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LongText Report for: 4JUI-pdb

Name Class
4JUI-pdb
HEADER    HYDROLASE                               24-MAR-13   4JUI              
TITLE     CRYSTAL STRUCTURE OF TANNASE FROM FROM LACTOBACILLUS PLANTARUM        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TANNASE;                                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: 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    GALLATE, HYDROLASE, HYDROLYSIS, TANNINS                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.REN,M.WU,Q.WANG,X.PENG,H.WEN,W.J.MCKINSTRY,Q.CHEN                   
REVDAT   1   22-MAY-13 4JUI    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.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 90551                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.180                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.690                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1530                            
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 19.5241 -  3.7725    0.98     8702   156  0.1346 0.1341        
REMARK   3     2  3.7725 -  2.9978    0.98     8665   152  0.1426 0.1610        
REMARK   3     3  2.9978 -  2.6199    0.96     8525   148  0.1600 0.2296        
REMARK   3     4  2.6199 -  2.3808    0.95     8443   144  0.1550 0.1909        
REMARK   3     5  2.3808 -  2.2104    0.94     8309   140  0.1542 0.1411        
REMARK   3     6  2.2104 -  2.0803    0.92     8120   137  0.1520 0.2092        
REMARK   3     7  2.0803 -  1.9762    0.90     7958   137  0.1583 0.1976        
REMARK   3     8  1.9762 -  1.8902    0.89     7855   136  0.1723 0.2022        
REMARK   3     9  1.8902 -  1.8175    0.86     7609   126  0.1754 0.2479        
REMARK   3    10  1.8175 -  1.7548    0.85     7497   130  0.1851 0.2185        
REMARK   3    11  1.7548 -  1.7000    0.83     7338   124  0.1904 0.2529        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
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)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.810           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.84                          
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      :  0.006           7533                                  
REMARK   3   ANGLE     :  1.058          10264                                  
REMARK   3   CHIRALITY :  0.071           1147                                  
REMARK   3   PLANARITY :  0.004           1340                                  
REMARK   3   DIHEDRAL  : 14.313           2707                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (chain A and resid 1:51)                               
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3614 114.8073  88.1600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3165 T22:   0.1065                                     
REMARK   3      T33:   0.0980 T12:  -0.0104                                     
REMARK   3      T13:  -0.0148 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7483 L22:   1.1360                                     
REMARK   3      L33:   2.0623 L12:  -0.1334                                     
REMARK   3      L13:  -0.0664 L23:  -0.1491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0108 S12:  -0.0641 S13:   0.0763                       
REMARK   3      S21:   0.0870 S22:   0.0151 S23:   0.0424                       
REMARK   3      S31:  -0.3954 S32:   0.0771 S33:   0.0018                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (chain A and resid 52:127)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6439 106.2992  84.8485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2090 T22:   0.0819                                     
REMARK   3      T33:   0.0813 T12:   0.0121                                     
REMARK   3      T13:  -0.0090 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7494 L22:   0.8362                                     
REMARK   3      L33:   3.0143 L12:   0.0097                                     
REMARK   3      L13:   0.6951 L23:   0.0307                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0431 S12:  -0.0290 S13:   0.0902                       
REMARK   3      S21:   0.0825 S22:  -0.0037 S23:   0.0405                       
REMARK   3      S31:  -0.3161 S32:  -0.1212 S33:   0.0444                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (chain A and resid 128:229)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.9078  98.7381  74.0715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1324 T22:   0.1279                                     
REMARK   3      T33:   0.0527 T12:   0.0126                                     
REMARK   3      T13:  -0.0005 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2958 L22:   1.9281                                     
REMARK   3      L33:   1.5814 L12:   0.4038                                     
REMARK   3      L13:   0.2969 L23:   0.9308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0021 S12:   0.0304 S13:   0.0369                       
REMARK   3      S21:  -0.0260 S22:   0.0008 S23:  -0.0198                       
REMARK   3      S31:  -0.1161 S32:   0.1485 S33:   0.0004                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (chain A and resid 230:242)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8068 104.1674  76.2288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7756 T22:   1.0871                                     
REMARK   3      T33:   1.3061 T12:   0.0338                                     
REMARK   3      T13:   0.0220 T23:  -0.3000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0461 L22:   3.6852                                     
REMARK   3      L33:   5.7136 L12:   3.6049                                     
REMARK   3      L13:   4.1019 L23:  -0.3758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1339 S12:  -1.0319 S13:   0.8455                       
REMARK   3      S21:   0.3667 S22:  -0.1474 S23:   0.0039                       
REMARK   3      S31:  -0.6308 S32:  -0.1984 S33:   0.2136                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (chain A and resid 243:282)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5935  80.2204  62.3439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1990 T22:   0.1434                                     
REMARK   3      T33:   0.0653 T12:   0.0653                                     
REMARK   3      T13:   0.0028 T23:  -0.0417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0575 L22:   1.7610                                     
REMARK   3      L33:   2.3428 L12:   0.8558                                     
REMARK   3      L13:   0.1324 L23:   0.2641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2267 S12:  -0.3186 S13:   0.1843                       
REMARK   3      S21:   0.1694 S22:   0.0947 S23:   0.0309                       
REMARK   3      S31:   0.0482 S32:  -0.1098 S33:   0.0799                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (chain A and resid 283:461)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  23.3945  84.9230  71.8328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1983 T22:   0.1063                                     
REMARK   3      T33:   0.0569 T12:   0.0152                                     
REMARK   3      T13:  -0.0110 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4874 L22:   1.0025                                     
REMARK   3      L33:   1.3120 L12:   0.1727                                     
REMARK   3      L13:   0.0613 L23:   0.2543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:  -0.0059 S13:   0.0201                       
REMARK   3      S21:   0.0848 S22:   0.0180 S23:  -0.0086                       
REMARK   3      S31:   0.2567 S32:   0.0294 S33:  -0.0115                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (chain A and resid 462:469)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1997  92.4264  93.4088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2593 T22:   0.1554                                     
REMARK   3      T33:   0.1141 T12:   0.0321                                     
REMARK   3      T13:  -0.0723 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1776 L22:   3.2640                                     
REMARK   3      L33:   6.2783 L12:  -0.1291                                     
REMARK   3      L13:  -1.0659 L23:  -1.3303                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0564 S12:  -0.4029 S13:   0.0593                       
REMARK   3      S21:   0.3238 S22:   0.0211 S23:  -0.2939                       
REMARK   3      S31:  -0.1017 S32:   0.5301 S33:   0.1002                       
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 4JUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078520.                                      
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) : NULL                               
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   : 90575                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 65.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 23.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.900                              
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: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 3000, 0.1M TRI-SODIUM      
REMARK 280  CITRATE PH 5.5, VAPOR DIFFUSION, 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 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   943     O    HOH A  1068              1.80            
REMARK 500   OE1  GLN A   310     O    HOH A  1030              1.80            
REMARK 500   O    HOH A   820     O    HOH A   939              1.83            
REMARK 500   O    HOH B  1155     O    HOH B  1156              1.84            
REMARK 500   O    HOH A   717     O    HOH B  1154              1.93            
REMARK 500   O    HOH B  1176     O    HOH B  1177              1.94            
REMARK 500   O    HOH A   826     O    HOH A  1044              1.95            
REMARK 500   NE2  GLN B   350     O    HOH B  1160              1.95            
REMARK 500   O    HOH B   976     O    HOH B  1202              1.95            
REMARK 500   O    HOH B   987     O    HOH B  1060              1.96            
REMARK 500   O    HOH A   863     O    HOH A   869              1.97            
REMARK 500   O    HOH A   989     O    HOH A  1060              1.98            
REMARK 500   OD1  ASN A    31     O    HOH A   823              1.98            
REMARK 500   O    HOH B   802     O    HOH B   999              1.99            
REMARK 500   O    HOH B   943     O    HOH B  1208              1.99            
REMARK 500   O    HOH B   822     O    HOH B  1052              2.00            
REMARK 500   O    HOH B   924     O    HOH B   991              2.01            
REMARK 500   O    HOH B  1145     O    HOH B  1172              2.01            
REMARK 500   O    HOH A   751     O    HOH B   894              2.02            
REMARK 500   OE1  GLN A   310     O    HOH A   854              2.04            
REMARK 500   OE1  GLN B   271     O    HOH B   959              2.04            
REMARK 500   O    HOH B  1063     O    HOH B  1187              2.04            
REMARK 500   NH2  ARG A    64     O    HOH A  1076              2.08            
REMARK 500   NE2  GLN A   350     O    HOH A   944              2.08            
REMARK 500   ND2  ASN A   325     O    HOH A  1091              2.08            
REMARK 500   OE1  GLU B   182     O    HOH B   917              2.10            
REMARK 500   O    HOH B   651     O    HOH B  1185              2.10            
REMARK 500   OE1  GLN A    22     O    HOH A   645              2.11            
REMARK 500   O    HOH A   832     O    HOH B   601              2.11            
REMARK 500   O    HOH B  1173     O    HOH B  1174              2.11            
REMARK 500   O    HOH B   962     O    HOH B  1052              2.13            
REMARK 500   O    HOH B  1157     O    HOH B  1158              2.13            
REMARK 500   O    HOH A  1077     O    HOH B  1128              2.13            
REMARK 500   OG1  THR B   401     O    HOH B   861              2.14            
REMARK 500   O    HOH B  1166     O    HOH B  1167              2.15            
REMARK 500   OE2  GLU A   357     O09  EGR A   501              2.15            
REMARK 500   NE2  GLN B   298     O    HOH B   801              2.15            
REMARK 500   O    HOH B   920     O    HOH B  1214              2.16            
REMARK 500   ND2  ASN B    94     O    HOH B   850              2.16            
REMARK 500   O    HOH B   991     O    HOH B  1218              2.16            
REMARK 500   O    HOH A   821     O    HOH A   934              2.17            
REMARK 500   O    HOH A  1035     O    HOH A  1063              2.17            
REMARK 500   O    HOH A   702     O    HOH A   938              2.17            
REMARK 500   O    HOH A   763     O    HOH A  1051              2.18            
REMARK 500   OD1  ASN B    31     O    HOH B   986              2.19            
REMARK 500   ND2  ASN A    94     O    HOH A   974              2.19            
REMARK 500   N    ALA B   233     O    HOH B  1204              2.19            
REMARK 500   OE2  GLU A   244     O    HOH A   912              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 163     -118.90     64.06                                   
REMARK 500    CYS A 204       58.48     30.22                                   
REMARK 500    ARG A 228     -158.07   -151.29                                   
REMARK 500    ALA A 233     -154.02    -71.28                                   
REMARK 500    THR A 340      145.37     78.29                                   
REMARK 500    ALA A 344     -157.35    -84.38                                   
REMARK 500    PHE A 371       15.87   -141.93                                   
REMARK 500    PRO B 130       31.59    -99.01                                   
REMARK 500    ALA B 163     -116.35     65.04                                   
REMARK 500    CYS B 204       54.26     32.93                                   
REMARK 500    ARG B 228     -150.23   -147.05                                   
REMARK 500    THR B 340      148.59     82.11                                   
REMARK 500    ALA B 344     -156.93    -82.54                                   
REMARK 500    PHE B 371       16.22   -144.85                                   
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 A1083        DISTANCE =  6.23 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGR A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EGR B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGE B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 506                 
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: 4J0I   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4J0K   RELATED DB: PDB                                   
DBREF  4JUI A    1   469  UNP    B3Y018   B3Y018_LACPN     1    469             
DBREF  4JUI B    1   469  UNP    B3Y018   B3Y018_LACPN     1    469             
SEQADV 4JUI SER A    0  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4JUI ALA A  163  UNP  B3Y018    SER   163 ENGINEERED MUTATION            
SEQADV 4JUI SER B    0  UNP  B3Y018              EXPRESSION TAG                 
SEQADV 4JUI ALA B  163  UNP  B3Y018    SER   163 ENGINEERED MUTATION            
SEQRES   1 A  470  SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU          
SEQRES   2 A  470  VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN          
SEQRES   3 A  470  TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO          
SEQRES   4 A  470  VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA          
SEQRES   5 A  470  ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG          
SEQRES   6 A  470  ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY          
SEQRES   7 A  470  TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR          
SEQRES   8 A  470  TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS          
SEQRES   9 A  470  ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG          
SEQRES  10 A  470  THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA          
SEQRES  11 A  470  PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR          
SEQRES  12 A  470  VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN          
SEQRES  13 A  470  ARG ILE ILE THR ASN GLY THR ALA ALA GLY GLY ALA THR          
SEQRES  14 A  470  SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE          
SEQRES  15 A  470  GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR          
SEQRES  16 A  470  ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS          
SEQRES  17 A  470  ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE          
SEQRES  18 A  470  ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA          
SEQRES  19 A  470  GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL          
SEQRES  20 A  470  SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU          
SEQRES  21 A  470  ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU          
SEQRES  22 A  470  LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN          
SEQRES  23 A  470  GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN          
SEQRES  24 A  470  LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY          
SEQRES  25 A  470  THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY          
SEQRES  26 A  470  ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS          
SEQRES  27 A  470  SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN          
SEQRES  28 A  470  LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP          
SEQRES  29 A  470  ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN          
SEQRES  30 A  470  THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU          
SEQRES  31 A  470  LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR          
SEQRES  32 A  470  THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS          
SEQRES  33 A  470  GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE          
SEQRES  34 A  470  ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE          
SEQRES  35 A  470  ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP          
SEQRES  36 A  470  TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU          
SEQRES  37 A  470  CYS GLN                                                      
SEQRES   1 B  470  SER MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU          
SEQRES   2 B  470  VAL PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN          
SEQRES   3 B  470  TYR TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO          
SEQRES   4 B  470  VAL ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA          
SEQRES   5 B  470  ALA TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG          
SEQRES   6 B  470  ALA THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY          
SEQRES   7 B  470  TYR LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR          
SEQRES   8 B  470  TRP PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS          
SEQRES   9 B  470  ARG GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG          
SEQRES  10 B  470  THR THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA          
SEQRES  11 B  470  PRO ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR          
SEQRES  12 B  470  VAL LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP ALA ASN          
SEQRES  13 B  470  ARG ILE ILE THR ASN GLY THR ALA ALA GLY GLY ALA THR          
SEQRES  14 B  470  SER ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE          
SEQRES  15 B  470  GLU PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR          
SEQRES  16 B  470  ASP ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS          
SEQRES  17 B  470  ASN LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE          
SEQRES  18 B  470  ASN GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA          
SEQRES  19 B  470  GLY THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL          
SEQRES  20 B  470  SER GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU          
SEQRES  21 B  470  ALA LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU          
SEQRES  22 B  470  LYS LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN          
SEQRES  23 B  470  GLU ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN          
SEQRES  24 B  470  LEU LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY          
SEQRES  25 B  470  THR ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY          
SEQRES  26 B  470  ASN GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS          
SEQRES  27 B  470  SER LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN          
SEQRES  28 B  470  LEU ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP          
SEQRES  29 B  470  ALA THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN          
SEQRES  30 B  470  THR ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU          
SEQRES  31 B  470  LEU ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR          
SEQRES  32 B  470  THR SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS          
SEQRES  33 B  470  GLY ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE          
SEQRES  34 B  470  ILE LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE          
SEQRES  35 B  470  ASP PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP          
SEQRES  36 B  470  TYR ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU          
SEQRES  37 B  470  CYS GLN                                                      
HET    EGR  A 501      14                                                       
HET    PG4  A 502      13                                                       
HET    PEG  A 503       7                                                       
HET    PGE  A 504      10                                                       
HET    PEG  A 505       7                                                       
HET    PEG  A 506       7                                                       
HET    PEG  A 507       7                                                       
HET    EGR  B 501      14                                                       
HET    PGE  B 502      10                                                       
HET    PEG  B 503       7                                                       
HET    PEG  B 504       7                                                       
HET    PEG  B 505       7                                                       
HET    PEG  B 506       7                                                       
HETNAM     EGR ETHYL 3,4,5-TRIHYDROXYBENZOATE                                   
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     EGR ETHYL GALLATE                                                    
FORMUL   3  EGR    2(C9 H10 O5)                                                 
FORMUL   4  PG4    C8 H18 O5                                                    
FORMUL   5  PEG    8(C4 H10 O3)                                                 
FORMUL   6  PGE    2(C6 H14 O4)                                                 
FORMUL  16  HOH   *1132(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  ARG A  104  1                                  11    
HELIX    4   4 PRO A  130  ASN A  146  1                                  17    
HELIX    5   5 ALA 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  GLN A  310  1                                  21    
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 ALA 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  HIS A 410   N  VAL A 200           
SHEET    9   A 9 GLY A 440  ALA A 444  1  O  GLY A 440   N  TRP A 411           
SHEET    1   B 2 ASP A 225  PRO A 231  0                                        
SHEET    2   B 2 PHE A 243  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  VAL B  47   N  ALA B  29           
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  MET B  71           
SHEET    7   D 9 ALA B 199  TYR B 203  1  O  SER B 201   N  THR B 159           
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  THR B 235  0                                        
SHEET    2   E 2 PRO B 241  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        -1.24                     
CISPEP   2 ALA A  129    PRO A  130          0         3.89                     
CISPEP   3 VAL A  345    PRO A  346          0        -3.21                     
CISPEP   4 TRP B   91    PRO B   92          0        -0.26                     
CISPEP   5 ALA B  129    PRO B  130          0         3.43                     
CISPEP   6 VAL B  345    PRO B  346          0        -6.79                     
SITE     1 AC1 13 GLY A  76  GLY A  77  TYR A  78  ALA A 163                    
SITE     2 AC1 13 ALA A 164  LYS A 343  GLU A 357  ASP A 421                    
SITE     3 AC1 13 HIS A 451  HOH A 711  HOH A 781  HOH A1035                    
SITE     4 AC1 13 HOH A1057                                                     
SITE     1 AC2 10 SER A 379  VAL A 381  THR A 382  ALA A 383                    
SITE     2 AC2 10 GLN B 124  LYS B 144  GLN B 147  ASN B 155                    
SITE     3 AC2 10 HOH B 754  HOH B1006                                          
SITE     1 AC3  3 ASN A 224  LEU A 250  GLN A 255                               
SITE     1 AC4 10 TRP A 218  LYS A 262  ALA A 287  GLY A 288                    
SITE     2 AC4 10 MET A 289  ARG A 293  LEU A 332  SER A 333                    
SITE     3 AC4 10 LEU A 336  HOH A1014                                          
SITE     1 AC5  1 HOH A 998                                                     
SITE     1 AC6  5 TYR A 180  HOH A 621  HOH A 784  PEG B 506                    
SITE     2 AC6  5 HOH B 899                                                     
SITE     1 AC7  4 ARG A 293  ARG A 297  SER A 333  HOH A 825                    
SITE     1 AC8 12 GLY B  76  GLY B  77  TYR B  78  ALA B 163                    
SITE     2 AC8 12 ALA B 164  ILE B 206  LYS B 343  PHE B 348                    
SITE     3 AC8 12 GLU B 357  ASP B 421  HIS B 451  HOH B 874                    
SITE     1 AC9  7 TRP B 218  LYS B 262  ALA B 287  GLY B 288                    
SITE     2 AC9  7 ARG B 293  SER B 333  LEU B 336                               
SITE     1 BC1  2 GLY B 324  ASN B 325                                          
SITE     1 BC2  5 ILE B 432  GLU B 435  HOH B 863  HOH B1040                    
SITE     2 BC2  5 HOH B1132                                                     
SITE     1 BC3  7 THR A 380  VAL A 381  ARG B 141  GLU B 182                    
SITE     2 BC3  7 PRO B 192  ALA B 193  HOH B 973                               
SITE     1 BC4  4 PEG A 506  HOH A 621  TYR B 180  HOH B 979                    
CRYST1   47.212   62.943   84.412  70.66  85.49  79.51 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      0.021181 -0.003920 -0.000427        0.00000                         
SCALE2      0.000000  0.016157 -0.005520        0.00000                         
SCALE3      0.000000  0.000000  0.012558        0.00000                         
TER    3617      GLN A 469                                                      
TER    7248      GLN B 469                                                      
MASTER      465    0   13   36   26    0   26    6 8421    2  117   74          
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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