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LongText Report for: 2PPL-pdb

Name Class
2PPL-pdb
HEADER    HYDROLASE                               30-APR-07   2PPL              
TITLE     HUMAN PANCREATIC LIPASE-RELATED PROTEIN 1                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PANCREATIC LIPASE-RELATED PROTEIN 1;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: PNLIPRP1, PLRP1;                                               
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HIGH5;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC N                              
KEYWDS    HYDROLASE, LIPID DEGRADATION, PANCREATIC LIPASE, STRUCTURAL           
KEYWDS   2 GENOMICS CONSORTIUM, SGC                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WALKER,T.DAVIS,A.SEITOVA,C.BUTLER-COLE,J.WEIGELT,                 
AUTHOR   2 M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-            
AUTHOR   3 PAGANON,STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
REVDAT   1   05-JUN-07 2PPL    0                                                
JRNL        AUTH   J.R.WALKER,T.DAVIS,A.SEITOVA,C.BUTLER-COLE,                  
JRNL        AUTH 2 J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,A.M.EDWARDS,            
JRNL        AUTH 3 A.BOCHKAREV,S.DHE-PAGANON                                    
JRNL        TITL   STRUCTURE OF THE HUMAN PANCREATIC LIPASE-RELATED             
JRNL        TITL 2 PROTEIN 1.                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.GILLER,P.BUCHWALD,D.BLUM-KAELIN,W.HUNZIKER                 
REMARK   1  TITL   TWO NOVEL HUMAN PANCREATIC LIPASE RELATED                    
REMARK   1  TITL 2 PROTEINS, HPLRP1 AND HPLRP2. DIFFERENCES IN                  
REMARK   1  TITL 3 COLIPASE DEPENDENCE AND IN LIPASE ACTIVITY                   
REMARK   1  REF    J.BIOL.CHEM.                  V. 267 16509 1992              
REMARK   1  REFN   ASTM JBCHA3  US ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.20 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30748                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1660                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2189                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 125                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 3822                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.29000                                              
REMARK   3    B22 (A**2) : 2.29000                                              
REMARK   3    B33 (A**2) : -4.58000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.905        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3721 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5056 ; 1.218 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   472 ; 5.936 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;39.496 ;24.826       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   592 ;15.636 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;19.414 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   544 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2897 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1597 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2514 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   230 ; 0.123 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     9 ; 0.123 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    28 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.080 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     1 ; 0.120 ; 0.200       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2325 ; 2.134 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3748 ; 3.456 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1446 ; 4.561 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1308 ; 6.353 ; 7.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    17        A    48                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4570 -10.2310  14.1860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1064 T22:   0.1691                                     
REMARK   3      T33:   0.2018 T12:  -0.0366                                     
REMARK   3      T13:   0.0175 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1799 L22:   2.8569                                     
REMARK   3      L33:   6.6754 L12:  -0.0520                                     
REMARK   3      L13:   0.3123 L23:   2.2759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0680 S12:   0.0397 S13:   0.0573                       
REMARK   3      S21:  -0.0365 S22:   0.2221 S23:  -0.2388                       
REMARK   3      S31:  -0.2126 S32:   0.4789 S33:  -0.1540                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    49        A   100                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7530 -24.6500   4.5940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1840 T22:   0.1520                                     
REMARK   3      T33:   0.2013 T12:  -0.0063                                     
REMARK   3      T13:   0.0113 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1266 L22:   0.2070                                     
REMARK   3      L33:   1.8930 L12:   0.1357                                     
REMARK   3      L13:   0.7297 L23:   0.1979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0025 S12:   0.0589 S13:  -0.0936                       
REMARK   3      S21:  -0.0145 S22:   0.0496 S23:  -0.0116                       
REMARK   3      S31:   0.0884 S32:   0.0866 S33:  -0.0471                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   101        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1280 -26.6710  12.5880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1884 T22:   0.1384                                     
REMARK   3      T33:   0.1727 T12:   0.0003                                     
REMARK   3      T13:   0.0146 T23:  -0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7435 L22:   1.1210                                     
REMARK   3      L33:   1.3826 L12:   1.1554                                     
REMARK   3      L13:   1.9902 L23:  -0.3922                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0473 S12:  -0.0764 S13:  -0.3627                       
REMARK   3      S21:  -0.0146 S22:   0.0030 S23:  -0.0561                       
REMARK   3      S31:   0.0633 S32:  -0.0722 S33:  -0.0503                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   131        A   162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.8920 -14.6830   6.1490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2005 T22:   0.2054                                     
REMARK   3      T33:   0.2085 T12:  -0.0184                                     
REMARK   3      T13:  -0.0029 T23:   0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9363 L22:   0.0042                                     
REMARK   3      L33:   1.4985 L12:   0.0031                                     
REMARK   3      L13:   0.9736 L23:   0.0485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0508 S12:   0.1545 S13:  -0.0176                       
REMARK   3      S21:  -0.0446 S22:   0.0172 S23:  -0.0507                       
REMARK   3      S31:  -0.0483 S32:   0.1352 S33:   0.0336                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   163        A   231                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2510 -12.2850  20.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1827 T22:   0.1889                                     
REMARK   3      T33:   0.2029 T12:  -0.0115                                     
REMARK   3      T13:   0.0069 T23:  -0.0034                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3511 L22:   0.4573                                     
REMARK   3      L33:   0.9807 L12:  -0.1470                                     
REMARK   3      L13:  -0.1189 L23:  -0.0735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:  -0.0512 S13:   0.0013                       
REMARK   3      S21:  -0.0173 S22:   0.0241 S23:  -0.0151                       
REMARK   3      S31:  -0.0361 S32:   0.0164 S33:  -0.0205                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   232        A   256                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7010 -15.3330  31.0800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1676 T22:   0.1825                                     
REMARK   3      T33:   0.1561 T12:  -0.0054                                     
REMARK   3      T13:  -0.0043 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1221 L22:   3.2150                                     
REMARK   3      L33:   1.3898 L12:  -0.5673                                     
REMARK   3      L13:  -0.0165 L23:  -0.5932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:   0.0005 S13:   0.0270                       
REMARK   3      S21:   0.0811 S22:   0.0396 S23:   0.0522                       
REMARK   3      S31:  -0.0862 S32:   0.0206 S33:  -0.0372                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   257        A   273                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5600 -25.0930  33.0060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2609 T22:   0.0671                                     
REMARK   3      T33:   0.1813 T12:  -0.0222                                     
REMARK   3      T13:   0.0010 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3049 L22:   0.8333                                     
REMARK   3      L33:  10.2247 L12:   0.1156                                     
REMARK   3      L13:  -3.5990 L23:  -1.1357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0372 S12:  -0.2738 S13:   0.0255                       
REMARK   3      S21:   0.2441 S22:   0.0346 S23:   0.0190                       
REMARK   3      S31:   0.1777 S32:   0.2910 S33:   0.0026                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   274        A   330                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2630 -17.3610  29.6280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1718 T22:   0.1676                                     
REMARK   3      T33:   0.1929 T12:  -0.0209                                     
REMARK   3      T13:   0.0009 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2835 L22:   0.4059                                     
REMARK   3      L33:   0.8846 L12:  -0.3716                                     
REMARK   3      L13:  -0.0706 L23:  -0.1347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0054 S12:  -0.0023 S13:  -0.0269                       
REMARK   3      S21:  -0.0094 S22:  -0.0068 S23:   0.0169                       
REMARK   3      S31:   0.0589 S32:  -0.0421 S33:   0.0014                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   331        A   353                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2640 -14.6150  28.9980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1331 T22:   0.1716                                     
REMARK   3      T33:   0.1728 T12:   0.0136                                     
REMARK   3      T13:   0.0151 T23:  -0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7191 L22:   4.3999                                     
REMARK   3      L33:   2.5123 L12:   0.4325                                     
REMARK   3      L13:   0.3133 L23:  -2.3478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0398 S12:  -0.0841 S13:   0.0968                       
REMARK   3      S21:   0.0593 S22:  -0.0673 S23:   0.0924                       
REMARK   3      S31:  -0.0176 S32:  -0.0035 S33:   0.0274                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   354        A   373                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9920 -19.5050  48.3230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1530 T22:   0.1915                                     
REMARK   3      T33:   0.1929 T12:  -0.0021                                     
REMARK   3      T13:  -0.0039 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4782 L22:   0.6471                                     
REMARK   3      L33:   4.5139 L12:   0.1601                                     
REMARK   3      L13:  -1.4116 L23:  -0.0187                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0623 S12:   0.0551 S13:   0.0008                       
REMARK   3      S21:   0.0349 S22:   0.0688 S23:   0.0065                       
REMARK   3      S31:  -0.0267 S32:  -0.1256 S33:  -0.1311                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   374        A   396                          
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7520 -23.5620  45.9980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1594 T22:   0.1588                                     
REMARK   3      T33:   0.1999 T12:   0.0132                                     
REMARK   3      T13:   0.0026 T23:   0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8891 L22:   1.8475                                     
REMARK   3      L33:   6.6140 L12:   0.9705                                     
REMARK   3      L13:   0.3857 L23:   2.5384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:  -0.0124 S13:  -0.0777                       
REMARK   3      S21:   0.0237 S22:   0.0618 S23:  -0.0793                       
REMARK   3      S31:   0.1402 S32:  -0.0747 S33:  -0.0424                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   397        A   443                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6810 -21.5530  48.1280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1484 T22:   0.1620                                     
REMARK   3      T33:   0.1886 T12:   0.0137                                     
REMARK   3      T13:  -0.0066 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3431 L22:   0.4598                                     
REMARK   3      L33:   3.3468 L12:   0.1015                                     
REMARK   3      L13:  -0.4062 L23:  -0.5998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0382 S12:   0.0026 S13:  -0.0167                       
REMARK   3      S21:  -0.0225 S22:   0.0318 S23:   0.0153                       
REMARK   3      S31:  -0.0046 S32:  -0.0963 S33:   0.0064                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   444        A   468                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3090 -20.3650  46.8970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1828 T22:   0.2240                                     
REMARK   3      T33:   0.1903 T12:   0.0096                                     
REMARK   3      T13:  -0.0102 T23:  -0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4514 L22:   1.1721                                     
REMARK   3      L33:   4.6607 L12:  -0.1075                                     
REMARK   3      L13:  -0.7784 L23:  -1.4182                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0433 S12:   0.0458 S13:  -0.1709                       
REMARK   3      S21:   0.0114 S22:  -0.0187 S23:   0.0985                       
REMARK   3      S31:   0.0598 S32:  -0.1981 S33:  -0.0246                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL      
REMARK   3  B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U         
REMARK   3  FACTORS                                                             
REMARK   4                                                                      
REMARK   4 2PPL COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-2007.                
REMARK 100 THE RCSB ID CODE IS RCSB042643.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-2007                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97923                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI (111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32518                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 12.200                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11300                            
REMARK 200   FOR THE DATA SET  : 27.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.30600                            
REMARK 200   FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1RP1                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.2M CA ACETATE, 0.1       
REMARK 280  NA CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 291.0K, PH 6.50                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,1/2+Z                                             
REMARK 290       3555   1/2-Y,1/2+X,1/4+Z                                       
REMARK 290       4555   1/2+Y,1/2-X,3/4+Z                                       
REMARK 290       5555   1/2-X,1/2+Y,1/4-Z                                       
REMARK 290       6555   1/2+X,1/2-Y,3/4-Z                                       
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,1/2-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.14000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.43550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.43550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       76.57000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.43550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.43550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      229.71000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.43550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.43550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       76.57000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.43550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.43550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      229.71000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      153.14000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    -7                                                      
REMARK 465     PRO A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     TYR A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     ILE A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     TYR A    12                                                      
REMARK 465     PHE A    13                                                      
REMARK 465     GLN A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     THR A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     GLU A   338                                                      
REMARK 465     SER A   469                                                      
REMARK 465     LEU A   470                                                      
REMARK 465     SER A   471                                                      
REMARK 465     ARG A   472                                                      
REMARK 465     SER A   473                                                      
REMARK 465     THR A   474                                                      
REMARK 465     ARG A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     SER A   477                                                      
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     LYS A  18    CE    NZ                                            
REMARK 470     LYS A  99    CG    CD    CE    NZ                                
REMARK 470     LYS A 126    NZ                                                  
REMARK 470     LYS A 307    CD    CE    NZ                                      
REMARK 470     LYS A 395    CD    CE    NZ                                      
REMARK 470     LYS A 445    CG    CD    CE    NZ                                
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A 373   CG1   ILE A 373   CD1    0.063                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A  18   N   -  CA  -  C   ANGL. DEV. =  7.5 DEGREES           
REMARK 500    LEU A 172   CA  -  CB  -  CG  ANGL. DEV. =  7.4 DEGREES           
REMARK 500    PRO A 229   C   -  N   -  CA  ANGL. DEV. =  8.4 DEGREES           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OXE   RELATED DB: PDB                                   
REMARK 900 PANCREATIC LIPASE-RELATED PROTEIN 2                                  
DBREF  2PPL A   18   467  UNP    P54315   LIPR1_HUMAN     18    467             
SEQADV 2PPL ALA A   -7  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL PRO A   -6  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL GLU A   -5  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A   -4  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A   -3  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A   -2  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A   -1  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A    0  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL HIS A    1  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ASP A    2  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL TYR A    3  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ASP A    4  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ILE A    5  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL PRO A    6  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL THR A    7  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL THR A    8  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL GLU A    9  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ASN A   10  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL LEU A   11  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL TYR A   12  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL PHE A   13  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL GLN A   14  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL GLY A   15  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ALA A   16  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL MET A   17  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ASP A  414  UNP  P54315    GLU   414 VARIANT                        
SEQADV 2PPL PRO A  468  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL SER A  469  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL LEU A  470  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL SER A  471  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ARG A  472  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL SER A  473  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL THR A  474  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL ARG A  475  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL GLY A  476  UNP  P54315              CLONING ARTIFACT               
SEQADV 2PPL SER A  477  UNP  P54315              CLONING ARTIFACT               
SEQRES   1 A  485  ALA PRO GLU HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE          
SEQRES   2 A  485  PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET LYS          
SEQRES   3 A  485  GLU VAL CYS TYR GLU ASP LEU GLY CYS PHE SER ASP THR          
SEQRES   4 A  485  GLU PRO TRP GLY GLY THR ALA ILE ARG PRO LEU LYS ILE          
SEQRES   5 A  485  LEU PRO TRP SER PRO GLU LYS ILE GLY THR ARG PHE LEU          
SEQRES   6 A  485  LEU TYR THR ASN GLU ASN PRO ASN ASN PHE GLN ILE LEU          
SEQRES   7 A  485  LEU LEU SER ASP PRO SER THR ILE GLU ALA SER ASN PHE          
SEQRES   8 A  485  GLN MET ASP ARG LYS THR ARG PHE ILE ILE HIS GLY PHE          
SEQRES   9 A  485  ILE ASP LYS GLY ASP GLU SER TRP VAL THR ASP MET CYS          
SEQRES  10 A  485  LYS LYS LEU PHE GLU VAL GLU GLU VAL ASN CYS ILE CYS          
SEQRES  11 A  485  VAL ASP TRP LYS LYS GLY SER GLN ALA THR TYR THR GLN          
SEQRES  12 A  485  ALA ALA ASN ASN VAL ARG VAL VAL GLY ALA GLN VAL ALA          
SEQRES  13 A  485  GLN MET LEU ASP ILE LEU LEU THR GLU TYR SER TYR PRO          
SEQRES  14 A  485  PRO SER LYS VAL HIS LEU ILE GLY HIS SER LEU GLY ALA          
SEQRES  15 A  485  HIS VAL ALA GLY GLU ALA GLY SER LYS THR PRO GLY LEU          
SEQRES  16 A  485  SER ARG ILE THR GLY LEU ASP PRO VAL GLU ALA SER PHE          
SEQRES  17 A  485  GLU SER THR PRO GLU GLU VAL ARG LEU ASP PRO SER ASP          
SEQRES  18 A  485  ALA ASP PHE VAL ASP VAL ILE HIS THR ASP ALA ALA PRO          
SEQRES  19 A  485  LEU ILE PRO PHE LEU GLY PHE GLY THR ASN GLN GLN MET          
SEQRES  20 A  485  GLY HIS LEU ASP PHE PHE PRO ASN GLY GLY GLU SER MET          
SEQRES  21 A  485  PRO GLY CYS LYS LYS ASN ALA LEU SER GLN ILE VAL ASP          
SEQRES  22 A  485  LEU ASP GLY ILE TRP ALA GLY THR ARG ASP PHE VAL ALA          
SEQRES  23 A  485  CYS ASN HIS LEU ARG SER TYR LYS TYR TYR LEU GLU SER          
SEQRES  24 A  485  ILE LEU ASN PRO ASP GLY PHE ALA ALA TYR PRO CYS THR          
SEQRES  25 A  485  SER TYR LYS SER PHE GLU SER ASP LYS CYS PHE PRO CYS          
SEQRES  26 A  485  PRO ASP GLN GLY CYS PRO GLN MET GLY HIS TYR ALA ASP          
SEQRES  27 A  485  LYS PHE ALA GLY ARG THR SER GLU GLU GLN GLN LYS PHE          
SEQRES  28 A  485  PHE LEU ASN THR GLY GLU ALA SER ASN PHE ALA ARG TRP          
SEQRES  29 A  485  ARG TYR GLY VAL SER ILE THR LEU SER GLY ARG THR ALA          
SEQRES  30 A  485  THR GLY GLN ILE LYS VAL ALA LEU PHE GLY ASN LYS GLY          
SEQRES  31 A  485  ASN THR HIS GLN TYR SER ILE PHE ARG GLY ILE LEU LYS          
SEQRES  32 A  485  PRO GLY SER THR HIS SER TYR GLU PHE ASP ALA LYS LEU          
SEQRES  33 A  485  ASP VAL GLY THR ILE ASP LYS VAL LYS PHE LEU TRP ASN          
SEQRES  34 A  485  ASN ASN VAL ILE ASN PRO THR LEU PRO LYS VAL GLY ALA          
SEQRES  35 A  485  THR LYS ILE THR VAL GLN LYS GLY GLU GLU LYS THR VAL          
SEQRES  36 A  485  TYR ASN PHE CYS SER GLU ASP THR VAL ARG GLU ASP THR          
SEQRES  37 A  485  LEU LEU THR LEU THR PRO CYS PRO SER LEU SER ARG SER          
SEQRES  38 A  485  THR ARG GLY SER                                              
HET     CA      1       1                                                       
HET     NA      2       1                                                       
HET     NA      3       1                                                       
HET     CA      4       1                                                       
HET     CA      5       1                                                       
HET     NA      6       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   2   CA    3(CA1 2+)                                                    
FORMUL   3   NA    3(NA1 1+)                                                    
FORMUL   8  HOH   *218(H2 O1)                                                   
HELIX    1   1 SER A   48  GLY A   53  1                                   6    
HELIX    2   2 PRO A   75  SER A   81  1                                   7    
HELIX    3   3 SER A  103  GLU A  116  1                                  14    
HELIX    4   4 TRP A  125  GLN A  130  1                                   6    
HELIX    5   5 THR A  132  SER A  159  1                                  28    
HELIX    6   6 PRO A  161  SER A  163  5                                   3    
HELIX    7   7 LEU A  172  LYS A  183  1                                  12    
HELIX    8   8 ASP A  210  ALA A  214  5                                   5    
HELIX    9   9 PRO A  226  LEU A  231  1                                   6    
HELIX   10  10 ASP A  265  ALA A  271  1                                   7    
HELIX   11  11 ALA A  278  ASN A  294  1                                  17    
HELIX   12  12 SER A  305  SER A  311  1                                   7    
HELIX   13  13 GLY A  326  PHE A  332  5                                   7    
SHEET    1   A 2 GLU A  19  TYR A  22  0                                        
SHEET    2   A 2 GLY A  26  SER A  29 -1  O  PHE A  28   N  VAL A  20           
SHEET    1   B10 GLN A  68  LEU A  70  0                                        
SHEET    2   B10 ARG A  55  TYR A  59 -1  N  LEU A  58   O  GLN A  68           
SHEET    3   B10 VAL A 118  ASP A 124 -1  O  CYS A 120   N  TYR A  59           
SHEET    4   B10 LYS A  88  ILE A  93  1  N  ILE A  92   O  ILE A 121           
SHEET    5   B10 VAL A 165  HIS A 170  1  O  ILE A 168   N  PHE A  91           
SHEET    6   B10 ARG A 189  LEU A 193  1  O  THR A 191   N  GLY A 169           
SHEET    7   B10 PHE A 216  ILE A 220  1  O  ILE A 220   N  GLY A 192           
SHEET    8   B10 LEU A 242  PRO A 246  1  O  PHE A 244   N  VAL A 219           
SHEET    9   B10 GLN A 341  LEU A 345  1  O  PHE A 343   N  ASP A 243           
SHEET   10   B10 TYR A 301  PRO A 302 -1  N  TYR A 301   O  PHE A 344           
SHEET    1   C 8 GLY A 382  ASN A 383  0                                        
SHEET    2   C 8 ALA A 369  GLY A 379 -1  N  GLY A 379   O  GLY A 382           
SHEET    3   C 8 ILE A 413  ASN A 421 -1  O  ASN A 421   N  GLN A 372           
SHEET    4   C 8 LEU A 462  PRO A 466 -1  O  LEU A 464   N  VAL A 416           
SHEET    5   C 8 VAL A 447  CYS A 451 -1  N  CYS A 451   O  THR A 465           
SHEET    6   C 8 VAL A 432  LYS A 441 -1  N  ILE A 437   O  PHE A 450           
SHEET    7   C 8 TRP A 356  GLY A 366 -1  N  GLY A 359   O  GLN A 440           
SHEET    8   C 8 THR A 399  ALA A 406 -1  O  ALA A 406   N  TRP A 356           
SHEET    1   D 7 TYR A 387  LEU A 394  0                                        
SHEET    2   D 7 ALA A 369  GLY A 379 -1  N  ALA A 369   O  LEU A 394           
SHEET    3   D 7 ILE A 413  ASN A 421 -1  O  ASN A 421   N  GLN A 372           
SHEET    4   D 7 LEU A 462  PRO A 466 -1  O  LEU A 464   N  VAL A 416           
SHEET    5   D 7 VAL A 447  CYS A 451 -1  N  CYS A 451   O  THR A 465           
SHEET    6   D 7 VAL A 432  LYS A 441 -1  N  ILE A 437   O  PHE A 450           
SHEET    7   D 7 THR A 455  VAL A 456 -1  O  VAL A 456   N  VAL A 432           
SSBOND   1 CYS A   21    CYS A   27                                             
SSBOND   2 CYS A  109    CYS A  120                                             
SSBOND   3 CYS A  255    CYS A  279                                             
SSBOND   4 CYS A  303    CYS A  314                                             
SSBOND   5 CYS A  317    CYS A  322                                             
SSBOND   6 CYS A  451    CYS A  467                                             
LINK         O   GLU A  79                NA    NA     2                        
LINK         O   SER A  81                NA    NA     2                        
LINK         O   LYS A 183                NA    NA     6                        
LINK         OE1 GLU A 197                NA    NA     3                        
LINK         O  AGLU A 205                CA    CA     1                        
LINK         O  BGLU A 205                CA    CA     1                        
LINK         O   ARG A 208                CA    CA     1                        
LINK         OD1 ASP A 210                CA    CA     1                        
LINK         OD1 ASP A 213                CA    CA     1                        
LINK         OD2 ASP A 213                CA    CA     1                        
LINK         O   ALA A 225                NA    NA     3                        
LINK         O   GLY A 232                NA    NA     3                        
LINK         O   GLY A 234                NA    NA     3                        
LINK         OD1 ASN A 421                CA    CA     4                        
LINK         O   ASN A 422                CA    CA     4                        
LINK         OD1 ASN A 422                CA    CA     5                        
LINK         O   VAL A 424                CA    CA     5                        
LINK         OD1 ASN A 426                CA    CA     5                        
LINK         OE1 GLU A 458                CA    CA     5                        
LINK         OE2 GLU A 458                CA    CA     4                        
LINK         OE2 GLU A 458                CA    CA     5                        
LINK        CA    CA     1                 O   HOH   104                        
LINK        CA    CA     1                 O   HOH    61                        
LINK        NA    NA     2                 O   HOH   126                        
LINK        NA    NA     2                 O   HOH     9                        
LINK        NA    NA     2                 O   HOH   221                        
LINK        NA    NA     2                 O   HOH   222                        
LINK        NA    NA     3                 O   HOH   112                        
LINK        CA    CA     5                 O   HOH   130                        
LINK        NA    NA     6                 O   HOH    80                        
LINK        NA    NA     6                 O   HOH    92                        
LINK        NA    NA     6                 O   HOH   150                        
CISPEP   1 GLU A   32    PRO A   33          0         2.51                     
CISPEP   2 ILE A  228    PRO A  229          0         2.58                     
CISPEP   3 PHE A  315    PRO A  316          0        -3.78                     
CISPEP   4 SER A  351    ASN A  352          0        -0.30                     
CRYST1   62.871   62.871  306.280  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015906  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003265        0.00000                         
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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