY          
SEQRES  25 B  501  SER ALA ILE GLN TRP LEU ARG ASP GLY LEU ARG MSE ILE          
SEQRES  26 B  501  ASN SER ALA PRO GLN SER GLU SER TYR ALA THR ARG VAL          
SEQRES  27 B  501  ASP SER THR GLU GLY VAL TYR VAL VAL PRO ALA PHE VAL          
SEQRES  28 B  501  GLY LEU GLY THR PRO TYR TRP ASP SER GLU ALA ARG GLY          
SEQRES  29 B  501  ALA ILE PHE GLY LEU THR ARG GLY THR GLU LYS GLU HIS          
SEQRES  30 B  501  PHE ILE ARG ALA THR LEU GLU SER LEU CYS TYR GLN THR          
SEQRES  31 B  501  ARG ASP VAL MSE GLU ALA MSE SER LYS ASP SER GLY ILE          
SEQRES  32 B  501  ASP VAL GLN SER LEU ARG VAL ASP GLY GLY ALA VAL LYS          
SEQRES  33 B  501  ASN ASN PHE ILE MSE GLN PHE GLN ALA ASP ILE VAL ASN          
SEQRES  34 B  501  THR SER VAL GLU ARG PRO GLU ILE GLN GLU THR THR ALA          
SEQRES  35 B  501  LEU GLY ALA ALA PHE LEU ALA GLY LEU ALA VAL GLY PHE          
SEQRES  36 B  501  TRP GLU SER LYS ASP ASP ILE ALA LYS ASN TRP LYS LEU          
SEQRES  37 B  501  GLU GLU LYS PHE ASP PRO LYS MSE ASP GLU GLY GLU ARG          
SEQRES  38 B  501  GLU LYS LEU TYR ARG GLY TRP LYS LYS ALA VAL GLU ALA          
SEQRES  39 B  501  THR GLN VAL PHE LYS THR GLU                                  
SEQRES   1 C  501  SER ASN ALA MSE GLU LYS TYR ILE LEU SER ILE ASP GLN          
SEQRES   2 C  501  GLY THR THR SER SER ARG ALA ILE LEU PHE ASN GLN LYS          
SEQRES   3 C  501  GLY GLU ILE ALA GLY VAL ALA GLN ARG GLU PHE LYS GLN          
SEQRES   4 C  501  TYR PHE PRO GLN SER GLY TRP VAL GLU HIS ASP ALA ASN          
SEQRES   5 C  501  GLU ILE TRP THR SER VAL LEU ALA VAL MSE THR GLU VAL          
SEQRES   6 C  501  ILE ASN GLU ASN ASP VAL ARG ALA ASP GLN ILE ALA GLY          
SEQRES   7 C  501  ILE GLY ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP          
SEQRES   8 C  501  ASP LYS HIS THR GLY ARG PRO ILE TYR HIS ALA ILE VAL          
SEQRES   9 C  501  TRP GLN SER ARG GLN THR GLN SER ILE CYS SER GLU LEU          
SEQRES  10 C  501  LYS GLN GLN GLY TYR GLU GLN THR PHE ARG ASP LYS THR          
SEQRES  11 C  501  GLY LEU LEU LEU ASP PRO TYR PHE ALA GLY THR LYS VAL          
SEQRES  12 C  501  LYS TRP ILE LEU ASP ASN VAL GLU GLY ALA ARG GLU LYS          
SEQRES  13 C  501  ALA GLU ASN GLY ASP LEU LEU PHE GLY THR ILE ASP THR          
SEQRES  14 C  501  TRP LEU VAL TRP LYS LEU SER GLY LYS ALA ALA HIS ILE          
SEQRES  15 C  501  THR ASP TYR SER ASN ALA SER ARG THR LEU MSE PHE ASN          
SEQRES  16 C  501  ILE HIS ASP LEU GLU TRP ASP ASP GLU LEU LEU GLU LEU          
SEQRES  17 C  501  LEU THR VAL PRO LYS ASN MSE LEU PRO GLU VAL LYS ALA          
SEQRES  18 C  501  SER SER GLU VAL TYR GLY LYS THR ILE ASP TYR HIS PHE          
SEQRES  19 C  501  TYR GLY GLN GLU VAL PRO ILE ALA GLY VAL ALA GLY ASP          
SEQRES  20 C  501  GLN GLN ALA ALA LEU PHE GLY GLN ALA CYS PHE GLU ARG          
SEQRES  21 C  501  GLY ASP VAL LYS ASN THR TYR GLY THR GLY GLY PHE MSE          
SEQRES  22 C  501  LEU MSE ASN THR GLY ASP LYS ALA VAL LYS SER GLU SER          
SEQRES  23 C  501  GLY LEU LEU THR THR ILE ALA TYR GLY ILE ASP GLY LYS          
SEQRES  24 C  501  VAL ASN TYR ALA LEU GLU GLY SER ILE PHE VAL SER GLY          
SEQRES  25 C  501  SER ALA ILE GLN TRP LEU ARG ASP GLY LEU ARG MSE ILE          
SEQRES  26 C  501  ASN SER ALA PRO GLN SER GLU SER TYR ALA THR ARG VAL          
SEQRES  27 C  501  ASP SER THR GLU GLY VAL TYR VAL VAL PRO ALA PHE VAL          
SEQRES  28 C  501  GLY LEU GLY THR PRO TYR TRP ASP SER GLU ALA ARG GLY          
SEQRES  29 C  501  ALA ILE PHE GLY LEU THR ARG GLY THR GLU LYS GLU HIS          
SEQRES  30 C  501  PHE ILE ARG ALA THR LEU GLU SER LEU CYS TYR GLN THR          
SEQRES  31 C  501  ARG ASP VAL MSE GLU ALA MSE SER LYS ASP SER GLY ILE          
SEQRES  32 C  501  ASP VAL GLN SER LEU ARG VAL ASP GLY GLY ALA VAL LYS          
SEQRES  33 C  501  ASN ASN PHE ILE MSE GLN PHE GLN ALA ASP ILE VAL ASN          
SEQRES  34 C  501  THR SER VAL GLU ARG PRO GLU ILE GLN GLU THR THR ALA          
SEQRES  35 C  501  LEU GLY ALA ALA PHE LEU ALA GLY LEU ALA VAL GLY PHE          
SEQRES  36 C  501  TRP GLU SER LYS ASP ASP ILE ALA LYS ASN TRP LYS LEU          
SEQRES  37 C  501  GLU GLU LYS PHE ASP PRO LYS MSE ASP GLU GLY GLU ARG          
SEQRES  38 C  501  GLU LYS LEU TYR ARG GLY TRP LYS LYS ALA VAL GLU ALA          
SEQRES  39 C  501  THR GLN VAL PHE LYS THR GLU                                  
SEQRES   1 D  501  SER ASN ALA MSE GLU LYS TYR ILE LEU SER ILE ASP GLN          
SEQRES   2 D  501  GLY THR THR SER SER ARG ALA ILE LEU PHE ASN GLN LYS          
SEQRES   3 D  501  GLY GLU ILE ALA GLY VAL ALA GLN ARG GLU PHE LYS GLN          
SEQRES   4 D  501  TYR PHE PRO GLN SER GLY TRP VAL GLU HIS ASP ALA ASN          
SEQRES   5 D  501  GLU ILE TRP THR SER VAL LEU ALA VAL MSE THR GLU VAL          
SEQRES   6 D  501  ILE ASN GLU ASN ASP VAL ARG ALA ASP GLN ILE ALA GLY          
SEQRES   7 D  501  ILE GLY ILE THR ASN GLN ARG GLU THR THR VAL VAL TRP          
SEQRES   8 D  501  ASP LYS HIS THR GLY ARG PRO ILE TYR HIS ALA ILE VAL          
SEQRES   9 D  501  TRP GLN SER ARG GLN THR GLN SER ILE CYS SER GLU LEU          
SEQRES  10 D  501  LYS GLN GLN GLY TYR GLU GLN THR PHE ARG ASP LYS THR          
SEQRES  11 D  501  GLY LEU LEU LEU ASP PRO TYR PHE ALA GLY THR LYS VAL          
SEQRES  12 D  501  LYS TRP ILE LEU ASP ASN VAL GLU GLY ALA ARG GLU LYS          
SEQRES  13 D  501  ALA GLU ASN GLY ASP LEU LEU PHE GLY THR ILE ASP THR          
SEQRES  14 D  501  TRP LEU VAL TRP LYS LEU SER GLY LYS ALA ALA HIS ILE          
SEQRES  15 D  501  THR ASP TYR SER ASN ALA SER ARG THR LEU MSE PHE ASN          
SEQRES  16 D  501  ILE HIS ASP LEU GLU TRP ASP ASP GLU LEU LEU GLU LEU          
SEQRES  17 D  501  LEU THR VAL PRO LYS ASN MSE LEU PRO GLU VAL LYS ALA          
SEQRES  18 D  501  SER SER GLU VAL TYR GLY LYS THR ILE ASP TYR HIS PHE          
SEQRES  19 D  501  TYR GLY GLN GLU VAL PRO ILE ALA GLY VAL ALA GLY ASP          
SEQRES  20 D  501  GLN GLN ALA ALA LEU PHE GLY GLN ALA CYS PHE GLU ARG          
SEQRES  21 D  501  GLY ASP VAL LYS ASN THR TYR GLY THR GLY GLY PHE MSE          
SEQRES  22 D  501  LEU MSE ASN THR GLY ASP LYS ALA VAL LYS SER GLU SER          
SEQRES  23 D  501  GLY LEU LEU THR THR ILE ALA TYR GLY ILE ASP GLY LYS          
SEQRES  24 D  501  VAL ASN TYR ALA LEU GLU GLY SER ILE PHE VAL SER GLY          
SEQRES  25 D  501  SER ALA ILE GLN TRP LEU ARG ASP GLY LEU ARG MSE ILE          
SEQRES  26 D  501  ASN SER ALA PRO GLN SER GLU SER TYR ALA THR ARG VAL          
SEQRES  27 D  501  ASP SER THR GLU GLY VAL TYR VAL VAL PRO ALA PHE VAL          
SEQRES  28 D  501  GLY LEU GLY THR PRO TYR TRP ASP SER GLU ALA ARG GLY          
SEQRES  29 D  501  ALA ILE PHE GLY LEU THR ARG GLY THR GLU LYS GLU HIS          
SEQRES  30 D  501  PHE ILE ARG ALA THR LEU GLU SER LEU CYS TYR GLN THR          
SEQRES  31 D  501  ARG ASP VAL MSE GLU ALA MSE SER LYS ASP SER GLY ILE          
SEQRES  32 D  501  ASP VAL GLN SER LEU ARG VAL ASP GLY GLY ALA VAL LYS          
SEQRES  33 D  501  ASN ASN PHE ILE MSE GLN PHE GLN ALA ASP ILE VAL ASN          
SEQRES  34 D  501  THR SER VAL GLU ARG PRO GLU ILE GLN GLU THR THR ALA          
SEQRES  35 D  501  LEU GLY ALA ALA PHE LEU ALA GLY LEU ALA VAL GLY PHE          
SEQRES  36 D  501  TRP GLU SER LYS ASP ASP ILE ALA LYS ASN TRP LYS LEU          
SEQRES  37 D  501  GLU GLU LYS PHE ASP PRO LYS MSE ASP GLU GLY GLU ARG          
SEQRES  38 D  501  GLU LYS LEU TYR ARG GLY TRP LYS LYS ALA VAL GLU ALA          
SEQRES  39 D  501  THR GLN VAL PHE LYS THR GLU                                  
MODRES 3GE1 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A   59  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  190  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  212  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  270  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  272  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  321  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  391  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  394  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  418  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE A  473  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B   59  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  190  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  212  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  270  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  272  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  321  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  391  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  394  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  418  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE B  473  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C   59  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  190  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  212  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  270  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  272  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  321  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  391  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  394  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  418  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE C  473  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D   59  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  190  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  212  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  270  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  272  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  321  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  391  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  394  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  418  MET  SELENOMETHIONINE                                   
MODRES 3GE1 MSE D  473  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  59       8                                                       
HET    MSE  A 190       8                                                       
HET    MSE  A 212       8                                                       
HET    MSE  A 270       8                                                       
HET    MSE  A 272       8                                                       
HET    MSE  A 321       8                                                       
HET    MSE  A 391       8                                                       
HET    MSE  A 394       8                                                       
HET    MSE  A 418       8                                                       
HET    MSE  A 473       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  59       8                                                       
HET    MSE  B 190       8                                                       
HET    MSE  B 212       8                                                       
HET    MSE  B 270       8                                                       
HET    MSE  B 272       8                                                       
HET    MSE  B 321       8                                                       
HET    MSE  B 391       8                                                       
HET    MSE  B 394       8                                                       
HET    MSE  B 418       8                                                       
HET    MSE  B 473       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  59       8                                                       
HET    MSE  C 190       8                                                       
HET    MSE  C 212       8                                                       
HET    MSE  C 270       8                                                       
HET    MSE  C 272       8                                                       
HET    MSE  C 321       8                                                       
HET    MSE  C 391       8                                                       
HET    MSE  C 394       8                                                       
HET    MSE  C 418       8                                                       
HET    MSE  C 473       8                                                       
HET    MSE  D  59       8                                                       
HET    MSE  D 190       8                                                       
HET    MSE  D 212       8                                                       
HET    MSE  D 270       8                                                       
HET    MSE  D 272       8                                                       
HET    MSE  D 321       8                                                       
HET    MSE  D 391       8                                                       
HET    MSE  D 394       8                                                       
HET    MSE  D 418       8                                                       
HET    MSE  D 473       8                                                       
HET    ADP  A 499      27                                                       
HET    GOL  A 500       6                                                       
HET    PO4  A 501       5                                                       
HET    PO4  A 502       5                                                       
HET    PO4  A 503       5                                                       
HET     CL  A 504       1                                                       
HET    ADP  B 499      27                                                       
HET    GOL  B 500       6                                                       
HET    PO4  B 501       5                                                       
HET     CL  B 502       1                                                       
HET    ADP  C 499      27                                                       
HET    GOL  C 500       6                                                       
HET    PO4  C 501       5                                                       
HET     CL  C 502       1                                                       
HET    ADP  D 499      27                                                       
HET    GOL  D 500       6                                                       
HET    PO4  D 501       5                                                       
HET    PO4  D 502       5                                                       
HET    PO4  D 503       5                                                       
HET     CL  D 504       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    43(C5 H11 N O2 SE)                                           
FORMUL   5  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL   6  GOL    4(C3 H8 O3)                                                  
FORMUL   7  PO4    8(O4 P 3-)                                                   
FORMUL  10   CL    4(CL 1-)                                                     
FORMUL  25  HOH   *274(H2 O)                                                    
HELIX    1   1 ASP A   47  GLU A   65  1                                  19    
HELIX    2   2 ARG A   69  ASP A   71  5                                   3    
HELIX    3   3 THR A  107  GLN A  117  1                                  11    
HELIX    4   4 TYR A  119  GLY A  128  1                                  10    
HELIX    5   5 PHE A  135  VAL A  147  1                                  13    
HELIX    6   6 GLY A  149  GLU A  155  1                                   7    
HELIX    7   7 ILE A  164  SER A  173  1                                  10    
HELIX    8   8 TYR A  182  SER A  186  1                                   5    
HELIX    9   9 ASP A  199  LEU A  206  1                                   8    
HELIX   10  10 ILE A  227  PHE A  231  5                                   5    
HELIX   11  11 ASP A  244  GLN A  252  1                                   9    
HELIX   12  12 SER A  308  GLY A  318  1                                  11    
HELIX   13  13 PRO A  326  THR A  333  1                                   8    
HELIX   14  14 GLU A  371  GLY A  399  1                                  29    
HELIX   15  15 GLY A  409  LYS A  413  5                                   5    
HELIX   16  16 ASN A  414  VAL A  425  1                                  12    
HELIX   17  17 GLU A  436  VAL A  450  1                                  15    
HELIX   18  18 ASP A  457  TRP A  463  1                                   7    
HELIX   19  19 ASP A  474  PHE A  495  1                                  22    
HELIX   20  20 ASP B   47  ASN B   66  1                                  20    
HELIX   21  21 ARG B   69  ASP B   71  5                                   3    
HELIX   22  22 THR B  107  GLN B  117  1                                  11    
HELIX   23  23 TYR B  119  GLY B  128  1                                  10    
HELIX   24  24 PHE B  135  VAL B  147  1                                  13    
HELIX   25  25 GLY B  149  ASN B  156  1                                   8    
HELIX   26  26 ILE B  164  SER B  173  1                                  10    
HELIX   27  27 TYR B  182  SER B  186  1                                   5    
HELIX   28  28 ASP B  199  LEU B  206  1                                   8    
HELIX   29  29 PRO B  209  LEU B  213  5                                   5    
HELIX   30  30 ILE B  227  PHE B  231  5                                   5    
HELIX   31  31 ASP B  244  GLN B  252  1                                   9    
HELIX   32  32 GLY B  309  GLY B  318  1                                  10    
HELIX   33  33 PRO B  326  THR B  333  1                                   8    
HELIX   34  34 GLU B  371  GLY B  399  1                                  29    
HELIX   35  35 GLY B  409  LYS B  413  5                                   5    
HELIX   36  36 ASN B  414  ASN B  426  1                                  13    
HELIX   37  37 GLU B  436  VAL B  450  1                                  15    
HELIX   38  38 LYS B  456  TRP B  463  1                                   8    
HELIX   39  39 ASP B  474  PHE B  495  1                                  22    
HELIX   40  40 ASP C   47  GLU C   65  1                                  19    
HELIX   41  41 ARG C   69  ASP C   71  5                                   3    
HELIX   42  42 THR C  107  GLN C  117  1                                  11    
HELIX   43  43 TYR C  119  GLY C  128  1                                  10    
HELIX   44  44 PHE C  135  VAL C  147  1                                  13    
HELIX   45  45 GLY C  149  GLU C  155  1                                   7    
HELIX   46  46 ILE C  164  SER C  173  1                                  10    
HELIX   47  47 TYR C  182  SER C  186  1                                   5    
HELIX   48  48 ASP C  199  LEU C  206  1                                   8    
HELIX   49  49 ILE C  227  PHE C  231  5                                   5    
HELIX   50  50 ASP C  244  GLY C  251  1                                   8    
HELIX   51  51 SER C  308  GLY C  318  1                                  11    
HELIX   52  52 SER C  324  PRO C  326  5                                   3    
HELIX   53  53 GLN C  327  THR C  333  1                                   7    
HELIX   54  54 GLU C  371  GLY C  399  1                                  29    
HELIX   55  55 GLY C  409  LYS C  413  5                                   5    
HELIX   56  56 ASN C  414  ASN C  426  1                                  13    
HELIX   57  57 GLU C  436  VAL C  450  1                                  15    
HELIX   58  58 LYS C  456  TRP C  463  1                                   8    
HELIX   59  59 ASP C  474  PHE C  495  1                                  22    
HELIX   60  60 ASP D   47  ASN D   66  1                                  20    
HELIX   61  61 ARG D   69  ASP D   71  5                                   3    
HELIX   62  62 THR D  107  GLN D  117  1                                  11    
HELIX   63  63 TYR D  119  GLY D  128  1                                  10    
HELIX   64  64 PHE D  135  VAL D  147  1                                  13    
HELIX   65  65 GLY D  149  ASN D  156  1                                   8    
HELIX   66  66 ILE D  164  SER D  173  1                                  10    
HELIX   67  67 TYR D  182  SER D  186  1                                   5    
HELIX   68  68 ASP D  199  LEU D  206  1                                   8    
HELIX   69  69 ILE D  227  PHE D  231  5                                   5    
HELIX   70  70 ASP D  244  GLN D  252  1                                   9    
HELIX   71  71 GLY D  309  GLY D  318  1                                  10    
HELIX   72  72 PRO D  326  THR D  333  1                                   8    
HELIX   73  73 GLU D  371  GLY D  399  1                                  29    
HELIX   74  74 GLY D  410  LYS D  413  5                                   4    
HELIX   75  75 ASN D  414  ASN D  426  1                                  13    
HELIX   76  76 GLU D  436  VAL D  450  1                                  15    
HELIX   77  77 LYS D  456  TRP D  463  1                                   8    
HELIX   78  78 ASP D  474  PHE D  495  1                                  22    
SHEET    1   A 6 ILE A  26  GLU A  33  0                                        
SHEET    2   A 6 SER A  14  PHE A  20 -1  N  SER A  15   O  ARG A  32           
SHEET    3   A 6 TYR A   4  GLN A  10 -1  N  SER A   7   O  ILE A  18           
SHEET    4   A 6 ILE A  73  ASN A  80  1  O  GLY A  77   N  LEU A   6           
SHEET    5   A 6 PRO A 237  GLY A 243  1  O  GLY A 240   N  ILE A  78           
SHEET    6   A 6 SER A 220  LYS A 225 -1  N  GLY A 224   O  ILE A 238           
SHEET    1   B 2 GLU A  45  HIS A  46  0                                        
SHEET    2   B 2 ALA A  99  ILE A 100 -1  O  ALA A  99   N  HIS A  46           
SHEET    1   C 2 THR A  85  ASP A  89  0                                        
SHEET    2   C 2 LEU A 159  THR A 163 -1  O  GLY A 162   N  VAL A  86           
SHEET    1   D 2 ILE A 179  ASP A 181  0                                        
SHEET    2   D 2 GLU A 215  LYS A 217  1  O  GLU A 215   N  THR A 180           
SHEET    1   E 2 PHE A 191  ASN A 192  0                                        
SHEET    2   E 2 GLU A 197  TRP A 198 -1  O  GLU A 197   N  ASN A 192           
SHEET    1   F 7 LEU A 286  ILE A 293  0                                        
SHEET    2   F 7 LYS A 296  ILE A 305 -1  O  GLU A 302   N  LEU A 286           
SHEET    3   F 7 GLY A 268  ASN A 273 -1  N  MSE A 270   O  GLY A 303           
SHEET    4   F 7 ASP A 259  TYR A 264 -1  N  THR A 263   O  PHE A 269           
SHEET    5   F 7 SER A 404  ASP A 408  1  O  ASP A 408   N  TYR A 264           
SHEET    6   F 7 SER A 428  PRO A 432  1  O  GLU A 430   N  LEU A 405           
SHEET    7   F 7 LEU A 465  PHE A 469 -1  O  GLU A 466   N  ARG A 431           
SHEET    1   G 4 TYR A 342  VAL A 344  0                                        
SHEET    2   G 4 GLY A 361  LEU A 366 -1  O  ALA A 362   N  VAL A 344           
SHEET    3   G 4 GLY B 361  LEU B 366 -1  O  LEU B 366   N  GLY A 361           
SHEET    4   G 4 TYR B 342  VAL B 344 -1  N  VAL B 344   O  ALA B 362           
SHEET    1   H 6 ILE B  26  GLU B  33  0                                        
SHEET    2   H 6 SER B  14  PHE B  20 -1  N  LEU B  19   O  ALA B  27           
SHEET    3   H 6 TYR B   4  GLN B  10 -1  N  SER B   7   O  ILE B  18           
SHEET    4   H 6 ILE B  73  ASN B  80  1  O  GLY B  77   N  ILE B   8           
SHEET    5   H 6 PRO B 237  GLY B 243  1  O  GLY B 240   N  ILE B  78           
SHEET    6   H 6 GLY B 224  LYS B 225 -1  N  GLY B 224   O  ILE B 238           
SHEET    1   I 2 GLU B  45  HIS B  46  0                                        
SHEET    2   I 2 ALA B  99  ILE B 100 -1  O  ALA B  99   N  HIS B  46           
SHEET    1   J 2 THR B  85  ASP B  89  0                                        
SHEET    2   J 2 LEU B 159  THR B 163 -1  O  LEU B 160   N  TRP B  88           
SHEET    1   K 2 ILE B 179  ASP B 181  0                                        
SHEET    2   K 2 GLU B 215  LYS B 217  1  O  LYS B 217   N  THR B 180           
SHEET    1   L 2 PHE B 191  ASN B 192  0                                        
SHEET    2   L 2 GLU B 197  TRP B 198 -1  O  GLU B 197   N  ASN B 192           
SHEET    1   M 7 LEU B 286  ILE B 293  0                                        
SHEET    2   M 7 LYS B 296  ILE B 305 -1  O  GLU B 302   N  LEU B 286           
SHEET    3   M 7 GLY B 268  ASN B 273 -1  N  MSE B 270   O  GLY B 303           
SHEET    4   M 7 VAL B 260  TYR B 264 -1  N  THR B 263   O  PHE B 269           
SHEET    5   M 7 SER B 404  ASP B 408  1  O  ASP B 408   N  TYR B 264           
SHEET    6   M 7 SER B 428  PRO B 432  1  O  GLU B 430   N  LEU B 405           
SHEET    7   M 7 LEU B 465  PHE B 469 -1  O  GLU B 466   N  ARG B 431           
SHEET    1   N 6 ILE C  26  GLU C  33  0                                        
SHEET    2   N 6 SER C  14  PHE C  20 -1  N  SER C  15   O  ARG C  32           
SHEET    3   N 6 TYR C   4  GLN C  10 -1  N  SER C   7   O  ILE C  18           
SHEET    4   N 6 ILE C  73  ASN C  80  1  O  GLY C  77   N  LEU C   6           
SHEET    5   N 6 PRO C 237  GLY C 243  1  O  GLY C 240   N  ILE C  78           
SHEET    6   N 6 GLY C 224  LYS C 225 -1  N  GLY C 224   O  ILE C 238           
SHEET    1   O 2 GLU C  45  HIS C  46  0                                        
SHEET    2   O 2 ALA C  99  ILE C 100 -1  O  ALA C  99   N  HIS C  46           
SHEET    1   P 2 THR C  85  ASP C  89  0                                        
SHEET    2   P 2 LEU C 159  THR C 163 -1  O  GLY C 162   N  VAL C  86           
SHEET    1   Q 2 ILE C 179  ASP C 181  0                                        
SHEET    2   Q 2 GLU C 215  LYS C 217  1  O  GLU C 215   N  THR C 180           
SHEET    1   R 2 PHE C 191  ASN C 192  0                                        
SHEET    2   R 2 GLU C 197  TRP C 198 -1  O  GLU C 197   N  ASN C 192           
SHEET    1   S 7 LEU C 286  ILE C 293  0                                        
SHEET    2   S 7 LYS C 296  ILE C 305 -1  O  GLU C 302   N  LEU C 286           
SHEET    3   S 7 GLY C 268  ASN C 273 -1  N  MSE C 270   O  GLY C 303           
SHEET    4   S 7 ASP C 259  TYR C 264 -1  N  THR C 263   O  PHE C 269           
SHEET    5   S 7 SER C 404  ASP C 408  1  O  ASP C 408   N  TYR C 264           
SHEET    6   S 7 SER C 428  PRO C 432  1  O  GLU C 430   N  LEU C 405           
SHEET    7   S 7 LEU C 465  PHE C 469 -1  O  PHE C 469   N  VAL C 429           
SHEET    1   T 4 TYR C 342  PRO C 345  0                                        
SHEET    2   T 4 GLY C 361  LEU C 366 -1  O  ALA C 362   N  VAL C 344           
SHEET    3   T 4 GLY D 361  LEU D 366 -1  O  LEU D 366   N  GLY C 361           
SHEET    4   T 4 TYR D 342  VAL D 344 -1  N  TYR D 342   O  PHE D 364           
SHEET    1   U 6 ILE D  26  GLU D  33  0                                        
SHEET    2   U 6 SER D  14  PHE D  20 -1  N  LEU D  19   O  ALA D  27           
SHEET    3   U 6 TYR D   4  GLN D  10 -1  N  SER D   7   O  ILE D  18           
SHEET    4   U 6 ILE D  73  ASN D  80  1  O  GLY D  77   N  ILE D   8           
SHEET    5   U 6 PRO D 237  GLY D 243  1  O  GLY D 240   N  ILE D  78           
SHEET    6   U 6 GLY D 224  LYS D 225 -1  N  GLY D 224   O  ILE D 238           
SHEET    1   V 2 GLU D  45  HIS D  46  0                                        
SHEET    2   V 2 ALA D  99  ILE D 100 -1  O  ALA D  99   N  HIS D  46           
SHEET    1   W 2 THR D  85  ASP D  89  0                                        
SHEET    2   W 2 LEU D 159  THR D 163 -1  O  LEU D 160   N  TRP D  88           
SHEET    1   X 2 ILE D 179  ASP D 181  0                                        
SHEET    2   X 2 GLU D 215  LYS D 217  1  O  LYS D 217   N  THR D 180           
SHEET    1   Y 2 PHE D 191  ASN D 192  0                                        
SHEET    2   Y 2 GLU D 197  TRP D 198 -1  O  GLU D 197   N  ASN D 192           
SHEET    1   Z 7 LEU D 286  ILE D 293  0                                        
SHEET    2   Z 7 LYS D 296  ILE D 305 -1  O  GLU D 302   N  LEU D 286           
SHEET    3   Z 7 GLY D 268  ASN D 273 -1  N  GLY D 268   O  ILE D 305           
SHEET    4   Z 7 VAL D 260  TYR D 264 -1  N  THR D 263   O  PHE D 269           
SHEET    5   Z 7 SER D 404  ASP D 408  1  O  ASP D 408   N  TYR D 264           
SHEET    6   Z 7 SER D 428  PRO D 432  1  O  GLU D 430   N  LEU D 405           
SHEET    7   Z 7 LEU D 465  PHE D 469 -1  O  GLU D 466   N  ARG D 431           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.31  
LINK         C   MSE A   1                 N   GLU A   2     1555   1555  1.33  
LINK         C   VAL A  58                 N   MSE A  59     1555   1555  1.33  
LINK         C   MSE A  59                 N   THR A  60     1555   1555  1.33  
LINK         C   LEU A 189                 N   MSE A 190     1555   1555  1.33  
LINK         C   MSE A 190                 N   PHE A 191     1555   1555  1.33  
LINK         C   ASN A 211                 N   MSE A 212     1555   1555  1.33  
LINK         C   MSE A 212                 N   LEU A 213     1555   1555  1.33  
LINK         C   PHE A 269                 N   MSE A 270     1555   1555  1.33  
LINK         C   MSE A 270                 N   LEU A 271     1555   1555  1.33  
LINK         C   LEU A 271                 N   MSE A 272     1555   1555  1.33  
LINK         C   MSE A 272                 N   ASN A 273     1555   1555  1.32  
LINK         C   ARG A 320                 N   MSE A 321     1555   1555  1.33  
LINK         C   MSE A 321                 N   ILE A 322     1555   1555  1.33  
LINK         C   VAL A 390                 N   MSE A 391     1555   1555  1.33  
LINK         C   MSE A 391                 N   GLU A 392     1555   1555  1.32  
LINK         C   ALA A 393                 N   MSE A 394     1555   1555  1.33  
LINK         C   MSE A 394                 N   SER A 395     1555   1555  1.33  
LINK         C   ILE A 417                 N   MSE A 418     1555   1555  1.33  
LINK         C   MSE A 418                 N   GLN A 419     1555   1555  1.33  
LINK         C   LYS A 472                 N   MSE A 473     1555   1555  1.33  
LINK         C   MSE A 473                 N   ASP A 474     1555   1555  1.33  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.34  
LINK         C   MSE B   1                 N   GLU B   2     1555   1555  1.32  
LINK         C   VAL B  58                 N   MSE B  59     1555   1555  1.33  
LINK         C   MSE B  59                 N   THR B  60     1555   1555  1.33  
LINK         C   LEU B 189                 N   MSE B 190     1555   1555  1.33  
LINK         C   MSE B 190                 N   PHE B 191     1555   1555  1.32  
LINK         C   ASN B 211                 N   MSE B 212     1555   1555  1.33  
LINK         C   MSE B 212                 N   LEU B 213     1555   1555  1.33  
LINK         C   PHE B 269                 N   MSE B 270     1555   1555  1.32  
LINK         C   MSE B 270                 N   LEU B 271     1555   1555  1.33  
LINK         C   LEU B 271                 N   MSE B 272     1555   1555  1.33  
LINK         C   MSE B 272                 N   ASN B 273     1555   1555  1.32  
LINK         C   ARG B 320                 N   MSE B 321     1555   1555  1.32  
LINK         C   MSE B 321                 N   ILE B 322     1555   1555  1.34  
LINK         C   VAL B 390                 N   MSE B 391     1555   1555  1.33  
LINK         C   MSE B 391                 N   GLU B 392     1555   1555  1.32  
LINK         C   ALA B 393                 N   MSE B 394     1555   1555  1.33  
LINK         C   MSE B 394                 N   SER B 395     1555   1555  1.33  
LINK         C   ILE B 417                 N   MSE B 418     1555   1555  1.33  
LINK         C   MSE B 418                 N   GLN B 419     1555   1555  1.33  
LINK         C   LYS B 472                 N   MSE B 473     1555   1555  1.33  
LINK         C   MSE B 473                 N   ASP B 474     1555   1555  1.33  
LINK         C   MSE C   1                 N   GLU C   2     1555   1555  1.33  
LINK         C   VAL C  58                 N   MSE C  59     1555   1555  1.33  
LINK         C   MSE C  59                 N   THR C  60     1555   1555  1.32  
LINK         C   LEU C 189                 N   MSE C 190     1555   1555  1.33  
LINK         C   MSE C 190                 N   PHE C 191     1555   1555  1.33  
LINK         C   ASN C 211                 N   MSE C 212     1555   1555  1.33  
LINK         C   MSE C 212                 N   LEU C 213     1555   1555  1.32  
LINK         C   PHE C 269                 N   MSE C 270     1555   1555  1.33  
LINK         C   MSE C 270                 N   LEU C 271     1555   1555  1.33  
LINK         C   LEU C 271                 N   MSE C 272     1555   1555  1.34  
LINK         C   MSE C 272                 N   ASN C 273     1555   1555  1.33  
LINK         C   ARG C 320                 N   MSE C 321     1555   1555  1.33  
LINK         C   MSE C 321                 N   ILE C 322     1555   1555  1.33  
LINK         C   VAL C 390                 N   MSE C 391     1555   1555  1.33  
LINK         C   MSE C 391                 N   GLU C 392     1555   1555  1.33  
LINK         C   ALA C 393                 N   MSE C 394     1555   1555  1.33  
LINK         C   MSE C 394                 N   SER C 395     1555   1555  1.33  
LINK         C   ILE C 417                 N   MSE C 418     1555   1555  1.33  
LINK         C   MSE C 418                 N   GLN C 419     1555   1555  1.33  
LINK         C   LYS C 472                 N   MSE C 473     1555   1555  1.33  
LINK         C   MSE C 473                 N   ASP C 474     1555   1555  1.33  
LINK         C   VAL D  58                 N   MSE D  59     1555   1555  1.34  
LINK         C   MSE D  59                 N   THR D  60     1555   1555  1.33  
LINK         C   LEU D 189                 N   MSE D 190     1555   1555  1.33  
LINK         C   MSE D 190                 N   PHE D 191     1555   1555  1.33  
LINK         C   ASN D 211                 N   MSE D 212     1555   1555  1.33  
LINK         C   MSE D 212                 N   LEU D 213     1555   1555  1.33  
LINK         C   PHE D 269                 N   MSE D 270     1555   1555  1.32  
LINK         C   MSE D 270                 N   LEU D 271     1555   1555  1.33  
LINK         C   LEU D 271                 N   MSE D 272     1555   1555  1.33  
LINK         C   MSE D 272                 N   ASN D 273     1555   1555  1.32  
LINK         C   ARG D 320                 N   MSE D 321     1555   1555  1.32  
LINK         C   MSE D 321                 N   ILE D 322     1555   1555  1.33  
LINK         C   VAL D 390                 N   MSE D 391     1555   1555  1.32  
LINK         C   MSE D 391                 N   GLU D 392     1555   1555  1.32  
LINK         C   ALA D 393                 N   MSE D 394     1555   1555  1.33  
LINK         C   MSE D 394                 N   SER D 395     1555   1555  1.32  
LINK         C   ILE D 417                 N   MSE D 418     1555   1555  1.33  
LINK         C   MSE D 418                 N   GLN D 419     1555   1555  1.33  
LINK         C   LYS D 472                 N   MSE D 473     1555   1555  1.33  
LINK         C   MSE D 473                 N   ASP D 474     1555   1555  1.33  
CISPEP   1 THR A  352    PRO A  353          0        -0.24                     
CISPEP   2 THR B  352    PRO B  353          0        -0.94                     
CISPEP   3 THR C  352    PRO C  353          0        -2.20                     
CISPEP   4 THR D  352    PRO D  353          0        -0.26                     
SITE     1 AC1 17 GLY A  11  THR A  12  THR A  13  ARG A  16                    
SITE     2 AC1 17 GLY A 265  THR A 266  GLY A 309  SER A 310                    
SITE     3 AC1 17 ILE A 312  GLN A 313  ALA A 325  PRO A 326                    
SITE     4 AC1 17 GLY A 410  ASN A 414  HOH A 535  HOH A 566                    
SITE     5 AC1 17 HOH A 567                                                     
SITE     1 AC2  7 ARG A  82  GLU A  83  TRP A 102  TYR A 134                    
SITE     2 AC2  7 ASP A 244  GLN A 245  PHE A 269                               
SITE     1 AC3  3 ARG A 320  TYR B 331  LYS B 372                               
SITE     1 AC4  3 TYR A 331  LYS A 372  ARG B 320                               
SITE     1 AC5  5 LYS A 171  GLY A 174  LYS A 175  TYR A 229                    
SITE     2 AC5  5 HIS A 230                                                     
SITE     1 AC6  3 SER A 337  THR A 338  GLU A 381                               
SITE     1 AC7 17 GLY B  11  THR B  12  THR B  13  ARG B  16                    
SITE     2 AC7 17 GLY B 265  THR B 266  GLY B 309  SER B 310                    
SITE     3 AC7 17 ILE B 312  GLN B 313  ALA B 325  PRO B 326                    
SITE     4 AC7 17 GLY B 410  ALA B 411  LYS B 413  ASN B 414                    
SITE     5 AC7 17 HOH B 519                                                     
SITE     1 AC8  7 ARG B  82  GLU B  83  TRP B 102  TYR B 134                    
SITE     2 AC8  7 ASP B 244  GLN B 245  PHE B 269                               
SITE     1 AC9  6 LYS B 171  GLY B 174  LYS B 175  ILE B 227                    
SITE     2 AC9  6 TYR B 229  HIS B 230                                          
SITE     1 BC1  3 SER B 337  THR B 338  GLU B 381                               
SITE     1 BC2 16 GLY C  11  THR C  12  THR C  13  ARG C  16                    
SITE     2 BC2 16 GLY C 265  THR C 266  GLY C 309  ILE C 312                    
SITE     3 BC2 16 GLN C 313  ALA C 325  PRO C 326  GLY C 410                    
SITE     4 BC2 16 ALA C 411  ASN C 414  GOL C 500  HOH C 510                    
SITE     1 BC3  9 GLN C  81  ARG C  82  GLU C  83  TRP C 102                    
SITE     2 BC3  9 TYR C 134  ASP C 244  GLN C 245  PHE C 269                    
SITE     3 BC3  9 ADP C 499                                                     
SITE     1 BC4  7 LYS C 171  GLY C 174  LYS C 175  ILE C 227                    
SITE     2 BC4  7 TYR C 229  HIS C 230  HOH C 547                               
SITE     1 BC5  3 SER C 337  THR C 338  GLU C 381                               
SITE     1 BC6 15 GLY D  11  THR D  12  ARG D  16  GLY D 265                    
SITE     2 BC6 15 THR D 266  GLY D 309  SER D 310  ILE D 312                    
SITE     3 BC6 15 ALA D 325  PRO D 326  GLY D 410  ALA D 411                    
SITE     4 BC6 15 LYS D 413  ASN D 414  HOH D 545                               
SITE     1 BC7  8 GLN D  81  ARG D  82  GLU D  83  TRP D 102                    
SITE     2 BC7  8 TYR D 134  ASP D 244  GLN D 245  PHE D 269                    
SITE     1 BC8  3 ARG C 320  TYR D 331  LYS D 372                               
SITE     1 BC9  3 TYR C 331  LYS C 372  ARG D 320                               
SITE     1 CC1  7 LYS D 171  GLY D 174  LYS D 175  ILE D 227                    
SITE     2 CC1  7 TYR D 229  HIS D 230  HOH D 506                               
SITE     1 CC2  4 SER D 337  THR D 338  ARG D 377  GLU D 381                    
CRYST1   63.412  193.651   91.844  90.00 106.01  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015770  0.000000  0.004525        0.00000                         
SCALE2      0.000000  0.005164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011327        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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