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LongText Report for: 3N0T-pdb

Name Class
3N0T-pdb
HEADER    HYDROLASE                               14-MAY-10   3N0T              
TITLE     HUMAN DIPEPTIDIL PEPTIDASE DPP7 COMPLEXED WITH INHIBITOR GSK237826A   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL PEPTIDASE 2;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: PEPTIDASE DOMAIN (UNP RESIDUES 28-492);                    
COMPND   5 SYNONYM: DIPEPTIDYL PEPTIDASE II, DPP II, DIPEPTIDYL AMINOPEPTIDASE  
COMPND   6 II, QUIESCENT CELL PROLINE DIPEPTIDASE, DIPEPTIDYL PEPTIDASE 7;      
COMPND   7 EC: 3.4.14.2;                                                        
COMPND   8 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: DPP2, DPP7, QPP;                                               
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,             
KEYWDS   2 AMINOPEPTIDASE, CLEAVAGE ON PAIR OF BASIC RESIDUES, CYTOPLASMIC      
KEYWDS   3 VESICLE, GLYCOPROTEIN, HYDROLASE, LYSOSOME, PROTEASE, SERINE         
KEYWDS   4 PROTEASE, ZYMOGEN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DOBROVETSKY,G.KHUTORESKAYA,A.SEITOVA,L.CROMBET,D.COSSAR,S.PAGANNON, 
AUTHOR   2 C.H.ARROWSMITH,C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,A.HASSELL,L.SHEWCHUK, 
AUTHOR   3 C.HAFFNER,A.BOCHKAREV,STRUCTURAL GENOMICS CONSORTIUM (SGC)           
REVDAT   1   21-JUL-10 3N0T    0                                                
JRNL        AUTH   E.DOBROVETSKY,G.KHUTORESKAYA,A.SEITOVA,L.CROMBET,D.COSSAR,   
JRNL        AUTH 2 S.PAGANNON,C.H.ARROWSMITH,C.BOUNTRA,A.M.EDWARDS,A.HASSELL,   
JRNL        AUTH 3 L.SHEWCHUK,C.HAFFNER,A.BOCHKAREV                             
JRNL        TITL   HUMAN DIPEPTIDYL PEPTIDASE DPP7                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 91963                          
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)  : 0.221                          
REMARK   3   R VALUE            (WORKING SET)  : 0.218                          
REMARK   3   FREE R VALUE                      : 0.260                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 4609                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.45                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.51                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 6674                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2530                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 6324                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2498                   
REMARK   3   BIN FREE R VALUE                        : 0.3102                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.24                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 350                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13833                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 248                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 50.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.90670                                              
REMARK   3    B22 (A**2) : -2.65200                                             
REMARK   3    B33 (A**2) : 0.74530                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -4.93630                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.36                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.862                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 14293  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 19476  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 4565   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 313    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2169   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 14241  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1884   ; 5.000  ; NULL                
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 16779  ; 4.000  ; NULL                
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.07                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.75                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.74                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   A 1001    A 1001                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.4764    0.2164   14.7866           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0604 T22:   -0.1058                                    
REMARK   3     T33:   -0.0107 T12:   -0.0072                                    
REMARK   3     T13:   -0.0841 T23:   -0.0175                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3572 L22:    0.7273                                    
REMARK   3     L33:    0.9603 L12:   -0.1996                                    
REMARK   3     L13:    0.0574 L23:   -0.3600                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0603 S12:   -0.0100 S13:    0.0137                     
REMARK   3     S21:    0.0414 S22:    0.0153 S23:   -0.0971                     
REMARK   3     S31:    0.0403 S32:   -0.0207 S33:    0.0450                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   B 1001    B 1001                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.3776   34.0102  -14.3854           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0325 T22:   -0.1183                                    
REMARK   3     T33:   -0.0121 T12:    0.0042                                    
REMARK   3     T13:   -0.0698 T23:   -0.0275                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4740 L22:    0.5665                                    
REMARK   3     L33:    0.7845 L12:    0.1860                                    
REMARK   3     L13:    0.0014 L23:   -0.3300                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0609 S12:    0.0103 S13:   -0.0162                     
REMARK   3     S21:   -0.0199 S22:    0.0430 S23:   -0.0549                     
REMARK   3     S31:   -0.0320 S32:   -0.0257 S33:    0.0179                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   C 1001    C 1001                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    2.8609   20.4232   65.3980           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0183 T22:   -0.1164                                    
REMARK   3     T33:   -0.1097 T12:   -0.0684                                    
REMARK   3     T13:   -0.0962 T23:   -0.0332                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8979 L22:    0.8973                                    
REMARK   3     L33:    1.0921 L12:   -0.4025                                    
REMARK   3     L13:    0.6301 L23:   -0.5916                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0142 S12:   -0.1446 S13:    0.1470                     
REMARK   3     S21:   -0.1327 S22:    0.0363 S23:   -0.0213                     
REMARK   3     S31:    0.0235 S32:   -0.0974 S33:   -0.0505                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   D 1001    D 1001                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   24.4180  -13.4173   84.9288           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0856 T22:   -0.1147                                    
REMARK   3     T33:   -0.1731 T12:   -0.0755                                    
REMARK   3     T13:   -0.0837 T23:   -0.0258                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1310 L22:    1.0245                                    
REMARK   3     L33:    0.6727 L12:   -0.5964                                    
REMARK   3     L13:    0.5660 L23:   -0.2447                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0325 S12:   -0.0878 S13:   -0.0527                     
REMARK   3     S21:   -0.1221 S22:    0.0689 S23:   -0.0313                     
REMARK   3     S31:    0.2604 S32:   -0.0905 S33:   -0.1014                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N0T COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059236.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92014                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 122.213                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3JYH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.2M SODIUM         
REMARK 280  ACETATE, 0.1M HEPES, 5% MPD, PH 7.5, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 300K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.25000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     ASP A    27                                                      
REMARK 465     GLN A   480                                                      
REMARK 465     GLN A   481                                                      
REMARK 465     PRO A   482                                                      
REMARK 465     ALA A   483                                                      
REMARK 465     LEU A   484                                                      
REMARK 465     ARG A   485                                                      
REMARK 465     GLY A   486                                                      
REMARK 465     GLY A   487                                                      
REMARK 465     PRO A   488                                                      
REMARK 465     ARG A   489                                                      
REMARK 465     LEU A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     LEU A   492                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     ASP B    27                                                      
REMARK 465     GLN B   480                                                      
REMARK 465     GLN B   481                                                      
REMARK 465     PRO B   482                                                      
REMARK 465     ALA B   483                                                      
REMARK 465     LEU B   484                                                      
REMARK 465     ARG B   485                                                      
REMARK 465     GLY B   486                                                      
REMARK 465     GLY B   487                                                      
REMARK 465     PRO B   488                                                      
REMARK 465     ARG B   489                                                      
REMARK 465     LEU B   490                                                      
REMARK 465     SER B   491                                                      
REMARK 465     LEU B   492                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     MET C    26                                                      
REMARK 465     ASP C    27                                                      
REMARK 465     GLU C   479                                                      
REMARK 465     GLN C   480                                                      
REMARK 465     GLN C   481                                                      
REMARK 465     PRO C   482                                                      
REMARK 465     ALA C   483                                                      
REMARK 465     LEU C   484                                                      
REMARK 465     ARG C   485                                                      
REMARK 465     GLY C   486                                                      
REMARK 465     GLY C   487                                                      
REMARK 465     PRO C   488                                                      
REMARK 465     ARG C   489                                                      
REMARK 465     LEU C   490                                                      
REMARK 465     SER C   491                                                      
REMARK 465     LEU C   492                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     MET D    26                                                      
REMARK 465     ASP D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     ARG D   478                                                      
REMARK 465     GLU D   479                                                      
REMARK 465     GLN D   480                                                      
REMARK 465     GLN D   481                                                      
REMARK 465     PRO D   482                                                      
REMARK 465     ALA D   483                                                      
REMARK 465     LEU D   484                                                      
REMARK 465     ARG D   485                                                      
REMARK 465     GLY D   486                                                      
REMARK 465     GLY D   487                                                      
REMARK 465     PRO D   488                                                      
REMARK 465     ARG D   489                                                      
REMARK 465     LEU D   490                                                      
REMARK 465     SER D   491                                                      
REMARK 465     LEU D   492                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  34    NH1  NH2                                            
REMARK 470     ARG A  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  62    CZ   NH1  NH2                                       
REMARK 470     ARG A  66    CZ   NH1  NH2                                       
REMARK 470     GLU A  68    CG   CD   OE1  OE2                                  
REMARK 470     ALA A  89    CB                                                  
REMARK 470     GLN A 119    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 208    CG   OD1  OD2                                       
REMARK 470     GLN A 212    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 215    CE   NZ                                             
REMARK 470     GLU A 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 253    CG   CD   CE   NZ                                   
REMARK 470     ARG A 380    CZ   NH1  NH2                                       
REMARK 470     ARG A 427    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 471    CD   OE1  OE2                                       
REMARK 470     LYS A 474    CG   CD   CE   NZ                                   
REMARK 470     ARG A 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 479    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  28    CG   OD1  OD2                                       
REMARK 470     GLN B  32    CD   OE1  NE2                                       
REMARK 470     ARG B  47    CZ   NH1  NH2                                       
REMARK 470     ARG B  62    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  68    CG   CD   OE1  OE2                                  
REMARK 470     ALA B  89    CB                                                  
REMARK 470     GLN B 119    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 215    CE   NZ                                             
REMARK 470     ARG B 221    CZ   NH1  NH2                                       
REMARK 470     GLN B 233    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 253    NZ                                                  
REMARK 470     ARG B 327    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 376    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 460    CD   OE1  OE2                                       
REMARK 470     LYS B 463    CD   CE   NZ                                        
REMARK 470     GLU B 471    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 474    CG   CD   CE   NZ                                   
REMARK 470     ARG B 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 479    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  28    CG   OD1  OD2                                       
REMARK 470     ARG C  47    CZ   NH1  NH2                                       
REMARK 470     ARG C  62    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG C  66    NE   CZ   NH1  NH2                                  
REMARK 470     ALA C  89    CB                                                  
REMARK 470     GLU C  97    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 119    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 127    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 153    CG   OD1  OD2                                       
REMARK 470     ASP C 197    CG   OD1  OD2                                       
REMARK 470     ASN C 199    CG   OD1  ND2                                       
REMARK 470     LYS C 215    CG   CD   CE   NZ                                   
REMARK 470     GLN C 218    CG   CD   OE1  NE2                                  
REMARK 470     LEU C 232    CG   CD1  CD2                                       
REMARK 470     GLU C 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 253    CE   NZ                                             
REMARK 470     LYS C 290    CD   CE   NZ                                        
REMARK 470     ARG C 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 427    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 471    CD   OE1  OE2                                       
REMARK 470     LYS C 474    CG   CD   CE   NZ                                   
REMARK 470     ARG C 477    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 478    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  47    NE   CZ   NH1  NH2                                  
REMARK 470     ARG D  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D  66    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  68    CG   CD   OE1  OE2                                  
REMARK 470     ALA D  89    CB                                                  
REMARK 470     GLU D  97    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  98    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 112    CD   CE   NZ                                        
REMARK 470     GLN D 119    CG   CD   OE1  NE2                                  
REMARK 470     ASP D 153    CG   OD1  OD2                                       
REMARK 470     LYS D 215    CE   NZ                                             
REMARK 470     GLN D 218    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 222    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 225    CD   NE   CZ   NH1  NH2                             
REMARK 470     LEU D 232    CG   CD1  CD2                                       
REMARK 470     GLU D 252    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 253    CG   CD   CE   NZ                                   
REMARK 470     ARG D 327    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 376    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 384    CG   OD1  OD2                                       
REMARK 470     LYS D 463    CG   CD   CE   NZ                                   
REMARK 470     GLU D 471    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 474    CE   NZ                                             
REMARK 470     ARG D 477    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  68      -24.51   -148.12                                   
REMARK 500    ASN A  77     -151.76   -105.77                                   
REMARK 500    GLU A  78       54.72    -67.36                                   
REMARK 500    TYR A 109       -4.21     83.29                                   
REMARK 500    ALA A 151       44.04   -143.57                                   
REMARK 500    SER A 162     -126.07     61.98                                   
REMARK 500    ALA A 235       53.05    -90.52                                   
REMARK 500    SER A 250      -30.82   -149.48                                   
REMARK 500    PHE A 280      -72.30    -90.40                                   
REMARK 500    THR A 353      -64.56   -122.02                                   
REMARK 500    SER A 430     -178.22   -173.65                                   
REMARK 500    ALA A 442     -137.27   -102.34                                   
REMARK 500    HIS A 444       53.45     35.33                                   
REMARK 500    ASN B  77     -155.54   -101.18                                   
REMARK 500    GLU B  78       48.23    -65.95                                   
REMARK 500    TYR B 109        6.68     80.15                                   
REMARK 500    SER B 162     -133.53     65.58                                   
REMARK 500    SER B 250      -31.64   -149.99                                   
REMARK 500    PHE B 280      -69.85    -93.02                                   
REMARK 500    THR B 353      -69.73   -120.46                                   
REMARK 500    LEU B 357       59.58   -117.18                                   
REMARK 500    THR B 358       46.76    -77.24                                   
REMARK 500    ASP B 370       98.04    -69.15                                   
REMARK 500    TRP B 400       -4.63     62.81                                   
REMARK 500    ALA B 442     -132.09    -97.05                                   
REMARK 500    GLU C  46      -60.53    -94.83                                   
REMARK 500    ARG C  66      131.33    -38.14                                   
REMARK 500    GLU C  68      -67.73   -149.85                                   
REMARK 500    ASN C  77     -152.15   -108.35                                   
REMARK 500    GLU C  78       44.65    -70.04                                   
REMARK 500    SER C 162     -127.56     62.67                                   
REMARK 500    SER C 250      -36.24   -153.11                                   
REMARK 500    PHE C 280      -71.41    -97.15                                   
REMARK 500    ASN C 315       41.19   -143.06                                   
REMARK 500    THR C 353      -67.57   -125.58                                   
REMARK 500    LEU C 357       56.85   -114.60                                   
REMARK 500    VAL C 364      -55.42   -131.88                                   
REMARK 500    TRP C 400      -10.05     64.71                                   
REMARK 500    ALA C 442     -134.46    -93.60                                   
REMARK 500    LYS D  51      125.96     -7.42                                   
REMARK 500    ARG D  66      105.48    -51.27                                   
REMARK 500    ASN D  77     -148.28   -115.50                                   
REMARK 500    GLU D  78       45.88    -67.34                                   
REMARK 500    SER D  88       60.09   -114.95                                   
REMARK 500    TYR D 109       -8.26     72.86                                   
REMARK 500    HIS D 125       -1.62   -143.24                                   
REMARK 500    SER D 162     -128.61     63.40                                   
REMARK 500    SER D 250      -38.43   -133.89                                   
REMARK 500    MET D 272       35.75    -96.86                                   
REMARK 500    PHE D 280      -75.17   -100.43                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      55 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  78        23.9      L          L   OUTSIDE RANGE           
REMARK 500    TRP A 394        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 399        24.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 444        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  78        24.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 127        24.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 399        23.5      L          L   OUTSIDE RANGE           
REMARK 500    TRP B 400        24.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS B 444        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN C  77        23.7      L          L   OUTSIDE RANGE           
REMARK 500    GLU C  78        24.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 189        24.7      L          L   OUTSIDE RANGE           
REMARK 500    TRP D 394        24.3      L          L   OUTSIDE RANGE           
REMARK 500    PHE D 399        24.5      L          L   OUTSIDE RANGE           
REMARK 500    TRP D 400        23.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 506        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH A 529        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH A 573        DISTANCE =  5.25 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY C 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OPY D 1001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3JYH   RELATED DB: PDB                                   
REMARK 900 HUMAN DPP7 IN APO FORM                                               
DBREF  3N0T A   28   492  UNP    Q9UHL4   DPP2_HUMAN      28    492             
DBREF  3N0T B   28   492  UNP    Q9UHL4   DPP2_HUMAN      28    492             
DBREF  3N0T C   28   492  UNP    Q9UHL4   DPP2_HUMAN      28    492             
DBREF  3N0T D   28   492  UNP    Q9UHL4   DPP2_HUMAN      28    492             
SEQADV 3N0T GLY A   24  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ALA A   25  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T MET A   26  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ASP A   27  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T GLY B   24  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ALA B   25  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T MET B   26  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ASP B   27  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T GLY C   24  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ALA C   25  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T MET C   26  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ASP C   27  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T GLY D   24  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ALA D   25  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T MET D   26  UNP  Q9UHL4              EXPRESSION TAG                 
SEQADV 3N0T ASP D   27  UNP  Q9UHL4              EXPRESSION TAG                 
SEQRES   1 A  469  GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE          
SEQRES   2 A  469  GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY          
SEQRES   3 A  469  ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG          
SEQRES   4 A  469  PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR          
SEQRES   5 A  469  GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER          
SEQRES   6 A  469  ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU          
SEQRES   7 A  469  LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU          
SEQRES   8 A  469  PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU          
SEQRES   9 A  469  LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU          
SEQRES  10 A  469  LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP          
SEQRES  11 A  469  ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET          
SEQRES  12 A  469  LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL          
SEQRES  13 A  469  ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL          
SEQRES  14 A  469  ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL          
SEQRES  15 A  469  THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN          
SEQRES  16 A  469  GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE          
SEQRES  17 A  469  LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY          
SEQRES  18 A  469  THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN          
SEQRES  19 A  469  LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA          
SEQRES  20 A  469  MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO          
SEQRES  21 A  469  LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU          
SEQRES  22 A  469  LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU          
SEQRES  23 A  469  ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS          
SEQRES  24 A  469  TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO          
SEQRES  25 A  469  THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP          
SEQRES  26 A  469  TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER          
SEQRES  27 A  469  ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR          
SEQRES  28 A  469  ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY          
SEQRES  29 A  469  VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP          
SEQRES  30 A  469  GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER          
SEQRES  31 A  469  ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG          
SEQRES  32 A  469  ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN          
SEQRES  33 A  469  GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO          
SEQRES  34 A  469  GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU          
SEQRES  35 A  469  ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG          
SEQRES  36 A  469  GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER          
SEQRES  37 A  469  LEU                                                          
SEQRES   1 B  469  GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE          
SEQRES   2 B  469  GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY          
SEQRES   3 B  469  ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG          
SEQRES   4 B  469  PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR          
SEQRES   5 B  469  GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER          
SEQRES   6 B  469  ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU          
SEQRES   7 B  469  LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU          
SEQRES   8 B  469  PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU          
SEQRES   9 B  469  LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU          
SEQRES  10 B  469  LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP          
SEQRES  11 B  469  ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET          
SEQRES  12 B  469  LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL          
SEQRES  13 B  469  ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL          
SEQRES  14 B  469  ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL          
SEQRES  15 B  469  THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN          
SEQRES  16 B  469  GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE          
SEQRES  17 B  469  LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY          
SEQRES  18 B  469  THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN          
SEQRES  19 B  469  LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA          
SEQRES  20 B  469  MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO          
SEQRES  21 B  469  LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU          
SEQRES  22 B  469  LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU          
SEQRES  23 B  469  ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS          
SEQRES  24 B  469  TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO          
SEQRES  25 B  469  THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP          
SEQRES  26 B  469  TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER          
SEQRES  27 B  469  ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR          
SEQRES  28 B  469  ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY          
SEQRES  29 B  469  VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP          
SEQRES  30 B  469  GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER          
SEQRES  31 B  469  ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG          
SEQRES  32 B  469  ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN          
SEQRES  33 B  469  GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO          
SEQRES  34 B  469  GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU          
SEQRES  35 B  469  ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG          
SEQRES  36 B  469  GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER          
SEQRES  37 B  469  LEU                                                          
SEQRES   1 C  469  GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE          
SEQRES   2 C  469  GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY          
SEQRES   3 C  469  ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG          
SEQRES   4 C  469  PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR          
SEQRES   5 C  469  GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER          
SEQRES   6 C  469  ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU          
SEQRES   7 C  469  LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU          
SEQRES   8 C  469  PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU          
SEQRES   9 C  469  LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU          
SEQRES  10 C  469  LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP          
SEQRES  11 C  469  ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET          
SEQRES  12 C  469  LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL          
SEQRES  13 C  469  ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL          
SEQRES  14 C  469  ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL          
SEQRES  15 C  469  THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN          
SEQRES  16 C  469  GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE          
SEQRES  17 C  469  LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY          
SEQRES  18 C  469  THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN          
SEQRES  19 C  469  LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA          
SEQRES  20 C  469  MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO          
SEQRES  21 C  469  LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU          
SEQRES  22 C  469  LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU          
SEQRES  23 C  469  ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS          
SEQRES  24 C  469  TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO          
SEQRES  25 C  469  THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP          
SEQRES  26 C  469  TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER          
SEQRES  27 C  469  ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR          
SEQRES  28 C  469  ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY          
SEQRES  29 C  469  VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP          
SEQRES  30 C  469  GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER          
SEQRES  31 C  469  ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG          
SEQRES  32 C  469  ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN          
SEQRES  33 C  469  GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO          
SEQRES  34 C  469  GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU          
SEQRES  35 C  469  ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG          
SEQRES  36 C  469  GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER          
SEQRES  37 C  469  LEU                                                          
SEQRES   1 D  469  GLY ALA MET ASP ASP PRO GLY PHE GLN GLU ARG PHE PHE          
SEQRES   2 D  469  GLN GLN ARG LEU ASP HIS PHE ASN PHE GLU ARG PHE GLY          
SEQRES   3 D  469  ASN LYS THR PHE PRO GLN ARG PHE LEU VAL SER ASP ARG          
SEQRES   4 D  469  PHE TRP VAL ARG GLY GLU GLY PRO ILE PHE PHE TYR THR          
SEQRES   5 D  469  GLY ASN GLU GLY ASP VAL TRP ALA PHE ALA ASN ASN SER          
SEQRES   6 D  469  ALA PHE VAL ALA GLU LEU ALA ALA GLU ARG GLY ALA LEU          
SEQRES   7 D  469  LEU VAL PHE ALA GLU HIS ARG TYR TYR GLY LYS SER LEU          
SEQRES   8 D  469  PRO PHE GLY ALA GLN SER THR GLN ARG GLY HIS THR GLU          
SEQRES   9 D  469  LEU LEU THR VAL GLU GLN ALA LEU ALA ASP PHE ALA GLU          
SEQRES  10 D  469  LEU LEU ARG ALA LEU ARG ARG ASP LEU GLY ALA GLN ASP          
SEQRES  11 D  469  ALA PRO ALA ILE ALA PHE GLY GLY SER TYR GLY GLY MET          
SEQRES  12 D  469  LEU SER ALA TYR LEU ARG MET LYS TYR PRO HIS LEU VAL          
SEQRES  13 D  469  ALA GLY ALA LEU ALA ALA SER ALA PRO VAL LEU ALA VAL          
SEQRES  14 D  469  ALA GLY LEU GLY ASP SER ASN GLN PHE PHE ARG ASP VAL          
SEQRES  15 D  469  THR ALA ASP PHE GLU GLY GLN SER PRO LYS CYS THR GLN          
SEQRES  16 D  469  GLY VAL ARG GLU ALA PHE ARG GLN ILE LYS ASP LEU PHE          
SEQRES  17 D  469  LEU GLN GLY ALA TYR ASP THR VAL ARG TRP GLU PHE GLY          
SEQRES  18 D  469  THR CYS GLN PRO LEU SER ASP GLU LYS ASP LEU THR GLN          
SEQRES  19 D  469  LEU PHE MET PHE ALA ARG ASN ALA PHE THR VAL LEU ALA          
SEQRES  20 D  469  MET MET ASP TYR PRO TYR PRO THR ASP PHE LEU GLY PRO          
SEQRES  21 D  469  LEU PRO ALA ASN PRO VAL LYS VAL GLY CYS ASP ARG LEU          
SEQRES  22 D  469  LEU SER GLU ALA GLN ARG ILE THR GLY LEU ARG ALA LEU          
SEQRES  23 D  469  ALA GLY LEU VAL TYR ASN ALA SER GLY SER GLU HIS CYS          
SEQRES  24 D  469  TYR ASP ILE TYR ARG LEU TYR HIS SER CYS ALA ASP PRO          
SEQRES  25 D  469  THR GLY CYS GLY THR GLY PRO ASP ALA ARG ALA TRP ASP          
SEQRES  26 D  469  TYR GLN ALA CYS THR GLU ILE ASN LEU THR PHE ALA SER          
SEQRES  27 D  469  ASN ASN VAL THR ASP MET PHE PRO ASP LEU PRO PHE THR          
SEQRES  28 D  469  ASP GLU LEU ARG GLN ARG TYR CYS LEU ASP THR TRP GLY          
SEQRES  29 D  469  VAL TRP PRO ARG PRO ASP TRP LEU LEU THR SER PHE TRP          
SEQRES  30 D  469  GLY GLY ASP LEU ARG ALA ALA SER ASN ILE ILE PHE SER          
SEQRES  31 D  469  ASN GLY ASN LEU ASP PRO TRP ALA GLY GLY GLY ILE ARG          
SEQRES  32 D  469  ARG ASN LEU SER ALA SER VAL ILE ALA VAL THR ILE GLN          
SEQRES  33 D  469  GLY GLY ALA HIS HIS LEU ASP LEU ARG ALA SER HIS PRO          
SEQRES  34 D  469  GLU ASP PRO ALA SER VAL VAL GLU ALA ARG LYS LEU GLU          
SEQRES  35 D  469  ALA THR ILE ILE GLY GLU TRP VAL LYS ALA ALA ARG ARG          
SEQRES  36 D  469  GLU GLN GLN PRO ALA LEU ARG GLY GLY PRO ARG LEU SER          
SEQRES  37 D  469  LEU                                                          
HET    OPY  A1001      13                                                       
HET    OPY  B1001      13                                                       
HET    OPY  C1001      13                                                       
HET    OPY  D1001      13                                                       
HETNAM     OPY (3S)-4-OXO-4-PIPERIDIN-1-YLBUTANE-1,3-DIAMINE                    
HETSYN     OPY GSK237826A                                                       
FORMUL   5  OPY    4(C9 H19 N3 O)                                               
FORMUL   9  HOH   *248(H2 O)                                                    
HELIX    1   1 ASP A   80  SER A   88  1                                   9    
HELIX    2   2 ALA A   89  GLY A   99  1                                  11    
HELIX    3   3 PHE A  116  SER A  120  5                                   5    
HELIX    4   4 THR A  130  GLY A  150  1                                  21    
HELIX    5   5 SER A  162  TYR A  175  1                                  14    
HELIX    6   6 PRO A  188  ALA A  193  1                                   6    
HELIX    7   7 ASN A  199  SER A  213  1                                  15    
HELIX    8   8 SER A  213  GLN A  233  1                                  21    
HELIX    9   9 ALA A  235  GLY A  244  1                                  10    
HELIX   10  10 ASP A  251  MET A  272  1                                  22    
HELIX   11  11 ASN A  287  SER A  298  1                                  12    
HELIX   12  12 GLN A  301  ASN A  315  1                                  15    
HELIX   13  13 GLY A  341  CYS A  352  1                                  12    
HELIX   14  14 THR A  374  GLY A  387  1                                  14    
HELIX   15  15 ASP A  393  TRP A  400  1                                   8    
HELIX   16  16 TRP A  420  GLY A  424  5                                   5    
HELIX   17  17 HIS A  444  ARG A  448  5                                   5    
HELIX   18  18 PRO A  455  ARG A  477  1                                  23    
HELIX   19  19 ASP B   80  SER B   88  1                                   9    
HELIX   20  20 SER B   88  GLY B   99  1                                  12    
HELIX   21  21 PHE B  116  SER B  120  5                                   5    
HELIX   22  22 THR B  130  GLY B  150  1                                  21    
HELIX   23  23 SER B  162  TYR B  175  1                                  14    
HELIX   24  24 PRO B  188  ALA B  193  1                                   6    
HELIX   25  25 ASN B  199  SER B  213  1                                  15    
HELIX   26  26 SER B  213  GLN B  233  1                                  21    
HELIX   27  27 ALA B  235  GLY B  244  1                                  10    
HELIX   28  28 ASP B  251  MET B  272  1                                  22    
HELIX   29  29 ASN B  287  SER B  298  1                                  12    
HELIX   30  30 GLN B  301  ASN B  315  1                                  15    
HELIX   31  31 GLY B  341  CYS B  352  1                                  12    
HELIX   32  32 THR B  374  GLY B  387  1                                  14    
HELIX   33  33 ASP B  393  TRP B  400  1                                   8    
HELIX   34  34 TRP B  420  GLY B  424  5                                   5    
HELIX   35  35 HIS B  444  ARG B  448  5                                   5    
HELIX   36  36 PRO B  455  GLU B  479  1                                  25    
HELIX   37  37 ASP C   80  SER C   88  1                                   9    
HELIX   38  38 SER C   88  GLY C   99  1                                  12    
HELIX   39  39 PHE C  116  GLN C  122  5                                   7    
HELIX   40  40 THR C  130  LEU C  149  1                                  20    
HELIX   41  41 SER C  162  TYR C  175  1                                  14    
HELIX   42  42 LEU C  190  GLY C  194  5                                   5    
HELIX   43  43 ASN C  199  GLY C  211  1                                  13    
HELIX   44  44 SER C  213  GLY C  234  1                                  22    
HELIX   45  45 ALA C  235  GLY C  244  1                                  10    
HELIX   46  46 ASP C  251  MET C  272  1                                  22    
HELIX   47  47 ASN C  287  GLU C  299  1                                  13    
HELIX   48  48 GLN C  301  ASN C  315  1                                  15    
HELIX   49  49 ASP C  324  TYR C  329  1                                   6    
HELIX   50  50 GLY C  341  ALA C  351  1                                  11    
HELIX   51  51 THR C  374  TRP C  386  1                                  13    
HELIX   52  52 ASP C  393  TRP C  400  1                                   8    
HELIX   53  53 TRP C  420  GLY C  424  5                                   5    
HELIX   54  54 PRO C  455  ARG C  477  1                                  23    
HELIX   55  55 ASP D   80  ASN D   86  1                                   7    
HELIX   56  56 ALA D   89  GLY D   99  1                                  11    
HELIX   57  57 PHE D  116  GLN D  122  5                                   7    
HELIX   58  58 THR D  130  LEU D  149  1                                  20    
HELIX   59  59 SER D  162  TYR D  175  1                                  14    
HELIX   60  60 PRO D  188  ALA D  193  1                                   6    
HELIX   61  61 ASN D  199  SER D  213  1                                  15    
HELIX   62  62 SER D  213  GLY D  234  1                                  22    
HELIX   63  63 ALA D  235  GLY D  244  1                                  10    
HELIX   64  64 ASP D  251  MET D  272  1                                  22    
HELIX   65  65 ASN D  287  GLU D  299  1                                  13    
HELIX   66  66 GLN D  301  ASN D  315  1                                  15    
HELIX   67  67 ASP D  324  TYR D  329  1                                   6    
HELIX   68  68 GLY D  341  GLU D  354  1                                  14    
HELIX   69  69 THR D  374  GLY D  387  1                                  14    
HELIX   70  70 ASP D  393  TRP D  400  1                                   8    
HELIX   71  71 TRP D  420  GLY D  424  5                                   5    
HELIX   72  72 HIS D  444  ARG D  448  5                                   5    
HELIX   73  73 PRO D  455  ARG D  477  1                                  23    
SHEET    1   A 8 GLN A  32  ARG A  39  0                                        
SHEET    2   A 8 THR A  52  SER A  60 -1  O  PHE A  57   N  ARG A  34           
SHEET    3   A 8 LEU A 101  ALA A 105 -1  O  LEU A 102   N  SER A  60           
SHEET    4   A 8 ILE A  71  THR A  75  1  N  TYR A  74   O  VAL A 103           
SHEET    5   A 8 ALA A 156  GLY A 161  1  O  ILE A 157   N  ILE A  71           
SHEET    6   A 8 GLY A 181  ALA A 185  1  O  LEU A 183   N  ALA A 158           
SHEET    7   A 8 ILE A 410  GLY A 415  1  O  ILE A 411   N  ALA A 184           
SHEET    8   A 8 VAL A 433  ILE A 438  1  O  ILE A 434   N  PHE A 412           
SHEET    1   B 2 THR A 278  ASP A 279  0                                        
SHEET    2   B 2 PRO A 283  LEU A 284 -1  O  LEU A 284   N  THR A 278           
SHEET    1   C 8 GLN B  32  ARG B  39  0                                        
SHEET    2   C 8 THR B  52  SER B  60 -1  O  GLN B  55   N  PHE B  36           
SHEET    3   C 8 LEU B 101  ALA B 105 -1  O  PHE B 104   N  LEU B  58           
SHEET    4   C 8 ILE B  71  THR B  75  1  N  PHE B  72   O  LEU B 101           
SHEET    5   C 8 ALA B 156  GLY B 161  1  O  PHE B 159   N  PHE B  73           
SHEET    6   C 8 GLY B 181  ALA B 185  1  O  GLY B 181   N  ALA B 158           
SHEET    7   C 8 ILE B 410  GLY B 415  1  O  ILE B 411   N  ALA B 184           
SHEET    8   C 8 VAL B 433  ILE B 438  1  O  ILE B 434   N  PHE B 412           
SHEET    1   D 2 THR B 278  ASP B 279  0                                        
SHEET    2   D 2 PRO B 283  LEU B 284 -1  O  LEU B 284   N  THR B 278           
SHEET    1   E 8 GLN C  32  ARG C  39  0                                        
SHEET    2   E 8 THR C  52  SER C  60 -1  O  GLN C  55   N  PHE C  36           
SHEET    3   E 8 LEU C 101  ALA C 105 -1  O  PHE C 104   N  LEU C  58           
SHEET    4   E 8 ILE C  71  THR C  75  1  N  TYR C  74   O  VAL C 103           
SHEET    5   E 8 ALA C 156  GLY C 161  1  O  ILE C 157   N  ILE C  71           
SHEET    6   E 8 GLY C 181  ALA C 185  1  O  LEU C 183   N  ALA C 158           
SHEET    7   E 8 ILE C 410  GLY C 415  1  O  ILE C 411   N  ALA C 184           
SHEET    8   E 8 VAL C 433  ILE C 438  1  O  ILE C 434   N  PHE C 412           
SHEET    1   F 2 THR C 278  ASP C 279  0                                        
SHEET    2   F 2 PRO C 283  LEU C 284 -1  O  LEU C 284   N  THR C 278           
SHEET    1   G 8 GLN D  32  ARG D  39  0                                        
SHEET    2   G 8 THR D  52  SER D  60 -1  O  PHE D  53   N  GLN D  38           
SHEET    3   G 8 LEU D 101  ALA D 105 -1  O  PHE D 104   N  LEU D  58           
SHEET    4   G 8 ILE D  71  THR D  75  1  N  PHE D  72   O  LEU D 101           
SHEET    5   G 8 ALA D 156  GLY D 161  1  O  ILE D 157   N  ILE D  71           
SHEET    6   G 8 GLY D 181  ALA D 185  1  O  LEU D 183   N  ALA D 158           
SHEET    7   G 8 ILE D 410  GLY D 415  1  O  ILE D 411   N  ALA D 184           
SHEET    8   G 8 VAL D 433  ILE D 438  1  O  ILE D 434   N  PHE D 412           
SHEET    1   H 2 THR D 278  ASP D 279  0                                        
SHEET    2   H 2 PRO D 283  LEU D 284 -1  O  LEU D 284   N  THR D 278           
SSBOND   1 CYS A  293    CYS A  216                          1555   1555  2.06  
SSBOND   2 CYS A  322    CYS A  246                          1555   1555  2.04  
SSBOND   3 CYS A  338    CYS A  332                          1555   1555  2.05  
SSBOND   4 CYS A  382    CYS A  352                          1555   1555  2.04  
SSBOND   5 CYS B  293    CYS B  216                          1555   1555  2.04  
SSBOND   6 CYS B  322    CYS B  246                          1555   1555  2.04  
SSBOND   7 CYS B  338    CYS B  332                          1555   1555  2.05  
SSBOND   8 CYS B  382    CYS B  352                          1555   1555  2.04  
SSBOND   9 CYS C  293    CYS C  216                          1555   1555  2.05  
SSBOND  10 CYS C  322    CYS C  246                          1555   1555  2.05  
SSBOND  11 CYS C  338    CYS C  332                          1555   1555  2.06  
SSBOND  12 CYS C  382    CYS C  352                          1555   1555  2.04  
SSBOND  13 CYS D  293    CYS D  216                          1555   1555  2.04  
SSBOND  14 CYS D  322    CYS D  246                          1555   1555  2.05  
SSBOND  15 CYS D  338    CYS D  332                          1555   1555  2.05  
SSBOND  16 CYS D  382    CYS D  352                          1555   1555  2.03  
SITE     1 AC1 11 GLU A  78  SER A 162  PRO A 188  MET A 271                    
SITE     2 AC1 11 ASP A 334  THR A 336  GLY A 337  TRP A 347                    
SITE     3 AC1 11 TRP A 420  HIS A 443  HOH A 545                               
SITE     1 AC2 10 GLU B  78  SER B 162  TYR B 163  PRO B 188                    
SITE     2 AC2 10 MET B 271  ASP B 334  THR B 336  GLY B 337                    
SITE     3 AC2 10 TRP B 347  TRP B 420                                          
SITE     1 AC3 10 GLU C  78  SER C 162  TYR C 163  PRO C 188                    
SITE     2 AC3 10 MET C 271  ASP C 334  THR C 336  GLY C 337                    
SITE     3 AC3 10 TRP C 347  TRP C 420                                          
SITE     1 AC4 10 GLU D  78  SER D 162  TYR D 163  PRO D 188                    
SITE     2 AC4 10 MET D 271  ASP D 334  THR D 336  GLY D 337                    
SITE     3 AC4 10 TRP D 347  TRP D 420                                          
CRYST1   80.546  130.500  125.075  90.00 102.28  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012415  0.000000  0.002702        0.00000                         
SCALE2      0.000000  0.007663  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008182        0.00000                         
TER    3487      GLU A 479                                                      
TER    6964      GLU B 479                                                      
TER   10414      ARG C 478                                                      
TER   13837      ARG D 477                                                      
MASTER      595    0    4   73   40    0   12    614133    4   84  148          
END                                                                             

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