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LongText Report for: 6t70-pdb

Name Class
6t70-pdb
HEADER    HYDROLASE                               20-OCT-19   6T70              
TITLE     STRUCTURE OF THE BOTTROMYCIN EPIMERASE BOTH IN COMPLEX WITH           
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 6T70    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.    1.58 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 32377                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.168                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1648                            
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 44.2200 -  3.6200    0.99     2695   152  0.1568 0.1934        
REMARK   3     2  3.6200 -  2.8700    0.99     2595   137  0.1540 0.1667        
REMARK   3     3  2.8700 -  2.5100    1.00     2561   153  0.1518 0.1836        
REMARK   3     4  2.5100 -  2.2800    1.00     2554   131  0.1562 0.2000        
REMARK   3     5  2.2800 -  2.1200    1.00     2578   135  0.1579 0.2160        
REMARK   3     6  2.1200 -  1.9900    1.00     2540   133  0.1611 0.1842        
REMARK   3     7  1.9900 -  1.8900    1.00     2547   123  0.1749 0.2257        
REMARK   3     8  1.8900 -  1.8100    1.00     2564   142  0.1909 0.2171        
REMARK   3     9  1.8100 -  1.7400    1.00     2534   129  0.2042 0.2409        
REMARK   3    10  1.7400 -  1.6800    1.00     2544   126  0.2194 0.2758        
REMARK   3    11  1.6800 -  1.6300    1.00     2495   148  0.2373 0.2565        
REMARK   3    12  1.6300 -  1.5800    1.00     2522   139  0.2392 0.3021        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.151            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.026           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.46                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.65                          
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      :  0.012           2057                                  
REMARK   3   ANGLE     :  1.254           2791                                  
REMARK   3   CHIRALITY :  0.066            294                                  
REMARK   3   PLANARITY :  0.008            375                                  
REMARK   3   DIHEDRAL  : 14.659           1175                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 10 THROUGH 83 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -25.9014  -8.1231 -11.3881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1111 T22:   0.1366                                     
REMARK   3      T33:   0.1076 T12:   0.0099                                     
REMARK   3      T13:  -0.0036 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1900 L22:   3.4708                                     
REMARK   3      L33:   1.0571 L12:   0.2724                                     
REMARK   3      L13:  -0.3025 L23:  -0.1929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0089 S12:  -0.0499 S13:  -0.0281                       
REMARK   3      S21:   0.0988 S22:  -0.0122 S23:   0.1044                       
REMARK   3      S31:   0.0567 S32:  -0.0382 S33:  -0.0025                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -18.1178  -5.2138  -5.0242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1379 T22:   0.1123                                     
REMARK   3      T33:   0.0979 T12:   0.0224                                     
REMARK   3      T13:  -0.0158 T23:  -0.0467                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2975 L22:   4.4844                                     
REMARK   3      L33:   6.8413 L12:  -0.8861                                     
REMARK   3      L13:  -1.2539 L23:  -0.6561                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0729 S12:  -0.3716 S13:  -0.0002                       
REMARK   3      S21:   0.2610 S22:  -0.0960 S23:   0.0369                       
REMARK   3      S31:   0.1364 S32:   0.3152 S33:   0.0928                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 167 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6091  -6.4975 -21.8593              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1466 T22:   0.1476                                     
REMARK   3      T33:   0.1416 T12:   0.0042                                     
REMARK   3      T13:   0.0071 T23:  -0.0187                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7726 L22:   1.3108                                     
REMARK   3      L33:   0.1059 L12:  -0.5135                                     
REMARK   3      L13:   0.1913 L23:  -0.1481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:   0.1884 S13:   0.0620                       
REMARK   3      S21:  -0.1087 S22:  -0.0340 S23:  -0.1228                       
REMARK   3      S31:  -0.0143 S32:   0.0752 S33:   0.0311                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 168 THROUGH 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.7942  -9.5753 -27.5513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1284 T22:   0.1468                                     
REMARK   3      T33:   0.1488 T12:  -0.0165                                     
REMARK   3      T13:  -0.0171 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1111 L22:   5.9558                                     
REMARK   3      L33:   9.5429 L12:  -4.7845                                     
REMARK   3      L13:  -4.9217 L23:   6.9820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0633 S12:   0.1983 S13:  -0.1977                       
REMARK   3      S21:  -0.1290 S22:  -0.1040 S23:   0.1451                       
REMARK   3      S31:   0.2515 S32:  -0.1865 S33:   0.1760                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 183 THROUGH 208 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.3066  -3.6917 -16.2385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1581 T22:   0.1413                                     
REMARK   3      T33:   0.1347 T12:  -0.0041                                     
REMARK   3      T13:   0.0044 T23:  -0.0554                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0395 L22:   8.4218                                     
REMARK   3      L33:   6.1305 L12:  -7.1994                                     
REMARK   3      L13:   6.2517 L23:  -6.4175                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1569 S12:  -0.0430 S13:   0.3928                       
REMARK   3      S21:   0.1254 S22:  -0.0162 S23:  -0.5405                       
REMARK   3      S31:  -0.0895 S32:   0.1096 S33:   0.1487                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3467 -19.6350 -21.9236              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1291 T22:   0.0938                                     
REMARK   3      T33:   0.1489 T12:   0.0493                                     
REMARK   3      T13:   0.0240 T23:   0.0013                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1690 L22:   3.4555                                     
REMARK   3      L33:   6.2621 L12:   3.0117                                     
REMARK   3      L13:   3.2525 L23:   2.6325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1065 S12:   0.1549 S13:  -0.0634                       
REMARK   3      S21:  -0.0937 S22:   0.1300 S23:  -0.2266                       
REMARK   3      S31:   0.0370 S32:   0.1398 S33:  -0.0313                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 243 THROUGH 262 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2569 -23.2017 -19.6032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1854 T22:   0.0900                                     
REMARK   3      T33:   0.1447 T12:   0.0079                                     
REMARK   3      T13:   0.0242 T23:  -0.0451                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2576 L22:   7.4512                                     
REMARK   3      L33:   3.7576 L12:   1.7303                                     
REMARK   3      L13:  -2.1124 L23:  -5.1162                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1683 S12:  -0.0125 S13:  -0.2077                       
REMARK   3      S21:  -0.2764 S22:   0.0674 S23:  -0.0693                       
REMARK   3      S31:   0.1906 S32:  -0.0399 S33:   0.0550                       
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 6T70 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_1292104928.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000031                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32388                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.220                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6T6H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
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       33.27200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.71500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       44.22200            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       33.27200            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.71500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.22200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       33.27200            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       39.71500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.22200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       33.27200            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       39.71500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       44.22200            
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: 560 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 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 ZN    ZN A 304  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 463  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 490  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 551  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 559  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 575  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 583  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   HE   ARG A   102     O    HOH A   402              1.44            
REMARK 500  HH11  ARG A   100     O    HOH A   401              1.50            
REMARK 500  HH21  ARG A    10     O    HOH A   403              1.51            
REMARK 500   NH1  ARG A   100     O    HOH A   401              1.91            
REMARK 500   NE   ARG A   102     O    HOH A   402              2.00            
REMARK 500   O    HOH A   403     O    HOH A   505              2.10            
REMARK 500   O    HOH A   539     O    HOH A   582              2.11            
REMARK 500   NH2  ARG A    10     O    HOH A   403              2.13            
REMARK 500   NH2  ARG A   102     O    HOH A   402              2.14            
REMARK 500   OE1  GLU A   146     O    HOH A   404              2.15            
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   HE   ARG A   199     HE   ARG A   199     2555     1.31            
REMARK 500   O    HOH A   566     O    HOH A   591     8544     1.90            
REMARK 500   O    HOH A   584     O    HOH A   599     2455     2.08            
REMARK 500   O    HOH A   585     O    HOH A   601     8444     2.13            
REMARK 500   O    HOH A   485     O    HOH A   485     4555     2.17            
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       37.87    -99.95                                   
REMARK 500    VAL A  76      -70.99   -124.90                                   
REMARK 500    PHE A 109     -126.15     59.46                                   
REMARK 500    HIS A 195       59.41   -119.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 304  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 158   ND1                                                    
REMARK 620 2 HOH A 451   O   108.1                                              
REMARK 620 3 HOH A 583   O   122.6  62.7                                        
REMARK 620 4 HIS A 158   ND1   0.0 108.1 122.6                                  
REMARK 620 5 HOH A 583   O   122.6  62.7   0.0 122.6                            
REMARK 620 6 HOH A 451   O   100.5 125.4  62.7 100.5  62.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MQZ A 306                 
DBREF  6T70 A    2   293  UNP    K4MHV9   K4MHV9_9ACTN     2    293             
SEQADV 6T70 HIS A  -16  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A  -15  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A  -14  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A  -13  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A  -12  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A  -11  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 SER A  -10  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 SER A   -9  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 GLY A   -8  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 LEU A   -7  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 VAL A   -6  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 PRO A   -5  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 ARG A   -4  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 GLY A   -3  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 SER A   -2  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 HIS A   -1  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 MET A    0  UNP  K4MHV9              EXPRESSION TAG                 
SEQADV 6T70 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     CL  A 301       1                                                       
HET    GOL  A 302      12                                                       
HET    SO4  A 303       5                                                       
HET     ZN  A 304       1                                                       
HET    GOL  A 305      12                                                       
HET    MQZ  A 306     122                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     MQZ BOTTROMYCIN A2 DERIVATIVE                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2   CL    CL 1-                                                        
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   7  MQZ    C42 H62 N8 O8 S2                                             
FORMUL   8  HOH   *201(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  SER A  27   N  ASP A  11           
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  SER A 104   N  VAL A  36           
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  TRP A 236   N  LEU A 212           
LINK         ND1 HIS A 158                ZN    ZN A 304     1555   1555  2.00  
LINK        ZN    ZN A 304                 O   HOH A 451     1555   1555  2.43  
LINK        ZN    ZN A 304                 O   HOH A 583     1555   1555  2.11  
LINK         ND1 HIS A 158                ZN    ZN A 304     1555   2455  2.00  
LINK        ZN    ZN A 304                 O   HOH A 583     1555   2455  2.11  
LINK        ZN    ZN A 304                 O   HOH A 451     1555   2455  2.43  
SITE     1 AC1  4 GLY A  40  VAL A  41  PHE A 109  PHE A 110                    
SITE     1 AC2  4 ARG A 100  ALA A 101  ARG A 102  HOH A 427                    
SITE     1 AC3  9 ARG A  46  ARG A 180  ASP A 182  PRO A 183                    
SITE     2 AC3  9 GLY A 184  HOH A 411  HOH A 439  HOH A 459                    
SITE     3 AC3  9 HOH A 497                                                     
SITE     1 AC4  3 HIS A 158  HOH A 451  HOH A 583                               
SITE     1 AC5  3 ARG A  18  ARG A  86  HOH A 538                               
SITE     1 AC6 15 PHE A 109  PHE A 110  ARG A 113  PRO A 141                    
SITE     2 AC6 15 GLU A 148  HIS A 164  PHE A 165  ARG A 168                    
SITE     3 AC6 15 THR A 190  LEU A 193  SER A 197  ILE A 244                    
SITE     4 AC6 15 HOH A 409  HOH A 499  HOH A 542                               
CRYST1   66.544   79.430   88.444  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      0.015028  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012590  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011307        0.00000                         
TER    3827      ALA A 262                                                      
MASTER      517    0    6   13    8    0   11    6 2209    1  155   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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