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LongText Report for: 6trw-pdb

Name Class
6trw-pdb
HEADER    HYDROLASE                               19-DEC-19   6TRW              
TITLE     CRYSTAL STRUCTURE OF DPP8 IN COMPLEX WITH THE EIL PEPTIDE             
TITLE    2 (SLRFLFEGQRIADNH)                                                    
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;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: SER-LEU-ARG-PHE-LEU-PHE-GLU-GLY-GLN-ARG;                   
COMPND  10 CHAIN: D, E, F;                                                      
COMPND  11 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;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606                                                 
KEYWDS    EIL PEPTIDE, DPP8, SUMO1, HYDROLASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ROSS,R.HUBER                                                        
REVDAT   1   13-JAN-21 6TRW    0                                                
JRNL        AUTH   B.ROSS,R.HUBER                                               
JRNL        TITL   THE AEROSOL-GENERATOR: DIRECT SOAKING OF NAKED PROTEIN       
JRNL        TITL 2 CRYSTALS FOR PROTEIN-LIGAND COMPLEXATION                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 99257                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5225                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7243                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.97                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3620                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 382                          
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20694                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 33                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 77.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 91.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.07000                                             
REMARK   3    B22 (A**2) : 4.85000                                              
REMARK   3    B33 (A**2) : -2.78000                                             
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): 0.658         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.316         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.262         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.252        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21260 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 19798 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28818 ; 1.133 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 45639 ; 0.849 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2528 ; 5.946 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1047 ;33.676 ;23.352       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3585 ;13.986 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   150 ;13.949 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3052 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23857 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5091 ; 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 : NULL                                                 
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 6TRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292104682.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99989                            
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   : 104482                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.427                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.4100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.53                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.27100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.990                              
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   (%): 70.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.46 M NA CITRATE PH 6.75, VAPOR         
REMARK 280  DIFFUSION, 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      130.71950            
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      130.71950            
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       81.52250            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      122.64150            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       81.52250            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      122.64150            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      130.71950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       81.52250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      122.64150            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      130.71950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       81.52250            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      122.64150            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8810 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 65230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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      522.87800            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 64550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, E, F                            
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     GLY A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
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     GLY A   106                                                      
REMARK 465     GLU A   107                                                      
REMARK 465     ASN A   108                                                      
REMARK 465     GLN A   140                                                      
REMARK 465     ALA A   141                                                      
REMARK 465     THR A   142                                                      
REMARK 465     LEU A   143                                                      
REMARK 465     ASP A   144                                                      
REMARK 465     TYR A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     MET A   147                                                      
REMARK 465     ILE A   898                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     ALA B    -3                                                      
REMARK 465     MET B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
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     GLY B    73                                                      
REMARK 465     TYR B    74                                                      
REMARK 465     MET B    75                                                      
REMARK 465     MET B    76                                                      
REMARK 465     GLY B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     ASN B   108                                                      
REMARK 465     PHE B   139                                                      
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     ILE B   898                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     ALA C    -3                                                      
REMARK 465     MET C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
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     GLY C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     ASN C   108                                                      
REMARK 465     PHE C   139                                                      
REMARK 465     GLN C   140                                                      
REMARK 465     ALA C   141                                                      
REMARK 465     THR C   142                                                      
REMARK 465     LEU C   143                                                      
REMARK 465     ASP C   144                                                      
REMARK 465     TYR C   145                                                      
REMARK 465     GLY C   146                                                      
REMARK 465     MET C   147                                                      
REMARK 465     ILE C   898                                                      
REMARK 465     ILE D    11                                                      
REMARK 465     ALA D    12                                                      
REMARK 465     ASP D    13                                                      
REMARK 465     ASN D    14                                                      
REMARK 465     HIS D    15                                                      
REMARK 465     ILE E    11                                                      
REMARK 465     ALA E    12                                                      
REMARK 465     ASP E    13                                                      
REMARK 465     ASN E    14                                                      
REMARK 465     HIS E    15                                                      
REMARK 465     ILE F    11                                                      
REMARK 465     ALA F    12                                                      
REMARK 465     ASP F    13                                                      
REMARK 465     ASN F    14                                                      
REMARK 465     HIS F    15                                                      
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 325     -167.57   -117.85                                   
REMARK 500    PHE A 372       61.97   -108.36                                   
REMARK 500    ILE A 445      -88.36    -93.75                                   
REMARK 500    PHE A 453      102.04   -167.08                                   
REMARK 500    GLU A 462       40.39   -101.06                                   
REMARK 500    ASN A 528     -155.40   -156.11                                   
REMARK 500    SER A 546      146.82   -172.36                                   
REMARK 500    VAL A 558      -61.25   -101.24                                   
REMARK 500    PRO A 594      171.84    -52.31                                   
REMARK 500    TYR A 669      -66.48   -127.54                                   
REMARK 500    VAL A 684      -69.73    -90.81                                   
REMARK 500    TYR A 686       43.27   -106.10                                   
REMARK 500    TYR A 720       -4.39     68.91                                   
REMARK 500    SER A 755     -107.11     65.22                                   
REMARK 500    LEU A 783      105.99   -164.36                                   
REMARK 500    ASN A 802       55.34   -157.69                                   
REMARK 500    SER A 820       33.22    -96.75                                   
REMARK 500    ARG A 864     -140.45   -101.30                                   
REMARK 500    LEU A 888      -63.64   -145.46                                   
REMARK 500    SER B 233       55.86     38.45                                   
REMARK 500    ASP B 418      105.76    -52.86                                   
REMARK 500    ILE B 445      -88.29    -97.15                                   
REMARK 500    PHE B 453      114.97   -170.99                                   
REMARK 500    GLU B 518       55.42    -90.48                                   
REMARK 500    VAL B 558      -61.18    -91.76                                   
REMARK 500    ASP B 655       72.48     64.07                                   
REMARK 500    TYR B 669      -75.50   -115.99                                   
REMARK 500    TYR B 686       44.92   -102.78                                   
REMARK 500    TYR B 720       -0.46     62.78                                   
REMARK 500    SER B 755     -111.08     65.13                                   
REMARK 500    ARG B 768       57.11   -119.89                                   
REMARK 500    LEU B 783      104.68   -164.38                                   
REMARK 500    ASN B 802       56.46   -160.90                                   
REMARK 500    ARG B 864     -137.18    -98.06                                   
REMARK 500    LEU B 888      -66.64   -141.88                                   
REMARK 500    MET C  76       -4.01     96.67                                   
REMARK 500    PRO C 293       48.14    -75.64                                   
REMARK 500    SER C 294       32.76   -156.44                                   
REMARK 500    PRO C 332       88.52    -69.04                                   
REMARK 500    ILE C 445      -87.46   -105.87                                   
REMARK 500    PHE C 453      112.14   -165.24                                   
REMARK 500    SER C 494       44.61    -88.48                                   
REMARK 500    GLU C 511       76.87   -153.77                                   
REMARK 500    GLU C 518       55.27    -93.38                                   
REMARK 500    PRO C 626      118.05    -34.02                                   
REMARK 500    TYR C 669      -74.32   -118.96                                   
REMARK 500    TYR C 686       47.01   -108.30                                   
REMARK 500    ARG C 748       73.33   -113.00                                   
REMARK 500    SER C 755     -113.74     62.99                                   
REMARK 500    LEU C 783       94.44   -161.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 901  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 158   O                                                      
REMARK 620 2 GLN A 274   O    87.3                                              
REMARK 620 3 ASP A 278   OD1 135.3  90.7                                        
REMARK 620 4 TYR A 280   OH   71.4  80.1  64.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 901  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B 158   O                                                      
REMARK 620 2 GLN B 274   O    87.4                                              
REMARK 620 3 ASP B 278   OD1 154.9  86.5                                        
REMARK 620 4 TYR B 280   OH   74.0  80.1  81.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 901  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 158   O                                                      
REMARK 620 2 GLN C 274   O    94.2                                              
REMARK 620 3 ASP C 278   OD1 143.1  79.9                                        
REMARK 620 4 TYR C 280   OH   75.6  73.6  67.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 901                  
DBREF  6TRW A    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  6TRW B    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  6TRW C    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  6TRW D    1    15  PDB    6TRW     6TRW             1     15             
DBREF  6TRW E    1    15  PDB    6TRW     6TRW             1     15             
DBREF  6TRW F    1    15  PDB    6TRW     6TRW             1     15             
SEQADV 6TRW GLY A   -4  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW ALA A   -3  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW MET A   -2  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW GLY A   -1  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW SER A    0  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW GLY B   -4  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW ALA B   -3  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW MET B   -2  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW GLY B   -1  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW SER B    0  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW GLY C   -4  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW ALA C   -3  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW MET C   -2  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW GLY C   -1  UNP  Q6V1X1              EXPRESSION TAG                 
SEQADV 6TRW SER C    0  UNP  Q6V1X1              EXPRESSION TAG                 
SEQRES   1 A  903  GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET          
SEQRES   2 A  903  LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET          
SEQRES   3 A  903  GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA          
SEQRES   4 A  903  ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS          
SEQRES   5 A  903  LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN          
SEQRES   6 A  903  LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY          
SEQRES   7 A  903  TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL          
SEQRES   8 A  903  LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE          
SEQRES   9 A  903  TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR          
SEQRES  10 A  903  LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA          
SEQRES  11 A  903  ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU          
SEQRES  12 A  903  PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU          
SEQRES  13 A  903  GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL          
SEQRES  14 A  903  GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR          
SEQRES  15 A  903  PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS          
SEQRES  16 A  903  ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG          
SEQRES  17 A  903  PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET          
SEQRES  18 A  903  ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA          
SEQRES  19 A  903  PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL          
SEQRES  20 A  903  THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU          
SEQRES  21 A  903  LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL          
SEQRES  22 A  903  ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER          
SEQRES  23 A  903  GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER          
SEQRES  24 A  903  GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP          
SEQRES  25 A  903  GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET          
SEQRES  26 A  903  LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS          
SEQRES  27 A  903  THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER          
SEQRES  28 A  903  GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL          
SEQRES  29 A  903  ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE          
SEQRES  30 A  903  GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO          
SEQRES  31 A  903  GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER          
SEQRES  32 A  903  GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU          
SEQRES  33 A  903  PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG          
SEQRES  34 A  903  LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE          
SEQRES  35 A  903  ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS          
SEQRES  36 A  903  ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU          
SEQRES  37 A  903  ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE          
SEQRES  38 A  903  ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER          
SEQRES  39 A  903  LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER          
SEQRES  40 A  903  ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR          
SEQRES  41 A  903  SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN          
SEQRES  42 A  903  ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU          
SEQRES  43 A  903  GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL          
SEQRES  44 A  903  VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR          
SEQRES  45 A  903  ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS          
SEQRES  46 A  903  CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN          
SEQRES  47 A  903  PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU          
SEQRES  48 A  903  ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR          
SEQRES  49 A  903  ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO          
SEQRES  50 A  903  PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR          
SEQRES  51 A  903  LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO          
SEQRES  52 A  903  GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY          
SEQRES  53 A  903  PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL          
SEQRES  54 A  903  LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR          
SEQRES  55 A  903  VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG          
SEQRES  56 A  903  GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY          
SEQRES  57 A  903  GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR          
SEQRES  58 A  903  LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL          
SEQRES  59 A  903  GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU          
SEQRES  60 A  903  MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA          
SEQRES  61 A  903  ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP          
SEQRES  62 A  903  THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN          
SEQRES  63 A  903  ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN          
SEQRES  64 A  903  ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU          
SEQRES  65 A  903  LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS          
SEQRES  66 A  903  THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS          
SEQRES  67 A  903  PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER          
SEQRES  68 A  903  ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS          
SEQRES  69 A  903  LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE          
SEQRES  70 A  903  ALA ALA LEU LYS VAL ILE                                      
SEQRES   1 B  903  GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET          
SEQRES   2 B  903  LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET          
SEQRES   3 B  903  GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA          
SEQRES   4 B  903  ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS          
SEQRES   5 B  903  LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN          
SEQRES   6 B  903  LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY          
SEQRES   7 B  903  TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL          
SEQRES   8 B  903  LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE          
SEQRES   9 B  903  TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR          
SEQRES  10 B  903  LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA          
SEQRES  11 B  903  ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU          
SEQRES  12 B  903  PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU          
SEQRES  13 B  903  GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL          
SEQRES  14 B  903  GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR          
SEQRES  15 B  903  PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS          
SEQRES  16 B  903  ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG          
SEQRES  17 B  903  PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET          
SEQRES  18 B  903  ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA          
SEQRES  19 B  903  PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL          
SEQRES  20 B  903  THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU          
SEQRES  21 B  903  LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL          
SEQRES  22 B  903  ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER          
SEQRES  23 B  903  GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER          
SEQRES  24 B  903  GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP          
SEQRES  25 B  903  GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET          
SEQRES  26 B  903  LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS          
SEQRES  27 B  903  THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER          
SEQRES  28 B  903  GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL          
SEQRES  29 B  903  ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE          
SEQRES  30 B  903  GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO          
SEQRES  31 B  903  GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER          
SEQRES  32 B  903  GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU          
SEQRES  33 B  903  PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG          
SEQRES  34 B  903  LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE          
SEQRES  35 B  903  ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS          
SEQRES  36 B  903  ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU          
SEQRES  37 B  903  ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE          
SEQRES  38 B  903  ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER          
SEQRES  39 B  903  LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER          
SEQRES  40 B  903  ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR          
SEQRES  41 B  903  SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN          
SEQRES  42 B  903  ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU          
SEQRES  43 B  903  GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL          
SEQRES  44 B  903  VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR          
SEQRES  45 B  903  ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS          
SEQRES  46 B  903  CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN          
SEQRES  47 B  903  PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU          
SEQRES  48 B  903  ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR          
SEQRES  49 B  903  ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO          
SEQRES  50 B  903  PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR          
SEQRES  51 B  903  LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO          
SEQRES  52 B  903  GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY          
SEQRES  53 B  903  PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL          
SEQRES  54 B  903  LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR          
SEQRES  55 B  903  VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG          
SEQRES  56 B  903  GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY          
SEQRES  57 B  903  GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR          
SEQRES  58 B  903  LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL          
SEQRES  59 B  903  GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU          
SEQRES  60 B  903  MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA          
SEQRES  61 B  903  ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP          
SEQRES  62 B  903  THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN          
SEQRES  63 B  903  ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN          
SEQRES  64 B  903  ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU          
SEQRES  65 B  903  LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS          
SEQRES  66 B  903  THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS          
SEQRES  67 B  903  PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER          
SEQRES  68 B  903  ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS          
SEQRES  69 B  903  LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE          
SEQRES  70 B  903  ALA ALA LEU LYS VAL ILE                                      
SEQRES   1 C  903  GLY ALA MET GLY SER MET TRP LYS ARG SER GLU GLN MET          
SEQRES   2 C  903  LYS ILE LYS SER GLY LYS CYS ASN MET ALA ALA ALA MET          
SEQRES   3 C  903  GLU THR GLU GLN LEU GLY VAL GLU ILE PHE GLU THR ALA          
SEQRES   4 C  903  ASP CYS GLU GLU ASN ILE GLU SER GLN ASP ARG PRO LYS          
SEQRES   5 C  903  LEU GLU PRO PHE TYR VAL GLU ARG TYR SER TRP SER GLN          
SEQRES   6 C  903  LEU LYS LYS LEU LEU ALA ASP THR ARG LYS TYR HIS GLY          
SEQRES   7 C  903  TYR MET MET ALA LYS ALA PRO HIS ASP PHE MET PHE VAL          
SEQRES   8 C  903  LYS ARG ASN ASP PRO ASP GLY PRO HIS SER ASP ARG ILE          
SEQRES   9 C  903  TYR TYR LEU ALA MET SER GLY GLU ASN ARG GLU ASN THR          
SEQRES  10 C  903  LEU PHE TYR SER GLU ILE PRO LYS THR ILE ASN ARG ALA          
SEQRES  11 C  903  ALA VAL LEU MET LEU SER TRP LYS PRO LEU LEU ASP LEU          
SEQRES  12 C  903  PHE GLN ALA THR LEU ASP TYR GLY MET TYR SER ARG GLU          
SEQRES  13 C  903  GLU GLU LEU LEU ARG GLU ARG LYS ARG ILE GLY THR VAL          
SEQRES  14 C  903  GLY ILE ALA SER TYR ASP TYR HIS GLN GLY SER GLY THR          
SEQRES  15 C  903  PHE LEU PHE GLN ALA GLY SER GLY ILE TYR HIS VAL LYS          
SEQRES  16 C  903  ASP GLY GLY PRO GLN GLY PHE THR GLN GLN PRO LEU ARG          
SEQRES  17 C  903  PRO ASN LEU VAL GLU THR SER CYS PRO ASN ILE ARG MET          
SEQRES  18 C  903  ASP PRO LYS LEU CYS PRO ALA ASP PRO ASP TRP ILE ALA          
SEQRES  19 C  903  PHE ILE HIS SER ASN ASP ILE TRP ILE SER ASN ILE VAL          
SEQRES  20 C  903  THR ARG GLU GLU ARG ARG LEU THR TYR VAL HIS ASN GLU          
SEQRES  21 C  903  LEU ALA ASN MET GLU GLU ASP ALA ARG SER ALA GLY VAL          
SEQRES  22 C  903  ALA THR PHE VAL LEU GLN GLU GLU PHE ASP ARG TYR SER          
SEQRES  23 C  903  GLY TYR TRP TRP CYS PRO LYS ALA GLU THR THR PRO SER          
SEQRES  24 C  903  GLY GLY LYS ILE LEU ARG ILE LEU TYR GLU GLU ASN ASP          
SEQRES  25 C  903  GLU SER GLU VAL GLU ILE ILE HIS VAL THR SER PRO MET          
SEQRES  26 C  903  LEU GLU THR ARG ARG ALA ASP SER PHE ARG TYR PRO LYS          
SEQRES  27 C  903  THR GLY THR ALA ASN PRO LYS VAL THR PHE LYS MET SER          
SEQRES  28 C  903  GLU ILE MET ILE ASP ALA GLU GLY ARG ILE ILE ASP VAL          
SEQRES  29 C  903  ILE ASP LYS GLU LEU ILE GLN PRO PHE GLU ILE LEU PHE          
SEQRES  30 C  903  GLU GLY VAL GLU TYR ILE ALA ARG ALA GLY TRP THR PRO          
SEQRES  31 C  903  GLU GLY LYS TYR ALA TRP SER ILE LEU LEU ASP ARG SER          
SEQRES  32 C  903  GLN THR ARG LEU GLN ILE VAL LEU ILE SER PRO GLU LEU          
SEQRES  33 C  903  PHE ILE PRO VAL GLU ASP ASP VAL MET GLU ARG GLN ARG          
SEQRES  34 C  903  LEU ILE GLU SER VAL PRO ASP SER VAL THR PRO LEU ILE          
SEQRES  35 C  903  ILE TYR GLU GLU THR THR ASP ILE TRP ILE ASN ILE HIS          
SEQRES  36 C  903  ASP ILE PHE HIS VAL PHE PRO GLN SER HIS GLU GLU GLU          
SEQRES  37 C  903  ILE GLU PHE ILE PHE ALA SER GLU CYS LYS THR GLY PHE          
SEQRES  38 C  903  ARG HIS LEU TYR LYS ILE THR SER ILE LEU LYS GLU SER          
SEQRES  39 C  903  LYS TYR LYS ARG SER SER GLY GLY LEU PRO ALA PRO SER          
SEQRES  40 C  903  ASP PHE LYS CYS PRO ILE LYS GLU GLU ILE ALA ILE THR          
SEQRES  41 C  903  SER GLY GLU TRP GLU VAL LEU GLY ARG HIS GLY SER ASN          
SEQRES  42 C  903  ILE GLN VAL ASP GLU VAL ARG ARG LEU VAL TYR PHE GLU          
SEQRES  43 C  903  GLY THR LYS ASP SER PRO LEU GLU HIS HIS LEU TYR VAL          
SEQRES  44 C  903  VAL SER TYR VAL ASN PRO GLY GLU VAL THR ARG LEU THR          
SEQRES  45 C  903  ASP ARG GLY TYR SER HIS SER CYS CYS ILE SER GLN HIS          
SEQRES  46 C  903  CYS ASP PHE PHE ILE SER LYS TYR SER ASN GLN LYS ASN          
SEQRES  47 C  903  PRO HIS CYS VAL SER LEU TYR LYS LEU SER SER PRO GLU          
SEQRES  48 C  903  ASP ASP PRO THR CYS LYS THR LYS GLU PHE TRP ALA THR          
SEQRES  49 C  903  ILE LEU ASP SER ALA GLY PRO LEU PRO ASP TYR THR PRO          
SEQRES  50 C  903  PRO GLU ILE PHE SER PHE GLU SER THR THR GLY PHE THR          
SEQRES  51 C  903  LEU TYR GLY MET LEU TYR LYS PRO HIS ASP LEU GLN PRO          
SEQRES  52 C  903  GLY LYS LYS TYR PRO THR VAL LEU PHE ILE TYR GLY GLY          
SEQRES  53 C  903  PRO GLN VAL GLN LEU VAL ASN ASN ARG PHE LYS GLY VAL          
SEQRES  54 C  903  LYS TYR PHE ARG LEU ASN THR LEU ALA SER LEU GLY TYR          
SEQRES  55 C  903  VAL VAL VAL VAL ILE ASP ASN ARG GLY SER CYS HIS ARG          
SEQRES  56 C  903  GLY LEU LYS PHE GLU GLY ALA PHE LYS TYR LYS MET GLY          
SEQRES  57 C  903  GLN ILE GLU ILE ASP ASP GLN VAL GLU GLY LEU GLN TYR          
SEQRES  58 C  903  LEU ALA SER ARG TYR ASP PHE ILE ASP LEU ASP ARG VAL          
SEQRES  59 C  903  GLY ILE HIS GLY TRP SER TYR GLY GLY TYR LEU SER LEU          
SEQRES  60 C  903  MET ALA LEU MET GLN ARG SER ASP ILE PHE ARG VAL ALA          
SEQRES  61 C  903  ILE ALA GLY ALA PRO VAL THR LEU TRP ILE PHE TYR ASP          
SEQRES  62 C  903  THR GLY TYR THR GLU ARG TYR MET GLY HIS PRO ASP GLN          
SEQRES  63 C  903  ASN GLU GLN GLY TYR TYR LEU GLY SER VAL ALA MET GLN          
SEQRES  64 C  903  ALA GLU LYS PHE PRO SER GLU PRO ASN ARG LEU LEU LEU          
SEQRES  65 C  903  LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS PHE ALA HIS          
SEQRES  66 C  903  THR SER ILE LEU LEU SER PHE LEU VAL ARG ALA GLY LYS          
SEQRES  67 C  903  PRO TYR ASP LEU GLN ILE TYR PRO GLN GLU ARG HIS SER          
SEQRES  68 C  903  ILE ARG VAL PRO GLU SER GLY GLU HIS TYR GLU LEU HIS          
SEQRES  69 C  903  LEU LEU HIS TYR LEU GLN GLU ASN LEU GLY SER ARG ILE          
SEQRES  70 C  903  ALA ALA LEU LYS VAL ILE                                      
SEQRES   1 D   15  SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP          
SEQRES   2 D   15  ASN HIS                                                      
SEQRES   1 E   15  SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP          
SEQRES   2 E   15  ASN HIS                                                      
SEQRES   1 F   15  SER LEU ARG PHE LEU PHE GLU GLY GLN ARG ILE ALA ASP          
SEQRES   2 F   15  ASN HIS                                                      
HET     NA  A 901       1                                                       
HET     NA  B 901       1                                                       
HET     NA  C 901       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   7   NA    3(NA 1+)                                                     
FORMUL  10  HOH   *33(H2 O)                                                     
HELIX    1 AA1 SER A   57  LYS A   70  1                                  14    
HELIX    2 AA2 TYR A   71  GLY A   73  5                                   3    
HELIX    3 AA3 SER A  149  LYS A  159  1                                  11    
HELIX    4 AA4 THR A  270  PHE A  277  1                                   8    
HELIX    5 AA5 MET A  320  ARG A  324  5                                   5    
HELIX    6 AA6 PRO A  367  PHE A  372  1                                   6    
HELIX    7 AA7 SER A  408  GLU A  410  5                                   3    
HELIX    8 AA8 ASP A  418  VAL A  429  1                                  12    
HELIX    9 AA9 TYR A  686  LEU A  695  1                                  10    
HELIX   10 AB1 GLY A  711  GLY A  716  1                                   6    
HELIX   11 AB2 ALA A  717  LYS A  719  5                                   3    
HELIX   12 AB3 ILE A  725  TYR A  741  1                                  17    
HELIX   13 AB4 SER A  755  ARG A  768  1                                  14    
HELIX   14 AB5 ASP A  788  GLY A  797  1                                  10    
HELIX   15 AB6 HIS A  798  GLN A  801  5                                   4    
HELIX   16 AB7 ASN A  802  SER A  810  1                                   9    
HELIX   17 AB8 VAL A  811  PHE A  818  5                                   8    
HELIX   18 AB9 PHE A  838  ALA A  851  1                                  14    
HELIX   19 AC1 VAL A  869  LEU A  888  1                                  20    
HELIX   20 AC2 SER A  890  VAL A  897  1                                   8    
HELIX   21 AC3 SER B   57  TYR B   71  1                                  15    
HELIX   22 AC4 SER B  149  LYS B  159  1                                  11    
HELIX   23 AC5 THR B  270  PHE B  277  1                                   8    
HELIX   24 AC6 MET B  320  ARG B  324  5                                   5    
HELIX   25 AC7 PRO B  367  PHE B  372  1                                   6    
HELIX   26 AC8 SER B  408  GLU B  410  5                                   3    
HELIX   27 AC9 ASP B  418  VAL B  429  1                                  12    
HELIX   28 AD1 TYR B  686  LEU B  695  1                                  10    
HELIX   29 AD2 GLY B  711  GLY B  716  1                                   6    
HELIX   30 AD3 ALA B  717  LYS B  719  5                                   3    
HELIX   31 AD4 ILE B  725  TYR B  741  1                                  17    
HELIX   32 AD5 SER B  755  ARG B  768  1                                  14    
HELIX   33 AD6 LEU B  783  TYR B  787  5                                   5    
HELIX   34 AD7 ASP B  788  MET B  796  1                                   9    
HELIX   35 AD8 HIS B  798  GLN B  801  5                                   4    
HELIX   36 AD9 ASN B  802  GLY B  809  1                                   8    
HELIX   37 AE1 SER B  810  PHE B  818  5                                   9    
HELIX   38 AE2 PHE B  838  ALA B  851  1                                  14    
HELIX   39 AE3 VAL B  869  LEU B  888  1                                  20    
HELIX   40 AE4 SER B  890  VAL B  897  1                                   8    
HELIX   41 AE5 SER C   57  HIS C   72  1                                  16    
HELIX   42 AE6 SER C  149  LYS C  159  1                                  11    
HELIX   43 AE7 THR C  270  PHE C  277  1                                   8    
HELIX   44 AE8 MET C  320  ARG C  324  5                                   5    
HELIX   45 AE9 PRO C  367  PHE C  372  1                                   6    
HELIX   46 AF1 SER C  408  GLU C  410  5                                   3    
HELIX   47 AF2 ASP C  418  VAL C  429  1                                  12    
HELIX   48 AF3 LYS C  492  GLY C  496  5                                   5    
HELIX   49 AF4 ALA C  500  PHE C  504  5                                   5    
HELIX   50 AF5 TYR C  686  GLY C  696  1                                  11    
HELIX   51 AF6 GLY C  711  GLY C  716  1                                   6    
HELIX   52 AF7 ALA C  717  LYS C  719  5                                   3    
HELIX   53 AF8 ILE C  725  TYR C  741  1                                  17    
HELIX   54 AF9 SER C  755  ARG C  768  1                                  14    
HELIX   55 AG1 LEU C  783  TYR C  787  5                                   5    
HELIX   56 AG2 ASP C  788  GLY C  797  1                                  10    
HELIX   57 AG3 ASN C  802  GLY C  809  1                                   8    
HELIX   58 AG4 SER C  810  PHE C  818  5                                   9    
HELIX   59 AG5 PHE C  838  ALA C  851  1                                  14    
HELIX   60 AG6 VAL C  869  LEU C  888  1                                  20    
HELIX   61 AG7 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  PRO A 663           
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  PHE A 636   O  GLY A 648           
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  ARG A 748   N  THR A 664           
SHEET    4 AA2 6 VAL A 774  GLY A 778  1  O  GLY A 778   N  GLY A 753           
SHEET    5 AA2 6 LEU A 825  GLY A 830  1  O  LEU A 826   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  MET A 104 -1  O  LEU A 102   N  HIS A  81           
SHEET    3 AA3 4 ASN A 111  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 ARG A 215  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 3 ARG A 264  ALA A 266  0                                        
SHEET    2 AA6 3 LYS A 297  ASP A 307 -1  O  ASN A 306   N  SER A 265           
SHEET    3 AA6 3 GLU A 290  THR A 291 -1  N  GLU A 290   O  ILE A 298           
SHEET    1 AA7 5 TYR A 283  TRP A 285  0                                        
SHEET    2 AA7 5 LYS A 297  ASP A 307 -1  O  LEU A 302   N  TRP A 284           
SHEET    3 AA7 5 THR A 342  ILE A 350 -1  O  ILE A 348   N  LEU A 299           
SHEET    4 AA7 5 ILE A 356  LEU A 364 -1  O  LYS A 362   N  MET A 345           
SHEET    5 AA7 5 PHE A 412  PRO A 414 -1  O  ILE A 413   N  GLU A 363           
SHEET    1 AA8 2 ILE A 313  THR A 317  0                                        
SHEET    2 AA8 2 ALA A 326  ARG A 330 -1  O  ASP A 327   N  VAL A 316           
SHEET    1 AA9 4 VAL A 375  TRP A 383  0                                        
SHEET    2 AA9 4 ALA A 390  ASP A 396 -1  O  ILE A 393   N  ARG A 380           
SHEET    3 AA9 4 ARG A 401  ILE A 407 -1  O  GLN A 403   N  LEU A 394           
SHEET    4 AA9 4 LEU A 436  THR A 442 -1  O  LEU A 436   N  LEU A 406           
SHEET    1 AB1 4 PHE A 453  VAL A 455  0                                        
SHEET    2 AB1 4 GLU A 463  SER A 470 -1  O  ILE A 467   N  HIS A 454           
SHEET    3 AB1 4 HIS A 478  ILE A 485 -1  O  ILE A 482   N  PHE A 466           
SHEET    4 AB1 4 ILE A 508  ALA A 513 -1  O  ILE A 512   N  LYS A 481           
SHEET    1 AB2 3 VAL A 521  LEU A 522  0                                        
SHEET    2 AB2 3 LEU A 537  GLY A 542 -1  O  GLU A 541   N  LEU A 522           
SHEET    3 AB2 3 ILE A 529  ASP A 532 -1  N  GLN A 530   O  TYR A 539           
SHEET    1 AB3 4 VAL A 521  LEU A 522  0                                        
SHEET    2 AB3 4 LEU A 537  GLY A 542 -1  O  GLU A 541   N  LEU A 522           
SHEET    3 AB3 4 HIS A 551  SER A 556 -1  O  TYR A 553   N  PHE A 540           
SHEET    4 AB3 4 THR A 564  ARG A 565 -1  O  THR A 564   N  VAL A 554           
SHEET    1 AB4 4 SER A 572  ILE A 577  0                                        
SHEET    2 AB4 4 PHE A 583  SER A 589 -1  O  LYS A 587   N  SER A 574           
SHEET    3 AB4 4 CYS A 596  SER A 603 -1  O  TYR A 600   N  PHE A 584           
SHEET    4 AB4 4 THR A 613  LEU A 621 -1  O  ALA A 618   N  LEU A 599           
SHEET    1 AB5 5 GLU B  49  PRO B  50  0                                        
SHEET    2 AB5 5 LYS B 660  PHE B 667  1  O  LYS B 661   N  GLU B  49           
SHEET    3 AB5 5 VAL B 698  ILE B 702  1  O  VAL B 698   N  VAL B 665           
SHEET    4 AB5 5 THR B 645  TYR B 651 -1  N  TYR B 651   O  VAL B 699           
SHEET    5 AB5 5 GLU B 634  GLU B 639 -1  N  PHE B 636   O  GLY B 648           
SHEET    1 AB6 6 GLU B  49  PRO B  50  0                                        
SHEET    2 AB6 6 LYS B 660  PHE B 667  1  O  LYS B 661   N  GLU B  49           
SHEET    3 AB6 6 ILE B 744  TRP B 754  1  O  GLY B 750   N  LEU B 666           
SHEET    4 AB6 6 PHE B 772  GLY B 778  1  O  ARG B 773   N  VAL B 749           
SHEET    5 AB6 6 LEU B 825  GLY B 830  1  O  LEU B 826   N  ALA B 775           
SHEET    6 AB6 6 ASP B 856  TYR B 860  1  O  ASP B 856   N  LEU B 827           
SHEET    1 AB7 4 HIS B  81  LYS B  87  0                                        
SHEET    2 AB7 4 HIS B  95  MET B 104 -1  O  ARG B  98   N  VAL B  86           
SHEET    3 AB7 4 ASN B 111  PRO B 119 -1  O  PHE B 114   N  TYR B 101           
SHEET    4 AB7 4 LYS B 133  PRO B 134 -1  O  LYS B 133   N  TYR B 115           
SHEET    1 AB8 4 ASP B 170  HIS B 172  0                                        
SHEET    2 AB8 4 THR B 177  ALA B 182 -1  O  LEU B 179   N  ASP B 170           
SHEET    3 AB8 4 GLY B 185  LYS B 190 -1  O  VAL B 189   N  PHE B 178           
SHEET    4 AB8 4 ASN B 205  LEU B 206 -1  O  ASN B 205   N  HIS B 188           
SHEET    1 AB9 4 ARG B 215  LEU B 220  0                                        
SHEET    2 AB9 4 TRP B 227  HIS B 232 -1  O  ILE B 231   N  MET B 216           
SHEET    3 AB9 4 ASP B 235  ASN B 240 -1  O  TRP B 237   N  PHE B 230           
SHEET    4 AB9 4 GLU B 246  ARG B 248 -1  O  ARG B 247   N  ILE B 238           
SHEET    1 AC1 3 ARG B 264  ALA B 266  0                                        
SHEET    2 AC1 3 LYS B 297  ASP B 307 -1  O  ASN B 306   N  SER B 265           
SHEET    3 AC1 3 GLU B 290  THR B 291 -1  N  GLU B 290   O  ILE B 298           
SHEET    1 AC2 5 TYR B 283  TRP B 285  0                                        
SHEET    2 AC2 5 LYS B 297  ASP B 307 -1  O  LEU B 302   N  TRP B 284           
SHEET    3 AC2 5 LYS B 340  ILE B 350 -1  O  ILE B 350   N  LYS B 297           
SHEET    4 AC2 5 ILE B 356  LEU B 364 -1  O  LYS B 362   N  MET B 345           
SHEET    5 AC2 5 PHE B 412  PRO B 414 -1  O  ILE B 413   N  GLU B 363           
SHEET    1 AC3 2 ILE B 313  THR B 317  0                                        
SHEET    2 AC3 2 ALA B 326  ARG B 330 -1  O  ASP B 327   N  VAL B 316           
SHEET    1 AC4 4 VAL B 375  TRP B 383  0                                        
SHEET    2 AC4 4 ALA B 390  ASP B 396 -1  O  LEU B 395   N  GLU B 376           
SHEET    3 AC4 4 ARG B 401  ILE B 407 -1  O  ILE B 407   N  ALA B 390           
SHEET    4 AC4 4 LEU B 436  THR B 442 -1  O  LEU B 436   N  LEU B 406           
SHEET    1 AC5 4 PHE B 453  VAL B 455  0                                        
SHEET    2 AC5 4 GLU B 463  SER B 470 -1  O  ILE B 467   N  HIS B 454           
SHEET    3 AC5 4 HIS B 478  ILE B 485 -1  O  ILE B 482   N  PHE B 466           
SHEET    4 AC5 4 ILE B 508  ALA B 513 -1  O  ILE B 512   N  LYS B 481           
SHEET    1 AC6 4 GLN B 530  ASP B 532  0                                        
SHEET    2 AC6 4 LEU B 537  SER B 546 -1  O  TYR B 539   N  GLN B 530           
SHEET    3 AC6 4 GLU B 549  SER B 556 -1  O  TYR B 553   N  PHE B 540           
SHEET    4 AC6 4 THR B 564  ARG B 565 -1  O  THR B 564   N  VAL B 554           
SHEET    1 AC7 4 SER B 572  ILE B 577  0                                        
SHEET    2 AC7 4 PHE B 583  SER B 589 -1  O  LYS B 587   N  SER B 574           
SHEET    3 AC7 4 CYS B 596  SER B 603 -1  O  TYR B 600   N  PHE B 584           
SHEET    4 AC7 4 THR B 613  LEU B 621 -1  O  ALA B 618   N  LEU B 599           
SHEET    1 AC8 5 GLU C  49  PRO C  50  0                                        
SHEET    2 AC8 5 LYS C 660  PHE C 667  1  O  LYS C 661   N  GLU C  49           
SHEET    3 AC8 5 VAL C 698  ILE C 702  1  O  VAL C 698   N  PRO C 663           
SHEET    4 AC8 5 THR C 645  TYR C 651 -1  N  TYR C 651   O  VAL C 699           
SHEET    5 AC8 5 GLU C 634  GLU C 639 -1  N  PHE C 638   O  LEU C 646           
SHEET    1 AC9 6 GLU C  49  PRO C  50  0                                        
SHEET    2 AC9 6 LYS C 660  PHE C 667  1  O  LYS C 661   N  GLU C  49           
SHEET    3 AC9 6 ILE C 744  TRP C 754  1  O  GLY C 750   N  THR C 664           
SHEET    4 AC9 6 PHE C 772  GLY C 778  1  O  ILE C 776   N  ILE C 751           
SHEET    5 AC9 6 LEU C 825  GLY C 830  1  O  LEU C 828   N  ALA C 777           
SHEET    6 AC9 6 ASP C 856  TYR C 860  1  O  ASP C 856   N  LEU C 827           
SHEET    1 AD1 4 HIS C  81  LYS C  87  0                                        
SHEET    2 AD1 4 HIS C  95  MET C 104 -1  O  ARG C  98   N  VAL C  86           
SHEET    3 AD1 4 ASN C 111  PRO C 119 -1  O  PHE C 114   N  TYR C 101           
SHEET    4 AD1 4 LYS C 133  PRO C 134 -1  O  LYS C 133   N  TYR C 115           
SHEET    1 AD2 4 ASP C 170  TYR C 171  0                                        
SHEET    2 AD2 4 THR C 177  ALA C 182 -1  O  LEU C 179   N  ASP C 170           
SHEET    3 AD2 4 GLY C 185  LYS C 190 -1  O  VAL C 189   N  PHE C 178           
SHEET    4 AD2 4 ASN C 205  LEU C 206 -1  O  ASN C 205   N  HIS C 188           
SHEET    1 AD3 4 MET C 216  LEU C 220  0                                        
SHEET    2 AD3 4 TRP C 227  ILE C 231 -1  O  ILE C 231   N  MET C 216           
SHEET    3 AD3 4 ILE C 236  ASN C 240 -1  O  TRP C 237   N  PHE C 230           
SHEET    4 AD3 4 GLU C 246  ARG C 248 -1  O  ARG C 247   N  ILE C 238           
SHEET    1 AD4 3 ARG C 264  ALA C 266  0                                        
SHEET    2 AD4 3 LYS C 297  ASP C 307 -1  O  ASN C 306   N  SER C 265           
SHEET    3 AD4 3 TYR C 283  TRP C 285 -1  N  TRP C 284   O  LEU C 302           
SHEET    1 AD5 5 ARG C 264  ALA C 266  0                                        
SHEET    2 AD5 5 LYS C 297  ASP C 307 -1  O  ASN C 306   N  SER C 265           
SHEET    3 AD5 5 LYS C 340  ILE C 350 -1  O  ILE C 348   N  LEU C 299           
SHEET    4 AD5 5 ILE C 356  LEU C 364 -1  O  LYS C 362   N  MET C 345           
SHEET    5 AD5 5 PHE C 412  PRO C 414 -1  O  ILE C 413   N  GLU C 363           
SHEET    1 AD6 2 ILE C 313  THR C 317  0                                        
SHEET    2 AD6 2 ALA C 326  ARG C 330 -1  O  ASP C 327   N  VAL C 316           
SHEET    1 AD7 4 VAL C 375  TRP C 383  0                                        
SHEET    2 AD7 4 ALA C 390  ASP C 396 -1  O  LEU C 395   N  TYR C 377           
SHEET    3 AD7 4 ARG C 401  ILE C 407 -1  O  ILE C 407   N  ALA C 390           
SHEET    4 AD7 4 LEU C 436  THR C 442 -1  O  LEU C 436   N  LEU C 406           
SHEET    1 AD8 4 PHE C 453  VAL C 455  0                                        
SHEET    2 AD8 4 GLU C 463  SER C 470 -1  O  ILE C 467   N  HIS C 454           
SHEET    3 AD8 4 HIS C 478  ILE C 485 -1  O  ILE C 482   N  PHE C 466           
SHEET    4 AD8 4 ILE C 508  ALA C 513 -1  O  ILE C 512   N  LYS C 481           
SHEET    1 AD9 4 ILE C 529  ASP C 532  0                                        
SHEET    2 AD9 4 LEU C 537  GLY C 542 -1  O  TYR C 539   N  GLN C 530           
SHEET    3 AD9 4 HIS C 551  SER C 556 -1  O  TYR C 553   N  PHE C 540           
SHEET    4 AD9 4 THR C 564  ARG C 565 -1  O  THR C 564   N  VAL C 554           
SHEET    1 AE1 4 SER C 572  ILE C 577  0                                        
SHEET    2 AE1 4 PHE C 583  SER C 589 -1  O  LYS C 587   N  SER C 574           
SHEET    3 AE1 4 CYS C 596  SER C 603 -1  O  TYR C 600   N  PHE C 584           
SHEET    4 AE1 4 THR C 613  LEU C 621 -1  O  ALA C 618   N  LEU C 599           
LINK         O   ARG A 158                NA    NA A 901     1555   1555  2.63  
LINK         O   GLN A 274                NA    NA A 901     1555   1555  2.92  
LINK         OD1 ASP A 278                NA    NA A 901     1555   1555  2.69  
LINK         OH  TYR A 280                NA    NA A 901     1555   1555  2.99  
LINK         O   ARG B 158                NA    NA B 901     1555   1555  2.56  
LINK         O   GLN B 274                NA    NA B 901     1555   1555  2.88  
LINK         OD1 ASP B 278                NA    NA B 901     1555   1555  2.81  
LINK         OH  TYR B 280                NA    NA B 901     1555   1555  2.76  
LINK         O   ARG C 158                NA    NA C 901     1555   1555  2.53  
LINK         O   GLN C 274                NA    NA C 901     1555   1555  3.07  
LINK         OD1 ASP C 278                NA    NA C 901     1555   1555  2.71  
LINK         OH  TYR C 280                NA    NA C 901     1555   1555  2.84  
SITE     1 AC1  5 ARG A 158  GLN A 274  GLU A 275  ASP A 278                    
SITE     2 AC1  5 TYR A 280                                                     
SITE     1 AC2  5 ARG B 158  GLN B 274  GLU B 275  ASP B 278                    
SITE     2 AC2  5 TYR B 280                                                     
SITE     1 AC3  5 ARG C 158  GLN C 274  GLU C 275  ASP C 278                    
SITE     2 AC3  5 TYR C 280                                                     
CRYST1  163.045  245.283  261.439  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      0.006133  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004077  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003825        0.00000                         
TER    6829      VAL A 897                                                      
TER   13615      VAL B 897                                                      
TER   20433      VAL C 897                                                      
TER   20522      ARG D  10                                                      
TER   20611      ARG E  10                                                      
TER   20700      ARG F  10                                                      
MASTER      603    0    3   61  150    0    6    620730    6   15  216          
END                                                                             

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