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LongText Report for: 4JH0-pdb

Name Class
4JH0-pdb
HEADER    HYDROLASE                               04-MAR-13   4JH0              
TITLE     CRYSTAL STRUCTURE OF DIPEPTIDYL-PEPTIDASE 4 (CD26, ADENOSINE DEAMINASE
TITLE    2 COMPLEXING PROTEIN 2) (DPP-IV-WT) COMPLEX WITH BMS-767778 AKA 2-(3-  
TITLE    3 (AMINOMETHYL)-4-(2,4- DICHLOROPHENYL)-2-METHYL-5-OXO-5,7-DIHYDRO-6H- 
TITLE    4 PYRROLO[3,4- B]PYRIDIN-6-YL)-N,N-DIMETHYLACETAMIDE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ADABP, ADENOSINE DEAMINASE COMPLEXING PROTEIN 2, ADCP-2,    
COMPND   5 DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL ACTIVATION ANTIGEN CD26,     
COMPND   6 TP103, DIPEPTIDYL PEPTIDASE 4 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE IV 
COMPND   7 MEMBRANE FORM, DIPEPTIDYL PEPTIDASE 4 SOLUBLE FORM, DIPEPTIDYL       
COMPND   8 PEPTIDASE IV 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, ADCP2, CD26;                                             
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: KM71H;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPICZ-A                                   
KEYWDS    EXOPEPTIDASE, ALPHA/BETA HYDROLASE FOLD, BETA BARREL, BETA PROPELLER, 
KEYWDS   2 DPP-IV, DIMER, HYDROLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.KLEI                                                              
REVDAT   1   04-SEP-13 4JH0    0                                                
JRNL        AUTH   P.DEVASTHALE,Y.WANG,W.WANG,J.M.FEVIG,J.FENG,A.WANG,          
JRNL        AUTH 2 T.HARRITY,D.EGAN,N.MORGAN,M.CAP,A.FURA,H.KLEI,K.KISH,        
JRNL        AUTH 3 C.WEIGELT,L.SUN,P.LEVESQUE,F.MOULIN,Y.X.LI,R.ZAHLER,M.KIRBY, 
JRNL        AUTH 4 L.G.HAMANN                                                   
JRNL        TITL   OPTIMIZATION OF ACTIVITY, SELECTIVITY, AND LIABILITY         
JRNL        TITL 2 PROFILES IN 5-OXOPYRROLOPYRIDINE DPP4 INHIBITORS LEADING TO  
JRNL        TITL 3 CLINICAL CANDIDATE                                           
JRNL        TITL 4 (SA)-2-(3-(AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-2-METHYL-5-   
JRNL        TITL 5 OXO-5H-PYRROLO[3,4-B]PYRIDIN-6(7H)-YL)-N,N-DIMETHYLACETAMIDE 
JRNL        TITL 6 (BMS-767778).                                                
JRNL        REF    J.MED.CHEM.                                2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23964740                                                     
JRNL        DOI    10.1021/JM4008906                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2005                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2900401.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 72725                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1546                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2440               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2430               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.272                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 2.100                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 1546                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : 0.0070               
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 72725                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5749                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3480                       
REMARK   3   BIN FREE R VALUE                    : 0.3990                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 148                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11926                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 74                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.17000                                             
REMARK   3    B22 (A**2) : 15.27000                                             
REMARK   3    B33 (A**2) : -7.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.36                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.940 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 7.150 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 6.350 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.360 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.33                                                 
REMARK   3   BSOL        : 29.21                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : LIGAND.PARAM                                   
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : LIGAND.TOP                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4JH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB078034.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-AUG-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72919                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
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: DIRECT SUBSTITUTION          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS-PROPANE, PH 7.8, 200     
REMARK 280  MM MGCL2, 15.9%(W/V) PEG 3350, 15%(V/V) GLYCEROL, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.65550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      211.88550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.55250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      211.88550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.65550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.55250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 4390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 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    ARG A  40      -51.33     68.58                                   
REMARK 500    ASN A  51       33.83     72.75                                   
REMARK 500    LEU A  57     -166.64   -112.17                                   
REMARK 500    TYR A  58       89.59   -152.51                                   
REMARK 500    SER A  64     -162.53   -177.86                                   
REMARK 500    HIS A  66        1.29   -153.80                                   
REMARK 500    GLU A  73     -107.70     58.56                                   
REMARK 500    GLN A 123      -94.10   -103.37                                   
REMARK 500    TRP A 124     -153.69    -95.19                                   
REMARK 500    TYR A 128      158.36    178.45                                   
REMARK 500    ARG A 140       58.71   -111.16                                   
REMARK 500    ILE A 193      -59.02   -124.81                                   
REMARK 500    ALA A 213       37.54   -145.89                                   
REMARK 500    SER A 242     -158.07     58.36                                   
REMARK 500    SER A 275       49.42    -90.62                                   
REMARK 500    PRO A 290      159.06    -49.99                                   
REMARK 500    GLN A 320       38.32    -89.44                                   
REMARK 500    LEU A 340      121.11    -37.63                                   
REMARK 500    LYS A 373      139.18   -171.05                                   
REMARK 500    ASP A 393     -174.01     61.82                                   
REMARK 500    ASP A 438       84.00   -173.49                                   
REMARK 500    LYS A 441       78.86   -103.00                                   
REMARK 500    GLN A 455       14.64   -144.09                                   
REMARK 500    GLU A 495      114.89   -164.32                                   
REMARK 500    LEU A 519      -78.38   -118.02                                   
REMARK 500    GLU A 521        8.87   -171.09                                   
REMARK 500    TYR A 547      -72.14   -115.76                                   
REMARK 500    ARG A 596        8.77     58.41                                   
REMARK 500    ARG A 597       53.61   -142.59                                   
REMARK 500    THR A 600      -93.02   -121.35                                   
REMARK 500    ARG A 623       73.60   -116.41                                   
REMARK 500    SER A 630     -120.38     59.95                                   
REMARK 500    PRO A 674       24.26    -77.59                                   
REMARK 500    ASP A 678      -77.65   -120.29                                   
REMARK 500    ASN A 679       23.51   -151.54                                   
REMARK 500    ASN A 710      -67.85   -108.47                                   
REMARK 500    ASP A 737       -1.66     82.75                                   
REMARK 500    ASP A 739     -156.90    -93.59                                   
REMARK 500    ILE A 742       56.76     19.39                                   
REMARK 500    THR B  94      152.24    -48.67                                   
REMARK 500    SER B 106      108.40   -164.21                                   
REMARK 500    GLN B 123     -102.01   -109.09                                   
REMARK 500    TRP B 124     -147.22    -89.71                                   
REMARK 500    ASN B 138       17.63    -65.46                                   
REMARK 500    LYS B 139     -121.23   -147.84                                   
REMARK 500    ARG B 140       11.93   -165.16                                   
REMARK 500    HIS B 162       39.99   -166.27                                   
REMARK 500    ASP B 192       -2.03     74.50                                   
REMARK 500    ILE B 193      -56.85   -126.77                                   
REMARK 500    VAL B 207      -69.61   -107.12                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      66 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B  110     GLY B  111                 -140.41                    
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 1MD A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1MD B 801                 
DBREF  4JH0 A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  4JH0 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    1MD  A 801      27                                                       
HET    1MD  B 801      27                                                       
HETNAM     1MD 2-[3-(AMINOMETHYL)-4-(2,4-DICHLOROPHENYL)-2-METHYL-5-            
HETNAM   2 1MD  OXO-5,7-DIHYDRO-6H-PYRROLO[3,4-B]PYRIDIN-6-YL]-N,N-             
HETNAM   3 1MD  DIMETHYLACETAMIDE                                               
FORMUL   3  1MD    2(C19 H20 CL2 N4 O2)                                         
FORMUL   5  HOH   *74(H2 O)                                                     
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
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 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 LEU A  340  GLN A  344  5                                   5    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 LYS A  463  ALA A  465  5                                   3    
HELIX    8   8 ASN A  497  GLN A  505  1                                   9    
HELIX    9   9 ASN A  562  THR A  570  1                                   9    
HELIX   10  10 GLY A  587  HIS A  592  1                                   6    
HELIX   11  11 ALA A  593  ASN A  595  5                                   3    
HELIX   12  12 THR A  600  MET A  616  1                                  17    
HELIX   13  13 SER A  630  GLY A  641  1                                  12    
HELIX   14  14 ARG A  658  TYR A  662  5                                   5    
HELIX   15  15 ASP A  663  GLY A  672  1                                  10    
HELIX   16  16 ASN A  679  SER A  686  1                                   8    
HELIX   17  17 THR A  687  VAL A  698  5                                  12    
HELIX   18  18 PHE A  713  GLY A  727  1                                  15    
HELIX   19  19 SER A  744  SER A  764  1                                  21    
HELIX   20  20 THR B   44  LYS B   50  1                                   7    
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 VAL B  341  GLN B  344  5                                   4    
HELIX   24  24 GLU B  421  MET B  425  5                                   5    
HELIX   25  25 LYS B  463  ALA B  465  5                                   3    
HELIX   26  26 ASN B  497  GLN B  505  1                                   9    
HELIX   27  27 ASN B  562  THR B  570  1                                   9    
HELIX   28  28 GLY B  587  HIS B  592  1                                   6    
HELIX   29  29 ALA B  593  ASN B  595  5                                   3    
HELIX   30  30 THR B  600  MET B  616  1                                  17    
HELIX   31  31 SER B  630  GLY B  641  1                                  12    
HELIX   32  32 ASP B  663  GLY B  672  1                                  10    
HELIX   33  33 ASN B  679  ASN B  685  1                                   7    
HELIX   34  34 SER B  686  THR B  687  5                                   2    
HELIX   35  35 VAL B  688  VAL B  698  5                                  11    
HELIX   36  36 HIS B  712  VAL B  726  1                                  15    
HELIX   37  37 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  LEU A  90   N  ILE A  76           
SHEET    1   C 4 ASP A 104  ILE A 107  0                                        
SHEET    2   C 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  ASP A 133   N  LEU A 116           
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   D 4 TRP A 154  TRP A 157  0                                        
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  TYR A 173   N  TYR A 166           
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  THR A 265   N  ASN A 229           
SHEET    4   F 4 SER A 284  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   G 2 LEU A 235  PHE A 240  0                                        
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   H 4 HIS A 298  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   H 4 TRP A 337  ASN A 338 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  THR A 307  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3   I 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
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  HIS A 383   N  ILE A 375           
SHEET    4   J 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   K 4 VAL A 404  LEU A 410  0                                        
SHEET    2   K 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3   K 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   K 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   L 4 TYR A 457  PHE A 461  0                                        
SHEET    2   L 4 TYR A 467  CYS A 472 -1  O  ARG A 471   N  SER A 458           
SHEET    3   L 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4   L 4 GLY A 490  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1   M 8 SER A 511  ILE A 518  0                                        
SHEET    2   M 8 LYS A 523  LEU A 530 -1  O  PHE A 524   N  ILE A 517           
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  ASP A 545  1  N  ASP A 545   O  ALA A 576           
SHEET    5   M 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 544           
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  TYR A 700           
SHEET    1   N 4 LEU B  60  TRP B  62  0                                        
SHEET    2   N 4 GLU B  67  GLN B  72 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   N 4 ASN B  75  ASN B  80 -1  O  ASN B  75   N  GLN B  72           
SHEET    4   N 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
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  TYR B 173   N  TYR B 166           
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  VAL B 271   N  LEU B 223           
SHEET    4   R 4 ILE B 285  ILE B 287 -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  LYS B 250   N  PHE B 240           
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  ASP B 326   N  LEU B 313           
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  ASP B 326   N  LEU B 313           
SHEET    4   U 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
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  CYS B 385   N  LYS B 373           
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  TYR B 416   N  ALA B 409           
SHEET    3   W 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   W 4 VAL B 442  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 LYS B 489  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  LEU B 530   N  SER B 511           
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  ASP B 545   O  ALA B 576           
SHEET    5   Y 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
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  ILE B 703   N  ALA B 652           
SHEET    8   Y 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  LEU B 702           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.74  
SSBOND   2 CYS A  385    CYS A  394                          1555   1555  2.94  
SSBOND   3 CYS A  444    CYS A  447                          1555   1555  2.74  
SSBOND   4 CYS A  454    CYS A  472                          1555   1555  2.73  
SSBOND   5 CYS A  649    CYS A  762                          1555   1555  2.80  
SSBOND   6 CYS B  328    CYS B  339                          1555   1555  2.79  
SSBOND   7 CYS B  385    CYS B  394                          1555   1555  2.62  
SSBOND   8 CYS B  444    CYS B  447                          1555   1555  2.59  
SSBOND   9 CYS B  454    CYS B  472                          1555   1555  2.79  
SSBOND  10 CYS B  649    CYS B  762                          1555   1555  2.85  
CISPEP   1 GLY A  474    PRO A  475          0         7.93                     
CISPEP   2 GLY B  474    PRO B  475          0         8.44                     
SITE     1 AC1  9 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 AC1  9 SER A 630  VAL A 656  TYR A 662  TYR A 666                    
SITE     3 AC1  9 ASN A 710                                                     
SITE     1 AC2  8 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 AC2  8 SER B 630  VAL B 656  TYR B 662  TYR B 666                    
CRYST1   65.311   67.105  423.771  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015311  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002360        0.00000                         
TER    5964      PRO A 766                                                      
TER   11928      PRO B 766                                                      
MASTER      318    0    2   37  100    0    5    612054    2   74  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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