GenomeNet

Database: PDB
Entry: 4JQL
LinkDB: 4JQL
Original site: 4JQL 
HEADER    CHAPERONE/INHIBITOR                     20-MAR-13   4JQL              
TITLE     SYNTHESIS OF BENZOQUINONE-ANSAMYCIN-INSPIRED MACROCYCLIC LACTAMS FROM 
TITLE    2 SHIKIMIC ACID                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT SHOCK PROTEIN HSP 90-ALPHA;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HEAT SHOCK 86 KDA, HSP 86, HSP86, RENAL CARCINOMA ANTIGEN   
COMPND   5 NY-REN-38;                                                           
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HSP90AA1, HSP90A, HSPC1, HSPCA;                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR DESIGN, HSP90, NUCLEOTIDE BINDING DOMAIN, CHAPERONE,        
KEYWDS   2 GELDANAMYCIN, CYTOSOLE, CHAPERONE-INHIBITOR COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.JESO,S.IQBAL,P.HERNANDEZ,M.D.CAMERON,H.PARK,P.V.LOGRASSO,           
AUTHOR   2 G.C.MICALIZIO                                                        
REVDAT   3   22-MAY-13 4JQL    1       JRNL                                     
REVDAT   2   24-APR-13 4JQL    1       JRNL                                     
REVDAT   1   10-APR-13 4JQL    0                                                
JRNL        AUTH   V.JESO,S.IQBAL,P.HERNANDEZ,M.D.CAMERON,H.PARK,P.V.LOGRASSO,  
JRNL        AUTH 2 G.C.MICALIZIO                                                
JRNL        TITL   SYNTHESIS OF BENZOQUINONE ANSAMYCIN-INSPIRED MACROCYCLIC     
JRNL        TITL 2 LACTAMS FROM SHIKIMIC ACID.                                  
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  52  4800 2013              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   23554224                                                     
JRNL        DOI    10.1002/ANIE.201301323                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.72 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24483                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.910                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1203                            
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 32.9285 -  3.5764    0.98     2631   136  0.1617 0.1764        
REMARK   3     2  3.5764 -  2.8392    0.99     2591   138  0.1613 0.1946        
REMARK   3     3  2.8392 -  2.4804    0.99     2580   132  0.1688 0.1800        
REMARK   3     4  2.4804 -  2.2537    1.00     2599   131  0.1660 0.2049        
REMARK   3     5  2.2537 -  2.0922    1.00     2591   136  0.1581 0.1838        
REMARK   3     6  2.0922 -  1.9689    1.00     2575   130  0.1706 0.2080        
REMARK   3     7  1.9689 -  1.8703    1.00     2569   128  0.1800 0.2583        
REMARK   3     8  1.8703 -  1.7889    1.00     2573   139  0.1994 0.2306        
REMARK   3     9  1.7889 -  1.7200    0.99     2571   133  0.2121 0.2477        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.007           1791                                  
REMARK   3   ANGLE     :  1.107           2422                                  
REMARK   3   CHIRALITY :  0.080            275                                  
REMARK   3   PLANARITY :  0.004            309                                  
REMARK   3   DIHEDRAL  : 14.893            675                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resid 10 through 23 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7075  -4.4449  77.2389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1408 T22:   0.1649                                     
REMARK   3      T33:   0.2594 T12:  -0.0418                                     
REMARK   3      T13:   0.0374 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0427 L22:   0.9669                                     
REMARK   3      L33:   9.0260 L12:  -1.0849                                     
REMARK   3      L13:   1.9388 L23:  -1.0076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2810 S12:  -0.1605 S13:  -0.1662                       
REMARK   3      S21:   0.1370 S22:   0.3403 S23:  -0.0121                       
REMARK   3      S31:  -0.5263 S32:  -0.7321 S33:   0.0385                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 24 through 40 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  43.6267  -8.8115  52.4480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2044 T22:   0.1650                                     
REMARK   3      T33:   0.2380 T12:   0.0312                                     
REMARK   3      T13:   0.0027 T23:  -0.0953                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6184 L22:   0.9872                                     
REMARK   3      L33:   2.8277 L12:   1.8017                                     
REMARK   3      L13:  -2.0677 L23:  -1.0268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0582 S12:   0.4182 S13:  -0.7073                       
REMARK   3      S21:  -0.2621 S22:  -0.1824 S23:   0.0485                       
REMARK   3      S31:   0.3041 S32:  -0.0916 S33:   0.1379                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 41 through 65 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  38.3920  13.0478  55.3191              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1433 T22:   0.1470                                     
REMARK   3      T33:   0.0982 T12:  -0.0059                                     
REMARK   3      T13:  -0.0347 T23:   0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8435 L22:   5.6002                                     
REMARK   3      L33:   1.9652 L12:  -3.6894                                     
REMARK   3      L13:  -0.3146 L23:   1.2831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0979 S12:   0.3395 S13:  -0.0205                       
REMARK   3      S21:   0.0247 S22:  -0.1554 S23:   0.3633                       
REMARK   3      S31:  -0.0884 S32:  -0.2302 S33:   0.1884                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 66 through 93 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1746  14.5962  65.7575              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1501 T22:   0.0947                                     
REMARK   3      T33:   0.0988 T12:  -0.0096                                     
REMARK   3      T13:  -0.0069 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3493 L22:   2.6701                                     
REMARK   3      L33:   1.7881 L12:  -1.5192                                     
REMARK   3      L13:  -0.4184 L23:   0.2876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0798 S12:  -0.1429 S13:   0.3398                       
REMARK   3      S21:   0.2650 S22:   0.0183 S23:  -0.0550                       
REMARK   3      S31:  -0.1621 S32:  -0.0196 S33:   0.0559                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 94 through 106 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  30.8923   6.1478  64.7099              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1020 T22:   0.1835                                     
REMARK   3      T33:   0.1554 T12:   0.0061                                     
REMARK   3      T13:  -0.0052 T23:  -0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5919 L22:   8.1814                                     
REMARK   3      L33:   0.8768 L12:   3.4005                                     
REMARK   3      L13:  -1.3077 L23:  -1.8189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1096 S12:  -0.0351 S13:   0.1413                       
REMARK   3      S21:   0.2365 S22:  -0.0820 S23:   0.6460                       
REMARK   3      S31:  -0.0580 S32:  -0.1324 S33:  -0.0378                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resid 107 through 124 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.9964  -6.4015  49.3066              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3550 T22:   0.4051                                     
REMARK   3      T33:   0.3494 T12:   0.0202                                     
REMARK   3      T13:  -0.0973 T23:  -0.1719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9375 L22:   3.0045                                     
REMARK   3      L33:   4.7259 L12:   0.4962                                     
REMARK   3      L13:  -1.6179 L23:  -0.4290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2031 S12:   0.3020 S13:  -0.1881                       
REMARK   3      S21:  -0.7393 S22:   0.0851 S23:   0.0941                       
REMARK   3      S31:   0.4846 S32:  -0.0132 S33:  -0.1478                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resid 125 through 136 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2179  -0.2619  45.2680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4215 T22:   0.3943                                     
REMARK   3      T33:   0.2300 T12:   0.1171                                     
REMARK   3      T13:  -0.0984 T23:  -0.1026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8610 L22:   2.5288                                     
REMARK   3      L33:   4.7064 L12:   2.7420                                     
REMARK   3      L13:   0.8427 L23:  -1.1914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0677 S12:   1.1176 S13:  -0.3915                       
REMARK   3      S21:  -1.0698 S22:  -0.1546 S23:   0.1952                       
REMARK   3      S31:   0.3259 S32:   0.9996 S33:   0.0741                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resid 137 through 168 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2609   1.8472  65.4887              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0898 T22:   0.0988                                     
REMARK   3      T33:   0.1151 T12:  -0.0172                                     
REMARK   3      T13:  -0.0050 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1253 L22:   2.9307                                     
REMARK   3      L33:   1.4594 L12:  -1.3086                                     
REMARK   3      L13:  -0.2572 L23:   0.4796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1027 S12:  -0.0555 S13:  -0.2606                       
REMARK   3      S21:   0.1729 S22:   0.0090 S23:   0.2977                       
REMARK   3      S31:   0.1101 S32:  -0.0952 S33:   0.1139                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resid 169 through 182 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8507   5.0723  72.8989              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1602 T22:   0.1509                                     
REMARK   3      T33:   0.1136 T12:  -0.0065                                     
REMARK   3      T13:   0.0134 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9299 L22:   4.6294                                     
REMARK   3      L33:   1.1153 L12:  -0.2338                                     
REMARK   3      L13:   0.2814 L23:  -1.0453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0978 S12:  -0.3004 S13:  -0.1158                       
REMARK   3      S21:   0.3895 S22:   0.0133 S23:  -0.3681                       
REMARK   3      S31:  -0.1903 S32:  -0.0585 S33:   0.0828                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'A' and (resid 183 through 210 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  54.3788   5.9210  57.7327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0875 T22:   0.1260                                     
REMARK   3      T33:   0.0825 T12:  -0.0190                                     
REMARK   3      T13:  -0.0012 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6297 L22:   2.3141                                     
REMARK   3      L33:   2.3914 L12:  -0.5155                                     
REMARK   3      L13:  -0.6345 L23:  -0.1855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0050 S12:   0.1565 S13:   0.0154                       
REMARK   3      S21:  -0.1829 S22:  -0.0510 S23:  -0.2042                       
REMARK   3      S31:  -0.0485 S32:   0.3338 S33:   0.0312                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'A' and (resid 211 through 224 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  49.8596  17.3178  57.7335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1539 T22:   0.1539                                     
REMARK   3      T33:   0.1508 T12:  -0.0277                                     
REMARK   3      T13:   0.0406 T23:   0.0289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1210 L22:   4.3596                                     
REMARK   3      L33:   3.0165 L12:  -1.6090                                     
REMARK   3      L13:   0.0374 L23:   0.0690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0168 S12:   0.7677 S13:   0.2727                       
REMARK   3      S21:  -0.2440 S22:   0.0636 S23:  -0.0598                       
REMARK   3      S31:  -0.2481 S32:   0.3373 S33:  -0.0623                       
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 4JQL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078379.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24793                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.720                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.922                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL, 0.2 M MGCL2, 30%         
REMARK 280  PEG4000, PH 8.5, VAPOR DIFFUSION, TEMPERATURE 277K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       22.24500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
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     ASP A     9                                                      
REMARK 465     GLU A   225                                                      
REMARK 465     ARG A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     GLU A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     SER A   231                                                      
REMARK 465     ASP A   232                                                      
REMARK 465     ASP A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     GLU A   236                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  74    CG   CD   CE   NZ                                   
REMARK 470     LYS A 224    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   637     O    HOH A   640              1.87            
REMARK 500   O    HOH A   612     O    HOH A   613              1.87            
REMARK 500   O    HOH A   631     O    HOH A   633              1.92            
REMARK 500   NZ   LYS A   112     O    HOH A   622              1.93            
REMARK 500   O    HOH A   621     O    HOH A   626              1.96            
REMARK 500   O    HOH A   518     O    HOH A   557              1.98            
REMARK 500   OE2  GLU A   120     O    HOH A   581              2.10            
REMARK 500   NE2  GLN A    85     O    HOH A   599              2.10            
REMARK 500   O    HOH A   476     O    HOH A   588              2.11            
REMARK 500   O    HOH A   591     O    HOH A   654              2.13            
REMARK 500   O    HOH A   502     O    HOH A   560              2.17            
REMARK 500   O    HOH A   617     O    HOH A   674              2.18            
REMARK 500   O    HOH A   575     O    HOH A   625              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    GLN A 123       31.32    -66.98                                   
REMARK 500    ALA A 166     -145.93     66.79                                   
REMARK 500    ARG A 182      142.49   -170.35                                   
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                              MG A 302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  54   OD2                                                    
REMARK 620 2 HOH A 598   O    89.7                                              
REMARK 620 3 HOH A 444   O    83.2  90.1                                        
REMARK 620 4 HOH A 494   O    87.7 173.0  96.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VJ6 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 302                  
DBREF  4JQL A    9   236  UNP    P07900   HS90A_HUMAN      9    236             
SEQADV 4JQL MET A  -20  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL GLY A  -19  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL SER A  -18  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL SER A  -17  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -16  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -15  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -14  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -13  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -12  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A  -11  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL SER A  -10  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL SER A   -9  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL GLY A   -8  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL LEU A   -7  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL VAL A   -6  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL PRO A   -5  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL ARG A   -4  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL GLY A   -3  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL SER A   -2  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL HIS A   -1  UNP  P07900              EXPRESSION TAG                 
SEQADV 4JQL MET A    0  UNP  P07900              EXPRESSION TAG                 
SEQRES   1 A  249  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  249  LEU VAL PRO ARG GLY SER HIS MET ASP GLN PRO MET GLU          
SEQRES   3 A  249  GLU GLU GLU VAL GLU THR PHE ALA PHE GLN ALA GLU ILE          
SEQRES   4 A  249  ALA GLN LEU MET SER LEU ILE ILE ASN THR PHE TYR SER          
SEQRES   5 A  249  ASN LYS GLU ILE PHE LEU ARG GLU LEU ILE SER ASN SER          
SEQRES   6 A  249  SER ASP ALA LEU ASP LYS ILE ARG TYR GLU SER LEU THR          
SEQRES   7 A  249  ASP PRO SER LYS LEU ASP SER GLY LYS GLU LEU HIS ILE          
SEQRES   8 A  249  ASN LEU ILE PRO ASN LYS GLN ASP ARG THR LEU THR ILE          
SEQRES   9 A  249  VAL ASP THR GLY ILE GLY MET THR LYS ALA ASP LEU ILE          
SEQRES  10 A  249  ASN ASN LEU GLY THR ILE ALA LYS SER GLY THR LYS ALA          
SEQRES  11 A  249  PHE MET GLU ALA LEU GLN ALA GLY ALA ASP ILE SER MET          
SEQRES  12 A  249  ILE GLY GLN PHE GLY VAL GLY PHE TYR SER ALA TYR LEU          
SEQRES  13 A  249  VAL ALA GLU LYS VAL THR VAL ILE THR LYS HIS ASN ASP          
SEQRES  14 A  249  ASP GLU GLN TYR ALA TRP GLU SER SER ALA GLY GLY SER          
SEQRES  15 A  249  PHE THR VAL ARG THR ASP THR GLY GLU PRO MET GLY ARG          
SEQRES  16 A  249  GLY THR LYS VAL ILE LEU HIS LEU LYS GLU ASP GLN THR          
SEQRES  17 A  249  GLU TYR LEU GLU GLU ARG ARG ILE LYS GLU ILE VAL LYS          
SEQRES  18 A  249  LYS HIS SER GLN PHE ILE GLY TYR PRO ILE THR LEU PHE          
SEQRES  19 A  249  VAL GLU LYS GLU ARG ASP LYS GLU VAL SER ASP ASP GLU          
SEQRES  20 A  249  ALA GLU                                                      
HET    VJ6  A 301      40                                                       
HET     MG  A 302       1                                                       
HETNAM     VJ6 VALERJESOMYCIN                                                   
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     VJ6 (4E,8S,9S,10E,12S,13R,14S)-13,14,20-TRIMETHOXY-4,10,12-          
HETSYN   2 VJ6  TRIMETHYL-3-OXO-16-OXA-2-AZABICYCLO[16.3.1]DOCOSA-              
HETSYN   3 VJ6  1(22),4,10,18,20-PENTAENE-8,9-DIYL DICARBAMATE                  
FORMUL   2  VJ6    C28 H41 N3 O9                                                
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  HOH   *276(H2 O)                                                    
HELIX    1   1 GLN A   23  THR A   36  1                                  14    
HELIX    2   2 GLU A   42  ASP A   66  1                                  25    
HELIX    3   3 PRO A   67  ASP A   71  5                                   5    
HELIX    4   4 THR A   99  LEU A  107  1                                   9    
HELIX    5   5 GLY A  114  GLN A  123  1                                  10    
HELIX    6   6 ASP A  127  GLY A  135  5                                   9    
HELIX    7   7 VAL A  136  LEU A  143  5                                   8    
HELIX    8   8 GLN A  194  LEU A  198  5                                   5    
HELIX    9   9 GLU A  199  SER A  211  1                                  13    
SHEET    1   A 8 GLU A  18  ALA A  21  0                                        
SHEET    2   A 8 SER A 169  THR A 174 -1  O  PHE A 170   N  PHE A  20           
SHEET    3   A 8 TYR A 160  SER A 164 -1  N  ALA A 161   O  ARG A 173           
SHEET    4   A 8 ALA A 145  LYS A 153 -1  N  VAL A 150   O  TRP A 162           
SHEET    5   A 8 GLY A 183  LEU A 190 -1  O  ILE A 187   N  THR A 149           
SHEET    6   A 8 THR A  88  ASP A  93 -1  N  ILE A  91   O  VAL A 186           
SHEET    7   A 8 ILE A  78  ASN A  83 -1  N  ILE A  81   O  THR A  90           
SHEET    8   A 8 ILE A 218  LEU A 220  1  O  THR A 219   N  LEU A  80           
LINK         OD2AASP A  54                MG    MG A 302     1555   1555  1.85  
LINK        MG    MG A 302                 O   HOH A 598     1555   1555  1.96  
LINK        MG    MG A 302                 O   HOH A 444     1555   1555  2.10  
LINK        MG    MG A 302                 O   HOH A 494     1555   1555  2.29  
SITE     1 AC1 19 ASN A  51  SER A  52  ASP A  54  ALA A  55                    
SITE     2 AC1 19 LYS A  58  ASP A  93  ILE A  96  ASP A 102                    
SITE     3 AC1 19 ASN A 106  LEU A 107  LYS A 112  GLY A 135                    
SITE     4 AC1 19 VAL A 136  GLY A 137  PHE A 138  THR A 184                    
SITE     5 AC1 19 VAL A 186  HOH A 401  HOH A 412                               
SITE     1 AC2  4 ASP A  54  HOH A 444  HOH A 494  HOH A 598                    
CRYST1   53.370   44.490   53.920  90.00 114.80  90.00 P 1 21 1      2          
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      0.018737  0.000000  0.008658        0.00000                         
SCALE2      0.000000  0.022477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system