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LongText Report for: 5y7k-pdb

Name Class
5y7k-pdb
HEADER    HYDROLASE                               17-AUG-17   5Y7K              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH INHIBITOR1            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: ADABP,ADENOSINE DEAMINASE COMPLEXING PROTEIN 2,ADCP-2,      
COMPND   5 DIPEPTIDYL PEPTIDASE IV,DPP IV,T-CELL ACTIVATION ANTIGEN CD26,TP103; 
COMPND   6 EC: 3.4.14.5;                                                        
COMPND   7 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: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    DPP4, INHIBITOR, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.K.LEE,E.E.KIM                                                       
REVDAT   1   20-MAR-19 5Y7K    0                                                
JRNL        AUTH   H.K.LEE,E.E.KIM                                              
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH INHIBITOR    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.440                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 126777                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6379                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.1418 -  7.7881    0.98     4147   226  0.2174 0.2478        
REMARK   3     2  7.7881 -  6.1884    1.00     4166   225  0.1918 0.2153        
REMARK   3     3  6.1884 -  5.4081    1.00     4122   221  0.1680 0.2109        
REMARK   3     4  5.4081 -  4.9145    1.00     4103   255  0.1470 0.1680        
REMARK   3     5  4.9145 -  4.5627    1.00     4170   201  0.1400 0.1720        
REMARK   3     6  4.5627 -  4.2940    1.00     4145   203  0.1494 0.1841        
REMARK   3     7  4.2940 -  4.0792    1.00     4124   209  0.1612 0.1662        
REMARK   3     8  4.0792 -  3.9018    1.00     4116   209  0.1735 0.2047        
REMARK   3     9  3.9018 -  3.7517    1.00     4096   205  0.1905 0.2303        
REMARK   3    10  3.7517 -  3.6223    0.99     4107   201  0.1945 0.2433        
REMARK   3    11  3.6223 -  3.5091    0.99     4126   203  0.2113 0.2612        
REMARK   3    12  3.5091 -  3.4088    0.99     4087   216  0.2217 0.2583        
REMARK   3    13  3.4088 -  3.3191    0.99     4044   236  0.2334 0.2704        
REMARK   3    14  3.3191 -  3.2382    0.99     4081   198  0.2313 0.2768        
REMARK   3    15  3.2382 -  3.1646    0.99     4109   199  0.2345 0.2930        
REMARK   3    16  3.1646 -  3.0973    0.99     4074   238  0.2359 0.2570        
REMARK   3    17  3.0973 -  3.0353    0.98     4042   212  0.2269 0.2801        
REMARK   3    18  3.0353 -  2.9781    0.98     4019   220  0.2423 0.2836        
REMARK   3    19  2.9781 -  2.9249    0.98     4020   201  0.2465 0.2908        
REMARK   3    20  2.9249 -  2.8753    0.98     3999   231  0.2468 0.2878        
REMARK   3    21  2.8753 -  2.8290    0.97     3999   217  0.2469 0.2965        
REMARK   3    22  2.8290 -  2.7854    0.96     3974   181  0.2467 0.2797        
REMARK   3    23  2.7854 -  2.7445    0.96     3912   223  0.2453 0.2838        
REMARK   3    24  2.7445 -  2.7058    0.96     3947   206  0.2503 0.3211        
REMARK   3    25  2.7058 -  2.6693    0.96     3946   219  0.2566 0.2914        
REMARK   3    26  2.6693 -  2.6346    0.95     3895   203  0.2589 0.2774        
REMARK   3    27  2.6346 -  2.6017    0.95     3876   212  0.2845 0.3538        
REMARK   3    28  2.6017 -  2.5704    0.94     3879   207  0.2982 0.3330        
REMARK   3    29  2.5704 -  2.5405    0.94     3802   218  0.2851 0.3248        
REMARK   3    30  2.5405 -  2.5119    0.79     3271   184  0.2901 0.3123        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          24642                                  
REMARK   3   ANGLE     :  0.463          33538                                  
REMARK   3   CHIRALITY :  0.041           3517                                  
REMARK   3   PLANARITY :  0.002           4257                                  
REMARK   3   DIHEDRAL  : 18.572          14342                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5Y7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004763.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5~8.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 129816                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.512                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.136                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.070                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1X70                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20~28% (W/V) POLYETHYLENE GLYCOL 4000,   
REMARK 280  0.1M HEPES OR TRIS PH 7.5~8.5, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.96000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 57370 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 4330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 57120 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     LEU C   765                                                      
REMARK 465     PRO C   766                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   133     NH1  ARG B   147              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C   970     O    HOH D   966     2747     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    HIS A  66       22.41   -154.80                                   
REMARK 500    GLU A  73      -18.19     75.67                                   
REMARK 500    GLN A 123      -91.86   -118.64                                   
REMARK 500    TRP A 124     -156.61    -99.02                                   
REMARK 500    HIS A 162       32.68   -145.34                                   
REMARK 500    ILE A 193      -64.15   -129.34                                   
REMARK 500    ASP A 200     -165.02    -77.53                                   
REMARK 500    VAL A 207      -68.53   -101.34                                   
REMARK 500    SER A 242     -161.33     59.52                                   
REMARK 500    THR A 307     -163.46   -121.26                                   
REMARK 500    GLN A 320       47.11    -81.83                                   
REMARK 500    THR A 411     -164.42   -126.13                                   
REMARK 500    LYS A 423       18.34     57.89                                   
REMARK 500    ASN A 450       76.95   -150.86                                   
REMARK 500    GLN A 508       90.09    -68.27                                   
REMARK 500    TYR A 547      -66.06   -128.94                                   
REMARK 500    ARG A 597       53.15   -146.26                                   
REMARK 500    THR A 600      -84.59   -127.09                                   
REMARK 500    SER A 630     -119.81     63.04                                   
REMARK 500    ASP A 678      -88.10   -126.49                                   
REMARK 500    ASN A 679       32.08   -143.29                                   
REMARK 500    ASN A 710      -73.60    -92.30                                   
REMARK 500    MET A 733      116.41   -169.21                                   
REMARK 500    SER B  64     -155.52   -146.19                                   
REMARK 500    GLN B  72      -71.82    -80.47                                   
REMARK 500    SER B  86     -168.40   -120.75                                   
REMARK 500    GLN B 123      -86.91    -93.97                                   
REMARK 500    TRP B 124     -152.83   -103.32                                   
REMARK 500    HIS B 162       31.95   -142.56                                   
REMARK 500    ILE B 193      -53.47   -130.02                                   
REMARK 500    ASP B 230       41.73   -107.61                                   
REMARK 500    SER B 242     -159.43     63.22                                   
REMARK 500    ARG B 356      -73.48    -76.11                                   
REMARK 500    ASP B 438      102.35   -162.10                                   
REMARK 500    SER B 462     -168.41    -75.16                                   
REMARK 500    GLU B 464       31.01    -97.67                                   
REMARK 500    ASN B 506       37.04    -92.25                                   
REMARK 500    TYR B 547      -65.90   -137.08                                   
REMARK 500    ARG B 597       48.60   -140.80                                   
REMARK 500    THR B 600      -82.40   -119.26                                   
REMARK 500    SER B 630     -115.74     59.95                                   
REMARK 500    ASP B 678      -77.90   -120.02                                   
REMARK 500    ASN B 679       27.13   -143.92                                   
REMARK 500    MET B 733      118.42   -162.73                                   
REMARK 500    ARG C  40       79.34     57.83                                   
REMARK 500    TYR C  58       71.84   -151.80                                   
REMARK 500    HIS C  66       21.60   -144.73                                   
REMARK 500    GLN C  72       77.64   -116.47                                   
REMARK 500    GLU C  73      -65.61     67.72                                   
REMARK 500    LEU C  90      139.48   -171.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 963        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A 964        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH A 965        DISTANCE =  7.90 ANGSTROMS                       
REMARK 525    HOH C 972        DISTANCE =  6.36 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VU A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VU B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VU C 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VU D 801                 
DBREF  5Y7K A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  5Y7K B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  5Y7K C   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  5Y7K D   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          
SEQRES   1 C  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 C  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 C  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 C  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 C  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 C  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 C  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 C  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 C  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 C  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 C  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 C  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 C  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 C  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 C  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 C  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 C  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 C  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 C  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 C  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 C  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 C  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 C  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 C  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 C  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 C  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 C  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 C  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 C  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 C  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 C  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 C  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 C  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 C  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 C  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 C  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 C  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 C  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 C  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 C  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 C  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 C  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 C  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 C  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 C  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 C  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 C  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 C  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 C  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 C  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 C  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 C  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 C  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 C  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 C  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 C  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
SEQRES   1 D  728  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 D  728  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 D  728  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 D  728  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 D  728  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 D  728  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 D  728  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 D  728  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 D  728  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 D  728  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 D  728  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 D  728  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 D  728  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 D  728  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 D  728  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 D  728  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 D  728  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 D  728  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 D  728  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 D  728  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 D  728  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 D  728  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 D  728  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 D  728  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 D  728  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 D  728  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 D  728  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 D  728  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 D  728  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 D  728  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 D  728  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 D  728  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 D  728  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 D  728  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 D  728  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 D  728  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 D  728  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 D  728  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 D  728  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 D  728  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 D  728  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 D  728  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 D  728  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 D  728  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 D  728  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 D  728  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 D  728  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 D  728  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 D  728  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 D  728  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 D  728  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 D  728  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 D  728  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 D  728  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 D  728  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 D  728  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO          
HET    8VU  A 801      54                                                       
HET    8VU  B 801      54                                                       
HET    8VU  C 801      54                                                       
HET    8VU  D 801      54                                                       
HETNAM     8VU (R)-4-((R)-3-AMINO-4-(2,4,5-TRIFLUOROPHENYL)BUTANOYL)-           
HETNAM   2 8VU  3-(TERT-BUTOXYMETHYL)PIPERAZINE-2-ONE                           
FORMUL   5  8VU    4(C19 H26 F3 N3 O3)                                          
FORMUL   9  HOH   *272(H2 O)                                                    
HELIX    1 AA1 THR A   44  ASN A   51  1                                   8    
HELIX    2 AA2 SER A   93  PHE A   95  5                                   3    
HELIX    3 AA3 ASP A  200  VAL A  207  1                                   8    
HELIX    4 AA4 ASP A  274  LEU A  276  5                                   3    
HELIX    5 AA5 PRO A  290  ILE A  295  1                                   6    
HELIX    6 AA6 VAL A  341  GLN A  344  5                                   4    
HELIX    7 AA7 GLU A  421  MET A  425  5                                   5    
HELIX    8 AA8 ASN A  497  GLN A  505  1                                   9    
HELIX    9 AA9 ASN A  562  THR A  570  1                                   9    
HELIX   10 AB1 GLY A  587  HIS A  592  1                                   6    
HELIX   11 AB2 ALA A  593  ASN A  595  5                                   3    
HELIX   12 AB3 THR A  600  LYS A  615  1                                  16    
HELIX   13 AB4 SER A  630  GLY A  641  1                                  12    
HELIX   14 AB5 ARG A  658  TYR A  662  5                                   5    
HELIX   15 AB6 ASP A  663  GLY A  672  1                                  10    
HELIX   16 AB7 ASN A  679  SER A  686  1                                   8    
HELIX   17 AB8 VAL A  688  VAL A  698  5                                  11    
HELIX   18 AB9 HIS A  712  VAL A  726  1                                  15    
HELIX   19 AC1 SER A  744  PHE A  763  1                                  20    
HELIX   20 AC2 THR B   44  LYS B   50  1                                   7    
HELIX   21 AC3 ASP B  200  VAL B  207  1                                   8    
HELIX   22 AC4 ASP B  274  LEU B  276  5                                   3    
HELIX   23 AC5 PRO B  290  ILE B  295  1                                   6    
HELIX   24 AC6 LEU B  340  ALA B  342  5                                   3    
HELIX   25 AC7 GLU B  421  MET B  425  5                                   5    
HELIX   26 AC8 ASN B  497  LEU B  504  1                                   8    
HELIX   27 AC9 ASN B  562  THR B  570  1                                   9    
HELIX   28 AD1 GLY B  587  HIS B  592  1                                   6    
HELIX   29 AD2 ALA B  593  ASN B  595  5                                   3    
HELIX   30 AD3 THR B  600  LYS B  615  1                                  16    
HELIX   31 AD4 SER B  630  GLY B  641  1                                  12    
HELIX   32 AD5 ASP B  663  GLY B  672  1                                  10    
HELIX   33 AD6 ASN B  679  SER B  686  1                                   8    
HELIX   34 AD7 THR B  687  VAL B  698  5                                  12    
HELIX   35 AD8 HIS B  712  VAL B  726  1                                  15    
HELIX   36 AD9 SER B  744  PHE B  763  1                                  20    
HELIX   37 AE1 THR C   44  ASN C   51  1                                   8    
HELIX   38 AE2 GLU C   91  ASP C   96  5                                   6    
HELIX   39 AE3 ASP C  200  VAL C  207  1                                   8    
HELIX   40 AE4 PRO C  290  ILE C  295  1                                   6    
HELIX   41 AE5 VAL C  341  GLN C  344  5                                   4    
HELIX   42 AE6 GLU C  421  MET C  425  5                                   5    
HELIX   43 AE7 ASN C  497  GLN C  505  1                                   9    
HELIX   44 AE8 ASN C  562  THR C  570  1                                   9    
HELIX   45 AE9 GLY C  587  HIS C  592  1                                   6    
HELIX   46 AF1 ALA C  593  ASN C  595  5                                   3    
HELIX   47 AF2 THR C  600  LYS C  615  1                                  16    
HELIX   48 AF3 SER C  630  GLY C  641  1                                  12    
HELIX   49 AF4 ARG C  658  TYR C  662  5                                   5    
HELIX   50 AF5 ASP C  663  GLY C  672  1                                  10    
HELIX   51 AF6 ASN C  679  SER C  686  1                                   8    
HELIX   52 AF7 VAL C  688  VAL C  698  5                                  11    
HELIX   53 AF8 PHE C  713  VAL C  726  1                                  14    
HELIX   54 AF9 SER C  744  SER C  764  1                                  21    
HELIX   55 AG1 THR D   44  ASN D   51  1                                   8    
HELIX   56 AG2 PHE D   95  GLY D   99  5                                   5    
HELIX   57 AG3 ASP D  200  VAL D  207  1                                   8    
HELIX   58 AG4 ASP D  274  LEU D  276  5                                   3    
HELIX   59 AG5 PRO D  290  ILE D  295  1                                   6    
HELIX   60 AG6 VAL D  341  GLN D  344  5                                   4    
HELIX   61 AG7 GLU D  421  MET D  425  5                                   5    
HELIX   62 AG8 ASN D  497  LEU D  504  1                                   8    
HELIX   63 AG9 ASN D  562  THR D  570  1                                   9    
HELIX   64 AH1 GLY D  587  HIS D  592  1                                   6    
HELIX   65 AH2 ALA D  593  ASN D  595  5                                   3    
HELIX   66 AH3 THR D  600  LYS D  615  1                                  16    
HELIX   67 AH4 SER D  630  GLY D  641  1                                  12    
HELIX   68 AH5 ARG D  658  TYR D  662  5                                   5    
HELIX   69 AH6 ASP D  663  GLY D  672  1                                  10    
HELIX   70 AH7 ASN D  679  SER D  686  1                                   8    
HELIX   71 AH8 VAL D  688  VAL D  698  5                                  11    
HELIX   72 AH9 HIS D  712  VAL D  726  1                                  15    
HELIX   73 AI1 SER D  744  PHE D  763  1                                  20    
SHEET    1 AA1 4 ARG A  61  TRP A  62  0                                        
SHEET    2 AA1 4 GLU A  67  LYS A  71 -1  O  LEU A  69   N  ARG A  61           
SHEET    3 AA1 4 ASN A  75  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4 AA1 4 SER A  86  GLU A  91 -1  O  PHE A  89   N  ILE A  76           
SHEET    1 AA2 4 ASP A 104  ILE A 107  0                                        
SHEET    2 AA2 4 PHE A 113  LYS A 122 -1  O  LEU A 115   N  SER A 106           
SHEET    3 AA2 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4 AA2 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1 AA3 4 TRP A 154  TRP A 157  0                                        
SHEET    2 AA3 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3 AA3 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4 AA3 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1 AA4 3 ILE A 194  ASN A 196  0                                        
SHEET    2 AA4 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA4 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1 AA5 4 ILE A 194  ASN A 196  0                                        
SHEET    2 AA5 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3 AA5 4 THR A 265  ASN A 272 -1  O  LYS A 267   N  GLN A 227           
SHEET    4 AA5 4 SER A 284  ILE A 287 -1  O  ILE A 285   N  VAL A 270           
SHEET    1 AA6 2 LEU A 235  PHE A 240  0                                        
SHEET    2 AA6 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1 AA7 4 HIS A 298  TRP A 305  0                                        
SHEET    2 AA7 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3 AA7 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4 AA7 4 ARG A 336  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1 AA8 4 HIS A 298  TRP A 305  0                                        
SHEET    2 AA8 4 ARG A 310  ARG A 317 -1  O  SER A 312   N  THR A 304           
SHEET    3 AA8 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4 AA8 4 HIS A 345  MET A 348 -1  O  GLU A 347   N  SER A 323           
SHEET    1 AA9 4 HIS A 363  PHE A 364  0                                        
SHEET    2 AA9 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3 AA9 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4 AA9 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1 AB1 4 VAL A 404  LEU A 410  0                                        
SHEET    2 AB1 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  GLU A 408           
SHEET    3 AB1 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4 AB1 4 ASP A 438  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1 AB2 4 TYR A 457  PHE A 461  0                                        
SHEET    2 AB2 4 TYR A 467  CYS A 472 -1  O  ARG A 471   N  SER A 458           
SHEET    3 AB2 4 LEU A 479  SER A 484 -1  O  LEU A 479   N  CYS A 472           
SHEET    4 AB2 4 LYS A 489  GLU A 495 -1  O  GLU A 495   N  TYR A 480           
SHEET    1 AB3 8 SER A 511  ILE A 518  0                                        
SHEET    2 AB3 8 LYS A 523  LEU A 530 -1  O  MET A 528   N  LYS A 513           
SHEET    3 AB3 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4 AB3 8 TYR A 540  VAL A 546  1  N  LEU A 543   O  ILE A 574           
SHEET    5 AB3 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 544           
SHEET    6 AB3 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7 AB3 8 GLU A 699  GLY A 705  1  O  ILE A 703   N  ALA A 652           
SHEET    8 AB3 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1 AB4 2 LYS B  41  THR B  42  0                                        
SHEET    2 AB4 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1 AB5 4 LEU B  60  TRP B  62  0                                        
SHEET    2 AB5 4 GLU B  67  LYS B  71 -1  O  LEU B  69   N  ARG B  61           
SHEET    3 AB5 4 ILE B  76  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4 AB5 4 SER B  86  LEU B  90 -1  O  SER B  87   N  VAL B  78           
SHEET    1 AB6 4 ILE B 102  ILE B 107  0                                        
SHEET    2 AB6 4 PHE B 113  LYS B 122 -1  O  LEU B 115   N  SER B 106           
SHEET    3 AB6 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4 AB6 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1 AB7 4 THR B 152  TRP B 157  0                                        
SHEET    2 AB7 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  GLN B 153           
SHEET    3 AB7 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4 AB7 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1 AB8 3 ILE B 194  ASN B 196  0                                        
SHEET    2 AB8 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AB8 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1 AB9 4 ILE B 194  ASN B 196  0                                        
SHEET    2 AB9 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3 AB9 4 THR B 265  ASN B 272 -1  O  LYS B 267   N  GLN B 227           
SHEET    4 AB9 4 SER B 284  GLN B 286 -1  O  ILE B 285   N  VAL B 270           
SHEET    1 AC1 2 LEU B 235  PHE B 240  0                                        
SHEET    2 AC1 2 LYS B 250  PRO B 255 -1  O  LYS B 250   N  PHE B 240           
SHEET    1 AC2 4 HIS B 298  TRP B 305  0                                        
SHEET    2 AC2 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3 AC2 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC2 4 ARG B 336  ASN B 338 -1  O  ARG B 336   N  ASP B 331           
SHEET    1 AC3 4 HIS B 298  TRP B 305  0                                        
SHEET    2 AC3 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3 AC3 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4 AC3 4 GLN B 344  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1 AC4 4 HIS B 363  PHE B 364  0                                        
SHEET    2 AC4 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3 AC4 4 ARG B 382  GLN B 388 -1  O  CYS B 385   N  LYS B 373           
SHEET    4 AC4 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1 AC5 4 VAL B 404  LEU B 410  0                                        
SHEET    2 AC5 4 TYR B 414  SER B 419 -1  O  ILE B 418   N  ILE B 405           
SHEET    3 AC5 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4 AC5 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1 AC6 4 TYR B 457  PHE B 461  0                                        
SHEET    2 AC6 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458           
SHEET    3 AC6 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4 AC6 4 GLY B 490  GLU B 495 -1  O  GLU B 495   N  TYR B 480           
SHEET    1 AC7 8 SER B 511  ILE B 518  0                                        
SHEET    2 AC7 8 LYS B 523  LEU B 530 -1  O  TYR B 526   N  ASP B 515           
SHEET    3 AC7 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4 AC7 8 TYR B 540  VAL B 546  1  N  LEU B 543   O  ILE B 574           
SHEET    5 AC7 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 542           
SHEET    6 AC7 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7 AC7 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8 AC7 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SHEET    1 AC8 4 ARG C  61  TRP C  62  0                                        
SHEET    2 AC8 4 GLU C  67  GLN C  72 -1  O  LEU C  69   N  ARG C  61           
SHEET    3 AC8 4 ASN C  75  ASN C  80 -1  O  LEU C  77   N  TYR C  70           
SHEET    4 AC8 4 SER C  86  LEU C  90 -1  O  PHE C  89   N  ILE C  76           
SHEET    1 AC9 4 ASP C 104  ILE C 107  0                                        
SHEET    2 AC9 4 PHE C 113  LYS C 122 -1  O  LEU C 115   N  SER C 106           
SHEET    3 AC9 4 TYR C 128  ASP C 136 -1  O  SER C 131   N  TYR C 118           
SHEET    4 AC9 4 GLN C 141  LEU C 142 -1  O  GLN C 141   N  ASP C 136           
SHEET    1 AD1 4 TRP C 154  TRP C 157  0                                        
SHEET    2 AD1 4 LEU C 164  TRP C 168 -1  O  VAL C 167   N  TRP C 154           
SHEET    3 AD1 4 ASP C 171  LYS C 175 -1  O  LYS C 175   N  LEU C 164           
SHEET    4 AD1 4 TYR C 183  ARG C 184 -1  O  TYR C 183   N  VAL C 174           
SHEET    1 AD2 3 ILE C 194  ASN C 196  0                                        
SHEET    2 AD2 3 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3 AD2 3 LEU C 214  TRP C 216 -1  N  TRP C 215   O  ALA C 224           
SHEET    1 AD3 4 ILE C 194  ASN C 196  0                                        
SHEET    2 AD3 4 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3 AD3 4 THR C 265  ASN C 272 -1  O  LYS C 267   N  GLN C 227           
SHEET    4 AD3 4 ILE C 285  ILE C 287 -1  O  ILE C 285   N  VAL C 270           
SHEET    1 AD4 2 LEU C 235  PHE C 240  0                                        
SHEET    2 AD4 2 LYS C 250  PRO C 255 -1  O  LYS C 250   N  PHE C 240           
SHEET    1 AD5 4 HIS C 298  THR C 307  0                                        
SHEET    2 AD5 4 ARG C 310  ARG C 317 -1  O  SER C 312   N  THR C 304           
SHEET    3 AD5 4 TYR C 322  TYR C 330 -1  O  ASP C 326   N  LEU C 313           
SHEET    4 AD5 4 TRP C 337  CYS C 339 -1  O  ASN C 338   N  ASP C 329           
SHEET    1 AD6 4 HIS C 298  THR C 307  0                                        
SHEET    2 AD6 4 ARG C 310  ARG C 317 -1  O  SER C 312   N  THR C 304           
SHEET    3 AD6 4 TYR C 322  TYR C 330 -1  O  ASP C 326   N  LEU C 313           
SHEET    4 AD6 4 HIS C 345  MET C 348 -1  O  HIS C 345   N  MET C 325           
SHEET    1 AD7 4 HIS C 363  PHE C 364  0                                        
SHEET    2 AD7 4 SER C 370  SER C 376 -1  O  TYR C 372   N  HIS C 363           
SHEET    3 AD7 4 ARG C 382  GLN C 388 -1  O  PHE C 387   N  PHE C 371           
SHEET    4 AD7 4 LYS C 391  PHE C 396 -1  O  THR C 395   N  TYR C 386           
SHEET    1 AD8 4 VAL C 404  LEU C 410  0                                        
SHEET    2 AD8 4 TYR C 414  SER C 419 -1  O  TYR C 416   N  ALA C 409           
SHEET    3 AD8 4 ASN C 430  GLN C 435 -1  O  TYR C 432   N  TYR C 417           
SHEET    4 AD8 4 VAL C 442  CYS C 444 -1  O  THR C 443   N  LYS C 433           
SHEET    1 AD9 4 TYR C 457  PHE C 461  0                                        
SHEET    2 AD9 4 TYR C 467  CYS C 472 -1  O  ARG C 471   N  SER C 458           
SHEET    3 AD9 4 LEU C 479  SER C 484 -1  O  LEU C 479   N  CYS C 472           
SHEET    4 AD9 4 LYS C 489  GLU C 495 -1  O  GLU C 495   N  TYR C 480           
SHEET    1 AE1 8 SER C 511  ILE C 518  0                                        
SHEET    2 AE1 8 LYS C 523  LEU C 530 -1  O  TYR C 526   N  ASP C 515           
SHEET    3 AE1 8 ILE C 574  PHE C 578 -1  O  VAL C 575   N  ILE C 529           
SHEET    4 AE1 8 TYR C 540  VAL C 546  1  N  ASP C 545   O  ALA C 576           
SHEET    5 AE1 8 VAL C 619  TRP C 629  1  O  ALA C 625   N  LEU C 544           
SHEET    6 AE1 8 CYS C 649  VAL C 653  1  O  VAL C 653   N  GLY C 628           
SHEET    7 AE1 8 GLU C 699  GLY C 705  1  O  ILE C 703   N  ALA C 652           
SHEET    8 AE1 8 GLN C 731  TYR C 735  1  O  GLN C 731   N  TYR C 700           
SHEET    1 AE2 2 LYS D  41  THR D  42  0                                        
SHEET    2 AE2 2 VAL D 507  GLN D 508  1  O  GLN D 508   N  LYS D  41           
SHEET    1 AE3 4 ARG D  61  TRP D  62  0                                        
SHEET    2 AE3 4 GLU D  67  LYS D  71 -1  O  LEU D  69   N  ARG D  61           
SHEET    3 AE3 4 ILE D  76  ASN D  80 -1  O  LEU D  77   N  TYR D  70           
SHEET    4 AE3 4 SER D  86  LEU D  90 -1  O  PHE D  89   N  ILE D  76           
SHEET    1 AE4 4 ILE D 102  ILE D 107  0                                        
SHEET    2 AE4 4 PHE D 113  LYS D 122 -1  O  LEU D 115   N  SER D 106           
SHEET    3 AE4 4 TYR D 128  ASP D 136 -1  O  THR D 129   N  VAL D 121           
SHEET    4 AE4 4 GLN D 141  LEU D 142 -1  O  GLN D 141   N  ASP D 136           
SHEET    1 AE5 4 THR D 152  TRP D 157  0                                        
SHEET    2 AE5 4 LEU D 164  TRP D 168 -1  O  VAL D 167   N  GLN D 153           
SHEET    3 AE5 4 ASP D 171  LYS D 175 -1  O  TYR D 173   N  TYR D 166           
SHEET    4 AE5 4 TYR D 183  ARG D 184 -1  O  TYR D 183   N  VAL D 174           
SHEET    1 AE6 3 ILE D 194  ASN D 196  0                                        
SHEET    2 AE6 3 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3 AE6 3 LEU D 214  TRP D 216 -1  N  TRP D 215   O  ALA D 224           
SHEET    1 AE7 4 ILE D 194  ASN D 196  0                                        
SHEET    2 AE7 4 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3 AE7 4 THR D 265  ASN D 272 -1  O  LYS D 267   N  GLN D 227           
SHEET    4 AE7 4 SER D 284  GLN D 286 -1  O  ILE D 285   N  VAL D 270           
SHEET    1 AE8 2 LEU D 235  PHE D 240  0                                        
SHEET    2 AE8 2 LYS D 250  PRO D 255 -1  O  LYS D 250   N  PHE D 240           
SHEET    1 AE9 4 HIS D 298  TRP D 305  0                                        
SHEET    2 AE9 4 ARG D 310  ARG D 317 -1  O  LEU D 316   N  TYR D 299           
SHEET    3 AE9 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4 AE9 4 TRP D 337  CYS D 339 -1  O  ASN D 338   N  ASP D 329           
SHEET    1 AF1 4 HIS D 298  TRP D 305  0                                        
SHEET    2 AF1 4 ARG D 310  ARG D 317 -1  O  LEU D 316   N  TYR D 299           
SHEET    3 AF1 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4 AF1 4 HIS D 345  MET D 348 -1  O  HIS D 345   N  MET D 325           
SHEET    1 AF2 4 HIS D 363  PHE D 364  0                                        
SHEET    2 AF2 4 SER D 370  SER D 376 -1  O  TYR D 372   N  HIS D 363           
SHEET    3 AF2 4 ARG D 382  GLN D 388 -1  O  PHE D 387   N  PHE D 371           
SHEET    4 AF2 4 THR D 395  PHE D 396 -1  O  THR D 395   N  TYR D 386           
SHEET    1 AF3 4 VAL D 404  LEU D 410  0                                        
SHEET    2 AF3 4 TYR D 414  SER D 419 -1  O  TYR D 416   N  GLU D 408           
SHEET    3 AF3 4 ASN D 430  GLN D 435 -1  O  TYR D 432   N  TYR D 417           
SHEET    4 AF3 4 VAL D 442  CYS D 444 -1  O  THR D 443   N  LYS D 433           
SHEET    1 AF4 4 TYR D 457  PHE D 461  0                                        
SHEET    2 AF4 4 TYR D 467  CYS D 472 -1  O  ARG D 471   N  SER D 458           
SHEET    3 AF4 4 LEU D 479  SER D 484 -1  O  LEU D 479   N  CYS D 472           
SHEET    4 AF4 4 LYS D 489  GLU D 495 -1  O  GLU D 495   N  TYR D 480           
SHEET    1 AF5 8 SER D 511  ILE D 518  0                                        
SHEET    2 AF5 8 LYS D 523  LEU D 530 -1  O  LEU D 530   N  SER D 511           
SHEET    3 AF5 8 ILE D 574  PHE D 578 -1  O  VAL D 575   N  ILE D 529           
SHEET    4 AF5 8 TYR D 540  VAL D 546  1  N  LEU D 543   O  ILE D 574           
SHEET    5 AF5 8 VAL D 619  TRP D 629  1  O  ASP D 620   N  TYR D 540           
SHEET    6 AF5 8 CYS D 649  VAL D 653  1  O  VAL D 653   N  GLY D 628           
SHEET    7 AF5 8 GLU D 699  GLY D 705  1  O  LEU D 701   N  ALA D 652           
SHEET    8 AF5 8 GLN D 731  TYR D 735  1  O  GLN D 731   N  TYR D 700           
SSBOND   1 CYS A  328    CYS A  339                          1555   1555  2.04  
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  2.04  
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  2.04  
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  
SSBOND  11 CYS C  328    CYS C  339                          1555   1555  2.04  
SSBOND  12 CYS C  385    CYS C  394                          1555   1555  2.04  
SSBOND  13 CYS C  444    CYS C  447                          1555   1555  2.03  
SSBOND  14 CYS C  454    CYS C  472                          1555   1555  2.03  
SSBOND  15 CYS C  649    CYS C  762                          1555   1555  2.03  
SSBOND  16 CYS D  328    CYS D  339                          1555   1555  2.04  
SSBOND  17 CYS D  385    CYS D  394                          1555   1555  2.04  
SSBOND  18 CYS D  444    CYS D  447                          1555   1555  2.03  
SSBOND  19 CYS D  454    CYS D  472                          1555   1555  2.03  
SSBOND  20 CYS D  649    CYS D  762                          1555   1555  2.04  
CISPEP   1 GLY A  474    PRO A  475          0         2.92                     
CISPEP   2 GLY B  474    PRO B  475          0         1.43                     
CISPEP   3 GLY C  474    PRO C  475          0         4.31                     
CISPEP   4 GLY D  474    PRO D  475          0         2.85                     
SITE     1 AC1 13 ARG A 125  GLU A 205  GLU A 206  SER A 209                    
SITE     2 AC1 13 PHE A 357  TYR A 547  SER A 630  TYR A 631                    
SITE     3 AC1 13 VAL A 656  TYR A 662  TYR A 666  ASN A 710                    
SITE     4 AC1 13 VAL A 711                                                     
SITE     1 AC2 13 ARG B 125  GLU B 205  GLU B 206  SER B 209                    
SITE     2 AC2 13 PHE B 357  SER B 630  TYR B 631  VAL B 656                    
SITE     3 AC2 13 TRP B 659  TYR B 662  TYR B 666  ASN B 710                    
SITE     4 AC2 13 VAL B 711                                                     
SITE     1 AC3 13 ARG C 125  GLU C 205  GLU C 206  SER C 209                    
SITE     2 AC3 13 PHE C 357  TYR C 547  SER C 630  TYR C 631                    
SITE     3 AC3 13 VAL C 656  TYR C 662  TYR C 666  ASN C 710                    
SITE     4 AC3 13 VAL C 711                                                     
SITE     1 AC4 14 ARG D 125  GLU D 205  GLU D 206  SER D 209                    
SITE     2 AC4 14 PHE D 357  SER D 630  TYR D 631  VAL D 656                    
SITE     3 AC4 14 TRP D 659  TYR D 662  TYR D 666  ASN D 710                    
SITE     4 AC4 14 VAL D 711  HIS D 740                                          
CRYST1  119.365  131.920  123.409  90.00  89.99  90.00 P 1 21 1      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      0.008378  0.000000 -0.000001        0.00000                         
SCALE2      0.000000  0.007580  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008103        0.00000                         
TER    5943      SER A 764                                                      
TER   11908      PRO B 766                                                      
TER   17857      SER C 764                                                      
TER   23822      PRO D 766                                                      
MASTER      369    0    4   73  200    0   16    624202    4  256  224          
END                                                                             

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