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LongText Report for: 7a3l-pdb

Name Class
7a3l-pdb
HEADER    HYDROLASE                               18-AUG-20   7A3L              
TITLE     CRYSTAL STRUCTURE OF DPP8 IN COMPLEX WITH A 4-OXO-B-LACTAM BASED      
TITLE    2 INHIBITOR, A241                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 8;                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: DP8,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 1,DPRP-1,       
COMPND   5 DIPEPTIDYL PEPTIDASE VIII,DPP VIII,PROLYL DIPEPTIDASE DPP8;          
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: DPP8, DPRP1, MSTP097, MSTP135, MSTP141;                        
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    DPP8, PROTEASE, HYDROLASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.H.ROSS,R.HUBER                                                      
REVDAT   1   30-JUN-21 7A3L    0                                                
JRNL        AUTH   L.FEHR,L.A.R.CARVALHO,B.H.ROSS,K.LUM,A.C.VIEIRA,             
JRNL        AUTH 2 R.KIEFERSAUER,R.GEISS-FRIEDLANDER,M.KAISER,T.RODRIGUES,      
JRNL        AUTH 3 S.D.LUCAS,B.F.CRAVATT,R.HUBER,R.MOREIRA                      
JRNL        TITL   DISCOVERY AND DEVELOPMENT OF 4-OXO-BETA-LACTAMS AS NOVEL     
JRNL        TITL 2 INHIBITORS OF DIPEPTIDYL PEPTIDASES 8 AND 9                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0238                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 126252                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6645                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9246                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 486                          
REMARK   3   BIN FREE R VALUE                    : 0.4260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20527                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 131                                     
REMARK   3   SOLVENT ATOMS            : 46                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.39                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64000                                              
REMARK   3    B22 (A**2) : 2.64000                                              
REMARK   3    B33 (A**2) : -3.28000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.419         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.282         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.224         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.618        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21236 ; 0.002 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A): 19256 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28809 ; 1.187 ; 1.652       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44712 ; 1.056 ; 1.579       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2524 ; 6.647 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1176 ;31.012 ;21.879       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3540 ;14.190 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   140 ;13.918 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2674 ; 0.038 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23652 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4706 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7A3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292108113.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 132897                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.418                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.67                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.29100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.080                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6EOO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.46 M NA CITRATE, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      130.61750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      130.61750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       82.01700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      126.38950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       82.01700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      126.38950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      130.61750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       82.01700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      126.38950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      130.61750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       82.01700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      126.38950            
REMARK 290   SMTRY3   8  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: 5790 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 69260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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: 5760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 66760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     MET A     1                                                      
REMARK 465     TRP A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     MET A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     ASN A    16                                                      
REMARK 465     MET A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     MET A    21                                                      
REMARK 465     GLU A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     VAL A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     ILE A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     THR A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     CYS A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     ASN A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     SER A    42                                                      
REMARK 465     GLN A    43                                                      
REMARK 465     ASP A    44                                                      
REMARK 465     ARG A    45                                                      
REMARK 465     PRO A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     ILE A   898                                                      
REMARK 465     MET B     1                                                      
REMARK 465     TRP B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     MET B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ILE B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     ASN B    16                                                      
REMARK 465     MET B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     MET B    21                                                      
REMARK 465     GLU B    22                                                      
REMARK 465     THR B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     VAL B    28                                                      
REMARK 465     GLU B    29                                                      
REMARK 465     ILE B    30                                                      
REMARK 465     PHE B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     CYS B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     ASN B    39                                                      
REMARK 465     ILE B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     SER B    42                                                      
REMARK 465     GLN B    43                                                      
REMARK 465     ASP B    44                                                      
REMARK 465     ARG B    45                                                      
REMARK 465     PRO B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     GLN B   140                                                      
REMARK 465     ALA B   141                                                      
REMARK 465     THR B   142                                                      
REMARK 465     LEU B   143                                                      
REMARK 465     ASP B   144                                                      
REMARK 465     TYR B   145                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     MET B   147                                                      
REMARK 465     TYR B   148                                                      
REMARK 465     SER B   149                                                      
REMARK 465     ARG B   150                                                      
REMARK 465     GLU B   151                                                      
REMARK 465     GLU B   152                                                      
REMARK 465     GLU B   153                                                      
REMARK 465     LEU B   154                                                      
REMARK 465     LEU B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     GLU B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     LYS B   159                                                      
REMARK 465     ARG B   160                                                      
REMARK 465     ILE B   161                                                      
REMARK 465     GLY B   162                                                      
REMARK 465     THR B   163                                                      
REMARK 465     ILE B   898                                                      
REMARK 465     MET C     1                                                      
REMARK 465     TRP C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ARG C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     MET C     8                                                      
REMARK 465     LYS C     9                                                      
REMARK 465     ILE C    10                                                      
REMARK 465     LYS C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     GLY C    13                                                      
REMARK 465     LYS C    14                                                      
REMARK 465     CYS C    15                                                      
REMARK 465     ASN C    16                                                      
REMARK 465     MET C    17                                                      
REMARK 465     ALA C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     MET C    21                                                      
REMARK 465     GLU C    22                                                      
REMARK 465     THR C    23                                                      
REMARK 465     GLU C    24                                                      
REMARK 465     GLN C    25                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     VAL C    28                                                      
REMARK 465     GLU C    29                                                      
REMARK 465     ILE C    30                                                      
REMARK 465     PHE C    31                                                      
REMARK 465     GLU C    32                                                      
REMARK 465     THR C    33                                                      
REMARK 465     ALA C    34                                                      
REMARK 465     ASP C    35                                                      
REMARK 465     CYS C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     ASN C    39                                                      
REMARK 465     ILE C    40                                                      
REMARK 465     GLU C    41                                                      
REMARK 465     SER C    42                                                      
REMARK 465     GLN C    43                                                      
REMARK 465     ASP C    44                                                      
REMARK 465     ARG C    45                                                      
REMARK 465     PRO C    46                                                      
REMARK 465     LYS C    47                                                      
REMARK 465     ILE C   898                                                      
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    ALA A  77      113.57   -161.82                                   
REMARK 500    GLN A 140       81.81     58.64                                   
REMARK 500    ALA A 141      112.07    -39.77                                   
REMARK 500    TYR A 145     -115.45     43.42                                   
REMARK 500    MET A 147      -62.62   -121.05                                   
REMARK 500    TYR A 148     -177.63     62.81                                   
REMARK 500    ILE A 161      -69.63    -91.08                                   
REMARK 500    ASP A 224       96.90   -166.39                                   
REMARK 500    ILE A 445      -89.46   -101.28                                   
REMARK 500    PHE A 453       94.61   -177.65                                   
REMARK 500    GLU A 518       58.33    -90.05                                   
REMARK 500    VAL A 534      -70.11    -74.52                                   
REMARK 500    SER A 546      144.07   -170.64                                   
REMARK 500    VAL A 558      -61.19    -91.27                                   
REMARK 500    ASN A 559       73.20   -114.88                                   
REMARK 500    ILE A 620      -60.45    -95.34                                   
REMARK 500    VAL A 684      -63.05   -104.32                                   
REMARK 500    TYR A 720       -0.75     74.79                                   
REMARK 500    SER A 755     -112.41     59.81                                   
REMARK 500    ALA A 779       53.79     38.19                                   
REMARK 500    LEU A 783      103.82   -160.97                                   
REMARK 500    ASN A 802       52.90   -157.10                                   
REMARK 500    ASN A 835      -70.01    -86.92                                   
REMARK 500    ARG A 864     -148.50    -86.51                                   
REMARK 500    LEU A 888      -61.28   -151.60                                   
REMARK 500    MET B  76       51.73    -93.79                                   
REMARK 500    ASP B 224      102.59   -162.98                                   
REMARK 500    VAL B 242      -60.24   -102.77                                   
REMARK 500    PHE B 372       64.29   -116.61                                   
REMARK 500    ILE B 445      -96.93    -98.09                                   
REMARK 500    PHE B 453       99.76   -175.34                                   
REMARK 500    GLU B 518       56.25    -92.36                                   
REMARK 500    SER B 546      142.82   -171.02                                   
REMARK 500    VAL B 558      -61.32    -91.10                                   
REMARK 500    ASN B 559       77.35   -117.60                                   
REMARK 500    ASP B 655       60.43     65.17                                   
REMARK 500    TYR B 669      -73.42   -117.84                                   
REMARK 500    VAL B 684      -67.00   -100.95                                   
REMARK 500    TYR B 720       -5.42     71.07                                   
REMARK 500    SER B 755     -112.15     62.96                                   
REMARK 500    ASN B 802       48.72   -155.50                                   
REMARK 500    ARG B 864     -144.73    -87.33                                   
REMARK 500    LEU B 888      -61.83   -141.43                                   
REMARK 500    TYR C  71       71.43   -112.10                                   
REMARK 500    HIS C  72       38.86   -148.86                                   
REMARK 500    PHE C 139      -78.35     64.46                                   
REMARK 500    ALA C 141     -160.06     51.67                                   
REMARK 500    LEU C 143       63.19     65.29                                   
REMARK 500    TYR C 145       98.20    -62.00                                   
REMARK 500    ARG C 160       43.06   -104.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6EOP   RELATED DB: PDB                                   
REMARK 900 DPP8 IN COMPLEX WITH AN INHIBITORY PEPTIDE                           
DBREF  7A3L A    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  7A3L B    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  7A3L C    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
SEQRES   1 A  898  MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY          
SEQRES   2 A  898  LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU          
SEQRES   3 A  898  GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN          
SEQRES   4 A  898  ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR          
SEQRES   5 A  898  VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU          
SEQRES   6 A  898  ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS          
SEQRES   7 A  898  ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO          
SEQRES   8 A  898  ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET          
SEQRES   9 A  898  SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU          
SEQRES  10 A  898  ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU          
SEQRES  11 A  898  SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU          
SEQRES  12 A  898  ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG          
SEQRES  13 A  898  GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR          
SEQRES  14 A  898  ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA          
SEQRES  15 A  898  GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN          
SEQRES  16 A  898  GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU          
SEQRES  17 A  898  THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS          
SEQRES  18 A  898  PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN          
SEQRES  19 A  898  ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG          
SEQRES  20 A  898  ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU          
SEQRES  21 A  898  GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU          
SEQRES  22 A  898  GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS          
SEQRES  23 A  898  PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU          
SEQRES  24 A  898  ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU          
SEQRES  25 A  898  ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG          
SEQRES  26 A  898  ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN          
SEQRES  27 A  898  PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP          
SEQRES  28 A  898  ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU          
SEQRES  29 A  898  ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR          
SEQRES  30 A  898  ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA          
SEQRES  31 A  898  TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN          
SEQRES  32 A  898  ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU          
SEQRES  33 A  898  ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL          
SEQRES  34 A  898  PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR          
SEQRES  35 A  898  THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL          
SEQRES  36 A  898  PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE          
SEQRES  37 A  898  ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS          
SEQRES  38 A  898  ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER          
SEQRES  39 A  898  SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO          
SEQRES  40 A  898  ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU          
SEQRES  41 A  898  VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU          
SEQRES  42 A  898  VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER          
SEQRES  43 A  898  PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN          
SEQRES  44 A  898  PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER          
SEQRES  45 A  898  HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE          
SEQRES  46 A  898  SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER          
SEQRES  47 A  898  LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS          
SEQRES  48 A  898  LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA          
SEQRES  49 A  898  GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER          
SEQRES  50 A  898  PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU          
SEQRES  51 A  898  TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO          
SEQRES  52 A  898  THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU          
SEQRES  53 A  898  VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU          
SEQRES  54 A  898  ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE          
SEQRES  55 A  898  ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU          
SEQRES  56 A  898  GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP          
SEQRES  57 A  898  ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR          
SEQRES  58 A  898  ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP          
SEQRES  59 A  898  SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN          
SEQRES  60 A  898  ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO          
SEQRES  61 A  898  VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU          
SEQRES  62 A  898  ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR          
SEQRES  63 A  898  TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO          
SEQRES  64 A  898  SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU          
SEQRES  65 A  898  ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU          
SEQRES  66 A  898  SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN          
SEQRES  67 A  898  ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU          
SEQRES  68 A  898  SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU          
SEQRES  69 A  898  GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL          
SEQRES  70 A  898  ILE                                                          
SEQRES   1 B  898  MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY          
SEQRES   2 B  898  LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU          
SEQRES   3 B  898  GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN          
SEQRES   4 B  898  ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR          
SEQRES   5 B  898  VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU          
SEQRES   6 B  898  ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS          
SEQRES   7 B  898  ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO          
SEQRES   8 B  898  ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET          
SEQRES   9 B  898  SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU          
SEQRES  10 B  898  ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU          
SEQRES  11 B  898  SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU          
SEQRES  12 B  898  ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG          
SEQRES  13 B  898  GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR          
SEQRES  14 B  898  ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA          
SEQRES  15 B  898  GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN          
SEQRES  16 B  898  GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU          
SEQRES  17 B  898  THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS          
SEQRES  18 B  898  PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN          
SEQRES  19 B  898  ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG          
SEQRES  20 B  898  ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU          
SEQRES  21 B  898  GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU          
SEQRES  22 B  898  GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS          
SEQRES  23 B  898  PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU          
SEQRES  24 B  898  ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU          
SEQRES  25 B  898  ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG          
SEQRES  26 B  898  ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN          
SEQRES  27 B  898  PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP          
SEQRES  28 B  898  ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU          
SEQRES  29 B  898  ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR          
SEQRES  30 B  898  ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA          
SEQRES  31 B  898  TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN          
SEQRES  32 B  898  ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU          
SEQRES  33 B  898  ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL          
SEQRES  34 B  898  PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR          
SEQRES  35 B  898  THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL          
SEQRES  36 B  898  PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE          
SEQRES  37 B  898  ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS          
SEQRES  38 B  898  ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER          
SEQRES  39 B  898  SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO          
SEQRES  40 B  898  ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU          
SEQRES  41 B  898  VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU          
SEQRES  42 B  898  VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER          
SEQRES  43 B  898  PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN          
SEQRES  44 B  898  PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER          
SEQRES  45 B  898  HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE          
SEQRES  46 B  898  SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER          
SEQRES  47 B  898  LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS          
SEQRES  48 B  898  LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA          
SEQRES  49 B  898  GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER          
SEQRES  50 B  898  PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU          
SEQRES  51 B  898  TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO          
SEQRES  52 B  898  THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU          
SEQRES  53 B  898  VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU          
SEQRES  54 B  898  ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE          
SEQRES  55 B  898  ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU          
SEQRES  56 B  898  GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP          
SEQRES  57 B  898  ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR          
SEQRES  58 B  898  ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP          
SEQRES  59 B  898  SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN          
SEQRES  60 B  898  ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO          
SEQRES  61 B  898  VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU          
SEQRES  62 B  898  ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR          
SEQRES  63 B  898  TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO          
SEQRES  64 B  898  SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU          
SEQRES  65 B  898  ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU          
SEQRES  66 B  898  SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN          
SEQRES  67 B  898  ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU          
SEQRES  68 B  898  SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU          
SEQRES  69 B  898  GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL          
SEQRES  70 B  898  ILE                                                          
SEQRES   1 C  898  MET TRP LYS ARG SER GLU GLN MET LYS ILE LYS SER GLY          
SEQRES   2 C  898  LYS CYS ASN MET ALA ALA ALA MET GLU THR GLU GLN LEU          
SEQRES   3 C  898  GLY VAL GLU ILE PHE GLU THR ALA ASP CYS GLU GLU ASN          
SEQRES   4 C  898  ILE GLU SER GLN ASP ARG PRO LYS LEU GLU PRO PHE TYR          
SEQRES   5 C  898  VAL GLU ARG TYR SER TRP SER GLN LEU LYS LYS LEU LEU          
SEQRES   6 C  898  ALA ASP THR ARG LYS TYR HIS GLY TYR MET MET ALA LYS          
SEQRES   7 C  898  ALA PRO HIS ASP PHE MET PHE VAL LYS ARG ASN ASP PRO          
SEQRES   8 C  898  ASP GLY PRO HIS SER ASP ARG ILE TYR TYR LEU ALA MET          
SEQRES   9 C  898  SER GLY GLU ASN ARG GLU ASN THR LEU PHE TYR SER GLU          
SEQRES  10 C  898  ILE PRO LYS THR ILE ASN ARG ALA ALA VAL LEU MET LEU          
SEQRES  11 C  898  SER TRP LYS PRO LEU LEU ASP LEU PHE GLN ALA THR LEU          
SEQRES  12 C  898  ASP TYR GLY MET TYR SER ARG GLU GLU GLU LEU LEU ARG          
SEQRES  13 C  898  GLU ARG LYS ARG ILE GLY THR VAL GLY ILE ALA SER TYR          
SEQRES  14 C  898  ASP TYR HIS GLN GLY SER GLY THR PHE LEU PHE GLN ALA          
SEQRES  15 C  898  GLY SER GLY ILE TYR HIS VAL LYS ASP GLY GLY PRO GLN          
SEQRES  16 C  898  GLY PHE THR GLN GLN PRO LEU ARG PRO ASN LEU VAL GLU          
SEQRES  17 C  898  THR SER CYS PRO ASN ILE ARG MET ASP PRO LYS LEU CYS          
SEQRES  18 C  898  PRO ALA ASP PRO ASP TRP ILE ALA PHE ILE HIS SER ASN          
SEQRES  19 C  898  ASP ILE TRP ILE SER ASN ILE VAL THR ARG GLU GLU ARG          
SEQRES  20 C  898  ARG LEU THR TYR VAL HIS ASN GLU LEU ALA ASN MET GLU          
SEQRES  21 C  898  GLU ASP ALA ARG SER ALA GLY VAL ALA THR PHE VAL LEU          
SEQRES  22 C  898  GLN GLU GLU PHE ASP ARG TYR SER GLY TYR TRP TRP CYS          
SEQRES  23 C  898  PRO LYS ALA GLU THR THR PRO SER GLY GLY LYS ILE LEU          
SEQRES  24 C  898  ARG ILE LEU TYR GLU GLU ASN ASP GLU SER GLU VAL GLU          
SEQRES  25 C  898  ILE ILE HIS VAL THR SER PRO MET LEU GLU THR ARG ARG          
SEQRES  26 C  898  ALA ASP SER PHE ARG TYR PRO LYS THR GLY THR ALA ASN          
SEQRES  27 C  898  PRO LYS VAL THR PHE LYS MET SER GLU ILE MET ILE ASP          
SEQRES  28 C  898  ALA GLU GLY ARG ILE ILE ASP VAL ILE ASP LYS GLU LEU          
SEQRES  29 C  898  ILE GLN PRO PHE GLU ILE LEU PHE GLU GLY VAL GLU TYR          
SEQRES  30 C  898  ILE ALA ARG ALA GLY TRP THR PRO GLU GLY LYS TYR ALA          
SEQRES  31 C  898  TRP SER ILE LEU LEU ASP ARG SER GLN THR ARG LEU GLN          
SEQRES  32 C  898  ILE VAL LEU ILE SER PRO GLU LEU PHE ILE PRO VAL GLU          
SEQRES  33 C  898  ASP ASP VAL MET GLU ARG GLN ARG LEU ILE GLU SER VAL          
SEQRES  34 C  898  PRO ASP SER VAL THR PRO LEU ILE ILE TYR GLU GLU THR          
SEQRES  35 C  898  THR ASP ILE TRP ILE ASN ILE HIS ASP ILE PHE HIS VAL          
SEQRES  36 C  898  PHE PRO GLN SER HIS GLU GLU GLU ILE GLU PHE ILE PHE          
SEQRES  37 C  898  ALA SER GLU CYS LYS THR GLY PHE ARG HIS LEU TYR LYS          
SEQRES  38 C  898  ILE THR SER ILE LEU LYS GLU SER LYS TYR LYS ARG SER          
SEQRES  39 C  898  SER GLY GLY LEU PRO ALA PRO SER ASP PHE LYS CYS PRO          
SEQRES  40 C  898  ILE LYS GLU GLU ILE ALA ILE THR SER GLY GLU TRP GLU          
SEQRES  41 C  898  VAL LEU GLY ARG HIS GLY SER ASN ILE GLN VAL ASP GLU          
SEQRES  42 C  898  VAL ARG ARG LEU VAL TYR PHE GLU GLY THR LYS ASP SER          
SEQRES  43 C  898  PRO LEU GLU HIS HIS LEU TYR VAL VAL SER TYR VAL ASN          
SEQRES  44 C  898  PRO GLY GLU VAL THR ARG LEU THR ASP ARG GLY TYR SER          
SEQRES  45 C  898  HIS SER CYS CYS ILE SER GLN HIS CYS ASP PHE PHE ILE          
SEQRES  46 C  898  SER LYS TYR SER ASN GLN LYS ASN PRO HIS CYS VAL SER          
SEQRES  47 C  898  LEU TYR LYS LEU SER SER PRO GLU ASP ASP PRO THR CYS          
SEQRES  48 C  898  LYS THR LYS GLU PHE TRP ALA THR ILE LEU ASP SER ALA          
SEQRES  49 C  898  GLY PRO LEU PRO ASP TYR THR PRO PRO GLU ILE PHE SER          
SEQRES  50 C  898  PHE GLU SER THR THR GLY PHE THR LEU TYR GLY MET LEU          
SEQRES  51 C  898  TYR LYS PRO HIS ASP LEU GLN PRO GLY LYS LYS TYR PRO          
SEQRES  52 C  898  THR VAL LEU PHE ILE TYR GLY GLY PRO GLN VAL GLN LEU          
SEQRES  53 C  898  VAL ASN ASN ARG PHE LYS GLY VAL LYS TYR PHE ARG LEU          
SEQRES  54 C  898  ASN THR LEU ALA SER LEU GLY TYR VAL VAL VAL VAL ILE          
SEQRES  55 C  898  ASP ASN ARG GLY SER CYS HIS ARG GLY LEU LYS PHE GLU          
SEQRES  56 C  898  GLY ALA PHE LYS TYR LYS MET GLY GLN ILE GLU ILE ASP          
SEQRES  57 C  898  ASP GLN VAL GLU GLY LEU GLN TYR LEU ALA SER ARG TYR          
SEQRES  58 C  898  ASP PHE ILE ASP LEU ASP ARG VAL GLY ILE HIS GLY TRP          
SEQRES  59 C  898  SER TYR GLY GLY TYR LEU SER LEU MET ALA LEU MET GLN          
SEQRES  60 C  898  ARG SER ASP ILE PHE ARG VAL ALA ILE ALA GLY ALA PRO          
SEQRES  61 C  898  VAL THR LEU TRP ILE PHE TYR ASP THR GLY TYR THR GLU          
SEQRES  62 C  898  ARG TYR MET GLY HIS PRO ASP GLN ASN GLU GLN GLY TYR          
SEQRES  63 C  898  TYR LEU GLY SER VAL ALA MET GLN ALA GLU LYS PHE PRO          
SEQRES  64 C  898  SER GLU PRO ASN ARG LEU LEU LEU LEU HIS GLY PHE LEU          
SEQRES  65 C  898  ASP GLU ASN VAL HIS PHE ALA HIS THR SER ILE LEU LEU          
SEQRES  66 C  898  SER PHE LEU VAL ARG ALA GLY LYS PRO TYR ASP LEU GLN          
SEQRES  67 C  898  ILE TYR PRO GLN GLU ARG HIS SER ILE ARG VAL PRO GLU          
SEQRES  68 C  898  SER GLY GLU HIS TYR GLU LEU HIS LEU LEU HIS TYR LEU          
SEQRES  69 C  898  GLN GLU ASN LEU GLY SER ARG ILE ALA ALA LEU LYS VAL          
SEQRES  70 C  898  ILE                                                          
HET    QXN  A 901      24                                                       
HET    GOL  A 902       6                                                       
HET    TMO  A 903       5                                                       
HET    GOL  A 904       6                                                       
HET     CL  A 905       1                                                       
HET    QXN  B 901      24                                                       
HET    GOL  B 902       6                                                       
HET    TMO  B 903       5                                                       
HET    TMO  B 904       5                                                       
HET    GOL  B 905       6                                                       
HET     CL  B 906       1                                                       
HET    QXN  C 901      24                                                       
HET    GOL  C 902       6                                                       
HET    TMO  C 903       5                                                       
HET    GOL  C 904       6                                                       
HET     CL  C 905       1                                                       
HETNAM     QXN 2-ETHYL-2-METHANOYL-~{N}-[3-[(4-METHYLPIPERAZIN-1-YL)            
HETNAM   2 QXN  METHYL]PHENYL]BUTANAMIDE                                        
HETNAM     GOL GLYCEROL                                                         
HETNAM     TMO TRIMETHYLAMINE OXIDE                                             
HETNAM      CL CHLORIDE ION                                                     
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  QXN    3(C19 H29 N3 O2)                                             
FORMUL   5  GOL    6(C3 H8 O3)                                                  
FORMUL   6  TMO    4(C3 H9 N O)                                                 
FORMUL   8   CL    3(CL 1-)                                                     
FORMUL  20  HOH   *46(H2 O)                                                     
HELIX    1 AA1 SER A   57  LYS A   70  1                                  14    
HELIX    2 AA2 THR A  270  ASP A  278  1                                   9    
HELIX    3 AA3 MET A  320  ARG A  324  5                                   5    
HELIX    4 AA4 PRO A  367  PHE A  372  1                                   6    
HELIX    5 AA5 SER A  408  GLU A  410  5                                   3    
HELIX    6 AA6 ASP A  418  VAL A  429  1                                  12    
HELIX    7 AA7 TYR A  686  LEU A  695  1                                  10    
HELIX    8 AA8 GLY A  711  GLY A  716  1                                   6    
HELIX    9 AA9 ALA A  717  LYS A  719  5                                   3    
HELIX   10 AB1 ILE A  725  TYR A  741  1                                  17    
HELIX   11 AB2 SER A  755  ARG A  768  1                                  14    
HELIX   12 AB3 ASP A  788  GLY A  797  1                                  10    
HELIX   13 AB4 HIS A  798  GLN A  801  5                                   4    
HELIX   14 AB5 ASN A  802  SER A  810  1                                   9    
HELIX   15 AB6 VAL A  811  PHE A  818  5                                   8    
HELIX   16 AB7 PHE A  838  ALA A  851  1                                  14    
HELIX   17 AB8 VAL A  869  LEU A  888  1                                  20    
HELIX   18 AB9 SER A  890  VAL A  897  1                                   8    
HELIX   19 AC1 SER B   57  ARG B   69  1                                  13    
HELIX   20 AC2 THR B  270  PHE B  277  1                                   8    
HELIX   21 AC3 PRO B  367  PHE B  372  1                                   6    
HELIX   22 AC4 SER B  408  GLU B  410  5                                   3    
HELIX   23 AC5 ASP B  418  VAL B  429  1                                  12    
HELIX   24 AC6 TYR B  686  LEU B  695  1                                  10    
HELIX   25 AC7 GLY B  711  GLY B  716  1                                   6    
HELIX   26 AC8 ALA B  717  LYS B  719  5                                   3    
HELIX   27 AC9 ILE B  725  TYR B  741  1                                  17    
HELIX   28 AD1 SER B  755  ARG B  768  1                                  14    
HELIX   29 AD2 ASP B  788  GLY B  797  1                                  10    
HELIX   30 AD3 HIS B  798  GLN B  801  5                                   4    
HELIX   31 AD4 ASN B  802  GLY B  809  1                                   8    
HELIX   32 AD5 SER B  810  PHE B  818  5                                   9    
HELIX   33 AD6 PHE B  838  ALA B  851  1                                  14    
HELIX   34 AD7 VAL B  869  LEU B  888  1                                  20    
HELIX   35 AD8 SER B  890  VAL B  897  1                                   8    
HELIX   36 AD9 SER C   57  LYS C   70  1                                  14    
HELIX   37 AE1 GLY C   73  ALA C   77  5                                   5    
HELIX   38 AE2 SER C  149  LEU C  154  1                                   6    
HELIX   39 AE3 ILE C  161  GLY C  165  5                                   5    
HELIX   40 AE4 THR C  270  ASP C  278  1                                   9    
HELIX   41 AE5 PRO C  367  PHE C  372  1                                   6    
HELIX   42 AE6 SER C  408  GLU C  410  5                                   3    
HELIX   43 AE7 ASP C  418  VAL C  429  1                                  12    
HELIX   44 AE8 TYR C  686  LEU C  695  1                                  10    
HELIX   45 AE9 GLY C  711  ALA C  717  1                                   7    
HELIX   46 AF1 ILE C  725  TYR C  741  1                                  17    
HELIX   47 AF2 SER C  755  ARG C  768  1                                  14    
HELIX   48 AF3 LEU C  783  TYR C  787  5                                   5    
HELIX   49 AF4 ASP C  788  GLY C  797  1                                  10    
HELIX   50 AF5 HIS C  798  GLN C  801  5                                   4    
HELIX   51 AF6 ASN C  802  GLY C  809  1                                   8    
HELIX   52 AF7 SER C  810  PHE C  818  5                                   9    
HELIX   53 AF8 PHE C  838  ALA C  851  1                                  14    
HELIX   54 AF9 VAL C  869  LEU C  888  1                                  20    
HELIX   55 AG1 SER C  890  VAL C  897  1                                   8    
SHEET    1 AA1 5 GLU A  49  PRO A  50  0                                        
SHEET    2 AA1 5 LYS A 660  PHE A 667  1  O  LYS A 661   N  GLU A  49           
SHEET    3 AA1 5 VAL A 698  ILE A 702  1  O  VAL A 698   N  VAL A 665           
SHEET    4 AA1 5 THR A 645  TYR A 651 -1  N  TYR A 651   O  VAL A 699           
SHEET    5 AA1 5 GLU A 634  GLU A 639 -1  N  GLU A 634   O  LEU A 650           
SHEET    1 AA2 6 GLU A  49  PRO A  50  0                                        
SHEET    2 AA2 6 LYS A 660  PHE A 667  1  O  LYS A 661   N  GLU A  49           
SHEET    3 AA2 6 ILE A 744  TRP A 754  1  O  GLY A 750   N  LEU A 666           
SHEET    4 AA2 6 PHE A 772  GLY A 778  1  O  ARG A 773   N  VAL A 749           
SHEET    5 AA2 6 LEU A 825  GLY A 830  1  O  LEU A 828   N  ALA A 777           
SHEET    6 AA2 6 ASP A 856  TYR A 860  1  O  ASP A 856   N  LEU A 827           
SHEET    1 AA3 4 HIS A  81  LYS A  87  0                                        
SHEET    2 AA3 4 HIS A  95  ALA A 103 -1  O  ARG A  98   N  VAL A  86           
SHEET    3 AA3 4 THR A 112  PRO A 119 -1  O  PHE A 114   N  TYR A 101           
SHEET    4 AA3 4 LYS A 133  PRO A 134 -1  O  LYS A 133   N  TYR A 115           
SHEET    1 AA4 4 ASP A 170  TYR A 171  0                                        
SHEET    2 AA4 4 THR A 177  ALA A 182 -1  O  LEU A 179   N  ASP A 170           
SHEET    3 AA4 4 GLY A 185  LYS A 190 -1  O  VAL A 189   N  PHE A 178           
SHEET    4 AA4 4 ASN A 205  LEU A 206 -1  O  ASN A 205   N  HIS A 188           
SHEET    1 AA5 4 MET A 216  LEU A 220  0                                        
SHEET    2 AA5 4 TRP A 227  HIS A 232 -1  O  ILE A 231   N  MET A 216           
SHEET    3 AA5 4 ASP A 235  ASN A 240 -1  O  TRP A 237   N  PHE A 230           
SHEET    4 AA5 4 GLU A 246  ARG A 248 -1  O  ARG A 247   N  ILE A 238           
SHEET    1 AA6 8 GLU A 290  THR A 291  0                                        
SHEET    2 AA6 8 PHE A 412  PRO A 414  0                                        
SHEET    3 AA6 8 ARG A 264  VAL A 268  0                                        
SHEET    4 AA6 8 SER A 281  TRP A 285 -1  O  GLY A 282   N  GLY A 267           
SHEET    5 AA6 8 LYS A 297  ASP A 307 -1  O  GLU A 304   N  GLY A 282           
SHEET    6 AA6 8 LYS A 340  ILE A 350 -1  O  ILE A 348   N  LEU A 299           
SHEET    7 AA6 8 ILE A 356  LEU A 364 -1  O  ILE A 360   N  GLU A 347           
SHEET    8 AA6 8 PHE A 412  PRO A 414 -1  O  ILE A 413   N  GLU A 363           
SHEET    1 AA7 2 ILE A 313  THR A 317  0                                        
SHEET    2 AA7 2 ALA A 326  ARG A 330 -1  O  ASP A 327   N  VAL A 316           
SHEET    1 AA8 4 TYR A 377  TRP A 383  0                                        
SHEET    2 AA8 4 ALA A 390  LEU A 395 -1  O  LEU A 395   N  TYR A 377           
SHEET    3 AA8 4 ARG A 401  ILE A 407 -1  O  ILE A 407   N  ALA A 390           
SHEET    4 AA8 4 LEU A 436  THR A 442 -1  O  LEU A 436   N  LEU A 406           
SHEET    1 AA9 4 PHE A 453  VAL A 455  0                                        
SHEET    2 AA9 4 GLU A 463  SER A 470 -1  O  ILE A 467   N  HIS A 454           
SHEET    3 AA9 4 HIS A 478  ILE A 485 -1  O  ILE A 482   N  PHE A 466           
SHEET    4 AA9 4 ILE A 508  ALA A 513 -1  O  ILE A 512   N  LYS A 481           
SHEET    1 AB1 3 VAL A 521  LEU A 522  0                                        
SHEET    2 AB1 3 LEU A 537  GLY A 542 -1  O  GLU A 541   N  LEU A 522           
SHEET    3 AB1 3 ILE A 529  ASP A 532 -1  N  GLN A 530   O  TYR A 539           
SHEET    1 AB2 4 VAL A 521  LEU A 522  0                                        
SHEET    2 AB2 4 LEU A 537  GLY A 542 -1  O  GLU A 541   N  LEU A 522           
SHEET    3 AB2 4 HIS A 551  SER A 556 -1  O  TYR A 553   N  PHE A 540           
SHEET    4 AB2 4 THR A 564  ARG A 565 -1  O  THR A 564   N  VAL A 554           
SHEET    1 AB3 4 SER A 572  ILE A 577  0                                        
SHEET    2 AB3 4 PHE A 583  SER A 589 -1  O  LYS A 587   N  SER A 574           
SHEET    3 AB3 4 CYS A 596  SER A 603 -1  O  CYS A 596   N  TYR A 588           
SHEET    4 AB3 4 THR A 613  LEU A 621 -1  O  ALA A 618   N  LEU A 599           
SHEET    1 AB4 5 GLU B  49  PRO B  50  0                                        
SHEET    2 AB4 5 LYS B 660  PHE B 667  1  O  LYS B 661   N  GLU B  49           
SHEET    3 AB4 5 VAL B 698  ILE B 702  1  O  VAL B 698   N  VAL B 665           
SHEET    4 AB4 5 THR B 645  TYR B 651 -1  N  TYR B 651   O  VAL B 699           
SHEET    5 AB4 5 GLU B 634  GLU B 639 -1  N  GLU B 634   O  LEU B 650           
SHEET    1 AB5 6 GLU B  49  PRO B  50  0                                        
SHEET    2 AB5 6 LYS B 660  PHE B 667  1  O  LYS B 661   N  GLU B  49           
SHEET    3 AB5 6 ILE B 744  TRP B 754  1  O  GLY B 750   N  LEU B 666           
SHEET    4 AB5 6 PHE B 772  GLY B 778  1  O  ARG B 773   N  VAL B 749           
SHEET    5 AB5 6 LEU B 825  GLY B 830  1  O  LEU B 828   N  ALA B 777           
SHEET    6 AB5 6 ASP B 856  TYR B 860  1  O  ASP B 856   N  LEU B 827           
SHEET    1 AB6 4 HIS B  81  LYS B  87  0                                        
SHEET    2 AB6 4 HIS B  95  ALA B 103 -1  O  ARG B  98   N  VAL B  86           
SHEET    3 AB6 4 THR B 112  PRO B 119 -1  O  PHE B 114   N  TYR B 101           
SHEET    4 AB6 4 LYS B 133  PRO B 134 -1  O  LYS B 133   N  TYR B 115           
SHEET    1 AB7 4 ASP B 170  HIS B 172  0                                        
SHEET    2 AB7 4 THR B 177  ALA B 182 -1  O  LEU B 179   N  ASP B 170           
SHEET    3 AB7 4 GLY B 185  LYS B 190 -1  O  VAL B 189   N  PHE B 178           
SHEET    4 AB7 4 ASN B 205  LEU B 206 -1  O  ASN B 205   N  HIS B 188           
SHEET    1 AB8 4 MET B 216  CYS B 221  0                                        
SHEET    2 AB8 4 ASP B 224  HIS B 232 -1  O  ILE B 231   N  MET B 216           
SHEET    3 AB8 4 ASP B 235  ASN B 240 -1  O  TRP B 237   N  PHE B 230           
SHEET    4 AB8 4 GLU B 246  ARG B 248 -1  O  ARG B 247   N  ILE B 238           
SHEET    1 AB9 8 GLU B 290  THR B 291  0                                        
SHEET    2 AB9 8 PHE B 412  PRO B 414  0                                        
SHEET    3 AB9 8 ARG B 264  VAL B 268  0                                        
SHEET    4 AB9 8 SER B 281  TRP B 285 -1  O  GLY B 282   N  GLY B 267           
SHEET    5 AB9 8 LYS B 297  ASP B 307 -1  O  GLU B 304   N  GLY B 282           
SHEET    6 AB9 8 LYS B 340  ILE B 350 -1  O  ILE B 350   N  LYS B 297           
SHEET    7 AB9 8 ILE B 356  LEU B 364 -1  O  LYS B 362   N  MET B 345           
SHEET    8 AB9 8 PHE B 412  PRO B 414 -1  O  ILE B 413   N  GLU B 363           
SHEET    1 AC1 2 ILE B 313  THR B 317  0                                        
SHEET    2 AC1 2 ALA B 326  ARG B 330 -1  O  PHE B 329   N  ILE B 314           
SHEET    1 AC2 4 VAL B 375  TRP B 383  0                                        
SHEET    2 AC2 4 ALA B 390  ASP B 396 -1  O  LEU B 395   N  TYR B 377           
SHEET    3 AC2 4 ARG B 401  ILE B 407 -1  O  ILE B 407   N  ALA B 390           
SHEET    4 AC2 4 LEU B 436  THR B 442 -1  O  LEU B 436   N  LEU B 406           
SHEET    1 AC3 4 PHE B 453  VAL B 455  0                                        
SHEET    2 AC3 4 GLU B 463  SER B 470 -1  O  ILE B 467   N  HIS B 454           
SHEET    3 AC3 4 HIS B 478  ILE B 485 -1  O  TYR B 480   N  PHE B 468           
SHEET    4 AC3 4 ILE B 508  ALA B 513 -1  O  ILE B 512   N  LYS B 481           
SHEET    1 AC4 4 GLN B 530  ASP B 532  0                                        
SHEET    2 AC4 4 LEU B 537  SER B 546 -1  O  TYR B 539   N  GLN B 530           
SHEET    3 AC4 4 GLU B 549  SER B 556 -1  O  TYR B 553   N  PHE B 540           
SHEET    4 AC4 4 THR B 564  ARG B 565 -1  O  THR B 564   N  VAL B 554           
SHEET    1 AC5 4 SER B 572  ILE B 577  0                                        
SHEET    2 AC5 4 PHE B 583  SER B 589 -1  O  ILE B 585   N  CYS B 576           
SHEET    3 AC5 4 CYS B 596  SER B 603 -1  O  TYR B 600   N  PHE B 584           
SHEET    4 AC5 4 THR B 613  LEU B 621 -1  O  ALA B 618   N  LEU B 599           
SHEET    1 AC6 5 GLU C  49  PRO C  50  0                                        
SHEET    2 AC6 5 LYS C 660  PHE C 667  1  O  LYS C 661   N  GLU C  49           
SHEET    3 AC6 5 VAL C 698  ILE C 702  1  O  VAL C 698   N  VAL C 665           
SHEET    4 AC6 5 THR C 645  TYR C 651 -1  N  TYR C 651   O  VAL C 699           
SHEET    5 AC6 5 GLU C 634  GLU C 639 -1  N  GLU C 634   O  LEU C 650           
SHEET    1 AC7 6 GLU C  49  PRO C  50  0                                        
SHEET    2 AC7 6 LYS C 660  PHE C 667  1  O  LYS C 661   N  GLU C  49           
SHEET    3 AC7 6 ILE C 744  TRP C 754  1  O  GLY C 750   N  LEU C 666           
SHEET    4 AC7 6 PHE C 772  GLY C 778  1  O  ARG C 773   N  VAL C 749           
SHEET    5 AC7 6 LEU C 825  GLY C 830  1  O  LEU C 828   N  ALA C 777           
SHEET    6 AC7 6 ASP C 856  TYR C 860  1  O  ASP C 856   N  LEU C 827           
SHEET    1 AC8 4 HIS C  81  LYS C  87  0                                        
SHEET    2 AC8 4 HIS C  95  MET C 104 -1  O  ARG C  98   N  VAL C  86           
SHEET    3 AC8 4 ASN C 111  PRO C 119 -1  O  PHE C 114   N  TYR C 101           
SHEET    4 AC8 4 LYS C 133  PRO C 134 -1  O  LYS C 133   N  TYR C 115           
SHEET    1 AC9 4 ASP C 170  HIS C 172  0                                        
SHEET    2 AC9 4 THR C 177  ALA C 182 -1  O  LEU C 179   N  ASP C 170           
SHEET    3 AC9 4 GLY C 185  LYS C 190 -1  O  VAL C 189   N  PHE C 178           
SHEET    4 AC9 4 ASN C 205  LEU C 206 -1  O  ASN C 205   N  HIS C 188           
SHEET    1 AD1 4 MET C 216  CYS C 221  0                                        
SHEET    2 AD1 4 ASP C 224  HIS C 232 -1  O  ILE C 231   N  MET C 216           
SHEET    3 AD1 4 ASP C 235  ASN C 240 -1  O  TRP C 237   N  PHE C 230           
SHEET    4 AD1 4 GLU C 246  ARG C 248 -1  O  ARG C 247   N  ILE C 238           
SHEET    1 AD2 8 GLU C 290  THR C 291  0                                        
SHEET    2 AD2 8 PHE C 412  PRO C 414  0                                        
SHEET    3 AD2 8 ARG C 264  VAL C 268  0                                        
SHEET    4 AD2 8 SER C 281  TRP C 285 -1  O  GLY C 282   N  GLY C 267           
SHEET    5 AD2 8 LYS C 297  ASP C 307 -1  O  LEU C 302   N  TRP C 284           
SHEET    6 AD2 8 LYS C 340  ILE C 350 -1  O  ILE C 348   N  LEU C 299           
SHEET    7 AD2 8 ILE C 356  LEU C 364 -1  O  ILE C 360   N  GLU C 347           
SHEET    8 AD2 8 PHE C 412  PRO C 414 -1  O  ILE C 413   N  GLU C 363           
SHEET    1 AD3 2 ILE C 313  THR C 317  0                                        
SHEET    2 AD3 2 ALA C 326  ARG C 330 -1  O  PHE C 329   N  ILE C 314           
SHEET    1 AD4 4 VAL C 375  TRP C 383  0                                        
SHEET    2 AD4 4 ALA C 390  ASP C 396 -1  O  LEU C 395   N  GLU C 376           
SHEET    3 AD4 4 ARG C 401  ILE C 407 -1  O  ILE C 407   N  ALA C 390           
SHEET    4 AD4 4 LEU C 436  THR C 442 -1  O  LEU C 436   N  LEU C 406           
SHEET    1 AD5 4 PHE C 453  VAL C 455  0                                        
SHEET    2 AD5 4 GLU C 463  SER C 470 -1  O  ILE C 467   N  HIS C 454           
SHEET    3 AD5 4 HIS C 478  ILE C 485 -1  O  ILE C 482   N  PHE C 466           
SHEET    4 AD5 4 ILE C 508  ALA C 513 -1  O  ILE C 512   N  LYS C 481           
SHEET    1 AD6 4 GLN C 530  ASP C 532  0                                        
SHEET    2 AD6 4 LEU C 537  GLY C 542 -1  O  LEU C 537   N  ASP C 532           
SHEET    3 AD6 4 HIS C 551  SER C 556 -1  O  TYR C 553   N  PHE C 540           
SHEET    4 AD6 4 THR C 564  ARG C 565 -1  O  THR C 564   N  VAL C 554           
SHEET    1 AD7 4 SER C 572  ILE C 577  0                                        
SHEET    2 AD7 4 PHE C 583  SER C 589 -1  O  ILE C 585   N  CYS C 576           
SHEET    3 AD7 4 CYS C 596  SER C 603 -1  O  TYR C 600   N  PHE C 584           
SHEET    4 AD7 4 THR C 613  LEU C 621 -1  O  ALA C 618   N  LEU C 599           
LINK         OG  SER A 755                 C6  QXN A 901     1555   1555  1.45  
LINK         OG  SER B 755                 C6  QXN B 901     1555   1555  1.45  
LINK         OG  SER C 755                 C6  QXN C 901     1555   1555  1.45  
CRYST1  164.034  252.779  261.235  90.00  90.00  90.00 C 2 2 21     24          
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      0.006096  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.003956  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003828        0.00000                         
TER    6911      VAL A 897                                                      
TER   13629      VAL B 897                                                      
TER   20540      VAL C 897                                                      
MASTER      518    0   16   55  150    0    0    620704    3  131  210          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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