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LongText Report for: 4J3J-pdb

Name Class
4J3J-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           05-FEB-13   4J3J              
TITLE     CRYSTAL STRUCTURE OF DPP-IV WITH COMPOUND C3                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 39-766;                                       
COMPND   5 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   6 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   7 TP103, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL PEPTIDASE IV  
COMPND   8 SOLUBLE FORM;                                                        
COMPND   9 EC: 3.4.14.5;                                                        
COMPND  10 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: DPP4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: 293F CELL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PTT28                                     
KEYWDS    INHIBITOR COMPLEX, SERINE EXOPEPTIDASE, HYDROLASE-HYDROLASE INHIBITOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.XIONG,L.R.ZHU,D.Q.CHEN,Y.L.ZHAO,F.JIANG,J.K.SHEN                    
REVDAT   1   05-FEB-14 4J3J    0                                                
JRNL        AUTH   L.ZHU,Y.LI,L.QIU,M.SU,X.WANG,C.XIA,Y.QU,J.LI,J.LI,B.XIONG,   
JRNL        AUTH 2 J.SHEN                                                       
JRNL        TITL   DESIGN AND SYNTHESIS OF                                      
JRNL        TITL 2 4-(2,4,5-TRIFLUOROPHENYL)BUTANE-1,3-DIAMINES AS DIPEPTIDYL   
JRNL        TITL 3 PEPTIDASE IV INHIBITORS                                      
JRNL        REF    CHEMMEDCHEM                   V.   8  1104 2013              
JRNL        REFN                   ISSN 1860-7179                               
JRNL        PMID   23671024                                                     
JRNL        DOI    10.1002/CMDC.201300104                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34045                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1695                            
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2324                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 110                          
REMARK   3   BIN FREE R VALUE                    : 0.4390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11899                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
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) : 119.03                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.16000                                              
REMARK   3    B22 (A**2) : 0.16000                                              
REMARK   3    B33 (A**2) : -0.53000                                             
REMARK   3    B12 (A**2) : 0.16000                                              
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): 0.535         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.430         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.563        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12316 ; 0.004 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 16763 ; 0.823 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1450 ; 4.600 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   616 ;32.248 ;23.961       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1990 ;13.301 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    60 ;10.626 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1757 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9536 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  5806 ; 2.201 ;11.829       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7254 ; 3.790 ;17.745       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6510 ; 1.981 ;11.932       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     40       A     764      1                      
REMARK   3           1     B     40       B     764      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    A (A**2):   1148 ; 5.500 ; 0.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 4J3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077550.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35912                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 3HAC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28%(W/V) PEG1500, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
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      194.84467            
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       97.42233            
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: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59090 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     SER A    39                                                      
REMARK 465     LEU A   765                                                      
REMARK 465     PRO A   766                                                      
REMARK 465     SER B    39                                                      
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    GLN A 123      -89.09   -103.62                                   
REMARK 500    TRP A 124     -144.64   -102.95                                   
REMARK 500    LYS A 139     -151.92    -99.11                                   
REMARK 500    ARG A 140       59.14   -140.69                                   
REMARK 500    HIS A 162       37.33   -149.96                                   
REMARK 500    VAL A 207      -70.15   -115.03                                   
REMARK 500    SER A 242     -150.81     51.51                                   
REMARK 500    THR A 307     -157.73   -130.77                                   
REMARK 500    GLN A 320       42.05    -83.04                                   
REMARK 500    THR A 401       49.73    -89.75                                   
REMARK 500    ASN A 420       33.09    -99.80                                   
REMARK 500    TYR A 547      -66.72   -123.27                                   
REMARK 500    ASN A 562     -159.25   -123.55                                   
REMARK 500    ARG A 597       38.20   -146.48                                   
REMARK 500    THR A 600      -90.45   -115.95                                   
REMARK 500    ASN A 621        5.22    -69.12                                   
REMARK 500    SER A 630     -111.54     61.75                                   
REMARK 500    ASP A 678      -85.61   -102.14                                   
REMARK 500    ASN A 679       27.92   -145.89                                   
REMARK 500    ALA A 707       40.02   -107.25                                   
REMARK 500    MET A 733      104.50   -164.80                                   
REMARK 500    SER B  64     -169.78   -125.65                                   
REMARK 500    HIS B  66       10.39   -145.82                                   
REMARK 500    GLN B 123      -89.28   -101.92                                   
REMARK 500    TRP B 124     -145.19   -102.06                                   
REMARK 500    LYS B 139     -152.00   -101.28                                   
REMARK 500    HIS B 162       38.64   -147.74                                   
REMARK 500    SER B 242     -152.65     52.66                                   
REMARK 500    THR B 307     -158.17   -131.91                                   
REMARK 500    GLN B 320       43.51    -84.43                                   
REMARK 500    THR B 401       48.37    -88.05                                   
REMARK 500    ASN B 420       33.97    -99.73                                   
REMARK 500    TYR B 547      -65.08   -127.42                                   
REMARK 500    ASN B 562     -160.67   -122.86                                   
REMARK 500    ARG B 597       38.87   -146.07                                   
REMARK 500    THR B 600      -87.73   -116.31                                   
REMARK 500    ASN B 621        6.87    -68.49                                   
REMARK 500    SER B 630     -110.80     59.01                                   
REMARK 500    ASP B 678      -84.87   -101.82                                   
REMARK 500    ASN B 679       27.69   -146.67                                   
REMARK 500    MET B 733      106.39   -160.77                                   
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 D3C A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D3C B 801                 
DBREF  4J3J A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  4J3J B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQRES   1 A  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 B  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
HET    D3C  A 801      30                                                       
HET    D3C  B 801      30                                                       
HETNAM     D3C N-[(3R)-3-AMINO-4-(2,4,5-TRIFLUOROPHENYL)BUTYL]-6-               
HETNAM   2 D3C  (TRIFLUOROMETHYL)-3,4-DIHYDROPYRROLO[1,2-A]PYRAZINE-            
HETNAM   3 D3C  2(1H)-CARBOXAMIDE                                               
FORMUL   3  D3C    2(C19 H20 F6 N4 O)                                           
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 VAL A  341  GLN A  344  5                                   4    
HELIX    5   5 GLU A  421  MET A  425  5                                   5    
HELIX    6   6 LYS A  463  ALA A  465  5                                   3    
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  LYS A  615  1                                  16    
HELIX   12  12 SER A  630  GLY A  641  1                                  12    
HELIX   13  13 ASP A  663  GLY A  672  1                                  10    
HELIX   14  14 ASN A  679  SER A  686  1                                   8    
HELIX   15  15 VAL A  688  VAL A  698  5                                  11    
HELIX   16  16 HIS A  712  VAL A  726  1                                  15    
HELIX   17  17 SER A  744  PHE A  763  1                                  20    
HELIX   18  18 THR B   44  LYS B   50  1                                   7    
HELIX   19  19 GLU B   91  ASP B   96  5                                   6    
HELIX   20  20 ASP B  200  VAL B  207  1                                   8    
HELIX   21  21 VAL B  341  GLN B  344  5                                   4    
HELIX   22  22 GLU B  421  MET B  425  5                                   5    
HELIX   23  23 LYS B  463  ALA B  465  5                                   3    
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 ASP B  663  GLY B  672  1                                  10    
HELIX   31  31 ASN B  679  SER B  686  1                                   8    
HELIX   32  32 VAL B  688  VAL B  698  5                                  11    
HELIX   33  33 HIS B  712  VAL B  726  1                                  15    
HELIX   34  34 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 ARG A  61  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  LEU A  77   N  TYR A  70           
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  SER A  87   N  VAL A  78           
SHEET    1   C 3 ASP A 104  ILE A 107  0                                        
SHEET    2   C 3 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   C 3 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
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  LYS A 267   N  GLN A 227           
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  TRP A 305  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  TRP A 305  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   I 4 TYR A 322  TYR A 330 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
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  ILE A 418   N  ILE A 405           
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  HIS A 483   N  TYR A 468           
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  SER A 577   N  GLN A 527           
SHEET    4   M 8 TYR A 540  VAL A 546  1  N  LEU A 543   O  ILE A 574           
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  LEU A 701   N  ALA A 652           
SHEET    8   M 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  LEU A 702           
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 ARG B  61  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  LEU B  77   N  TYR B  70           
SHEET    4   O 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1   P 3 ASP B 104  ILE B 107  0                                        
SHEET    2   P 3 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3   P 3 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
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  LYS B 267   N  GLN B 227           
SHEET    4   S 4 SER B 284  ILE B 287 -1  O  ILE B 287   N  PHE B 268           
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  TRP B 305  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  ASP B 326   N  LEU B 313           
SHEET    4   U 4 TRP B 337  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   V 4 HIS B 298  TRP B 305  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  ASP B 326   N  LEU B 313           
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  GLU B 347   N  SER B 323           
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  ILE B 418   N  ILE B 405           
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   X 4 VAL B 442  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  ARG B 471   N  SER B 458           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  HIS B 483   N  TYR B 468           
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  SER B 577   N  GLN B 527           
SHEET    4   Z 8 TYR B 540  VAL B 546  1  N  LEU B 543   O  ILE B 574           
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  ASP B 620   N  TYR B 540           
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  LEU B 701   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.03  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.04  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.03  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.03  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.03  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.03  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.03  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.03  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.03  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.03  
CISPEP   1 GLY A  474    PRO A  475          0        -0.18                     
CISPEP   2 GLY B  474    PRO B  475          0        -0.12                     
SITE     1 AC1 12 ARG A 125  GLU A 205  GLU A 206  PHE A 357                    
SITE     2 AC1 12 TYR A 585  SER A 630  TYR A 631  VAL A 656                    
SITE     3 AC1 12 TYR A 662  TYR A 666  ASN A 710  VAL A 711                    
SITE     1 AC2 12 ARG B 125  GLU B 205  GLU B 206  PHE B 357                    
SITE     2 AC2 12 TYR B 585  SER B 630  TYR B 631  VAL B 656                    
SITE     3 AC2 12 TYR B 662  TYR B 666  ASN B 710  VAL B 711                    
CRYST1   79.648   79.648  292.267  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      0.012555  0.007249  0.000000        0.00000                         
SCALE2      0.000000  0.014498  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003422        0.00000                         
TER    5943      SER A 764                                                      
TER   11901      PRO B 766                                                      
MASTER      321    0    2   34  100    0    6    611959    2   80  112          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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