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LongText Report for: 3CCB-pdb

Name Class
3CCB-pdb
HEADER    HYDROLASE                               25-FEB-08   3CCB              
TITLE     CRYSTAL STRUCTURE OF HUMAN DPP4 IN COMPLEX WITH A                     
TITLE    2 BENZIMIDAZOLE DERIVATIVE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 4;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: DIPEPTIDYL PEPTIDASE IV, DPP IV, T-CELL                     
COMPND   5 ACTIVATION ANTIGEN CD26, TP103, ADENOSINE DEAMINASE                  
COMPND   6 COMPLEXING PROTEIN 2, ADABP;                                         
COMPND   7 EC: 3.4.14.5;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 GENE: DPP4, ADCP2, CD26;                                             
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PSXB9                                      
KEYWDS    STRUCTURE-BASED DESIGN, DENZIMIDAZOLE DERIVATIVES,                    
KEYWDS   2 PEPTIDASE, AMINOPEPTIDASE, GLYCOPROTEIN, HYDROLASE,                  
KEYWDS   3 MEMBRANE, PROTEASE, SECRETED, SERINE PROTEASE, SIGNAL-               
KEYWDS   4 ANCHOR, TRANSMEMBRANE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.B.WALLACE,R.J.SKENE                                                 
REVDAT   1   21-OCT-08 3CCB    0                                                
JRNL        AUTH   M.B.WALLACE,J.FENG,Z.ZHANG,R.J.SKENE,L.SHI,                  
JRNL        AUTH 2 C.L.CASTER,D.B.KASSEL,R.XU,S.L.GWALTNEY                      
JRNL        TITL   STRUCTURE-BASED DESIGN AND SYNTHESIS OF                      
JRNL        TITL 2 BENZIMIDAZOLE DERIVATIVES AS DIPEPTIDYL PEPTIDASE            
JRNL        TITL 3 IV INHIBITORS.                                               
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  18  2362 2008              
JRNL        REFN   ASTM BMCLE8  UK ISSN 0960-894X                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.49 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 133885                         
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6730                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.49                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8663                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2960                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 470                          
REMARK   3   BIN FREE R VALUE                    : 0.3560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 24805                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.45000                                             
REMARK   3    B22 (A**2) : 2.13000                                              
REMARK   3    B33 (A**2) : 0.21000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.05000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.481         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.275         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.200         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.781        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 24876 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 33856 ; 1.239 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2896 ; 5.344 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1224 ;32.964 ;23.938       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3969 ;16.156 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   118 ;17.026 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3602 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 19082 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 11711 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 16940 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1263 ; 0.132 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   111 ; 0.161 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.168 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 14778 ; 1.025 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 23455 ; 1.648 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 11811 ; 0.962 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 10401 ; 1.459 ; 3.000       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    41        A   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7110  -0.8600  19.1050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1330 T22:  -0.1688                                     
REMARK   3      T33:  -0.1332 T12:   0.0645                                     
REMARK   3      T13:  -0.0085 T23:   0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1938 L22:   0.7449                                     
REMARK   3      L33:   0.8055 L12:   0.2398                                     
REMARK   3      L13:  -0.0087 L23:   0.0274                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0680 S12:  -0.1708 S13:  -0.2529                       
REMARK   3      S21:   0.1138 S22:   0.0498 S23:  -0.2298                       
REMARK   3      S31:   0.0063 S32:   0.2178 S33:   0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    36        B   801                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2220  -7.3430  20.9970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1307 T22:  -0.1660                                     
REMARK   3      T33:  -0.1033 T12:   0.0474                                     
REMARK   3      T13:   0.0332 T23:   0.1193                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5944 L22:   0.7527                                     
REMARK   3      L33:   0.6754 L12:  -0.0126                                     
REMARK   3      L13:  -0.2597 L23:   0.1511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1276 S12:  -0.1466 S13:  -0.2463                       
REMARK   3      S21:  -0.0148 S22:   0.0841 S23:   0.2237                       
REMARK   3      S31:  -0.0382 S32:  -0.1584 S33:   0.0435                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    41        C   801                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.0590  -0.5000 -33.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0783 T22:  -0.0835                                     
REMARK   3      T33:  -0.1785 T12:  -0.0600                                     
REMARK   3      T13:   0.0259 T23:  -0.0152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9748 L22:   0.5566                                     
REMARK   3      L33:   0.7204 L12:   0.0267                                     
REMARK   3      L13:   0.3972 L23:   0.1411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1031 S12:   0.2450 S13:   0.1922                       
REMARK   3      S21:  -0.0608 S22:  -0.0305 S23:  -0.1567                       
REMARK   3      S31:  -0.0867 S32:   0.3577 S33:  -0.0726                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    41        D   801                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.2070 -63.3690  46.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0282 T22:   0.0247                                     
REMARK   3      T33:  -0.0098 T12:  -0.0363                                     
REMARK   3      T13:  -0.0462 T23:   0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2573 L22:   0.9001                                     
REMARK   3      L33:   0.8552 L12:  -0.0064                                     
REMARK   3      L13:   0.1187 L23:  -0.3060                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0681 S12:  -0.2133 S13:   0.0715                       
REMARK   3      S21:   0.0834 S22:  -0.1636 S23:  -0.4139                       
REMARK   3      S31:  -0.0017 S32:   0.4076 S33:   0.0955                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3CCB COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007                        
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.                               
REMARK 100 THE RCSB ID CODE IS RCSB046603.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-AUG-2003                        
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 133909                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 2000MME, 0.1M BICINE, PH       
REMARK 280  7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,1/2+Y,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       61.50500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/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: 7880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 59110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.3 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: 6460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 58410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                 
REMARK 465                                                                      
REMARK 465   M RES C  SSEQI                                                     
REMARK 465     ALA A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     HIS A    37                                                      
REMARK 465     HIS A    38                                                      
REMARK 465     SER A    39                                                      
REMARK 465     ARG A    40                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     ASP C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     GLY C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     SER C    32                                                      
REMARK 465     HIS C    33                                                      
REMARK 465     HIS C    34                                                      
REMARK 465     HIS C    35                                                      
REMARK 465     HIS C    36                                                      
REMARK 465     HIS C    37                                                      
REMARK 465     HIS C    38                                                      
REMARK 465     SER C    39                                                      
REMARK 465     ARG C    40                                                      
REMARK 465     GLU C    73                                                      
REMARK 465     ASN C    74                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     GLY D    30                                                      
REMARK 465     GLY D    31                                                      
REMARK 465     SER D    32                                                      
REMARK 465     HIS D    33                                                      
REMARK 465     HIS D    34                                                      
REMARK 465     HIS D    35                                                      
REMARK 465     HIS D    36                                                      
REMARK 465     HIS D    37                                                      
REMARK 465     HIS D    38                                                      
REMARK 465     SER D    39                                                      
REMARK 465     ARG D    40                                                      
REMARK 465     GLU D    73                                                      
REMARK 465     ASN D    74                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS B  38    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG B  40    CG   CD   NE   CZ   NH1  NH2                        
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    SER A  64     -156.76   -151.92                                   
REMARK 500    HIS A  66        0.78   -151.50                                   
REMARK 500    PHE A  95       60.21   -106.49                                   
REMARK 500    GLU A  97       49.01    -73.93                                   
REMARK 500    GLN A 123      -99.07   -108.25                                   
REMARK 500    TRP A 124     -145.66    -90.45                                   
REMARK 500    ARG A 140       72.66     48.97                                   
REMARK 500    HIS A 162       32.79   -144.93                                   
REMARK 500    PRO A 181      150.58    -47.37                                   
REMARK 500    ILE A 193      -57.07   -130.86                                   
REMARK 500    SER A 242     -165.51     62.06                                   
REMARK 500    GLN A 320       39.87    -83.16                                   
REMARK 500    GLU A 332      -77.85    -70.60                                   
REMARK 500    ASN A 420       43.79   -102.64                                   
REMARK 500    ASN A 450       81.06   -159.28                                   
REMARK 500    GLN A 508       98.34    -62.29                                   
REMARK 500    PRO A 531      156.96    -48.42                                   
REMARK 500    TYR A 547      -66.09   -126.11                                   
REMARK 500    THR A 600      -93.29   -128.04                                   
REMARK 500    SER A 630     -120.56     61.38                                   
REMARK 500    ASP A 678      -99.18   -122.80                                   
REMARK 500    ASN A 710      -68.71    -98.14                                   
REMARK 500    ASP A 737       -3.06     68.85                                   
REMARK 500    ASP A 739     -155.99   -100.12                                   
REMARK 500    HIS B  37      -14.64    113.74                                   
REMARK 500    SER B  64     -150.55   -135.64                                   
REMARK 500    GLN B 123     -101.49   -115.45                                   
REMARK 500    TRP B 124     -144.16    -91.86                                   
REMARK 500    HIS B 162       38.47   -153.55                                   
REMARK 500    ASP B 192      -15.59     70.89                                   
REMARK 500    VAL B 207      -61.10   -107.41                                   
REMARK 500    SER B 242     -167.39     68.32                                   
REMARK 500    GLN B 320       41.29    -82.64                                   
REMARK 500    THR B 411     -162.57   -119.14                                   
REMARK 500    ALA B 465       13.06     59.31                                   
REMARK 500    GLN B 508       80.83    -69.70                                   
REMARK 500    TYR B 547      -65.41   -127.12                                   
REMARK 500    THR B 600      -97.81   -119.51                                   
REMARK 500    SER B 630     -115.05     57.51                                   
REMARK 500    ALA B 654       56.43     39.38                                   
REMARK 500    ASP B 678      -89.23   -131.25                                   
REMARK 500    ASN B 679       21.33   -140.86                                   
REMARK 500    ASN B 710      -70.49    -99.49                                   
REMARK 500    ASP B 739     -160.59   -103.72                                   
REMARK 500    TYR C  83      -58.87   -121.76                                   
REMARK 500    ASN C  92      -74.91    -54.92                                   
REMARK 500    SER C  93       47.09    -89.34                                   
REMARK 500    PHE C  95       41.45   -102.37                                   
REMARK 500    PHE C  98      -51.89   -127.09                                   
REMARK 500    GLN C 123     -102.18   -103.46                                   
REMARK 500    TRP C 124     -144.69    -90.13                                   
REMARK 500    HIS C 162       27.62   -148.55                                   
REMARK 500    ILE C 193      -56.94   -134.70                                   
REMARK 500    VAL C 207      -60.71   -103.07                                   
REMARK 500    ALA C 213       50.71   -141.22                                   
REMARK 500    SER C 242     -160.17     63.41                                   
REMARK 500    GLN C 320       38.40    -82.04                                   
REMARK 500    THR C 411     -157.00   -108.10                                   
REMARK 500    LYS C 423       47.21     31.33                                   
REMARK 500    ASN C 450       72.56   -163.93                                   
REMARK 500    TYR C 547      -71.04   -118.02                                   
REMARK 500    ARG C 597       40.75   -144.35                                   
REMARK 500    THR C 600      -93.45   -124.37                                   
REMARK 500    SER C 630     -121.71     65.08                                   
REMARK 500    ASP C 678      -93.04   -127.08                                   
REMARK 500    ASN C 710      -74.31    -91.43                                   
REMARK 500    ASP C 739     -159.84   -103.76                                   
REMARK 500    ILE C 742       51.79     37.27                                   
REMARK 500    SER D  64     -157.50   -132.25                                   
REMARK 500    PRO D 109      -33.31    -33.20                                   
REMARK 500    GLN D 123     -104.47   -103.35                                   
REMARK 500    TRP D 124     -145.53    -90.86                                   
REMARK 500    ILE D 193      -55.19   -132.63                                   
REMARK 500    VAL D 207      -63.30   -106.92                                   
REMARK 500    SER D 242     -170.02     63.84                                   
REMARK 500    GLN D 320       45.57    -84.64                                   
REMARK 500    PHE D 357      -41.81   -131.19                                   
REMARK 500    ASP D 413      -62.04    -90.73                                   
REMARK 500    ASN D 420       40.95   -105.81                                   
REMARK 500    LYS D 423       17.99     54.09                                   
REMARK 500    ASN D 487       34.71   -154.43                                   
REMARK 500    THR D 600      -97.17   -121.64                                   
REMARK 500    SER D 630     -120.94     60.47                                   
REMARK 500    ALA D 654       60.66     35.59                                   
REMARK 500    ASP D 678     -100.03   -126.65                                   
REMARK 500    ALA D 707       32.33    -99.36                                   
REMARK 500    ASN D 710      -71.31   -102.34                                   
REMARK 500    GLN D 714      -50.41    -28.31                                   
REMARK 500    ASP D 739     -163.28   -102.25                                   
REMARK 500    ILE D 742       51.97     31.00                                   
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 B 936        DISTANCE =  6.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 801                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 802                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 803                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 804                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 806                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 807                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 808                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 802                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 803                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 804                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 805                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 802                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 803                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 804                 
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 801                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 802                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 804                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2Y A 800                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2Y B 800                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2Y C 800                 
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B2Y D 800                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3CCC   RELATED DB: PDB                                   
DBREF  3CCB A   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3CCB B   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3CCB C   39   766  UNP    P27487   DPP4_HUMAN      39    766             
DBREF  3CCB D   39   766  UNP    P27487   DPP4_HUMAN      39    766             
SEQADV 3CCB ALA A   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ASP A   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB PRO A   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY A   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY A   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB SER A   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS A   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ALA B   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ASP B   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB PRO B   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY B   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY B   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB SER B   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS B   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ALA C   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ASP C   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB PRO C   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY C   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY C   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB SER C   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS C   38  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ALA D   27  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB ASP D   28  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB PRO D   29  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY D   30  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB GLY D   31  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB SER D   32  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   33  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   34  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   35  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   36  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   37  UNP  P27487              EXPRESSION TAG                 
SEQADV 3CCB HIS D   38  UNP  P27487              EXPRESSION TAG                 
SEQRES   1 A  740  ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 A  740  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   3 A  740  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   4 A  740  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   5 A  740  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   6 A  740  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   7 A  740  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   8 A  740  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   9 A  740  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES  10 A  740  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  11 A  740  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  12 A  740  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  13 A  740  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  14 A  740  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  15 A  740  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  16 A  740  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  17 A  740  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  18 A  740  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  19 A  740  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  20 A  740  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  21 A  740  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  22 A  740  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  23 A  740  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  24 A  740  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  25 A  740  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  26 A  740  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  27 A  740  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  28 A  740  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  29 A  740  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  30 A  740  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  31 A  740  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  32 A  740  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  33 A  740  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  34 A  740  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  35 A  740  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  36 A  740  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  37 A  740  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  38 A  740  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  39 A  740  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  40 A  740  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  41 A  740  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  42 A  740  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  43 A  740  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  44 A  740  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  45 A  740  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  46 A  740  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  47 A  740  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  48 A  740  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  49 A  740  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  50 A  740  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  51 A  740  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  52 A  740  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  53 A  740  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  54 A  740  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  55 A  740  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  56 A  740  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  57 A  740  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO              
SEQRES   1 B  740  ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 B  740  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   3 B  740  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   4 B  740  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   5 B  740  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   6 B  740  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   7 B  740  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   8 B  740  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   9 B  740  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES  10 B  740  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  11 B  740  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  12 B  740  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  13 B  740  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  14 B  740  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  15 B  740  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  16 B  740  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  17 B  740  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  18 B  740  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  19 B  740  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  20 B  740  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  21 B  740  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  22 B  740  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  23 B  740  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  24 B  740  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  25 B  740  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  26 B  740  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  27 B  740  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  28 B  740  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  29 B  740  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  30 B  740  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  31 B  740  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  32 B  740  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  33 B  740  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  34 B  740  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  35 B  740  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  36 B  740  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  37 B  740  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  38 B  740  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  39 B  740  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  40 B  740  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  41 B  740  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  42 B  740  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  43 B  740  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  44 B  740  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  45 B  740  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  46 B  740  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  47 B  740  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  48 B  740  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  49 B  740  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  50 B  740  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  51 B  740  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  52 B  740  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  53 B  740  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  54 B  740  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  55 B  740  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  56 B  740  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  57 B  740  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO              
SEQRES   1 C  740  ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 C  740  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   3 C  740  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   4 C  740  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   5 C  740  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   6 C  740  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   7 C  740  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   8 C  740  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   9 C  740  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES  10 C  740  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  11 C  740  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  12 C  740  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  13 C  740  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  14 C  740  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  15 C  740  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  16 C  740  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  17 C  740  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  18 C  740  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  19 C  740  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  20 C  740  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  21 C  740  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  22 C  740  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  23 C  740  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  24 C  740  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  25 C  740  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  26 C  740  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  27 C  740  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  28 C  740  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  29 C  740  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  30 C  740  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  31 C  740  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  32 C  740  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  33 C  740  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  34 C  740  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  35 C  740  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  36 C  740  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  37 C  740  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  38 C  740  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  39 C  740  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  40 C  740  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  41 C  740  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  42 C  740  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  43 C  740  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  44 C  740  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  45 C  740  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  46 C  740  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  47 C  740  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  48 C  740  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  49 C  740  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  50 C  740  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  51 C  740  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  52 C  740  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  53 C  740  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  54 C  740  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  55 C  740  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  56 C  740  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  57 C  740  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO              
SEQRES   1 D  740  ALA ASP PRO GLY GLY SER HIS HIS HIS HIS HIS HIS SER          
SEQRES   2 D  740  ARG LYS THR TYR THR LEU THR ASP TYR LEU LYS ASN THR          
SEQRES   3 D  740  TYR ARG LEU LYS LEU TYR SER LEU ARG TRP ILE SER ASP          
SEQRES   4 D  740  HIS GLU TYR LEU TYR LYS GLN GLU ASN ASN ILE LEU VAL          
SEQRES   5 D  740  PHE ASN ALA GLU TYR GLY ASN SER SER VAL PHE LEU GLU          
SEQRES   6 D  740  ASN SER THR PHE ASP GLU PHE GLY HIS SER ILE ASN ASP          
SEQRES   7 D  740  TYR SER ILE SER PRO ASP GLY GLN PHE ILE LEU LEU GLU          
SEQRES   8 D  740  TYR ASN TYR VAL LYS GLN TRP ARG HIS SER TYR THR ALA          
SEQRES   9 D  740  SER TYR ASP ILE TYR ASP LEU ASN LYS ARG GLN LEU ILE          
SEQRES  10 D  740  THR GLU GLU ARG ILE PRO ASN ASN THR GLN TRP VAL THR          
SEQRES  11 D  740  TRP SER PRO VAL GLY HIS LYS LEU ALA TYR VAL TRP ASN          
SEQRES  12 D  740  ASN ASP ILE TYR VAL LYS ILE GLU PRO ASN LEU PRO SER          
SEQRES  13 D  740  TYR ARG ILE THR TRP THR GLY LYS GLU ASP ILE ILE TYR          
SEQRES  14 D  740  ASN GLY ILE THR ASP TRP VAL TYR GLU GLU GLU VAL PHE          
SEQRES  15 D  740  SER ALA TYR SER ALA LEU TRP TRP SER PRO ASN GLY THR          
SEQRES  16 D  740  PHE LEU ALA TYR ALA GLN PHE ASN ASP THR GLU VAL PRO          
SEQRES  17 D  740  LEU ILE GLU TYR SER PHE TYR SER ASP GLU SER LEU GLN          
SEQRES  18 D  740  TYR PRO LYS THR VAL ARG VAL PRO TYR PRO LYS ALA GLY          
SEQRES  19 D  740  ALA VAL ASN PRO THR VAL LYS PHE PHE VAL VAL ASN THR          
SEQRES  20 D  740  ASP SER LEU SER SER VAL THR ASN ALA THR SER ILE GLN          
SEQRES  21 D  740  ILE THR ALA PRO ALA SER MET LEU ILE GLY ASP HIS TYR          
SEQRES  22 D  740  LEU CYS ASP VAL THR TRP ALA THR GLN GLU ARG ILE SER          
SEQRES  23 D  740  LEU GLN TRP LEU ARG ARG ILE GLN ASN TYR SER VAL MET          
SEQRES  24 D  740  ASP ILE CYS ASP TYR ASP GLU SER SER GLY ARG TRP ASN          
SEQRES  25 D  740  CYS LEU VAL ALA ARG GLN HIS ILE GLU MET SER THR THR          
SEQRES  26 D  740  GLY TRP VAL GLY ARG PHE ARG PRO SER GLU PRO HIS PHE          
SEQRES  27 D  740  THR LEU ASP GLY ASN SER PHE TYR LYS ILE ILE SER ASN          
SEQRES  28 D  740  GLU GLU GLY TYR ARG HIS ILE CYS TYR PHE GLN ILE ASP          
SEQRES  29 D  740  LYS LYS ASP CYS THR PHE ILE THR LYS GLY THR TRP GLU          
SEQRES  30 D  740  VAL ILE GLY ILE GLU ALA LEU THR SER ASP TYR LEU TYR          
SEQRES  31 D  740  TYR ILE SER ASN GLU TYR LYS GLY MET PRO GLY GLY ARG          
SEQRES  32 D  740  ASN LEU TYR LYS ILE GLN LEU SER ASP TYR THR LYS VAL          
SEQRES  33 D  740  THR CYS LEU SER CYS GLU LEU ASN PRO GLU ARG CYS GLN          
SEQRES  34 D  740  TYR TYR SER VAL SER PHE SER LYS GLU ALA LYS TYR TYR          
SEQRES  35 D  740  GLN LEU ARG CYS SER GLY PRO GLY LEU PRO LEU TYR THR          
SEQRES  36 D  740  LEU HIS SER SER VAL ASN ASP LYS GLY LEU ARG VAL LEU          
SEQRES  37 D  740  GLU ASP ASN SER ALA LEU ASP LYS MET LEU GLN ASN VAL          
SEQRES  38 D  740  GLN MET PRO SER LYS LYS LEU ASP PHE ILE ILE LEU ASN          
SEQRES  39 D  740  GLU THR LYS PHE TRP TYR GLN MET ILE LEU PRO PRO HIS          
SEQRES  40 D  740  PHE ASP LYS SER LYS LYS TYR PRO LEU LEU LEU ASP VAL          
SEQRES  41 D  740  TYR ALA GLY PRO CYS SER GLN LYS ALA ASP THR VAL PHE          
SEQRES  42 D  740  ARG LEU ASN TRP ALA THR TYR LEU ALA SER THR GLU ASN          
SEQRES  43 D  740  ILE ILE VAL ALA SER PHE ASP GLY ARG GLY SER GLY TYR          
SEQRES  44 D  740  GLN GLY ASP LYS ILE MET HIS ALA ILE ASN ARG ARG LEU          
SEQRES  45 D  740  GLY THR PHE GLU VAL GLU ASP GLN ILE GLU ALA ALA ARG          
SEQRES  46 D  740  GLN PHE SER LYS MET GLY PHE VAL ASP ASN LYS ARG ILE          
SEQRES  47 D  740  ALA ILE TRP GLY TRP SER TYR GLY GLY TYR VAL THR SER          
SEQRES  48 D  740  MET VAL LEU GLY SER GLY SER GLY VAL PHE LYS CYS GLY          
SEQRES  49 D  740  ILE ALA VAL ALA PRO VAL SER ARG TRP GLU TYR TYR ASP          
SEQRES  50 D  740  SER VAL TYR THR GLU ARG TYR MET GLY LEU PRO THR PRO          
SEQRES  51 D  740  GLU ASP ASN LEU ASP HIS TYR ARG ASN SER THR VAL MET          
SEQRES  52 D  740  SER ARG ALA GLU ASN PHE LYS GLN VAL GLU TYR LEU LEU          
SEQRES  53 D  740  ILE HIS GLY THR ALA ASP ASP ASN VAL HIS PHE GLN GLN          
SEQRES  54 D  740  SER ALA GLN ILE SER LYS ALA LEU VAL ASP VAL GLY VAL          
SEQRES  55 D  740  ASP PHE GLN ALA MET TRP TYR THR ASP GLU ASP HIS GLY          
SEQRES  56 D  740  ILE ALA SER SER THR ALA HIS GLN HIS ILE TYR THR HIS          
SEQRES  57 D  740  MET SER HIS PHE ILE LYS GLN CYS PHE SER LEU PRO              
MODRES 3CCB ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN A  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN A  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN A  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN A  281  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN A  321  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN B   85  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN B  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN B  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN B  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN B  281  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN C  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN C  219  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN C  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN D  150  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN D  229  ASN  GLYCOSYLATION SITE                                 
MODRES 3CCB ASN D  281  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 801      14                                                       
HET    NAG  A 802      14                                                       
HET    NAG  A 803      14                                                       
HET    NAG  A 804      14                                                       
HET    NAG  A 805      14                                                       
HET    NAG  A 806      14                                                       
HET    NAG  A 807      14                                                       
HET    NAG  A 808      14                                                       
HET    NAG  B 801      14                                                       
HET    NAG  B 802      14                                                       
HET    NAG  B 803      14                                                       
HET    NAG  B 804      14                                                       
HET    NAG  B 805      14                                                       
HET    NAG  B 806      14                                                       
HET    NAG  C 801      14                                                       
HET    NAG  C 802      14                                                       
HET    NAG  C 803      14                                                       
HET    NAG  C 804      14                                                       
HET    NAG  D 801      14                                                       
HET    NAG  D 802      14                                                       
HET    NAG  D 803      14                                                       
HET    NAG  D 804      14                                                       
HET    B2Y  A 800      14                                                       
HET    B2Y  B 800      14                                                       
HET    B2Y  C 800      14                                                       
HET    B2Y  D 800      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     B2Y 1-BIPHENYL-2-YLMETHANAMINE                                       
HETSYN     NAG NAG                                                              
FORMUL   5  NAG    22(C8 H15 N O6)                                              
FORMUL  22  B2Y    4(C13 H13 N)                                                 
FORMUL  26  HOH   *676(H2 O)                                                    
HELIX    1   1 THR A   44  ASN A   51  1                                   8    
HELIX    2   2 PHE A   95  GLY A   99  5                                   5    
HELIX    3   3 ASP A  200  VAL A  207  1                                   8    
HELIX    4   4 PRO A  290  ILE A  295  1                                   6    
HELIX    5   5 VAL A  341  GLN A  344  5                                   4    
HELIX    6   6 GLU A  421  MET A  425  5                                   5    
HELIX    7   7 ASN A  497  LEU A  504  1                                   8    
HELIX    8   8 GLN A  505  VAL A  507  5                                   3    
HELIX    9   9 ASN A  562  ASN A  572  1                                  11    
HELIX   10  10 GLY A  587  HIS A  592  1                                   6    
HELIX   11  11 ALA A  593  ASN A  595  5                                   3    
HELIX   12  12 THR A  600  LYS A  615  1                                  16    
HELIX   13  13 SER A  630  GLY A  641  1                                  12    
HELIX   14  14 ARG A  658  TYR A  662  5                                   5    
HELIX   15  15 ASP A  663  GLY A  672  1                                  10    
HELIX   16  16 ASN A  679  SER A  686  1                                   8    
HELIX   17  17 VAL A  688  VAL A  698  5                                  11    
HELIX   18  18 HIS A  712  VAL A  726  1                                  15    
HELIX   19  19 SER A  744  PHE A  763  1                                  20    
HELIX   20  20 THR B   44  ASN B   51  1                                   8    
HELIX   21  21 GLU B   91  ASP B   96  5                                   6    
HELIX   22  22 ASP B  200  VAL B  207  1                                   8    
HELIX   23  23 PRO B  290  ILE B  295  1                                   6    
HELIX   24  24 VAL B  341  GLN B  344  5                                   4    
HELIX   25  25 GLU B  421  MET B  425  5                                   5    
HELIX   26  26 ASN B  497  GLN B  505  1                                   9    
HELIX   27  27 ASN B  562  THR B  570  1                                   9    
HELIX   28  28 GLY B  587  HIS B  592  1                                   6    
HELIX   29  29 THR B  600  LYS B  615  1                                  16    
HELIX   30  30 SER B  630  GLY B  641  1                                  12    
HELIX   31  31 ARG B  658  TYR B  662  5                                   5    
HELIX   32  32 ASP B  663  GLY B  672  1                                  10    
HELIX   33  33 ASN B  679  SER B  686  1                                   8    
HELIX   34  34 VAL B  688  VAL B  698  5                                  11    
HELIX   35  35 HIS B  712  VAL B  726  1                                  15    
HELIX   36  36 SER B  744  PHE B  763  1                                  20    
HELIX   37  37 THR C   44  ASN C   51  1                                   8    
HELIX   38  38 GLU C   91  PHE C   95  5                                   5    
HELIX   39  39 ASP C  200  GLU C  206  1                                   7    
HELIX   40  40 ASP C  274  LEU C  276  5                                   3    
HELIX   41  41 PRO C  290  ILE C  295  1                                   6    
HELIX   42  42 VAL C  341  GLN C  344  5                                   4    
HELIX   43  43 GLU C  421  MET C  425  5                                   5    
HELIX   44  44 ASN C  497  GLN C  505  1                                   9    
HELIX   45  45 ASN C  562  THR C  570  1                                   9    
HELIX   46  46 GLY C  587  HIS C  592  1                                   6    
HELIX   47  47 ALA C  593  ASN C  595  5                                   3    
HELIX   48  48 THR C  600  LYS C  615  1                                  16    
HELIX   49  49 SER C  630  GLY C  641  1                                  12    
HELIX   50  50 ARG C  658  TYR C  662  5                                   5    
HELIX   51  51 ASP C  663  GLY C  672  1                                  10    
HELIX   52  52 ASN C  679  SER C  686  1                                   8    
HELIX   53  53 VAL C  688  VAL C  698  5                                  11    
HELIX   54  54 HIS C  712  GLY C  727  1                                  16    
HELIX   55  55 SER C  744  PHE C  763  1                                  20    
HELIX   56  56 THR D   44  ASN D   51  1                                   8    
HELIX   57  57 ASP D  200  VAL D  207  1                                   8    
HELIX   58  58 PRO D  290  ILE D  295  1                                   6    
HELIX   59  59 GLU D  421  MET D  425  5                                   5    
HELIX   60  60 ASN D  497  GLN D  505  1                                   9    
HELIX   61  61 ASN D  562  THR D  570  1                                   9    
HELIX   62  62 GLY D  587  HIS D  592  1                                   6    
HELIX   63  63 ALA D  593  ASN D  595  5                                   3    
HELIX   64  64 THR D  600  LYS D  615  1                                  16    
HELIX   65  65 SER D  630  GLY D  641  1                                  12    
HELIX   66  66 ARG D  658  TYR D  662  5                                   5    
HELIX   67  67 ASP D  663  GLY D  672  1                                  10    
HELIX   68  68 ASN D  679  SER D  686  1                                   8    
HELIX   69  69 THR D  687  VAL D  698  5                                  12    
HELIX   70  70 HIS D  712  VAL D  726  1                                  15    
HELIX   71  71 SER D  744  PHE D  763  1                                  20    
SHEET    1   A 4 ARG A  61  TRP A  62  0                                        
SHEET    2   A 4 GLU A  67  TYR A  70 -1  O  LEU A  69   N  ARG A  61           
SHEET    3   A 4 ILE A  76  ASN A  80 -1  O  LEU A  77   N  TYR A  70           
SHEET    4   A 4 SER A  86  LEU A  90 -1  O  PHE A  89   N  ILE A  76           
SHEET    1   B 4 ASP A 104  ILE A 107  0                                        
SHEET    2   B 4 PHE A 113  LYS A 122 -1  O  GLU A 117   N  ASP A 104           
SHEET    3   B 4 TYR A 128  ASP A 136 -1  O  SER A 131   N  TYR A 118           
SHEET    4   B 4 GLN A 141  LEU A 142 -1  O  GLN A 141   N  ASP A 136           
SHEET    1   C 4 THR A 152  TRP A 157  0                                        
SHEET    2   C 4 LEU A 164  TRP A 168 -1  O  VAL A 167   N  TRP A 154           
SHEET    3   C 4 ASP A 171  LYS A 175 -1  O  LYS A 175   N  LEU A 164           
SHEET    4   C 4 TYR A 183  ARG A 184 -1  O  TYR A 183   N  VAL A 174           
SHEET    1   D 3 ILE A 194  ASN A 196  0                                        
SHEET    2   D 3 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   D 3 LEU A 214  TRP A 216 -1  N  TRP A 215   O  ALA A 224           
SHEET    1   E 4 ILE A 194  ASN A 196  0                                        
SHEET    2   E 4 PHE A 222  ASN A 229 -1  O  PHE A 228   N  TYR A 195           
SHEET    3   E 4 THR A 265  ASN A 272 -1  O  VAL A 271   N  LEU A 223           
SHEET    4   E 4 SER A 284  GLN A 286 -1  O  ILE A 285   N  VAL A 270           
SHEET    1   F 2 LEU A 235  PHE A 240  0                                        
SHEET    2   F 2 LYS A 250  PRO A 255 -1  O  VAL A 252   N  TYR A 238           
SHEET    1   G 4 HIS A 298  THR A 307  0                                        
SHEET    2   G 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3   G 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   G 4 TRP A 337  CYS A 339 -1  O  ASN A 338   N  ASP A 329           
SHEET    1   H 4 HIS A 298  THR A 307  0                                        
SHEET    2   H 4 ARG A 310  ARG A 317 -1  O  ARG A 310   N  ALA A 306           
SHEET    3   H 4 TYR A 322  TYR A 330 -1  O  CYS A 328   N  ILE A 311           
SHEET    4   H 4 HIS A 345  MET A 348 -1  O  HIS A 345   N  MET A 325           
SHEET    1   I 4 HIS A 363  PHE A 364  0                                        
SHEET    2   I 4 SER A 370  SER A 376 -1  O  TYR A 372   N  HIS A 363           
SHEET    3   I 4 ARG A 382  GLN A 388 -1  O  PHE A 387   N  PHE A 371           
SHEET    4   I 4 THR A 395  PHE A 396 -1  O  THR A 395   N  TYR A 386           
SHEET    1   J 4 VAL A 404  LEU A 410  0                                        
SHEET    2   J 4 TYR A 414  SER A 419 -1  O  TYR A 416   N  ALA A 409           
SHEET    3   J 4 ASN A 430  GLN A 435 -1  O  TYR A 432   N  TYR A 417           
SHEET    4   J 4 VAL A 442  CYS A 444 -1  O  THR A 443   N  LYS A 433           
SHEET    1   K 4 TYR A 457  PHE A 461  0                                        
SHEET    2   K 4 TYR A 467  CYS A 472 -1  O  ARG A 471   N  SER A 458           
SHEET    3   K 4 LEU A 479  SER A 484 -1  O  THR A 481   N  LEU A 470           
SHEET    4   K 4 GLY A 490  GLU A 495 -1  O  LEU A 494   N  TYR A 480           
SHEET    1   L 8 SER A 511  ILE A 518  0                                        
SHEET    2   L 8 LYS A 523  LEU A 530 -1  O  TYR A 526   N  ASP A 515           
SHEET    3   L 8 ILE A 574  ASP A 579 -1  O  ASP A 579   N  TRP A 525           
SHEET    4   L 8 TYR A 540  VAL A 546  1  N  ASP A 545   O  ALA A 576           
SHEET    5   L 8 VAL A 619  TRP A 629  1  O  ALA A 625   N  LEU A 544           
SHEET    6   L 8 CYS A 649  VAL A 653  1  O  VAL A 653   N  GLY A 628           
SHEET    7   L 8 GLU A 699  GLY A 705  1  O  LEU A 701   N  ALA A 652           
SHEET    8   L 8 GLN A 731  TYR A 735  1  O  GLN A 731   N  TYR A 700           
SHEET    1   M 4 ARG B  61  TRP B  62  0                                        
SHEET    2   M 4 GLU B  67  TYR B  70 -1  O  LEU B  69   N  ARG B  61           
SHEET    3   M 4 ILE B  76  ASN B  80 -1  O  LEU B  77   N  TYR B  70           
SHEET    4   M 4 SER B  86  LEU B  90 -1  O  LEU B  90   N  ILE B  76           
SHEET    1   N 4 ASP B 104  ILE B 107  0                                        
SHEET    2   N 4 PHE B 113  LYS B 122 -1  O  GLU B 117   N  ASP B 104           
SHEET    3   N 4 TYR B 128  ASP B 136 -1  O  SER B 131   N  TYR B 118           
SHEET    4   N 4 GLN B 141  LEU B 142 -1  O  GLN B 141   N  ASP B 136           
SHEET    1   O 4 THR B 152  TRP B 157  0                                        
SHEET    2   O 4 LEU B 164  TRP B 168 -1  O  VAL B 167   N  GLN B 153           
SHEET    3   O 4 ASP B 171  LYS B 175 -1  O  LYS B 175   N  LEU B 164           
SHEET    4   O 4 TYR B 183  ARG B 184 -1  O  TYR B 183   N  VAL B 174           
SHEET    1   P 3 ILE B 194  ASN B 196  0                                        
SHEET    2   P 3 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   P 3 LEU B 214  TRP B 216 -1  N  TRP B 215   O  ALA B 224           
SHEET    1   Q 4 ILE B 194  ASN B 196  0                                        
SHEET    2   Q 4 PHE B 222  ASN B 229 -1  O  PHE B 228   N  TYR B 195           
SHEET    3   Q 4 THR B 265  ASN B 272 -1  O  PHE B 269   N  TYR B 225           
SHEET    4   Q 4 SER B 284  ILE B 287 -1  O  ILE B 285   N  VAL B 270           
SHEET    1   R 2 LEU B 235  PHE B 240  0                                        
SHEET    2   R 2 LYS B 250  PRO B 255 -1  O  LYS B 250   N  PHE B 240           
SHEET    1   S 4 HIS B 298  THR B 307  0                                        
SHEET    2   S 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   S 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4   S 4 ARG B 336  CYS B 339 -1  O  ARG B 336   N  ASP B 331           
SHEET    1   T 4 HIS B 298  THR B 307  0                                        
SHEET    2   T 4 ARG B 310  ARG B 317 -1  O  ARG B 310   N  ALA B 306           
SHEET    3   T 4 TYR B 322  ASP B 331 -1  O  CYS B 328   N  ILE B 311           
SHEET    4   T 4 HIS B 345  MET B 348 -1  O  HIS B 345   N  MET B 325           
SHEET    1   U 4 HIS B 363  PHE B 364  0                                        
SHEET    2   U 4 SER B 370  SER B 376 -1  O  TYR B 372   N  HIS B 363           
SHEET    3   U 4 ARG B 382  GLN B 388 -1  O  PHE B 387   N  PHE B 371           
SHEET    4   U 4 THR B 395  PHE B 396 -1  O  THR B 395   N  TYR B 386           
SHEET    1   V 4 VAL B 404  LEU B 410  0                                        
SHEET    2   V 4 TYR B 414  SER B 419 -1  O  TYR B 416   N  ALA B 409           
SHEET    3   V 4 ASN B 430  GLN B 435 -1  O  TYR B 432   N  TYR B 417           
SHEET    4   V 4 ASP B 438  CYS B 444 -1  O  THR B 443   N  LYS B 433           
SHEET    1   W 4 TYR B 457  PHE B 461  0                                        
SHEET    2   W 4 TYR B 467  CYS B 472 -1  O  ARG B 471   N  SER B 458           
SHEET    3   W 4 LEU B 479  SER B 484 -1  O  LEU B 479   N  CYS B 472           
SHEET    4   W 4 GLY B 490  GLU B 495 -1  O  LEU B 491   N  LEU B 482           
SHEET    1   X 8 SER B 511  LEU B 519  0                                        
SHEET    2   X 8 THR B 522  LEU B 530 -1  O  TYR B 526   N  ASP B 515           
SHEET    3   X 8 ILE B 574  PHE B 578 -1  O  VAL B 575   N  ILE B 529           
SHEET    4   X 8 TYR B 540  VAL B 546  1  N  ASP B 545   O  ALA B 576           
SHEET    5   X 8 VAL B 619  TRP B 629  1  O  ALA B 625   N  LEU B 544           
SHEET    6   X 8 CYS B 649  VAL B 653  1  O  VAL B 653   N  GLY B 628           
SHEET    7   X 8 GLU B 699  GLY B 705  1  O  ILE B 703   N  ALA B 652           
SHEET    8   X 8 GLN B 731  TYR B 735  1  O  GLN B 731   N  TYR B 700           
SHEET    1   Y 4 LEU C  60  TRP C  62  0                                        
SHEET    2   Y 4 GLU C  67  TYR C  70 -1  O  LEU C  69   N  ARG C  61           
SHEET    3   Y 4 ILE C  76  ASN C  80 -1  O  PHE C  79   N  TYR C  68           
SHEET    4   Y 4 SER C  86  LEU C  90 -1  O  LEU C  90   N  ILE C  76           
SHEET    1   Z 7 ASP C 104  ILE C 107  0                                        
SHEET    2   Z 7 PHE C 113  LYS C 122 -1  O  GLU C 117   N  ASP C 104           
SHEET    3   Z 7 TYR C 128  ASP C 136 -1  O  SER C 131   N  TYR C 118           
SHEET    4   Z 7 ILE C 148  TRP C 157 -1  O  THR C 152   N  ALA C 130           
SHEET    5   Z 7 LEU C 164  TRP C 168 -1  O  VAL C 167   N  GLN C 153           
SHEET    6   Z 7 ASP C 171  LYS C 175 -1  O  LYS C 175   N  LEU C 164           
SHEET    7   Z 7 TYR C 183  ARG C 184 -1  O  TYR C 183   N  VAL C 174           
SHEET    1  AA 3 ILE C 194  ASN C 196  0                                        
SHEET    2  AA 3 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3  AA 3 LEU C 214  TRP C 216 -1  N  TRP C 215   O  ALA C 224           
SHEET    1  AB 4 ILE C 194  ASN C 196  0                                        
SHEET    2  AB 4 PHE C 222  ASN C 229 -1  O  PHE C 228   N  TYR C 195           
SHEET    3  AB 4 THR C 265  ASN C 272 -1  O  PHE C 269   N  TYR C 225           
SHEET    4  AB 4 ILE C 285  GLN C 286 -1  O  ILE C 285   N  VAL C 270           
SHEET    1  AC 2 LEU C 235  PHE C 240  0                                        
SHEET    2  AC 2 LYS C 250  PRO C 255 -1  O  LYS C 250   N  PHE C 240           
SHEET    1  AD 4 HIS C 298  TRP C 305  0                                        
SHEET    2  AD 4 ARG C 310  ARG C 317 -1  O  GLN C 314   N  CYS C 301           
SHEET    3  AD 4 TYR C 322  TYR C 330 -1  O  CYS C 328   N  ILE C 311           
SHEET    4  AD 4 TRP C 337  CYS C 339 -1  O  ASN C 338   N  ASP C 329           
SHEET    1  AE 4 HIS C 298  TRP C 305  0                                        
SHEET    2  AE 4 ARG C 310  ARG C 317 -1  O  GLN C 314   N  CYS C 301           
SHEET    3  AE 4 TYR C 322  TYR C 330 -1  O  CYS C 328   N  ILE C 311           
SHEET    4  AE 4 HIS C 345  MET C 348 -1  O  HIS C 345   N  MET C 325           
SHEET    1  AF 4 HIS C 363  PHE C 364  0                                        
SHEET    2  AF 4 SER C 370  SER C 376 -1  O  TYR C 372   N  HIS C 363           
SHEET    3  AF 4 ARG C 382  GLN C 388 -1  O  CYS C 385   N  LYS C 373           
SHEET    4  AF 4 THR C 395  PHE C 396 -1  O  THR C 395   N  TYR C 386           
SHEET    1  AG 4 VAL C 404  LEU C 410  0                                        
SHEET    2  AG 4 TYR C 414  SER C 419 -1  O  ILE C 418   N  ILE C 405           
SHEET    3  AG 4 ASN C 430  GLN C 435 -1  O  TYR C 432   N  TYR C 417           
SHEET    4  AG 4 VAL C 442  CYS C 444 -1  O  THR C 443   N  LYS C 433           
SHEET    1  AH 4 TYR C 457  PHE C 461  0                                        
SHEET    2  AH 4 TYR C 467  CYS C 472 -1  O  GLN C 469   N  SER C 460           
SHEET    3  AH 4 LEU C 479  SER C 484 -1  O  HIS C 483   N  TYR C 468           
SHEET    4  AH 4 GLY C 490  GLU C 495 -1  O  GLU C 495   N  TYR C 480           
SHEET    1  AI 8 SER C 511  LEU C 519  0                                        
SHEET    2  AI 8 THR C 522  LEU C 530 -1  O  LEU C 530   N  SER C 511           
SHEET    3  AI 8 ILE C 574  ASP C 579 -1  O  VAL C 575   N  ILE C 529           
SHEET    4  AI 8 TYR C 540  VAL C 546  1  N  ASP C 545   O  ALA C 576           
SHEET    5  AI 8 VAL C 619  TRP C 629  1  O  ALA C 625   N  LEU C 542           
SHEET    6  AI 8 CYS C 649  VAL C 653  1  O  VAL C 653   N  GLY C 628           
SHEET    7  AI 8 GLU C 699  GLY C 705  1  O  ILE C 703   N  ALA C 652           
SHEET    8  AI 8 GLN C 731  TYR C 735  1  O  GLN C 731   N  TYR C 700           
SHEET    1  AJ 4 ARG D  61  TRP D  62  0                                        
SHEET    2  AJ 4 GLU D  67  TYR D  70 -1  O  LEU D  69   N  ARG D  61           
SHEET    3  AJ 4 ILE D  76  ASN D  80 -1  O  LEU D  77   N  TYR D  70           
SHEET    4  AJ 4 SER D  86  LEU D  90 -1  O  LEU D  90   N  ILE D  76           
SHEET    1  AK 3 ASP D 104  ILE D 107  0                                        
SHEET    2  AK 3 PHE D 113  LYS D 122 -1  O  LEU D 115   N  SER D 106           
SHEET    3  AK 3 TYR D 128  ASP D 136 -1  O  SER D 131   N  TYR D 118           
SHEET    1  AL 4 THR D 152  TRP D 157  0                                        
SHEET    2  AL 4 LEU D 164  TRP D 168 -1  O  VAL D 167   N  GLN D 153           
SHEET    3  AL 4 ASP D 171  LYS D 175 -1  O  LYS D 175   N  LEU D 164           
SHEET    4  AL 4 TYR D 183  ARG D 184 -1  O  TYR D 183   N  VAL D 174           
SHEET    1  AM 3 ILE D 194  ASN D 196  0                                        
SHEET    2  AM 3 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3  AM 3 LEU D 214  TRP D 216 -1  N  TRP D 215   O  ALA D 224           
SHEET    1  AN 4 ILE D 194  ASN D 196  0                                        
SHEET    2  AN 4 PHE D 222  ASN D 229 -1  O  PHE D 228   N  TYR D 195           
SHEET    3  AN 4 THR D 265  ASN D 272 -1  O  PHE D 269   N  TYR D 225           
SHEET    4  AN 4 ILE D 285  ILE D 287 -1  O  ILE D 285   N  VAL D 270           
SHEET    1  AO 2 LEU D 235  PHE D 240  0                                        
SHEET    2  AO 2 LYS D 250  PRO D 255 -1  O  VAL D 252   N  TYR D 238           
SHEET    1  AP 4 HIS D 298  TRP D 305  0                                        
SHEET    2  AP 4 ARG D 310  ARG D 317 -1  O  LEU D 316   N  TYR D 299           
SHEET    3  AP 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4  AP 4 TRP D 337  ASN D 338 -1  O  ASN D 338   N  ASP D 329           
SHEET    1  AQ 4 HIS D 298  TRP D 305  0                                        
SHEET    2  AQ 4 ARG D 310  ARG D 317 -1  O  LEU D 316   N  TYR D 299           
SHEET    3  AQ 4 TYR D 322  TYR D 330 -1  O  ASP D 326   N  LEU D 313           
SHEET    4  AQ 4 HIS D 345  MET D 348 -1  O  GLU D 347   N  SER D 323           
SHEET    1  AR 4 HIS D 363  PHE D 364  0                                        
SHEET    2  AR 4 SER D 370  SER D 376 -1  O  TYR D 372   N  HIS D 363           
SHEET    3  AR 4 ARG D 382  GLN D 388 -1  O  PHE D 387   N  PHE D 371           
SHEET    4  AR 4 CYS D 394  PHE D 396 -1  O  THR D 395   N  TYR D 386           
SHEET    1  AS 4 VAL D 404  LEU D 410  0                                        
SHEET    2  AS 4 TYR D 414  SER D 419 -1  O  ILE D 418   N  ILE D 405           
SHEET    3  AS 4 ASN D 430  GLN D 435 -1  O  TYR D 432   N  TYR D 417           
SHEET    4  AS 4 VAL D 442  CYS D 444 -1  O  THR D 443   N  LYS D 433           
SHEET    1  AT 4 TYR D 457  PHE D 461  0                                        
SHEET    2  AT 4 TYR D 467  CYS D 472 -1  O  ARG D 471   N  SER D 458           
SHEET    3  AT 4 LEU D 479  SER D 484 -1  O  HIS D 483   N  TYR D 468           
SHEET    4  AT 4 GLY D 490  GLU D 495 -1  O  GLU D 495   N  TYR D 480           
SHEET    1  AU 8 SER D 511  LEU D 519  0                                        
SHEET    2  AU 8 THR D 522  LEU D 530 -1  O  TYR D 526   N  ASP D 515           
SHEET    3  AU 8 ILE D 574  PHE D 578 -1  O  VAL D 575   N  ILE D 529           
SHEET    4  AU 8 TYR D 540  ASP D 545  1  N  ASP D 545   O  ALA D 576           
SHEET    5  AU 8 VAL D 619  TRP D 629  1  O  ALA D 625   N  LEU D 544           
SHEET    6  AU 8 CYS D 649  VAL D 653  1  O  VAL D 653   N  GLY D 628           
SHEET    7  AU 8 GLU D 699  GLY D 705  1  O  LEU D 701   N  ALA D 652           
SHEET    8  AU 8 GLN D 731  TYR D 735  1  O  GLN D 731   N  TYR D 700           
SSBOND   1 CYS A  328    CYS A  339                        1555   1555    2.03  
SSBOND   2 CYS A  385    CYS A  394                        1555   1555    2.04  
SSBOND   3 CYS A  444    CYS A  447                        1555   1555    2.02  
SSBOND   4 CYS A  454    CYS A  472                        1555   1555    2.06  
SSBOND   5 CYS A  649    CYS A  762                        1555   1555    2.04  
SSBOND   6 CYS B  328    CYS B  339                        1555   1555    2.03  
SSBOND   7 CYS B  385    CYS B  394                        1555   1555    2.04  
SSBOND   8 CYS B  444    CYS B  447                        1555   1555    2.02  
SSBOND   9 CYS B  454    CYS B  472                        1555   1555    2.05  
SSBOND  10 CYS B  649    CYS B  762                        1555   1555    2.05  
SSBOND  11 CYS C  328    CYS C  339                        1555   1555    2.04  
SSBOND  12 CYS C  385    CYS C  394                        1555   1555    2.04  
SSBOND  13 CYS C  444    CYS C  447                        1555   1555    2.03  
SSBOND  14 CYS C  454    CYS C  472                        1555   1555    2.04  
SSBOND  15 CYS C  649    CYS C  762                        1555   1555    2.04  
SSBOND  16 CYS D  328    CYS D  339                        1555   1555    2.04  
SSBOND  17 CYS D  385    CYS D  394                        1555   1555    2.04  
SSBOND  18 CYS D  444    CYS D  447                        1555   1555    2.03  
SSBOND  19 CYS D  454    CYS D  472                        1555   1555    2.04  
SSBOND  20 CYS D  649    CYS D  762                        1555   1555    2.04  
LINK         ND2 ASN A  85                 C1  NAG A 801   1555   1555    1.45  
LINK         ND2 ASN A 150                 C1  NAG A 802   1555   1555    1.46  
LINK         ND2 ASN A 219                 C1  NAG A 803   1555   1555    1.45  
LINK         ND2 ASN A 229                 C1  NAG A 804   1555   1555    1.44  
LINK         ND2 ASN A 281                 C1  NAG A 806   1555   1555    1.46  
LINK         ND2 ASN A 321                 C1  NAG A 808   1555   1555    1.45  
LINK         ND2 ASN B  85                 C1  NAG B 801   1555   1555    1.46  
LINK         ND2 ASN B 150                 C1  NAG B 802   1555   1555    1.46  
LINK         ND2 ASN B 219                 C1  NAG B 803   1555   1555    1.45  
LINK         ND2 ASN B 229                 C1  NAG B 804   1555   1555    1.44  
LINK         ND2 ASN B 281                 C1  NAG B 806   1555   1555    1.46  
LINK         ND2 ASN C 150                 C1  NAG C 801   1555   1555    1.45  
LINK         ND2 ASN C 219                 C1  NAG C 802   1555   1555    1.44  
LINK         ND2 ASN C 229                 C1  NAG C 803   1555   1555    1.45  
LINK         ND2 ASN D 150                 C1  NAG D 801   1555   1555    1.45  
LINK         ND2 ASN D 229                 C1  NAG D 802   1555   1555    1.45  
LINK         ND2 ASN D 281                 C1  NAG D 804   1555   1555    1.46  
LINK         O4  NAG A 804                 C1  NAG A 805   1555   1555    1.45  
LINK         O4  NAG A 806                 C1  NAG A 807   1555   1555    1.45  
LINK         O4  NAG B 804                 C1  NAG B 805   1555   1555    1.44  
LINK         O4  NAG C 803                 C1  NAG C 804   1555   1555    1.44  
LINK         O4  NAG D 802                 C1  NAG D 803   1555   1555    1.45  
SITE     1 AC1  2 ASN A  85  SER A  87                                          
SITE     1 AC2  2 ILE A 148  ASN A 150                                          
SITE     1 AC3  4 ASN A 219  THR A 221  GLN A 308  GLU A 309                    
SITE     1 AC4  4 ILE A 194  ASN A 229  THR A 231  GLU A 232                    
SITE     1 AC5  2 TRP A 187  ASN A 281                                          
SITE     1 AC6  1 TRP A 187                                                     
SITE     1 AC7  3 ILE A 319  ASN A 321  SER A 349                               
SITE     1 AC8  3 ARG B 147  ILE B 148  ASN B 150                               
SITE     1 AC9  4 ASN B 219  THR B 221  GLN B 308  GLU B 309                    
SITE     1 BC1  3 ILE B 194  ASN B 229  THR B 231                               
SITE     1 BC2  1 GLU B 232                                                     
SITE     1 BC3  4 ASN C 219  THR C 221  GLN C 308  GLU C 309                    
SITE     1 BC4  3 GLN C 227  ASN C 229  THR C 231                               
SITE     1 BC5  1 GLU C 232                                                     
SITE     1 BC6  3 ARG D 147  ILE D 148  ASN D 150                               
SITE     1 BC7  4 ILE D 194  ASN D 229  THR D 231  GLU D 232                    
SITE     1 BC8  2 TRP D 187  ASN D 281                                          
SITE     1 BC9  6 ARG A 125  GLU A 205  GLU A 206  TYR A 547                    
SITE     2 BC9  6 SER A 630  TYR A 662                                          
SITE     1 CC1  8 ARG B 125  GLU B 205  GLU B 206  TYR B 547                    
SITE     2 CC1  8 SER B 630  TYR B 662  TYR B 666  HIS B 740                    
SITE     1 CC2  6 ARG C 125  GLU C 205  GLU C 206  TYR C 547                    
SITE     2 CC2  6 TYR C 662  TYR C 666                                          
SITE     1 CC3  7 ARG D 125  GLU D 205  GLU D 206  TYR D 547                    
SITE     2 CC3  7 SER D 630  TYR D 662  TYR D 666                               
CRYST1  122.086  123.010  144.651  90.00 114.84  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008191  0.000000  0.003791        0.00000                         
SCALE2      0.000000  0.008129  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007618        0.00000                         
TER    5936      PRO A 766                                                      
TER   11902      PRO B 766                                                      
TER   17839      PRO C 766                                                      
TER   23769      PRO D 766                                                      
MASTER      548    0   26   71  194    0   25    624805    4  421  228          
END                                                                             

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