Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 2G5T-pdb

Name Class
2G5T-pdb
HEADER    HYDROLASE                               23-FEB-06   2G5T              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPPIV)            
TITLE    2 COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 21AG          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM;                       
COMPND   5 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL                     
COMPND   6 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE                  
COMPND   7 COMPLEXING PROTEIN 2, ADABP, CONTAINS: DIPEPTIDYL                    
COMPND   8 PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV                   
COMPND   9 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM,                  
COMPND  10 DIPEPTIDYL PEPTIDASE IV SOLUBLE FORM;                                
COMPND  11 EC: 3.4.14.5;                                                        
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM                              
KEYWDS    SERINE PEPTIDASE, BETA-PROPELLER                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.LONGENECKER,E.H.FRY,M.R.LAKE,L.R.SOLOMON,Z.PEI,X.LI               
REVDAT   1   04-JUL-06 2G5T    0                                                
JRNL        AUTH   Z.PEI,X.LI,K.LONGENECKER,T.W.VON GELDERN,                    
JRNL        AUTH 2 P.E.WIEDEMAN,T.H.LUBBEN,B.A.ZINKER,K.STEWART,                
JRNL        AUTH 3 S.J.BALLARON,M.A.STASHKO,A.K.MIKA,D.W.BENO,M.LONG,           
JRNL        AUTH 4 H.WELLS,A.J.KEMPF-GROTE,D.J.MADAR,T.S.MCDERMOTT,             
JRNL        AUTH 5 L.BHAGAVATULA,M.G.FICKES,D.PIREH,L.R.SOLOMON,                
JRNL        AUTH 6 M.R.LAKE,R.EDALJI,E.H.FRY,H.L.SHAM,J.M.TREVILLYAN            
JRNL        TITL   DISCOVERY, STRUCTURE-ACTIVITY RELATIONSHIP, AND              
JRNL        TITL 2 PHARMACOLOGICAL EVALUATION OF                                
JRNL        TITL 3 (5-SUBSTITUTED-PYRROLIDINYL-2-CARBONYL)-2-                   
JRNL        TITL 4 CYANOPYRROLIDINES AS POTENT DIPEPTIDYL PEPTIDASE             
JRNL        TITL 5 IV INHIBITORS.                                               
JRNL        REF    J.MED.CHEM.                   V.  49  3520 2006              
JRNL        REFN   ASTM JMCMAR  US ISSN 0022-2623                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.30 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 75599                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3734                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11898                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 1421                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.68800                                             
REMARK   3    B22 (A**2) : -0.38300                                             
REMARK   3    B33 (A**2) : 2.07200                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.00400                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : 1.35                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REPADD.PARAM                           
REMARK   3  PARAMETER FILE  2  : MSI_CNX_TOPPAR:WATER_REP.PARAM                 
REMARK   3  PARAMETER FILE  3  : ADD.PAR                                        
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2G5T COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-2006.                
REMARK 100 THE RCSB ID CODE IS RCSB036724.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75716                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+Y,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.39400            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 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, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   OG   SER B   630     O    HOH    1140              2.19            
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    VAL A 207   CA    VAL A 207   CB     0.041                        
REMARK 500    MET A 325   SD    MET A 325   CE    -0.058                        
REMARK 500    MET A 528   SD    MET A 528   CE    -0.056                        
REMARK 500    SER A 630   C     SER A 630   O      0.179                        
REMARK 500    MET A 755   SD    MET A 755   CE    -0.073                        
REMARK 500    PRO B 255   CB    PRO B 255   CG     0.047                        
REMARK 500    MET B 325   SD    MET B 325   CE    -0.038                        
REMARK 500    MET B 591   SD    MET B 591   CE    -0.041                        
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    GLN A  72   N   -  CA  -  C   ANGL. DEV. =-10.7 DEGREES           
REMARK 500    ASN A  80   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    LEU A  90   CA  -  CB  -  CG  ANGL. DEV. =  8.2 DEGREES           
REMARK 500    VAL A 160   N   -  CA  -  C   ANGL. DEV. = 11.4 DEGREES           
REMARK 500    GLU A 206   N   -  CA  -  C   ANGL. DEV. =  9.7 DEGREES           
REMARK 500    ILE A 236   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    PHE A 240   N   -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 500    PRO A 290   C   -  N   -  CA  ANGL. DEV. = 10.8 DEGREES           
REMARK 500    LEU A 300   N   -  CA  -  C   ANGL. DEV. =-13.7 DEGREES           
REMARK 500    ILE A 319   N   -  CA  -  C   ANGL. DEV. =-12.1 DEGREES           
REMARK 500    ALA A 342   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    GLN A 388   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    VAL A 404   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    LEU A 415   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES           
REMARK 500    GLU A 448   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES           
REMARK 500    SER A 458   N   -  CA  -  C   ANGL. DEV. =-12.8 DEGREES           
REMARK 500    ILE A 529   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    TYR A 547   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    LEU A 561   N   -  CA  -  C   ANGL. DEV. = -8.1 DEGREES           
REMARK 500    SER A 630   CA  -  C   -  O   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    VAL A 656   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    TRP A 659   N   -  CA  -  C   ANGL. DEV. =  8.7 DEGREES           
REMARK 500    VAL A 711   N   -  CA  -  C   ANGL. DEV. =-10.7 DEGREES           
REMARK 500    ALA A 743   N   -  CA  -  C   ANGL. DEV. =  9.2 DEGREES           
REMARK 500    GLN B  72   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES           
REMARK 500    ASN B  80   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    LEU B  90   CA  -  CB  -  CG  ANGL. DEV. = 11.0 DEGREES           
REMARK 500    SER B 158   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    VAL B 160   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES           
REMARK 500    ASP B 200   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES           
REMARK 500    GLU B 206   N   -  CA  -  C   ANGL. DEV. = 10.0 DEGREES           
REMARK 500    ILE B 236   N   -  CA  -  C   ANGL. DEV. = -9.5 DEGREES           
REMARK 500    PHE B 240   N   -  CA  -  C   ANGL. DEV. =-11.2 DEGREES           
REMARK 500    PRO B 290   C   -  N   -  CA  ANGL. DEV. =  9.1 DEGREES           
REMARK 500    LEU B 300   N   -  CA  -  C   ANGL. DEV. =-13.0 DEGREES           
REMARK 500    ILE B 319   N   -  CA  -  C   ANGL. DEV. =-12.3 DEGREES           
REMARK 500    ILE B 327   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    VAL B 341   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    ALA B 342   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    THR B 365   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES           
REMARK 500    GLU B 378   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES           
REMARK 500    GLN B 388   N   -  CA  -  C   ANGL. DEV. =-16.0 DEGREES           
REMARK 500    TRP B 402   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    LEU B 415   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    GLU B 448   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES           
REMARK 500    SER B 458   N   -  CA  -  C   ANGL. DEV. =-10.1 DEGREES           
REMARK 500    ILE B 529   N   -  CA  -  C   ANGL. DEV. =-10.1 DEGREES           
REMARK 500    TYR B 547   N   -  CA  -  C   ANGL. DEV. = -8.4 DEGREES           
REMARK 500    ALA B 548   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES           
REMARK 500    LEU B 561   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES           
REMARK 500    VAL B 656   N   -  CA  -  C   ANGL. DEV. =-12.5 DEGREES           
REMARK 500    TRP B 659   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES           
REMARK 500    VAL B 711   N   -  CA  -  C   ANGL. DEV. = -9.2 DEGREES           
REMARK 500    ALA B 743   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  40      159.58     54.50                                   
REMARK 500    SER A 630     -115.44     55.40                                   
REMARK 500    ARG B  40      142.58     75.83                                   
REMARK 500    GLU B 521      -41.74     76.10                                   
REMARK 500    SER B 630     -109.71     53.18                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH   526        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH   618        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH   885        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH   906        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH  1075        DISTANCE =  6.38 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G5P   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPPIV)           
REMARK 900 COMPLEXED WITH CYANOPYRROLIDINE (C5-PRO-PRO) INHIBITOR 16AC          
DBREF  2G5T A   39   764  UNP    P27487   DPP4_HUMAN      39    764             
DBREF  2G5T B   39   764  UNP    P27487   DPP4_HUMAN      39    764             
SEQRES   1 A  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
SEQRES   1 B  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
HET    ACF  A 800      26                                                       
HETNAM     ACF 3-{[(2R,5S)-5-{[(2S)-2-(AMINOMETHYL)PYRROLIDIN-1-                
HETNAM   2 ACF  YL]CARBONYL}PYRROLIDIN-2-YL]METHOXY}-4-CHLOROBENZOIC            
HETNAM   3 ACF  ACID                                                            
FORMUL   3  ACF    C18 H24 N3 O4 CL1                                            
FORMUL   4  HOH   *1421(H2 O1)                                                  
HELIX    1   1 THR A   44  LYS A   50  1                                   7    
HELIX    2   2 PHE A   95  GLY A   99  5                                   5    
HELIX    3   3 ASP A  200  VAL A  207  1                                   8    
HELIX    4   4 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 GLU A  332  GLY A  335  5                                   4    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 ASN A  497  GLN A  505  1                                   9    
HELIX    8   8 ASN A  562  THR A  570  1                                   9    
HELIX    9   9 GLY A  587  HIS A  592  1                                   6    
HELIX   10  10 ALA A  593  ASN A  595  5                                   3    
HELIX   11  11 THR A  600  SER A  614  1                                  15    
HELIX   12  12 SER A  630  GLY A  641  1                                  12    
HELIX   13  13 ARG A  658  TYR A  662  5                                   5    
HELIX   14  14 ASP A  663  GLY A  672  1                                  10    
HELIX   15  15 ASN A  679  SER A  686  1                                   8    
HELIX   16  16 VAL A  688  VAL A  698  5                                  11    
HELIX   17  17 HIS A  712  GLY A  727  1                                  16    
HELIX   18  18 SER A  744  SER A  764  1                                  21    
HELIX   19  19 THR B   44  LYS B   50  1                                   7    
HELIX   20  20 GLU B   91  ASP B   96  5                                   6    
HELIX   21  21 ASP B  200  VAL B  207  1                                   8    
HELIX   22  22 PRO B  290  ILE B  295  1                                   6    
HELIX   23  23 GLU B  421  MET B  425  5                                   5    
HELIX   24  24 ASN B  497  GLN B  505  1                                   9    
HELIX   25  25 ASN B  562  THR B  570  1                                   9    
HELIX   26  26 GLY B  587  HIS B  592  1                                   6    
HELIX   27  27 ALA B  593  ASN B  595  5                                   3    
HELIX   28  28 THR B  600  LYS B  615  1                                  16    
HELIX   29  29 SER B  630  GLY B  641  1                                  12    
HELIX   30  30 ARG B  658  TYR B  662  5                                   5    
HELIX   31  31 ASP B  663  GLY B  672  1                                  10    
HELIX   32  32 ASN B  679  SER B  686  1                                   8    
HELIX   33  33 VAL B  688  VAL B  698  5                                  11    
HELIX   34  34 HIS B  712  GLY B  727  1                                  16    
HELIX   35  35 SER B  744  SER B  764  1                                  21    
SHEET    1   A 4 LEU A  60  TRP A  62  0                                        
SHEET    2   A 4 GLU A  67  LYS A  71 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   A 4 ILE A  76  ASN A  80 -1  O  PHE A  79   N  TYR A  68           
SHEET    4   A 4 SER A  86  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1   B 4 ILE A 102  ASP A 104  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASP A 104           
SHEET    3   B 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   B 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   C 4 TRP A 154  TRP A 157  0                                        
SHEET    2   C 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   C 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   C 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   D 3 ILE A 194  ASN A 196  0                                        
SHEET    2   D 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   D 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   E 4 ILE A 194  ASN A 196  0                                        
SHEET    2   E 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 4 THR A 265  ASN A 272 -1  O  PHE A 269   N  TYR A 225           
SHEET    4   E 4 ILE A 285  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   F 2 LEU A 235  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   G 4 HIS A 298  TRP A 305  0                                        
SHEET    2   G 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   G 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   G 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 HIS A 298  TRP A 305  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  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1   I 4 HIS A 363  PHE A 364  0                                        
SHEET    2   I 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   I 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4   I 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   J 4 VAL A 404  LEU A 410  0                                        
SHEET    2   J 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   K 4 TYR A 457  PHE A 461  0                                        
SHEET    2   K 4 TYR A 467  CYS A 472 -1  O  GLN A 469   N  SER A 460           
SHEET    3   K 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   K 4 LYS A 489  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1   L 8 SER A 511  LEU A 519  0                                        
SHEET    2   L 8 THR A 522  LEU A 530 -1  O  LEU A 530   N  SER A 511           
SHEET    3   L 8 ILE A 574  PHE A 578 -1  O  SER A 577   N  GLN A 527           
SHEET    4   L 8 TYR A 540  VAL A 546  1  N  ASP A 545   O  ALA A 576           
SHEET    5   L 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 542           
SHEET    6   L 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   L 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652           
SHEET    8   L 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1   M 2 LYS B  41  THR B  42  0                                        
SHEET    2   M 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   N 4 LEU B  60  TRP B  62  0                                        
SHEET    2   N 4 GLU B  67  LYS B  71 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   N 4 ILE B  76  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4   N 4 SER B  86  LEU B  90 -1  O  PHE B  89   N  ILE B  76           
SHEET    1   O 4 ILE B 102  ILE B 107  0                                        
SHEET    2   O 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   O 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4   O 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   P 4 TRP B 154  TRP B 157  0                                        
SHEET    2   P 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  TRP B 154           
SHEET    3   P 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   P 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   Q 3 ILE B 194  ASN B 196  0                                        
SHEET    2   Q 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   Q 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   R 4 ILE B 194  ASN B 196  0                                        
SHEET    2   R 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4   R 4 SER B 284  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   S 2 LEU B 235  PHE B 240  0                                        
SHEET    2   S 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   T 4 HIS B 298  THR B 307  0                                        
SHEET    2   T 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   T 4 TYR B 322  TYR B 330 -1  O  VAL B 324   N  TRP B 315           
SHEET    4   T 4 TRP B 337  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   U 4 HIS B 298  THR B 307  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  VAL B 324   N  TRP B 315           
SHEET    4   U 4 HIS B 345  MET B 348 -1  O  GLU B 347   N  SER B 323           
SHEET    1   V 4 HIS B 363  PHE B 364  0                                        
SHEET    2   V 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   V 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4   V 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   W 4 VAL B 404  LEU B 410  0                                        
SHEET    2   W 4 TYR B 414  SER B 419 -1  O  ILE B 418   N  ILE B 405           
SHEET    3   W 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   W 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   X 4 TYR B 457  PHE B 461  0                                        
SHEET    2   X 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458           
SHEET    3   X 4 LEU B 479  SER B 484 -1  O  THR B 481   N  LEU B 470           
SHEET    4   X 4 GLY B 490  GLU B 495 -1  O  LEU B 494   N  TYR B 480           
SHEET    1   Y 8 SER B 511  LEU B 519  0                                        
SHEET    2   Y 8 THR B 522  LEU B 530 -1  O  THR B 522   N  LEU B 519           
SHEET    3   Y 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   Y 8 TYR B 540  ASP B 545  1  N  LEU B 543   O  ILE B 574           
SHEET    5   Y 8 VAL B 619  TRP B 629  1  O  ASP B 620   N  TYR B 540           
SHEET    6   Y 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Y 8 GLU B 699  GLY B 705  1  O  LEU B 701   N  ALA B 652           
SHEET    8   Y 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SSBOND   1 CYS A  328    CYS A  339                                             
SSBOND   2 CYS A  385    CYS A  394                                             
SSBOND   3 CYS A  444    CYS A  447                                             
SSBOND   4 CYS A  454    CYS A  472                                             
SSBOND   5 CYS A  649    CYS A  762                                             
SSBOND   6 CYS B  328    CYS B  339                                             
SSBOND   7 CYS B  385    CYS B  394                                             
SSBOND   8 CYS B  444    CYS B  447                                             
SSBOND   9 CYS B  454    CYS B  472                                             
SSBOND  10 CYS B  649    CYS B  762                                             
LINK         OG  SER A 630                 C21 ACF A 800                        
CISPEP   1 ALA A  289    PRO A  290          0         0.59                     
CISPEP   2 GLY A  474    PRO A  475          0         0.16                     
CISPEP   3 ALA B  289    PRO B  290          0        -0.50                     
CISPEP   4 GLY B  474    PRO B  475          0         0.30                     
CRYST1   65.733  126.788  112.292  90.00  99.49  90.00 P 1 21 1      4          
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      0.015213  0.000000  0.002543        0.00000                         
SCALE2      0.000000  0.007887  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009029        0.00000                         
TER    5950      SER A 764                                                      
TER   11900      SER B 764                                                      
MASTER      340    0    1   35  100    0    0    613345    2   47  112          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer