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LongText Report for: 4J0J-pdb

Name Class
4J0J-pdb
HEADER    HYDROLASE                               31-JAN-13   4J0J              
TITLE     TANNIN ACYL HYDROLASE IN COMPLEX WITH ETHYL 3,5-DIHYDROXYBENZOATE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TANNASE;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;                        
SOURCE   3 ORGANISM_TAXID: 1590;                                                
SOURCE   4 GENE: TANLPL;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    TANNIN, HYDROLASE, HYDROLYSIS                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.REN,M.WU,Q.WANG,X.PENG,H.WEN,Q.CHEN,W.J.MCKINSTRY                   
REVDAT   1   22-MAY-13 4J0J    0                                                
JRNL        AUTH   B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN          
JRNL        TITL   CRYSTAL STRUCTURE OF TANNASE FROM LACTOBACILLUS PLANTARUM    
JRNL        REF    J.MOL.BIOL.                                2013              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   23648840                                                     
JRNL        DOI    10.1016/J.JMB.2013.04.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.2_869)                    
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.220                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 112872                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5659                            
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 19.6924 -  6.1528    0.97     3636   184  0.1787 0.1788        
REMARK   3     2  6.1528 -  4.9086    0.98     3634   186  0.1868 0.2017        
REMARK   3     3  4.9086 -  4.2954    0.99     3666   191  0.1533 0.1492        
REMARK   3     4  4.2954 -  3.9060    0.98     3594   181  0.1543 0.1797        
REMARK   3     5  3.9060 -  3.6279    0.98     3685   194  0.1708 0.1958        
REMARK   3     6  3.6279 -  3.4152    0.98     3687   191  0.1630 0.2069        
REMARK   3     7  3.4152 -  3.2450    0.98     3623   185  0.1694 0.2265        
REMARK   3     8  3.2450 -  3.1043    0.98     3603   188  0.1760 0.2162        
REMARK   3     9  3.1043 -  2.9852    0.98     3616   182  0.1730 0.2239        
REMARK   3    10  2.9852 -  2.8825    0.98     3639   172  0.1763 0.1758        
REMARK   3    11  2.8825 -  2.7926    0.98     3659   204  0.1874 0.2256        
REMARK   3    12  2.7926 -  2.7130    0.97     3554   172  0.1887 0.2105        
REMARK   3    13  2.7130 -  2.6418    0.98     3707   203  0.1827 0.2171        
REMARK   3    14  2.6418 -  2.5774    0.97     3561   164  0.1792 0.2241        
REMARK   3    15  2.5774 -  2.5190    0.97     3596   210  0.1886 0.2320        
REMARK   3    16  2.5190 -  2.4655    0.96     3608   183  0.1843 0.2292        
REMARK   3    17  2.4655 -  2.4162    0.96     3523   203  0.1794 0.2397        
REMARK   3    18  2.4162 -  2.3707    0.96     3593   226  0.1818 0.2270        
REMARK   3    19  2.3707 -  2.3284    0.96     3490   184  0.1916 0.2302        
REMARK   3    20  2.3284 -  2.2890    0.95     3619   161  0.2025 0.2910        
REMARK   3    21  2.2890 -  2.2522    0.95     3535   189  0.2042 0.2486        
REMARK   3    22  2.2522 -  2.2176    0.96     3550   169  0.2039 0.2428        
REMARK   3    23  2.2176 -  2.1850    0.95     3520   203  0.2115 0.2436        
REMARK   3    24  2.1850 -  2.1543    0.94     3501   184  0.2163 0.2766        
REMARK   3    25  2.1543 -  2.1252    0.94     3482   168  0.2233 0.2319        
REMARK   3    26  2.1252 -  2.0976    0.94     3473   171  0.2174 0.2508        
REMARK   3    27  2.0976 -  2.0714    0.94     3518   212  0.2417 0.2494        
REMARK   3    28  2.0714 -  2.0465    0.94     3488   200  0.2464 0.3044        
REMARK   3    29  2.0465 -  2.0227    0.94     3382   182  0.2574 0.3016        
REMARK   3    30  2.0227 -  2.0000    0.93     3471   217  0.2658 0.3178        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.90                                          
REMARK   3   SHRINKAGE RADIUS   : 0.60                                          
REMARK   3   K_SOL              : 0.43                                          
REMARK   3   B_SOL              : 60.67                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.790           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 6.73350                                              
REMARK   3    B22 (A**2) : -16.52350                                            
REMARK   3    B33 (A**2) : -1.38440                                             
REMARK   3    B12 (A**2) : -4.16070                                             
REMARK   3    B13 (A**2) : 12.64530                                             
REMARK   3    B23 (A**2) : -4.84510                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           7453                                  
REMARK   3   ANGLE     :  0.917          10193                                  
REMARK   3   CHIRALITY :  0.062           1147                                  
REMARK   3   PLANARITY :  0.004           1340                                  
REMARK   3   DIHEDRAL  : 14.815           2651                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 0:188)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5678 108.9390  83.7433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2644 T22:   0.1427                                     
REMARK   3      T33:   0.1399 T12:   0.0113                                     
REMARK   3      T13:  -0.0021 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5179 L22:   1.6485                                     
REMARK   3      L33:   1.8121 L12:   0.1767                                     
REMARK   3      L13:   0.0398 L23:   0.3227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0441 S12:  -0.0211 S13:   0.0708                       
REMARK   3      S21:   0.1482 S22:   0.0318 S23:  -0.1427                       
REMARK   3      S31:  -0.2450 S32:  -0.0037 S33:   0.0020                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 189:272)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4495  89.4083  67.2430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2077 T22:   0.2122                                     
REMARK   3      T33:   0.2347 T12:   0.0344                                     
REMARK   3      T13:  -0.0138 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8144 L22:   2.0908                                     
REMARK   3      L33:   1.7792 L12:   0.9954                                     
REMARK   3      L13:   0.4224 L23:   0.7618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0933 S12:   0.0217 S13:   0.3086                       
REMARK   3      S21:  -0.0881 S22:  -0.0981 S23:   0.5042                       
REMARK   3      S31:   0.0730 S32:  -0.3282 S33:   0.0590                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 273:469)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9518  85.0419  73.3173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1880 T22:   0.1584                                     
REMARK   3      T33:   0.1206 T12:   0.0278                                     
REMARK   3      T13:  -0.0188 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3794 L22:   1.6183                                     
REMARK   3      L33:   1.3393 L12:   0.1802                                     
REMARK   3      L13:  -0.2142 L23:   0.0259                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0278 S12:   0.0108 S13:  -0.0041                       
REMARK   3      S21:   0.0661 S22:   0.0424 S23:  -0.0936                       
REMARK   3      S31:   0.1231 S32:  -0.0150 S33:  -0.0164                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 0:208)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2959  42.4589  34.3720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0992 T22:   0.1597                                     
REMARK   3      T33:   0.1650 T12:   0.0068                                     
REMARK   3      T13:  -0.0091 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4411 L22:   0.8963                                     
REMARK   3      L33:   0.3221 L12:  -0.1154                                     
REMARK   3      L13:  -0.1575 L23:   0.3668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0285 S12:   0.0082 S13:  -0.1207                       
REMARK   3      S21:  -0.1163 S22:   0.0138 S23:  -0.0969                       
REMARK   3      S31:   0.0717 S32:  -0.0161 S33:  -0.0024                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 209:235)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  23.5839  69.1856  38.2149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2611 T22:   0.2481                                     
REMARK   3      T33:   0.1620 T12:  -0.0127                                     
REMARK   3      T13:  -0.0958 T23:  -0.0202                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0789 L22:   0.9387                                     
REMARK   3      L33:   0.1241 L12:   0.0640                                     
REMARK   3      L13:   0.0053 L23:   0.3122                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:   0.1291 S13:  -0.1200                       
REMARK   3      S21:  -0.5477 S22:   0.0705 S23:   0.1836                       
REMARK   3      S31:  -0.0370 S32:  -0.0182 S33:   0.0673                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 236:272)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9300  69.0219  40.1278              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3089 T22:   0.2251                                     
REMARK   3      T33:   0.2070 T12:   0.0650                                     
REMARK   3      T13:  -0.0384 T23:  -0.0393                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3085 L22:   0.2131                                     
REMARK   3      L33:   0.2132 L12:   0.1985                                     
REMARK   3      L13:  -0.2104 L23:  -0.1189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1870 S12:   0.0710 S13:  -0.0048                       
REMARK   3      S21:  -0.1440 S22:  -0.0698 S23:   0.1167                       
REMARK   3      S31:   0.0426 S32:  -0.0231 S33:   0.0131                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 273:469)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1910  66.6476  41.3061              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1301 T22:   0.1969                                     
REMARK   3      T33:   0.1540 T12:  -0.0011                                     
REMARK   3      T13:  -0.0219 T23:  -0.0081                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5325 L22:   0.9772                                     
REMARK   3      L33:   0.2721 L12:  -0.0307                                     
REMARK   3      L13:  -0.1165 L23:   0.1481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0123 S12:  -0.0380 S13:   0.0656                       
REMARK   3      S21:  -0.1171 S22:   0.0332 S23:  -0.1006                       
REMARK   3      S31:  -0.0651 S32:   0.0299 S33:   0.0103                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_    
REMARK   3  PLUS/MINUS COLUMNS                                                  
REMARK   4                                                                      
REMARK   4 4J0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077442.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113748                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: STRUCTURE FACTOR FILE CONTAINS FRIEDEL'S PAIRS               
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.5, 20%      
REMARK 280  PEG 3000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 281K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     THR A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     VAL B   -11                                                      
REMARK 465     ASP B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     THR B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PHE B    -2                                                      
REMARK 465     GLN B    -1                                                      
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     SER A 163    OG                                                  
REMARK 470     SER B 163    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   823     O    HOH B   843              1.87            
REMARK 500   OD2  ASP B     8     O    HOH B   814              1.96            
REMARK 500   O    LEU B   150     O    HOH B   686              1.99            
REMARK 500   O    HOH A   688     O    HOH A   721              1.99            
REMARK 500   O    HOH B   829     O    HOH B   837              2.01            
REMARK 500   O    HOH B   758     O    HOH B   826              2.01            
REMARK 500   OD2  ASP A   363     O    HOH A   759              2.11            
REMARK 500   OE2  GLU A   357     O12  E35 A   501              2.12            
REMARK 500   O    HOH B   671     O    HOH B   673              2.13            
REMARK 500   NE2  GLN A   298     O    HOH A   744              2.14            
REMARK 500   OG   SER A     2     O    HOH A   697              2.16            
REMARK 500   O    HOH A   715     O    HOH A   726              2.16            
REMARK 500   NH1  ARG A   297     O    HOH A   783              2.17            
REMARK 500   NE2  GLN B   271     O    HOH B   803              2.17            
REMARK 500   O    HOH B   830     O    HOH B   852              2.18            
REMARK 500   ND2  ASN B    94     O    HOH B   870              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   656     O    HOH B   669     1545     2.06            
REMARK 500   O    HOH A   679     O    HOH B   704     1556     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A 130       40.54   -103.95                                   
REMARK 500    SER A 163     -117.08     61.36                                   
REMARK 500    CYS A 204       57.72     29.30                                   
REMARK 500    PRO A 231      130.68    -37.41                                   
REMARK 500    ALA A 233     -116.70   -133.37                                   
REMARK 500    THR A 236     -160.19   -108.39                                   
REMARK 500    ASN A 238       26.83   -157.01                                   
REMARK 500    THR A 340      143.37     75.01                                   
REMARK 500    PHE A 371       18.55   -141.91                                   
REMARK 500    PRO B 130       37.86    -99.26                                   
REMARK 500    SER B 163     -118.60     64.32                                   
REMARK 500    CYS B 204       57.31     30.04                                   
REMARK 500    ARG B 228     -159.00   -151.01                                   
REMARK 500    ALA B 233      104.62     19.36                                   
REMARK 500    THR B 235     -163.17   -128.05                                   
REMARK 500    THR B 236     -141.58    -97.58                                   
REMARK 500    THR B 340      143.88     69.74                                   
REMARK 500    PHE B 371       15.48   -143.41                                   
REMARK 500    THR B 403       64.12   -118.34                                   
REMARK 500    HIS B 451       97.31    -65.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 860        DISTANCE =  5.27 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E35 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E35 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4J0C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JUI   RELATED DB: PDB                                   
DBREF  4J0J A    1   469  UNP    B3Y018   B3Y018_LACPN     1    469             
DBREF  4J0J B    1   469  UNP    B3Y018   B3Y018_LACPN     1    469             
SEQADV 4J0J MET A  -21  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -20  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -19  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -18  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -17  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -16  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS A  -15  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER A  -14  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER A  -13  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLY A  -12  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J VAL A  -11  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J ASP A  -10  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J LEU A   -9  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLY A   -8  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J THR A   -7  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLU A   -6  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J ASN A   -5  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J LEU A   -4  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J TYR A   -3  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J PHE A   -2  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLN A   -1  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER A    0  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J MET B  -21  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -20  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -19  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -18  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -17  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -16  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J HIS B  -15  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER B  -14  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER B  -13  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLY B  -12  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J VAL B  -11  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J ASP B  -10  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J LEU B   -9  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLY B   -8  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J THR B   -7  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLU B   -6  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J ASN B   -5  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J LEU B   -4  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J TYR B   -3  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J PHE B   -2  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J GLN B   -1  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4J0J SER B    0  UNP  B3Y018              EXPRESSION TAG                 
SEQRES   1 A  491  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  491  GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG          
SEQRES   3 A  491  LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL          
SEQRES   4 A  491  GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG          
SEQRES   5 A  491  ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN          
SEQRES   6 A  491  VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY          
SEQRES   7 A  491  SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE          
SEQRES   8 A  491  LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO          
SEQRES   9 A  491  ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA          
SEQRES  10 A  491  GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL          
SEQRES  11 A  491  VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS          
SEQRES  12 A  491  SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL          
SEQRES  13 A  491  ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN          
SEQRES  14 A  491  GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN          
SEQRES  15 A  491  GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY          
SEQRES  16 A  491  ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR          
SEQRES  17 A  491  ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA          
SEQRES  18 A  491  VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA          
SEQRES  19 A  491  ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP          
SEQRES  20 A  491  TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN          
SEQRES  21 A  491  GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR          
SEQRES  22 A  491  VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN          
SEQRES  23 A  491  PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER          
SEQRES  24 A  491  ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY          
SEQRES  25 A  491  SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER          
SEQRES  26 A  491  ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS          
SEQRES  27 A  491  TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP          
SEQRES  28 A  491  LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET          
SEQRES  29 A  491  LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER          
SEQRES  30 A  491  PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA          
SEQRES  31 A  491  LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL          
SEQRES  32 A  491  THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE          
SEQRES  33 A  491  ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL          
SEQRES  34 A  491  ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG          
SEQRES  35 A  491  ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET          
SEQRES  36 A  491  LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO          
SEQRES  37 A  491  TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP          
SEQRES  38 A  491  LEU PHE SER TRP ILE ASP GLY LEU CYS GLN                      
SEQRES   1 B  491  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  491  GLY THR GLU ASN LEU TYR PHE GLN SER MET SER ASN ARG          
SEQRES   3 B  491  LEU ILE PHE ASP ALA ASP TRP LEU VAL PRO GLU GLN VAL          
SEQRES   4 B  491  GLN VAL ALA GLY GLN ALA ILE GLN TYR TYR ALA ALA ARG          
SEQRES   5 B  491  ASN ILE GLN TYR VAL GLN HIS PRO VAL ALA ALA ILE GLN          
SEQRES   6 B  491  VAL LEU ASN VAL PHE VAL PRO ALA ALA TYR LEU HIS GLY          
SEQRES   7 B  491  SER SER VAL ASN GLY TYR GLN ARG ALA THR ALA PRO ILE          
SEQRES   8 B  491  LEU MET PRO ASN THR VAL GLY GLY TYR LEU PRO GLY PRO          
SEQRES   9 B  491  ALA ASP ASP PRO GLN ARG VAL THR TRP PRO THR ASN ALA          
SEQRES  10 B  491  GLY THR ILE GLN GLN ALA LEU LYS ARG GLY TYR VAL VAL          
SEQRES  11 B  491  VAL ALA ALA GLY ILE ARG GLY ARG THR THR VAL ASP LYS          
SEQRES  12 B  491  SER GLY GLN ARG VAL GLY GLN ALA PRO ALA PHE ILE VAL          
SEQRES  13 B  491  ASP MET LYS ALA ALA ILE ARG TYR VAL LYS TYR ASN GLN          
SEQRES  14 B  491  GLY ARG LEU PRO GLY ASP ALA ASN ARG ILE ILE THR ASN          
SEQRES  15 B  491  GLY THR SER ALA GLY GLY ALA THR SER ALA LEU ALA GLY          
SEQRES  16 B  491  ALA SER GLY ASN SER ALA TYR PHE GLU PRO ALA LEU THR          
SEQRES  17 B  491  ALA LEU GLY ALA ALA PRO ALA THR ASP ASP ILE PHE ALA          
SEQRES  18 B  491  VAL SER ALA TYR CYS PRO ILE HIS ASN LEU GLU HIS ALA          
SEQRES  19 B  491  ASP MET ALA TYR GLU TRP GLN PHE ASN GLY ILE ASN ASP          
SEQRES  20 B  491  TRP HIS ARG TYR GLN PRO VAL ALA GLY THR THR LYS ASN          
SEQRES  21 B  491  GLY ARG PRO LYS PHE GLU PRO VAL SER GLY GLN LEU THR          
SEQRES  22 B  491  VAL GLU GLU GLN ALA LEU SER LEU ALA LEU LYS ALA GLN          
SEQRES  23 B  491  PHE SER THR TYR LEU ASN GLN LEU LYS LEU THR ALA SER          
SEQRES  24 B  491  ASP GLY THR HIS LEU THR LEU ASN GLU ALA GLY MET GLY          
SEQRES  25 B  491  SER PHE ARG ASP VAL VAL ARG GLN LEU LEU ILE SER SER          
SEQRES  26 B  491  ALA GLN THR ALA PHE ASP GLN GLY THR ASP ILE HIS LYS          
SEQRES  27 B  491  TYR ALA GLY PHE VAL VAL THR GLY ASN GLN VAL THR ASP          
SEQRES  28 B  491  LEU ASP LEU SER ALA TYR LEU LYS SER LEU THR ARG MET          
SEQRES  29 B  491  LYS ALA VAL PRO ALA PHE ASP GLN LEU ASP LEU THR SER          
SEQRES  30 B  491  PRO GLU ASN ASN LEU PHE GLY ASP ALA THR ALA LYS ALA          
SEQRES  31 B  491  LYS HIS PHE THR ALA LEU ALA GLN THR ARG SER THR VAL          
SEQRES  32 B  491  THR ALA GLN LEU ALA ASP ALA GLU LEU ILE GLN ALA ILE          
SEQRES  33 B  491  ASN PRO LEU SER TYR LEU THR THR THR SER SER GLN VAL          
SEQRES  34 B  491  ALA LYS HIS TRP ARG ILE ARG HIS GLY ALA ALA ASP ARG          
SEQRES  35 B  491  ASP THR SER PHE ALA ILE PRO ILE ILE LEU ALA ILE MET          
SEQRES  36 B  491  LEU GLU ASN HIS GLY TYR GLY ILE ASP PHE ALA LEU PRO          
SEQRES  37 B  491  TRP ASP ILE PRO HIS SER GLY ASP TYR ASP LEU GLY ASP          
SEQRES  38 B  491  LEU PHE SER TRP ILE ASP GLY LEU CYS GLN                      
HET    E35  A 501      13                                                       
HET    E35  B 501      13                                                       
HETNAM     E35 ETHYL 3,5-DIHYDROXYBENZOATE                                      
FORMUL   3  E35    2(C9 H10 O4)                                                 
FORMUL   5  HOH   *501(H2 O)                                                    
HELIX    1   1 ASP A    8  LEU A   12  5                                   5    
HELIX    2   2 ALA A   52  HIS A   55  5                                   4    
HELIX    3   3 ASN A   94  GLY A  105  1                                  12    
HELIX    4   4 PRO A  130  ASN A  146  1                                  17    
HELIX    5   5 SER A  163  SER A  175  1                                  13    
HELIX    6   6 SER A  178  TYR A  180  5                                   3    
HELIX    7   7 PHE A  181  GLY A  189  1                                   9    
HELIX    8   8 ASN A  208  ASN A  221  1                                  14    
HELIX    9   9 THR A  251  LEU A  272  1                                  22    
HELIX   10  10 GLY A  290  ASP A  309  1                                  20    
HELIX   11  11 ASP A  313  TYR A  317  5                                   5    
HELIX   12  12 ASP A  331  THR A  340  1                                  10    
HELIX   13  13 SER A  355  PHE A  361  1                                   7    
HELIX   14  14 THR A  372  ARG A  378  1                                   7    
HELIX   15  15 ASP A  387  ILE A  394  1                                   8    
HELIX   16  16 ASN A  395  LEU A  400  5                                   6    
HELIX   17  17 PHE A  424  HIS A  437  1                                  14    
HELIX   18  18 ASP A  456  GLN A  469  1                                  14    
HELIX   19  19 ASP B    8  LEU B   12  5                                   5    
HELIX   20  20 ALA B   52  HIS B   55  5                                   4    
HELIX   21  21 ASN B   94  GLY B  105  1                                  12    
HELIX   22  22 PRO B  130  ASN B  146  1                                  17    
HELIX   23  23 SER B  163  SER B  175  1                                  13    
HELIX   24  24 SER B  178  TYR B  180  5                                   3    
HELIX   25  25 PHE B  181  GLY B  189  1                                   9    
HELIX   26  26 ASN B  208  ASN B  221  1                                  14    
HELIX   27  27 THR B  251  LEU B  272  1                                  22    
HELIX   28  28 GLY B  290  ASP B  309  1                                  20    
HELIX   29  29 ASP B  313  TYR B  317  5                                   5    
HELIX   30  30 ASP B  331  THR B  340  1                                  10    
HELIX   31  31 SER B  355  PHE B  361  1                                   7    
HELIX   32  32 THR B  372  ARG B  378  1                                   7    
HELIX   33  33 ASP B  387  ILE B  394  1                                   8    
HELIX   34  34 ASN B  395  LEU B  400  5                                   6    
HELIX   35  35 PHE B  424  HIS B  437  1                                  14    
HELIX   36  36 ASP B  456  GLN B  469  1                                  14    
SHEET    1   A 9 VAL A  13  VAL A  19  0                                        
SHEET    2   A 9 GLN A  22  GLN A  33 -1  O  ILE A  24   N  VAL A  17           
SHEET    3   A 9 VAL A  44  PRO A  50 -1  O  VAL A  47   N  ALA A  29           
SHEET    4   A 9 VAL A 107  ALA A 111 -1  O  VAL A 108   N  PHE A  48           
SHEET    5   A 9 ILE A  69  PRO A  72  1  N  LEU A  70   O  VAL A 107           
SHEET    6   A 9 ILE A 157  THR A 162  1  O  ILE A 158   N  MET A  71           
SHEET    7   A 9 ALA A 199  TYR A 203  1  O  TYR A 203   N  GLY A 161           
SHEET    8   A 9 HIS A 410  ARG A 414  1  O  ARG A 412   N  VAL A 200           
SHEET    9   A 9 GLY A 440  ALA A 444  1  O  ASP A 442   N  ILE A 413           
SHEET    1   B 2 ASP A 225  VAL A 232  0                                        
SHEET    2   B 2 LYS A 242  GLN A 249 -1  O  GLU A 244   N  GLN A 230           
SHEET    1   C 2 PHE A 320  THR A 323  0                                        
SHEET    2   C 2 GLN A 326  LEU A 330 -1  O  GLN A 326   N  THR A 323           
SHEET    1   D 9 VAL B  13  VAL B  19  0                                        
SHEET    2   D 9 GLN B  22  GLN B  33 -1  O  TYR B  26   N  GLU B  15           
SHEET    3   D 9 VAL B  44  PRO B  50 -1  O  LEU B  45   N  ILE B  32           
SHEET    4   D 9 VAL B 107  ALA B 111 -1  O  VAL B 108   N  PHE B  48           
SHEET    5   D 9 ILE B  69  PRO B  72  1  N  LEU B  70   O  VAL B 107           
SHEET    6   D 9 ILE B 157  ASN B 160  1  O  ILE B 158   N  ILE B  69           
SHEET    7   D 9 ALA B 199  TYR B 203  1  O  ALA B 199   N  ILE B 157           
SHEET    8   D 9 HIS B 410  ARG B 414  1  O  ARG B 412   N  VAL B 200           
SHEET    9   D 9 GLY B 440  ALA B 444  1  O  ASP B 442   N  TRP B 411           
SHEET    1   E 2 ASP B 225  PRO B 231  0                                        
SHEET    2   E 2 PHE B 243  GLN B 249 -1  O  VAL B 246   N  ARG B 228           
SHEET    1   F 2 PHE B 320  THR B 323  0                                        
SHEET    2   F 2 GLN B 326  LEU B 330 -1  O  GLN B 326   N  THR B 323           
CISPEP   1 TRP A   91    PRO A   92          0        -5.64                     
CISPEP   2 ALA A  129    PRO A  130          0         3.68                     
CISPEP   3 VAL A  345    PRO A  346          0        -6.63                     
CISPEP   4 TRP B   91    PRO B   92          0        -3.47                     
CISPEP   5 ALA B  129    PRO B  130          0         1.94                     
CISPEP   6 VAL B  345    PRO B  346          0        -4.25                     
SITE     1 AC1 10 GLY A  76  GLY A  77  TYR A  78  SER A 163                    
SITE     2 AC1 10 ALA A 164  ILE A 206  LYS A 343  GLU A 357                    
SITE     3 AC1 10 ASP A 421  HIS A 451                                          
SITE     1 AC2 10 GLY B  76  GLY B  77  TYR B  78  SER B 163                    
SITE     2 AC2 10 ALA B 164  ILE B 206  LYS B 343  GLU B 357                    
SITE     3 AC2 10 ASP B 421  HIS B 451                                          
CRYST1   46.251   62.726   83.466  70.47  86.55  79.13 P 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      0.021621 -0.004153  0.000067        0.00000                         
SCALE2      0.000000  0.016234 -0.005663        0.00000                         
SCALE3      0.000000  0.000000  0.012712        0.00000                         
TER    3617      GLN A 469                                                      
TER    7248      GLN B 469                                                      
MASTER      492    0    2   36   26    0    6    6 7699    2   26   76          
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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