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LongText Report for: 3E3A-pdb

Name Class
3E3A-pdb
HEADER    OXIDOREDUCTASE                          06-AUG-08   3E3A              
TITLE     THE STRUCTURE OF RV0554 FROM MYCOBACTERIUM TUBERCULOSIS               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POSSIBLE PEROXIDASE BPOC;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NON-HAEM PEROXIDASE, PUTATIVE BROMOPEROXIDASE;              
COMPND   5 EC: 1.11.1.-;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37 RV;                                                      
SOURCE   5 GENE: BPOC, MT0580, RV0554;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPROEX                                    
KEYWDS    ALPHA/BETA HYDROLASE, OXIDOREDUCTASE, PEROXIDASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.JOHNSTON,E.N.BAKER                                                
REVDAT   1   23-JUN-09 3E3A    0                                                
JRNL        AUTH   J.M.JOHNSTON,E.N.BAKER                                       
JRNL        TITL   THE STRUCTURE OF RV0554 FROM M. TUBERCULOSIS                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0078                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26997                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2703                            
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1378                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.79                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 156                          
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4211                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.95000                                             
REMARK   3    B22 (A**2) : 0.08000                                              
REMARK   3    B33 (A**2) : 1.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.360         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.256         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.191         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.869        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4327 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5893 ; 1.680 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 6.049 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   200 ;35.127 ;23.200       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   645 ;17.730 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;18.790 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   652 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3394 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2745 ; 0.731 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4395 ; 1.337 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1582 ; 2.443 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1498 ; 3.785 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     260      6                      
REMARK   3           1     B      1       B     260      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1982 ; 0.310 ; 5.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1982 ; 2.430 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
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   -11        A     9                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1280  11.9250  -0.7580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9917 T22:   0.2869                                     
REMARK   3      T33:   0.0050 T12:  -0.0158                                     
REMARK   3      T13:   0.0317 T23:  -0.0344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6742 L22:   1.8879                                     
REMARK   3      L33:   5.4229 L12:   3.9286                                     
REMARK   3      L13:   2.8323 L23:   0.5837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4600 S12:   0.1304 S13:   0.3491                       
REMARK   3      S21:   0.2169 S22:  -0.3874 S23:   0.0036                       
REMARK   3      S31:   0.1934 S32:   0.3724 S33:  -0.0727                       
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    10        A   126                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6640   1.0020  -8.0320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7435 T22:   0.2276                                     
REMARK   3      T33:   0.0395 T12:  -0.0381                                     
REMARK   3      T13:   0.0078 T23:   0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8506 L22:   1.7503                                     
REMARK   3      L33:   1.9846 L12:   0.0120                                     
REMARK   3      L13:   0.0528 L23:  -0.1753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0038 S12:  -0.0365 S13:   0.0323                       
REMARK   3      S21:   0.3537 S22:   0.0005 S23:   0.1134                       
REMARK   3      S31:   0.0570 S32:   0.0239 S33:   0.0033                       
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   127        A   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.4520   3.1510 -26.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7219 T22:   0.2160                                     
REMARK   3      T33:   0.0467 T12:   0.0168                                     
REMARK   3      T13:   0.0031 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5549 L22:   1.1766                                     
REMARK   3      L33:   2.3461 L12:  -0.1599                                     
REMARK   3      L13:   0.1195 L23:   0.9271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1534 S12:   0.0335 S13:  -0.1084                       
REMARK   3      S21:  -0.0289 S22:  -0.0220 S23:  -0.1055                       
REMARK   3      S31:   0.0184 S32:   0.1663 S33:  -0.1315                       
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   188        A   262                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3140  -9.6260 -13.3950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7535 T22:   0.1967                                     
REMARK   3      T33:   0.0925 T12:  -0.0951                                     
REMARK   3      T13:   0.0238 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8933 L22:   2.4806                                     
REMARK   3      L33:   3.0408 L12:  -0.6812                                     
REMARK   3      L13:   0.1415 L23:   0.0669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1121 S12:   0.0253 S13:  -0.1603                       
REMARK   3      S21:   0.1145 S22:  -0.0095 S23:   0.1957                       
REMARK   3      S31:   0.4959 S32:  -0.2463 S33:  -0.1026                       
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 :   B   -12        B    26                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1040  33.7230 -15.8770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7408 T22:   0.2836                                     
REMARK   3      T33:   0.1319 T12:   0.0140                                     
REMARK   3      T13:  -0.0025 T23:  -0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1845 L22:   2.2557                                     
REMARK   3      L33:   4.1792 L12:  -0.2528                                     
REMARK   3      L13:  -0.8576 L23:   0.5697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0943 S12:   0.1121 S13:  -0.0459                       
REMARK   3      S21:   0.0601 S22:  -0.1409 S23:   0.3526                       
REMARK   3      S31:  -0.3112 S32:  -0.2645 S33:   0.0467                       
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 :   B    27        B   126                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9260  35.0200 -19.4250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7542 T22:   0.2287                                     
REMARK   3      T33:   0.0534 T12:  -0.0119                                     
REMARK   3      T13:  -0.0043 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4815 L22:   1.7712                                     
REMARK   3      L33:   1.6027 L12:   0.4348                                     
REMARK   3      L13:  -0.2860 L23:  -0.2746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0778 S12:  -0.0499 S13:   0.0602                       
REMARK   3      S21:   0.3079 S22:  -0.0861 S23:   0.0702                       
REMARK   3      S31:  -0.2472 S32:   0.0282 S33:   0.0084                       
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 :   B   127        B   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9500  40.1580 -38.1880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7036 T22:   0.2192                                     
REMARK   3      T33:   0.0789 T12:   0.0065                                     
REMARK   3      T13:  -0.0265 T23:   0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5758 L22:   2.2940                                     
REMARK   3      L33:   5.4401 L12:  -0.2403                                     
REMARK   3      L13:  -1.7539 L23:   1.1958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0053 S12:   0.0590 S13:   0.0128                       
REMARK   3      S21:   0.0944 S22:  -0.0895 S23:   0.2908                       
REMARK   3      S31:   0.0986 S32:  -0.4083 S33:   0.0841                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   188        B   261                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3020  31.7890 -24.8000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6564 T22:   0.2574                                     
REMARK   3      T33:   0.0732 T12:  -0.0320                                     
REMARK   3      T13:  -0.0266 T23:   0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5495 L22:   3.2620                                     
REMARK   3      L33:   2.8729 L12:   0.5670                                     
REMARK   3      L13:  -0.2797 L23:  -1.0646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.0519 S13:  -0.0426                       
REMARK   3      S21:  -0.0089 S22:  -0.1780 S23:  -0.3822                       
REMARK   3      S31:   0.0465 S32:   0.3689 S33:   0.1231                       
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          
REMARK   4                                                                      
REMARK   4 3E3A COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB048820.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.92                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97907                            
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29742                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE PH 4.92, 7.5%        
REMARK 280  MPD, VAPOR DIFFUSION, TEMPERATURE 292K                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.35200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.08250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.94500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.08250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.35200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.94500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     TYR A   -28                                                      
REMARK 465     TYR A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     ASP A   -20                                                      
REMARK 465     TYR A   -19                                                      
REMARK 465     ASP A   -18                                                      
REMARK 465     ILE A   -17                                                      
REMARK 465     PRO A   -16                                                      
REMARK 465     THR A   -15                                                      
REMARK 465     THR A   -14                                                      
REMARK 465     GLU A   -13                                                      
REMARK 465     ASN A   -12                                                      
REMARK 465     MET B   -30                                                      
REMARK 465     SER B   -29                                                      
REMARK 465     TYR B   -28                                                      
REMARK 465     TYR B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     HIS B   -25                                                      
REMARK 465     HIS B   -24                                                      
REMARK 465     HIS B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     ASP B   -20                                                      
REMARK 465     TYR B   -19                                                      
REMARK 465     ASP B   -18                                                      
REMARK 465     ILE B   -17                                                      
REMARK 465     PRO B   -16                                                      
REMARK 465     THR B   -15                                                      
REMARK 465     THR B   -14                                                      
REMARK 465     ALA B   262                                                      
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   O    HOH B   368     O    HOH B   370              2.15            
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    ASP A   8   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    LEU A 148   CA  -  CB  -  CG  ANGL. DEV. =  16.4 DEGREES          
REMARK 500    ARG B  21   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG B  21   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP B 117   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 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    PRO A  -3      -19.12    -43.94                                   
REMARK 500    ASN A  48      143.56    -37.45                                   
REMARK 500    SER A  87     -118.35     53.72                                   
REMARK 500    ASP A 117     -179.44    -65.85                                   
REMARK 500    HIS B  31      -46.34   -130.79                                   
REMARK 500    SER B  87     -116.32     59.84                                   
REMARK 500    PRO B 188       90.79    -61.13                                   
REMARK 500    LEU B 240       33.95    -96.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 265                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 263                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RV0554   RELATED DB: TARGETDB                            
DBREF  3E3A A   -5   262  UNP    O06420   O06420_MYCTU     1    262             
DBREF  3E3A B   -5   262  UNP    O06420   O06420_MYCTU     1    262             
SEQADV 3E3A MET A  -30  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A SER A  -29  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR A  -28  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR A  -27  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -26  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -25  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -24  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -23  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -22  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS A  -21  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP A  -20  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR A  -19  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP A  -18  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ILE A  -17  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PRO A  -16  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A THR A  -15  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A THR A  -14  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLU A  -13  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASN A  -12  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A LEU A  -11  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR A  -10  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PHE A   -9  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLN A   -8  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLY A   -7  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ALA A   -6  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP A   -4  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PRO A   -3  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLU A   -2  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PHE A   -1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ARG A    0  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A VAL A    1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A MET B  -30  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A SER B  -29  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR B  -28  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR B  -27  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -26  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -25  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -24  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -23  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -22  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A HIS B  -21  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP B  -20  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR B  -19  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP B  -18  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ILE B  -17  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PRO B  -16  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A THR B  -15  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A THR B  -14  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLU B  -13  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASN B  -12  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A LEU B  -11  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A TYR B  -10  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PHE B   -9  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLN B   -8  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLY B   -7  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ALA B   -6  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ASP B   -4  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PRO B   -3  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A GLU B   -2  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A PHE B   -1  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A ARG B    0  UNP  O06420              EXPRESSION TAG                 
SEQADV 3E3A VAL B    1  UNP  O06420              EXPRESSION TAG                 
SEQRES   1 A  293  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 A  293  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 A  293  ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP          
SEQRES   4 A  293  ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG          
SEQRES   5 A  293  GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO          
SEQRES   6 A  293  ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP          
SEQRES   7 A  293  ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE          
SEQRES   8 A  293  THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE          
SEQRES   9 A  293  GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL          
SEQRES  10 A  293  SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL          
SEQRES  11 A  293  ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR          
SEQRES  12 A  293  ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS          
SEQRES  13 A  293  ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO          
SEQRES  14 A  293  PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE          
SEQRES  15 A  293  SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP          
SEQRES  16 A  293  TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR          
SEQRES  17 A  293  PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR          
SEQRES  18 A  293  ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL          
SEQRES  19 A  293  LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO          
SEQRES  20 A  293  TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY          
SEQRES  21 A  293  ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE          
SEQRES  22 A  293  PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS          
SEQRES  23 A  293  PHE PHE ALA SER VAL LYS ALA                                  
SEQRES   1 B  293  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP          
SEQRES   2 B  293  ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET          
SEQRES   3 B  293  ASP PRO GLU PHE ARG VAL ILE ASN LEU ALA TYR ASP ASP          
SEQRES   4 B  293  ASN GLY THR GLY ASP PRO VAL VAL PHE ILE ALA GLY ARG          
SEQRES   5 B  293  GLY GLY ALA GLY ARG THR TRP HIS PRO HIS GLN VAL PRO          
SEQRES   6 B  293  ALA PHE LEU ALA ALA GLY TYR ARG CYS ILE THR PHE ASP          
SEQRES   7 B  293  ASN ARG GLY ILE GLY ALA THR GLU ASN ALA GLU GLY PHE          
SEQRES   8 B  293  THR THR GLN THR MET VAL ALA ASP THR ALA ALA LEU ILE          
SEQRES   9 B  293  GLU THR LEU ASP ILE ALA PRO ALA ARG VAL VAL GLY VAL          
SEQRES  10 B  293  SER MET GLY ALA PHE ILE ALA GLN GLU LEU MET VAL VAL          
SEQRES  11 B  293  ALA PRO GLU LEU VAL SER SER ALA VAL LEU MET ALA THR          
SEQRES  12 B  293  ARG GLY ARG LEU ASP ARG ALA ARG GLN PHE PHE ASN LYS          
SEQRES  13 B  293  ALA GLU ALA GLU LEU TYR ASP SER GLY VAL GLN LEU PRO          
SEQRES  14 B  293  PRO THR TYR ASP ALA ARG ALA ARG LEU LEU GLU ASN PHE          
SEQRES  15 B  293  SER ARG LYS THR LEU ASN ASP ASP VAL ALA VAL GLY ASP          
SEQRES  16 B  293  TRP ILE ALA MET PHE SER MET TRP PRO ILE LYS SER THR          
SEQRES  17 B  293  PRO GLY LEU ARG CYS GLN LEU ASP CYS ALA PRO GLN THR          
SEQRES  18 B  293  ASN ARG LEU PRO ALA TYR ARG ASN ILE ALA ALA PRO VAL          
SEQRES  19 B  293  LEU VAL ILE GLY PHE ALA ASP ASP VAL VAL THR PRO PRO          
SEQRES  20 B  293  TYR LEU GLY ARG GLU VAL ALA ASP ALA LEU PRO ASN GLY          
SEQRES  21 B  293  ARG TYR LEU GLN ILE PRO ASP ALA GLY HIS LEU GLY PHE          
SEQRES  22 B  293  PHE GLU ARG PRO GLU ALA VAL ASN THR ALA MET LEU LYS          
SEQRES  23 B  293  PHE PHE ALA SER VAL LYS ALA                                  
HET    ACT  A 264       4                                                       
HET    MPD  A 265       8                                                       
HET    ACT  B 263       4                                                       
HETNAM     ACT ACETATE ION                                                      
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
FORMUL   3  ACT    2(C2 H3 O2 1-)                                               
FORMUL   4  MPD    C6 H14 O2                                                    
FORMUL   6  HOH   *215(H2 O)                                                    
HELIX    1   1 ALA A   24  HIS A   29  5                                   6    
HELIX    2   2 GLN A   32  ALA A   39  1                                   8    
HELIX    3   3 ILE A   51  GLU A   55  5                                   5    
HELIX    4   4 THR A   61  LEU A   76  1                                  16    
HELIX    5   5 SER A   87  ALA A  100  1                                  14    
HELIX    6   6 ASP A  117  SER A  133  1                                  17    
HELIX    7   7 PRO A  138  PHE A  151  1                                  14    
HELIX    8   8 SER A  152  ASN A  157  1                                   6    
HELIX    9   9 ASP A  158  TRP A  172  1                                  15    
HELIX   10  10 THR A  177  ASP A  185  1                                   9    
HELIX   11  11 ARG A  192  ARG A  197  1                                   6    
HELIX   12  12 PRO A  215  LEU A  226  1                                  12    
HELIX   13  13 LEU A  240  ARG A  245  1                                   6    
HELIX   14  14 ARG A  245  SER A  259  1                                  15    
HELIX   15  15 ALA B   24  HIS B   29  5                                   6    
HELIX   16  16 HIS B   31  ALA B   39  1                                   9    
HELIX   17  17 ILE B   51  GLU B   55  5                                   5    
HELIX   18  18 THR B   61  LEU B   76  1                                  16    
HELIX   19  19 SER B   87  ALA B  100  1                                  14    
HELIX   20  20 ASP B  117  SER B  133  1                                  17    
HELIX   21  21 PRO B  138  PHE B  151  1                                  14    
HELIX   22  22 SER B  152  ASN B  157  1                                   6    
HELIX   23  23 ASP B  158  TRP B  172  1                                  15    
HELIX   24  24 THR B  177  LEU B  184  1                                   8    
HELIX   25  25 ARG B  192  ILE B  199  5                                   8    
HELIX   26  26 PRO B  215  LEU B  226  1                                  12    
HELIX   27  27 LEU B  240  ARG B  245  1                                   6    
HELIX   28  28 ARG B  245  VAL B  260  1                                  16    
SHEET    1   A 8 TYR A -10  GLN A  -8  0                                        
SHEET    2   A 8 ASN A   3  ASN A   9 -1  O  LEU A   4   N  PHE A  -9           
SHEET    3   A 8 TYR A  41  PHE A  46 -1  O  THR A  45   N  ASP A   7           
SHEET    4   A 8 ASP A  13  ILE A  18  1  N  VAL A  15   O  ILE A  44           
SHEET    5   A 8 ALA A  81  VAL A  86  1  O  ARG A  82   N  VAL A  16           
SHEET    6   A 8 VAL A 104  MET A 110  1  O  VAL A 108   N  VAL A  83           
SHEET    7   A 8 VAL A 203  PHE A 208  1  O  ILE A 206   N  LEU A 109           
SHEET    8   A 8 GLY A 229  ILE A 234  1  O  ILE A 234   N  GLY A 207           
SHEET    1   B 8 LEU B -11  GLN B  -8  0                                        
SHEET    2   B 8 ASN B   3  ASN B   9 -1  O  TYR B   6   N  LEU B -11           
SHEET    3   B 8 TYR B  41  PHE B  46 -1  O  THR B  45   N  ASP B   7           
SHEET    4   B 8 ASP B  13  ILE B  18  1  N  VAL B  15   O  ILE B  44           
SHEET    5   B 8 ALA B  81  VAL B  86  1  O  VAL B  84   N  ILE B  18           
SHEET    6   B 8 VAL B 104  MET B 110  1  O  VAL B 108   N  VAL B  83           
SHEET    7   B 8 VAL B 203  PHE B 208  1  O  LEU B 204   N  LEU B 109           
SHEET    8   B 8 GLY B 229  ILE B 234  1  O  LEU B 232   N  GLY B 207           
CISPEP   1 ALA A   79    PRO A   80          0        -3.51                     
CISPEP   2 ALA B   79    PRO B   80          0        -3.34                     
SITE     1 AC1  3 ARG A 146  LEU A 240  PHE A 243                               
SITE     1 AC2  1 MET B  -5                                                     
CRYST1   48.704   97.890  146.165  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020532  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010216  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006842        0.00000                         
TER    2101      ALA A 262                                                      
TER    4213      LYS B 261                                                      
MASTER      501    0    3   28   16    0    2    6 4442    2   16   46          
END                                                                             

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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.
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