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LongText Report for: 6hp8-pdb

Name Class
6hp8-pdb
HEADER    HYDROLASE                               19-SEP-18   6HP8              
TITLE     CRYSTAL STRUCTURE OF DPP8 IN COMPLEX WITH VAL-BOROPRO                 
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    VAL-BOROPRO, DPP8, PROTEASE, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.H.ROSS,R.HUBER                                                      
REVDAT   1   31-JUL-19 6HP8    0                                                
JRNL        AUTH   B.H.ROSS                                                     
JRNL        TITL   IMPROVEMENT OF PROTEIN CRYSTAL DIFFRACTION USING             
JRNL        TITL 2 POST-CRYSTALLIZATION METHODS: INFRARED LASER RADIATION       
JRNL        TITL 3 CONTROLS CRYSTAL ORDER                                       
JRNL        REF    THESIS                                     2019              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 7.0                                           
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 170840                         
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8992                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12436                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.32                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 655                          
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20379                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 138                                     
REMARK   3   SOLVENT ATOMS            : 715                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.58                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.62000                                             
REMARK   3    B22 (A**2) : 1.12000                                              
REMARK   3    B33 (A**2) : -0.49000                                             
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): 0.258         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.205         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.165         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.978         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21095 ; 0.002 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A): 19187 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 28598 ; 0.916 ; 1.649       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44563 ; 0.261 ; 1.576       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2505 ; 6.496 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1174 ;30.022 ;21.814       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3530 ;14.195 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   144 ;15.584 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2664 ; 0.037 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23437 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4655 ; 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): 10038 ; 1.388 ; 5.189       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 10037 ; 1.388 ; 5.189       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12537 ; 2.492 ; 7.777       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 12538 ; 2.492 ; 7.777       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11056 ; 1.159 ; 5.287       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 11057 ; 1.159 ; 5.287       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 16062 ; 2.085 ; 7.870       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 22590 ; 4.086 ;57.210       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 22591 ; 4.086 ;57.212       
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                                                           
REMARK   4                                                                      
REMARK   4 6HP8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011967.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-DEC-17                          
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) : 0.99992                            
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   : 179844                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.6400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.46 M NA-CITRATE, PH 6.75,              
REMARK 280  EVAPORATION, TEMPERATURE 293K                                       
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      130.79400            
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      130.79400            
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       81.58150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      122.65850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       81.58150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      122.65850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      130.79400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       81.58150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      122.65850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      130.79400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       81.58150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      122.65850            
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: 8050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 65080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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      490.63400            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      523.17600            
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: 8070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 64550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1179  LIES ON A SPECIAL POSITION.                          
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     TYR A    71                                                      
REMARK 465     HIS A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     TYR A    74                                                      
REMARK 465     MET A    75                                                      
REMARK 465     MET A    76                                                      
REMARK 465     PHE A   139                                                      
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     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     TYR B    71                                                      
REMARK 465     HIS B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     TYR B    74                                                      
REMARK 465     MET B    75                                                      
REMARK 465     MET B    76                                                      
REMARK 465     LEU B   138                                                      
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     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     TYR C    71                                                      
REMARK 465     HIS C    72                                                      
REMARK 465     GLY C    73                                                      
REMARK 465     TYR C    74                                                      
REMARK 465     MET C    75                                                      
REMARK 465     MET C    76                                                      
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 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    ASP A 418      105.62    -55.84                                   
REMARK 500    ILE A 445      -86.74   -105.20                                   
REMARK 500    PHE A 453      108.95   -166.34                                   
REMARK 500    GLU A 462       47.58   -106.33                                   
REMARK 500    VAL A 558      -63.83    -93.32                                   
REMARK 500    ASN A 559       74.73   -118.87                                   
REMARK 500    PRO A 594      170.28    -58.21                                   
REMARK 500    VAL A 684      -76.06    -98.67                                   
REMARK 500    TYR A 720       -8.14     73.10                                   
REMARK 500    LYS A 721       46.57   -140.10                                   
REMARK 500    SER A 755     -121.17     64.56                                   
REMARK 500    ALA A 779       57.39     37.45                                   
REMARK 500    ASN A 802       56.16   -156.90                                   
REMARK 500    SER A 820       46.82    -88.00                                   
REMARK 500    ASN A 835      -74.09    -90.83                                   
REMARK 500    ARG A 864     -130.17    -95.88                                   
REMARK 500    LEU A 888      -57.06   -142.48                                   
REMARK 500    SER B 294      -18.67    178.29                                   
REMARK 500    ILE B 445      -87.83   -102.29                                   
REMARK 500    PHE B 453      114.21   -162.18                                   
REMARK 500    VAL B 558      -65.16    -92.90                                   
REMARK 500    ASN B 559       77.86   -115.71                                   
REMARK 500    PRO B 626      117.91    -35.48                                   
REMARK 500    VAL B 684      -74.89    -94.34                                   
REMARK 500    TYR B 720       -2.30     71.46                                   
REMARK 500    SER B 755     -116.14     62.17                                   
REMARK 500    ASN B 802       57.82   -159.20                                   
REMARK 500    ASN B 835      -71.94    -96.49                                   
REMARK 500    ARG B 864     -127.52    -95.38                                   
REMARK 500    LEU B 888      -51.51   -147.37                                   
REMARK 500    ASP C 224      101.57   -160.61                                   
REMARK 500    ILE C 445      -84.75   -105.37                                   
REMARK 500    PHE C 453      113.42   -161.43                                   
REMARK 500    VAL C 558      -65.06    -95.40                                   
REMARK 500    ASN C 559       79.44   -117.01                                   
REMARK 500    ASP C 655       61.51     64.59                                   
REMARK 500    TYR C 669      -72.34   -111.44                                   
REMARK 500    VAL C 684      -78.94   -103.77                                   
REMARK 500    TYR C 720       -5.61     74.63                                   
REMARK 500    SER C 755     -118.22     63.17                                   
REMARK 500    ASN C 802       55.30   -158.60                                   
REMARK 500    SER C 820       33.62    -93.15                                   
REMARK 500    ASN C 835      -68.49    -90.76                                   
REMARK 500    ARG C 864     -132.58    -97.43                                   
REMARK 500    LEU C 888      -57.62   -147.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     GOL A   906                                                      
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 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 158   O                                                      
REMARK 620 2 GLN A 274   O    96.4                                              
REMARK 620 3 ASP A 278   OD1 140.0  89.6                                        
REMARK 620 4 TYR A 280   OH   75.0  79.8  67.3                                  
REMARK 620 5 HOH A1234   O    89.2 148.2  67.1  71.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG B 158   O                                                      
REMARK 620 2 GLN B 274   O   102.1                                              
REMARK 620 3 ASP B 278   OD1 150.2  97.5                                        
REMARK 620 4 TYR B 280   OH   82.6  91.2  74.7                                  
REMARK 620 5 HOH B1131   O    93.7 110.9 100.0 157.8                            
REMARK 620 6 HOH B1192   O    80.7 158.1  72.9  67.4  90.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 902  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 158   O                                                      
REMARK 620 2 GLN C 274   O    98.5                                              
REMARK 620 3 ASP C 278   OD1 154.7  94.3                                        
REMARK 620 4 TYR C 280   OH   83.4  91.1  74.6                                  
REMARK 620 5 HOH C1007   O    93.3 100.0 105.9 168.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GK2 A 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GK2 B 901 and SER B    
REMARK 800  755                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GK2 C 901 and SER C    
REMARK 800  755                                                                 
DBREF  6HP8 A    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  6HP8 B    1   898  UNP    Q6V1X1   DPP8_HUMAN       1    898             
DBREF  6HP8 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    GK2  A 901      15                                                       
HET     NA  A 902       1                                                       
HET    GOL  A 903       6                                                       
HET    GOL  A 904       6                                                       
HET    GOL  A 905       6                                                       
HET    GOL  A 906       6                                                       
HET    GOL  A 907       6                                                       
HET    GK2  B 901      15                                                       
HET     NA  B 902       1                                                       
HET    GOL  B 903       6                                                       
HET    GOL  B 904       6                                                       
HET    GOL  B 905       6                                                       
HET    GOL  B 906       6                                                       
HET    GOL  B 907       6                                                       
HET    GK2  C 901      15                                                       
HET     NA  C 902       1                                                       
HET    GOL  C 903       6                                                       
HET    GOL  C 904       6                                                       
HET    GOL  C 905       6                                                       
HET    GOL  C 906       6                                                       
HET    GOL  C 907       6                                                       
HETNAM     GK2 [(2~{R})-1-[(2~{R})-2-AZANYL-3-METHYL-                           
HETNAM   2 GK2  BUTANOYL]PYRROLIDIN-2-YL]BORONIC ACID                           
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  GK2    3(C9 H19 B N2 O3)                                            
FORMUL   5   NA    3(NA 1+)                                                     
FORMUL   6  GOL    15(C3 H8 O3)                                                 
FORMUL  25  HOH   *715(H2 O)                                                    
HELIX    1 AA1 SER A   57  LYS A   70  1                                  14    
HELIX    2 AA2 SER A  149  ARG A  160  1                                  12    
HELIX    3 AA3 THR A  270  PHE A  277  1                                   8    
HELIX    4 AA4 MET A  320  ARG A  324  5                                   5    
HELIX    5 AA5 PRO A  367  PHE A  372  1                                   6    
HELIX    6 AA6 SER A  408  GLU A  410  5                                   3    
HELIX    7 AA7 ASP A  418  SER A  428  1                                  11    
HELIX    8 AA8 LYS A  492  GLY A  496  5                                   5    
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 LEU A  783  TYR A  787  5                                   5    
HELIX   15 AB6 ASP A  788  GLY A  797  1                                  10    
HELIX   16 AB7 HIS A  798  GLN A  801  5                                   4    
HELIX   17 AB8 ASN A  802  SER A  810  1                                   9    
HELIX   18 AB9 VAL A  811  PHE A  818  5                                   8    
HELIX   19 AC1 PHE A  838  ALA A  851  1                                  14    
HELIX   20 AC2 VAL A  869  LEU A  888  1                                  20    
HELIX   21 AC3 SER A  890  VAL A  897  1                                   8    
HELIX   22 AC4 SER B   57  LYS B   70  1                                  14    
HELIX   23 AC5 SER B  149  ARG B  160  1                                  12    
HELIX   24 AC6 THR B  270  PHE B  277  1                                   8    
HELIX   25 AC7 MET B  320  ARG B  324  5                                   5    
HELIX   26 AC8 PRO B  367  PHE B  372  1                                   6    
HELIX   27 AC9 SER B  408  GLU B  410  5                                   3    
HELIX   28 AD1 ASP B  418  SER B  428  1                                  11    
HELIX   29 AD2 LYS B  492  GLY B  496  5                                   5    
HELIX   30 AD3 TYR B  686  LEU B  695  1                                  10    
HELIX   31 AD4 GLY B  711  GLY B  716  1                                   6    
HELIX   32 AD5 ALA B  717  LYS B  719  5                                   3    
HELIX   33 AD6 ILE B  725  TYR B  741  1                                  17    
HELIX   34 AD7 SER B  755  ARG B  768  1                                  14    
HELIX   35 AD8 LEU B  783  TYR B  787  5                                   5    
HELIX   36 AD9 ASP B  788  GLY B  797  1                                  10    
HELIX   37 AE1 HIS B  798  GLN B  801  5                                   4    
HELIX   38 AE2 ASN B  802  GLY B  809  1                                   8    
HELIX   39 AE3 SER B  810  PHE B  818  5                                   9    
HELIX   40 AE4 PHE B  838  ALA B  851  1                                  14    
HELIX   41 AE5 VAL B  869  LEU B  888  1                                  20    
HELIX   42 AE6 SER B  890  VAL B  897  1                                   8    
HELIX   43 AE7 SER C   57  LYS C   70  1                                  14    
HELIX   44 AE8 SER C  149  ARG C  160  1                                  12    
HELIX   45 AE9 THR C  270  PHE C  277  1                                   8    
HELIX   46 AF1 MET C  320  ARG C  324  5                                   5    
HELIX   47 AF2 PRO C  367  PHE C  372  1                                   6    
HELIX   48 AF3 SER C  408  GLU C  410  5                                   3    
HELIX   49 AF4 ASP C  418  VAL C  429  1                                  12    
HELIX   50 AF5 LYS C  492  GLY C  496  5                                   5    
HELIX   51 AF6 TYR C  686  LEU C  695  1                                  10    
HELIX   52 AF7 GLY C  711  GLY C  716  1                                   6    
HELIX   53 AF8 ALA C  717  LYS C  719  5                                   3    
HELIX   54 AF9 ILE C  725  TYR C  741  1                                  17    
HELIX   55 AG1 SER C  755  ARG C  768  1                                  14    
HELIX   56 AG2 LEU C  783  TYR C  787  5                                   5    
HELIX   57 AG3 ASP C  788  GLY C  797  1                                  10    
HELIX   58 AG4 HIS C  798  GLN C  801  5                                   4    
HELIX   59 AG5 ASN C  802  GLY C  809  1                                   8    
HELIX   60 AG6 SER C  810  PHE C  818  5                                   9    
HELIX   61 AG7 PHE C  838  ALA C  851  1                                  14    
HELIX   62 AG8 VAL C  869  LEU C  888  1                                  20    
HELIX   63 AG9 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  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  GLY A 750   N  LEU A 666           
SHEET    4 AA2 6 VAL A 774  GLY A 778  1  O  ILE A 776   N  ILE A 751           
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  GLN A 858   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  ARG A  98   N  VAL A  86           
SHEET    3 AA3 4 ASN A 111  PRO A 119 -1  O  ILE A 118   N  ASP A  97           
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  HIS A 172  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  CYS A 221  0                                        
SHEET    2 AA5 4 ASP A 224  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 LYS A 340  ILE A 350 -1  O  ILE A 348   N  LEU A 299           
SHEET    4 AA7 5 ILE A 356  LEU A 364 -1  O  ILE A 357   N  MET A 349           
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  LEU A 395   N  TYR A 377           
SHEET    3 AA9 4 ARG A 401  ILE A 407 -1  O  ILE A 407   N  ALA A 390           
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 GLN A 530  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  ILE A 585   N  CYS A 576           
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  GLU B 634   O  LEU B 650           
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  THR B 664           
SHEET    4 AB6 6 VAL B 774  GLY B 778  1  O  ILE B 776   N  ILE B 751           
SHEET    5 AB6 6 LEU B 825  GLY B 830  1  O  LEU B 828   N  ALA B 777           
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  ALA B 103 -1  O  ARG B  98   N  VAL B  86           
SHEET    3 AB7 4 THR B 112  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  TYR B 171  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  CYS B 221  0                                        
SHEET    2 AB9 4 ASP B 224  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 348   N  LEU B 299           
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  TRP B 391   N  GLY B 382           
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 ILE B 529  ASP B 532  0                                        
SHEET    2 AC6 4 LEU B 537  GLY B 542 -1  O  TYR B 539   N  GLN B 530           
SHEET    3 AC6 4 HIS B 551  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  CYS B 596   N  TYR B 588           
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  VAL C 665           
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 636   O  GLY C 648           
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  LEU C 666           
SHEET    4 AC9 6 VAL C 774  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  GLN C 858   N  LEU C 827           
SHEET    1 AD1 4 HIS C  81  LYS C  87  0                                        
SHEET    2 AD1 4 HIS C  95  ALA C 103 -1  O  ARG C  98   N  VAL C  86           
SHEET    3 AD1 4 THR C 112  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  HIS C 172  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 ARG C 215  CYS C 221  0                                        
SHEET    2 AD3 4 ASP C 224  HIS C 232 -1  O  ILE C 231   N  MET C 216           
SHEET    3 AD3 4 ASP C 235  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 GLU C 290  THR C 291 -1  N  GLU C 290   O  ILE C 298           
SHEET    1 AD5 5 TYR C 283  TRP C 285  0                                        
SHEET    2 AD5 5 LYS C 297  ASP C 307 -1  O  LEU C 302   N  TRP C 284           
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  ILE C 360   N  GLU C 347           
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  ILE C 393   N  ARG C 380           
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 GLN C 530  ASP C 532  0                                        
SHEET    2 AD9 4 LEU C 537  SER C 546 -1  O  TYR C 539   N  GLN C 530           
SHEET    3 AD9 4 GLU C 549  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  ASN C 590 -1  O  LYS C 587   N  SER C 574           
SHEET    3 AE1 4 ASN C 593  SER C 603 -1  O  CYS C 596   N  TYR C 588           
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 902     1555   1555  2.46  
LINK         O   GLN A 274                NA    NA A 902     1555   1555  2.78  
LINK         OD1 ASP A 278                NA    NA A 902     1555   1555  2.48  
LINK         OH  TYR A 280                NA    NA A 902     1555   1555  2.86  
LINK         OG  SER A 755                 B15 GK2 A 901     1555   1555  1.43  
LINK         O   ARG B 158                NA    NA B 902     1555   1555  2.40  
LINK         O   GLN B 274                NA    NA B 902     1555   1555  2.60  
LINK         OD1 ASP B 278                NA    NA B 902     1555   1555  2.38  
LINK         OH  TYR B 280                NA    NA B 902     1555   1555  2.56  
LINK         OG  SER B 755                 B15 GK2 B 901     1555   1555  1.44  
LINK         O   ARG C 158                NA    NA C 902     1555   1555  2.32  
LINK         O   GLN C 274                NA    NA C 902     1555   1555  2.64  
LINK         OD1 ASP C 278                NA    NA C 902     1555   1555  2.32  
LINK         OH  TYR C 280                NA    NA C 902     1555   1555  2.71  
LINK         OG  SER C 755                 B15 GK2 C 901     1555   1555  1.43  
LINK        NA    NA A 902                 O   HOH A1234     1555   1555  3.15  
LINK        NA    NA B 902                 O   HOH B1131     1555   1555  2.43  
LINK        NA    NA B 902                 O   HOH B1192     1555   1555  3.13  
LINK        NA    NA C 902                 O   HOH C1007     1555   1555  2.33  
SITE     1 AC1 11 ARG A 160  GLU A 275  GLU A 276  TYR A 669                    
SITE     2 AC1 11 GLN A 673  SER A 755  TYR A 756  TYR A 787                    
SITE     3 AC1 11 TYR A 791  ASN A 835  HIS A 865                               
SITE     1 AC2  5 ARG A 158  GLN A 274  GLU A 275  ASP A 278                    
SITE     2 AC2  5 TYR A 280                                                     
SITE     1 AC3  7 HIS A 315  THR A 317  ARG A 324  ALA A 326                    
SITE     2 AC3  7 PHE A 831  HIS A 837  HOH A1083                               
SITE     1 AC4  5 HIS A 188  LEU A 206  GLU A 208  ILE A 241                    
SITE     2 AC4  5 HOH A1003                                                     
SITE     1 AC5  9 GLY A 526  SER A 527  ASN A 528  ILE A 529                    
SITE     2 AC5  9 GLN A 530  GLU A 541  CYS A 575  ILE A 577                    
SITE     3 AC5  9 HOH A1014                                                     
SITE     1 AC6  7 ASN A 448  HIS A 525  GLN A 673  HOH A1031                    
SITE     2 AC6  7 HOH A1102  HOH A1166  HOH A1201                               
SITE     1 AC7  6 TRP A 383  THR A 384  PRO A 385  TRP A 391                    
SITE     2 AC7  6 PHE A 453  VAL A 455                                          
SITE     1 AC8  5 ARG B 158  GLN B 274  ASP B 278  TYR B 280                    
SITE     2 AC8  5 HOH B1131                                                     
SITE     1 AC9  6 THR B 317  ARG B 324  ARG B 325  HIS C 315                    
SITE     2 AC9  6 HIS C 837  GOL C 903                                          
SITE     1 AD1  6 HOH A1011  HIS B 188  LEU B 206  GLU B 208                    
SITE     2 AD1  6 ILE B 241  ARG B 244                                          
SITE     1 AD2  6 TRP B 383  TRP B 391  PHE B 453  HIS B 454                    
SITE     2 AD2  6 VAL B 455  HOH B1002                                          
SITE     1 AD3  7 ASN B 448  ILE B 449  ARG B 524  GLN B 673                    
SITE     2 AD3  7 ARG B 794  HOH B1025  HOH B1051                               
SITE     1 AD4  8 GLY B 526  SER B 527  ASN B 528  GLN B 530                    
SITE     2 AD4  8 GLU B 541  CYS B 575  ILE B 577  HOH B1174                    
SITE     1 AD5  5 ARG C 158  GLN C 274  ASP C 278  TYR C 280                    
SITE     2 AD5  5 HOH C1007                                                     
SITE     1 AD6  8 HIS B 315  HIS B 837  GOL B 903  HOH B1115                    
SITE     2 AD6  8 THR C 317  ARG C 324  ALA C 326  PHE C 831                    
SITE     1 AD7  5 TRP C 383  TRP C 391  PHE C 453  HIS C 454                    
SITE     2 AD7  5 VAL C 455                                                     
SITE     1 AD8 10 ASN C 448  ARG C 524  HIS C 525  GLN C 673                    
SITE     2 AD8 10 ARG C 794  HOH C1004  HOH C1030  HOH C1067                    
SITE     3 AD8 10 HOH C1123  HOH C1166                                          
SITE     1 AD9  6 GLY C 526  SER C 527  ASN C 528  GLU C 541                    
SITE     2 AD9  6 CYS C 575  ILE C 577                                          
SITE     1 AE1  2 HIS C 595  LYS C 682                                          
SITE     1 AE2 17 ARG B 160  GLU B 275  GLU B 276  TYR B 669                    
SITE     2 AE2 17 GLN B 673  TRP B 754  TYR B 756  GLY B 757                    
SITE     3 AE2 17 GLY B 758  TYR B 759  GLY B 778  ALA B 779                    
SITE     4 AE2 17 PRO B 780  TYR B 787  TYR B 791  ASN B 835                    
SITE     5 AE2 17 HIS B 865                                                     
SITE     1 AE3 17 ARG C 160  GLU C 275  GLU C 276  TYR C 669                    
SITE     2 AE3 17 GLN C 673  TRP C 754  TYR C 756  GLY C 757                    
SITE     3 AE3 17 GLY C 758  TYR C 759  GLY C 778  ALA C 779                    
SITE     4 AE3 17 TYR C 787  TYR C 791  ASN C 835  HIS C 865                    
SITE     5 AE3 17 HOH C1150                                                     
CRYST1  163.163  245.317  261.588  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      0.006129  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004076  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003823        0.00000                         
TER    6804      ILE A 898                                                      
TER   13600      ILE B 898                                                      
TER   20415      ILE C 898                                                      
MASTER      663    0   21   63  150    0   50    621232    3  160  210          
END                                                                             

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