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LongText Report for: 2I78-pdb

Name Class
2I78-pdb
HEADER    HYDROLASE                               30-AUG-06   2I78              
TITLE     CRYSTAL STRUCTURE OF HUMAN DIPEPTIDYL PEPTIDASE IV (DPP IV)           
TITLE    2 COMPLEXED WITH ABT-341, A CYCLOHEXENE-CONSTRAINED                    
TITLE    3 PHENETHYLAMINE INHIBITOR                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE IV;                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DIPEPTIDYL PEPTIDASE 4, DPP IV, T-CELL ACTIVATION           
COMPND   5 ANTIGEN CD26, TP103, ADENOSINE DEAMINASE COMPLEXING                  
COMPND   6 PROTEIN 2, ADABP;                                                    
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM                              
KEYWDS    SERINE PEPTIDASE,, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.LONGENECKER,Z.PEI,X.LI                                            
REVDAT   1   09-OCT-07 2I78    0                                                
JRNL        AUTH   Z.PEI,X.LI,T.W.VONGELDERN,D.J.MADAR,                         
JRNL        AUTH 2 K.L LONGENECKER,H.YONG,T.H.LUBBEN,K.D.STEWART,               
JRNL        AUTH 3 B.A.ZINKER,B.J.BACKES,A.S.JUDD,M.MULHERN,                    
JRNL        AUTH 4 S.J.BALLARON,M.A.STASHKO,A.K.MIKA,D.W.A.BENO,                
JRNL        AUTH 5 G.A.REINHART,R.M.FRYER,L.C.PREUSSER,                         
JRNL        AUTH 6 A.J.KEMPF-GROTE,H.L.SHAM,J.M.TREVILLYAN                      
JRNL        TITL   DISCOVERY OF CYCLOHEXENE-CONSTRAINED                         
JRNL        TITL 2 PHENETHYLAMINE ABT-341, A HIGHLY POTENT,                     
JRNL        TITL 3 SELECTIVE, ORALLY BIOAVAILABLE, SAFE AND POTENTIAL           
JRNL        TITL 4 NEXT-GENERATION DIPEPTIDYL PEPTIDASE IV INHIBITOR            
JRNL        TITL 5 FOR THE TREATMENT OF TYPE 2 DIABETES                         
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.50 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 129.10                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 126792                         
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6375                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7246                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 345                          
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 24449                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.27000                                             
REMARK   3    B22 (A**2) : 0.12000                                              
REMARK   3    B33 (A**2) : 1.25000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.26000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.575         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.317         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.232         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.455        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.876                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 24534 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 33384 ; 1.341 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2900 ; 6.844 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1232 ;34.886 ;23.961       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3980 ;18.838 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   120 ;18.036 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3507 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19010 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 11247 ; 0.219 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 16549 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1213 ; 0.172 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    70 ; 0.225 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.306 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 14809 ; 0.541 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23471 ; 0.960 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11465 ; 1.118 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  9913 ; 1.782 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     39       A     764      4                      
REMARK   3           1     B     39       B     764      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   5949 ; 0.310 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   5949 ; 0.750 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     39       C     764      4                      
REMARK   3           1     D     39       D     764      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):   5949 ; 0.280 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    C (A**2):   5949 ; 0.540 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2I78 COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB039224.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 126817                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+Y,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.20950            
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 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 300                                                                      
REMARK 300 REMARK: A DIMER OF DPP4 MOLECULES IS THOUGHT TO BE                   
REMARK 300 BIOLOGICALLY RELEVANT, AND THE ASYMMETRIC UNIT IS COMPRISED          
REMARK 300 OF TWO DIMERS.                                                       
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: DIMER                             
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: DIMER                             
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI                             
REMARK 500   O    HOH A   765     O    HOH A   952              2.08            
REMARK 500   NZ   LYS D   539     O    GLY D   617              2.13            
REMARK 500   ND2  ASN B   219     O    HOH B  1092              2.16            
REMARK 500   O    HOH C   863     O    HOH C   864              2.17            
REMARK 500   NE   ARG A   691     O    HOH A   949              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  90   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    LEU A 415   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    LEU B 276   CA  -  CB  -  CG  ANGL. DEV. =  14.9 DEGREES          
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    ARG A  40      156.13     46.62                                   
REMARK 500    LYS A  71       89.28    -68.75                                   
REMARK 500    ASN A  74      -89.71    -76.08                                   
REMARK 500    GLN A 123     -109.13   -106.24                                   
REMARK 500    TRP A 124     -145.63    -86.39                                   
REMARK 500    HIS A 162       26.10   -151.76                                   
REMARK 500    PRO A 181      147.79    -39.82                                   
REMARK 500    ASP A 192       -0.25     71.16                                   
REMARK 500    ILE A 193      -66.38   -122.00                                   
REMARK 500    SER A 242     -163.69     67.06                                   
REMARK 500    GLU A 244      -45.62    -27.69                                   
REMARK 500    SER A 278      -15.27     56.49                                   
REMARK 500    ALA A 289     -147.86     70.85                                   
REMARK 500    ILE A 295        3.37    -66.89                                   
REMARK 500    GLN A 320       31.80    -78.65                                   
REMARK 500    ALA A 342      -34.98    129.79                                   
REMARK 500    ASN A 377     -179.50    -53.52                                   
REMARK 500    LYS A 423       17.34     57.54                                   
REMARK 500    ASN A 450       76.75   -172.01                                   
REMARK 500    GLN A 508       90.03    -60.72                                   
REMARK 500    ASN A 520       85.15      1.80                                   
REMARK 500    GLU A 521      -55.40     97.00                                   
REMARK 500    TYR A 547      -73.92   -118.86                                   
REMARK 500    ASN A 562     -159.96   -139.29                                   
REMARK 500    ARG A 597       44.20   -141.80                                   
REMARK 500    THR A 600      -95.17   -127.58                                   
REMARK 500    SER A 630     -125.40     75.00                                   
REMARK 500    ASP A 678      -95.45   -120.04                                   
REMARK 500    ASN A 710      -70.70    -91.40                                   
REMARK 500    ASP A 739     -160.50   -107.30                                   
REMARK 500    ILE A 742       54.95     29.77                                   
REMARK 500    ARG B  40     -149.38     41.79                                   
REMARK 500    GLN B  72     -144.00   -148.05                                   
REMARK 500    ASN B  74      -80.14   -122.52                                   
REMARK 500    GLN B 123     -103.90   -112.11                                   
REMARK 500    TRP B 124     -151.06    -89.29                                   
REMARK 500    ARG B 140       28.97     44.00                                   
REMARK 500    HIS B 162       24.81   -149.81                                   
REMARK 500    GLU B 191      123.74    -38.40                                   
REMARK 500    ILE B 193      -63.54   -120.74                                   
REMARK 500    SER B 242     -166.54     65.42                                   
REMARK 500    GLU B 244      -37.99    -36.15                                   
REMARK 500    SER B 277     -118.32    -65.44                                   
REMARK 500    SER B 278       32.08    166.13                                   
REMARK 500    ASN B 281      107.97    -48.13                                   
REMARK 500    ALA B 289     -148.52     74.72                                   
REMARK 500    GLN B 320       49.41    -78.33                                   
REMARK 500    SER B 334      -17.14   -175.55                                   
REMARK 500    ALA B 342      -43.44    117.42                                   
REMARK 500    ASP B 438      103.28   -161.09                                   
REMARK 500    ASN B 450       74.66   -169.59                                   
REMARK 500    ASN B 520       71.21      7.28                                   
REMARK 500    GLU B 521      -57.33     92.64                                   
REMARK 500    TYR B 547      -70.19   -133.78                                   
REMARK 500    ARG B 597       49.03   -141.48                                   
REMARK 500    THR B 600      -94.04   -106.09                                   
REMARK 500    SER B 630     -128.29     65.38                                   
REMARK 500    ALA B 654       58.92     39.96                                   
REMARK 500    PRO B 674       43.45    -83.02                                   
REMARK 500    ASP B 678     -101.20    -90.04                                   
REMARK 500    ASP B 708       97.94    -66.92                                   
REMARK 500    ASN B 710      -72.14   -101.10                                   
REMARK 500    ASP B 739     -160.54   -101.30                                   
REMARK 500    ARG C  40     -142.26    -69.75                                   
REMARK 500    ASN C  51       38.50     72.57                                   
REMARK 500    LYS C  71      107.08    -45.20                                   
REMARK 500    ASN C  74      -61.16   -104.44                                   
REMARK 500    GLN C 123     -106.01   -116.79                                   
REMARK 500    TRP C 124     -143.78    -87.63                                   
REMARK 500    LYS C 139       13.93   -144.43                                   
REMARK 500    PRO C 178       -3.99    -43.95                                   
REMARK 500    GLU C 191      124.01    -25.59                                   
REMARK 500    ASP C 192       12.44     59.71                                   
REMARK 500    ILE C 193      -59.95   -129.44                                   
REMARK 500    ALA C 213       38.04   -145.26                                   
REMARK 500    SER C 242     -166.22     62.62                                   
REMARK 500    SER C 277      -17.36   -152.12                                   
REMARK 500    SER C 278      -35.73     78.04                                   
REMARK 500    ALA C 282      133.40    -37.81                                   
REMARK 500    THR C 288     -122.96    -85.35                                   
REMARK 500    ALA C 289      167.81     64.08                                   
REMARK 500    GLN C 308      -19.51    -46.48                                   
REMARK 500    GLN C 320       30.59    -79.62                                   
REMARK 500    SER C 334      -62.90   -175.90                                   
REMARK 500    ALA C 342       -6.99     73.73                                   
REMARK 500    LYS C 423        9.14     58.96                                   
REMARK 500    TYR C 439       21.65    -66.65                                   
REMARK 500    ASN C 450       79.57   -156.21                                   
REMARK 500    ASN C 520       83.26      6.20                                   
REMARK 500    GLU C 521      -38.35     85.32                                   
REMARK 500    TYR C 547      -65.43   -127.33                                   
REMARK 500    THR C 600      -96.08   -107.12                                   
REMARK 500    SER C 630     -127.49     64.04                                   
REMARK 500    ASP C 678      -95.55   -114.91                                   
REMARK 500    ASN C 679       31.42   -140.01                                   
REMARK 500    ASN C 710      -74.92    -86.81                                   
REMARK 500    ASP C 739     -159.67   -106.07                                   
REMARK 500    ILE C 742       53.09     36.37                                   
REMARK 500    ARG D  40      -76.89    -23.81                                   
REMARK 500    ASN D  74      -80.97    -78.91                                   
REMARK 500    PRO D 109       38.40    -69.04                                   
REMARK 500    GLN D 123     -103.41   -106.08                                   
REMARK 500    TRP D 124     -143.45    -91.43                                   
REMARK 500    LYS D 139       26.64   -151.53                                   
REMARK 500    HIS D 162       16.33   -140.94                                   
REMARK 500    ASP D 192       -3.31     69.60                                   
REMARK 500    ILE D 193      -56.70   -120.29                                   
REMARK 500    SER D 242     -166.79     57.66                                   
REMARK 500    SER D 278       -3.56     71.15                                   
REMARK 500    THR D 288     -166.50   -108.82                                   
REMARK 500    ALA D 289     -159.93     65.47                                   
REMARK 500    ALA D 306      -64.60    -94.95                                   
REMARK 500    THR D 307     -156.47   -120.82                                   
REMARK 500    GLN D 320       39.84    -90.07                                   
REMARK 500    SER D 334      -47.36   -174.58                                   
REMARK 500    ASN D 450       71.91   -166.48                                   
REMARK 500    ASN D 487       16.34   -142.95                                   
REMARK 500    ARG D 492      159.25    179.64                                   
REMARK 500    GLN D 508       81.60    -64.44                                   
REMARK 500    ASN D 520       52.91     38.49                                   
REMARK 500    TYR D 547      -71.22   -109.07                                   
REMARK 500    SER D 583      152.56    -49.67                                   
REMARK 500    ARG D 597       38.46   -146.99                                   
REMARK 500    THR D 600      -91.33   -111.66                                   
REMARK 500    SER D 630     -125.38     65.41                                   
REMARK 500    ASP D 678      -75.24   -107.42                                   
REMARK 500    ASN D 679       18.84   -152.34                                   
REMARK 500    ASN D 710      -77.34    -95.31                                   
REMARK 500    ASP D 739     -156.35   -102.19                                   
REMARK 500    ILE D 742       57.44     31.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2I78 A   39   764  UNP    P27487   DPP4_HUMAN      39    764             
DBREF  2I78 B   39   764  UNP    P27487   DPP4_HUMAN      39    764             
DBREF  2I78 C   39   764  UNP    P27487   DPP4_HUMAN      39    764             
DBREF  2I78 D   39   764  UNP    P27487   DPP4_HUMAN      39    764             
SEQRES   1 A  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 A  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 A  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 A  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 A  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 A  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 A  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 A  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 A  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 A  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 A  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 A  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 A  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 A  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 A  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 A  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 A  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 A  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 A  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 A  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 A  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 A  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 A  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 A  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 A  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 A  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 A  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 A  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 A  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 A  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 A  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 A  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 A  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 A  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 A  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 A  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 A  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 A  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 A  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 A  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 A  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 A  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 A  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 A  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 A  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 A  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 A  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 A  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 A  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 A  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 A  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 A  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 A  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 A  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 A  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 A  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
SEQRES   1 B  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 B  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 B  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 B  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 B  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 B  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 B  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 B  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 B  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 B  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 B  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 B  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 B  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 B  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 B  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 B  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 B  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 B  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 B  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 B  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 B  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 B  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 B  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 B  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 B  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 B  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 B  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 B  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 B  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 B  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 B  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 B  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 B  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 B  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 B  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 B  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 B  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 B  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 B  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 B  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 B  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 B  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 B  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 B  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 B  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 B  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 B  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 B  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 B  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 B  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 B  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 B  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 B  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 B  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 B  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 B  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
SEQRES   1 C  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 C  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 C  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 C  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 C  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 C  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 C  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 C  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 C  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 C  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 C  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 C  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 C  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 C  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 C  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 C  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 C  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 C  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 C  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 C  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 C  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 C  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 C  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 C  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 C  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 C  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 C  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 C  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 C  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 C  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 C  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 C  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 C  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 C  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 C  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 C  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 C  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 C  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 C  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 C  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 C  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 C  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 C  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 C  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 C  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 C  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 C  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 C  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 C  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 C  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 C  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 C  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 C  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 C  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 C  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 C  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
SEQRES   1 D  726  SER ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN          
SEQRES   2 D  726  THR TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER          
SEQRES   3 D  726  ASP HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU          
SEQRES   4 D  726  VAL PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU          
SEQRES   5 D  726  GLU ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN          
SEQRES   6 D  726  ASP TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU          
SEQRES   7 D  726  GLU TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR          
SEQRES   8 D  726  ALA SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU          
SEQRES   9 D  726  ILE THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL          
SEQRES  10 D  726  THR TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP          
SEQRES  11 D  726  ASN ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO          
SEQRES  12 D  726  SER TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE          
SEQRES  13 D  726  TYR ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL          
SEQRES  14 D  726  PHE SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY          
SEQRES  15 D  726  THR PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL          
SEQRES  16 D  726  PRO LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU          
SEQRES  17 D  726  GLN TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA          
SEQRES  18 D  726  GLY ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN          
SEQRES  19 D  726  THR ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE          
SEQRES  20 D  726  GLN ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS          
SEQRES  21 D  726  TYR LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE          
SEQRES  22 D  726  SER LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL          
SEQRES  23 D  726  MET ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP          
SEQRES  24 D  726  ASN CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR          
SEQRES  25 D  726  THR GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS          
SEQRES  26 D  726  PHE THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER          
SEQRES  27 D  726  ASN GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE          
SEQRES  28 D  726  ASP LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP          
SEQRES  29 D  726  GLU VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU          
SEQRES  30 D  726  TYR TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY          
SEQRES  31 D  726  ARG ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS          
SEQRES  32 D  726  VAL THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS          
SEQRES  33 D  726  GLN TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR          
SEQRES  34 D  726  TYR GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR          
SEQRES  35 D  726  THR LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL          
SEQRES  36 D  726  LEU GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN          
SEQRES  37 D  726  VAL GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU          
SEQRES  38 D  726  ASN GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO          
SEQRES  39 D  726  HIS PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP          
SEQRES  40 D  726  VAL TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL          
SEQRES  41 D  726  PHE ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU          
SEQRES  42 D  726  ASN ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY          
SEQRES  43 D  726  TYR GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG          
SEQRES  44 D  726  LEU GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA          
SEQRES  45 D  726  ARG GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG          
SEQRES  46 D  726  ILE ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR          
SEQRES  47 D  726  SER MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS          
SEQRES  48 D  726  GLY ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR          
SEQRES  49 D  726  ASP SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR          
SEQRES  50 D  726  PRO GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL          
SEQRES  51 D  726  MET SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU          
SEQRES  52 D  726  LEU ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN          
SEQRES  53 D  726  GLN SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY          
SEQRES  54 D  726  VAL ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS          
SEQRES  55 D  726  GLY ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR          
SEQRES  56 D  726  HIS MET SER HIS PHE ILE LYS GLN CYS PHE SER                  
HET    KIQ  B 901      31                                                       
HETNAM     KIQ (1S,6R)-3-{[3-(TRIFLUOROMETHYL)-5,6-DIHYDRO[1,2,                 
HETNAM   2 KIQ  4]TRIAZOLO[4,3-A]PYRAZIN-7(8H)-YL]CARBONYL}-6-(2,4,5-           
HETNAM   3 KIQ  TRIFLUOROPHENYL)CYCLOHEX-3-EN-1-AMINE                           
FORMUL   5  KIQ    C19 H17 F6 N5 O                                              
FORMUL   6  HOH   *622(H2 O)                                                    
HELIX    1   1 THR A   44  LYS A   50  1                                   7    
HELIX    2   2 ASP A  200  VAL A  207  1                                   8    
HELIX    3   3 PRO A  290  ILE A  295  1                                   6    
HELIX    4   4 GLU A  421  MET A  425  5                                   5    
HELIX    5   5 ASN A  497  GLN A  505  1                                   9    
HELIX    6   6 ASN A  562  THR A  570  1                                   9    
HELIX    7   7 GLY A  587  HIS A  592  1                                   6    
HELIX    8   8 ALA A  593  ASN A  595  5                                   3    
HELIX    9   9 THR A  600  LYS A  615  1                                  16    
HELIX   10  10 SER A  630  GLY A  641  1                                  12    
HELIX   11  11 ARG A  658  TYR A  662  5                                   5    
HELIX   12  12 ASP A  663  GLY A  672  1                                  10    
HELIX   13  13 ASN A  679  SER A  686  1                                   8    
HELIX   14  14 VAL A  688  VAL A  698  5                                  11    
HELIX   15  15 HIS A  712  VAL A  726  1                                  15    
HELIX   16  16 SER A  744  SER A  764  1                                  21    
HELIX   17  17 THR B   44  ASN B   51  1                                   8    
HELIX   18  18 PHE B   95  GLY B   99  5                                   5    
HELIX   19  19 ASP B  200  VAL B  207  1                                   8    
HELIX   20  20 PRO B  290  ILE B  295  1                                   6    
HELIX   21  21 GLU B  421  MET B  425  5                                   5    
HELIX   22  22 ASN B  497  GLN B  505  1                                   9    
HELIX   23  23 ASN B  562  ASN B  572  1                                  11    
HELIX   24  24 GLY B  587  HIS B  592  1                                   6    
HELIX   25  25 THR B  600  LYS B  615  1                                  16    
HELIX   26  26 SER B  630  LEU B  640  1                                  11    
HELIX   27  27 ARG B  658  TYR B  662  5                                   5    
HELIX   28  28 ASP B  663  GLY B  672  1                                  10    
HELIX   29  29 ASN B  679  SER B  686  1                                   8    
HELIX   30  30 VAL B  688  VAL B  698  5                                  11    
HELIX   31  31 PHE B  713  ASP B  725  1                                  13    
HELIX   32  32 SER B  744  SER B  764  1                                  21    
HELIX   33  33 THR C   44  ASN C   51  1                                   8    
HELIX   34  34 GLU C   91  ASP C   96  5                                   6    
HELIX   35  35 ASP C  200  VAL C  207  1                                   8    
HELIX   36  36 PRO C  290  ILE C  295  1                                   6    
HELIX   37  37 GLU C  421  MET C  425  5                                   5    
HELIX   38  38 ASN C  497  GLN C  505  1                                   9    
HELIX   39  39 ASN C  562  THR C  570  1                                   9    
HELIX   40  40 GLY C  587  HIS C  592  1                                   6    
HELIX   41  41 ALA C  593  ASN C  595  5                                   3    
HELIX   42  42 THR C  600  MET C  616  1                                  17    
HELIX   43  43 SER C  630  GLY C  641  1                                  12    
HELIX   44  44 ARG C  658  TYR C  662  5                                   5    
HELIX   45  45 ASP C  663  GLY C  672  1                                  10    
HELIX   46  46 ASN C  679  SER C  686  1                                   8    
HELIX   47  47 VAL C  688  VAL C  698  5                                  11    
HELIX   48  48 PHE C  713  VAL C  726  1                                  14    
HELIX   49  49 SER C  744  SER C  764  1                                  21    
HELIX   50  50 THR D   44  LYS D   50  1                                   7    
HELIX   51  51 ASP D  200  VAL D  207  1                                   8    
HELIX   52  52 PRO D  290  ILE D  295  1                                   6    
HELIX   53  53 GLU D  421  MET D  425  5                                   5    
HELIX   54  54 ASN D  497  GLN D  505  1                                   9    
HELIX   55  55 ASN D  562  THR D  570  1                                   9    
HELIX   56  56 GLY D  587  HIS D  592  1                                   6    
HELIX   57  57 ALA D  593  ASN D  595  5                                   3    
HELIX   58  58 THR D  600  LYS D  615  1                                  16    
HELIX   59  59 SER D  630  GLY D  641  1                                  12    
HELIX   60  60 ARG D  658  TYR D  662  5                                   5    
HELIX   61  61 ASP D  663  GLY D  672  1                                  10    
HELIX   62  62 ASN D  679  SER D  686  1                                   8    
HELIX   63  63 VAL D  688  VAL D  698  5                                  11    
HELIX   64  64 HIS D  712  VAL D  726  1                                  15    
HELIX   65  65 SER D  744  SER D  764  1                                  21    
SHEET    1   A 2 LYS A  41  THR A  42  0                                        
SHEET    2   A 2 VAL A 507  GLN A 508  1  O  GLN A 508   N  LYS A  41           
SHEET    1   B 4 LEU A  60  TRP A  62  0                                        
SHEET    2   B 4 GLU A  67  LYS A  71 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   B 4 ILE A  76  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   B 4 SER A  86  LEU A  90 -1  O  PHE A  89   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  GLU A 117   N  ASP A 104           
SHEET    3   C 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   C 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   D 4 THR A 152  TRP A 157  0                                        
SHEET    2   D 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  GLN A 153           
SHEET    3   D 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   D 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   E 3 ILE A 194  ASN A 196  0                                        
SHEET    2   E 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   F 4 ILE A 194  ASN A 196  0                                        
SHEET    2   F 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   F 4 THR A 265  ASN A 272 -1  O  VAL A 271   N  LEU A 223           
SHEET    4   F 4 SER A 284  ILE A 287 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   G 2 LEU A 235  PHE A 240  0                                        
SHEET    2   G 2 LYS A 250  PRO A 255 -1  O  LYS A 250   N  PHE A 240           
SHEET    1   H 4 HIS A 298  TRP A 305  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   H 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   H 4 ARG A 336  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   I 4 HIS A 298  TRP A 305  0                                        
SHEET    2   I 4 ARG A 310  ARG A 317 -1  O  LEU A 316   N  TYR A 299           
SHEET    3   I 4 TYR A 322  ASP A 331 -1  O  ASP A 326   N  LEU A 313           
SHEET    4   I 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1   J 4 HIS A 363  PHE A 364  0                                        
SHEET    2   J 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   J 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
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  ALA A 409           
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 LYS A 489  GLU A 495 -1  O  LEU A 494   N  TYR A 480           
SHEET    1   M 8 SER A 511  LEU A 519  0                                        
SHEET    2   M 8 THR A 522  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   M 8 ILE A 574  PHE A 578 -1  O  VAL A 575   N  ILE A 529           
SHEET    4   M 8 TYR A 540  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 2 LYS B  41  THR B  42  0                                        
SHEET    2   N 2 VAL B 507  GLN B 508  1  O  GLN B 508   N  LYS B  41           
SHEET    1   O 4 ARG B  61  TRP B  62  0                                        
SHEET    2   O 4 GLU B  67  TYR B  70 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   O 4 ILE B  76  ASN B  80 -1  O  PHE B  79   N  TYR B  68           
SHEET    4   O 4 SER B  86  LEU B  90 -1  O  PHE B  89   N  ILE B  76           
SHEET    1   P 4 ILE B 102  ILE B 107  0                                        
SHEET    2   P 4 PHE B 113  LYS B 122 -1  O  GLU B 117   N  ASN B 103           
SHEET    3   P 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4   P 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   Q 4 THR B 152  TRP B 157  0                                        
SHEET    2   Q 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  GLN B 153           
SHEET    3   Q 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   Q 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   R 3 ILE B 194  ASN B 196  0                                        
SHEET    2   R 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   R 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   S 4 ILE B 194  ASN B 196  0                                        
SHEET    2   S 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   S 4 THR B 265  ASN B 272 -1  O  VAL B 271   N  LEU B 223           
SHEET    4   S 4 SER B 284  ILE B 287 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   T 2 LEU B 235  PHE B 240  0                                        
SHEET    2   T 2 LYS B 250  PRO B 255 -1  O  VAL B 252   N  TYR B 238           
SHEET    1   U 4 HIS B 298  TRP B 305  0                                        
SHEET    2   U 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   U 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   U 4 TRP B 337  CYS B 339 -1  O  ASN B 338   N  ASP B 329           
SHEET    1   V 4 HIS B 298  TRP B 305  0                                        
SHEET    2   V 4 ARG B 310  ARG B 317 -1  O  LEU B 316   N  TYR B 299           
SHEET    3   V 4 TYR B 322  TYR B 330 -1  O  ASP B 326   N  LEU B 313           
SHEET    4   V 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   W 4 HIS B 363  PHE B 364  0                                        
SHEET    2   W 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   W 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4   W 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   X 4 VAL B 404  LEU B 410  0                                        
SHEET    2   X 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  GLU B 408           
SHEET    3   X 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   X 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   Y 4 TYR B 457  PHE B 461  0                                        
SHEET    2   Y 4 TYR B 467  CYS B 472 -1  O  GLN B 469   N  SER B 460           
SHEET    3   Y 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4   Y 4 LYS B 489  GLU B 495 -1  O  LEU B 494   N  TYR B 480           
SHEET    1   Z 8 SER B 511  LEU B 519  0                                        
SHEET    2   Z 8 THR B 522  LEU B 530 -1  O  LEU B 530   N  SER B 511           
SHEET    3   Z 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   Z 8 TYR B 540  VAL B 546  1  N  LEU B 543   O  ILE B 574           
SHEET    5   Z 8 VAL B 619  TRP B 629  1  O  TRP B 627   N  VAL B 546           
SHEET    6   Z 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   Z 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8   Z 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SHEET    1  AA 4 ARG C  61  TRP C  62  0                                        
SHEET    2  AA 4 GLU C  67  LYS C  71 -1  O  LEU C  69   N  ARG C  61           
SHEET    3  AA 4 ILE C  76  ASN C  80 -1  O  PHE C  79   N  TYR C  68           
SHEET    4  AA 4 SER C  86  LEU C  90 -1  O  SER C  87   N  VAL C  78           
SHEET    1  AB 4 ASP C 104  ILE C 107  0                                        
SHEET    2  AB 4 PHE C 113  LYS C 122 -1  O  LEU C 115   N  SER C 106           
SHEET    3  AB 4 TYR C 128  ASP C 136 -1  O  ASP C 133   N  LEU C 116           
SHEET    4  AB 4 GLN C 141  LEU C 142 -1  O  GLN C 141   N  ASP C 136           
SHEET    1  AC 4 TRP C 154  TRP C 157  0                                        
SHEET    2  AC 4 LEU C 164  TRP C 168 -1  O  ALA C 165   N  THR C 156           
SHEET    3  AC 4 ASP C 171  LYS C 175 -1  O  TYR C 173   N  TYR C 166           
SHEET    4  AC 4 TYR C 183  ARG C 184 -1  O  TYR C 183   N  VAL C 174           
SHEET    1  AD 3 ILE C 194  ASN C 196  0                                        
SHEET    2  AD 3 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3  AD 3 LEU C 214  TRP C 216 -1  N  TRP C 215   O  ALA C 224           
SHEET    1  AE 4 ILE C 194  ASN C 196  0                                        
SHEET    2  AE 4 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3  AE 4 THR C 265  ASN C 272 -1  O  LYS C 267   N  GLN C 227           
SHEET    4  AE 4 SER C 284  ILE C 287 -1  O  ILE C 285   N  VAL C 270           
SHEET    1  AF 2 LEU C 235  PHE C 240  0                                        
SHEET    2  AF 2 LYS C 250  PRO C 255 -1  O  LYS C 250   N  PHE C 240           
SHEET    1  AG 4 HIS C 298  THR C 307  0                                        
SHEET    2  AG 4 ARG C 310  ARG C 317 -1  O  SER C 312   N  THR C 304           
SHEET    3  AG 4 TYR C 322  TYR C 330 -1  O  ASP C 326   N  LEU C 313           
SHEET    4  AG 4 TRP C 337  CYS C 339 -1  O  ASN C 338   N  ASP C 329           
SHEET    1  AH 4 HIS C 298  THR C 307  0                                        
SHEET    2  AH 4 ARG C 310  ARG C 317 -1  O  SER C 312   N  THR C 304           
SHEET    3  AH 4 TYR C 322  TYR C 330 -1  O  ASP C 326   N  LEU C 313           
SHEET    4  AH 4 HIS C 345  MET C 348 -1  O  HIS C 345   N  MET C 325           
SHEET    1  AI 4 HIS C 363  PHE C 364  0                                        
SHEET    2  AI 4 SER C 370  SER C 376 -1  O  TYR C 372   N  HIS C 363           
SHEET    3  AI 4 ARG C 382  GLN C 388 -1  O  PHE C 387   N  PHE C 371           
SHEET    4  AI 4 THR C 395  PHE C 396 -1  O  THR C 395   N  TYR C 386           
SHEET    1  AJ 4 VAL C 404  LEU C 410  0                                        
SHEET    2  AJ 4 TYR C 414  SER C 419 -1  O  TYR C 416   N  ALA C 409           
SHEET    3  AJ 4 ASN C 430  GLN C 435 -1  O  TYR C 432   N  TYR C 417           
SHEET    4  AJ 4 VAL C 442  CYS C 444 -1  O  THR C 443   N  LYS C 433           
SHEET    1  AK 4 TYR C 457  PHE C 461  0                                        
SHEET    2  AK 4 TYR C 467  CYS C 472 -1  O  ARG C 471   N  SER C 458           
SHEET    3  AK 4 LEU C 479  SER C 484 -1  O  THR C 481   N  LEU C 470           
SHEET    4  AK 4 LYS C 489  GLU C 495 -1  O  GLU C 495   N  TYR C 480           
SHEET    1  AL 8 SER C 511  LEU C 519  0                                        
SHEET    2  AL 8 THR C 522  LEU C 530 -1  O  TYR C 526   N  ASP C 515           
SHEET    3  AL 8 ILE C 574  PHE C 578 -1  O  VAL C 575   N  ILE C 529           
SHEET    4  AL 8 TYR C 540  VAL C 546  1  N  ASP C 545   O  ALA C 576           
SHEET    5  AL 8 VAL C 619  TRP C 629  1  O  ALA C 625   N  LEU C 542           
SHEET    6  AL 8 CYS C 649  VAL C 653  1  O  VAL C 653   N  GLY C 628           
SHEET    7  AL 8 GLU C 699  GLY C 705  1  O  LEU C 701   N  ALA C 652           
SHEET    8  AL 8 GLN C 731  TYR C 735  1  O  GLN C 731   N  TYR C 700           
SHEET    1  AM 4 LEU D  60  TRP D  62  0                                        
SHEET    2  AM 4 GLU D  67  LYS D  71 -1  O  LEU D  69   N  ARG D  61           
SHEET    3  AM 4 ILE D  76  ASN D  80 -1  O  LEU D  77   N  TYR D  70           
SHEET    4  AM 4 SER D  86  LEU D  90 -1  O  PHE D  89   N  ILE D  76           
SHEET    1  AN 4 ASP D 104  ILE D 107  0                                        
SHEET    2  AN 4 PHE D 113  LYS D 122 -1  O  LEU D 115   N  SER D 106           
SHEET    3  AN 4 TYR D 128  ASP D 136 -1  O  THR D 129   N  VAL D 121           
SHEET    4  AN 4 GLN D 141  LEU D 142 -1  O  GLN D 141   N  ASP D 136           
SHEET    1  AO 4 TRP D 154  TRP D 157  0                                        
SHEET    2  AO 4 LEU D 164  TRP D 168 -1  O  VAL D 167   N  TRP D 154           
SHEET    3  AO 4 ASP D 171  LYS D 175 -1  O  TYR D 173   N  TYR D 166           
SHEET    4  AO 4 TYR D 183  ARG D 184 -1  O  TYR D 183   N  VAL D 174           
SHEET    1  AP 3 ILE D 194  ASN D 196  0                                        
SHEET    2  AP 3 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3  AP 3 LEU D 214  TRP D 216 -1  N  TRP D 215   O  ALA D 224           
SHEET    1  AQ 4 ILE D 194  ASN D 196  0                                        
SHEET    2  AQ 4 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3  AQ 4 THR D 265  ASN D 272 -1  O  LYS D 267   N  GLN D 227           
SHEET    4  AQ 4 ILE D 285  ILE D 287 -1  O  ILE D 285   N  VAL D 270           
SHEET    1  AR 2 LEU D 235  PHE D 240  0                                        
SHEET    2  AR 2 LYS D 250  PRO D 255 -1  O  LYS D 250   N  PHE D 240           
SHEET    1  AS 4 HIS D 298  TRP D 305  0                                        
SHEET    2  AS 4 ARG D 310  ARG D 317 -1  O  SER D 312   N  THR D 304           
SHEET    3  AS 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4  AS 4 TRP D 337  ASN D 338 -1  O  ASN D 338   N  ASP D 329           
SHEET    1  AT 4 HIS D 298  TRP D 305  0                                        
SHEET    2  AT 4 ARG D 310  ARG D 317 -1  O  SER D 312   N  THR D 304           
SHEET    3  AT 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4  AT 4 HIS D 345  MET D 348 -1  O  GLU D 347   N  SER D 323           
SHEET    1  AU 4 HIS D 363  PHE D 364  0                                        
SHEET    2  AU 4 SER D 370  SER D 376 -1  O  TYR D 372   N  HIS D 363           
SHEET    3  AU 4 ARG D 382  GLN D 388 -1  O  PHE D 387   N  PHE D 371           
SHEET    4  AU 4 THR D 395  PHE D 396 -1  O  THR D 395   N  TYR D 386           
SHEET    1  AV 4 VAL D 404  LEU D 410  0                                        
SHEET    2  AV 4 TYR D 414  SER D 419 -1  O  ILE D 418   N  ILE D 405           
SHEET    3  AV 4 ASN D 430  GLN D 435 -1  O  TYR D 432   N  TYR D 417           
SHEET    4  AV 4 VAL D 442  CYS D 444 -1  O  THR D 443   N  LYS D 433           
SHEET    1  AW 4 TYR D 457  PHE D 461  0                                        
SHEET    2  AW 4 TYR D 467  CYS D 472 -1  O  GLN D 469   N  SER D 460           
SHEET    3  AW 4 LEU D 479  SER D 484 -1  O  LEU D 479   N  CYS D 472           
SHEET    4  AW 4 LYS D 489  GLU D 495 -1  O  LEU D 491   N  LEU D 482           
SHEET    1  AX 8 SER D 511  LEU D 519  0                                        
SHEET    2  AX 8 THR D 522  LEU D 530 -1  O  THR D 522   N  LEU D 519           
SHEET    3  AX 8 ILE D 574  PHE D 578 -1  O  VAL D 575   N  ILE D 529           
SHEET    4  AX 8 TYR D 540  ASP D 545  1  N  LEU D 543   O  ILE D 574           
SHEET    5  AX 8 VAL D 619  TRP D 629  1  O  ASP D 620   N  TYR D 540           
SHEET    6  AX 8 CYS D 649  VAL D 653  1  O  ILE D 651   N  ILE D 626           
SHEET    7  AX 8 GLU D 699  GLY D 705  1  O  LEU D 701   N  ALA D 652           
SHEET    8  AX 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    2.06  
SSBOND   5 CYS A  649    CYS A  762                        1555   1555    2.07  
SSBOND   6 CYS B  328    CYS B  339                        1555   1555    2.04  
SSBOND   7 CYS B  385    CYS B  394                        1555   1555    2.05  
SSBOND   8 CYS B  444    CYS B  447                        1555   1555    2.03  
SSBOND   9 CYS B  454    CYS B  472                        1555   1555    2.08  
SSBOND  10 CYS B  649    CYS B  762                        1555   1555    2.05  
SSBOND  11 CYS C  328    CYS C  339                        1555   1555    2.04  
SSBOND  12 CYS C  385    CYS C  394                        1555   1555    2.05  
SSBOND  13 CYS C  444    CYS C  447                        1555   1555    2.04  
SSBOND  14 CYS C  454    CYS C  472                        1555   1555    2.04  
SSBOND  15 CYS C  649    CYS C  762                        1555   1555    2.04  
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    2.04  
SSBOND  19 CYS D  454    CYS D  472                        1555   1555    2.04  
SSBOND  20 CYS D  649    CYS D  762                        1555   1555    2.06  
CISPEP   1 ALA A  289    PRO A  290          0        -4.66                     
CISPEP   2 GLY A  474    PRO A  475          0         9.83                     
CISPEP   3 ALA B  289    PRO B  290          0        -8.38                     
CISPEP   4 GLY B  474    PRO B  475          0         5.77                     
CISPEP   5 ALA C  289    PRO C  290          0       -21.05                     
CISPEP   6 GLY C  474    PRO C  475          0         5.03                     
CISPEP   7 ALA D  289    PRO D  290          0        -6.12                     
CISPEP   8 GLY D  474    PRO D  475          0         2.68                     
CRYST1  119.933  126.419  127.531  90.00 100.26  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      0.008338  0.000000  0.001509        0.00000                         
SCALE2      0.000000  0.007910  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007969        0.00000                         
TER    5950      SER A 764                                                      
TER   11900      SER B 764                                                      
TER   17850      SER C 764                                                      
TER   23800      SER D 764                                                      
MASTER      430    0    1   65  200    0    0    624449    4   71  224          
END                                                                             

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