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LongText Report for: 1MO2-pdb

Name Class
1MO2-pdb
HEADER    TRANSFERASE                             05-SEP-02   1MO2              
TITLE     THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE                
TITLE    2 (DEBS TE), PH 8.5                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ERYTHRONOLIDE SYNTHASE, MODULES 5 AND 6;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: THIOESTERASE DOMAIN;                                       
COMPND   5 SYNONYM: 6-DEOXYERYTHRONOLIDE B SYNTHASE III; DEBS 3; DEBS           
COMPND   6 TE; ERYTHRONOLIDE SYNTHASE III;                                      
COMPND   7 EC: 2.3.1.94;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;                    
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 GENE: ERYA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21C                                    
KEYWDS    THIOESTERASE, POLYKETIDE SYNTHASE, OPEN SUBSTRATE CHANNEL,            
KEYWDS   2 TE, PKS,  ALPHA BETA HYDROLASE, 6-DEOXYERYTHRONOLIDE,                
KEYWDS   3 PICROMYCIN, PIKROMYCIN, ERYTHROMYCIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD                           
REVDAT   1   04-FEB-03 1MO2    0                                                
JRNL        AUTH   S.-C.TSAI,H.LU,D.E.CANE,C.KHOSLA,R.M.STROUD                  
JRNL        TITL   INSIGHTS INTO CHANNEL ARCHITECTURE AND SUBSTRATE             
JRNL        TITL 2 SPECIFICITY FROM CRYSTAL STRUCTURES OF TWO                   
JRNL        TITL 3 MACROCYCLE-FORMING THIOESTERASES OF MODULAR                  
JRNL        TITL 4 POLYKETIDE SYNTHASES                                         
JRNL        REF    BIOCHEMISTRY                  V.  41 12598 2002              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 3.00 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1                                           
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22595                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1223                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1531                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 3832                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.40000                                              
REMARK   3    B22 (A**2) : -1.03000                                             
REMARK   3    B33 (A**2) : -3.37000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.893                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.855                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3880 ; 0.043 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5304 ; 3.562 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   498 ;12.597 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   580 ; 0.240 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3058 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2049 ; 0.336 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   179 ; 0.241 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   326 ; 0.748 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.570 ; 0.200       
REMARK   3   SYMMETRY H-BOND 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):  2494 ; 1.318 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3984 ; 2.470 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1386 ; 4.183 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1320 ; 6.983 ; 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 : 0                                 
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    26        A   160                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2379  50.7432  63.4611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2426 T22:   0.0783                                     
REMARK   3      T33:   0.1628 T12:  -0.0073                                     
REMARK   3      T13:  -0.0176 T23:  -0.0491                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9796 L22:   4.0227                                     
REMARK   3      L33:   8.0957 L12:   0.5264                                     
REMARK   3      L13:  -0.3124 L23:  -3.7010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1379 S12:  -0.2848 S13:   0.1926                       
REMARK   3      S21:   0.6558 S22:   0.0078 S23:   0.1722                       
REMARK   3      S31:  -0.7097 S32:  -0.0596 S33:  -0.1457                       
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   161        A   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5046  39.5223  62.0341              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2792 T22:   0.3817                                     
REMARK   3      T33:   0.3010 T12:   0.1346                                     
REMARK   3      T13:   0.0090 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9896 L22:   5.2681                                     
REMARK   3      L33:   6.5389 L12:  -0.3886                                     
REMARK   3      L13:   0.1494 L23:  -0.8359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0683 S12:  -0.1288 S13:  -0.4295                       
REMARK   3      S21:   0.1066 S22:  -0.0219 S23:  -0.6599                       
REMARK   3      S31:   0.9077 S32:   1.3865 S33:  -0.0464                       
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   221        A   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.5248  37.2728  46.4705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4539 T22:   0.3279                                     
REMARK   3      T33:   0.3903 T12:  -0.0486                                     
REMARK   3      T13:   0.1565 T23:  -0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.4036 L22:  14.0993                                     
REMARK   3      L33:  11.4652 L12:  -0.3289                                     
REMARK   3      L13:  -2.4054 L23:   0.7738                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8356 S12:  -0.6464 S13:  -2.3100                       
REMARK   3      S21:  -1.9777 S22:   0.6412 S23:  -1.2321                       
REMARK   3      S31:   0.9234 S32:   1.6924 S33:   0.1944                       
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   251        A   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7673  50.9046  43.2633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3398 T22:   0.1333                                     
REMARK   3      T33:   0.1023 T12:   0.0641                                     
REMARK   3      T13:   0.0910 T23:   0.0594                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0159 L22:   8.9776                                     
REMARK   3      L33:   7.2555 L12:  -1.6598                                     
REMARK   3      L13:  -1.0714 L23:  -3.1028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3739 S12:  -0.3891 S13:   0.5271                       
REMARK   3      S21:  -0.7895 S22:  -0.6408 S23:  -0.8896                       
REMARK   3      S31:   0.5868 S32:   0.9843 S33:   0.2668                       
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    26        B   160                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8513  32.3085  98.4186              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0267 T22:   0.1633                                     
REMARK   3      T33:   0.1072 T12:   0.0327                                     
REMARK   3      T13:   0.0509 T23:   0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3949 L22:   2.4245                                     
REMARK   3      L33:   6.1430 L12:  -0.1336                                     
REMARK   3      L13:   2.2441 L23:   0.2726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1171 S12:   0.2069 S13:   0.0802                       
REMARK   3      S21:  -0.4922 S22:   0.0540 S23:  -0.1221                       
REMARK   3      S31:   0.1775 S32:   0.0338 S33:  -0.1711                       
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   161        B   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3030  35.2171  99.5533              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2971 T22:   0.5326                                     
REMARK   3      T33:   0.3385 T12:   0.1382                                     
REMARK   3      T13:  -0.0030 T23:  -0.0551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7237 L22:   3.6171                                     
REMARK   3      L33:   7.7213 L12:   1.2652                                     
REMARK   3      L13:   3.2158 L23:   0.2943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1019 S12:  -0.4187 S13:   0.3179                       
REMARK   3      S21:  -0.6052 S22:   0.2133 S23:   1.2628                       
REMARK   3      S31:  -0.4100 S32:  -1.9267 S33:  -0.1114                       
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   221        B   250                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0816  33.7765 115.0855              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2892 T22:   0.7483                                     
REMARK   3      T33:   0.6294 T12:   0.0210                                     
REMARK   3      T13:   0.1069 T23:  -0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.8375 L22:   5.0728                                     
REMARK   3      L33:  13.3263 L12:   7.4091                                     
REMARK   3      L13:  -4.5828 L23:   2.6574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4684 S12:  -0.6468 S13:   0.9059                       
REMARK   3      S21:   0.3249 S22:  -0.4265 S23:   2.6659                       
REMARK   3      S31:  -0.8170 S32:  -2.1137 S33:  -0.0419                       
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   251        B   280                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.3683  43.5914 118.4553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0497 T22:   0.3977                                     
REMARK   3      T33:   0.2695 T12:   0.0456                                     
REMARK   3      T13:   0.0695 T23:  -0.0876                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8040 L22:   7.8034                                     
REMARK   3      L33:   3.0840 L12:   0.0251                                     
REMARK   3      L13:   1.2589 L23:   2.6878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1319 S12:  -0.5668 S13:   0.9318                       
REMARK   3      S21:  -0.0126 S22:  -0.4000 S23:   0.0956                       
REMARK   3      S31:  -0.4596 S32:  -0.9797 S33:   0.5319                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1MO2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PRAGUE ON 19-SEP-2002.              
REMARK 100 THE RCSB ID CODE IS RCSB017046.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-1999                        
REMARK 200  TEMPERATURE           (KELVIN) : 190.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26440                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 13.200                             
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 1KEZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 79.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, BICINE, MAGNESIUM               
REMARK 280  CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP AT 277K             
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   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-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       40.25000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.25000            
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     TYR A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     ASP A   192                                                      
REMARK 465     ARG A   193                                                      
REMARK 465     GLU A   194                                                      
REMARK 465     THR A   195                                                      
REMARK 465     GLY A   281                                                      
REMARK 465     ASN A   282                                                      
REMARK 465     SER A   283                                                      
REMARK 465     SER A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     VAL A   286                                                      
REMARK 465     ASP A   287                                                      
REMARK 465     LYS A   288                                                      
REMARK 465     LEU A   289                                                      
REMARK 465     ALA A   290                                                      
REMARK 465     ALA A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     ASP B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     SER B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     ARG B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     TYR B    22                                                      
REMARK 465     ARG B    23                                                      
REMARK 465     GLN B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     ASP B   192                                                      
REMARK 465     ARG B   193                                                      
REMARK 465     GLU B   194                                                      
REMARK 465     THR B   195                                                      
REMARK 465     GLY B   281                                                      
REMARK 465     ASN B   282                                                      
REMARK 465     SER B   283                                                      
REMARK 465     SER B   284                                                      
REMARK 465     SER B   285                                                      
REMARK 465     VAL B   286                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     LYS B   288                                                      
REMARK 465     LEU B   289                                                      
REMARK 465     ALA B   290                                                      
REMARK 465     ALA B   291                                                      
REMARK 465     ALA B   292                                                      
REMARK 465     LEU B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N    THR A   261     N    HIS B   259     2564     2.19            
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),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 233   CG    PRO A 233   CB     0.106                        
REMARK 500    PHE A 260   C     PHE A 260   CA     0.084                        
REMARK 500    ILE B 128   CB    ILE B 128   CA     0.059                        
REMARK 500    PRO B 233   CG    PRO B 233   CB     0.058                        
REMARK 500    MET B 234   CE    MET B 234   SD     0.064                        
REMARK 500    HIS B 259   CA    HIS B 259   N     -0.057                        
REMARK 500    THR B 261   CB    THR B 261   CA     0.081                        
REMARK 500    MET B 262   CE    MET B 262   SD    -0.074                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  29   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    GLY A  64   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    GLN A 176   N   -  CA  -  C   ANGL. DEV. =-12.8 DEGREES           
REMARK 500    LEU A 190   N   -  CA  -  C   ANGL. DEV. =-11.1 DEGREES           
REMARK 500    PRO A 247   N   -  CA  -  C   ANGL. DEV. =-10.3 DEGREES           
REMARK 500    HIS A 259   N   -  CA  -  C   ANGL. DEV. = 14.0 DEGREES           
REMARK 500    PHE A 260   N   -  CA  -  C   ANGL. DEV. = 19.0 DEGREES           
REMARK 500    VAL B 138   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    HIS B 259   N   -  CA  -  C   ANGL. DEV. = 10.2 DEGREES           
REMARK 500    HIS B 266   N   -  CA  -  C   ANGL. DEV. =-13.9 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 142      -51.49    134.64                                   
REMARK 500    TYR A 171      160.06     63.64                                   
REMARK 500    ASP A 177      -33.99     73.02                                   
REMARK 500    ARG A 197      153.36     74.03                                   
REMARK 500    PHE A 248      129.93     80.81                                   
REMARK 500    HIS A 259     -127.50    172.73                                   
REMARK 500    SER B  80      147.02     50.21                                   
REMARK 500    SER B 142      -60.55     63.76                                   
REMARK 500    TYR B 171      153.08     65.95                                   
REMARK 500    ASP B 177      -67.93     76.45                                   
REMARK 500    ARG B 197      127.95     64.01                                   
REMARK 500    SER B 241     -101.66   -164.38                                   
REMARK 500    PHE B 248      155.17     54.18                                   
REMARK 500    THR B 261     -116.10    175.98                                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KEZ   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM 6-DEOXYERYTHRONOLIDE SYNTHASE               
REMARK 900 (DEBS TE), PH 7.2                                                    
REMARK 900 RELATED ID: 1MN6   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS TE), PH 7.6                                                    
REMARK 900 RELATED ID: 1MNA   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS TE), PH 8.0                                                    
REMARK 900 RELATED ID: 1MNQ   RELATED DB: PDB                                   
REMARK 900 THIOESTERASE DOMAIN FROM PICROMYCIN POLYKETIDE SYNTHASE              
REMARK 900 (PICS TE), PH 8.4                                                    
DBREF  1MO2 A    4   283  SWS    Q03133   ERY3_SACER    2893   3172             
DBREF  1MO2 B    4   283  SWS    Q03133   ERY3_SACER    2893   3172             
SEQADV 1MO2 MET A    1       Q03133              INSERTION                      
SEQADV 1MO2 ALA A    2       Q03133              INSERTION                      
SEQADV 1MO2 SER A    3       Q03133              INSERTION                      
SEQADV 1MO2 SER A  284       Q03133              INSERTION                      
SEQADV 1MO2 SER A  285       Q03133              INSERTION                      
SEQADV 1MO2 VAL A  286       Q03133              INSERTION                      
SEQADV 1MO2 ASP A  287       Q03133              INSERTION                      
SEQADV 1MO2 LYS A  288       Q03133              INSERTION                      
SEQADV 1MO2 LEU A  289       Q03133              INSERTION                      
SEQADV 1MO2 ALA A  290       Q03133              INSERTION                      
SEQADV 1MO2 ALA A  291       Q03133              INSERTION                      
SEQADV 1MO2 ALA A  292       Q03133              INSERTION                      
SEQADV 1MO2 LEU A  293       Q03133              INSERTION                      
SEQADV 1MO2 GLU A  294       Q03133              INSERTION                      
SEQADV 1MO2 MET B    1       Q03133              INSERTION                      
SEQADV 1MO2 ALA B    2       Q03133              INSERTION                      
SEQADV 1MO2 SER B    3       Q03133              INSERTION                      
SEQADV 1MO2 SER B  284       Q03133              INSERTION                      
SEQADV 1MO2 SER B  285       Q03133              INSERTION                      
SEQADV 1MO2 VAL B  286       Q03133              INSERTION                      
SEQADV 1MO2 ASP B  287       Q03133              INSERTION                      
SEQADV 1MO2 LYS B  288       Q03133              INSERTION                      
SEQADV 1MO2 LEU B  289       Q03133              INSERTION                      
SEQADV 1MO2 ALA B  290       Q03133              INSERTION                      
SEQADV 1MO2 ALA B  291       Q03133              INSERTION                      
SEQADV 1MO2 ALA B  292       Q03133              INSERTION                      
SEQADV 1MO2 LEU B  293       Q03133              INSERTION                      
SEQADV 1MO2 GLU B  294       Q03133              INSERTION                      
SEQRES   1 A  294  MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU          
SEQRES   2 A  294  ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY          
SEQRES   3 A  294  VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA          
SEQRES   4 A  294  GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP          
SEQRES   5 A  294  GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO          
SEQRES   6 A  294  GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA          
SEQRES   7 A  294  ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA          
SEQRES   8 A  294  LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO          
SEQRES   9 A  294  GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA          
SEQRES  10 A  294  ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR          
SEQRES  11 A  294  GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA          
SEQRES  12 A  294  GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU          
SEQRES  13 A  294  ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP          
SEQRES  14 A  294  VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP          
SEQRES  15 A  294  LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR          
SEQRES  16 A  294  VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA          
SEQRES  17 A  294  TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR          
SEQRES  18 A  294  GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET          
SEQRES  19 A  294  GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO          
SEQRES  20 A  294  PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE          
SEQRES  21 A  294  THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS          
SEQRES  22 A  294  ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL          
SEQRES  23 A  294  ASP LYS LEU ALA ALA ALA LEU GLU                              
SEQRES   1 B  294  MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU          
SEQRES   2 B  294  ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY          
SEQRES   3 B  294  VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA          
SEQRES   4 B  294  GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP          
SEQRES   5 B  294  GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO          
SEQRES   6 B  294  GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA          
SEQRES   7 B  294  ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA          
SEQRES   8 B  294  LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO          
SEQRES   9 B  294  GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA          
SEQRES  10 B  294  ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR          
SEQRES  11 B  294  GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA          
SEQRES  12 B  294  GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU          
SEQRES  13 B  294  ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP          
SEQRES  14 B  294  VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP          
SEQRES  15 B  294  LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR          
SEQRES  16 B  294  VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA          
SEQRES  17 B  294  TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR          
SEQRES  18 B  294  GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET          
SEQRES  19 B  294  GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO          
SEQRES  20 B  294  PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE          
SEQRES  21 B  294  THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS          
SEQRES  22 B  294  ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL          
SEQRES  23 B  294  ASP LYS LEU ALA ALA ALA LEU GLU                              
FORMUL   3  HOH   *56(H2 O1)                                                    
HELIX    1   1 GLY A   29  ASP A   43  1                                  15    
HELIX    2   2 GLY A   81  GLU A   84  5                                   4    
HELIX    3   3 PHE A   85  ARG A   93  1                                   9    
HELIX    4   4 SER A  115  THR A  130  1                                  16    
HELIX    5   5 GLY A  144  GLY A  159  1                                  16    
HELIX    6   6 GLY A  174  ALA A  188  1                                  15    
HELIX    7   7 ASP A  199  TRP A  216  1                                  18    
HELIX    8   8 HIS A  266  GLY A  279  1                                  14    
HELIX    9   9 GLY B   29  ASP B   43  1                                  15    
HELIX   10  10 GLY B   81  GLU B   84  5                                   4    
HELIX   11  11 PHE B   85  ARG B   93  1                                   9    
HELIX   12  12 SER B  115  THR B  130  1                                  16    
HELIX   13  13 GLY B  144  ARG B  158  1                                  15    
HELIX   14  14 GLY B  174  THR B  187  1                                  14    
HELIX   15  15 ALA B  188  LEU B  190  5                                   3    
HELIX   16  16 ASP B  199  GLN B  215  1                                  17    
HELIX   17  17 HIS B  266  GLY B  280  1                                  15    
SHEET    1   A 2 HIS A  47  PHE A  48  0                                        
SHEET    2   A 2 LEU A 112  PRO A 113  1  O  LEU A 112   N  PHE A  48           
SHEET    1   B 7 VAL A  59  ALA A  62  0                                        
SHEET    2   B 7 VAL A  98  VAL A 101 -1  O  VAL A  98   N  ALA A  62           
SHEET    3   B 7 THR A  69  CYS A  73  1  N  CYS A  72   O  VAL A 101           
SHEET    4   B 7 PHE A 136  GLY A 140  1  O  ALA A 139   N  CYS A  73           
SHEET    5   B 7 GLY A 164  ASP A 169  1  O  ILE A 168   N  GLY A 140           
SHEET    6   B 7 THR A 225  SER A 229  1  O  VAL A 228   N  LEU A 167           
SHEET    7   B 7 ASP A 251  ALA A 254  1  O  VAL A 253   N  SER A 229           
SHEET    1   C 2 HIS B  47  PHE B  48  0                                        
SHEET    2   C 2 LEU B 112  PRO B 113  1  O  LEU B 112   N  PHE B  48           
SHEET    1   D 7 VAL B  59  ALA B  62  0                                        
SHEET    2   D 7 VAL B  98  VAL B 101 -1  O  VAL B  98   N  ALA B  62           
SHEET    3   D 7 THR B  69  CYS B  73  1  N  CYS B  72   O  VAL B 101           
SHEET    4   D 7 PHE B 136  GLY B 140  1  O  VAL B 137   N  ILE B  71           
SHEET    5   D 7 GLY B 164  LEU B 167  1  O  VAL B 166   N  GLY B 140           
SHEET    6   D 7 THR B 225  SER B 229  1  O  VAL B 228   N  LEU B 167           
SHEET    7   D 7 ASP B 251  ALA B 254  1  O  ASP B 251   N  LEU B 227           
CRYST1   80.500  102.500  156.500  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      0.012422  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009756  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006390        0.00000                         
TER    1888      GLY A 280                                                      
TER    3776      GLY B 280                                                      
MASTER      556    0    0   17   18    0    0    6 3830    2    0   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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