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LongText Report for: 7zxs-pdb

Name Class
7zxs-pdb
HEADER    HYDROLASE                               22-MAY-22   7ZXS              
TITLE     CRYSTAL STRUCTURE OF DPP9 IN COMPLEX WITH A 4-OXO-B-LACTAM BASED      
TITLE    2 INHIBITOR, A295                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 9;                                    
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: EXTCOLOR{RED}{>FRAGMENT<};                                 
COMPND   5 SYNONYM: DP9,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2,DPRP-2,       
COMPND   6 DIPEPTIDYL PEPTIDASE IX,DPP IX,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 9,  
COMPND   7 DPLP9;                                                               
COMPND   8 EC: 3.4.14.5;                                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: DIPEPTIDYL PEPTIDASE 9;                                    
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 SYNONYM: DP9,DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2,DPRP-2,       
COMPND  14 DIPEPTIDYL PEPTIDASE IX,DPP IX,DIPEPTIDYL PEPTIDASE-LIKE PROTEIN 9,  
COMPND  15 DPLP9;                                                               
COMPND  16 EC: 3.4.14.5;                                                        
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DPP9, DPRP2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: DPP9, DPRP2;                                                   
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    DIPEPTIDYL PEPTIDASE, DPP9, HYDROLASE                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ROSS,R.HUBER                                                        
REVDAT   1   28-SEP-22 7ZXS    0                                                
JRNL        AUTH   L.A.R.CARVALHO,B.ROSS,L.FEHR,O.BOLGI,S.WOHRLE,K.M.LUM,       
JRNL        AUTH 2 D.PODLESAINSKI,A.C.VIEIRA,R.KIEFERSAUER,R.FELIX,T.RODRIGUES, 
JRNL        AUTH 3 S.D.LUCAS,O.GROSS,R.GEISS-FRIEDLANDER,B.F.CRAVATT,R.HUBER,   
JRNL        AUTH 4 M.KAISER,R.MOREIRA                                           
JRNL        TITL   CHEMOPROTEOMICS-ENABLED IDENTIFICATION OF 4-OXO-BETA-LACTAMS 
JRNL        TITL 2 AS INHIBITORS OF DIPEPTIDYL PEPTIDASES 8 AND 9.              
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.                    2022              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   36089535                                                     
JRNL        DOI    10.1002/ANIE.202210498                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 106.09                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 64.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 219248                         
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1707                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1059                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 4.22                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 10                           
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 27210                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 321                                     
REMARK   3   SOLVENT ATOMS            : 1653                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.04000                                             
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.07000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : -0.06000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.193         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.678         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 27958 ; 0.005 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A): 25440 ; 0.002 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 37983 ; 1.357 ; 1.649       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 58559 ; 1.191 ; 1.573       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3417 ; 7.188 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1439 ;31.955 ;22.147       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  4295 ;12.978 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   147 ;19.179 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3454 ; 0.061 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 31833 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  6645 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    22    865       B    22    865    9791 0.030 0.050     
REMARK   3    2     A    22    865       C    22    865    9765 0.030 0.050     
REMARK   3    3     A    22    865       D    22    865    9696 0.030 0.050     
REMARK   3    4     B    21    865       C    21    865    9845 0.030 0.050     
REMARK   3    5     B    22    864       D    22    864    9790 0.030 0.050     
REMARK   3    6     C    22    865       D    22    865    9817 0.020 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7ZXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292123050.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-22                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : X-GEN                              
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 220955                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.807                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 106.900                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 64.6                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200   FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 15.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.45900                            
REMARK 200   FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6EOR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTAL IS GROWN IN A CONDITION      
REMARK 280  CONTAINING PEG 2K MME BUFFERED BY TRIS PH 7, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,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                                                                      
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 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A    20                                                      
REMARK 465     ALA A    21                                                      
REMARK 465     HIS A   866                                                      
REMARK 465     HIS A   867                                                      
REMARK 465     HIS A   868                                                      
REMARK 465     HIS A   869                                                      
REMARK 465     TYR B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     LEU B    47                                                      
REMARK 465     ILE B    48                                                      
REMARK 465     VAL B    49                                                      
REMARK 465     ASN B    50                                                      
REMARK 465     HIS B   866                                                      
REMARK 465     HIS B   867                                                      
REMARK 465     HIS B   868                                                      
REMARK 465     HIS B   869                                                      
REMARK 465     PRO C    20                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     VAL C   120                                                      
REMARK 465     HIS C   866                                                      
REMARK 465     HIS C   867                                                      
REMARK 465     HIS C   868                                                      
REMARK 465     HIS C   869                                                      
REMARK 465     PRO D    20                                                      
REMARK 465     ALA D    21                                                      
REMARK 465     TYR D    44                                                      
REMARK 465     SER D    45                                                      
REMARK 465     GLY D    46                                                      
REMARK 465     LEU D    47                                                      
REMARK 465     ILE D    48                                                      
REMARK 465     VAL D    49                                                      
REMARK 465     HIS D   866                                                      
REMARK 465     HIS D   867                                                      
REMARK 465     HIS D   868                                                      
REMARK 465     HIS D   869                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A   28   CE   NZ                                             
REMARK 480     LYS A   43   NZ                                                  
REMARK 480     ASN A   50   CG   OD1  ND2                                       
REMARK 480     LYS A   51   CG   CD   CE   NZ                                   
REMARK 480     THR A   62   OG1  CG2                                            
REMARK 480     TYR A   79   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     ARG A   82   CD   NE   CZ   NH1  NH2                             
REMARK 480     ILE A   91   CD1                                                 
REMARK 480     LYS A   93   NZ                                                  
REMARK 480     LYS A   94   CD   CE   NZ                                        
REMARK 480     ARG A   96   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A   97   CG   CD   CE   NZ                                   
REMARK 480     GLU A   98   CG   CD   OE1  OE2                                  
REMARK 480     GLN A  113   CD   OE1  NE2                                       
REMARK 480     HIS A  117   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LYS A  132   NZ                                                  
REMARK 480     ILE A  139   CD1                                                 
REMARK 480     GLU A  147   CD   OE1  OE2                                       
REMARK 480     LYS A  167   CD   CE   NZ                                        
REMARK 480     ASN A  168   CG   OD1  ND2                                       
REMARK 480     MET A  175   CE                                                  
REMARK 480     LYS A  176   CD   CE   NZ                                        
REMARK 480     LEU A  178   CD1  CD2                                            
REMARK 480     LYS A  181   CD   CE   NZ                                        
REMARK 480     SER A  267   OG                                                  
REMARK 480     GLU A  268   CD   OE1  OE2                                       
REMARK 480     LYS A  299   NZ                                                  
REMARK 480     LYS A  311   NZ                                                  
REMARK 480     SER A  326   OG                                                  
REMARK 480     GLN A  327   CD   OE1  NE2                                       
REMARK 480     LYS A  329   CE   NZ                                             
REMARK 480     ILE A  330   CD1                                                 
REMARK 480     LYS A  348   NZ                                                  
REMARK 480     LYS A  362   CE   NZ                                             
REMARK 480     GLU A  391   CG   CD   OE1  OE2                                  
REMARK 480     GLU A  394   CG   CD   OE1  OE2                                  
REMARK 480     ILE A  426   CD1                                                 
REMARK 480     LYS A  462   CG   CD   CE   NZ                                   
REMARK 480     GLU A  470   CD   OE1  OE2                                       
REMARK 480     PHE A  472   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     SER A  473   OG                                                  
REMARK 480     GLU A  476   CG   CD   OE1  OE2                                  
REMARK 480     LYS A  480   NZ                                                  
REMARK 480     LYS A  503   NZ                                                  
REMARK 480     GLU A  509   CD   OE1  OE2                                       
REMARK 480     GLU A  533   CD   OE1  OE2                                       
REMARK 480     MET A  558   CE                                                  
REMARK 480     LYS A  576   CE   NZ                                             
REMARK 480     GLN A  588   CD   OE1  NE2                                       
REMARK 480     ARG A  590   CZ   NH1  NH2                                       
REMARK 480     SER A  600   OG                                                  
REMARK 480     ASP A  618   CG   OD1  OD2                                       
REMARK 480     GLN A  632   CD   OE1  NE2                                       
REMARK 480     LYS A  635   NZ                                                  
REMARK 480     LYS A  660   NZ                                                  
REMARK 480     LYS A  748   CE   NZ                                             
REMARK 480     GLN A  778   CD   OE1  NE2                                       
REMARK 480     LYS B   43   CE   NZ                                             
REMARK 480     LYS B   51   CD   CE   NZ                                        
REMARK 480     GLU B   64   CG   CD   OE1  OE2                                  
REMARK 480     TYR B   79   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     ARG B   82   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B   94   CD   CE   NZ                                        
REMARK 480     ARG B   96   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B   97   CD   CE   NZ                                        
REMARK 480     GLU B   98   CG   CD   OE1  OE2                                  
REMARK 480     LEU B  100   CD1  CD2                                            
REMARK 480     LEU B  102   CD1  CD2                                            
REMARK 480     LYS B  106   CE   NZ                                             
REMARK 480     GLN B  113   CD   OE1  NE2                                       
REMARK 480     HIS B  117   CG   ND1  CD2  CE1  NE2                             
REMARK 480     HIS B  118   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU B  147   CD   OE1  OE2                                       
REMARK 480     LYS B  167   CD   CE   NZ                                        
REMARK 480     ASN B  168   CG   OD1  ND2                                       
REMARK 480     MET B  175   CE                                                  
REMARK 480     LYS B  176   CD   CE   NZ                                        
REMARK 480     LYS B  181   CD   CE   NZ                                        
REMARK 480     ILE B  214   CD1                                                 
REMARK 480     SER B  267   OG                                                  
REMARK 480     GLU B  268   CD   OE1  OE2                                       
REMARK 480     GLU B  297   CD   OE1  OE2                                       
REMARK 480     LYS B  299   NZ                                                  
REMARK 480     LYS B  314   NZ                                                  
REMARK 480     SER B  326   OG                                                  
REMARK 480     GLN B  327   CG   CD   OE1  NE2                                  
REMARK 480     LYS B  329   NZ                                                  
REMARK 480     LYS B  348   CE   NZ                                             
REMARK 480     GLU B  391   CD   OE1  OE2                                       
REMARK 480     GLU B  393   CD   OE1  OE2                                       
REMARK 480     LYS B  462   CD   CE   NZ                                        
REMARK 480     GLU B  470   CD   OE1  OE2                                       
REMARK 480     GLU B  476   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  484   NZ                                                  
REMARK 480     LYS B  503   CE   NZ                                             
REMARK 480     GLU B  509   CD   OE1  OE2                                       
REMARK 480     LYS B  576   NZ                                                  
REMARK 480     ARG B  590   CZ   NH1  NH2                                       
REMARK 480     SER B  600   OG                                                  
REMARK 480     LYS B  660   CE   NZ                                             
REMARK 480     ARG B  688   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  791   CD   OE1  OE2                                       
REMARK 480     LYS B  792   NZ                                                  
REMARK 480     LYS C   28   NZ                                                  
REMARK 480     LYS C   43   CD   CE   NZ                                        
REMARK 480     TYR C   44   CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 480     SER C   45   OG                                                  
REMARK 480     LEU C   47   CD1  CD2                                            
REMARK 480     ILE C   48   CD1                                                 
REMARK 480     VAL C   49   CG1  CG2                                            
REMARK 480     ASN C   50   CG   OD1  ND2                                       
REMARK 480     LYS C   51   CG   CD   CE   NZ                                   
REMARK 480     GLU C   64   CD   OE1  OE2                                       
REMARK 480     ARG C   82   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS C   94   CE   NZ                                             
REMARK 480     ARG C   96   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS C   97   CG   CD   CE   NZ                                   
REMARK 480     GLU C   98   CG   CD   OE1  OE2                                  
REMARK 480     ASP C  110   CG   OD1  OD2                                       
REMARK 480     HIS C  111   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLN C  113   CD   OE1  NE2                                       
REMARK 480     HIS C  117   CG   ND1  CD2  CE1  NE2                             
REMARK 480     HIS C  118   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU C  124   CD   OE1  OE2                                       
REMARK 480     LYS C  132   NZ                                                  
REMARK 480     ARG C  133   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     VAL C  136   CG1  CG2                                            
REMARK 480     GLU C  147   CD   OE1  OE2                                       
REMARK 480     SER C  156   OG                                                  
REMARK 480     LYS C  167   CG   CD   CE   NZ                                   
REMARK 480     ASN C  168   CG   OD1  ND2                                       
REMARK 480     SER C  173   OG                                                  
REMARK 480     LYS C  176   CG   CD   CE   NZ                                   
REMARK 480     LYS C  181   CE   NZ                                             
REMARK 480     ILE C  214   CD1                                                 
REMARK 480     LYS C  237   NZ                                                  
REMARK 480     SER C  267   OG                                                  
REMARK 480     LYS C  299   NZ                                                  
REMARK 480     LYS C  311   NZ                                                  
REMARK 480     GLN C  327   CD   OE1  NE2                                       
REMARK 480     LYS C  348   NZ                                                  
REMARK 480     GLU C  394   CD   OE1  OE2                                       
REMARK 480     GLU C  434   CG   CD   OE1  OE2                                  
REMARK 480     GLU C  476   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  480   NZ                                                  
REMARK 480     GLU C  509   CD   OE1  OE2                                       
REMARK 480     GLU C  533   CG   CD   OE1  OE2                                  
REMARK 480     LYS C  576   NZ                                                  
REMARK 480     ARG C  590   CD   NE   CZ   NH1  NH2                             
REMARK 480     SER C  600   OG                                                  
REMARK 480     LYS C  660   NZ                                                  
REMARK 480     ARG C  688   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLN C  745   CD   OE1  NE2                                       
REMARK 480     MET C  760   CE                                                  
REMARK 480     GLU C  775   CD   OE1  OE2                                       
REMARK 480     LYS C  792   NZ                                                  
REMARK 480     GLU C  809   CD   OE1  OE2                                       
REMARK 480     ARG C  843   NE   CZ   NH1  NH2                                  
REMARK 480     LYS D   43   NZ                                                  
REMARK 480     ASN D   50   CG   OD1  ND2                                       
REMARK 480     LYS D   51   CD   CE   NZ                                        
REMARK 480     GLU D   64   CD   OE1  OE2                                       
REMARK 480     ARG D   82   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS D   94   CE   NZ                                             
REMARK 480     ARG D   96   NE   CZ   NH1  NH2                                  
REMARK 480     LYS D   97   CG   CD   CE   NZ                                   
REMARK 480     GLU D   98   CG   CD   OE1  OE2                                  
REMARK 480     ASP D  110   CG   OD1  OD2                                       
REMARK 480     GLN D  113   CG   CD   OE1  NE2                                  
REMARK 480     HIS D  117   CG   ND1  CD2  CE1  NE2                             
REMARK 480     HIS D  118   CG   ND1  CD2  CE1  NE2                             
REMARK 480     VAL D  120   CG1  CG2                                            
REMARK 480     ARG D  129   CZ   NH1  NH2                                       
REMARK 480     LYS D  132   NZ                                                  
REMARK 480     LEU D  134   CG   CD1  CD2                                       
REMARK 480     VAL D  136   CG1  CG2                                            
REMARK 480     PHE D  137   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     LYS D  167   CG   CD   CE   NZ                                   
REMARK 480     MET D  175   CE                                                  
REMARK 480     LYS D  176   NZ                                                  
REMARK 480     LYS D  181   CE   NZ                                             
REMARK 480     GLU D  268   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  299   NZ                                                  
REMARK 480     LYS D  311   NZ                                                  
REMARK 480     GLU D  393   CD   OE1  OE2                                       
REMARK 480     GLU D  394   CG   CD   OE1  OE2                                  
REMARK 480     GLN D  395   CD   OE1  NE2                                       
REMARK 480     ARG D  401   CZ   NH1  NH2                                       
REMARK 480     GLN D  464   CG   CD   OE1  NE2                                  
REMARK 480     GLU D  470   CD   OE1  OE2                                       
REMARK 480     GLU D  476   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  480   CE   NZ                                             
REMARK 480     LYS D  576   NZ                                                  
REMARK 480     SER D  600   OG                                                  
REMARK 480     GLN D  632   CD   OE1  NE2                                       
REMARK 480     LYS D  635   NZ                                                  
REMARK 480     ARG D  688   CZ   NH1  NH2                                       
REMARK 480     MET D  760   SD   CE                                             
REMARK 480     GLN D  778   CD   OE1  NE2                                       
REMARK 480     LYS D  792   NZ                                                  
REMARK 480     ARG D  843   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    GLU A  98       54.64   -102.51                                   
REMARK 500    HIS A 111       73.19     30.11                                   
REMARK 500    ALA A 155      139.98   -170.66                                   
REMARK 500    VAL A 419      -99.42    -97.13                                   
REMARK 500    THR A 521      144.22   -173.85                                   
REMARK 500    TYR A 644      -72.10   -110.41                                   
REMARK 500    GLN A 696       39.06   -144.89                                   
REMARK 500    SER A 730     -114.67     68.16                                   
REMARK 500    ALA A 754       57.06     37.66                                   
REMARK 500    ASP A 772     -176.70     66.64                                   
REMARK 500    ASN A 777       50.74   -150.28                                   
REMARK 500    ASN A 810      -67.95   -107.23                                   
REMARK 500    ARG A 839     -133.39    -81.53                                   
REMARK 500    THR B  62       52.94   -118.12                                   
REMARK 500    GLU B  98       42.21    -99.41                                   
REMARK 500    HIS B 111       74.47     30.27                                   
REMARK 500    ALA B 155      141.45   -170.94                                   
REMARK 500    VAL B 419     -100.31   -100.16                                   
REMARK 500    GLU B 493       59.90    -91.24                                   
REMARK 500    THR B 521      142.62   -175.22                                   
REMARK 500    ALA B 534       71.55   -114.43                                   
REMARK 500    TYR B 644      -73.50   -109.55                                   
REMARK 500    GLN B 696       39.44   -143.13                                   
REMARK 500    SER B 730     -114.06     70.80                                   
REMARK 500    ALA B 754       55.72     39.31                                   
REMARK 500    ASP B 772     -175.72     65.86                                   
REMARK 500    ASN B 777       52.68   -152.77                                   
REMARK 500    ASN B 810      -67.53   -107.36                                   
REMARK 500    ARG B 839     -135.10    -82.53                                   
REMARK 500    TYR C  44       45.13   -101.43                                   
REMARK 500    GLU C  98       51.81   -100.95                                   
REMARK 500    HIS C 111       75.71     28.58                                   
REMARK 500    ALA C 155      138.16   -171.32                                   
REMARK 500    VAL C 419     -100.08    -97.51                                   
REMARK 500    ASP C 437       30.21    -98.94                                   
REMARK 500    THR C 521      143.39   -172.81                                   
REMARK 500    ALA C 534       70.18   -110.55                                   
REMARK 500    TYR C 644      -73.00   -110.19                                   
REMARK 500    GLN C 696       40.15   -144.80                                   
REMARK 500    SER C 730     -113.33     69.29                                   
REMARK 500    ASP C 772     -173.39     65.41                                   
REMARK 500    ASN C 777       51.99   -151.43                                   
REMARK 500    ASN C 810      -69.59   -102.04                                   
REMARK 500    ARG C 839     -138.00    -85.11                                   
REMARK 500    ASP D  55       65.19     61.75                                   
REMARK 500    GLU D  98       52.77   -101.53                                   
REMARK 500    HIS D 111       76.24     28.34                                   
REMARK 500    VAL D 419     -100.58    -97.55                                   
REMARK 500    PHE D 479       -0.17     77.76                                   
REMARK 500    GLU D 493       58.81    -90.05                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     KBO A   901                                                      
REMARK 615     KBO B   901                                                      
REMARK 615     KBO C   901                                                      
REMARK 615     KBO D   901                                                      
DBREF  7ZXS A   20   863  UNP    Q86TI2   DPP9_HUMAN      20    863             
DBREF  7ZXS B   20   863  UNP    Q86TI2   DPP9_HUMAN      20    863             
DBREF  7ZXS C   20   863  UNP    Q86TI2   DPP9_HUMAN      20    863             
DBREF  7ZXS D   20   863  UNP    Q86TI2   DPP9_HUMAN      20    863             
SEQADV 7ZXS HIS A  864  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS A  865  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS A  866  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS A  867  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS A  868  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS A  869  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  864  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  865  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  866  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  867  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  868  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS B  869  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  864  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  865  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  866  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  867  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  868  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS C  869  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  864  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  865  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  866  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  867  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  868  UNP  Q86TI2              EXPRESSION TAG                 
SEQADV 7ZXS HIS D  869  UNP  Q86TI2              EXPRESSION TAG                 
SEQRES   1 A  850  PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP          
SEQRES   2 A  850  GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER          
SEQRES   3 A  850  GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE          
SEQRES   4 A  850  VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG          
SEQRES   5 A  850  LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN          
SEQRES   6 A  850  SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS          
SEQRES   7 A  850  GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP          
SEQRES   8 A  850  HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG          
SEQRES   9 A  850  GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL          
SEQRES  10 A  850  PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY          
SEQRES  11 A  850  LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS          
SEQRES  12 A  850  ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET          
SEQRES  13 A  850  LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG          
SEQRES  14 A  850  MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE          
SEQRES  15 A  850  SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE          
SEQRES  16 A  850  GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN          
SEQRES  17 A  850  GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY          
SEQRES  18 A  850  VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE          
SEQRES  19 A  850  THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY          
SEQRES  20 A  850  SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU          
SEQRES  21 A  850  VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER          
SEQRES  22 A  850  PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR          
SEQRES  23 A  850  PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS          
SEQRES  24 A  850  LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL          
SEQRES  25 A  850  SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER          
SEQRES  26 A  850  LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP          
SEQRES  27 A  850  THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP          
SEQRES  28 A  850  ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO          
SEQRES  29 A  850  ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG          
SEQRES  30 A  850  LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO          
SEQRES  31 A  850  TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN          
SEQRES  32 A  850  VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY          
SEQRES  33 A  850  GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS          
SEQRES  34 A  850  THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU          
SEQRES  35 A  850  LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO          
SEQRES  36 A  850  GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE          
SEQRES  37 A  850  ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS          
SEQRES  38 A  850  GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL          
SEQRES  39 A  850  TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS          
SEQRES  40 A  850  LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL          
SEQRES  41 A  850  ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET          
SEQRES  42 A  850  SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER          
SEQRES  43 A  850  VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER          
SEQRES  44 A  850  GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE          
SEQRES  45 A  850  TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP          
SEQRES  46 A  850  TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER          
SEQRES  47 A  850  ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA          
SEQRES  48 A  850  LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL          
SEQRES  49 A  850  TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE          
SEQRES  50 A  850  LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER          
SEQRES  51 A  850  LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER          
SEQRES  52 A  850  CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN          
SEQRES  53 A  850  GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY          
SEQRES  54 A  850  LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU          
SEQRES  55 A  850  SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE          
SEQRES  56 A  850  LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE          
SEQRES  57 A  850  LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET          
SEQRES  58 A  850  ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL          
SEQRES  59 A  850  PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL          
SEQRES  60 A  850  ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG          
SEQRES  61 A  850  LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS          
SEQRES  62 A  850  PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG          
SEQRES  63 A  850  ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU          
SEQRES  64 A  850  ARG HIS SER ILE ARG CSO PRO GLU SER GLY GLU HIS TYR          
SEQRES  65 A  850  GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS          
SEQRES  66 A  850  HIS HIS HIS HIS HIS                                          
SEQRES   1 B  850  PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP          
SEQRES   2 B  850  GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER          
SEQRES   3 B  850  GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE          
SEQRES   4 B  850  VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG          
SEQRES   5 B  850  LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN          
SEQRES   6 B  850  SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS          
SEQRES   7 B  850  GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP          
SEQRES   8 B  850  HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG          
SEQRES   9 B  850  GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL          
SEQRES  10 B  850  PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY          
SEQRES  11 B  850  LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS          
SEQRES  12 B  850  ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET          
SEQRES  13 B  850  LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG          
SEQRES  14 B  850  MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE          
SEQRES  15 B  850  SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE          
SEQRES  16 B  850  GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN          
SEQRES  17 B  850  GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY          
SEQRES  18 B  850  VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE          
SEQRES  19 B  850  THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY          
SEQRES  20 B  850  SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU          
SEQRES  21 B  850  VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER          
SEQRES  22 B  850  PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR          
SEQRES  23 B  850  PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS          
SEQRES  24 B  850  LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL          
SEQRES  25 B  850  SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER          
SEQRES  26 B  850  LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP          
SEQRES  27 B  850  THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP          
SEQRES  28 B  850  ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO          
SEQRES  29 B  850  ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG          
SEQRES  30 B  850  LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO          
SEQRES  31 B  850  TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN          
SEQRES  32 B  850  VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY          
SEQRES  33 B  850  GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS          
SEQRES  34 B  850  THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU          
SEQRES  35 B  850  LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO          
SEQRES  36 B  850  GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE          
SEQRES  37 B  850  ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS          
SEQRES  38 B  850  GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL          
SEQRES  39 B  850  TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS          
SEQRES  40 B  850  LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL          
SEQRES  41 B  850  ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET          
SEQRES  42 B  850  SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER          
SEQRES  43 B  850  VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER          
SEQRES  44 B  850  GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE          
SEQRES  45 B  850  TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP          
SEQRES  46 B  850  TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER          
SEQRES  47 B  850  ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA          
SEQRES  48 B  850  LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL          
SEQRES  49 B  850  TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE          
SEQRES  50 B  850  LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER          
SEQRES  51 B  850  LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER          
SEQRES  52 B  850  CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN          
SEQRES  53 B  850  GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY          
SEQRES  54 B  850  LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU          
SEQRES  55 B  850  SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE          
SEQRES  56 B  850  LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE          
SEQRES  57 B  850  LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET          
SEQRES  58 B  850  ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL          
SEQRES  59 B  850  PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL          
SEQRES  60 B  850  ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG          
SEQRES  61 B  850  LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS          
SEQRES  62 B  850  PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG          
SEQRES  63 B  850  ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU          
SEQRES  64 B  850  ARG HIS SER ILE ARG CYS PRO GLU SER GLY GLU HIS TYR          
SEQRES  65 B  850  GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS          
SEQRES  66 B  850  HIS HIS HIS HIS HIS                                          
SEQRES   1 C  850  PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP          
SEQRES   2 C  850  GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER          
SEQRES   3 C  850  GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE          
SEQRES   4 C  850  VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG          
SEQRES   5 C  850  LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN          
SEQRES   6 C  850  SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS          
SEQRES   7 C  850  GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP          
SEQRES   8 C  850  HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG          
SEQRES   9 C  850  GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL          
SEQRES  10 C  850  PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY          
SEQRES  11 C  850  LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS          
SEQRES  12 C  850  ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET          
SEQRES  13 C  850  LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG          
SEQRES  14 C  850  MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE          
SEQRES  15 C  850  SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE          
SEQRES  16 C  850  GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN          
SEQRES  17 C  850  GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY          
SEQRES  18 C  850  VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE          
SEQRES  19 C  850  THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY          
SEQRES  20 C  850  SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU          
SEQRES  21 C  850  VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER          
SEQRES  22 C  850  PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR          
SEQRES  23 C  850  PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS          
SEQRES  24 C  850  LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL          
SEQRES  25 C  850  SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER          
SEQRES  26 C  850  LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP          
SEQRES  27 C  850  THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP          
SEQRES  28 C  850  ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO          
SEQRES  29 C  850  ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG          
SEQRES  30 C  850  LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO          
SEQRES  31 C  850  TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN          
SEQRES  32 C  850  VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY          
SEQRES  33 C  850  GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS          
SEQRES  34 C  850  THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU          
SEQRES  35 C  850  LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO          
SEQRES  36 C  850  GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE          
SEQRES  37 C  850  ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS          
SEQRES  38 C  850  GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL          
SEQRES  39 C  850  TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS          
SEQRES  40 C  850  LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL          
SEQRES  41 C  850  ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET          
SEQRES  42 C  850  SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER          
SEQRES  43 C  850  VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER          
SEQRES  44 C  850  GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE          
SEQRES  45 C  850  TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP          
SEQRES  46 C  850  TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER          
SEQRES  47 C  850  ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA          
SEQRES  48 C  850  LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL          
SEQRES  49 C  850  TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE          
SEQRES  50 C  850  LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER          
SEQRES  51 C  850  LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER          
SEQRES  52 C  850  CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN          
SEQRES  53 C  850  GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY          
SEQRES  54 C  850  LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU          
SEQRES  55 C  850  SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE          
SEQRES  56 C  850  LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE          
SEQRES  57 C  850  LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET          
SEQRES  58 C  850  ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL          
SEQRES  59 C  850  PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL          
SEQRES  60 C  850  ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG          
SEQRES  61 C  850  LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS          
SEQRES  62 C  850  PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG          
SEQRES  63 C  850  ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU          
SEQRES  64 C  850  ARG HIS SER ILE ARG CSO PRO GLU SER GLY GLU HIS TYR          
SEQRES  65 C  850  GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS          
SEQRES  66 C  850  HIS HIS HIS HIS HIS                                          
SEQRES   1 D  850  PRO ALA ALA ARG PHE GLN VAL GLN LYS HIS SER TRP ASP          
SEQRES   2 D  850  GLY LEU ARG SER ILE ILE HIS GLY SER ARG LYS TYR SER          
SEQRES   3 D  850  GLY LEU ILE VAL ASN LYS ALA PRO HIS ASP PHE GLN PHE          
SEQRES   4 D  850  VAL GLN LYS THR ASP GLU SER GLY PRO HIS SER HIS ARG          
SEQRES   5 D  850  LEU TYR TYR LEU GLY MET PRO TYR GLY SER ARG GLU ASN          
SEQRES   6 D  850  SER LEU LEU TYR SER GLU ILE PRO LYS LYS VAL ARG LYS          
SEQRES   7 D  850  GLU ALA LEU LEU LEU LEU SER TRP LYS GLN MET LEU ASP          
SEQRES   8 D  850  HIS PHE GLN ALA THR PRO HIS HIS GLY VAL TYR SER ARG          
SEQRES   9 D  850  GLU GLU GLU LEU LEU ARG GLU ARG LYS ARG LEU GLY VAL          
SEQRES  10 D  850  PHE GLY ILE THR SER TYR ASP PHE HIS SER GLU SER GLY          
SEQRES  11 D  850  LEU PHE LEU PHE GLN ALA SER ASN SER LEU PHE HIS CYS          
SEQRES  12 D  850  ARG ASP GLY GLY LYS ASN GLY PHE MET VAL SER PRO MET          
SEQRES  13 D  850  LYS PRO LEU GLU ILE LYS THR GLN CYS SER GLY PRO ARG          
SEQRES  14 D  850  MET ASP PRO LYS ILE CYS PRO ALA ASP PRO ALA PHE PHE          
SEQRES  15 D  850  SER PHE ILE ASN ASN SER ASP LEU TRP VAL ALA ASN ILE          
SEQRES  16 D  850  GLU THR GLY GLU GLU ARG ARG LEU THR PHE CYS HIS GLN          
SEQRES  17 D  850  GLY LEU SER ASN VAL LEU ASP ASP PRO LYS SER ALA GLY          
SEQRES  18 D  850  VAL ALA THR PHE VAL ILE GLN GLU GLU PHE ASP ARG PHE          
SEQRES  19 D  850  THR GLY TYR TRP TRP CYS PRO THR ALA SER TRP GLU GLY          
SEQRES  20 D  850  SER GLU GLY LEU LYS THR LEU ARG ILE LEU TYR GLU GLU          
SEQRES  21 D  850  VAL ASP GLU SER GLU VAL GLU VAL ILE HIS VAL PRO SER          
SEQRES  22 D  850  PRO ALA LEU GLU GLU ARG LYS THR ASP SER TYR ARG TYR          
SEQRES  23 D  850  PRO ARG THR GLY SER LYS ASN PRO LYS ILE ALA LEU LYS          
SEQRES  24 D  850  LEU ALA GLU PHE GLN THR ASP SER GLN GLY LYS ILE VAL          
SEQRES  25 D  850  SER THR GLN GLU LYS GLU LEU VAL GLN PRO PHE SER SER          
SEQRES  26 D  850  LEU PHE PRO LYS VAL GLU TYR ILE ALA ARG ALA GLY TRP          
SEQRES  27 D  850  THR ARG ASP GLY LYS TYR ALA TRP ALA MET PHE LEU ASP          
SEQRES  28 D  850  ARG PRO GLN GLN TRP LEU GLN LEU VAL LEU LEU PRO PRO          
SEQRES  29 D  850  ALA LEU PHE ILE PRO SER THR GLU ASN GLU GLU GLN ARG          
SEQRES  30 D  850  LEU ALA SER ALA ARG ALA VAL PRO ARG ASN VAL GLN PRO          
SEQRES  31 D  850  TYR VAL VAL TYR GLU GLU VAL THR ASN VAL TRP ILE ASN          
SEQRES  32 D  850  VAL HIS ASP ILE PHE TYR PRO PHE PRO GLN SER GLU GLY          
SEQRES  33 D  850  GLU ASP GLU LEU CYS PHE LEU ARG ALA ASN GLU CYS LYS          
SEQRES  34 D  850  THR GLY PHE CYS HIS LEU TYR LYS VAL THR ALA VAL LEU          
SEQRES  35 D  850  LYS SER GLN GLY TYR ASP TRP SER GLU PRO PHE SER PRO          
SEQRES  36 D  850  GLY GLU ASP GLU PHE LYS CYS PRO ILE LYS GLU GLU ILE          
SEQRES  37 D  850  ALA LEU THR SER GLY GLU TRP GLU VAL LEU ALA ARG HIS          
SEQRES  38 D  850  GLY SER LYS ILE TRP VAL ASN GLU GLU THR LYS LEU VAL          
SEQRES  39 D  850  TYR PHE GLN GLY THR LYS ASP THR PRO LEU GLU HIS HIS          
SEQRES  40 D  850  LEU TYR VAL VAL SER TYR GLU ALA ALA GLY GLU ILE VAL          
SEQRES  41 D  850  ARG LEU THR THR PRO GLY PHE SER HIS SER CYS SER MET          
SEQRES  42 D  850  SER GLN ASN PHE ASP MET PHE VAL SER HIS TYR SER SER          
SEQRES  43 D  850  VAL SER THR PRO PRO CYS VAL HIS VAL TYR LYS LEU SER          
SEQRES  44 D  850  GLY PRO ASP ASP ASP PRO LEU HIS LYS GLN PRO ARG PHE          
SEQRES  45 D  850  TRP ALA SER MET MET GLU ALA ALA SER CYS PRO PRO ASP          
SEQRES  46 D  850  TYR VAL PRO PRO GLU ILE PHE HIS PHE HIS THR ARG SER          
SEQRES  47 D  850  ASP VAL ARG LEU TYR GLY MET ILE TYR LYS PRO HIS ALA          
SEQRES  48 D  850  LEU GLN PRO GLY LYS LYS HIS PRO THR VAL LEU PHE VAL          
SEQRES  49 D  850  TYR GLY GLY PRO GLN VAL GLN LEU VAL ASN ASN SER PHE          
SEQRES  50 D  850  LYS GLY ILE LYS TYR LEU ARG LEU ASN THR LEU ALA SER          
SEQRES  51 D  850  LEU GLY TYR ALA VAL VAL VAL ILE ASP GLY ARG GLY SER          
SEQRES  52 D  850  CYS GLN ARG GLY LEU ARG PHE GLU GLY ALA LEU LYS ASN          
SEQRES  53 D  850  GLN MET GLY GLN VAL GLU ILE GLU ASP GLN VAL GLU GLY          
SEQRES  54 D  850  LEU GLN PHE VAL ALA GLU LYS TYR GLY PHE ILE ASP LEU          
SEQRES  55 D  850  SER ARG VAL ALA ILE HIS GLY TRP SER TYR GLY GLY PHE          
SEQRES  56 D  850  LEU SER LEU MET GLY LEU ILE HIS LYS PRO GLN VAL PHE          
SEQRES  57 D  850  LYS VAL ALA ILE ALA GLY ALA PRO VAL THR VAL TRP MET          
SEQRES  58 D  850  ALA TYR ASP THR GLY TYR THR GLU ARG TYR MET ASP VAL          
SEQRES  59 D  850  PRO GLU ASN ASN GLN HIS GLY TYR GLU ALA GLY SER VAL          
SEQRES  60 D  850  ALA LEU HIS VAL GLU LYS LEU PRO ASN GLU PRO ASN ARG          
SEQRES  61 D  850  LEU LEU ILE LEU HIS GLY PHE LEU ASP GLU ASN VAL HIS          
SEQRES  62 D  850  PHE PHE HIS THR ASN PHE LEU VAL SER GLN LEU ILE ARG          
SEQRES  63 D  850  ALA GLY LYS PRO TYR GLN LEU GLN ILE TYR PRO ASN GLU          
SEQRES  64 D  850  ARG HIS SER ILE ARG CYS PRO GLU SER GLY GLU HIS TYR          
SEQRES  65 D  850  GLU VAL THR LEU LEU HIS PHE LEU GLN GLU TYR LEU HIS          
SEQRES  66 D  850  HIS HIS HIS HIS HIS                                          
MODRES 7ZXS CSO A  844  CYS  MODIFIED RESIDUE                                   
MODRES 7ZXS CSO C  844  CYS  MODIFIED RESIDUE                                   
HET    CSO  A 844       7                                                       
HET    CSO  C 844       7                                                       
HET    KBO  A 901      34                                                       
HET    EDO  A 902       4                                                       
HET    EDO  A 903       4                                                       
HET    EDO  A 904       4                                                       
HET    EDO  A 905       4                                                       
HET    EDO  A 906       4                                                       
HET    EDO  A 907       4                                                       
HET    EDO  A 908       4                                                       
HET    KBO  B 901      34                                                       
HET    EDO  B 902       4                                                       
HET    EDO  B 903       4                                                       
HET    EDO  B 904       4                                                       
HET    EDO  B 905       4                                                       
HET    EDO  B 906       4                                                       
HET    EDO  B 907       4                                                       
HET    EDO  B 908       4                                                       
HET    EDO  B 909       4                                                       
HET    EDO  B 910       4                                                       
HET    EDO  B 911       4                                                       
HET    EDO  B 912       4                                                       
HET    PEG  B 913       7                                                       
HET    EDO  B 914       4                                                       
HET    KBO  C 901      34                                                       
HET    EDO  C 902       4                                                       
HET    EDO  C 903       4                                                       
HET    EDO  C 904       4                                                       
HET    EDO  C 905       4                                                       
HET    EDO  C 906       4                                                       
HET    EDO  C 907       4                                                       
HET    EDO  C 908       4                                                       
HET    PEG  C 909       7                                                       
HET    EDO  C 910       4                                                       
HET    EDO  C 911       4                                                       
HET    EDO  C 912       4                                                       
HET    KBO  D 901      34                                                       
HET    EDO  D 902       4                                                       
HET    EDO  D 903       4                                                       
HET    EDO  D 904       4                                                       
HET    EDO  D 905       4                                                       
HET    EDO  D 906       4                                                       
HET    EDO  D 907       4                                                       
HET    EDO  D 908       4                                                       
HET    EDO  D 909       4                                                       
HET    EDO  D 910       4                                                       
HET    EDO  D 911       4                                                       
HET    PEG  D 912       7                                                       
HET    EDO  D 913       4                                                       
HET    EDO  D 914       4                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     KBO 2-ETHYL-2-METHANOYL-~{N}-[3-[[4-(QUINOLIN-8-YLMETHYL)            
HETNAM   2 KBO  PIPERAZIN-1-YL]METHYL]PHENYL]BUTANAMIDE                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   5  KBO    4(C28 H34 N4 O2)                                             
FORMUL   6  EDO    41(C2 H6 O2)                                                 
FORMUL  25  PEG    3(C4 H10 O3)                                                 
FORMUL  53  HOH   *1653(H2 O)                                                   
HELIX    1 AA1 SER A   30  VAL A   49  1                                  20    
HELIX    2 AA2 PRO A  116  VAL A  120  5                                   5    
HELIX    3 AA3 SER A  122  LYS A  132  1                                  11    
HELIX    4 AA4 ASN A  231  ASP A  235  5                                   5    
HELIX    5 AA5 THR A  243  ASP A  251  1                                   9    
HELIX    6 AA6 ALA A  294  ARG A  298  5                                   5    
HELIX    7 AA7 PRO A  341  PHE A  346  1                                   6    
HELIX    8 AA8 PRO A  382  ALA A  384  5                                   3    
HELIX    9 AA9 ASN A  392  VAL A  403  1                                  12    
HELIX   10 AB1 ASP A  583  LYS A  587  5                                   5    
HELIX   11 AB2 TYR A  661  LEU A  670  1                                  10    
HELIX   12 AB3 GLY A  686  GLY A  691  1                                   6    
HELIX   13 AB4 ALA A  692  LYS A  694  5                                   3    
HELIX   14 AB5 VAL A  700  GLY A  717  1                                  18    
HELIX   15 AB6 SER A  730  LYS A  743  1                                  14    
HELIX   16 AB7 VAL A  758  TYR A  762  5                                   5    
HELIX   17 AB8 ASP A  763  ASP A  772  1                                  10    
HELIX   18 AB9 VAL A  773  ASN A  776  5                                   4    
HELIX   19 AC1 ASN A  777  SER A  785  1                                   9    
HELIX   20 AC2 VAL A  786  LEU A  793  5                                   8    
HELIX   21 AC3 PHE A  813  ALA A  826  1                                  14    
HELIX   22 AC4 CSO A  844  LEU A  863  1                                  20    
HELIX   23 AC5 SER B   30  ARG B   42  1                                  13    
HELIX   24 AC6 PRO B  116  VAL B  120  5                                   5    
HELIX   25 AC7 SER B  122  LYS B  132  1                                  11    
HELIX   26 AC8 ASN B  231  ASP B  235  5                                   5    
HELIX   27 AC9 THR B  243  ASP B  251  1                                   9    
HELIX   28 AD1 ALA B  294  ARG B  298  5                                   5    
HELIX   29 AD2 PRO B  341  PHE B  346  1                                   6    
HELIX   30 AD3 PRO B  382  ALA B  384  5                                   3    
HELIX   31 AD4 ASN B  392  ALA B  402  1                                  11    
HELIX   32 AD5 ASP B  583  LYS B  587  5                                   5    
HELIX   33 AD6 TYR B  661  LEU B  670  1                                  10    
HELIX   34 AD7 GLY B  686  GLY B  691  1                                   6    
HELIX   35 AD8 ALA B  692  LYS B  694  5                                   3    
HELIX   36 AD9 VAL B  700  GLY B  717  1                                  18    
HELIX   37 AE1 SER B  730  LYS B  743  1                                  14    
HELIX   38 AE2 VAL B  758  TYR B  762  5                                   5    
HELIX   39 AE3 ASP B  763  ASP B  772  1                                  10    
HELIX   40 AE4 VAL B  773  ASN B  776  5                                   4    
HELIX   41 AE5 ASN B  777  SER B  785  1                                   9    
HELIX   42 AE6 VAL B  786  LEU B  793  5                                   8    
HELIX   43 AE7 PHE B  813  ALA B  826  1                                  14    
HELIX   44 AE8 CYS B  844  LEU B  863  1                                  20    
HELIX   45 AE9 SER C   30  TYR C   44  1                                  15    
HELIX   46 AF1 SER C  122  LYS C  132  1                                  11    
HELIX   47 AF2 ASN C  231  ASP C  235  5                                   5    
HELIX   48 AF3 THR C  243  ASP C  251  1                                   9    
HELIX   49 AF4 ALA C  294  ARG C  298  5                                   5    
HELIX   50 AF5 PRO C  341  PHE C  346  1                                   6    
HELIX   51 AF6 PRO C  382  ALA C  384  5                                   3    
HELIX   52 AF7 ASN C  392  ALA C  402  1                                  11    
HELIX   53 AF8 ASP C  583  LYS C  587  5                                   5    
HELIX   54 AF9 TYR C  661  LEU C  670  1                                  10    
HELIX   55 AG1 GLY C  686  GLY C  691  1                                   6    
HELIX   56 AG2 ALA C  692  LYS C  694  5                                   3    
HELIX   57 AG3 VAL C  700  GLY C  717  1                                  18    
HELIX   58 AG4 SER C  730  LYS C  743  1                                  14    
HELIX   59 AG5 VAL C  758  TYR C  762  5                                   5    
HELIX   60 AG6 ASP C  763  ASP C  772  1                                  10    
HELIX   61 AG7 VAL C  773  ASN C  776  5                                   4    
HELIX   62 AG8 ASN C  777  SER C  785  1                                   9    
HELIX   63 AG9 VAL C  786  LEU C  793  5                                   8    
HELIX   64 AH1 PHE C  813  ALA C  826  1                                  14    
HELIX   65 AH2 CSO C  844  LEU C  863  1                                  20    
HELIX   66 AH3 SER D   30  LYS D   43  1                                  14    
HELIX   67 AH4 PRO D  116  VAL D  120  5                                   5    
HELIX   68 AH5 SER D  122  LYS D  132  1                                  11    
HELIX   69 AH6 ASN D  231  ASP D  235  5                                   5    
HELIX   70 AH7 THR D  243  ASP D  251  1                                   9    
HELIX   71 AH8 ALA D  294  ARG D  298  5                                   5    
HELIX   72 AH9 PRO D  341  PHE D  346  1                                   6    
HELIX   73 AI1 PRO D  382  ALA D  384  5                                   3    
HELIX   74 AI2 ASN D  392  ALA D  402  1                                  11    
HELIX   75 AI3 ASP D  583  LYS D  587  5                                   5    
HELIX   76 AI4 TYR D  661  LEU D  670  1                                  10    
HELIX   77 AI5 GLY D  686  GLY D  691  1                                   6    
HELIX   78 AI6 ALA D  692  LYS D  694  5                                   3    
HELIX   79 AI7 VAL D  700  GLY D  717  1                                  18    
HELIX   80 AI8 SER D  730  LYS D  743  1                                  14    
HELIX   81 AI9 VAL D  758  TYR D  762  5                                   5    
HELIX   82 AJ1 ASP D  763  ASP D  772  1                                  10    
HELIX   83 AJ2 VAL D  773  ASN D  776  5                                   4    
HELIX   84 AJ3 ASN D  777  SER D  785  1                                   9    
HELIX   85 AJ4 VAL D  786  LEU D  793  5                                   8    
HELIX   86 AJ5 PHE D  813  ALA D  826  1                                  14    
HELIX   87 AJ6 CYS D  844  LEU D  863  1                                  20    
SHEET    1 AA1 4 HIS A  54  GLN A  60  0                                        
SHEET    2 AA1 4 HIS A  68  GLY A  76 -1  O  LEU A  75   N  HIS A  54           
SHEET    3 AA1 4 SER A  85  PRO A  92 -1  O  LEU A  87   N  TYR A  74           
SHEET    4 AA1 4 LYS A 106  GLN A 107 -1  O  LYS A 106   N  TYR A  88           
SHEET    1 AA2 4 ASP A 143  HIS A 145  0                                        
SHEET    2 AA2 4 LEU A 150  ALA A 155 -1  O  LEU A 152   N  ASP A 143           
SHEET    3 AA2 4 SER A 158  ARG A 163 -1  O  CYS A 162   N  PHE A 151           
SHEET    4 AA2 4 LEU A 178  GLU A 179 -1  O  LEU A 178   N  HIS A 161           
SHEET    1 AA3 4 MET A 189  ILE A 193  0                                        
SHEET    2 AA3 4 PHE A 200  ASN A 205 -1  O  ILE A 204   N  MET A 189           
SHEET    3 AA3 4 ASP A 208  ASN A 213 -1  O  TRP A 210   N  PHE A 203           
SHEET    4 AA3 4 GLU A 219  ARG A 221 -1  O  ARG A 220   N  VAL A 211           
SHEET    1 AA4 3 LYS A 237  ALA A 239  0                                        
SHEET    2 AA4 3 LYS A 271  ASP A 281 -1  O  VAL A 280   N  SER A 238           
SHEET    3 AA4 3 TYR A 256  TRP A 258 -1  N  TRP A 257   O  LEU A 276           
SHEET    1 AA5 5 LYS A 237  ALA A 239  0                                        
SHEET    2 AA5 5 LYS A 271  ASP A 281 -1  O  VAL A 280   N  SER A 238           
SHEET    3 AA5 5 LYS A 314  THR A 324 -1  O  ALA A 320   N  ILE A 275           
SHEET    4 AA5 5 ILE A 330  LEU A 338 -1  O  LYS A 336   N  LEU A 319           
SHEET    5 AA5 5 PHE A 386  PRO A 388 -1  O  ILE A 387   N  GLU A 337           
SHEET    1 AA6 2 VAL A 287  PRO A 291  0                                        
SHEET    2 AA6 2 THR A 300  ARG A 304 -1  O  ASP A 301   N  VAL A 290           
SHEET    1 AA7 4 TYR A 351  TRP A 357  0                                        
SHEET    2 AA7 4 ALA A 364  LEU A 369 -1  O  MET A 367   N  ARG A 354           
SHEET    3 AA7 4 TRP A 375  LEU A 381 -1  O  LEU A 381   N  ALA A 364           
SHEET    4 AA7 4 TYR A 410  VAL A 416 -1  O  GLU A 415   N  LEU A 376           
SHEET    1 AA8 4 PHE A 427  PRO A 429  0                                        
SHEET    2 AA8 4 GLU A 438  ASN A 445 -1  O  LEU A 442   N  TYR A 428           
SHEET    3 AA8 4 HIS A 453  VAL A 460 -1  O  VAL A 457   N  PHE A 441           
SHEET    4 AA8 4 ILE A 483  ALA A 488 -1  O  ILE A 487   N  LYS A 456           
SHEET    1 AA9 4 TRP A 505  ASN A 507  0                                        
SHEET    2 AA9 4 LEU A 512  GLY A 517 -1  O  TYR A 514   N  TRP A 505           
SHEET    3 AA9 4 HIS A 526  SER A 531 -1  O  TYR A 528   N  PHE A 515           
SHEET    4 AA9 4 VAL A 539  ARG A 540 -1  O  VAL A 539   N  VAL A 529           
SHEET    1 AB1 4 SER A 547  MET A 552  0                                        
SHEET    2 AB1 4 MET A 558  SER A 564 -1  O  HIS A 562   N  SER A 549           
SHEET    3 AB1 4 CYS A 571  SER A 578 -1  O  TYR A 575   N  PHE A 559           
SHEET    4 AB1 4 GLN A 588  MET A 596 -1  O  GLN A 588   N  SER A 578           
SHEET    1 AB2 8 GLU A 609  HIS A 614  0                                        
SHEET    2 AB2 8 ARG A 620  TYR A 626 -1  O  ILE A 625   N  GLU A 609           
SHEET    3 AB2 8 ALA A 673  ASP A 678 -1  O  VAL A 674   N  TYR A 626           
SHEET    4 AB2 8 HIS A 637  PHE A 642  1  N  VAL A 640   O  ALA A 673           
SHEET    5 AB2 8 ILE A 719  TRP A 729  1  O  ALA A 725   N  LEU A 641           
SHEET    6 AB2 8 VAL A 749  GLY A 753  1  O  GLY A 753   N  GLY A 728           
SHEET    7 AB2 8 LEU A 800  GLY A 805  1  O  LEU A 801   N  ALA A 752           
SHEET    8 AB2 8 GLN A 831  TYR A 835  1  O  GLN A 833   N  ILE A 802           
SHEET    1 AB3 5 ALA B  22  ARG B  23  0                                        
SHEET    2 AB3 5 LYS B 635  PHE B 642  1  O  LYS B 636   N  ALA B  22           
SHEET    3 AB3 5 ALA B 673  ASP B 678  1  O  ALA B 673   N  VAL B 640           
SHEET    4 AB3 5 ARG B 620  TYR B 626 -1  N  TYR B 626   O  VAL B 674           
SHEET    5 AB3 5 GLU B 609  HIS B 614 -1  N  GLU B 609   O  ILE B 625           
SHEET    1 AB4 6 ALA B  22  ARG B  23  0                                        
SHEET    2 AB4 6 LYS B 635  PHE B 642  1  O  LYS B 636   N  ALA B  22           
SHEET    3 AB4 6 ILE B 719  TRP B 729  1  O  ALA B 725   N  LEU B 641           
SHEET    4 AB4 6 VAL B 749  GLY B 753  1  O  GLY B 753   N  GLY B 728           
SHEET    5 AB4 6 LEU B 800  GLY B 805  1  O  LEU B 801   N  ALA B 752           
SHEET    6 AB4 6 GLN B 831  TYR B 835  1  O  GLN B 831   N  ILE B 802           
SHEET    1 AB5 4 HIS B  54  GLN B  60  0                                        
SHEET    2 AB5 4 HIS B  68  GLY B  76 -1  O  LEU B  75   N  HIS B  54           
SHEET    3 AB5 4 SER B  85  PRO B  92 -1  O  LEU B  87   N  TYR B  74           
SHEET    4 AB5 4 LYS B 106  GLN B 107 -1  O  LYS B 106   N  TYR B  88           
SHEET    1 AB6 4 ASP B 143  HIS B 145  0                                        
SHEET    2 AB6 4 LEU B 150  ALA B 155 -1  O  LEU B 152   N  ASP B 143           
SHEET    3 AB6 4 SER B 158  ARG B 163 -1  O  CYS B 162   N  PHE B 151           
SHEET    4 AB6 4 LEU B 178  GLU B 179 -1  O  LEU B 178   N  HIS B 161           
SHEET    1 AB7 4 MET B 189  ILE B 193  0                                        
SHEET    2 AB7 4 PHE B 200  ASN B 205 -1  O  ILE B 204   N  MET B 189           
SHEET    3 AB7 4 ASP B 208  ASN B 213 -1  O  TRP B 210   N  PHE B 203           
SHEET    4 AB7 4 GLU B 219  ARG B 221 -1  O  ARG B 220   N  VAL B 211           
SHEET    1 AB8 3 LYS B 237  ALA B 239  0                                        
SHEET    2 AB8 3 LYS B 271  ASP B 281 -1  O  VAL B 280   N  SER B 238           
SHEET    3 AB8 3 TYR B 256  TRP B 258 -1  N  TRP B 257   O  LEU B 276           
SHEET    1 AB9 5 LYS B 237  ALA B 239  0                                        
SHEET    2 AB9 5 LYS B 271  ASP B 281 -1  O  VAL B 280   N  SER B 238           
SHEET    3 AB9 5 LYS B 314  THR B 324 -1  O  ALA B 320   N  ILE B 275           
SHEET    4 AB9 5 ILE B 330  LEU B 338 -1  O  LYS B 336   N  LEU B 319           
SHEET    5 AB9 5 PHE B 386  PRO B 388 -1  O  ILE B 387   N  GLU B 337           
SHEET    1 AC1 2 VAL B 287  PRO B 291  0                                        
SHEET    2 AC1 2 THR B 300  ARG B 304 -1  O  ASP B 301   N  VAL B 290           
SHEET    1 AC2 4 TYR B 351  TRP B 357  0                                        
SHEET    2 AC2 4 ALA B 364  LEU B 369 -1  O  MET B 367   N  ARG B 354           
SHEET    3 AC2 4 TRP B 375  LEU B 381 -1  O  LEU B 381   N  ALA B 364           
SHEET    4 AC2 4 TYR B 410  VAL B 416 -1  O  GLU B 415   N  LEU B 376           
SHEET    1 AC3 4 PHE B 427  PRO B 429  0                                        
SHEET    2 AC3 4 GLU B 438  ASN B 445 -1  O  LEU B 442   N  TYR B 428           
SHEET    3 AC3 4 HIS B 453  VAL B 460 -1  O  VAL B 457   N  PHE B 441           
SHEET    4 AC3 4 ILE B 483  ALA B 488 -1  O  GLU B 485   N  THR B 458           
SHEET    1 AC4 4 TRP B 505  ASN B 507  0                                        
SHEET    2 AC4 4 LEU B 512  GLY B 517 -1  O  TYR B 514   N  TRP B 505           
SHEET    3 AC4 4 HIS B 526  SER B 531 -1  O  TYR B 528   N  PHE B 515           
SHEET    4 AC4 4 VAL B 539  ARG B 540 -1  O  VAL B 539   N  VAL B 529           
SHEET    1 AC5 4 SER B 547  MET B 552  0                                        
SHEET    2 AC5 4 MET B 558  SER B 564 -1  O  HIS B 562   N  SER B 549           
SHEET    3 AC5 4 CYS B 571  SER B 578 -1  O  TYR B 575   N  PHE B 559           
SHEET    4 AC5 4 GLN B 588  MET B 596 -1  O  ARG B 590   N  LYS B 576           
SHEET    1 AC6 5 ALA C  22  ARG C  23  0                                        
SHEET    2 AC6 5 LYS C 635  PHE C 642  1  O  LYS C 636   N  ALA C  22           
SHEET    3 AC6 5 ALA C 673  ASP C 678  1  O  ALA C 673   N  VAL C 640           
SHEET    4 AC6 5 ARG C 620  TYR C 626 -1  N  TYR C 626   O  VAL C 674           
SHEET    5 AC6 5 GLU C 609  HIS C 614 -1  N  GLU C 609   O  ILE C 625           
SHEET    1 AC7 6 ALA C  22  ARG C  23  0                                        
SHEET    2 AC7 6 LYS C 635  PHE C 642  1  O  LYS C 636   N  ALA C  22           
SHEET    3 AC7 6 ILE C 719  TRP C 729  1  O  ALA C 725   N  LEU C 641           
SHEET    4 AC7 6 VAL C 749  GLY C 753  1  O  GLY C 753   N  GLY C 728           
SHEET    5 AC7 6 LEU C 800  GLY C 805  1  O  LEU C 801   N  ALA C 752           
SHEET    6 AC7 6 GLN C 831  TYR C 835  1  O  GLN C 831   N  ILE C 802           
SHEET    1 AC8 4 HIS C  54  GLN C  60  0                                        
SHEET    2 AC8 4 HIS C  68  GLY C  76 -1  O  LEU C  75   N  HIS C  54           
SHEET    3 AC8 4 SER C  85  PRO C  92 -1  O  LEU C  87   N  TYR C  74           
SHEET    4 AC8 4 LYS C 106  GLN C 107 -1  O  LYS C 106   N  TYR C  88           
SHEET    1 AC9 4 ASP C 143  HIS C 145  0                                        
SHEET    2 AC9 4 LEU C 150  ALA C 155 -1  O  LEU C 152   N  ASP C 143           
SHEET    3 AC9 4 SER C 158  ARG C 163 -1  O  CYS C 162   N  PHE C 151           
SHEET    4 AC9 4 LEU C 178  GLU C 179 -1  O  LEU C 178   N  HIS C 161           
SHEET    1 AD1 4 MET C 189  ILE C 193  0                                        
SHEET    2 AD1 4 PHE C 200  ASN C 205 -1  O  ILE C 204   N  MET C 189           
SHEET    3 AD1 4 ASP C 208  ASN C 213 -1  O  TRP C 210   N  PHE C 203           
SHEET    4 AD1 4 GLU C 219  ARG C 221 -1  O  ARG C 220   N  VAL C 211           
SHEET    1 AD2 3 LYS C 237  ALA C 239  0                                        
SHEET    2 AD2 3 LYS C 271  ASP C 281 -1  O  VAL C 280   N  SER C 238           
SHEET    3 AD2 3 TYR C 256  TRP C 258 -1  N  TRP C 257   O  LEU C 276           
SHEET    1 AD3 5 LYS C 237  ALA C 239  0                                        
SHEET    2 AD3 5 LYS C 271  ASP C 281 -1  O  VAL C 280   N  SER C 238           
SHEET    3 AD3 5 LYS C 314  THR C 324 -1  O  ALA C 320   N  ILE C 275           
SHEET    4 AD3 5 ILE C 330  LEU C 338 -1  O  LYS C 336   N  LEU C 319           
SHEET    5 AD3 5 PHE C 386  PRO C 388 -1  O  ILE C 387   N  GLU C 337           
SHEET    1 AD4 2 VAL C 287  PRO C 291  0                                        
SHEET    2 AD4 2 THR C 300  ARG C 304 -1  O  ASP C 301   N  VAL C 290           
SHEET    1 AD5 4 TYR C 351  TRP C 357  0                                        
SHEET    2 AD5 4 ALA C 364  LEU C 369 -1  O  MET C 367   N  ARG C 354           
SHEET    3 AD5 4 TRP C 375  LEU C 381 -1  O  GLN C 377   N  PHE C 368           
SHEET    4 AD5 4 TYR C 410  VAL C 416 -1  O  GLU C 415   N  LEU C 376           
SHEET    1 AD6 4 PHE C 427  PRO C 429  0                                        
SHEET    2 AD6 4 GLU C 438  ASN C 445 -1  O  LEU C 442   N  TYR C 428           
SHEET    3 AD6 4 HIS C 453  VAL C 460 -1  O  VAL C 457   N  PHE C 441           
SHEET    4 AD6 4 ILE C 483  ALA C 488 -1  O  GLU C 485   N  THR C 458           
SHEET    1 AD7 4 TRP C 505  ASN C 507  0                                        
SHEET    2 AD7 4 LEU C 512  GLY C 517 -1  O  TYR C 514   N  TRP C 505           
SHEET    3 AD7 4 HIS C 526  SER C 531 -1  O  TYR C 528   N  PHE C 515           
SHEET    4 AD7 4 VAL C 539  ARG C 540 -1  O  VAL C 539   N  VAL C 529           
SHEET    1 AD8 4 SER C 547  MET C 552  0                                        
SHEET    2 AD8 4 MET C 558  SER C 565 -1  O  HIS C 562   N  SER C 549           
SHEET    3 AD8 4 THR C 568  SER C 578 -1  O  TYR C 575   N  PHE C 559           
SHEET    4 AD8 4 GLN C 588  MET C 596 -1  O  GLN C 588   N  SER C 578           
SHEET    1 AD9 4 HIS D  54  GLN D  60  0                                        
SHEET    2 AD9 4 HIS D  68  GLY D  76 -1  O  LEU D  75   N  HIS D  54           
SHEET    3 AD9 4 SER D  85  PRO D  92 -1  O  LEU D  87   N  TYR D  74           
SHEET    4 AD9 4 LYS D 106  GLN D 107 -1  O  LYS D 106   N  TYR D  88           
SHEET    1 AE1 4 ASP D 143  HIS D 145  0                                        
SHEET    2 AE1 4 LEU D 150  ALA D 155 -1  O  LEU D 152   N  ASP D 143           
SHEET    3 AE1 4 SER D 158  ARG D 163 -1  O  CYS D 162   N  PHE D 151           
SHEET    4 AE1 4 LEU D 178  GLU D 179 -1  O  LEU D 178   N  HIS D 161           
SHEET    1 AE2 4 MET D 189  ILE D 193  0                                        
SHEET    2 AE2 4 PHE D 200  ASN D 205 -1  O  ILE D 204   N  MET D 189           
SHEET    3 AE2 4 ASP D 208  ASN D 213 -1  O  TRP D 210   N  PHE D 203           
SHEET    4 AE2 4 GLU D 219  ARG D 221 -1  O  ARG D 220   N  VAL D 211           
SHEET    1 AE3 3 LYS D 237  ALA D 239  0                                        
SHEET    2 AE3 3 LYS D 271  ASP D 281 -1  O  VAL D 280   N  SER D 238           
SHEET    3 AE3 3 TYR D 256  TRP D 258 -1  N  TRP D 257   O  LEU D 276           
SHEET    1 AE4 5 LYS D 237  ALA D 239  0                                        
SHEET    2 AE4 5 LYS D 271  ASP D 281 -1  O  VAL D 280   N  SER D 238           
SHEET    3 AE4 5 LYS D 314  THR D 324 -1  O  ALA D 320   N  ILE D 275           
SHEET    4 AE4 5 ILE D 330  LEU D 338 -1  O  LYS D 336   N  LEU D 319           
SHEET    5 AE4 5 PHE D 386  PRO D 388 -1  O  ILE D 387   N  GLU D 337           
SHEET    1 AE5 2 VAL D 287  PRO D 291  0                                        
SHEET    2 AE5 2 THR D 300  ARG D 304 -1  O  ASP D 301   N  VAL D 290           
SHEET    1 AE6 4 TYR D 351  TRP D 357  0                                        
SHEET    2 AE6 4 ALA D 364  LEU D 369 -1  O  MET D 367   N  ARG D 354           
SHEET    3 AE6 4 TRP D 375  LEU D 381 -1  O  GLN D 377   N  PHE D 368           
SHEET    4 AE6 4 TYR D 410  VAL D 416 -1  O  GLU D 415   N  LEU D 376           
SHEET    1 AE7 4 PHE D 427  PRO D 429  0                                        
SHEET    2 AE7 4 GLU D 438  ASN D 445 -1  O  LEU D 442   N  TYR D 428           
SHEET    3 AE7 4 HIS D 453  VAL D 460 -1  O  VAL D 457   N  PHE D 441           
SHEET    4 AE7 4 ILE D 483  ALA D 488 -1  O  GLU D 485   N  THR D 458           
SHEET    1 AE8 4 TRP D 505  ASN D 507  0                                        
SHEET    2 AE8 4 LEU D 512  GLY D 517 -1  O  TYR D 514   N  TRP D 505           
SHEET    3 AE8 4 HIS D 526  SER D 531 -1  O  TYR D 528   N  PHE D 515           
SHEET    4 AE8 4 VAL D 539  ARG D 540 -1  O  VAL D 539   N  VAL D 529           
SHEET    1 AE9 4 SER D 547  MET D 552  0                                        
SHEET    2 AE9 4 MET D 558  SER D 565 -1  O  HIS D 562   N  SER D 549           
SHEET    3 AE9 4 THR D 568  SER D 578 -1  O  TYR D 575   N  PHE D 559           
SHEET    4 AE9 4 GLN D 588  MET D 596 -1  O  GLN D 588   N  SER D 578           
SHEET    1 AF1 8 GLU D 609  HIS D 614  0                                        
SHEET    2 AF1 8 ARG D 620  TYR D 626 -1  O  ILE D 625   N  GLU D 609           
SHEET    3 AF1 8 ALA D 673  ASP D 678 -1  O  VAL D 674   N  TYR D 626           
SHEET    4 AF1 8 HIS D 637  PHE D 642  1  N  VAL D 640   O  ALA D 673           
SHEET    5 AF1 8 ILE D 719  TRP D 729  1  O  ALA D 725   N  LEU D 641           
SHEET    6 AF1 8 VAL D 749  GLY D 753  1  O  GLY D 753   N  GLY D 728           
SHEET    7 AF1 8 LEU D 800  GLY D 805  1  O  LEU D 801   N  ALA D 752           
SHEET    8 AF1 8 GLN D 831  TYR D 835  1  O  GLN D 831   N  ILE D 802           
LINK         OG  SER A 730                 C   KBO A 901     1555   1555  1.45  
LINK         C   ARG A 843                 N   CSO A 844     1555   1555  1.34  
LINK         C   CSO A 844                 N   PRO A 845     1555   1555  1.35  
LINK         OG  SER B 730                 C   KBO B 901     1555   1555  1.45  
LINK         OG  SER C 730                 C   KBO C 901     1555   1555  1.46  
LINK         C   ARG C 843                 N   CSO C 844     1555   1555  1.34  
LINK         C   CSO C 844                 N   PRO C 845     1555   1555  1.36  
LINK         OG  SER D 730                 C   KBO D 901     1555   1555  1.44  
CRYST1   88.350  106.176  121.127  65.25  70.43  75.86 P 1           2          
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      0.011319 -0.002850 -0.003199        0.00000                         
SCALE2      0.000000  0.009712 -0.003852        0.00000                         
SCALE3      0.000000  0.000000  0.009426        0.00000                         
TER    6855      HIS A 865                                                      
TER   13711      HIS B 865                                                      
TER   20593      HIS C 865                                                      
TER   27424      HIS D 865                                                      
MASTER      569    0   50   87  190    0    0    629184    4  343  264          
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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