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LongText Report for: 5yp3-pdb

Name Class
5yp3-pdb
HEADER    HYDROLASE                               01-NOV-17   5YP3              
TITLE     CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP IV) WITH ILE-PRO    
TITLE    2 FROM PSEUDOXANTHOMONAS MEXICANA                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE 4;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV,DAP IV;                        
COMPND   5 EC: 3.4.14.5;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOXANTHOMONAS MEXICANA;                     
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS SP. WO24;                               
SOURCE   4 ORGANISM_TAXID: 128785;                                              
SOURCE   5 STRAIN: WO24;                                                        
SOURCE   6 GENE: DAP4;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PUC19                                     
KEYWDS    DAP IV, CLAN SC S9, PEPTIDASE, DPP4, DPP8, DPP9, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUIMOTO,S.MORISAWA,I.IIZUKA,          
AUTHOR   2 A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,Y.SAKAMOTO,T.NONAKA  
REVDAT   1   21-FEB-18 5YP3    0                                                
JRNL        AUTH   S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUJIMOTO,S.MORISAWA,         
JRNL        AUTH 2 I.IIZUKA,A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,    
JRNL        AUTH 3 Y.SAKAMOTO,T.NONAKA                                          
JRNL        TITL   CRYSTAL STRUCTURES OF A BACTERIAL DIPEPTIDYL PEPTIDASE IV    
JRNL        TITL 2 REVEAL A NOVEL SUBSTRATE RECOGNITION MECHANISM DISTINCT FROM 
JRNL        TITL 3 THAT OF MAMMALIAN ORTHOLOGUES.                               
JRNL        REF    SCI REP                       V.   8  2714 2018              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29426867                                                     
JRNL        DOI    10.1038/S41598-018-21056-Y                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 130819                         
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) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6835                            
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) : 2.44                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8212                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 399                          
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22640                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 452                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.14000                                             
REMARK   3    B22 (A**2) : 1.86000                                              
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.465         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.302         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.246         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.689        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 23265 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 21282 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 31645 ; 1.772 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 49162 ; 1.065 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2892 ; 8.032 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1088 ;32.745 ;23.051       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3664 ;17.379 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   204 ;17.650 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3433 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 26284 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  5056 ; 0.002 ; 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): 11592 ; 3.139 ; 4.377       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 11592 ; 3.139 ; 4.377       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14476 ; 4.761 ; 6.559       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 14477 ; 4.761 ; 6.559       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11673 ; 2.717 ; 4.462       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 11673 ; 2.717 ; 4.462       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 17170 ; 4.106 ; 6.632       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 26007 ; 6.572 ;49.843       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 26003 ; 6.574 ;49.844       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5YP3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005661.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9788                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2 0.5.436                       
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139194                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.060                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5YP1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 20000, 0.1M MES PH6.5, 20%       
REMARK 280  GLYCEROL, 5.5MM DIPROTINA(IPI), VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       59.94000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      131.26500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.06000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      131.26500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       59.94000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.06000            
REMARK 290   SMTRY3   4  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: 2390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     PHE A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     PHE B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     PHE C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     LEU C     8                                                      
REMARK 465     PHE C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     LEU C    11                                                      
REMARK 465     ILE C    12                                                      
REMARK 465     THR C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     ALA C    15                                                      
REMARK 465     THR C    16                                                      
REMARK 465     ALA C    17                                                      
REMARK 465     LEU C    18                                                      
REMARK 465     PRO C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     HIS C    21                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     LEU D     5                                                      
REMARK 465     PHE D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     LEU D     8                                                      
REMARK 465     PHE D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     ILE D    12                                                      
REMARK 465     THR D    13                                                      
REMARK 465     VAL D    14                                                      
REMARK 465     ALA D    15                                                      
REMARK 465     THR D    16                                                      
REMARK 465     ALA D    17                                                      
REMARK 465     LEU D    18                                                      
REMARK 465     PRO D    19                                                      
REMARK 465     ALA D    20                                                      
REMARK 465     HIS D    21                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    98     O    HOH A   901              2.09            
REMARK 500   O    LYS A   580     OG1  THR A   583              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 104   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 104   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 104   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B 104   NE  -  CZ  -  NH2 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG B 568   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP B 641   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG C 104   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG C 731   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D 104   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP D 231   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG D 309   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG D 309   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG D 591   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  36      -64.88   -131.57                                   
REMARK 500    ASN A 151       61.74   -164.13                                   
REMARK 500    LEU A 181      -55.38     88.78                                   
REMARK 500    ASP A 222       13.29     95.35                                   
REMARK 500    THR A 248       87.59   -150.44                                   
REMARK 500    THR A 336      -94.01   -100.95                                   
REMARK 500    ARG A 351      173.61    -57.25                                   
REMARK 500    GLU A 369      -49.32    -26.23                                   
REMARK 500    SER A 417       24.76     45.58                                   
REMARK 500    GLN A 426      -64.28    -91.54                                   
REMARK 500    ALA A 460      -38.72    -36.21                                   
REMARK 500    ASP A 475       99.15    -60.98                                   
REMARK 500    ALA A 476      -12.57    -47.85                                   
REMARK 500    TYR A 527      -63.79   -120.38                                   
REMARK 500    ARG A 542        2.17    -68.01                                   
REMARK 500    SER A 543     -119.92   -115.72                                   
REMARK 500    ARG A 569       12.35   -144.19                                   
REMARK 500    TYR A 578      108.91    -57.71                                   
REMARK 500    LYS A 580       38.38   -154.77                                   
REMARK 500    THR A 583      -90.65   -124.65                                   
REMARK 500    SER A 613     -108.94     70.54                                   
REMARK 500    HIS A 626       53.77   -142.04                                   
REMARK 500    ALA A 637       58.25     26.44                                   
REMARK 500    ASP A 655      178.61     67.87                                   
REMARK 500    ASN A 660       58.83   -148.37                                   
REMARK 500    ASN A 691      -82.74   -136.06                                   
REMARK 500    LYS A 720     -141.67    -97.69                                   
REMARK 500    LYS A 744       74.80     54.97                                   
REMARK 500    LEU B  36      -58.12   -144.57                                   
REMARK 500    ASP B 144       -6.75     76.65                                   
REMARK 500    ARG B 247      168.69     69.09                                   
REMARK 500    PRO B 272       56.00    -91.08                                   
REMARK 500    THR B 336      -89.73   -115.07                                   
REMARK 500    ASN B 342       53.86   -118.50                                   
REMARK 500    ASP B 391       73.26   -103.28                                   
REMARK 500    ASP B 404       20.65    -78.69                                   
REMARK 500    GLN B 426      -83.17    -92.48                                   
REMARK 500    ALA B 497      173.33    -52.82                                   
REMARK 500    TYR B 527      -63.48   -120.57                                   
REMARK 500    ARG B 542       83.90    -54.24                                   
REMARK 500    SER B 543     -137.85   -158.29                                   
REMARK 500    SER B 613     -105.65     56.36                                   
REMARK 500    HIS B 626       50.37   -145.27                                   
REMARK 500    ALA B 637       50.41     34.97                                   
REMARK 500    ASP B 646      145.94    -36.88                                   
REMARK 500    ASP B 655      172.79     69.34                                   
REMARK 500    ASN B 660       43.82   -141.45                                   
REMARK 500    ILE B 676      107.20    -59.53                                   
REMARK 500    ASN B 691      -76.15   -115.46                                   
REMARK 500    LYS B 720     -138.72   -109.64                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     111 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A  192     GLY A  193                 -146.25                    
REMARK 500 PRO B  638     VAL B  639                  147.27                    
REMARK 500 LYS D  164     GLY D  165                 -148.43                    
REMARK 500 PRO D  638     VAL D  639                  149.81                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1041        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A1042        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH A1043        DISTANCE =  8.97 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE A 801 and PRO A    
REMARK 800  802                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE B 801 and PRO B    
REMARK 800  802                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO B 802 and SER B    
REMARK 800  613                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE C 801 and PRO C    
REMARK 800  802                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO C 802 and SER C    
REMARK 800  613                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide ILE D 801 and PRO D    
REMARK 800  802                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide PRO D 802 and SER D    
REMARK 800  613                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5YP1   RELATED DB: PDB                                   
REMARK 900 5YP1 IS THE SAME PROTEIN APO FORM.                                   
REMARK 900 RELATED ID: 5YP2   RELATED DB: PDB                                   
REMARK 900 5YP2 IS THE SAME PROTEIN COMPLEXED WITH DPP4 INHIBITOR-1C            
REMARK 900 RELATED ID: 5YP4   RELATED DB: PDB                                   
REMARK 900 5YP4 IS THE SAME PROTEIN COMPLEXED WITH LYS-PRO.                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE M12I IS MUTAGENESIS ACCORDING TO SEQUENCE DATABASE           
REMARK 999 UNIPORTKB Q6F3I7 (DAP4_PSEMX).                                       
DBREF  5YP3 A    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
DBREF  5YP3 B    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
DBREF  5YP3 C    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
DBREF  5YP3 D    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
SEQADV 5YP3 ILE A   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQADV 5YP3 ILE B   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQADV 5YP3 ILE C   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQADV 5YP3 ILE D   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQRES   1 A  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 A  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 A  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 A  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 A  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 A  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 A  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 A  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 A  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 A  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 A  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 A  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 A  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 A  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 A  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 A  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 A  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 A  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 A  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 A  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 A  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 A  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 A  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 A  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 A  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 A  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 A  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 A  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 A  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 A  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 A  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 A  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 A  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 A  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 A  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 A  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 A  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 A  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 A  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 A  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 A  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 A  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 A  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 A  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 A  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 A  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 A  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 A  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 A  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 A  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 A  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 A  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 A  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 A  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 A  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 A  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 A  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 A  745  CYS LEU LYS PRO                                              
SEQRES   1 B  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 B  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 B  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 B  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 B  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 B  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 B  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 B  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 B  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 B  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 B  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 B  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 B  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 B  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 B  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 B  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 B  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 B  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 B  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 B  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 B  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 B  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 B  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 B  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 B  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 B  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 B  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 B  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 B  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 B  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 B  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 B  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 B  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 B  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 B  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 B  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 B  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 B  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 B  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 B  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 B  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 B  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 B  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 B  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 B  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 B  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 B  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 B  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 B  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 B  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 B  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 B  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 B  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 B  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 B  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 B  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 B  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 B  745  CYS LEU LYS PRO                                              
SEQRES   1 C  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 C  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 C  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 C  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 C  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 C  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 C  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 C  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 C  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 C  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 C  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 C  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 C  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 C  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 C  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 C  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 C  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 C  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 C  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 C  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 C  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 C  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 C  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 C  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 C  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 C  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 C  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 C  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 C  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 C  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 C  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 C  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 C  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 C  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 C  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 C  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 C  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 C  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 C  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 C  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 C  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 C  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 C  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 C  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 C  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 C  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 C  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 C  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 C  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 C  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 C  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 C  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 C  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 C  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 C  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 C  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 C  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 C  745  CYS LEU LYS PRO                                              
SEQRES   1 D  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 D  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 D  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 D  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 D  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 D  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 D  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 D  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 D  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 D  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 D  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 D  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 D  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 D  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 D  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 D  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 D  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 D  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 D  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 D  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 D  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 D  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 D  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 D  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 D  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 D  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 D  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 D  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 D  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 D  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 D  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 D  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 D  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 D  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 D  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 D  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 D  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 D  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 D  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 D  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 D  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 D  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 D  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 D  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 D  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 D  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 D  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 D  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 D  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 D  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 D  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 D  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 D  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 D  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 D  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 D  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 D  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 D  745  CYS LEU LYS PRO                                              
HET    ILE  A 801       8                                                       
HET    PRO  A 802       7                                                       
HET    ILE  B 801       8                                                       
HET    PRO  B 802       7                                                       
HET    ILE  C 801       8                                                       
HET    PRO  C 802       7                                                       
HET    GOL  D 803       6                                                       
HET    ILE  D 801       8                                                       
HET    PRO  D 802       7                                                       
HETNAM     ILE ISOLEUCINE                                                       
HETNAM     PRO PROLINE                                                          
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  ILE    4(C6 H13 N O2)                                               
FORMUL   6  PRO    4(C5 H9 N O2)                                                
FORMUL  11  GOL    C3 H8 O3                                                     
FORMUL  14  HOH   *452(H2 O)                                                    
HELIX    1 AA1 THR A   26  GLY A   32  1                                   7    
HELIX    2 AA2 ASP A   83  LEU A   88  1                                   6    
HELIX    3 AA3 SER A   95  GLN A  105  1                                  11    
HELIX    4 AA4 GLU A  203  MET A  210  1                                   8    
HELIX    5 AA5 TYR A  480  ARG A  484  5                                   5    
HELIX    6 AA6 SER A  543  GLN A  554  1                                  12    
HELIX    7 AA7 GLY A  570  GLY A  575  1                                   6    
HELIX    8 AA8 ALA A  576  TYR A  578  5                                   3    
HELIX    9 AA9 THR A  583  SER A  598  1                                  16    
HELIX   10 AB1 SER A  613  HIS A  626  1                                  14    
HELIX   11 AB2 ASP A  641  TYR A  645  5                                   5    
HELIX   12 AB3 ASP A  646  ASP A  655  1                                  10    
HELIX   13 AB4 LEU A  656  ALA A  659  5                                   4    
HELIX   14 AB5 ASN A  660  SER A  668  1                                   9    
HELIX   15 AB6 VAL A  669  ILE A  676  5                                   8    
HELIX   16 AB7 PHE A  694  ARG A  707  1                                  14    
HELIX   17 AB8 ARG A  724  LEU A  743  1                                  20    
HELIX   18 AB9 THR B   26  GLY B   32  1                                   7    
HELIX   19 AC1 ASP B   83  LEU B   88  1                                   6    
HELIX   20 AC2 SER B   95  GLN B  105  1                                  11    
HELIX   21 AC3 GLU B  203  MET B  210  1                                   8    
HELIX   22 AC4 TYR B  480  ARG B  484  5                                   5    
HELIX   23 AC5 SER B  543  GLN B  554  1                                  12    
HELIX   24 AC6 GLY B  570  GLY B  575  1                                   6    
HELIX   25 AC7 THR B  583  SER B  598  1                                  16    
HELIX   26 AC8 SER B  613  HIS B  626  1                                  14    
HELIX   27 AC9 ASP B  646  ASP B  655  1                                  10    
HELIX   28 AD1 ASN B  660  ALA B  667  1                                   8    
HELIX   29 AD2 VAL B  669  VAL B  673  5                                   5    
HELIX   30 AD3 PHE B  694  ARG B  707  1                                  14    
HELIX   31 AD4 ARG B  724  LYS B  744  1                                  21    
HELIX   32 AD5 THR C   26  GLY C   32  1                                   7    
HELIX   33 AD6 SER C   95  GLN C  105  1                                  11    
HELIX   34 AD7 GLU C  203  MET C  210  1                                   8    
HELIX   35 AD8 TYR C  480  ALA C  485  1                                   6    
HELIX   36 AD9 SER C  543  GLN C  554  1                                  12    
HELIX   37 AE1 GLY C  570  ALA C  576  1                                   7    
HELIX   38 AE2 THR C  583  GLN C  599  1                                  17    
HELIX   39 AE3 SER C  613  ASP C  627  1                                  15    
HELIX   40 AE4 ASP C  641  TYR C  645  5                                   5    
HELIX   41 AE5 ASP C  646  ASP C  655  1                                  10    
HELIX   42 AE6 ASN C  660  SER C  668  1                                   9    
HELIX   43 AE7 VAL C  669  HIS C  672  5                                   4    
HELIX   44 AE8 PHE C  694  ARG C  707  1                                  14    
HELIX   45 AE9 GLY C  725  LYS C  744  1                                  20    
HELIX   46 AF1 THR D   26  GLY D   32  1                                   7    
HELIX   47 AF2 ASP D   83  LEU D   88  1                                   6    
HELIX   48 AF3 SER D   95  ARG D  106  1                                  12    
HELIX   49 AF4 GLY D  142  ASP D  144  5                                   3    
HELIX   50 AF5 GLU D  203  MET D  210  1                                   8    
HELIX   51 AF6 TYR D  480  ALA D  485  1                                   6    
HELIX   52 AF7 SER D  543  GLN D  554  1                                  12    
HELIX   53 AF8 GLY D  570  GLY D  575  1                                   6    
HELIX   54 AF9 ALA D  576  TYR D  578  5                                   3    
HELIX   55 AG1 THR D  583  GLN D  599  1                                  17    
HELIX   56 AG2 SER D  613  HIS D  626  1                                  14    
HELIX   57 AG3 ASP D  641  TYR D  645  5                                   5    
HELIX   58 AG4 ASP D  646  ASP D  655  1                                  10    
HELIX   59 AG5 LEU D  656  ALA D  659  5                                   4    
HELIX   60 AG6 ASN D  660  SER D  668  1                                   9    
HELIX   61 AG7 SER D  668  VAL D  673  1                                   6    
HELIX   62 AG8 ASP D  674  ILE D  676  5                                   3    
HELIX   63 AG9 PHE D  694  ARG D  707  1                                  14    
HELIX   64 AH1 ARG D  724  LYS D  744  1                                  21    
SHEET    1 AA1 4 LEU A  41  ILE A  46  0                                        
SHEET    2 AA1 4 ARG A  52  GLY A  58 -1  O  LEU A  56   N  THR A  42           
SHEET    3 AA1 4 ARG A  65  ASP A  72 -1  O  TRP A  69   N  PHE A  55           
SHEET    4 AA1 4 LEU A  80  VAL A  82 -1  O  VAL A  82   N  LEU A  68           
SHEET    1 AA2 4 LEU A  41  ILE A  46  0                                        
SHEET    2 AA2 4 ARG A  52  GLY A  58 -1  O  LEU A  56   N  THR A  42           
SHEET    3 AA2 4 ARG A  65  ASP A  72 -1  O  TRP A  69   N  PHE A  55           
SHEET    4 AA2 4 SER A 111  GLY A 112  1  O  SER A 111   N  LEU A  66           
SHEET    1 AA3 4 GLN A 117  TRP A 118  0                                        
SHEET    2 AA3 4 LEU A 125  LEU A 129 -1  O  LEU A 126   N  GLN A 117           
SHEET    3 AA3 4 GLU A 132  TYR A 136 -1  O  TYR A 134   N  PHE A 127           
SHEET    4 AA3 4 VAL A 146  LYS A 148 -1  O  ARG A 147   N  PHE A 135           
SHEET    1 AA4 4 THR A 157  ILE A 161  0                                        
SHEET    2 AA4 4 VAL A 168  ARG A 172 -1  O  ILE A 171   N  THR A 157           
SHEET    3 AA4 4 ASN A 175  ILE A 179 -1  O  TRP A 177   N  PHE A 170           
SHEET    4 AA4 4 GLU A 186  GLN A 188 -1  O  VAL A 187   N  ALA A 178           
SHEET    1 AA5 3 ILE A 197  ASN A 199  0                                        
SHEET    2 AA5 3 ILE A 225  ASP A 231 -1  O  ILE A 230   N  GLY A 198           
SHEET    3 AA5 3 TYR A 216  TRP A 218 -1  N  TRP A 217   O  ALA A 226           
SHEET    1 AA6 4 ILE A 197  ASN A 199  0                                        
SHEET    2 AA6 4 ILE A 225  ASP A 231 -1  O  ILE A 230   N  GLY A 198           
SHEET    3 AA6 4 ARG A 264  ILE A 270 -1  O  ARG A 264   N  ASP A 231           
SHEET    4 AA6 4 ARG A 279  ILE A 281 -1  O  ILE A 281   N  LEU A 267           
SHEET    1 AA7 2 VAL A 237  ARG A 240  0                                        
SHEET    2 AA7 2 VAL A 251  ARG A 254 -1  O  GLN A 253   N  GLN A 238           
SHEET    1 AA8 4 ILE A 289  TRP A 296  0                                        
SHEET    2 AA8 4 ARG A 301  SER A 308 -1  O  GLN A 305   N  ARG A 293           
SHEET    3 AA8 4 LYS A 313  THR A 320 -1  O  GLU A 315   N  ARG A 306           
SHEET    4 AA8 4 THR A 325  THR A 333 -1  O  THR A 325   N  THR A 320           
SHEET    1 AA9 4 ARG A 345  PHE A 346  0                                        
SHEET    2 AA9 4 PHE A 352  SER A 356 -1  O  LEU A 353   N  ARG A 345           
SHEET    3 AA9 4 HIS A 363  ALA A 367 -1  O  TYR A 365   N  TRP A 354           
SHEET    4 AA9 4 LEU A 374  ALA A 376 -1  O  THR A 375   N  VAL A 366           
SHEET    1 AB1 4 VAL A 384  ASP A 391  0                                        
SHEET    2 AB1 4 LEU A 396  GLY A 401 -1  O  TYR A 398   N  ALA A 389           
SHEET    3 AB1 4 HIS A 410  PRO A 415 -1  O  TYR A 412   N  VAL A 399           
SHEET    4 AB1 4 ARG A 422  ARG A 423 -1  O  ARG A 422   N  ALA A 413           
SHEET    1 AB2 4 MET A 430  PHE A 435  0                                        
SHEET    2 AB2 4 VAL A 441  SER A 447 -1  O  VAL A 443   N  THR A 434           
SHEET    3 AB2 4 GLN A 454  LYS A 459 -1  O  GLN A 454   N  TRP A 446           
SHEET    4 AB2 4 LYS A 464  THR A 467 -1  O  ALA A 466   N  LEU A 457           
SHEET    1 AB3 8 THR A 490  THR A 496  0                                        
SHEET    2 AB3 8 PRO A 503  ILE A 509 -1  O  LEU A 508   N  ALA A 491           
SHEET    3 AB3 8 VAL A 557  LEU A 561 -1  O  VAL A 558   N  ILE A 509           
SHEET    4 AB3 8 TYR A 520  VAL A 526  1  N  VAL A 523   O  VAL A 557           
SHEET    5 AB3 8 VAL A 602  TRP A 612  1  O  GLY A 608   N  VAL A 522           
SHEET    6 AB3 8 CYS A 632  GLY A 636  1  O  VAL A 634   N  VAL A 609           
SHEET    7 AB3 8 LEU A 681  GLY A 686  1  O  ILE A 684   N  ALA A 635           
SHEET    8 AB3 8 GLU A 712  TYR A 716  1  O  GLU A 712   N  LEU A 681           
SHEET    1 AB4 4 LEU B  41  ILE B  46  0                                        
SHEET    2 AB4 4 ARG B  52  GLY B  58 -1  O  LEU B  56   N  THR B  42           
SHEET    3 AB4 4 ARG B  65  ASP B  72 -1  O  TYR B  71   N  VAL B  53           
SHEET    4 AB4 4 GLN B  77  VAL B  82 -1  O  LEU B  81   N  LEU B  68           
SHEET    1 AB5 4 LEU B  41  ILE B  46  0                                        
SHEET    2 AB5 4 ARG B  52  GLY B  58 -1  O  LEU B  56   N  THR B  42           
SHEET    3 AB5 4 ARG B  65  ASP B  72 -1  O  TYR B  71   N  VAL B  53           
SHEET    4 AB5 4 SER B 111  GLY B 112  1  O  SER B 111   N  LEU B  66           
SHEET    1 AB6 4 GLN B 117  TRP B 118  0                                        
SHEET    2 AB6 4 ALA B 124  LEU B 129 -1  O  LEU B 126   N  GLN B 117           
SHEET    3 AB6 4 GLU B 132  ASP B 137 -1  O  GLU B 132   N  LEU B 129           
SHEET    4 AB6 4 VAL B 146  LYS B 148 -1  O  ARG B 147   N  PHE B 135           
SHEET    1 AB7 4 THR B 157  ILE B 161  0                                        
SHEET    2 AB7 4 PHE B 167  ARG B 172 -1  O  ILE B 171   N  THR B 157           
SHEET    3 AB7 4 ASN B 175  ASP B 180 -1  O  TRP B 177   N  PHE B 170           
SHEET    4 AB7 4 LYS B 185  GLN B 188 -1  O  VAL B 187   N  ALA B 178           
SHEET    1 AB8 3 ILE B 197  ASN B 199  0                                        
SHEET    2 AB8 3 ILE B 225  ASP B 231 -1  O  ILE B 230   N  GLY B 198           
SHEET    3 AB8 3 TYR B 216  TRP B 218 -1  N  TRP B 217   O  ALA B 226           
SHEET    1 AB9 4 ILE B 197  ASN B 199  0                                        
SHEET    2 AB9 4 ILE B 225  ASP B 231 -1  O  ILE B 230   N  GLY B 198           
SHEET    3 AB9 4 ARG B 264  ILE B 270 -1  O  ARG B 264   N  ASP B 231           
SHEET    4 AB9 4 ARG B 279  ILE B 281 -1  O  ILE B 281   N  LEU B 267           
SHEET    1 AC1 2 VAL B 237  VAL B 243  0                                        
SHEET    2 AC1 2 THR B 248  ARG B 254 -1  O  GLN B 253   N  GLN B 238           
SHEET    1 AC2 4 ILE B 289  ASP B 298  0                                        
SHEET    2 AC2 4 ARG B 301  SER B 308 -1  O  GLN B 305   N  ALA B 292           
SHEET    3 AC2 4 LYS B 313  THR B 320 -1  O  GLU B 315   N  ARG B 306           
SHEET    4 AC2 4 GLN B 326  THR B 333 -1  O  VAL B 330   N  LEU B 316           
SHEET    1 AC3 3 PHE B 352  SER B 356  0                                        
SHEET    2 AC3 3 HIS B 363  ALA B 367 -1  O  TYR B 365   N  TRP B 354           
SHEET    3 AC3 3 LEU B 374  ALA B 376 -1  O  THR B 375   N  VAL B 366           
SHEET    1 AC4 4 VAL B 384  ASP B 391  0                                        
SHEET    2 AC4 4 LEU B 396  GLY B 401 -1  O  TYR B 398   N  ALA B 389           
SHEET    3 AC4 4 HIS B 410  PRO B 415 -1  O  VAL B 414   N  ALA B 397           
SHEET    4 AC4 4 ARG B 422  ARG B 423 -1  O  ARG B 422   N  ALA B 413           
SHEET    1 AC5 4 MET B 430  PHE B 435  0                                        
SHEET    2 AC5 4 VAL B 441  SER B 448 -1  O  VAL B 443   N  THR B 434           
SHEET    3 AC5 4 THR B 451  LYS B 459 -1  O  GLN B 454   N  TRP B 446           
SHEET    4 AC5 4 LYS B 464  THR B 467 -1  O  ALA B 466   N  LEU B 457           
SHEET    1 AC6 8 THR B 490  THR B 496  0                                        
SHEET    2 AC6 8 PRO B 503  ILE B 509 -1  O  LEU B 504   N  LEU B 495           
SHEET    3 AC6 8 VAL B 557  LEU B 561 -1  O  VAL B 558   N  ILE B 509           
SHEET    4 AC6 8 TYR B 520  PHE B 525  1  N  PRO B 521   O  VAL B 557           
SHEET    5 AC6 8 VAL B 602  TRP B 612  1  O  ARG B 606   N  VAL B 522           
SHEET    6 AC6 8 CYS B 632  GLY B 636  1  O  GLY B 636   N  GLY B 611           
SHEET    7 AC6 8 LEU B 681  GLY B 686  1  O  ILE B 684   N  ALA B 635           
SHEET    8 AC6 8 GLU B 712  TYR B 716  1  O  GLU B 712   N  LEU B 681           
SHEET    1 AC7 4 LEU C  41  ILE C  46  0                                        
SHEET    2 AC7 4 ARG C  52  GLY C  58 -1  O  THR C  54   N  GLN C  45           
SHEET    3 AC7 4 ARG C  65  ASP C  72 -1  O  ASP C  67   N  ARG C  57           
SHEET    4 AC7 4 THR C  78  VAL C  82 -1  O  LEU C  81   N  LEU C  68           
SHEET    1 AC8 4 LEU C  41  ILE C  46  0                                        
SHEET    2 AC8 4 ARG C  52  GLY C  58 -1  O  THR C  54   N  GLN C  45           
SHEET    3 AC8 4 ARG C  65  ASP C  72 -1  O  ASP C  67   N  ARG C  57           
SHEET    4 AC8 4 SER C 111  GLY C 112  1  O  SER C 111   N  LEU C  66           
SHEET    1 AC9 4 GLN C 117  TRP C 118  0                                        
SHEET    2 AC9 4 ALA C 124  LEU C 129 -1  O  LEU C 126   N  GLN C 117           
SHEET    3 AC9 4 GLU C 132  ASP C 137 -1  O  GLU C 132   N  LEU C 129           
SHEET    4 AC9 4 ARG C 147  LYS C 148 -1  O  ARG C 147   N  PHE C 135           
SHEET    1 AD1 4 THR C 157  ILE C 161  0                                        
SHEET    2 AD1 4 PHE C 167  ARG C 172 -1  O  ILE C 171   N  THR C 157           
SHEET    3 AD1 4 ASN C 175  ASP C 180 -1  O  ASN C 175   N  ARG C 172           
SHEET    4 AD1 4 LYS C 185  GLN C 188 -1  O  VAL C 187   N  ALA C 178           
SHEET    1 AD2 3 ILE C 197  ASN C 199  0                                        
SHEET    2 AD2 3 ILE C 225  ASP C 231 -1  O  ILE C 230   N  GLY C 198           
SHEET    3 AD2 3 TYR C 216  TRP C 218 -1  N  TRP C 217   O  ALA C 226           
SHEET    1 AD3 4 ILE C 197  ASN C 199  0                                        
SHEET    2 AD3 4 ILE C 225  ASP C 231 -1  O  ILE C 230   N  GLY C 198           
SHEET    3 AD3 4 ARG C 264  ILE C 270 -1  O  GLN C 266   N  ARG C 229           
SHEET    4 AD3 4 ARG C 279  TRP C 280 -1  O  ARG C 279   N  VAL C 269           
SHEET    1 AD4 2 VAL C 237  VAL C 243  0                                        
SHEET    2 AD4 2 THR C 248  ARG C 254 -1  O  GLN C 253   N  GLN C 238           
SHEET    1 AD5 4 ILE C 289  ASP C 298  0                                        
SHEET    2 AD5 4 ARG C 301  SER C 308 -1  O  GLN C 305   N  ARG C 293           
SHEET    3 AD5 4 LYS C 313  THR C 320 -1  O  GLU C 315   N  ARG C 306           
SHEET    4 AD5 4 GLN C 326  THR C 333 -1  O  LEU C 329   N  LEU C 316           
SHEET    1 AD6 3 PHE C 352  SER C 356  0                                        
SHEET    2 AD6 3 HIS C 363  ALA C 367 -1  O  TYR C 365   N  TRP C 354           
SHEET    3 AD6 3 LEU C 374  ALA C 376 -1  O  THR C 375   N  VAL C 366           
SHEET    1 AD7 4 VAL C 384  ASP C 391  0                                        
SHEET    2 AD7 4 LEU C 396  GLY C 401 -1  O  LEU C 396   N  ASP C 391           
SHEET    3 AD7 4 HIS C 410  PRO C 415 -1  O  VAL C 414   N  ALA C 397           
SHEET    4 AD7 4 ARG C 422  ARG C 423 -1  O  ARG C 422   N  ALA C 413           
SHEET    1 AD8 4 MET C 430  PHE C 435  0                                        
SHEET    2 AD8 4 VAL C 441  SER C 447 -1  O  VAL C 443   N  THR C 434           
SHEET    3 AD8 4 GLN C 454  LYS C 459 -1  O  GLN C 454   N  TRP C 446           
SHEET    4 AD8 4 LYS C 464  THR C 467 -1  O  ALA C 466   N  LEU C 457           
SHEET    1 AD9 8 THR C 490  THR C 496  0                                        
SHEET    2 AD9 8 PRO C 503  ILE C 509 -1  O  LEU C 508   N  ALA C 491           
SHEET    3 AD9 8 VAL C 557  LEU C 561 -1  O  VAL C 558   N  ILE C 509           
SHEET    4 AD9 8 TYR C 520  PHE C 525  1  N  VAL C 523   O  VAL C 557           
SHEET    5 AD9 8 VAL C 602  TRP C 612  1  O  GLY C 608   N  VAL C 522           
SHEET    6 AD9 8 CYS C 632  GLY C 636  1  O  VAL C 634   N  VAL C 609           
SHEET    7 AD9 8 LEU C 681  GLY C 686  1  O  ILE C 684   N  ALA C 635           
SHEET    8 AD9 8 GLU C 712  TYR C 716  1  O  GLU C 712   N  LEU C 681           
SHEET    1 AE1 4 LEU D  41  ILE D  46  0                                        
SHEET    2 AE1 4 ARG D  52  GLY D  58 -1  O  THR D  54   N  GLN D  45           
SHEET    3 AE1 4 ARG D  65  ASP D  72 -1  O  TRP D  69   N  PHE D  55           
SHEET    4 AE1 4 GLN D  77  VAL D  82 -1  O  LEU D  81   N  LEU D  68           
SHEET    1 AE2 4 LEU D  41  ILE D  46  0                                        
SHEET    2 AE2 4 ARG D  52  GLY D  58 -1  O  THR D  54   N  GLN D  45           
SHEET    3 AE2 4 ARG D  65  ASP D  72 -1  O  TRP D  69   N  PHE D  55           
SHEET    4 AE2 4 SER D 111  GLY D 112  1  O  SER D 111   N  LEU D  66           
SHEET    1 AE3 4 GLN D 117  TRP D 118  0                                        
SHEET    2 AE3 4 ALA D 124  LEU D 129 -1  O  LEU D 126   N  GLN D 117           
SHEET    3 AE3 4 GLU D 132  ASP D 137 -1  O  GLU D 132   N  LEU D 129           
SHEET    4 AE3 4 VAL D 146  LYS D 148 -1  O  ARG D 147   N  PHE D 135           
SHEET    1 AE4 4 THR D 157  ILE D 161  0                                        
SHEET    2 AE4 4 PHE D 167  ARG D 172 -1  O  ILE D 171   N  THR D 157           
SHEET    3 AE4 4 ASN D 175  ASP D 180 -1  O  ASN D 175   N  ARG D 172           
SHEET    4 AE4 4 GLU D 186  GLN D 188 -1  O  VAL D 187   N  ALA D 178           
SHEET    1 AE5 3 ILE D 197  ASN D 199  0                                        
SHEET    2 AE5 3 ILE D 225  ASP D 231 -1  O  ILE D 230   N  GLY D 198           
SHEET    3 AE5 3 TYR D 216  TRP D 218 -1  N  TRP D 217   O  ALA D 226           
SHEET    1 AE6 4 ILE D 197  ASN D 199  0                                        
SHEET    2 AE6 4 ILE D 225  ASP D 231 -1  O  ILE D 230   N  GLY D 198           
SHEET    3 AE6 4 ARG D 264  ILE D 270 -1  O  ILE D 270   N  ILE D 225           
SHEET    4 AE6 4 ARG D 279  TRP D 280 -1  O  ARG D 279   N  VAL D 269           
SHEET    1 AE7 2 VAL D 237  VAL D 243  0                                        
SHEET    2 AE7 2 THR D 248  ARG D 254 -1  O  GLN D 253   N  GLN D 238           
SHEET    1 AE8 4 ILE D 289  ASP D 298  0                                        
SHEET    2 AE8 4 ARG D 301  SER D 308 -1  O  THR D 303   N  ASP D 295           
SHEET    3 AE8 4 LYS D 313  THR D 320 -1  O  GLU D 315   N  ARG D 306           
SHEET    4 AE8 4 THR D 325  THR D 333 -1  O  VAL D 330   N  LEU D 316           
SHEET    1 AE9 4 ARG D 345  PHE D 346  0                                        
SHEET    2 AE9 4 PHE D 352  SER D 356 -1  O  LEU D 353   N  ARG D 345           
SHEET    3 AE9 4 HIS D 363  ALA D 367 -1  O  ALA D 367   N  PHE D 352           
SHEET    4 AE9 4 LEU D 374  ALA D 376 -1  O  THR D 375   N  VAL D 366           
SHEET    1 AF1 4 VAL D 384  ASP D 391  0                                        
SHEET    2 AF1 4 LEU D 396  GLY D 401 -1  O  SER D 400   N  ASP D 385           
SHEET    3 AF1 4 HIS D 410  PRO D 415 -1  O  VAL D 414   N  ALA D 397           
SHEET    4 AF1 4 ARG D 422  ARG D 423 -1  O  ARG D 422   N  ALA D 413           
SHEET    1 AF2 4 MET D 430  PHE D 435  0                                        
SHEET    2 AF2 4 VAL D 441  SER D 447 -1  O  VAL D 443   N  THR D 434           
SHEET    3 AF2 4 GLN D 454  LYS D 459 -1  O  GLN D 454   N  TRP D 446           
SHEET    4 AF2 4 LYS D 464  THR D 467 -1  O  ALA D 466   N  LEU D 457           
SHEET    1 AF3 8 THR D 490  THR D 496  0                                        
SHEET    2 AF3 8 PRO D 503  ILE D 509 -1  O  LEU D 504   N  LEU D 495           
SHEET    3 AF3 8 VAL D 557  LEU D 561 -1  O  VAL D 558   N  ILE D 509           
SHEET    4 AF3 8 TYR D 520  PHE D 525  1  N  PHE D 525   O  PHE D 559           
SHEET    5 AF3 8 VAL D 602  TRP D 612  1  O  GLY D 608   N  VAL D 522           
SHEET    6 AF3 8 CYS D 632  GLY D 636  1  O  VAL D 634   N  VAL D 609           
SHEET    7 AF3 8 LEU D 681  GLY D 686  1  O  ILE D 684   N  ALA D 635           
SHEET    8 AF3 8 GLU D 712  TYR D 716  1  O  GLU D 712   N  LEU D 681           
LINK         OG  SER A 613                 C   PRO A 802     1555   1555  1.33  
LINK         OG  SER B 613                 C   PRO B 802     1555   1555  1.33  
LINK         OG  SER C 613                 C   PRO C 802     1555   1555  1.35  
LINK         OG  SER D 613                 C   PRO D 802     1555   1555  1.35  
LINK         C   ILE A 801                 N   PRO A 802     1555   1555  1.35  
LINK         C   ILE B 801                 N   PRO B 802     1555   1555  1.34  
LINK         C   ILE C 801                 N   PRO C 802     1555   1555  1.35  
LINK         C   ILE D 801                 N   PRO D 802     1555   1555  1.34  
SITE     1 AC1 11 PRO D 339  GLU D 357  THR D 566  PRO D 567                    
SITE     2 AC1 11 ARG D 568  ARG D 569  GLY D 570  ALA D 571                    
SITE     3 AC1 11 GLY D 574  HOH D 965  HOH D 969                               
SITE     1 AC2 12 ARG A 106  GLU A 208  GLU A 209  TYR A 527                    
SITE     2 AC2 12 ALA A 531  SER A 613  ASN A 614  TYR A 645                    
SITE     3 AC2 12 TYR A 649  ASN A 691  VAL A 692  HIS A 721                    
SITE     1 AC3 12 ARG B 106  GLU B 208  GLU B 209  TYR B 527                    
SITE     2 AC3 12 ALA B 531  SER B 613  ASN B 614  VAL B 639                    
SITE     3 AC3 12 TYR B 645  TYR B 649  ASN B 691  HIS B 721                    
SITE     1 AC4 13 TYR B 527  TRP B 612  ASN B 614  GLY B 615                    
SITE     2 AC4 13 GLY B 616  TYR B 617  GLY B 636  ALA B 637                    
SITE     3 AC4 13 VAL B 639  TYR B 645  TYR B 649  HIS B 721                    
SITE     4 AC4 13 ILE B 801                                                     
SITE     1 AC5 10 ARG C 106  GLU C 208  GLU C 209  TYR C 527                    
SITE     2 AC5 10 ALA C 531  SER C 613  ASN C 614  TYR C 645                    
SITE     3 AC5 10 TYR C 649  ASN C 691                                          
SITE     1 AC6 12 TYR C 527  TRP C 612  ASN C 614  GLY C 615                    
SITE     2 AC6 12 GLY C 616  TYR C 617  GLY C 636  ALA C 637                    
SITE     3 AC6 12 TYR C 645  TYR C 649  HIS C 721  ILE C 801                    
SITE     1 AC7 12 ARG D 106  GLU D 208  GLU D 209  TYR D 527                    
SITE     2 AC7 12 ALA D 531  SER D 613  ASN D 614  TYR D 645                    
SITE     3 AC7 12 TYR D 649  ASN D 691  VAL D 692  HOH D 959                    
SITE     1 AC8 15 TYR D 527  TRP D 612  ASN D 614  GLY D 615                    
SITE     2 AC8 15 GLY D 616  TYR D 617  GLY D 636  ALA D 637                    
SITE     3 AC8 15 PRO D 638  TYR D 645  TYR D 649  VAL D 692                    
SITE     4 AC8 15 HIS D 721  ILE D 801  HOH D 959                               
CRYST1  119.880  120.120  262.530  90.00  90.00  90.00 P 21 21 21   16          
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      0.008342  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003809        0.00000                         
TER    5661      PRO A 745                                                      
TER   11322      PRO B 745                                                      
TER   16983      PRO C 745                                                      
TER   22644      PRO D 745                                                      
MASTER      537    0    9   64  194    0   26    623158    4   22  232          
END                                                                             

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