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LongText Report for: 6u2m-pdb

Name Class
6u2m-pdb
HEADER    HYDROLASE                               20-AUG-19   6U2M              
TITLE     CRYSTAL STRUCTURE OF A HALOTAG-BASED CALCIUM INDICATOR, HALOCAMP V2,  
TITLE    2 BOUND TO JF635                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOCAMP V2;                                               
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;                                
SOURCE   3 ORGANISM_TAXID: 1831;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HALOTAG, CALCIUM, SENSOR, FLUORESCENT, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.DEO,E.R.SCHREITER                                                   
REVDAT   1   30-SEP-20 6U2M    0                                                
JRNL        AUTH   C.DEO,L.D.LAVIS,E.R.SCHREITER                                
JRNL        TITL   CRYSTAL STRUCTURE OF A HALOTAG-BASED CALCIUM INDICATOR,      
JRNL        TITL 2 HALOCAMP V2                                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 122.58                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 86312                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4438                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6270                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 323                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7420                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 110                                     
REMARK   3   SOLVENT ATOMS            : 203                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 52.53                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.16000                                             
REMARK   3    B22 (A**2) : -0.75000                                             
REMARK   3    B33 (A**2) : 1.90000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.09000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.142         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.135         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.639        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7724 ; 0.026 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7086 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10492 ; 2.440 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16456 ; 1.285 ; 2.983       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   924 ; 7.406 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   382 ;33.783 ;24.136       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1268 ;16.937 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    54 ;21.358 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1108 ; 0.163 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8568 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1582 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
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     4        A    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.0790  38.1540  75.9960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1483 T22:   0.0477                                     
REMARK   3      T33:   0.1964 T12:  -0.0197                                     
REMARK   3      T13:   0.0145 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0590 L22:   2.1199                                     
REMARK   3      L33:   2.0479 L12:   1.9960                                     
REMARK   3      L13:  -2.0886 L23:  -2.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0166 S12:   0.0491 S13:  -0.1307                       
REMARK   3      S21:  -0.0714 S22:  -0.0356 S23:   0.0289                       
REMARK   3      S31:   0.0485 S32:   0.0386 S33:   0.0190                       
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    27        A    31                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5466  31.2902  60.7087              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1277 T22:   0.1812                                     
REMARK   3      T33:   0.0400 T12:  -0.0802                                     
REMARK   3      T13:   0.0324 T23:  -0.0709                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5921 L22:  15.1139                                     
REMARK   3      L33:  29.7974 L12:  -3.7662                                     
REMARK   3      L13:   2.3335 L23:   7.2582                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1884 S12:  -0.0829 S13:  -0.0712                       
REMARK   3      S21:   0.7658 S22:  -0.0454 S23:   0.3268                       
REMARK   3      S31:   0.4566 S32:  -0.6810 S33:   0.2338                       
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    32        A   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0250  24.7376  45.0532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0794 T22:   0.2080                                     
REMARK   3      T33:   0.2147 T12:  -0.0382                                     
REMARK   3      T13:   0.0146 T23:  -0.1168                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6256 L22:   0.9200                                     
REMARK   3      L33:   0.8898 L12:  -0.3899                                     
REMARK   3      L13:  -0.6199 L23:  -0.0450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0778 S12:  -0.3586 S13:   0.2045                       
REMARK   3      S21:   0.1119 S22:   0.2441 S23:   0.0530                       
REMARK   3      S31:  -0.1804 S32:   0.3401 S33:  -0.3219                       
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   110        A   159                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2776   4.5467  50.3778              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2027 T22:   0.2521                                     
REMARK   3      T33:   0.2158 T12:   0.1836                                     
REMARK   3      T13:   0.0450 T23:   0.1668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2762 L22:   2.4985                                     
REMARK   3      L33:   1.8114 L12:   0.9382                                     
REMARK   3      L13:  -0.7610 L23:   1.0911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4554 S12:  -0.5770 S13:  -0.3126                       
REMARK   3      S21:   0.1745 S22:   0.2263 S23:   0.2043                       
REMARK   3      S31:   0.3982 S32:   0.5174 S33:   0.2291                       
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   160        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6347  -3.0227  41.1947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2007 T22:   0.0549                                     
REMARK   3      T33:   0.2502 T12:   0.0869                                     
REMARK   3      T13:   0.0155 T23:   0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7212 L22:   5.6940                                     
REMARK   3      L33:   6.5898 L12:   4.2196                                     
REMARK   3      L13:   2.5054 L23:   4.8665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2058 S12:  -0.1232 S13:  -0.3212                       
REMARK   3      S21:   0.1566 S22:   0.0188 S23:  -0.2538                       
REMARK   3      S31:   0.6398 S32:   0.2021 S33:   0.1871                       
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   202        A   335                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.5045  11.3174  33.7627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0962 T22:   0.0242                                     
REMARK   3      T33:   0.2196 T12:   0.0107                                     
REMARK   3      T13:  -0.0332 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1972 L22:   0.5396                                     
REMARK   3      L33:   0.9352 L12:  -0.0306                                     
REMARK   3      L13:  -0.7590 L23:  -0.0716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0554 S12:  -0.1031 S13:  -0.0953                       
REMARK   3      S21:  -0.0845 S22:   0.0738 S23:  -0.0296                       
REMARK   3      S31:   0.0680 S32:   0.0867 S33:  -0.0184                       
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   336        A   351                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9949  21.3339  65.9808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2085 T22:   0.2449                                     
REMARK   3      T33:   0.2043 T12:   0.1002                                     
REMARK   3      T13:  -0.0359 T23:  -0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2299 L22:   1.1493                                     
REMARK   3      L33:   9.7994 L12:   1.1828                                     
REMARK   3      L13:   3.4568 L23:   3.3153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2497 S12:   0.1742 S13:  -0.0869                       
REMARK   3      S21:   0.2582 S22:   0.1132 S23:  -0.0562                       
REMARK   3      S31:   0.8129 S32:   0.5238 S33:  -0.3630                       
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   352        A   419                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.2102  30.7691  86.2387              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1124 T22:   0.0587                                     
REMARK   3      T33:   0.2042 T12:  -0.0328                                     
REMARK   3      T13:   0.0141 T23:  -0.0697                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8315 L22:   1.0288                                     
REMARK   3      L33:   0.1433 L12:   0.8363                                     
REMARK   3      L13:  -0.2146 L23:  -0.3619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2609 S12:  -0.1805 S13:   0.0384                       
REMARK   3      S21:  -0.0098 S22:  -0.1861 S23:   0.0956                       
REMARK   3      S31:   0.0059 S32:   0.0793 S33:  -0.0748                       
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   420        A   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5987  42.2963  73.7193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1473 T22:   0.0388                                     
REMARK   3      T33:   0.2035 T12:   0.0063                                     
REMARK   3      T13:  -0.0561 T23:  -0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8527 L22:   1.7402                                     
REMARK   3      L33:   5.3473 L12:   0.8616                                     
REMARK   3      L13:   2.7303 L23:  -0.0243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0997 S12:   0.0339 S13:  -0.0514                       
REMARK   3      S21:   0.1235 S22:   0.1314 S23:   0.0368                       
REMARK   3      S31:   0.1480 S32:  -0.0867 S33:  -0.2312                       
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   437        A   489                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8191  49.9831  73.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1564 T22:   0.0562                                     
REMARK   3      T33:   0.1642 T12:  -0.0427                                     
REMARK   3      T13:  -0.0546 T23:   0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7092 L22:   0.7762                                     
REMARK   3      L33:   1.1315 L12:  -0.2941                                     
REMARK   3      L13:   0.1330 L23:  -0.4767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0927 S12:   0.2878 S13:   0.2805                       
REMARK   3      S21:   0.1172 S22:  -0.1162 S23:  -0.0418                       
REMARK   3      S31:  -0.2183 S32:   0.1819 S33:   0.2090                       
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 :   C     4        C    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8961  26.4791 136.7338              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.0453                                     
REMARK   3      T33:   0.2663 T12:   0.0383                                     
REMARK   3      T13:  -0.0132 T23:   0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1440 L22:   2.2756                                     
REMARK   3      L33:   0.9251 L12:   2.0869                                     
REMARK   3      L13:   0.9548 L23:   1.2734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0361 S12:   0.0410 S13:   0.0816                       
REMARK   3      S21:  -0.0371 S22:  -0.0368 S23:   0.0604                       
REMARK   3      S31:  -0.0010 S32:  -0.0830 S33:   0.0729                       
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 :   C    27        C    31                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8231  33.6916 121.9078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2027 T22:   0.3120                                     
REMARK   3      T33:   0.1020 T12:  -0.0205                                     
REMARK   3      T13:   0.0271 T23:   0.0561                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0537 L22:   2.8450                                     
REMARK   3      L33:  11.6139 L12:  -0.3860                                     
REMARK   3      L13:  -0.7754 L23:   5.7437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0463 S12:   0.0424 S13:  -0.0151                       
REMARK   3      S21:   0.2451 S22:  -0.2652 S23:   0.1464                       
REMARK   3      S31:   0.4541 S32:  -0.5557 S33:   0.3115                       
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 :   C    32        C   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9997  39.9834 106.9309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0941 T22:   0.2778                                     
REMARK   3      T33:   0.2252 T12:  -0.1150                                     
REMARK   3      T13:  -0.0517 T23:   0.0745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3616 L22:   1.0725                                     
REMARK   3      L33:   0.8622 L12:  -0.4114                                     
REMARK   3      L13:   0.5048 L23:  -0.5603                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0878 S12:  -0.2948 S13:  -0.1170                       
REMARK   3      S21:   0.0922 S22:   0.2212 S23:  -0.0136                       
REMARK   3      S31:   0.1190 S32:  -0.3627 S33:  -0.3090                       
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 :   C   110        C   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1215  60.9782 112.5217              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1439 T22:   0.3155                                     
REMARK   3      T33:   0.3042 T12:   0.1951                                     
REMARK   3      T13:  -0.1802 T23:  -0.2870                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3886 L22:   2.8013                                     
REMARK   3      L33:   0.7400 L12:   2.6410                                     
REMARK   3      L13:   0.1764 L23:  -0.8362                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4172 S12:  -0.8080 S13:   0.4291                       
REMARK   3      S21:   0.0774 S22:  -0.0349 S23:  -0.2940                       
REMARK   3      S31:  -0.2726 S32:  -0.3809 S33:   0.4521                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   155        C   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9617  54.8929  97.2107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0787 T22:   0.0413                                     
REMARK   3      T33:   0.2206 T12:   0.0000                                     
REMARK   3      T13:   0.0015 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8617 L22:   0.5142                                     
REMARK   3      L33:   0.9286 L12:   0.0520                                     
REMARK   3      L13:   0.7457 L23:   0.0606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0847 S12:  -0.1499 S13:   0.1440                       
REMARK   3      S21:  -0.1103 S22:   0.0316 S23:   0.0279                       
REMARK   3      S31:  -0.0554 S32:  -0.1218 S33:   0.0532                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   338        C   345                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9521  46.0877 123.5233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1373 T22:   0.2533                                     
REMARK   3      T33:   0.1435 T12:   0.0627                                     
REMARK   3      T13:   0.0461 T23:   0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9001 L22:   6.4042                                     
REMARK   3      L33:   8.3649 L12:   2.9030                                     
REMARK   3      L13:  -1.5760 L23:  -6.1320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0274 S12:   0.4019 S13:  -0.1940                       
REMARK   3      S21:   0.2206 S22:   0.6411 S23:   0.1015                       
REMARK   3      S31:  -0.4526 S32:  -0.4061 S33:  -0.6137                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   346        C   357                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4311  37.6750 137.8942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1176 T22:   0.1015                                     
REMARK   3      T33:   0.1244 T12:   0.0434                                     
REMARK   3      T13:  -0.0378 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0675 L22:   2.5727                                     
REMARK   3      L33:   6.9170 L12:   1.1378                                     
REMARK   3      L13:   0.6132 L23:  -1.7039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0533 S12:  -0.0474 S13:  -0.0298                       
REMARK   3      S21:  -0.0710 S22:  -0.0707 S23:   0.1436                       
REMARK   3      S31:  -0.1669 S32:  -0.2640 S33:   0.0173                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   358        C   419                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7964  33.7107 147.4929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0982 T22:   0.0661                                     
REMARK   3      T33:   0.2035 T12:  -0.0023                                     
REMARK   3      T13:  -0.0153 T23:   0.0616                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0302 L22:   0.7813                                     
REMARK   3      L33:   0.1947 L12:   0.7821                                     
REMARK   3      L13:   0.2464 L23:   0.1942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2566 S12:  -0.1901 S13:  -0.0563                       
REMARK   3      S21:   0.0107 S22:  -0.2092 S23:  -0.0653                       
REMARK   3      S31:  -0.0009 S32:  -0.0634 S33:  -0.0473                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   420        C   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3417  22.1922 134.6044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1105 T22:   0.0476                                     
REMARK   3      T33:   0.2056 T12:   0.0662                                     
REMARK   3      T13:   0.0024 T23:  -0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1515 L22:   4.7335                                     
REMARK   3      L33:   3.4427 L12:   1.0164                                     
REMARK   3      L13:  -3.7773 L23:  -0.8976                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1273 S12:   0.1900 S13:   0.2175                       
REMARK   3      S21:   0.2149 S22:   0.1029 S23:  -0.0759                       
REMARK   3      S31:  -0.1057 S32:  -0.1638 S33:  -0.2302                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   437        C   489                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1069  14.6671 134.5818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1653 T22:   0.0388                                     
REMARK   3      T33:   0.1870 T12:  -0.0119                                     
REMARK   3      T13:   0.0210 T23:  -0.0527                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0650 L22:   0.1536                                     
REMARK   3      L33:   1.6940 L12:  -0.4113                                     
REMARK   3      L13:  -0.2414 L23:   0.4322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:   0.2533 S13:  -0.2725                       
REMARK   3      S21:   0.0681 S22:  -0.0715 S23:   0.0531                       
REMARK   3      S31:   0.1955 S32:  -0.1709 S33:   0.0817                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6U2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243781.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9774                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90798                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 122.580                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09600                            
REMARK 200   FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.34700                            
REMARK 200  R SYM FOR SHELL            (I) : 1.34700                            
REMARK 200   FOR SHELL         : 0.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5UY1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) PEG 200, 100 MM MES/ SODIUM    
REMARK 280  HYDROXIDE PH 6.0, AND 5% (W/V) PEG 3000, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     GLY A   185                                                      
REMARK 465     SER A   186                                                      
REMARK 465     GLY A   187                                                      
REMARK 465     GLY A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     GLY A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     GLY A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     THR A   195                                                      
REMARK 465     GLY A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     SER A   198                                                      
REMARK 465     MET A   199                                                      
REMARK 465     ALA A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     LYS A   490                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     HIS C    -3                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     HIS C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     GLY C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     GLY C   182                                                      
REMARK 465     THR C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     GLY C   185                                                      
REMARK 465     SER C   186                                                      
REMARK 465     GLY C   187                                                      
REMARK 465     GLY C   188                                                      
REMARK 465     THR C   189                                                      
REMARK 465     GLY C   190                                                      
REMARK 465     GLY C   191                                                      
REMARK 465     SER C   192                                                      
REMARK 465     GLY C   193                                                      
REMARK 465     GLY C   194                                                      
REMARK 465     THR C   195                                                      
REMARK 465     GLY C   196                                                      
REMARK 465     GLY C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     MET C   199                                                      
REMARK 465     ALA C   200                                                      
REMARK 465     GLU C   201                                                      
REMARK 465     LYS C   490                                                      
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   OD1  ASP A   304     C27  PUJ A   600              1.96            
REMARK 500   OD1  ASP C   304     C27  PUJ C   600              2.09            
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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A   6   CD    ARG A   6   NE     -0.117                       
REMARK 500    THR A  31   CB    THR A  31   CG2     0.225                       
REMARK 500    ASP A 110   CB    ASP A 110   CG     -0.155                       
REMARK 500    GLU A 291   CD    GLU A 291   OE2     0.068                       
REMARK 500    GLU A 319   CG    GLU A 319   CD      0.112                       
REMARK 500    TRP A 339   CB    TRP A 339   CG      0.177                       
REMARK 500    GLU A 396   CG    GLU A 396   CD      0.094                       
REMARK 500    GLU A 396   CD    GLU A 396   OE2    -0.068                       
REMARK 500    ILE C   4   N     ILE C   4   CA      0.125                       
REMARK 500    ARG C   6   CD    ARG C   6   NE     -0.120                       
REMARK 500    GLU C 177   CG    GLU C 177   CD      0.097                       
REMARK 500    GLU C 319   CG    GLU C 319   CD      0.113                       
REMARK 500    GLU C 353   CD    GLU C 353   OE1     0.067                       
REMARK 500    GLU C 396   CD    GLU C 396   OE2    -0.080                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A   6   CD  -  NE  -  CZ  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG A   6   NE  -  CZ  -  NH1 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ARG A   6   NE  -  CZ  -  NH2 ANGL. DEV. = -11.8 DEGREES          
REMARK 500    LEU A  12   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG A  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  73   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    LEU A 104   CA  -  CB  -  CG  ANGL. DEV. =  23.0 DEGREES          
REMARK 500    LEU A 104   CB  -  CG  -  CD1 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    MET A 109   CG  -  SD  -  CE  ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASP A 110   CB  -  CG  -  OD2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    PRO A 152   C   -  N   -  CA  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    GLU A 319   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    ARG A 379   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    MET A 393   CG  -  SD  -  CE  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ASP A 437   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG C   6   CD  -  NE  -  CZ  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ARG C   6   NE  -  CZ  -  NH2 ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP C   8   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    LEU C  12   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG C  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG C  73   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    LEU C 104   CA  -  CB  -  CG  ANGL. DEV. =  21.8 DEGREES          
REMARK 500    LEU C 104   CB  -  CG  -  CD2 ANGL. DEV. =  17.4 DEGREES          
REMARK 500    ASP C 110   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP C 149   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    GLU C 177   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG C 219   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ASP C 274   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    GLU C 319   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    ASP C 366   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ARG C 448   CG  -  CD  -  NE  ANGL. DEV. = -12.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  29      -46.00     72.94                                   
REMARK 500    GLU A  30      -54.36     72.68                                   
REMARK 500    THR A  31      -61.40     87.94                                   
REMARK 500    ASP A  39      -56.26     82.13                                   
REMARK 500    VAL A 128      -70.27   -128.90                                   
REMARK 500    LEU A 154      -97.29   -115.68                                   
REMARK 500    ASN A 161       62.35   -150.48                                   
REMARK 500    THR A 241     -164.10   -101.59                                   
REMARK 500    GLU A 296      -86.76   -110.23                                   
REMARK 500    ASP A 304     -130.38     60.02                                   
REMARK 500    ASN A 317       48.52   -140.67                                   
REMARK 500    TRP A 339       -8.60    -50.25                                   
REMARK 500    ASP A 344       73.24   -108.71                                   
REMARK 500    GLN A 345       98.81   -179.79                                   
REMARK 500    GLU A 424      -63.14    121.77                                   
REMARK 500    PHE C  26      -71.57   -105.45                                   
REMARK 500    ARG C  27       -5.75     59.67                                   
REMARK 500    PRO C  28       89.26    -38.64                                   
REMARK 500    LYS C  29      -85.47     69.35                                   
REMARK 500    GLU C  30      -88.16    118.01                                   
REMARK 500    THR C  31      -97.59    109.51                                   
REMARK 500    THR C  38      -72.61    -28.61                                   
REMARK 500    VAL C 128      -66.27   -128.52                                   
REMARK 500    LEU C 154     -100.04   -115.48                                   
REMARK 500    PRO C 240       50.05   -109.13                                   
REMARK 500    THR C 241     -163.47   -101.52                                   
REMARK 500    GLU C 296      -89.15   -106.75                                   
REMARK 500    ASP C 304     -124.18     56.00                                   
REMARK 500    ASN C 317       53.60   -140.35                                   
REMARK 500    ASP C 337       58.10   -111.38                                   
REMARK 500    TRP C 339      -54.07    -20.73                                   
REMARK 500    ASP C 344       50.87   -100.01                                   
REMARK 500    GLU C 424      -67.72    114.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A  207     PHE A  208                 -139.66                    
REMARK 500 ARG C   27     PRO C   28                 -137.29                    
REMARK 500 PRO C  207     PHE C  208                 -144.85                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG C   6         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 362   OD1                                                    
REMARK 620 2 ASP A 364   OD1  80.5                                              
REMARK 620 3 ASP A 366   OD1  83.3  89.5                                        
REMARK 620 4 THR A 368   O    83.7 156.9  72.0                                  
REMARK 620 5 GLU A 373   OE1 112.2 121.2 146.7  80.4                            
REMARK 620 6 GLU A 373   OE2  99.7  69.2 157.4 130.5  52.4                      
REMARK 620 7 HOH A 766   O   157.6  80.7  84.6 110.1  87.9  84.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 398   OD1                                                    
REMARK 620 2 ASP A 400   OD1  65.7                                              
REMARK 620 3 ASN A 402   OD1  91.7  65.5                                        
REMARK 620 4 THR A 404   O    99.4 146.5  86.1                                  
REMARK 620 5 GLU A 409   OE1  77.1  85.4 150.9 121.9                            
REMARK 620 6 GLU A 409   OE2 110.8 128.8 156.6  84.1  47.2                      
REMARK 620 7 HOH A 784   O   149.1  91.1  97.0 110.6  81.2  67.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 435   OD1                                                    
REMARK 620 2 ASP A 437   OD1  83.2                                              
REMARK 620 3 ASN A 439   OD1  86.5  76.1                                        
REMARK 620 4 TYR A 441   O    93.6 161.9  85.9                                  
REMARK 620 5 GLU A 446   OE1 106.8 127.1 153.6  70.9                            
REMARK 620 6 GLU A 446   OE2  99.8  76.6 151.0 121.5  50.7                      
REMARK 620 7 HOH A 802   O   171.6  89.8  87.4  91.7  81.1  82.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 471   OD1                                                    
REMARK 620 2 ASP A 473   OD1  80.6                                              
REMARK 620 3 ASP A 475   OD1  88.0  79.2                                        
REMARK 620 4 GLN A 477   O    82.3 148.1  73.5                                  
REMARK 620 5 GLU A 482   OE1  95.2  82.2 160.4 126.2                            
REMARK 620 6 GLU A 482   OE2 116.3 131.7 141.2  80.2  52.9                      
REMARK 620 7 HOH A 788   O   163.3  87.1  78.5 103.0  94.3  80.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 362   OD1                                                    
REMARK 620 2 ASP C 364   OD1  77.7                                              
REMARK 620 3 ASP C 366   OD1  85.5  79.0                                        
REMARK 620 4 THR C 368   O    88.0 154.2  78.6                                  
REMARK 620 5 GLU C 373   OE1 114.9 126.6 148.8  78.9                            
REMARK 620 6 GLU C 373   OE2  99.0  76.9 153.8 127.1  50.5                      
REMARK 620 7 HOH C 741   O   161.0  83.7  86.9 107.6  79.7  80.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 603  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 398   OD1                                                    
REMARK 620 2 ASP C 400   OD1  65.7                                              
REMARK 620 3 ASN C 402   OD1  94.1  72.4                                        
REMARK 620 4 THR C 404   O   101.7 153.0  85.5                                  
REMARK 620 5 GLU C 409   OE1  76.6  79.8 152.0 122.0                            
REMARK 620 6 GLU C 409   OE2 112.0 122.7 153.3  83.8  47.6                      
REMARK 620 7 HOH C 752   O   147.9  86.2  91.5 110.2  83.8  69.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 604  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 435   OD1                                                    
REMARK 620 2 ASP C 437   OD1  82.2                                              
REMARK 620 3 ASN C 439   OD1  88.7  74.9                                        
REMARK 620 4 TYR C 441   O    88.3 155.8  82.8                                  
REMARK 620 5 GLU C 446   OE1 106.0 124.5 156.4  79.4                            
REMARK 620 6 GLU C 446   OE2 100.7  71.1 143.0 132.7  53.4                      
REMARK 620 7 HOH C 783   O   168.4  95.9  79.8  88.9  84.5  89.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 605  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 471   OD1                                                    
REMARK 620 2 ASP C 473   OD1  77.7                                              
REMARK 620 3 ASP C 475   OD1  85.1  84.2                                        
REMARK 620 4 GLN C 477   O    86.3 155.7  76.3                                  
REMARK 620 5 GLU C 482   OE1  86.4  75.2 158.9 122.4                            
REMARK 620 6 GLU C 482   OE2 109.1 125.6 148.5  76.8  52.5                      
REMARK 620 7 HOH C 769   O   165.3  91.9  83.5 100.0 101.2  85.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PUJ A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PUJ C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 605                  
DBREF  6U2M A   -7   490  PDB    6U2M     6U2M            -7    490             
DBREF  6U2M C   -7   490  PDB    6U2M     6U2M            -7    490             
SEQRES   1 A  498  MET HIS HIS HIS HIS HIS HIS GLY VAL ARG VAL ILE PRO          
SEQRES   2 A  498  ARG LEU ASP THR LEU ILE LEU VAL LYS ALA MET GLY HIS          
SEQRES   3 A  498  ARG LYS ARG PHE GLY ASN PRO PHE ARG PRO LYS GLU THR          
SEQRES   4 A  498  PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG LYS LEU          
SEQRES   5 A  498  ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR LEU PRO          
SEQRES   6 A  498  MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU MET ASP          
SEQRES   7 A  498  HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP ARG GLU          
SEQRES   8 A  498  PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE ALA GLY          
SEQRES   9 A  498  GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU TYR MET          
SEQRES  10 A  498  ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU LEU PHE          
SEQRES  11 A  498  TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA GLU ALA          
SEQRES  12 A  498  ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS ALA VAL          
SEQRES  13 A  498  ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU ASP ASN          
SEQRES  14 A  498  PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP LEU SER          
SEQRES  15 A  498  THR LEU GLU ILE SER GLY GLY GLY THR GLY GLY SER GLY          
SEQRES  16 A  498  GLY THR GLY GLY SER GLY GLY THR GLY GLY SER MET ALA          
SEQRES  17 A  498  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES  18 A  498  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES  19 A  498  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES  20 A  498  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES  21 A  498  VAL ALA PRO LYS HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES  22 A  498  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES  23 A  498  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES  24 A  498  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  25 A  498  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  26 A  498  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  27 A  498  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO PHE ALA ARG          
SEQRES  28 A  498  ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU          
SEQRES  29 A  498  ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE          
SEQRES  30 A  498  THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY          
SEQRES  31 A  498  GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN          
SEQRES  32 A  498  GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO          
SEQRES  33 A  498  GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR          
SEQRES  34 A  498  ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE          
SEQRES  35 A  498  ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU          
SEQRES  36 A  498  ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP          
SEQRES  37 A  498  GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP          
SEQRES  38 A  498  GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET          
SEQRES  39 A  498  MET THR ALA LYS                                              
SEQRES   1 C  498  MET HIS HIS HIS HIS HIS HIS GLY VAL ARG VAL ILE PRO          
SEQRES   2 C  498  ARG LEU ASP THR LEU ILE LEU VAL LYS ALA MET GLY HIS          
SEQRES   3 C  498  ARG LYS ARG PHE GLY ASN PRO PHE ARG PRO LYS GLU THR          
SEQRES   4 C  498  PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG LYS LEU          
SEQRES   5 C  498  ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR LEU PRO          
SEQRES   6 C  498  MET GLY VAL VAL ARG PRO LEU THR GLU VAL GLU MET ASP          
SEQRES   7 C  498  HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP ARG GLU          
SEQRES   8 C  498  PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE ALA GLY          
SEQRES   9 C  498  GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU TYR MET          
SEQRES  10 C  498  ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU LEU PHE          
SEQRES  11 C  498  TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA GLU ALA          
SEQRES  12 C  498  ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS ALA VAL          
SEQRES  13 C  498  ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU ASP ASN          
SEQRES  14 C  498  PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP LEU SER          
SEQRES  15 C  498  THR LEU GLU ILE SER GLY GLY GLY THR GLY GLY SER GLY          
SEQRES  16 C  498  GLY THR GLY GLY SER GLY GLY THR GLY GLY SER MET ALA          
SEQRES  17 C  498  GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL          
SEQRES  18 C  498  GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY          
SEQRES  19 C  498  PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN          
SEQRES  20 C  498  PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS          
SEQRES  21 C  498  VAL ALA PRO LYS HIS ARG CYS ILE ALA PRO ASP LEU ILE          
SEQRES  22 C  498  GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE          
SEQRES  23 C  498  PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU          
SEQRES  24 C  498  ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP          
SEQRES  25 C  498  TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN          
SEQRES  26 C  498  PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE          
SEQRES  27 C  498  ARG PRO ILE PRO THR TRP ASP GLU TRP PRO PHE ALA ARG          
SEQRES  28 C  498  ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU          
SEQRES  29 C  498  ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE          
SEQRES  30 C  498  THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY          
SEQRES  31 C  498  GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN          
SEQRES  32 C  498  GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO          
SEQRES  33 C  498  GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR          
SEQRES  34 C  498  ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE          
SEQRES  35 C  498  ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU          
SEQRES  36 C  498  ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP          
SEQRES  37 C  498  GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP          
SEQRES  38 C  498  GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET          
SEQRES  39 C  498  MET THR ALA LYS                                              
HET    PUJ  A 600      50                                                       
HET     CL  A 601       1                                                       
HET     CA  A 602       1                                                       
HET     CA  A 603       1                                                       
HET     CA  A 604       1                                                       
HET     CA  A 605       1                                                       
HET    PUJ  C 600      50                                                       
HET     CL  C 601       1                                                       
HET     CA  C 602       1                                                       
HET     CA  C 603       1                                                       
HET     CA  C 604       1                                                       
HET     CA  C 605       1                                                       
HETNAM     PUJ (1E,3S)-1-{10-[2-CARBOXY-5-({2-[2-(HEXYLOXY)                     
HETNAM   2 PUJ  ETHOXY]ETHYL}CARBAMOYL)PHENYL]-7-(3-FLUOROAZETIDIN-1-           
HETNAM   3 PUJ  YL)-5,5-DIMETHYLDIBENZ O[B,E]SILIN-3(5H)-YLIDENE}-3-            
HETNAM   4 PUJ  FLUOROAZETIDIN-1-IUM                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM      CA CALCIUM ION                                                      
HETSYN     PUJ JF635                                                            
FORMUL   3  PUJ    2(C39 H48 F2 N3 O5 SI 1+)                                    
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5   CA    8(CA 2+)                                                     
FORMUL  15  HOH   *203(H2 O)                                                    
HELIX    1 AA1 ARG A    6  ARG A   19  1                                  14    
HELIX    2 AA2 THR A   31  ARG A   36  1                                   6    
HELIX    3 AA3 ASP A   39  ILE A   46  1                                   8    
HELIX    4 AA4 ASN A   49  GLY A   54  1                                   6    
HELIX    5 AA5 LEU A   56  VAL A   60  5                                   5    
HELIX    6 AA6 THR A   65  GLU A   74  1                                  10    
HELIX    7 AA7 PRO A   75  LEU A   77  5                                   3    
HELIX    8 AA8 ASN A   78  ASP A   81  5                                   4    
HELIX    9 AA9 ARG A   82  PHE A   88  1                                   7    
HELIX   10 AB1 PRO A   98  SER A  115  1                                  18    
HELIX   11 AB2 PRO A  131  LEU A  142  1                                  12    
HELIX   12 AB3 LEU A  156  ASN A  161  1                                   6    
HELIX   13 AB4 ASN A  161  LEU A  176  1                                  16    
HELIX   14 AB5 SER A  242  ARG A  247  5                                   6    
HELIX   15 AB6 ILE A  249  ALA A  254  1                                   6    
HELIX   16 AB7 PHE A  278  LEU A  293  1                                  16    
HELIX   17 AB8 ASP A  304  ASN A  317  1                                  14    
HELIX   18 AB9 THR A  347  ASP A  362  1                                  16    
HELIX   19 AC1 THR A  370  LEU A  381  1                                  12    
HELIX   20 AC2 THR A  386  GLU A  396  1                                  11    
HELIX   21 AC3 PHE A  407  MET A  418  1                                  12    
HELIX   22 AC4 GLU A  424  ASP A  435  1                                  12    
HELIX   23 AC5 SER A  443  LEU A  454  1                                  12    
HELIX   24 AC6 THR A  459  ASP A  471  1                                  13    
HELIX   25 AC7 TYR A  480  ALA A  489  1                                  10    
HELIX   26 AC8 ARG C    6  LYS C   20  1                                  15    
HELIX   27 AC9 THR C   31  ARG C   36  1                                   6    
HELIX   28 AD1 THR C   37  ILE C   46  1                                  10    
HELIX   29 AD2 ASN C   49  GLY C   54  1                                   6    
HELIX   30 AD3 LEU C   56  VAL C   60  5                                   5    
HELIX   31 AD4 THR C   65  GLU C   74  1                                  10    
HELIX   32 AD5 PRO C   75  LEU C   77  5                                   3    
HELIX   33 AD6 ASN C   78  ASP C   81  5                                   4    
HELIX   34 AD7 ARG C   82  LEU C   92  1                                  11    
HELIX   35 AD8 PRO C   98  SER C  115  1                                  18    
HELIX   36 AD9 PRO C  131  LEU C  142  1                                  12    
HELIX   37 AE1 LEU C  156  ASN C  161  1                                   6    
HELIX   38 AE2 ASN C  161  THR C  175  1                                  15    
HELIX   39 AE3 SER C  242  ARG C  247  5                                   6    
HELIX   40 AE4 ILE C  249  VAL C  253  5                                   5    
HELIX   41 AE5 PHE C  278  LEU C  293  1                                  16    
HELIX   42 AE6 ASP C  304  ASN C  317  1                                  14    
HELIX   43 AE7 THR C  347  ASP C  362  1                                  16    
HELIX   44 AE8 THR C  370  LEU C  381  1                                  12    
HELIX   45 AE9 THR C  386  GLU C  396  1                                  11    
HELIX   46 AF1 PHE C  407  ASP C  420  1                                  14    
HELIX   47 AF2 GLU C  424  ASP C  435  1                                  12    
HELIX   48 AF3 ALA C  444  LEU C  454  1                                  11    
HELIX   49 AF4 THR C  459  ASP C  471  1                                  13    
HELIX   50 AF5 TYR C  480  THR C  488  1                                   9    
SHEET    1 AA1 8 CYS A 145  GLY A 153  0                                        
SHEET    2 AA1 8 LYS A 119  PRO A 126  1  N  TRP A 123   O  ILE A 150           
SHEET    3 AA1 8 VAL A 321  MET A 327  1  O  PHE A 326   N  LEU A 120           
SHEET    4 AA1 8 VAL A 298  HIS A 303  1  N  ILE A 302   O  ALA A 325           
SHEET    5 AA1 8 VAL A 233  LEU A 236  1  N  LEU A 234   O  VAL A 299           
SHEET    6 AA1 8 CYS A 259  PRO A 262  1  O  ILE A 260   N  PHE A 235           
SHEET    7 AA1 8 GLU A 218  VAL A 225 -1  N  VAL A 225   O  CYS A 259           
SHEET    8 AA1 8 HIS A 211  VAL A 215 -1  N  VAL A 215   O  GLU A 218           
SHEET    1 AA2 2 THR A 368  ILE A 369  0                                        
SHEET    2 AA2 2 ILE A 405  ASP A 406 -1  O  ILE A 405   N  ILE A 369           
SHEET    1 AA3 2 TYR A 441  ILE A 442  0                                        
SHEET    2 AA3 2 VAL A 478  ASN A 479 -1  O  VAL A 478   N  ILE A 442           
SHEET    1 AA4 8 CYS C 145  GLY C 153  0                                        
SHEET    2 AA4 8 LYS C 119  PRO C 126  1  N  LEU C 121   O  LYS C 146           
SHEET    3 AA4 8 VAL C 321  MET C 327  1  O  PHE C 326   N  LEU C 120           
SHEET    4 AA4 8 VAL C 298  HIS C 303  1  N  ILE C 302   O  ALA C 325           
SHEET    5 AA4 8 VAL C 233  LEU C 236  1  N  LEU C 234   O  VAL C 301           
SHEET    6 AA4 8 CYS C 259  PRO C 262  1  O  ILE C 260   N  PHE C 235           
SHEET    7 AA4 8 GLU C 218  VAL C 225 -1  N  VAL C 225   O  CYS C 259           
SHEET    8 AA4 8 HIS C 211  VAL C 215 -1  N  VAL C 215   O  GLU C 218           
SHEET    1 AA5 2 THR C 368  ILE C 369  0                                        
SHEET    2 AA5 2 ILE C 405  ASP C 406 -1  O  ILE C 405   N  ILE C 369           
SHEET    1 AA6 2 TYR C 441  SER C 443  0                                        
SHEET    2 AA6 2 GLN C 477  ASN C 479 -1  O  VAL C 478   N  ILE C 442           
LINK         OD1 ASP A 362                CA    CA A 605     1555   1555  2.30  
LINK         OD1 ASP A 364                CA    CA A 605     1555   1555  2.43  
LINK         OD1 ASP A 366                CA    CA A 605     1555   1555  2.34  
LINK         O   THR A 368                CA    CA A 605     1555   1555  2.38  
LINK         OE1 GLU A 373                CA    CA A 605     1555   1555  2.37  
LINK         OE2 GLU A 373                CA    CA A 605     1555   1555  2.51  
LINK         OD1 ASP A 398                CA    CA A 602     1555   1555  2.58  
LINK         OD1 ASP A 400                CA    CA A 602     1555   1555  2.92  
LINK         OD1 ASN A 402                CA    CA A 602     1555   1555  2.49  
LINK         O   THR A 404                CA    CA A 602     1555   1555  2.45  
LINK         OE1 GLU A 409                CA    CA A 602     1555   1555  2.66  
LINK         OE2 GLU A 409                CA    CA A 602     1555   1555  2.72  
LINK         OD1 ASP A 435                CA    CA A 603     1555   1555  2.37  
LINK         OD1 ASP A 437                CA    CA A 603     1555   1555  2.22  
LINK         OD1 ASN A 439                CA    CA A 603     1555   1555  2.42  
LINK         O   TYR A 441                CA    CA A 603     1555   1555  2.20  
LINK         OE1 GLU A 446                CA    CA A 603     1555   1555  2.57  
LINK         OE2 GLU A 446                CA    CA A 603     1555   1555  2.46  
LINK         OD1 ASP A 471                CA    CA A 604     1555   1555  2.15  
LINK         OD1 ASP A 473                CA    CA A 604     1555   1555  2.39  
LINK         OD1 ASP A 475                CA    CA A 604     1555   1555  2.53  
LINK         O   GLN A 477                CA    CA A 604     1555   1555  2.53  
LINK         OE1 GLU A 482                CA    CA A 604     1555   1555  2.37  
LINK         OE2 GLU A 482                CA    CA A 604     1555   1555  2.57  
LINK        CA    CA A 602                 O   HOH A 784     1555   1555  2.45  
LINK        CA    CA A 603                 O   HOH A 802     1555   1555  2.42  
LINK        CA    CA A 604                 O   HOH A 788     1555   1555  2.07  
LINK        CA    CA A 605                 O   HOH A 766     1555   1555  2.20  
LINK         OD1 ASP C 362                CA    CA C 602     1555   1555  2.33  
LINK         OD1 ASP C 364                CA    CA C 602     1555   1555  2.65  
LINK         OD1 ASP C 366                CA    CA C 602     1555   1555  2.34  
LINK         O   THR C 368                CA    CA C 602     1555   1555  2.33  
LINK         OE1 GLU C 373                CA    CA C 602     1555   1555  2.39  
LINK         OE2 GLU C 373                CA    CA C 602     1555   1555  2.59  
LINK         OD1 ASP C 398                CA    CA C 603     1555   1555  2.50  
LINK         OD1 ASP C 400                CA    CA C 603     1555   1555  2.96  
LINK         OD1 ASN C 402                CA    CA C 603     1555   1555  2.46  
LINK         O   THR C 404                CA    CA C 603     1555   1555  2.47  
LINK         OE1 GLU C 409                CA    CA C 603     1555   1555  2.60  
LINK         OE2 GLU C 409                CA    CA C 603     1555   1555  2.74  
LINK         OD1 ASP C 435                CA    CA C 604     1555   1555  2.39  
LINK         OD1 ASP C 437                CA    CA C 604     1555   1555  2.38  
LINK         OD1 ASN C 439                CA    CA C 604     1555   1555  2.48  
LINK         O   TYR C 441                CA    CA C 604     1555   1555  2.22  
LINK         OE1 GLU C 446                CA    CA C 604     1555   1555  2.47  
LINK         OE2 GLU C 446                CA    CA C 604     1555   1555  2.55  
LINK         OD1 ASP C 471                CA    CA C 605     1555   1555  2.31  
LINK         OD1 ASP C 473                CA    CA C 605     1555   1555  2.33  
LINK         OD1 ASP C 475                CA    CA C 605     1555   1555  2.28  
LINK         O   GLN C 477                CA    CA C 605     1555   1555  2.51  
LINK         OE1 GLU C 482                CA    CA C 605     1555   1555  2.41  
LINK         OE2 GLU C 482                CA    CA C 605     1555   1555  2.59  
LINK        CA    CA C 602                 O   HOH C 741     1555   1555  2.10  
LINK        CA    CA C 603                 O   HOH C 752     1555   1555  2.43  
LINK        CA    CA C 604                 O   HOH C 783     1555   1555  2.46  
LINK        CA    CA C 605                 O   HOH C 769     1555   1555  2.39  
CISPEP   1 GLU A   97    PRO A   98          0        -9.00                     
CISPEP   2 THR A  125    PRO A  126          0         2.42                     
CISPEP   3 ASN A  239    PRO A  240          0         9.91                     
CISPEP   4 GLU C   97    PRO C   98          0        -6.89                     
CISPEP   5 THR C  125    PRO C  126          0        -5.50                     
CISPEP   6 ASN C  239    PRO C  240          0        -1.18                     
SITE     1 AC1 12 THR A  31  PHE A  32  LEU A  44  GLN A  48                    
SITE     2 AC1 12 GLU A  53  GLY A  54  THR A  55  MET A  58                    
SITE     3 AC1 12 VAL A 128  ASN A 155  ASP A 304   CL A 601                    
SITE     1 AC2  4 PRO A  89  ASN A 239  TRP A 305  PUJ A 600                    
SITE     1 AC3  6 ASP A 398  ASP A 400  ASN A 402  THR A 404                    
SITE     2 AC3  6 GLU A 409  HOH A 784                                          
SITE     1 AC4  6 ASP A 435  ASP A 437  ASN A 439  TYR A 441                    
SITE     2 AC4  6 GLU A 446  HOH A 802                                          
SITE     1 AC5  6 ASP A 471  ASP A 473  ASP A 475  GLN A 477                    
SITE     2 AC5  6 GLU A 482  HOH A 788                                          
SITE     1 AC6  6 ASP A 362  ASP A 364  ASP A 366  THR A 368                    
SITE     2 AC6  6 GLU A 373  HOH A 766                                          
SITE     1 AC7 12 THR C  31  LEU C  44  GLN C  48  GLU C  53                    
SITE     2 AC7 12 THR C  55  PRO C  57  MET C  58  VAL C 128                    
SITE     3 AC7 12 ASN C 155  ASN C 239  ASP C 304   CL C 601                    
SITE     1 AC8  4 PRO C  89  ASN C 239  TRP C 305  PUJ C 600                    
SITE     1 AC9  6 ASP C 362  ASP C 364  ASP C 366  THR C 368                    
SITE     2 AC9  6 GLU C 373  HOH C 741                                          
SITE     1 AD1  6 ASP C 398  ASP C 400  ASN C 402  THR C 404                    
SITE     2 AD1  6 GLU C 409  HOH C 752                                          
SITE     1 AD2  6 ASP C 435  ASP C 437  ASN C 439  TYR C 441                    
SITE     2 AD2  6 GLU C 446  HOH C 783                                          
SITE     1 AD3  6 ASP C 471  ASP C 473  ASP C 475  GLN C 477                    
SITE     2 AD3  6 GLU C 482  HOH C 769                                          
CRYST1   92.560   60.662  122.600  90.00  91.02  90.00 P 1 2 1       4          
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      0.010804  0.000000  0.000192        0.00000                         
SCALE2      0.000000  0.016485  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008158        0.00000                         
TER    3711      ALA A 489                                                      
TER    7422      ALA C 489                                                      
MASTER      992    0   12   50   24    0   24    6 7733    2  172   78          
END                                                                             

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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