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LongText Report for: 2JBW-pdb

Name Class
2JBW-pdb
HEADER    HYDROLASE                               14-DEC-06   2JBW              
TITLE     CRYSTAL STRUCTURE OF THE 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE             
TITLE    2 HYDROLASE.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE;                
COMPND   3 SYNONYM: DHPON-HYDROLASE;                                            
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 EC: 3.7.1.-;                                                         
COMPND   6 FRAGMENT: RESIDUES 1-365;                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   3 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   4 EXPRESSION_SYSTEM_PLASMID: PH6EX3.DHPONH;                            
SOURCE   5 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS                     
KEYWDS    ALPHA/BETA HYDROLASE, META-CLEAVAGE PATHWAY,                          
KEYWDS   2 RETRO- FRIEDEL-CRAFTS ACYLATION,                                     
KEYWDS   3 NICOTINE DEGRADATION, HYPOTHETICAL PROTEIN,                          
KEYWDS   4 PLASMID, CATALYTIC TRIAD, C-C BOND CLEAVAGE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.SCHLEBERGER,P.SACHELARU,R.BRANDSCH,G.E.SCHULZ                       
REVDAT   1   04-JAN-07 2JBW    0                                                
JRNL        AUTH   C.SCHLEBERGER,P.SACHELARU,R.BRANDSCH,G.E.SCHULZ              
JRNL        TITL   STRUCTURE AND ACTION OF A C-C BOND CLEAVING                  
JRNL        TITL 2 ALPHABETA-HYDROLASE INVOLVED IN NICOTINE                     
JRNL        TITL 3 DEGRADATION                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.1  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.87                          
REMARK   3   NUMBER OF REFLECTIONS             : 86393                          
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) : 0.18303                         
REMARK   3   R VALUE            (WORKING SET) : 0.18140                         
REMARK   3   FREE R VALUE                     : 0.23791                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2580                            
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) : 2.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.154                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6256                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.208                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 186                          
REMARK   3   BIN FREE R VALUE                    : 0.265                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10898                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 348                                     
REMARK   3   SOLVENT ATOMS            : 964                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.2                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.893                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.53                                                
REMARK   3    B22 (A**2) : 0.18                                                 
REMARK   3    B33 (A**2) : -0.40                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -1.63                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.190         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.136         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.260         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES    COUNT    RMS    WEIGHT          
REMARK   3   BOND LENGTHS REFINED           (A): 11517 ; 0.022 ; 0.022          
REMARK   3   BOND LENGTHS OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   BOND ANGLES REFINED      (DEGREES): 15652 ; 1.527 ; 1.969          
REMARK   3   BOND ANGLES OTHERS       (DEGREES):  NULL ;  NULL ;  NULL          
REMARK   3   TORSION ANGLES, PERIOD 1 (DEGREES):  1425 ; 5.919 ; 5.000          
REMARK   3   TORSION ANGLES, PERIOD 2 (DEGREES):   525 ;33.240 ;24.133          
REMARK   3   TORSION ANGLES, PERIOD 3 (DEGREES):  1927 ;16.836 ;15.000          
REMARK   3   TORSION ANGLES, PERIOD 4 (DEGREES):    72 ;17.916 ;15.000          
REMARK   3   CHIRAL-CENTER RESTRAINTS    (A**3):  1699 ; 0.111 ; 0.200          
REMARK   3   GENERAL PLANES REFINED         (A):  8820 ; 0.006 ; 0.020          
REMARK   3   GENERAL PLANES OTHERS          (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED CONTACTS REFINED    (A):  5855 ; 0.214 ; 0.200          
REMARK   3   NON-BONDED CONTACTS OTHERS     (A):  NULL ;  NULL ;  NULL          
REMARK   3   NON-BONDED TORSION REFINED     (A):  7767 ; 0.303 ; 0.200          
REMARK   3   NON-BONDED TORSION OTHERS      (A):  NULL ;  NULL ;  NULL          
REMARK   3   H-BOND (X...Y) REFINED         (A):  1068 ; 0.164 ; 0.200          
REMARK   3   SYMMETRY VDW REFINED           (A):    73 ; 0.182 ; 0.200          
REMARK   3   SYMMETRY VDW OTHERS            (A):  NULL ;  NULL ;  NULL          
REMARK   3   SYMMETRY H-BOND REFINED        (A):    17 ; 0.160 ; 0.200          
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT  RMS   WEIGHT            
REMARK   3   MAIN-CHAIN BOND REFINED   (A**2):  7116 ; 0.754 ; 1.500            
REMARK   3   MAIN-CHAIN ANGLE REFINED  (A**2): 11417 ; 1.333 ; 2.000            
REMARK   3   SIDE-CHAIN BOND REFINED   (A**2):  4637 ; 2.405 ; 3.000            
REMARK   3   SIDE-CHAIN ANGLE REFINED  (A**2):  4235 ; 3.328 ; 4.500            
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF NCS GROUPS : 2                                           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   1                                
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    139       A     384      5                      
REMARK   3           1     B    139       B     384      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    904 ;  0.16 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    850 ;  0.46 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    904 ;  1.40 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    850 ;  2.12 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               :   2                                
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP :    1                            
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     40       A     111      5                      
REMARK   3           1     B     40       B     111      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    288 ;  0.10 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    302 ;  0.45 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    288 ;  0.73 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    302 ;  1.44 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 30                                         
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     8        A    28                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.7520  27.2414 132.3267              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0502 T22:   0.0065                                     
REMARK   3      T33:  -0.1287 T12:  -0.0415                                     
REMARK   3      T13:   0.0084 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0628 L22:   3.7311                                     
REMARK   3      L33:   4.3453 L12:  -0.3222                                     
REMARK   3      L13:   2.6548 L23:   1.9958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0268 S12:   0.0910 S13:  -0.0464                       
REMARK   3      S21:  -0.2393 S22:  -0.0620 S23:  -0.5312                       
REMARK   3      S31:  -0.2023 S32:   0.1388 S33:   0.0352                       
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    29        A    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.2240  33.6607 125.7500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0528 T22:   0.0885                                     
REMARK   3      T33:  -0.1573 T12:  -0.0485                                     
REMARK   3      T13:  -0.0260 T23:   0.0539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.3292 L22:  19.7423                                     
REMARK   3      L33:   7.8610 L12:   4.7310                                     
REMARK   3      L13:  -3.6790 L23:  16.4392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7001 S12:   0.0366 S13:   0.7685                       
REMARK   3      S21:   0.2533 S22:   0.7954 S23:  -0.6688                       
REMARK   3      S31:   0.5226 S32:   0.8039 S33:  -0.0953                       
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    36        A    60                          
REMARK   3    ORIGIN FOR THE GROUP (A):  79.2784  41.4957 133.7179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1700 T22:  -0.1038                                     
REMARK   3      T33:  -0.1860 T12:   0.0177                                     
REMARK   3      T13:  -0.1121 T23:  -0.0368                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.3801 L22:   2.9060                                     
REMARK   3      L33:   4.8527 L12:   0.3647                                     
REMARK   3      L13:  -1.4259 L23:   0.1500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0945 S12:   0.4224 S13:   1.2259                       
REMARK   3      S21:  -0.2057 S22:  -0.0803 S23:  -0.4096                       
REMARK   3      S31:  -1.1259 S32:  -0.0102 S33:   0.1748                       
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    61        A    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.9604  36.0452 139.5102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1386 T22:   0.0615                                     
REMARK   3      T33:  -0.1598 T12:   0.0908                                     
REMARK   3      T13:  -0.0895 T23:  -0.1463                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7295 L22:   1.2063                                     
REMARK   3      L33:   2.9805 L12:  -1.2168                                     
REMARK   3      L13:   3.6017 L23:  -1.1064                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1776 S12:  -0.5142 S13:   0.1282                       
REMARK   3      S21:   0.0620 S22:  -0.2648 S23:  -0.1117                       
REMARK   3      S31:  -0.4284 S32:  -0.4634 S33:   0.0872                       
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    90        A   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.6863  39.9627 146.0872              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1222 T22:  -0.0627                                     
REMARK   3      T33:  -0.1088 T12:  -0.0284                                     
REMARK   3      T13:  -0.1114 T23:  -0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.1142 L22:   1.1501                                     
REMARK   3      L33:   9.7074 L12:  -2.0592                                     
REMARK   3      L13:  -1.3794 L23:  -0.4021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:  -0.1882 S13:   1.6104                       
REMARK   3      S21:  -0.1018 S22:  -0.1291 S23:  -0.3698                       
REMARK   3      S31:  -1.1102 S32:   0.5859 S33:   0.2170                       
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   101        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  69.6351  33.6623 152.5738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0797 T22:   0.2098                                     
REMARK   3      T33:  -0.2291 T12:   0.0927                                     
REMARK   3      T13:   0.0235 T23:  -0.1734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2272 L22:   2.7884                                     
REMARK   3      L33:   9.6638 L12:  -0.2232                                     
REMARK   3      L13:   1.3444 L23:  -0.6170                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0246 S12:  -0.6747 S13:   0.1841                       
REMARK   3      S21:   0.4501 S22:  -0.2518 S23:   0.2771                       
REMARK   3      S31:  -0.8848 S32:  -1.3492 S33:   0.2764                       
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   123        A   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2872  24.5040 152.6217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0569 T22:   0.3390                                     
REMARK   3      T33:  -0.2601 T12:  -0.1013                                     
REMARK   3      T13:   0.0899 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5496 L22:   3.3327                                     
REMARK   3      L33:   4.0338 L12:  -1.4441                                     
REMARK   3      L13:   1.1086 L23:   1.2403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0530 S12:  -0.4549 S13:   0.0092                       
REMARK   3      S21:   0.3697 S22:  -0.1128 S23:   0.3949                       
REMARK   3      S31:   0.2657 S32:  -1.0078 S33:   0.1658                       
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 :   A   150        A   176                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.8052  23.9128 147.4054              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0387 T22:   0.1983                                     
REMARK   3      T33:  -0.2278 T12:  -0.0134                                     
REMARK   3      T13:   0.0550 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0923 L22:   3.4720                                     
REMARK   3      L33:   3.9869 L12:   2.3216                                     
REMARK   3      L13:   2.2820 L23:   2.0980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0893 S12:  -0.3601 S13:  -0.0571                       
REMARK   3      S21:   0.2275 S22:  -0.0627 S23:   0.2354                       
REMARK   3      S31:   0.0513 S32:  -0.6867 S33:   0.1520                       
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 :   A   177        A   208                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1445  25.0766 160.5712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0736 T22:   0.3617                                     
REMARK   3      T33:  -0.3438 T12:  -0.0442                                     
REMARK   3      T13:   0.0481 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0498 L22:   1.3484                                     
REMARK   3      L33:   1.5240 L12:  -0.9013                                     
REMARK   3      L13:  -0.1420 L23:   1.6469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1923 S12:  -0.6439 S13:  -0.0084                       
REMARK   3      S21:   0.6948 S22:  -0.0488 S23:   0.0418                       
REMARK   3      S31:   0.1263 S32:  -0.6001 S33:   0.2411                       
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 :   A   209        A   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):  78.2425  14.9043 155.9425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1115 T22:   0.1631                                     
REMARK   3      T33:  -0.2928 T12:  -0.1703                                     
REMARK   3      T13:   0.0204 T23:   0.1235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7870 L22:   1.1727                                     
REMARK   3      L33:   1.9946 L12:   1.4285                                     
REMARK   3      L13:  -1.0557 L23:   2.6321                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0858 S12:  -0.7077 S13:  -0.3401                       
REMARK   3      S21:   0.5390 S22:  -0.0097 S23:  -0.1500                       
REMARK   3      S31:   0.9164 S32:  -0.6536 S33:   0.0955                       
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 :   A   238        A   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  96.4881  22.5207 149.2701              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0400 T22:  -0.0551                                     
REMARK   3      T33:  -0.0890 T12:   0.0174                                     
REMARK   3      T13:  -0.1188 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7040 L22:   2.4818                                     
REMARK   3      L33:   3.9016 L12:   0.5265                                     
REMARK   3      L13:   0.7170 L23:   0.6221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:  -0.1994 S13:  -0.0450                       
REMARK   3      S21:   0.3256 S22:   0.1996 S23:  -0.6722                       
REMARK   3      S31:   0.1344 S32:   0.4081 S33:  -0.1637                       
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 :   A   273        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.8449  11.1438 151.8790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:  -0.0495                                     
REMARK   3      T33:  -0.2133 T12:   0.0294                                     
REMARK   3      T13:  -0.0838 T23:   0.0831                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9063 L22:   2.5805                                     
REMARK   3      L33:   4.9452 L12:  -0.0670                                     
REMARK   3      L13:   2.3491 L23:   1.0520                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2131 S12:  -0.3664 S13:  -0.3045                       
REMARK   3      S21:   0.5735 S22:   0.1293 S23:  -0.3164                       
REMARK   3      S31:   0.9062 S32:   0.0127 S33:  -0.3423                       
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 :   A   307        A   336                          
REMARK   3    ORIGIN FOR THE GROUP (A):  83.9705   7.0061 144.5282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1394 T22:  -0.1078                                     
REMARK   3      T33:  -0.1553 T12:  -0.0781                                     
REMARK   3      T13:  -0.0561 T23:   0.0975                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5908 L22:   3.3322                                     
REMARK   3      L33:   5.5298 L12:  -1.4705                                     
REMARK   3      L13:   2.3935 L23:  -2.1275                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3110 S12:  -0.2742 S13:  -0.6396                       
REMARK   3      S21:   0.3372 S22:  -0.0814 S23:  -0.1232                       
REMARK   3      S31:   1.0084 S32:  -0.2103 S33:  -0.2297                       
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 :   A   337        A   350                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.9594  10.5045 143.4769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0144 T22:   0.0492                                     
REMARK   3      T33:  -0.1780 T12:  -0.1931                                     
REMARK   3      T13:   0.0570 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6956 L22:   5.0748                                     
REMARK   3      L33:  11.2777 L12:   4.8333                                     
REMARK   3      L13:  -3.2579 L23:  -4.2781                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2279 S12:  -0.1155 S13:  -0.7705                       
REMARK   3      S21:   0.3597 S22:  -0.2156 S23:   0.0502                       
REMARK   3      S31:   0.8865 S32:  -0.6730 S33:  -0.0123                       
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 :   A   351        A   366                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.4760   0.2110 144.9677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2516 T22:  -0.3287                                     
REMARK   3      T33:  -0.1036 T12:  -0.3034                                     
REMARK   3      T13:  -0.1485 T23:   0.0828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  51.2325 L22:  14.5749                                     
REMARK   3      L33:   9.0092 L12: -18.6466                                     
REMARK   3      L13: -17.6795 L23:   5.8692                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0619 S12:  -1.9183 S13:  -2.3055                       
REMARK   3      S21:   0.6002 S22:   0.7554 S23:   0.3855                       
REMARK   3      S31:   1.2957 S32:   0.0936 S33:   0.3066                       
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 :   B     6        B    28                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.5553  22.7097 117.3385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1134 T22:   0.0582                                     
REMARK   3      T33:  -0.0838 T12:   0.0709                                     
REMARK   3      T13:   0.0269 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1838 L22:   2.0808                                     
REMARK   3      L33:   5.3872 L12:   1.8041                                     
REMARK   3      L13:   5.0378 L23:   0.1324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0111 S12:   0.3190 S13:   0.1072                       
REMARK   3      S21:  -0.0415 S22:  -0.0686 S23:  -0.1627                       
REMARK   3      S31:  -0.0051 S32:   0.6141 S33:   0.0575                       
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 :   B    29        B    55                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.8648  10.3788 119.0301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0110 T22:  -0.0228                                     
REMARK   3      T33:  -0.0694 T12:   0.0670                                     
REMARK   3      T13:  -0.0513 T23:  -0.0969                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5428 L22:   2.9476                                     
REMARK   3      L33:   3.8200 L12:   2.6637                                     
REMARK   3      L13:   0.6896 L23:   0.6571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:   0.1782 S13:  -0.1783                       
REMARK   3      S21:  -0.3058 S22:   0.1085 S23:  -0.1717                       
REMARK   3      S31:   0.9392 S32:   0.4693 S33:  -0.1223                       
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 :   B    56        B    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.7786   4.8101 135.9422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0186 T22:   0.0788                                     
REMARK   3      T33:  -0.1412 T12:  -0.2800                                     
REMARK   3      T13:   0.0280 T23:   0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -3.2840 L22:  20.6794                                     
REMARK   3      L33:  32.9756 L12:  11.1727                                     
REMARK   3      L13:  -1.7515 L23:   4.1487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5785 S12:  -0.2887 S13:  -0.3047                       
REMARK   3      S21:  -0.1221 S22:   0.3293 S23:   1.0834                       
REMARK   3      S31:   2.0331 S32:  -0.6500 S33:  -0.9078                       
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 :   B    67        B    89                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.5750  13.6844 117.4541              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0179 T22:   0.0119                                     
REMARK   3      T33:  -0.0950 T12:  -0.0774                                     
REMARK   3      T13:  -0.0301 T23:  -0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8039 L22:   1.3206                                     
REMARK   3      L33:  12.7344 L12:   0.6360                                     
REMARK   3      L13:   0.2805 L23:  -2.9766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2046 S12:  -0.0139 S13:  -0.2095                       
REMARK   3      S21:  -0.1161 S22:  -0.1972 S23:   0.0811                       
REMARK   3      S31:   0.6344 S32:  -0.4818 S33:  -0.0074                       
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 :   B    90        B   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.2834   9.1374 117.6898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0626 T22:   0.0616                                     
REMARK   3      T33:  -0.1054 T12:  -0.1850                                     
REMARK   3      T13:  -0.0532 T23:  -0.0441                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9259 L22:   4.2988                                     
REMARK   3      L33:  16.3563 L12:   0.1586                                     
REMARK   3      L13:  -2.9327 L23:   0.9388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1301 S12:  -0.0512 S13:  -0.6408                       
REMARK   3      S21:   0.1497 S22:  -0.1785 S23:  -0.0039                       
REMARK   3      S31:   1.7634 S32:  -0.8002 S33:   0.0484                       
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 :   B   109        B   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.5768  14.9102 122.9940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3766 T22:   0.6868                                     
REMARK   3      T33:  -0.2178 T12:  -0.1740                                     
REMARK   3      T13:   0.1751 T23:  -0.0871                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.3874 L22:   5.3886                                     
REMARK   3      L33:  31.9881 L12:  -1.5935                                     
REMARK   3      L13:  12.3867 L23:  -2.9248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1937 S12:  -0.9989 S13:  -0.9023                       
REMARK   3      S21:   0.2045 S22:  -0.1967 S23:   0.4905                       
REMARK   3      S31:   1.1346 S32:  -2.2785 S33:   0.0030                       
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 :   B   121        B   137                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.5459  19.1857 123.4101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3935 T22:   0.6453                                     
REMARK   3      T33:  -0.1324 T12:  -0.1080                                     
REMARK   3      T13:   0.0818 T23:  -0.1066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8604 L22:   8.1453                                     
REMARK   3      L33:  15.2395 L12:   0.6847                                     
REMARK   3      L13:  -0.5923 L23:   4.6258                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0362 S12:  -0.7206 S13:  -0.0132                       
REMARK   3      S21:   0.4761 S22:  -0.5085 S23:   0.8129                       
REMARK   3      S31:   0.5342 S32:  -1.7400 S33:   0.4722                       
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 :   B   138        B   158                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.0178  23.7433 120.5573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1940 T22:   0.3236                                     
REMARK   3      T33:  -0.1582 T12:   0.0197                                     
REMARK   3      T13:   0.0155 T23:  -0.1056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1594 L22:   2.1886                                     
REMARK   3      L33:   4.4517 L12:  -1.0237                                     
REMARK   3      L13:  -0.1097 L23:  -0.0103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0570 S12:  -0.3640 S13:  -0.1104                       
REMARK   3      S21:   0.2031 S22:  -0.3800 S23:   0.0767                       
REMARK   3      S31:  -0.0546 S32:  -0.8460 S33:   0.3230                       
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 :   B   159        B   178                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3877  23.5874 121.9382              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1931 T22:   0.3088                                     
REMARK   3      T33:  -0.1724 T12:   0.0027                                     
REMARK   3      T13:   0.0799 T23:  -0.0609                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8281 L22:   3.0476                                     
REMARK   3      L33:   7.1457 L12:  -1.3070                                     
REMARK   3      L13:   1.1277 L23:   3.1592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0188 S12:  -0.5260 S13:  -0.1760                       
REMARK   3      S21:   0.2297 S22:  -0.2582 S23:   0.4669                       
REMARK   3      S31:   0.1641 S32:  -1.1430 S33:   0.2770                       
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 :   B   179        B   203                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.2497  21.3882 110.3458              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2808 T22:   0.4832                                     
REMARK   3      T33:  -0.0997 T12:   0.0373                                     
REMARK   3      T13:  -0.0627 T23:  -0.1513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1618 L22:   2.7795                                     
REMARK   3      L33:   7.1906 L12:  -0.5352                                     
REMARK   3      L13:  -1.3440 L23:   0.6611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1275 S12:  -0.5111 S13:  -0.2617                       
REMARK   3      S21:  -0.1405 S22:  -0.1732 S23:   0.5935                       
REMARK   3      S31:   0.3219 S32:  -1.5172 S33:   0.0457                       
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 :   B   204        B   221                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9321  29.5449 120.3021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1985 T22:   0.4814                                     
REMARK   3      T33:  -0.1625 T12:   0.1809                                     
REMARK   3      T13:   0.0223 T23:  -0.1587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.9716 L22:   3.0813                                     
REMARK   3      L33:   5.1189 L12:   0.8726                                     
REMARK   3      L13:   0.1667 L23:  -1.0296                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2424 S12:  -0.4858 S13:  -0.1248                       
REMARK   3      S21:   0.2474 S22:  -0.2658 S23:   0.5582                       
REMARK   3      S31:  -0.1760 S32:  -0.9715 S33:   0.0234                       
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 :   B   222        B   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.9937  33.9200 111.8985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0865 T22:   0.2395                                     
REMARK   3      T33:  -0.1422 T12:   0.2850                                     
REMARK   3      T13:  -0.0608 T23:  -0.2509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4774 L22:   1.0520                                     
REMARK   3      L33:   3.0610 L12:  -0.5446                                     
REMARK   3      L13:   0.5644 L23:  -1.8486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0018 S12:  -0.5102 S13:   0.1979                       
REMARK   3      S21:  -0.1122 S22:  -0.0401 S23:   0.3029                       
REMARK   3      S31:  -0.4701 S32:  -0.8709 S33:   0.0383                       
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 :   B   246        B   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.4111  32.5120 103.3612              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0439 T22:   0.0131                                     
REMARK   3      T33:  -0.1456 T12:   0.1507                                     
REMARK   3      T13:  -0.0554 T23:  -0.0993                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4686 L22:   1.4666                                     
REMARK   3      L33:   3.7584 L12:  -0.0602                                     
REMARK   3      L13:   1.3025 L23:   1.0861                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2334 S12:   0.0494 S13:   0.1335                       
REMARK   3      S21:  -0.1527 S22:  -0.0225 S23:   0.0692                       
REMARK   3      S31:  -0.5602 S32:  -0.0953 S33:   0.2559                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :    29                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   310        B   351                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.2089  39.4149 120.3773              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0895 T22:   0.1323                                     
REMARK   3      T33:  -0.1103 T12:   0.2654                                     
REMARK   3      T13:  -0.0851 T23:  -0.2130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3197 L22:   0.5227                                     
REMARK   3      L33:   3.4226 L12:   0.4173                                     
REMARK   3      L13:   1.5565 L23:  -1.4950                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4074 S12:  -0.4328 S13:   0.4879                       
REMARK   3      S21:   0.1674 S22:  -0.0238 S23:  -0.1422                       
REMARK   3      S31:  -1.0468 S32:  -0.4799 S33:   0.4313                       
REMARK   3                                                                      
REMARK   3   TLS GROUP :    30                                                  
REMARK   3    NUMBER OF COMPONENTS GROUP :    1                                 
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   352        B   365                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.1130  47.7920 120.9040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3768 T22:  -0.0434                                     
REMARK   3      T33:  -0.2318 T12:   0.3995                                     
REMARK   3      T13:  -0.1536 T23:  -0.3919                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  44.0339 L22:   8.9936                                     
REMARK   3      L33:  33.6313 L12:  13.3557                                     
REMARK   3      L13: -35.8968 L23: -14.5303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5950 S12:  -0.0238 S13:   2.2368                       
REMARK   3      S21:   0.2575 S22:   0.6834 S23:   0.8967                       
REMARK   3      S31:  -0.8680 S32:  -1.7511 S33:  -0.0885                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2JBW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 14-DEC-2006.                
REMARK 100 THE EBI ID CODE IS EBI-30821.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY BEAMLINE PX-BL14.1           
REMARK 200  BEAMLINE                       : PX-BL14.1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 172409                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 1.9                                
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD, SHARP                                         
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEINSOLUTION: 50 MM TRIS-HCL          
REMARK 280  PH 7.4, 200 MM NACL, 0.5 M TCEP RESERVOIR: 35% PEG 10000,           
REMARK 280  O.1 M TRIS-HCL PH 8.8 HANGING DROP, MIXED 1:1,                      
REMARK 280  MICROSEEDING                                                        
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       28.51000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 295                                                                      
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY                                        
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW             
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS              
REMARK 295 IN THIS ENTRY.  APPLYING THE APPROPRIATE MTRIX                       
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD               
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.              
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH             
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.                                   
REMARK 295                                                                      
REMARK 295               APPLIED TO          TRANSFORMED TO                     
REMARK 295   TRANSFORM CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD           
REMARK 295    M  1       B    8 .. 365         A    8 .. 365     0.342          
REMARK 295    M  2       D   15 .. 365         C   15 .. 365     0.429          
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   4 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: DIMERIC                         
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     MSE A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLN A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     MSE A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     PRO A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     HIS A   368                                                      
REMARK 465     HIS A   369                                                      
REMARK 465     HIS A   370                                                      
REMARK 465     HIS A   371                                                      
REMARK 465     HIS A   372                                                      
REMARK 465     ALA B   -13                                                      
REMARK 465     SER B   -12                                                      
REMARK 465     MSE B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLN B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     MSE B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     HIS B   367                                                      
REMARK 465     HIS B   368                                                      
REMARK 465     HIS B   369                                                      
REMARK 465     HIS B   370                                                      
REMARK 465     HIS B   371                                                      
REMARK 465     HIS B   372                                                      
REMARK 465     ALA C   -13                                                      
REMARK 465     SER C   -12                                                      
REMARK 465     MSE C   -11                                                      
REMARK 465     THR C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     GLN C    -7                                                      
REMARK 465     GLN C    -6                                                      
REMARK 465     MSE C    -5                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     ASP C    -2                                                      
REMARK 465     PRO C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     THR C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     VAL C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     GLU C    12                                                      
REMARK 465     MSE C    13                                                      
REMARK 465     ASP C    14                                                      
REMARK 465     HIS C   367                                                      
REMARK 465     HIS C   368                                                      
REMARK 465     HIS C   369                                                      
REMARK 465     HIS C   370                                                      
REMARK 465     HIS C   371                                                      
REMARK 465     HIS C   372                                                      
REMARK 465     ALA D   -13                                                      
REMARK 465     SER D   -12                                                      
REMARK 465     MSE D   -11                                                      
REMARK 465     THR D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     GLN D    -7                                                      
REMARK 465     GLN D    -6                                                      
REMARK 465     MSE D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     ASP D    -2                                                      
REMARK 465     PRO D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     VAL D     3                                                      
REMARK 465     THR D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     HIS D   367                                                      
REMARK 465     HIS D   368                                                      
REMARK 465     HIS D   369                                                      
REMARK 465     HIS D   370                                                      
REMARK 465     HIS D   371                                                      
REMARK 465     HIS D   372                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 367    CA   C    O    CB   CG   ND1  CD2  CE1  NE2         
REMARK 470     GLN B   6    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 355    CG   CD   CE   NZ                                   
REMARK 470     GLU B 366    CA   C    O    CB   CG   CD   OE1  OE2              
REMARK 470     GLU C 366    CA   C    O    CB   CG   CD   OE1  OE2              
REMARK 470     GLU D 366    CA   C    O    CB   CG   CD   OE1  OE2              
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA B 352   N   -  CA  -  C   ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LYS B 354   CB  -  CA  -  C   ANGL. DEV. = -10.6 DEGREES          
REMARK 500    LYS B 354   CG  -  CD  -  CE  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    LEU C 268   CA  -  CB  -  CG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    LEU D  48   CA  -  CB  -  CG  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    LEU D  72   CA  -  CB  -  CG  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    LEU D  72   CB  -  CG  -  CD1 ANGL. DEV. =  11.5 DEGREES          
REMARK 500    LEU D  85   CB  -  CG  -  CD1 ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG D  97   CG  -  CD  -  NE  ANGL. DEV. = -10.5 DEGREES          
REMARK 500    LYS D 260   CD  -  CE  -  NZ  ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LEU D 321   CA  -  CB  -  CG  ANGL. DEV. =   9.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL                
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 500 NUMBER; I=INSERTION CODE).                                           
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)           
REMARK 500                                                                      
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991                               
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP A 198  CB     ASP A 198  CG       0.308                       
REMARK 500    GLU A 204  CD     GLU A 204  OE2      0.186                       
REMARK 500    ASP A 209  CB     ASP A 209  CG       0.202                       
REMARK 500    ASP A 209  CG     ASP A 209  OD2      0.169                       
REMARK 500    PRO A 231  C      PRO A 231  O        0.153                       
REMARK 500    LEU A 233  C      LEU A 233  O        0.201                       
REMARK 500    LEU A 233  C      ALA A 234  N        0.154                       
REMARK 500    GLU B 114  CD     GLU B 114  OE2      0.158                       
REMARK 500    LYS B 202  CE     LYS B 202  NZ       0.167                       
REMARK 500    ASN B 208  CG     ASN B 208  ND2      0.156                       
REMARK 500    ALA B 234  CA     ALA B 234  CB       0.160                       
REMARK 500    VAL B 351  C      VAL B 351  O        0.220                       
REMARK 500    ALA B 352  C      ALA B 352  O        0.157                       
REMARK 500    GLY B 353  N      GLY B 353  CA       0.355                       
REMARK 500    LYS B 354  C      LYS B 354  O        0.214                       
REMARK 500    LYS B 354  CD     LYS B 354  CE       0.927                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CE   MSE A    13     O    HOH Z    17               2.11           
REMARK 500   OE2  GLU C    53     NZ   LYS C   104               2.13           
REMARK 500   CD2  HIS C   138     O    HOH X   168               2.09           
REMARK 500   OD1  ASP D    11     O    HOH W     8               2.17           
REMARK 500   NE2  GLN D    54     O    HOH W    70               1.98           
REMARK 500   CD2  HIS D   138     O    HOH W   188               2.19           
REMARK 500   O    HOH W    50     O    HOH W   120               2.15           
REMARK 500   O    HOH Z     6     O    HOH Z    10               2.09           
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO                 
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY            
REMARK 525 ASSOCIATED WITH:                                                     
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN                                       
REMARK 525     A              Z                                                 
REMARK 525     B              Y                                                 
REMARK 525     C              X                                                 
REMARK 525     D              W                                                 
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM NA    NA A1368  THE COORDINATION ANGLES ARE:          
REMARK 600  1 LEU    203A  O                                                    
REMARK 600  2 ILE    206A  O        104.4                                       
REMARK 600  3 ASN    208A  OD1      164.4  88.4                                 
REMARK 600                             1     2                                  
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM NA    NA B1367  THE COORDINATION ANGLES ARE:          
REMARK 600  1 LEU    203B  O                                                    
REMARK 600  2 ASN    208B  OD1      162.9                                       
REMARK 600                             1                                        
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM NA    NA C1367  THE COORDINATION ANGLES ARE:          
REMARK 600  1 LEU    203C  O                                                    
REMARK 600  2 HOH    169X  O         96.8                                       
REMARK 600  3 LEU    200C  O         91.8 160.9                                 
REMARK 600  4 ILE    206C  O         98.6  82.8 112.8                           
REMARK 600                             1     2     3                            
REMARK 600                                                                      
REMARK 600 FOR METAL ATOM NA    NA D1367  THE COORDINATION ANGLES ARE:          
REMARK 600  1 ILE    206D  O                                                    
REMARK 600  2 ASN    208D  OD1       90.0                                       
REMARK 600  3 LEU    203D  O         95.5 171.3                                 
REMARK 600                             1     2                                  
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: TRI                                                 
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIADS                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN A                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN B                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN C                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN D                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN D                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN B                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN A                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN C                        
DBREF  2JBW A  -13     0  PDB    2JBW     2JBW           -13      0             
DBREF  2JBW A    1   365  UNP    Q93NG6   Q93NG6_ARTNI     1    365             
DBREF  2JBW A  366   372  PDB    2JBW     2JBW           366    372             
DBREF  2JBW B  -13     0  PDB    2JBW     2JBW           -13      0             
DBREF  2JBW B    1   365  UNP    Q93NG6   Q93NG6_ARTNI     1    365             
DBREF  2JBW B  366   372  PDB    2JBW     2JBW           366    372             
DBREF  2JBW C  -13     0  PDB    2JBW     2JBW           -13      0             
DBREF  2JBW C    1   365  UNP    Q93NG6   Q93NG6_ARTNI     1    365             
DBREF  2JBW C  366   372  PDB    2JBW     2JBW           366    372             
DBREF  2JBW D  -13     0  PDB    2JBW     2JBW           -13      0             
DBREF  2JBW D    1   365  UNP    Q93NG6   Q93NG6_ARTNI     1    365             
DBREF  2JBW D  366   372  PDB    2JBW     2JBW           366    372             
SEQADV 2JBW ASP A   14  UNP  Q93NG6    LEU    14 CONFLICT                       
SEQADV 2JBW ASP B   14  UNP  Q93NG6    LEU    14 CONFLICT                       
SEQADV 2JBW ASP C   14  UNP  Q93NG6    LEU    14 CONFLICT                       
SEQADV 2JBW ASP D   14  UNP  Q93NG6    LEU    14 CONFLICT                       
SEQRES   1 A  386  ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO          
SEQRES   2 A  386  GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU          
SEQRES   3 A  386  MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER          
SEQRES   4 A  386  TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU          
SEQRES   5 A  386  ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU          
SEQRES   6 A  386  TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS          
SEQRES   7 A  386  ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU          
SEQRES   8 A  386  CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG          
SEQRES   9 A  386  ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN          
SEQRES  10 A  386  LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS          
SEQRES  11 A  386  GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL          
SEQRES  12 A  386  ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE          
SEQRES  13 A  386  MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE          
SEQRES  14 A  386  GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR          
SEQRES  15 A  386  ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU          
SEQRES  16 A  386  TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER          
SEQRES  17 A  386  ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG          
SEQRES  18 A  386  ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY          
SEQRES  19 A  386  ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU          
SEQRES  20 A  386  ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP          
SEQRES  21 A  386  TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP          
SEQRES  22 A  386  LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG          
SEQRES  23 A  386  LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU          
SEQRES  24 A  386  SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL          
SEQRES  25 A  386  HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU          
SEQRES  26 A  386  GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU          
SEQRES  27 A  386  LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG          
SEQRES  28 A  386  PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU          
SEQRES  29 A  386  VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP          
SEQRES  30 A  386  PRO LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  386  ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO          
SEQRES   2 B  386  GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU          
SEQRES   3 B  386  MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER          
SEQRES   4 B  386  TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU          
SEQRES   5 B  386  ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU          
SEQRES   6 B  386  TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS          
SEQRES   7 B  386  ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU          
SEQRES   8 B  386  CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG          
SEQRES   9 B  386  ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN          
SEQRES  10 B  386  LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS          
SEQRES  11 B  386  GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL          
SEQRES  12 B  386  ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE          
SEQRES  13 B  386  MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE          
SEQRES  14 B  386  GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR          
SEQRES  15 B  386  ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU          
SEQRES  16 B  386  TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER          
SEQRES  17 B  386  ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG          
SEQRES  18 B  386  ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY          
SEQRES  19 B  386  ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU          
SEQRES  20 B  386  ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP          
SEQRES  21 B  386  TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP          
SEQRES  22 B  386  LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG          
SEQRES  23 B  386  LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU          
SEQRES  24 B  386  SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL          
SEQRES  25 B  386  HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU          
SEQRES  26 B  386  GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU          
SEQRES  27 B  386  LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG          
SEQRES  28 B  386  PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU          
SEQRES  29 B  386  VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP          
SEQRES  30 B  386  PRO LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 C  386  ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO          
SEQRES   2 C  386  GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU          
SEQRES   3 C  386  MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER          
SEQRES   4 C  386  TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU          
SEQRES   5 C  386  ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU          
SEQRES   6 C  386  TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS          
SEQRES   7 C  386  ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU          
SEQRES   8 C  386  CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG          
SEQRES   9 C  386  ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN          
SEQRES  10 C  386  LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS          
SEQRES  11 C  386  GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL          
SEQRES  12 C  386  ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE          
SEQRES  13 C  386  MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE          
SEQRES  14 C  386  GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR          
SEQRES  15 C  386  ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU          
SEQRES  16 C  386  TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER          
SEQRES  17 C  386  ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG          
SEQRES  18 C  386  ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY          
SEQRES  19 C  386  ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU          
SEQRES  20 C  386  ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP          
SEQRES  21 C  386  TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP          
SEQRES  22 C  386  LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG          
SEQRES  23 C  386  LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU          
SEQRES  24 C  386  SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL          
SEQRES  25 C  386  HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU          
SEQRES  26 C  386  GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU          
SEQRES  27 C  386  LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG          
SEQRES  28 C  386  PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU          
SEQRES  29 C  386  VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP          
SEQRES  30 C  386  PRO LEU GLU HIS HIS HIS HIS HIS HIS                          
SEQRES   1 D  386  ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO          
SEQRES   2 D  386  GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU          
SEQRES   3 D  386  MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER          
SEQRES   4 D  386  TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU          
SEQRES   5 D  386  ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU          
SEQRES   6 D  386  TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS          
SEQRES   7 D  386  ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU          
SEQRES   8 D  386  CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG          
SEQRES   9 D  386  ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN          
SEQRES  10 D  386  LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS          
SEQRES  11 D  386  GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL          
SEQRES  12 D  386  ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE          
SEQRES  13 D  386  MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE          
SEQRES  14 D  386  GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR          
SEQRES  15 D  386  ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU          
SEQRES  16 D  386  TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER          
SEQRES  17 D  386  ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG          
SEQRES  18 D  386  ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY          
SEQRES  19 D  386  ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU          
SEQRES  20 D  386  ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP          
SEQRES  21 D  386  TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP          
SEQRES  22 D  386  LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG          
SEQRES  23 D  386  LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU          
SEQRES  24 D  386  SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL          
SEQRES  25 D  386  HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU          
SEQRES  26 D  386  GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU          
SEQRES  27 D  386  LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG          
SEQRES  28 D  386  PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU          
SEQRES  29 D  386  VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP          
SEQRES  30 D  386  PRO LEU GLU HIS HIS HIS HIS HIS HIS                          
MODRES 2JBW MSE A   13  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A   29  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A   46  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A   73  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  125  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  143  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  157  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  166  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  342  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE A  360  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B   13  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B   29  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B   46  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B   73  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  125  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  143  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  157  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  166  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  179  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  342  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE B  360  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C   29  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C   46  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C   73  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  125  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  143  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  157  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  166  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  179  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  342  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE C  360  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D   13  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D   29  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D   46  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D   73  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  125  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  143  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  157  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  166  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  179  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  342  MET  SELENOMETHIONINE                                   
MODRES 2JBW MSE D  360  MET  SELENOMETHIONINE                                   
HET    MSE  A  13       8                                                       
HET    MSE  A  29       8                                                       
HET    MSE  A  46       8                                                       
HET    MSE  A  73       8                                                       
HET    MSE  A 125       8                                                       
HET    MSE  A 143       8                                                       
HET    MSE  A 157       8                                                       
HET    MSE  A 166       8                                                       
HET    MSE  A 179       8                                                       
HET    MSE  A 342       8                                                       
HET    MSE  A 360       8                                                       
HET    MSE  B  13       8                                                       
HET    MSE  B  29       8                                                       
HET    MSE  B  46       8                                                       
HET    MSE  B  73       8                                                       
HET    MSE  B 125       8                                                       
HET    MSE  B 143       8                                                       
HET    MSE  B 157       8                                                       
HET    MSE  B 166       8                                                       
HET    MSE  B 179       8                                                       
HET    MSE  B 342       8                                                       
HET    MSE  B 360       8                                                       
HET    MSE  C  29       8                                                       
HET    MSE  C  46       8                                                       
HET    MSE  C  73       8                                                       
HET    MSE  C 125       8                                                       
HET    MSE  C 143       8                                                       
HET    MSE  C 157       8                                                       
HET    MSE  C 166       8                                                       
HET    MSE  C 179       8                                                       
HET    MSE  C 342       8                                                       
HET    MSE  C 360       8                                                       
HET    MSE  D  13       8                                                       
HET    MSE  D  29       8                                                       
HET    MSE  D  46       8                                                       
HET    MSE  D  73       8                                                       
HET    MSE  D 125       8                                                       
HET    MSE  D 143       8                                                       
HET    MSE  D 157       8                                                       
HET    MSE  D 166       8                                                       
HET    MSE  D 179       8                                                       
HET    MSE  D 342       8                                                       
HET    MSE  D 360       8                                                       
HET     NA  D1367       1                                                       
HET     NA  B1367       1                                                       
HET     NA  A1368       1                                                       
HET     NA  C1367       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   5   NA    4(NA1 1+)                                                    
FORMUL   6  MSE    43(C5 H11 N1 O2 SE1)                                         
FORMUL   7  HOH   *964(H2 O1)                                                   
HELIX    1   1 LYS A    8  ASP A   14  1                                   7    
HELIX    2   2 ASN A   15  GLY A   23  1                                   9    
HELIX    3   3 SER A   25  ASP A   34  1                                  10    
HELIX    4   4 THR A   40  LEU A   62  1                                  23    
HELIX    5   5 HIS A   64  PHE A   84  1                                  21    
HELIX    6   6 GLU A   89  ALA A  106  1                                  18    
HELIX    7   7 PRO A  107  LEU A  109  5                                   3    
HELIX    8   8 SER A  154  ARG A  164  1                                  11    
HELIX    9   9 GLN A  176  PHE A  180  5                                   5    
HELIX   10  10 ASP A  188  LEU A  203  1                                  16    
HELIX   11  11 SER A  217  GLU A  230  1                                  14    
HELIX   12  12 TYR A  247  GLU A  251  5                                   5    
HELIX   13  13 THR A  252  SER A  263  1                                  12    
HELIX   14  14 THR A  267  LEU A  279  1                                  13    
HELIX   15  15 VAL A  284  ILE A  288  5                                   5    
HELIX   16  16 LEU A  304  VAL A  314  1                                  11    
HELIX   17  17 PRO A  315  GLU A  317  5                                   3    
HELIX   18  18 ASP A  328  GLY A  335  5                                   8    
HELIX   19  19 ILE A  336  VAL A  351  1                                  16    
HELIX   20  20 LYS B    8  ASP B   14  1                                   7    
HELIX   21  21 ASN B   15  ASP B   22  1                                   8    
HELIX   22  22 SER B   25  ASP B   34  1                                  10    
HELIX   23  23 THR B   40  LEU B   62  1                                  23    
HELIX   24  24 HIS B   64  PHE B   84  1                                  21    
HELIX   25  25 ARG B   90  ALA B  106  1                                  17    
HELIX   26  26 PRO B  107  LEU B  109  5                                   3    
HELIX   27  27 THR B  150  GLU B  153  5                                   4    
HELIX   28  28 SER B  154  ASP B  163  1                                  10    
HELIX   29  29 TYR B  189  LEU B  203  1                                  15    
HELIX   30  30 SER B  217  CYS B  229  1                                  13    
HELIX   31  31 TYR B  247  GLU B  251  5                                   5    
HELIX   32  32 THR B  252  LYS B  264  1                                  13    
HELIX   33  33 THR B  267  LEU B  279  1                                  13    
HELIX   34  34 VAL B  284  ILE B  288  5                                   5    
HELIX   35  35 LEU B  304  VAL B  314  1                                  11    
HELIX   36  36 ASP B  328  GLY B  335  5                                   8    
HELIX   37  37 ILE B  336  VAL B  351  1                                  16    
HELIX   38  38 ASN C   15  GLY C   23  1                                   9    
HELIX   39  39 SER C   25  ASP C   34  1                                  10    
HELIX   40  40 THR C   40  LEU C   62  1                                  23    
HELIX   41  41 HIS C   64  GLN C   83  1                                  20    
HELIX   42  42 ASP C   88  ALA C  106  1                                  19    
HELIX   43  43 PRO C  107  LEU C  109  5                                   3    
HELIX   44  44 THR C  150  GLU C  153  5                                   4    
HELIX   45  45 SER C  154  ARG C  164  1                                  11    
HELIX   46  46 GLN C  176  LYS C  183  5                                   8    
HELIX   47  47 ASP C  188  LEU C  203  1                                  16    
HELIX   48  48 SER C  217  GLU C  230  1                                  14    
HELIX   49  49 TYR C  247  GLU C  251  5                                   5    
HELIX   50  50 THR C  252  LYS C  264  1                                  13    
HELIX   51  51 THR C  267  LEU C  279  1                                  13    
HELIX   52  52 VAL C  284  ILE C  288  5                                   5    
HELIX   53  53 LEU C  304  VAL C  314  1                                  11    
HELIX   54  54 ASP C  328  GLY C  335  5                                   8    
HELIX   55  55 ILE C  336  VAL C  351  1                                  16    
HELIX   56  56 LYS D    8  GLU D   12  5                                   5    
HELIX   57  57 ASN D   15  GLY D   23  1                                   9    
HELIX   58  58 SER D   25  ASP D   34  1                                  10    
HELIX   59  59 THR D   40  LEU D   62  1                                  23    
HELIX   60  60 HIS D   64  GLN D   83  1                                  20    
HELIX   61  61 ASP D   88  ALA D  106  1                                  19    
HELIX   62  62 PRO D  107  LEU D  109  5                                   3    
HELIX   63  63 THR D  150  GLU D  153  5                                   4    
HELIX   64  64 SER D  154  ARG D  164  1                                  11    
HELIX   65  65 GLN D  176  PHE D  180  5                                   5    
HELIX   66  66 ASP D  188  THR D  201  1                                  14    
HELIX   67  67 SER D  217  GLU D  230  1                                  14    
HELIX   68  68 TYR D  247  GLU D  251  5                                   5    
HELIX   69  69 THR D  252  LYS D  264  1                                  13    
HELIX   70  70 THR D  267  LEU D  279  1                                  13    
HELIX   71  71 VAL D  284  ILE D  288  5                                   5    
HELIX   72  72 LEU D  304  VAL D  314  1                                  11    
HELIX   73  73 ASP D  328  GLY D  335  5                                   8    
HELIX   74  74 ILE D  336  VAL D  351  1                                  16    
SHEET    1  AA 9 ALA A 113  VAL A 120  0                                        
SHEET    2  AA 9 ILE A 123  ARG A 130 -1  O  ILE A 123   N  VAL A 120           
SHEET    3  AA 9 ALA A 167  PHE A 171 -1  O  THR A 168   N  ARG A 130           
SHEET    4  AA 9 HIS A 138  LEU A 144  1  O  PRO A 139   N  ALA A 167           
SHEET    5  AA 9 ILE A 206  ARG A 216  1  N  ARG A 207   O  HIS A 138           
SHEET    6  AA 9 ALA A 235  TRP A 239  1  O  ALA A 235   N  VAL A 213           
SHEET    7  AA 9 THR A 292  GLY A 297  1  O  TYR A 293   N  SER A 238           
SHEET    8  AA 9 LEU A 319  GLU A 324  1  O  ASN A 320   N  ILE A 294           
SHEET    9  AA 9 MSE A 360  LYS A 361  1  O  LYS A 361   N  VAL A 323           
SHEET    1  BA 9 ALA B 113  VAL B 120  0                                        
SHEET    2  BA 9 ILE B 123  ARG B 130 -1  O  ILE B 123   N  VAL B 120           
SHEET    3  BA 9 ALA B 167  PHE B 171 -1  O  THR B 168   N  ARG B 130           
SHEET    4  BA 9 HIS B 138  LEU B 144  1  O  PRO B 139   N  ALA B 167           
SHEET    5  BA 9 ILE B 206  ARG B 216  1  N  ARG B 207   O  HIS B 138           
SHEET    6  BA 9 CYS B 236  TRP B 239  1  O  ILE B 237   N  GLY B 215           
SHEET    7  BA 9 THR B 292  GLY B 297  1  O  TYR B 293   N  SER B 238           
SHEET    8  BA 9 LEU B 319  GLU B 324  1  O  ASN B 320   N  ILE B 294           
SHEET    9  BA 9 THR B 359  LYS B 361  1  O  THR B 359   N  LEU B 321           
SHEET    1  CA 9 ALA C 113  VAL C 120  0                                        
SHEET    2  CA 9 ILE C 123  ARG C 130 -1  O  ILE C 123   N  VAL C 120           
SHEET    3  CA 9 ALA C 167  PHE C 171 -1  O  THR C 168   N  ARG C 130           
SHEET    4  CA 9 HIS C 138  LEU C 144  1  O  PRO C 139   N  ALA C 167           
SHEET    5  CA 9 ILE C 206  ARG C 216  1  N  ARG C 207   O  HIS C 138           
SHEET    6  CA 9 CYS C 236  TRP C 239  1  O  ILE C 237   N  GLY C 215           
SHEET    7  CA 9 THR C 292  GLY C 297  1  O  TYR C 293   N  SER C 238           
SHEET    8  CA 9 LEU C 319  GLU C 324  1  O  ASN C 320   N  ILE C 294           
SHEET    9  CA 9 THR C 359  LYS C 361  1  O  THR C 359   N  LEU C 321           
SHEET    1  DA 9 ALA D 113  VAL D 120  0                                        
SHEET    2  DA 9 ILE D 123  ARG D 130 -1  O  ILE D 123   N  VAL D 120           
SHEET    3  DA 9 ALA D 167  PHE D 171 -1  O  THR D 168   N  ARG D 130           
SHEET    4  DA 9 HIS D 138  LEU D 144  1  O  PRO D 139   N  ALA D 167           
SHEET    5  DA 9 ILE D 206  ARG D 216  1  N  ARG D 207   O  HIS D 138           
SHEET    6  DA 9 CYS D 236  TRP D 239  1  O  ILE D 237   N  GLY D 215           
SHEET    7  DA 9 THR D 292  GLY D 297  1  O  TYR D 293   N  SER D 238           
SHEET    8  DA 9 LEU D 319  GLU D 324  1  O  ASN D 320   N  ILE D 294           
SHEET    9  DA 9 THR D 359  LYS D 361  1  O  THR D 359   N  LEU D 321           
LINK         C   GLU A  12                 N   MSE A  13     1555   1555        
LINK         C   MSE A  13                 N   ASP A  14     1555   1555        
LINK         C   ASP A  28                 N   MSE A  29     1555   1555        
LINK         C   MSE A  29                 N   VAL A  30     1555   1555        
LINK         C   TRP A  45                 N   MSE A  46     1555   1555        
LINK         C   MSE A  46                 N   SER A  47     1555   1555        
LINK         C   LEU A  72                 N   MSE A  73     1555   1555        
LINK         C   MSE A  73                 N   SER A  74     1555   1555        
LINK         C   PRO A 124                 N   MSE A 125     1555   1555        
LINK         C   MSE A 125                 N   PRO A 126     1555   1555        
LINK         C   ILE A 142                 N   MSE A 143     1555   1555        
LINK         C   MSE A 143                 N   LEU A 144     1555   1555        
LINK         C   GLN A 156                 N   MSE A 157     1555   1555        
LINK         C   MSE A 157                 N   GLU A 158     1555   1555        
LINK         C   GLY A 165                 N   MSE A 166     1555   1555        
LINK         C   MSE A 166                 N   ALA A 167     1555   1555        
LINK         C   GLU A 178                 N   MSE A 179     1555   1555        
LINK         C   MSE A 179                 N   PHE A 180     1555   1555        
LINK         C   GLU A 341                 N   MSE A 342     1555   1555        
LINK         C   MSE A 342                 N   ALA A 343     1555   1555        
LINK         C   THR A 359                 N   MSE A 360     1555   1555        
LINK         C   MSE A 360                 N   LYS A 361     1555   1555        
LINK        NA    NA A1368                 O   LEU A 203     1555   1555        
LINK        NA    NA A1368                 O   ILE A 206     1555   1555        
LINK        NA    NA A1368                 OD1 ASN A 208     1555   1555        
LINK         C   GLU B  12                 N   MSE B  13     1555   1555        
LINK         C   MSE B  13                 N   ASP B  14     1555   1555        
LINK         C   ASP B  28                 N   MSE B  29     1555   1555        
LINK         C   MSE B  29                 N   VAL B  30     1555   1555        
LINK         C   TRP B  45                 N   MSE B  46     1555   1555        
LINK         C   MSE B  46                 N   SER B  47     1555   1555        
LINK         C   LEU B  72                 N   MSE B  73     1555   1555        
LINK         C   MSE B  73                 N   SER B  74     1555   1555        
LINK         C   PRO B 124                 N   MSE B 125     1555   1555        
LINK         C   MSE B 125                 N   PRO B 126     1555   1555        
LINK         C   ILE B 142                 N   MSE B 143     1555   1555        
LINK         C   MSE B 143                 N   LEU B 144     1555   1555        
LINK         C   GLN B 156                 N   MSE B 157     1555   1555        
LINK         C   MSE B 157                 N   GLU B 158     1555   1555        
LINK         C   GLY B 165                 N   MSE B 166     1555   1555        
LINK         C   MSE B 166                 N   ALA B 167     1555   1555        
LINK         C   GLU B 178                 N   MSE B 179     1555   1555        
LINK         C   MSE B 179                 N   PHE B 180     1555   1555        
LINK         C   GLU B 341                 N   MSE B 342     1555   1555        
LINK         C   MSE B 342                 N   ALA B 343     1555   1555        
LINK         C   THR B 359                 N   MSE B 360     1555   1555        
LINK         C   MSE B 360                 N   LYS B 361     1555   1555        
LINK        NA    NA B1367                 O   LEU B 203     1555   1555        
LINK        NA    NA B1367                 OD1 ASN B 208     1555   1555        
LINK         C   ASP C  28                 N   MSE C  29     1555   1555        
LINK         C   MSE C  29                 N   VAL C  30     1555   1555        
LINK         C   TRP C  45                 N   MSE C  46     1555   1555        
LINK         C   MSE C  46                 N   SER C  47     1555   1555        
LINK         C   LEU C  72                 N   MSE C  73     1555   1555        
LINK         C   MSE C  73                 N   SER C  74     1555   1555        
LINK         C   PRO C 124                 N   MSE C 125     1555   1555        
LINK         C   MSE C 125                 N   PRO C 126     1555   1555        
LINK         C   ILE C 142                 N   MSE C 143     1555   1555        
LINK         C   MSE C 143                 N   LEU C 144     1555   1555        
LINK         C   GLN C 156                 N   MSE C 157     1555   1555        
LINK         C   MSE C 157                 N   GLU C 158     1555   1555        
LINK         C   GLY C 165                 N   MSE C 166     1555   1555        
LINK         C   MSE C 166                 N   ALA C 167     1555   1555        
LINK         C   GLU C 178                 N   MSE C 179     1555   1555        
LINK         C   MSE C 179                 N   PHE C 180     1555   1555        
LINK         C   GLU C 341                 N   MSE C 342     1555   1555        
LINK         C   MSE C 342                 N   ALA C 343     1555   1555        
LINK         C   THR C 359                 N   MSE C 360     1555   1555        
LINK         C   MSE C 360                 N   LYS C 361     1555   1555        
LINK        NA    NA C1367                 O   ILE C 206     1555   1555        
LINK        NA    NA C1367                 O   LEU C 200     1555   1555        
LINK        NA    NA C1367                 O   HOH X 169     1555   1555        
LINK        NA    NA C1367                 O   LEU C 203     1555   1555        
LINK         C   GLU D  12                 N   MSE D  13     1555   1555        
LINK         C   MSE D  13                 N   ASP D  14     1555   1555        
LINK         C   ASP D  28                 N   MSE D  29     1555   1555        
LINK         C   MSE D  29                 N   VAL D  30     1555   1555        
LINK         C   TRP D  45                 N   MSE D  46     1555   1555        
LINK         C   MSE D  46                 N   SER D  47     1555   1555        
LINK         C   LEU D  72                 N   MSE D  73     1555   1555        
LINK         C   MSE D  73                 N   SER D  74     1555   1555        
LINK         C   PRO D 124                 N   MSE D 125     1555   1555        
LINK         C   MSE D 125                 N   PRO D 126     1555   1555        
LINK         C   ILE D 142                 N   MSE D 143     1555   1555        
LINK         C   MSE D 143                 N   LEU D 144     1555   1555        
LINK         C   GLN D 156                 N   MSE D 157     1555   1555        
LINK         C   MSE D 157                 N   GLU D 158     1555   1555        
LINK         C   GLY D 165                 N   MSE D 166     1555   1555        
LINK         C   MSE D 166                 N   ALA D 167     1555   1555        
LINK         C   GLU D 178                 N   MSE D 179     1555   1555        
LINK         C   MSE D 179                 N   PHE D 180     1555   1555        
LINK         C   GLU D 341                 N   MSE D 342     1555   1555        
LINK         C   MSE D 342                 N   ALA D 343     1555   1555        
LINK         C   THR D 359                 N   MSE D 360     1555   1555        
LINK         C   MSE D 360                 N   LYS D 361     1555   1555        
LINK        NA    NA D1367                 O   LEU D 203     1555   1555        
LINK        NA    NA D1367                 OD1 ASN D 208     1555   1555        
LINK        NA    NA D1367                 O   ILE D 206     1555   1555        
CISPEP   1 SER A  110    PRO A  111          0         0.46                     
CISPEP   2 GLY A  136    PRO A  137          0        -1.62                     
CISPEP   3 TRP A  363    PRO A  364          0         1.53                     
CISPEP   4 SER B  110    PRO B  111          0        -4.74                     
CISPEP   5 GLY B  136    PRO B  137          0        -9.84                     
CISPEP   6 TRP B  363    PRO B  364          0        -3.69                     
CISPEP   7 SER C  110    PRO C  111          0        -1.38                     
CISPEP   8 GLY C  136    PRO C  137          0        -2.05                     
CISPEP   9 TRP C  363    PRO C  364          0        -3.65                     
CISPEP  10 SER D  110    PRO D  111          0        -5.02                     
CISPEP  11 GLY D  136    PRO D  137          0         3.20                     
CISPEP  12 TRP D  363    PRO D  364          0        -0.70                     
CISPEP  13 LEU B  365    GLU B  366          0       -27.09                     
SITE     1 TRI 12 SER A 217  ASP A 300  HIS A 329  SER B 217                    
SITE     2 TRI 12 ASP B 300  HIS B 329  SER C 217  ASP C 300                    
SITE     3 TRI 12 HIS C 329  SER D 217  ASP D 300  HIS D 329                    
SITE     1 AS1  5 ARG A  18  ASP A  22  GLU A 148  SER A 149                    
SITE     2 AS1  5 ARG A 216                                                     
SITE     1 AS2  5 ARG B  18  ASP B  22  GLU B 148  SER B 149                    
SITE     2 AS2  5 ARG B 216                                                     
SITE     1 AS3  5 ARG C  18  ASP C  22  GLU C 148  SER C 149                    
SITE     2 AS3  5 ARG C 216                                                     
SITE     1 AS3  5 ARG D  18  ASP D  22  GLU D 148  SER D 149                    
SITE     2 AS3  5 ARG D 216                                                     
SITE     1 AC1  4 LEU D 200  LEU D 203  ILE D 206  ASN D 208                    
SITE     1 AC2  6 LEU B 200  THR B 201  LEU B 203  ILE B 206                    
SITE     2 AC2  6 ASN B 208  HOH Y  95                                          
SITE     1 AC3  5 LEU A 200  THR A 201  LEU A 203  ILE A 206                    
SITE     2 AC3  5 ASN A 208                                                     
SITE     1 AC4  6 LEU C 200  THR C 201  LEU C 203  ILE C 206                    
SITE     2 AC4  6 ASN C 208  HOH X 169                                          
CRYST1   90.570   57.020  152.697  90.00 103.35  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      0.011041  0.000000  0.002620        0.00000                         
SCALE2      0.000000  0.017538  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006731        0.00000                         
MTRIX1   1  0.421495  0.102558 -0.901013      157.08570    1                    
MTRIX2   1  0.109886 -0.992039 -0.061514       48.19570    1                    
MTRIX3   1 -0.900149 -0.073081 -0.429409      253.29300    1                    
MTRIX1   2  0.580614  0.013364 -0.814069       63.86340    1                    
MTRIX2   2  0.005988 -0.999908 -0.012143       50.72710    1                    
MTRIX3   2 -0.814157  0.002176 -0.580641      124.82560    1                    

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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