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LongText Report for: 4PV7-pdb

Name Class
4PV7-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-MAR-14   4PV7              
TITLE     COCRYSTAL STRUCTURE OF DIPEPTIDYL-PEPTIDASE 4 WITH AN INDOLE SCAFFOLD 
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   6 TP103, DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;                         
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ADCP2, CD26, DPP4;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    BETA-PROPELLER, HYDROLASE, EXTROCELLULAR SIDE, HYDROLASE-HYDROLASE    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.XIAO,R.GUO,S.HUANG,H.CUI,S.YE,Z.ZHANG                               
REVDAT   1   18-MAR-15 4PV7    0                                                
JRNL        AUTH   P.XIAO,R.GUO,S.HUANG,H.CUI,S.YE,Z.ZHANG                      
JRNL        TITL   DISCOVERY OF DIPEPTIDYL PEPTIDASE IV (DPP4) INHIBITORS BASED 
JRNL        TITL 2 ON A NOVEL INDOLE SCAFFOLD                                   
JRNL        REF    CHIN.CHEM.LETT.               V.  25   673 2014              
JRNL        REFN                   ISSN 1001-8417                               
JRNL        DOI    10.1016/J.CCLET.2014.03.047                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.24 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) : 3.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.75                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 31241                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1332                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.32                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2354                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 86                           
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11902                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 146.73                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.88000                                              
REMARK   3    B22 (A**2) : 4.88000                                              
REMARK   3    B33 (A**2) : -7.32000                                             
REMARK   3    B12 (A**2) : 2.44000                                              
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): 0.536         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.449         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.906        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12306 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16754 ; 1.163 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1452 ; 5.905 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   614 ;34.885 ;24.007       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1986 ;17.622 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;16.843 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1758 ; 0.078 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9530 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5479 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8247 ; 0.314 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   434 ; 0.136 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.396 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     3 ; 0.242 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
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):  7386 ; 0.205 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11748 ; 0.366 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5798 ; 0.578 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  5006 ; 0.955 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     40       A     766      1                      
REMARK   3           1     B     40       B     766      1                      
REMARK   3           2     A   1000       A    1000      1                      
REMARK   3           2     B   1000       B    1000      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   5974 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   5974 ;  0.07 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
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    40        A    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3384  14.2155  30.0950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1738 T22:   0.5216                                     
REMARK   3      T33:   0.7124 T12:   0.0994                                     
REMARK   3      T13:  -0.0444 T23:   0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5410 L22:   3.6453                                     
REMARK   3      L33:   2.9468 L12:   1.2092                                     
REMARK   3      L13:  -3.0897 L23:  -1.8758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3510 S12:   0.0959 S13:  -1.6257                       
REMARK   3      S21:  -0.3701 S22:  -0.3594 S23:   0.1235                       
REMARK   3      S31:   1.0546 S32:  -0.2088 S33:   0.7104                       
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    91        A   206                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5127  21.2204  23.5853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2285 T22:   0.0084                                     
REMARK   3      T33:  -0.0203 T12:  -0.1639                                     
REMARK   3      T13:   0.1358 T23:  -0.1918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9331 L22:   3.1843                                     
REMARK   3      L33:   3.6180 L12:   0.4237                                     
REMARK   3      L13:  -0.0813 L23:  -0.4517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1919 S12:   0.3073 S13:  -1.1465                       
REMARK   3      S21:  -0.4229 S22:  -0.0818 S23:   0.3073                       
REMARK   3      S31:   1.0518 S32:  -0.2805 S33:   0.2737                       
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   207        A   284                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.1322  36.4325  25.5941              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.5093 T22:  -0.0761                                     
REMARK   3      T33:  -0.3593 T12:  -0.0195                                     
REMARK   3      T13:   0.0143 T23:  -0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0644 L22:   2.8430                                     
REMARK   3      L33:   3.1259 L12:   1.5182                                     
REMARK   3      L13:  -2.1640 L23:  -2.0570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2793 S12:  -0.0294 S13:  -0.0843                       
REMARK   3      S21:   0.0436 S22:   0.2058 S23:   0.4821                       
REMARK   3      S31:   0.6654 S32:  -0.4440 S33:   0.0734                       
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   285        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.3918  38.9268  45.6360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0427 T22:   0.3307                                     
REMARK   3      T33:  -0.4164 T12:  -0.1193                                     
REMARK   3      T13:   0.3374 T23:  -0.0733                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4951 L22:   3.3194                                     
REMARK   3      L33:   0.4441 L12:  -0.6065                                     
REMARK   3      L13:   0.3838 L23:  -0.7698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2085 S12:  -0.8981 S13:   0.0711                       
REMARK   3      S21:   1.1945 S22:  -0.3134 S23:   0.8775                       
REMARK   3      S31:  -0.2201 S32:  -0.0435 S33:   0.1049                       
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   359        A   429                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4586  32.1417  54.0449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2225 T22:   0.4949                                     
REMARK   3      T33:  -0.5561 T12:  -0.0327                                     
REMARK   3      T13:  -0.0914 T23:   0.1198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3173 L22:   2.4550                                     
REMARK   3      L33:   2.3190 L12:   0.9172                                     
REMARK   3      L13:   0.3057 L23:  -1.9718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1123 S12:  -1.0285 S13:  -0.6501                       
REMARK   3      S21:   1.1890 S22:  -0.1390 S23:   0.2173                       
REMARK   3      S31:  -0.0607 S32:   0.2428 S33:   0.2513                       
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   430        A   578                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1650  28.6782  40.8542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1870 T22:   0.4437                                     
REMARK   3      T33:  -0.2040 T12:   0.0709                                     
REMARK   3      T13:  -0.2535 T23:   0.3029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8650 L22:   3.2396                                     
REMARK   3      L33:   2.2032 L12:  -0.4213                                     
REMARK   3      L13:  -0.8703 L23:  -0.8054                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0488 S12:  -0.6221 S13:  -0.8045                       
REMARK   3      S21:   0.7118 S22:  -0.4804 S23:  -0.6893                       
REMARK   3      S31:   0.3135 S32:   0.6945 S33:   0.5291                       
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   579        A   671                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.4401  50.6043  34.5202              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4269 T22:   0.0245                                     
REMARK   3      T33:  -0.4510 T12:  -0.0664                                     
REMARK   3      T13:  -0.2087 T23:   0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6010 L22:   2.9450                                     
REMARK   3      L33:   4.0397 L12:   0.3592                                     
REMARK   3      L13:  -0.6996 L23:  -0.9449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1409 S12:  -0.5840 S13:   0.1558                       
REMARK   3      S21:   0.6780 S22:  -0.4714 S23:  -0.7382                       
REMARK   3      S31:  -0.3247 S32:   0.6042 S33:   0.3305                       
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   672        A   712                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3619  56.5813  26.4625              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4719 T22:  -0.1377                                     
REMARK   3      T33:  -0.5048 T12:  -0.0692                                     
REMARK   3      T13:  -0.2091 T23:  -0.1071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7149 L22:   4.6436                                     
REMARK   3      L33:   5.1690 L12:  -1.2967                                     
REMARK   3      L13:  -3.1660 L23:   1.3232                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3038 S12:  -1.0178 S13:   0.1122                       
REMARK   3      S21:   0.1066 S22:  -0.5408 S23:   0.0119                       
REMARK   3      S31:  -0.7493 S32:   0.6824 S33:   0.2371                       
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   713        A   766                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0419  46.2766  16.4535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.6969 T22:  -0.1784                                     
REMARK   3      T33:  -0.3867 T12:   0.0814                                     
REMARK   3      T13:  -0.1135 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5807 L22:   2.8040                                     
REMARK   3      L33:   4.8711 L12:  -0.6677                                     
REMARK   3      L13:  -1.7304 L23:  -0.8205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3121 S12:  -0.5380 S13:   0.0116                       
REMARK   3      S21:  -0.1609 S22:  -0.5244 S23:  -0.8219                       
REMARK   3      S31:   0.2275 S32:   0.8316 S33:   0.2123                       
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 :   B    40        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.9534  84.5922  -9.0291              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2962 T22:   0.3951                                     
REMARK   3      T33:   0.5222 T12:   0.0150                                     
REMARK   3      T13:   0.0791 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2421 L22:   1.3955                                     
REMARK   3      L33:   4.2632 L12:  -1.7145                                     
REMARK   3      L13:   4.8270 L23:  -0.6254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3595 S12:  -0.4202 S13:   1.7940                       
REMARK   3      S21:  -0.1394 S22:  -0.3607 S23:  -0.1402                       
REMARK   3      S31:  -1.1367 S32:  -0.1716 S33:   0.7201                       
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 :   B    91        B   206                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5423  77.0707  -5.0900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0743 T22:   0.0427                                     
REMARK   3      T33:   0.1634 T12:   0.2925                                     
REMARK   3      T13:  -0.1642 T23:   0.1326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9749 L22:   6.2752                                     
REMARK   3      L33:   5.7828 L12:  -1.1797                                     
REMARK   3      L13:  -0.3491 L23:  -0.5695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1013 S12:  -0.1589 S13:   0.8494                       
REMARK   3      S21:  -0.2626 S22:   0.3559 S23:   1.1545                       
REMARK   3      S31:  -1.2241 S32:  -0.7128 S33:  -0.4572                       
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 :   B   207        B   284                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5903  61.8239  -7.2122              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3809 T22:   0.1292                                     
REMARK   3      T33:  -0.2033 T12:   0.0630                                     
REMARK   3      T13:  -0.3680 T23:   0.1390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6185 L22:   4.2664                                     
REMARK   3      L33:   6.3683 L12:  -0.6392                                     
REMARK   3      L13:   0.9225 L23:  -3.5223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:   0.3048 S13:   0.3530                       
REMARK   3      S21:  -1.0912 S22:   0.3994 S23:   0.9280                       
REMARK   3      S31:  -0.1533 S32:  -1.0335 S33:  -0.3585                       
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 :   B   285        B   358                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.5749  59.2817 -27.2619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6465 T22:   0.5644                                     
REMARK   3      T33:  -0.2974 T12:  -0.0628                                     
REMARK   3      T13:  -0.6418 T23:   0.1236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7463 L22:   1.0365                                     
REMARK   3      L33:   1.6581 L12:  -0.5685                                     
REMARK   3      L13:  -1.6305 L23:   0.1908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3995 S12:   1.1216 S13:   0.1345                       
REMARK   3      S21:  -1.3086 S22:   0.2824 S23:   0.5993                       
REMARK   3      S31:   0.0528 S32:  -1.0304 S33:   0.1172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   359        B   429                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.9666  66.4176 -33.8861              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8919 T22:   0.2250                                     
REMARK   3      T33:  -0.5683 T12:  -0.0939                                     
REMARK   3      T13:  -0.1223 T23:   0.0718                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6484 L22:   4.3791                                     
REMARK   3      L33:   3.3555 L12:  -1.2202                                     
REMARK   3      L13:   3.6198 L23:  -3.2933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0490 S12:   1.1131 S13:   0.1785                       
REMARK   3      S21:  -1.4556 S22:   0.1307 S23:   0.2600                       
REMARK   3      S31:   0.2442 S32:  -0.0569 S33:  -0.0817                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   430        B   578                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0059  70.3151 -18.7345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2081 T22:   0.0662                                     
REMARK   3      T33:  -0.2305 T12:  -0.1142                                     
REMARK   3      T13:   0.2430 T23:   0.1219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3982 L22:   2.3650                                     
REMARK   3      L33:   2.9707 L12:  -0.2541                                     
REMARK   3      L13:   0.6037 L23:  -0.7678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0691 S12:   0.5166 S13:   0.6179                       
REMARK   3      S21:  -1.2172 S22:  -0.1961 S23:  -0.7653                       
REMARK   3      S31:  -0.3712 S32:   0.7524 S33:   0.2653                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   579        B   671                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2207  48.2966 -12.8706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0272 T22:  -0.2382                                     
REMARK   3      T33:  -0.4707 T12:   0.0749                                     
REMARK   3      T13:   0.1842 T23:  -0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9988 L22:   1.9563                                     
REMARK   3      L33:   3.2458 L12:   0.4443                                     
REMARK   3      L13:   0.5681 L23:  -0.0980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2445 S12:   0.2670 S13:  -0.2274                       
REMARK   3      S21:  -1.1611 S22:  -0.1022 S23:  -0.6845                       
REMARK   3      S31:   0.4474 S32:   0.4437 S33:   0.3467                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   672        B   712                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4129  42.1724  -5.6045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2445 T22:  -0.3241                                     
REMARK   3      T33:  -0.5484 T12:   0.0237                                     
REMARK   3      T13:   0.1756 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.3972 L22:   4.8651                                     
REMARK   3      L33:   4.7716 L12:  -1.0500                                     
REMARK   3      L13:   2.4072 L23:   0.7045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0147 S12:   0.7419 S13:  -0.6649                       
REMARK   3      S21:  -0.7937 S22:  -0.2254 S23:  -0.1710                       
REMARK   3      S31:   0.7761 S32:   0.3423 S33:   0.2402                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   713        B   766                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6032  52.6748   5.2342              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.6175 T22:  -0.0843                                     
REMARK   3      T33:  -0.4714 T12:   0.1106                                     
REMARK   3      T13:  -0.0086 T23:   0.0043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8101 L22:   5.0768                                     
REMARK   3      L33:   3.3640 L12:   1.0978                                     
REMARK   3      L13:  -1.0401 L23:  -0.2739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2788 S12:  -0.3880 S13:  -0.0385                       
REMARK   3      S21:  -0.2498 S22:  -0.4266 S23:  -0.7308                       
REMARK   3      S31:   0.1273 S32:   0.8514 S33:   0.1477                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4PV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085259.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32631                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : 0.11000                            
REMARK 200   FOR THE DATA SET  : 29.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00000                            
REMARK 200  R SYM FOR SHELL            (I) : 1.00000                            
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 2000, 0.1M BICINE, PH 8.0,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      191.17067            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       95.58533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     HIS A    18                                                      
REMARK 465     HIS A    19                                                      
REMARK 465     HIS A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     TYR A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     ILE A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     THR A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     ASN A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     TYR A    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     GLN A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     MET A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     SER A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     HIS B    19                                                      
REMARK 465     HIS B    20                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     TYR B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     ILE B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     THR B    27                                                      
REMARK 465     GLU B    28                                                      
REMARK 465     ASN B    29                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     TYR B    31                                                      
REMARK 465     PHE B    32                                                      
REMARK 465     GLN B    33                                                      
REMARK 465     GLY B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     MET B    36                                                      
REMARK 465     GLY B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     SER B    39                                                      
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     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  40    CG   CD   NE   CZ   NH1  NH2                        
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    SER A  64     -145.78   -118.47                                   
REMARK 500    HIS A  66       11.32   -156.26                                   
REMARK 500    GLU A  73      -59.34     57.87                                   
REMARK 500    GLN A 123      -97.26   -107.88                                   
REMARK 500    TRP A 124     -150.32    -99.23                                   
REMARK 500    HIS A 162       38.68   -159.13                                   
REMARK 500    ASN A 169       56.56     33.23                                   
REMARK 500    ILE A 193      -58.58   -128.88                                   
REMARK 500    VAL A 207      -63.04   -103.37                                   
REMARK 500    SER A 242     -162.93     62.45                                   
REMARK 500    SER A 275       49.58   -106.86                                   
REMARK 500    ILE A 295      -18.76    -46.68                                   
REMARK 500    GLN A 320       45.26    -74.88                                   
REMARK 500    ALA A 342        0.82    -63.55                                   
REMARK 500    ALA A 409      144.33   -174.29                                   
REMARK 500    ASN A 450       79.46   -151.90                                   
REMARK 500    GLN A 455      -10.75   -140.55                                   
REMARK 500    ASP A 488        9.26     55.86                                   
REMARK 500    GLN A 508       97.61    -69.69                                   
REMARK 500    ASN A 520       54.71     35.66                                   
REMARK 500    ASN A 562     -168.27   -127.10                                   
REMARK 500    ARG A 596       14.47     51.55                                   
REMARK 500    THR A 600      -97.53   -131.94                                   
REMARK 500    SER A 630     -104.39     64.30                                   
REMARK 500    ALA A 654       62.03     33.76                                   
REMARK 500    ASP A 678      -85.37   -112.75                                   
REMARK 500    ASN A 679       16.71   -147.16                                   
REMARK 500    ASN A 710      -79.32    -79.59                                   
REMARK 500    ASP A 737       -0.75     64.80                                   
REMARK 500    ASP A 739     -147.22    -99.40                                   
REMARK 500    ILE A 742       50.30     37.23                                   
REMARK 500    SER B  64     -145.77   -119.08                                   
REMARK 500    HIS B  66       10.74   -156.97                                   
REMARK 500    GLU B  73      -59.40     57.67                                   
REMARK 500    SER B  93        4.33    -69.73                                   
REMARK 500    GLN B 123      -94.93   -107.96                                   
REMARK 500    TRP B 124     -145.22   -100.31                                   
REMARK 500    HIS B 162       36.47   -159.46                                   
REMARK 500    ASN B 169       55.08     34.74                                   
REMARK 500    ILE B 193      -57.86   -129.98                                   
REMARK 500    VAL B 207      -64.37   -103.06                                   
REMARK 500    SER B 242     -164.11     62.60                                   
REMARK 500    SER B 275       47.52   -106.96                                   
REMARK 500    GLN B 320       47.12    -76.38                                   
REMARK 500    ALA B 342        2.49    -61.45                                   
REMARK 500    ILE B 389      -39.96    -37.08                                   
REMARK 500    ALA B 409      146.53   -173.34                                   
REMARK 500    ASN B 450       79.18   -152.82                                   
REMARK 500    GLN B 455       -8.81   -142.80                                   
REMARK 500    ASP B 488        7.23     55.07                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CJP A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CJP B 1000                
DBREF  4PV7 A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  4PV7 B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 4PV7 HIS A   15  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS A   16  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS A   17  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS A   18  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS A   19  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS A   20  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASP A   21  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 TYR A   22  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASP A   23  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ILE A   24  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 PRO A   25  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 THR A   26  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 THR A   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLU A   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASN A   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 LEU A   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 TYR A   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 PHE A   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLN A   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLY A   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ALA A   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 MET A   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLY A   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 SER A   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   15  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   16  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   17  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   18  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   19  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 HIS B   20  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASP B   21  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 TYR B   22  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASP B   23  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ILE B   24  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 PRO B   25  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 THR B   26  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 THR B   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLU B   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ASN B   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 LEU B   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 TYR B   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 PHE B   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLN B   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLY B   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 ALA B   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 MET B   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 GLY B   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 4PV7 SER B   38  UNP  P27487              EXPRESSION TAG                 
SEQRES   1 A  752  HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR          
SEQRES   2 A  752  GLU ASN LEU TYR PHE GLN GLY ALA MET GLY SER SER ARG          
SEQRES   3 A  752  LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR          
SEQRES   4 A  752  ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS          
SEQRES   5 A  752  GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE          
SEQRES   6 A  752  ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN          
SEQRES   7 A  752  SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR          
SEQRES   8 A  752  SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR          
SEQRES   9 A  752  ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER          
SEQRES  10 A  752  TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR          
SEQRES  11 A  752  GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP          
SEQRES  12 A  752  SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN          
SEQRES  13 A  752  ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR          
SEQRES  14 A  752  ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN          
SEQRES  15 A  752  GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER          
SEQRES  16 A  752  ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE          
SEQRES  17 A  752  LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU          
SEQRES  18 A  752  ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR          
SEQRES  19 A  752  PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA          
SEQRES  20 A  752  VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP          
SEQRES  21 A  752  SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE          
SEQRES  22 A  752  THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU          
SEQRES  23 A  752  CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU          
SEQRES  24 A  752  GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP          
SEQRES  25 A  752  ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS          
SEQRES  26 A  752  LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY          
SEQRES  27 A  752  TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR          
SEQRES  28 A  752  LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU          
SEQRES  29 A  752  GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS          
SEQRES  30 A  752  LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL          
SEQRES  31 A  752  ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR          
SEQRES  32 A  752  ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN          
SEQRES  33 A  752  LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR          
SEQRES  34 A  752  CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR          
SEQRES  35 A  752  TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN          
SEQRES  36 A  752  LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU          
SEQRES  37 A  752  HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU          
SEQRES  38 A  752  ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN          
SEQRES  39 A  752  MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU          
SEQRES  40 A  752  THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE          
SEQRES  41 A  752  ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR          
SEQRES  42 A  752  ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG          
SEQRES  43 A  752  LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE          
SEQRES  44 A  752  ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN          
SEQRES  45 A  752  GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY          
SEQRES  46 A  752  THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN          
SEQRES  47 A  752  PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA          
SEQRES  48 A  752  ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET          
SEQRES  49 A  752  VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE          
SEQRES  50 A  752  ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER          
SEQRES  51 A  752  VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU          
SEQRES  52 A  752  ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER          
SEQRES  53 A  752  ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE          
SEQRES  54 A  752  HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER          
SEQRES  55 A  752  ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP          
SEQRES  56 A  752  PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE          
SEQRES  57 A  752  ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET          
SEQRES  58 A  752  SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO                  
SEQRES   1 B  752  HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR          
SEQRES   2 B  752  GLU ASN LEU TYR PHE GLN GLY ALA MET GLY SER SER ARG          
SEQRES   3 B  752  LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR TYR          
SEQRES   4 B  752  ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP HIS          
SEQRES   5 B  752  GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL PHE          
SEQRES   6 B  752  ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU ASN          
SEQRES   7 B  752  SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP TYR          
SEQRES   8 B  752  SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU TYR          
SEQRES   9 B  752  ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA SER          
SEQRES  10 B  752  TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE THR          
SEQRES  11 B  752  GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR TRP          
SEQRES  12 B  752  SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN ASN          
SEQRES  13 B  752  ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER TYR          
SEQRES  14 B  752  ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR ASN          
SEQRES  15 B  752  GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE SER          
SEQRES  16 B  752  ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR PHE          
SEQRES  17 B  752  LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO LEU          
SEQRES  18 B  752  ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN TYR          
SEQRES  19 B  752  PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY ALA          
SEQRES  20 B  752  VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR ASP          
SEQRES  21 B  752  SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN ILE          
SEQRES  22 B  752  THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR LEU          
SEQRES  23 B  752  CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER LEU          
SEQRES  24 B  752  GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET ASP          
SEQRES  25 B  752  ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN CYS          
SEQRES  26 B  752  LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR GLY          
SEQRES  27 B  752  TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE THR          
SEQRES  28 B  752  LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN GLU          
SEQRES  29 B  752  GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP LYS          
SEQRES  30 B  752  LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU VAL          
SEQRES  31 B  752  ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR TYR          
SEQRES  32 B  752  ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG ASN          
SEQRES  33 B  752  LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL THR          
SEQRES  34 B  752  CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN TYR          
SEQRES  35 B  752  TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR GLN          
SEQRES  36 B  752  LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR LEU          
SEQRES  37 B  752  HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU GLU          
SEQRES  38 B  752  ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL GLN          
SEQRES  39 B  752  MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN GLU          
SEQRES  40 B  752  THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS PHE          
SEQRES  41 B  752  ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL TYR          
SEQRES  42 B  752  ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE ARG          
SEQRES  43 B  752  LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN ILE          
SEQRES  44 B  752  ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR GLN          
SEQRES  45 B  752  GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU GLY          
SEQRES  46 B  752  THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG GLN          
SEQRES  47 B  752  PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE ALA          
SEQRES  48 B  752  ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER MET          
SEQRES  49 B  752  VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY ILE          
SEQRES  50 B  752  ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP SER          
SEQRES  51 B  752  VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO GLU          
SEQRES  52 B  752  ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET SER          
SEQRES  53 B  752  ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU ILE          
SEQRES  54 B  752  HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN SER          
SEQRES  55 B  752  ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL ASP          
SEQRES  56 B  752  PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY ILE          
SEQRES  57 B  752  ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS MET          
SEQRES  58 B  752  SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO                  
HET    CJP  A1000      23                                                       
HET    CJP  B1000      23                                                       
HETNAM     CJP 1-[2-(2,4-DICHLOROPHENYL)-1-(METHYLSULFONYL)-1H-INDOL-           
HETNAM   2 CJP  3-YL]METHANAMINE                                                
FORMUL   3  CJP    2(C16 H14 CL2 N2 O2 S)                                       
HELIX    1   1 THR A   44  LYS A   50  1                                   7    
HELIX    2   2 GLU A   91  ASP A   96  5                                   6    
HELIX    3   3 ASP A  200  VAL A  207  1                                   8    
HELIX    4   4 ASP A  274  LEU A  276  5                                   3    
HELIX    5   5 PRO A  290  ILE A  295  1                                   6    
HELIX    6   6 LEU A  340  GLN A  344  5                                   5    
HELIX    7   7 GLU A  421  MET A  425  5                                   5    
HELIX    8   8 ASN A  497  GLN A  505  1                                   9    
HELIX    9   9 ASN A  562  ASN A  572  1                                  11    
HELIX   10  10 GLY A  587  HIS A  592  1                                   6    
HELIX   11  11 ALA A  593  ASN A  595  5                                   3    
HELIX   12  12 THR A  600  LYS A  615  1                                  16    
HELIX   13  13 SER A  630  GLY A  641  1                                  12    
HELIX   14  14 ARG A  658  TYR A  662  5                                   5    
HELIX   15  15 ASP A  663  GLY A  672  1                                  10    
HELIX   16  16 ASN A  679  ASN A  685  1                                   7    
HELIX   17  17 SER A  686  THR A  687  5                                   2    
HELIX   18  18 VAL A  688  VAL A  698  5                                  11    
HELIX   19  19 HIS A  712  VAL A  726  1                                  15    
HELIX   20  20 SER A  744  PHE A  763  1                                  20    
HELIX   21  21 THR B   44  LYS B   50  1                                   7    
HELIX   22  22 GLU B   91  ASP B   96  5                                   6    
HELIX   23  23 ASP B  200  VAL B  207  1                                   8    
HELIX   24  24 ASP B  274  LEU B  276  5                                   3    
HELIX   25  25 PRO B  290  ILE B  295  1                                   6    
HELIX   26  26 LEU B  340  GLN B  344  5                                   5    
HELIX   27  27 GLU B  421  MET B  425  5                                   5    
HELIX   28  28 ASN B  497  GLN B  505  1                                   9    
HELIX   29  29 ASN B  562  ASN B  572  1                                  11    
HELIX   30  30 GLY B  587  HIS B  592  1                                   6    
HELIX   31  31 ALA B  593  ASN B  595  5                                   3    
HELIX   32  32 THR B  600  LYS B  615  1                                  16    
HELIX   33  33 SER B  630  GLY B  641  1                                  12    
HELIX   34  34 ARG B  658  TYR B  662  5                                   5    
HELIX   35  35 ASP B  663  GLY B  672  1                                  10    
HELIX   36  36 ASN B  679  ASN B  685  1                                   7    
HELIX   37  37 SER B  686  THR B  687  5                                   2    
HELIX   38  38 VAL B  688  VAL B  698  5                                  11    
HELIX   39  39 HIS B  712  VAL B  726  1                                  15    
HELIX   40  40 SER B  744  PHE B  763  1                                  20    
SHEET    1   A 2 LYS A  41  THR A  42  0                                        
SHEET    2   A 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1   B 4 LEU A  60  TRP A  62  0                                        
SHEET    2   B 4 GLU A  67  GLN A  72 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   B 4 ASN A  75  ASN A  80 -1  O  ASN A  75   N  GLN A  72           
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  LEU A  90   N  ILE A  76           
SHEET    1   C 4 ILE A 102  ILE A 107  0                                        
SHEET    2   C 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  ASP A 133   N  LEU A 116           
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   D 4 TRP A 154  TRP A 157  0                                        
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   D 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   E 3 ILE A 194  ASN A 196  0                                        
SHEET    2   E 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   F 4 ILE A 194  ASN A 196  0                                        
SHEET    2   F 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   F 4 THR A 265  ASN A 272 -1  O  VAL A 271   N  LEU A 223           
SHEET    4   F 4 SER A 284  ILE A 287 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   G 2 LEU A 235  PHE A 240  0                                        
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   H 4 HIS A 298  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   H 4 TYR A 322  ASP A 331 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   H 4 ARG A 336  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  THR A 307  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   I 4 TYR A 322  ASP A 331 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1   J 4 HIS A 363  PHE A 364  0                                        
SHEET    2   J 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   J 4 ARG A 382  GLN A 388 -1  O  CYS A 385   N  LYS A 373           
SHEET    4   J 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   K 4 VAL A 404  LEU A 410  0                                        
SHEET    2   K 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3   K 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   K 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   L 4 TYR A 457  PHE A 461  0                                        
SHEET    2   L 4 TYR A 467  CYS A 472 -1  O  ARG A 471   N  SER A 458           
SHEET    3   L 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   L 4 GLY A 490  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1   M 8 SER A 511  LEU A 519  0                                        
SHEET    2   M 8 THR A 522  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   M 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   M 8 TYR A 540  VAL A 546  1  N  ASP A 545   O  ALA A 576           
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  ASP A 620   N  TYR A 540           
SHEET    6   M 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   M 8 GLU A 699  GLY A 705  1  O  ILE A 703   N  ALA A 652           
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1   N 2 LYS B  41  THR B  42  0                                        
SHEET    2   N 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   O 4 LEU B  60  TRP B  62  0                                        
SHEET    2   O 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   O 4 ASN B  75  ASN B  80 -1  O  ASN B  75   N  GLN B  72           
SHEET    4   O 4 SER B  86  LEU B  90 -1  O  LEU B  90   N  ILE B  76           
SHEET    1   P 4 ILE B 102  ILE B 107  0                                        
SHEET    2   P 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   P 4 TYR B 128  ASP B 136 -1  O  ASP B 133   N  LEU B 116           
SHEET    4   P 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   Q 4 TRP B 154  TRP B 157  0                                        
SHEET    2   Q 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   Q 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   Q 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   R 3 ILE B 194  ASN B 196  0                                        
SHEET    2   R 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   S 4 ILE B 194  ASN B 196  0                                        
SHEET    2   S 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   S 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4   S 4 ILE B 285  ILE B 287 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   T 2 LEU B 235  PHE B 240  0                                        
SHEET    2   T 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   U 4 HIS B 298  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  SER B 312   N  THR B 304           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  VAL B 324   N  TRP B 315           
SHEET    4   U 4 TRP B 337  ASN B 338 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   V 4 HIS B 298  THR B 307  0                                        
SHEET    2   V 4 ARG B 310  ARG B 317 -1  O  SER B 312   N  THR B 304           
SHEET    3   V 4 TYR B 322  TYR B 330 -1  O  VAL B 324   N  TRP B 315           
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   W 4 HIS B 363  PHE B 364  0                                        
SHEET    2   W 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   W 4 ARG B 382  GLN B 388 -1  O  CYS B 385   N  LYS B 373           
SHEET    4   W 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   X 4 VAL B 404  LEU B 410  0                                        
SHEET    2   X 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  GLU B 408           
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   X 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   Y 4 TYR B 457  PHE B 461  0                                        
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4   Y 4 GLY B 490  GLU B 495 -1  O  GLU B 495   N  TYR B 480           
SHEET    1   Z 8 SER B 511  LEU B 519  0                                        
SHEET    2   Z 8 THR B 522  LEU B 530 -1  O  TYR B 526   N  ASP B 515           
SHEET    3   Z 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   Z 8 TYR B 540  VAL B 546  1  N  ASP B 545   O  ALA B 576           
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
SHEET    6   Z 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Z 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.05  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.05  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.04  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.05  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.04  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.05  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.05  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.04  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.05  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.05  
CISPEP   1 GLY A  474    PRO A  475          0         4.97                     
CISPEP   2 GLY B  474    PRO B  475          0         2.33                     
SITE     1 AC1 10 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 AC1 10 SER A 630  VAL A 656  TYR A 662  TYR A 666                    
SITE     3 AC1 10 ASN A 710  HIS A 740                                          
SITE     1 AC2  9 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 AC2  9 SER B 630  VAL B 656  TYR B 662  TYR B 666                    
SITE     3 AC2  9 HIS B 740                                                     
CRYST1   79.815   79.815  286.756  90.00  90.00 120.00 P 32          6          
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      0.012529  0.007234  0.000000        0.00000                         
SCALE2      0.000000  0.014467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003487        0.00000                         
TER    5952      PRO A 766                                                      
TER   11904      PRO B 766                                                      
MASTER      713    0    2   40  102    0    6    611948    2   66  116          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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