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LongText Report for: 6t6z-pdb

Name Class
6t6z-pdb
HEADER    HYDROLASE                               20-OCT-19   6T6Z              
TITLE     STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH A         
TITLE    2 BOTTROMYCIN A2 DERIVATIVE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BOTH;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. BC16019;                       
SOURCE   3 ORGANISM_TAXID: 1109705;                                             
SOURCE   4 GENE: BOTH;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2                                 
KEYWDS    BOTTROMYCIN, RIPP, EPIMERASE, ABH, HYDROLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KOEHNKE,A.SIKANDAR                                                  
REVDAT   1   15-JUL-20 6T6Z    0                                                
JRNL        AUTH   A.SIKANDAR,L.FRANZ,S.ADAM,J.SANTOS-ABERTURAS,L.HORBAL,       
JRNL        AUTH 2 A.LUZHETSKYY,A.W.TRUMAN,O.V.KALININA,J.KOEHNKE               
JRNL        TITL   THE BOTTROMYCIN EPIMERASE BOTH DEFINES A GROUP OF ATYPICAL   
JRNL        TITL 2 ALPHA / BETA-HYDROLASE-FOLD ENZYMES.                         
JRNL        REF    NAT.CHEM.BIOL.                             2020              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   32601484                                                     
JRNL        DOI    10.1038/S41589-020-0569-Y                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,         
REMARK   1  AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,     
REMARK   1  AUTH 3 P.H.ZWART,P.D.ADAMS                                          
REMARK   1  TITL   TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH 
REMARK   1  TITL 2 PHENIX.REFINE.                                               
REMARK   1  REF    ACTA CRYSTALLOGR. D BIOL.     V.  68   352 2012              
REMARK   1  REF  2 CRYSTALLOGR.                                                 
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   22505256                                                     
REMARK   1  DOI    10.1107/S0907444912001308                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY                      
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26135                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1295                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.5200 -  3.5400    0.97     2874   138  0.1636 0.1980        
REMARK   3     2  3.5400 -  2.8100    1.00     2808   143  0.1617 0.1864        
REMARK   3     3  2.8100 -  2.4500    1.00     2795   132  0.1543 0.1881        
REMARK   3     4  2.4500 -  2.2300    0.99     2765   132  0.1538 0.1965        
REMARK   3     5  2.2300 -  2.0700    0.99     2719   156  0.1599 0.2218        
REMARK   3     6  2.0700 -  1.9500    0.99     2730   154  0.1704 0.2082        
REMARK   3     7  1.9500 -  1.8500    0.99     2694   158  0.2043 0.2627        
REMARK   3     8  1.8500 -  1.7700    0.99     2753   132  0.2272 0.2363        
REMARK   3     9  1.7700 -  1.7000    0.99     2702   150  0.2460 0.2880        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.164            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.166           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           2046                                  
REMARK   3   ANGLE     :  0.902           2780                                  
REMARK   3   CHIRALITY :  0.050            295                                  
REMARK   3   PLANARITY :  0.005            375                                  
REMARK   3   DIHEDRAL  : 12.304           1175                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 28 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7555  -3.8806  -6.2233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1561 T22:   0.1652                                     
REMARK   3      T33:   0.1278 T12:   0.0112                                     
REMARK   3      T13:   0.0051 T23:  -0.0063                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3944 L22:   3.3659                                     
REMARK   3      L33:   1.3787 L12:   0.2384                                     
REMARK   3      L13:  -0.1579 L23:   0.1049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0579 S12:  -0.1792 S13:   0.0265                       
REMARK   3      S21:   0.0359 S22:  -0.1452 S23:   0.3105                       
REMARK   3      S31:   0.0106 S32:  -0.0877 S33:   0.0428                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 29 THROUGH 65 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -26.0501 -15.5603 -12.3766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1109 T22:   0.1322                                     
REMARK   3      T33:   0.1345 T12:   0.0072                                     
REMARK   3      T13:  -0.0020 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5810 L22:   1.9633                                     
REMARK   3      L33:   4.4047 L12:  -0.4252                                     
REMARK   3      L13:   0.3534 L23:  -0.4866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0223 S12:  -0.0819 S13:  -0.0917                       
REMARK   3      S21:  -0.0125 S22:   0.0435 S23:   0.1105                       
REMARK   3      S31:   0.1752 S32:  -0.1897 S33:  -0.0459                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 66 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -23.5874   2.5500 -15.8516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1298 T22:   0.1300                                     
REMARK   3      T33:   0.1465 T12:   0.0223                                     
REMARK   3      T13:  -0.0263 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0310 L22:   6.6735                                     
REMARK   3      L33:   4.8294 L12:   2.9480                                     
REMARK   3      L13:  -3.7866 L23:  -3.1493                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1053 S12:   0.1591 S13:   0.2872                       
REMARK   3      S21:  -0.1767 S22:   0.1903 S23:   0.2981                       
REMARK   3      S31:   0.1172 S32:  -0.1116 S33:  -0.0759                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -18.2862  -5.2158  -4.9256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1544 T22:   0.1246                                     
REMARK   3      T33:   0.1148 T12:   0.0183                                     
REMARK   3      T13:  -0.0171 T23:  -0.0327                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9761 L22:   2.5396                                     
REMARK   3      L33:   5.9075 L12:  -0.2123                                     
REMARK   3      L13:  -0.7882 L23:  -1.4922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0360 S12:  -0.2512 S13:  -0.0590                       
REMARK   3      S21:   0.2334 S22:  -0.1773 S23:  -0.0192                       
REMARK   3      S31:   0.0251 S32:   0.2222 S33:   0.1191                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 141 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.6864 -10.6230 -14.5746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1102 T22:   0.1070                                     
REMARK   3      T33:   0.1450 T12:   0.0175                                     
REMARK   3      T13:  -0.0047 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1621 L22:   1.7251                                     
REMARK   3      L33:   1.3750 L12:  -0.4518                                     
REMARK   3      L13:   0.2981 L23:  -0.2157                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0426 S12:   0.0090 S13:   0.0285                       
REMARK   3      S21:  -0.0809 S22:   0.0072 S23:  -0.1677                       
REMARK   3      S31:  -0.0091 S32:   0.1091 S33:   0.0352                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 167 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6798  -0.2538 -33.1633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2180 T22:   0.2594                                     
REMARK   3      T33:   0.1458 T12:   0.0231                                     
REMARK   3      T13:   0.0129 T23:   0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1144 L22:   2.8225                                     
REMARK   3      L33:   1.2820 L12:  -0.0349                                     
REMARK   3      L13:   0.5324 L23:   0.2771                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0604 S12:   0.5460 S13:   0.1967                       
REMARK   3      S21:  -0.3767 S22:  -0.0849 S23:   0.0459                       
REMARK   3      S31:  -0.0019 S32:   0.3570 S33:   0.0696                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.8469  -9.5128 -27.6583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1512 T22:   0.1576                                     
REMARK   3      T33:   0.1547 T12:  -0.0031                                     
REMARK   3      T13:   0.0159 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9908 L22:   7.5983                                     
REMARK   3      L33:   3.8933 L12:  -2.4395                                     
REMARK   3      L13:   0.2514 L23:   3.2458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1041 S12:   0.1534 S13:  -0.0227                       
REMARK   3      S21:  -0.2104 S22:  -0.1260 S23:  -0.0960                       
REMARK   3      S31:   0.0653 S32:  -0.0378 S33:  -0.0011                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 208 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.4015  -3.5786 -16.3239              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1540 T22:   0.1668                                     
REMARK   3      T33:   0.1457 T12:  -0.0135                                     
REMARK   3      T13:   0.0030 T23:  -0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8903 L22:   3.1665                                     
REMARK   3      L33:   2.7581 L12:  -2.2074                                     
REMARK   3      L13:   1.7265 L23:  -2.0461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1188 S12:  -0.0971 S13:   0.2491                       
REMARK   3      S21:   0.1575 S22:   0.0094 S23:  -0.3714                       
REMARK   3      S31:  -0.1875 S32:   0.1929 S33:   0.1053                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3558 -19.6314 -22.0102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1314 T22:   0.1327                                     
REMARK   3      T33:   0.1549 T12:   0.0355                                     
REMARK   3      T13:   0.0066 T23:   0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6249 L22:   1.6057                                     
REMARK   3      L33:   2.0895 L12:   0.9337                                     
REMARK   3      L13:   0.4850 L23:   0.7702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0831 S12:   0.0702 S13:  -0.0573                       
REMARK   3      S21:  -0.0269 S22:   0.1289 S23:  -0.1408                       
REMARK   3      S31:   0.1142 S32:   0.1714 S33:  -0.0361                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2696 -23.1914 -19.7897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1907 T22:   0.1265                                     
REMARK   3      T33:   0.1585 T12:   0.0194                                     
REMARK   3      T13:  -0.0013 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1429 L22:   3.0651                                     
REMARK   3      L33:   8.0705 L12:   0.4297                                     
REMARK   3      L13:  -1.5500 L23:  -2.9686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2670 S12:   0.0190 S13:  -0.1462                       
REMARK   3      S21:  -0.2436 S22:  -0.0309 S23:  -0.2086                       
REMARK   3      S31:   0.5609 S32:  -0.1441 S33:   0.2452                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6T6Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-OCT-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292104927.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873130                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 X 2M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26141                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
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: 6T6H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, AMMONIUM SULFATE, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       33.35800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.76500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.51600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.35800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.76500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.51600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.35800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       39.76500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.51600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.35800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       39.76500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       44.51600            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 10310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 403  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 496  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 498  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 503  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 559  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 595  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 602  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 639  LIES ON A SPECIAL POSITION.                          
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     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PRO A    -5                                                      
REMARK 465     ARG A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     MET A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     GLU A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     GLY A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     GLY A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     GLY A   269                                                      
REMARK 465     ASP A   270                                                      
REMARK 465     ALA A   271                                                      
REMARK 465     PRO A   272                                                      
REMARK 465     ALA A   273                                                      
REMARK 465     GLU A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     ARG A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     THR A   278                                                      
REMARK 465     GLY A   279                                                      
REMARK 465     ASP A   280                                                      
REMARK 465     ALA A   281                                                      
REMARK 465     PRO A   282                                                      
REMARK 465     ALA A   283                                                      
REMARK 465     GLU A   284                                                      
REMARK 465     ALA A   285                                                      
REMARK 465     ARG A   286                                                      
REMARK 465     ALA A   287                                                      
REMARK 465     SER A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     THR A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     VAL A   292                                                      
REMARK 465     VAL A   293                                                      
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  HH22  ARG A    46     O    HOH A   408              1.51            
REMARK 500   N    ARG A    10     O    HOH A   401              1.92            
REMARK 500   O    HOH A   532     O    HOH A   613              1.92            
REMARK 500   O    HOH A   487     O    HOH A   605              2.06            
REMARK 500   O    HOH A   434     O    HOH A   447              2.10            
REMARK 500   OE2  GLU A   252     O    HOH A   402              2.11            
REMARK 500   O    HOH A   404     O    HOH A   589              2.12            
REMARK 500   O    HOH A   597     O    HOH A   601              2.14            
REMARK 500   O    HOH A   464     O    HOH A   487              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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   O    HOH A   441     O    HOH A   486     4555     1.76            
REMARK 500   O    HOH A   619     O    HOH A   626     8544     1.86            
REMARK 500   O    HOH A   591     O    HOH A   608     2455     1.89            
REMARK 500   O    HOH A   521     O    HOH A   521     3455     1.96            
REMARK 500   O    HOH A   584     O    HOH A   613     8544     2.03            
REMARK 500   O    HOH A   584     O    HOH A   627     8544     2.11            
REMARK 500   O    HOH A   424     O    HOH A   521     4555     2.19            
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    ALA A  42       40.63    -96.61                                   
REMARK 500    LEU A  57       78.98   -117.00                                   
REMARK 500    VAL A  76      -70.32   -124.78                                   
REMARK 500    PHE A 109     -122.67     56.97                                   
REMARK 500    HIS A 195       59.07   -118.55                                   
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 MRB A 301                 
DBREF  6T6Z A    2   293  UNP    K4MHV9   K4MHV9_9ACTN     2    293             
SEQADV 6T6Z HIS A  -16  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A  -15  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A  -14  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A  -13  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A  -12  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A  -11  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z SER A  -10  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z SER A   -9  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z GLY A   -8  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z LEU A   -7  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z VAL A   -6  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z PRO A   -5  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z ARG A   -4  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z GLY A   -3  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z SER A   -2  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z HIS A   -1  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z MET A    0  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T6Z VAL A    1  UNP  K4MHV9              EXPRESSION TAG                 
SEQRES   1 A  310  HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG          
SEQRES   2 A  310  GLY SER HIS MET VAL ARG ASP GLY ASN GLY THR SER ARG          
SEQRES   3 A  310  ARG ASP VAL PHE GLU VAL PHE SER ARG ASP GLY THR PRO          
SEQRES   4 A  310  ILE ARG GLY PHE SER ARG PRO GLY PRO GLY GLU THR VAL          
SEQRES   5 A  310  VAL LEU VAL HIS GLY VAL ALA MET ASP ARG ARG ILE TRP          
SEQRES   6 A  310  ALA GLU SER GLY PHE LEU ASP ALA LEU PRO ASP ALA HIS          
SEQRES   7 A  310  VAL LEU ALA LEU ASP LEU ARG GLY ARG GLY GLU SER GLY          
SEQRES   8 A  310  ARG VAL GLY THR ALA GLU GLY HIS ALA LEU ARG ARG TYR          
SEQRES   9 A  310  VAL GLU ASP VAL ARG ALA VAL LEU ASP ARG PHE GLY ARG          
SEQRES  10 A  310  ALA ARG TYR SER LEU PHE GLY THR PHE PHE GLY GLY ARG          
SEQRES  11 A  310  ILE ALA LEU GLN VAL ALA ALA VAL ASP THR ARG VAL ALA          
SEQRES  12 A  310  ARG ALA PHE SER PHE CYS ALA HIS ALA GLU GLN VAL GLU          
SEQRES  13 A  310  ILE PRO GLU ASP ALA VAL GLU GLU GLU ALA VAL ALA VAL          
SEQRES  14 A  310  GLU GLY PRO GLY GLY HIS ALA TYR LEU ARG ASP HIS PHE          
SEQRES  15 A  310  THR GLY ARG GLY ALA PRO PRO TRP MET VAL GLU ALA CYS          
SEQRES  16 A  310  ALA ARG VAL ASP PRO GLY GLU LEU GLY ALA ALA THR ARG          
SEQRES  17 A  310  GLY LEU LEU HIS GLY SER ASP ARG ARG THR GLU ARG GLY          
SEQRES  18 A  310  HIS PRO ASP GLN GLU LEU VAL LEU ILE THR ALA ASP GLY          
SEQRES  19 A  310  ASP ALA ASP LEU ALA PRO PHE HIS ALA GLY GLU ARG ARG          
SEQRES  20 A  310  LEU GLY ALA HIS LEU TRP LEU VAL ASP ALA PRO THR ARG          
SEQRES  21 A  310  ILE LYS ALA ALA GLY ARG LEU ALA GLU VAL GLY ARG ARG          
SEQRES  22 A  310  VAL ALA GLY VAL LEU ALA GLU GLY GLY HIS GLY THR GLY          
SEQRES  23 A  310  ASP ALA PRO ALA GLU ALA ARG THR THR GLY ASP ALA PRO          
SEQRES  24 A  310  ALA GLU ALA ARG ALA SER GLY THR GLY VAL VAL                  
HET    MRB  A 301     121                                                       
HETNAM     MRB BOTTROMYCIN A2 DERIVATIVE                                        
FORMUL   2  MRB    C42 H62 N8 O7 S2                                             
FORMUL   3  HOH   *246(H2 O)                                                    
HELIX    1 AA1 ARG A   46  SER A   51  1                                   6    
HELIX    2 AA2 PHE A   53  LEU A   57  5                                   5    
HELIX    3 AA3 ALA A   79  HIS A   82  5                                   4    
HELIX    4 AA4 ALA A   83  GLY A   99  1                                  17    
HELIX    5 AA5 PHE A  109  ASP A  122  1                                  14    
HELIX    6 AA6 PRO A  141  GLY A  154  1                                  14    
HELIX    7 AA7 GLY A  156  ARG A  168  1                                  13    
HELIX    8 AA8 PRO A  171  CYS A  178  1                                   8    
HELIX    9 AA9 ALA A  179  VAL A  181  5                                   3    
HELIX   10 AB1 ASP A  182  LEU A  193  1                                  12    
HELIX   11 AB2 LEU A  221  GLY A  232  1                                  12    
HELIX   12 AB3 THR A  242  ALA A  247  1                                   6    
HELIX   13 AB4 ARG A  249  ALA A  262  1                                  14    
SHEET    1 AA1 8 ASP A  11  PHE A  16  0                                        
SHEET    2 AA1 8 PRO A  22  ARG A  28 -1  O  ILE A  23   N  VAL A  15           
SHEET    3 AA1 8 HIS A  61  LEU A  65 -1  O  VAL A  62   N  ARG A  28           
SHEET    4 AA1 8 THR A  34  VAL A  38  1  N  VAL A  35   O  LEU A  63           
SHEET    5 AA1 8 TYR A 103  THR A 108  1  O  PHE A 106   N  VAL A  38           
SHEET    6 AA1 8 VAL A 125  PHE A 131  1  O  PHE A 131   N  GLY A 107           
SHEET    7 AA1 8 GLU A 209  ALA A 215  1  O  VAL A 211   N  SER A 130           
SHEET    8 AA1 8 HIS A 234  VAL A 238  1  O  HIS A 234   N  LEU A 212           
SITE     1 AC1 15 PHE A 109  PHE A 110  ARG A 113  PRO A 141                    
SITE     2 AC1 15 GLU A 148  TYR A 160  LEU A 161  HIS A 164                    
SITE     3 AC1 15 PHE A 165  THR A 190  LEU A 193  SER A 197                    
SITE     4 AC1 15 HOH A 407  HOH A 531  HOH A 545                               
CRYST1   66.716   79.530   89.032  90.00  90.00  90.00 I 2 2 2       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      0.014989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012574  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011232        0.00000                         
TER    3836      ALA A 262                                                      
MASTER      527    0    1   13    8    0    4    6 2234    1  121   24          
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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