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LongText Report for: 5yp2-pdb

Name Class
5yp2-pdb
HEADER    HYDROLASE                               01-NOV-17   5YP2              
TITLE     CRYSTAL STRUCTURE OF DIPEPTIDYL PEPTIDASE IV (DPP IV) WITH DPP4       
TITLE    2 INHIBITOR FROM PSEUDOXANTHOMONAS MEXICANA WO24                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE 4;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE IV,DAP IV;                        
COMPND   5 EC: 3.4.14.5;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOXANTHOMONAS MEXICANA;                     
SOURCE   3 ORGANISM_COMMON: PSEUDOMONAS SP. WO24;                               
SOURCE   4 ORGANISM_TAXID: 128785;                                              
SOURCE   5 STRAIN: WO24;                                                        
SOURCE   6 GENE: DAP4;                                                          
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: K-12;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PUC19                                     
KEYWDS    DAP IV, CLAN SC S9, PEPTIDASE, DPP4, DPP8, DPP9, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUIMOTO,S.MORISAWA,I.IIZUKA,          
AUTHOR   2 A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,Y.SAKAMOTO,T.NONAKA  
REVDAT   1   21-FEB-18 5YP2    0                                                
JRNL        AUTH   S.ROPPONGI,Y.SUZUKI,C.TATEOKA,M.FUJIMOTO,S.MORISAWA,         
JRNL        AUTH 2 I.IIZUKA,A.NAKAMURA,N.HONMA,Y.SHIDA,W.OGASAWARA,N.TANAKA,    
JRNL        AUTH 3 Y.SAKAMOTO,T.NONAKA                                          
JRNL        TITL   CRYSTAL STRUCTURES OF A BACTERIAL DIPEPTIDYL PEPTIDASE IV    
JRNL        TITL 2 REVEAL A NOVEL SUBSTRATE RECOGNITION MECHANISM DISTINCT FROM 
JRNL        TITL 3 THAT OF MAMMALIAN ORTHOLOGUES.                               
JRNL        REF    SCI REP                       V.   8  2714 2018              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   29426867                                                     
JRNL        DOI    10.1038/S41598-018-21056-Y                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 89236                          
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) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4652                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.13                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.19                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6117                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3080                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 305                          
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11320                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 700                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.76000                                              
REMARK   3    B22 (A**2) : -0.81000                                             
REMARK   3    B33 (A**2) : 0.06000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.210         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.181         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.468         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11657 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 10660 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15853 ; 1.864 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 24632 ; 1.052 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1446 ; 7.321 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   544 ;31.277 ;23.051       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1832 ;15.063 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   102 ;19.460 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1721 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13142 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2528 ; 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):  5790 ; 2.517 ; 3.053       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5789 ; 2.516 ; 3.052       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7234 ; 3.592 ; 4.571       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  7235 ; 3.592 ; 4.572       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5867 ; 3.148 ; 3.358       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  5867 ; 3.148 ; 3.358       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  8620 ; 4.744 ; 4.903       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 13024 ; 6.256 ;35.739       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 12929 ; 6.232 ;35.668       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5YP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005660.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-1A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2 0.5.170                       
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93976                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.050                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.13                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.87600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5YP1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 20000, 100MM MES PH6.5, 20%      
REMARK 280  GLYCEROL, 1.5MM INHIBITOR 1C, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.94000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.94500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.11000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.94500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.94000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.11000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: 3100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 54130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     PHE A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     PHE A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     ILE A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     PHE B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     PHE B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     LEU B    11                                                      
REMARK 465     ILE B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     VAL B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     ALA B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN A   379     O    HOH A   901              1.92            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 192   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 297   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B 403   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 537   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 542   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 542   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG B 568   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG B 606   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG B 606   NE  -  CZ  -  NH2 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ASP B 641   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  36      -58.90   -121.65                                   
REMARK 500    LEU A 129      126.49   -171.74                                   
REMARK 500    SER A 162      146.83    -39.55                                   
REMARK 500    PRO A 272       44.63    -76.90                                   
REMARK 500    THR A 336      -93.90    -98.38                                   
REMARK 500    THR A 501      -42.91   -134.25                                   
REMARK 500    TYR A 527      -71.15   -118.41                                   
REMARK 500    ARG A 542       32.48    -77.05                                   
REMARK 500    SER A 543     -117.19   -112.81                                   
REMARK 500    LYS A 580       54.46   -147.16                                   
REMARK 500    THR A 583      -71.58   -113.69                                   
REMARK 500    SER A 613     -105.34     63.01                                   
REMARK 500    HIS A 626       49.75   -141.52                                   
REMARK 500    ALA A 637       58.79     29.16                                   
REMARK 500    ASP A 655      176.82     67.49                                   
REMARK 500    ASN A 660       59.97   -144.62                                   
REMARK 500    ASN A 691      -75.04   -117.37                                   
REMARK 500    LYS A 720     -142.27   -102.05                                   
REMARK 500    LYS A 744       61.74     62.59                                   
REMARK 500    LEU B  36      -66.45   -135.03                                   
REMARK 500    THR B 336      -88.63   -106.34                                   
REMARK 500    GLU B 381       58.72    -90.14                                   
REMARK 500    THR B 501      -37.09   -138.91                                   
REMARK 500    TYR B 527      -64.06   -120.16                                   
REMARK 500    SER B 543     -138.55   -152.83                                   
REMARK 500    LYS B 580       41.14   -145.94                                   
REMARK 500    THR B 583      -84.23   -120.13                                   
REMARK 500    SER B 613     -110.42     69.24                                   
REMARK 500    HIS B 626       51.87   -141.38                                   
REMARK 500    ALA B 637       56.61     36.13                                   
REMARK 500    ASP B 655      176.92     67.20                                   
REMARK 500    ASN B 660       58.13   -147.82                                   
REMARK 500    ASN B 691      -74.33   -120.04                                   
REMARK 500    LYS B 720     -140.19   -109.21                                   
REMARK 500    LYS B 744       71.61     43.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP A  144     ALA A  145                  147.24                    
REMARK 500 PRO A  638     VAL A  639                  149.85                    
REMARK 500 GLY A  718     ALA A  719                 -148.76                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8YC A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 8YC B 801 and SER B    
REMARK 800  613                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5YP1   RELATED DB: PDB                                   
REMARK 900 5YP1 IS THE SAME PROTEIN APO FORM.                                   
REMARK 900 RELATED ID: 5YP3   RELATED DB: PDB                                   
REMARK 900 5YP3 IS THE SAME PROTEIN COMPLEXED WITH ILE-PRO.                     
REMARK 900 RELATED ID: 5YP4   RELATED DB: PDB                                   
REMARK 900 5YP4 IS THE SAME PROTEIN COMPLEXED WITH LYS-PRO.                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE M12I IS MUTAGENESIS ACCORDING TO SEQUENCE DATABASE           
REMARK 999 UNIPORTKB Q6F3I7 (DAP4_PSEMX).                                       
DBREF  5YP2 A    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
DBREF  5YP2 B    1   745  UNP    Q6F3I7   DAP4_PSEMX       1    745             
SEQADV 5YP2 ILE A   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQADV 5YP2 ILE B   12  UNP  Q6F3I7    MET    12 SEE SEQUENCE DETAILS           
SEQRES   1 A  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 A  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 A  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 A  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 A  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 A  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 A  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 A  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 A  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 A  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 A  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 A  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 A  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 A  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 A  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 A  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 A  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 A  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 A  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 A  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 A  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 A  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 A  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 A  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 A  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 A  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 A  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 A  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 A  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 A  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 A  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 A  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 A  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 A  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 A  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 A  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 A  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 A  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 A  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 A  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 A  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 A  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 A  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 A  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 A  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 A  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 A  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 A  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 A  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 A  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 A  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 A  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 A  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 A  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 A  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 A  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 A  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 A  745  CYS LEU LYS PRO                                              
SEQRES   1 B  745  MET ARG LEU ALA LEU PHE ALA LEU PHE ALA LEU ILE THR          
SEQRES   2 B  745  VAL ALA THR ALA LEU PRO ALA HIS ALA GLU LYS LEU THR          
SEQRES   3 B  745  LEU GLU ALA ILE THR GLY SER ALA PRO LEU SER GLY PRO          
SEQRES   4 B  745  THR LEU THR LYS PRO GLN ILE ALA PRO ASP GLY SER ARG          
SEQRES   5 B  745  VAL THR PHE LEU ARG GLY LYS ASP ARG ASP ARG ASN ARG          
SEQRES   6 B  745  LEU ASP LEU TRP GLU TYR ASP ILE ALA SER GLY GLN THR          
SEQRES   7 B  745  ARG LEU LEU VAL ASP SER SER VAL VAL LEU PRO GLY GLU          
SEQRES   8 B  745  GLU VAL LEU SER ASP GLU GLU LYS ALA ARG ARG GLU ARG          
SEQRES   9 B  745  GLN ARG ILE ALA ALA LEU SER GLY ILE VAL ASP TYR GLN          
SEQRES  10 B  745  TRP SER PRO ASP GLY LYS ALA LEU LEU PHE PRO LEU GLY          
SEQRES  11 B  745  GLY GLU LEU TYR PHE TYR ASP LEU THR LYS SER GLY ARG          
SEQRES  12 B  745  ASP ALA VAL ARG LYS LEU THR ASN GLY GLY GLY PHE ALA          
SEQRES  13 B  745  THR ASP PRO LYS ILE SER PRO LYS GLY GLY PHE VAL SER          
SEQRES  14 B  745  PHE ILE ARG ASP ARG ASN LEU TRP ALA ILE ASP LEU ALA          
SEQRES  15 B  745  SER GLY LYS GLU VAL GLN LEU THR ARG ASP GLY SER ASP          
SEQRES  16 B  745  THR ILE GLY ASN GLY VAL ALA GLU PHE VAL ALA ASP GLU          
SEQRES  17 B  745  GLU MET ASP ARG HIS THR GLY TYR TRP TRP ALA PRO ASP          
SEQRES  18 B  745  ASP ALA ALA ILE ALA PHE ALA ARG ILE ASP GLU THR PRO          
SEQRES  19 B  745  VAL PRO VAL GLN LYS ARG TYR GLU VAL TYR PRO ASP ARG          
SEQRES  20 B  745  THR GLU VAL VAL GLU GLN ARG TYR PRO ALA ALA GLY ASP          
SEQRES  21 B  745  HIS ASN VAL ARG VAL GLN LEU GLY VAL ILE ALA PRO LYS          
SEQRES  22 B  745  THR GLY ALA ARG PRO ARG TRP ILE ASP LEU GLY LYS ASP          
SEQRES  23 B  745  PRO ASP ILE TYR LEU ALA ARG VAL ASP TRP ARG ASP PRO          
SEQRES  24 B  745  GLN ARG LEU THR PHE GLN ARG GLN SER ARG ASP GLN LYS          
SEQRES  25 B  745  LYS ILE GLU LEU ILE GLU THR THR LEU THR ASN GLY THR          
SEQRES  26 B  745  GLN ARG THR LEU VAL THR GLU THR SER THR THR TRP VAL          
SEQRES  27 B  745  PRO LEU HIS ASN ASP LEU ARG PHE LEU LYS ASP GLY ARG          
SEQRES  28 B  745  PHE LEU TRP SER SER GLU ARG SER GLY PHE GLU HIS LEU          
SEQRES  29 B  745  TYR VAL ALA SER GLU ASP GLY SER THR LEU THR ALA LEU          
SEQRES  30 B  745  THR GLN GLY GLU TRP VAL VAL ASP SER LEU LEU ALA ILE          
SEQRES  31 B  745  ASP GLU ALA ALA GLY LEU ALA TYR VAL SER GLY THR ARG          
SEQRES  32 B  745  ASP GLY ALA THR GLU ALA HIS VAL TYR ALA VAL PRO LEU          
SEQRES  33 B  745  SER GLY GLY GLU PRO ARG ARG LEU THR GLN ALA PRO GLY          
SEQRES  34 B  745  MET HIS ALA ALA THR PHE ALA ARG ASN ALA SER VAL PHE          
SEQRES  35 B  745  VAL ASP SER TRP SER SER ASP THR THR LEU PRO GLN ILE          
SEQRES  36 B  745  GLU LEU PHE LYS ALA ASP GLY THR LYS LEU ALA THR LEU          
SEQRES  37 B  745  LEU VAL ASN ASP VAL SER ASP ALA THR HIS PRO TYR ALA          
SEQRES  38 B  745  LYS TYR ARG ALA ALA HIS GLN PRO THR ALA TYR GLY THR          
SEQRES  39 B  745  LEU THR ALA ALA ASP GLY THR THR PRO LEU HIS TYR SER          
SEQRES  40 B  745  LEU ILE LYS PRO ALA GLY PHE ASP PRO LYS LYS GLN TYR          
SEQRES  41 B  745  PRO VAL VAL VAL PHE VAL TYR GLY GLY PRO ALA ALA GLN          
SEQRES  42 B  745  THR VAL THR ARG ALA TRP PRO GLY ARG SER ASP SER PHE          
SEQRES  43 B  745  PHE ASN GLN TYR LEU ALA GLN GLN GLY TYR VAL VAL PHE          
SEQRES  44 B  745  THR LEU ASP ASN ARG GLY THR PRO ARG ARG GLY ALA ALA          
SEQRES  45 B  745  PHE GLY GLY ALA LEU TYR GLY LYS GLN GLY THR VAL GLU          
SEQRES  46 B  745  VAL ASP ASP GLN LEU ARG GLY ILE GLU TRP LEU LYS SER          
SEQRES  47 B  745  GLN ALA PHE VAL ASP PRO ALA ARG ILE GLY VAL TYR GLY          
SEQRES  48 B  745  TRP SER ASN GLY GLY TYR MET THR LEU MET LEU LEU ALA          
SEQRES  49 B  745  LYS HIS ASP GLU ALA TYR ALA CYS GLY VAL ALA GLY ALA          
SEQRES  50 B  745  PRO VAL THR ASP TRP ALA LEU TYR ASP THR HIS TYR THR          
SEQRES  51 B  745  GLU ARG TYR MET ASP LEU PRO LYS ALA ASN GLU ALA GLY          
SEQRES  52 B  745  TYR ARG GLU ALA SER VAL PHE THR HIS VAL ASP GLY ILE          
SEQRES  53 B  745  GLY ALA GLY LYS LEU LEU LEU ILE HIS GLY MET ALA ASP          
SEQRES  54 B  745  ASP ASN VAL LEU PHE THR ASN SER THR LYS LEU MET SER          
SEQRES  55 B  745  GLU LEU GLN LYS ARG GLY THR PRO PHE GLU LEU MET THR          
SEQRES  56 B  745  TYR PRO GLY ALA LYS HIS GLY LEU ARG GLY SER ASP LEU          
SEQRES  57 B  745  LEU HIS ARG TYR ARG LEU THR GLU ASP PHE PHE ALA ARG          
SEQRES  58 B  745  CYS LEU LYS PRO                                              
HET    8YC  A 801      20                                                       
HET    GOL  A 802       6                                                       
HET    GOL  A 803       6                                                       
HET    8YC  B 801      20                                                       
HET    GOL  B 802       6                                                       
HETNAM     8YC (2S,5R)-1-[2-[[1-(HYDROXYMETHYL)                                 
HETNAM   2 8YC  CYCLOPENTYL]AMINO]ETHANOYL]PYRROLIDINE-2,5-                     
HETNAM   3 8YC  DICARBONITRILE                                                  
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  8YC    2(C14 H20 N4 O2)                                             
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *700(H2 O)                                                    
HELIX    1 AA1 THR A   26  GLY A   32  1                                   7    
HELIX    2 AA2 ASP A   83  LEU A   88  1                                   6    
HELIX    3 AA3 SER A   95  GLN A  105  1                                  11    
HELIX    4 AA4 SER A  141  ASP A  144  5                                   4    
HELIX    5 AA5 GLU A  203  MET A  210  1                                   8    
HELIX    6 AA6 TYR A  480  ALA A  485  1                                   6    
HELIX    7 AA7 SER A  543  GLN A  554  1                                  12    
HELIX    8 AA8 GLY A  570  ALA A  576  1                                   7    
HELIX    9 AA9 THR A  583  SER A  598  1                                  16    
HELIX   10 AB1 SER A  613  HIS A  626  1                                  14    
HELIX   11 AB2 ASP A  641  TYR A  645  5                                   5    
HELIX   12 AB3 ASP A  646  ASP A  655  1                                  10    
HELIX   13 AB4 ASN A  660  SER A  668  1                                   9    
HELIX   14 AB5 SER A  668  VAL A  673  1                                   6    
HELIX   15 AB6 ASP A  674  ILE A  676  5                                   3    
HELIX   16 AB7 PHE A  694  GLY A  708  1                                  15    
HELIX   17 AB8 GLY A  725  LYS A  744  1                                  20    
HELIX   18 AB9 THR B   26  GLY B   32  1                                   7    
HELIX   19 AC1 ASP B   83  LEU B   88  1                                   6    
HELIX   20 AC2 SER B   95  GLN B  105  1                                  11    
HELIX   21 AC3 SER B  141  ASP B  144  5                                   4    
HELIX   22 AC4 GLU B  203  MET B  210  1                                   8    
HELIX   23 AC5 TYR B  480  ARG B  484  5                                   5    
HELIX   24 AC6 SER B  543  GLN B  554  1                                  12    
HELIX   25 AC7 GLY B  570  ALA B  576  1                                   7    
HELIX   26 AC8 THR B  583  SER B  598  1                                  16    
HELIX   27 AC9 SER B  613  HIS B  626  1                                  14    
HELIX   28 AD1 ASP B  641  TYR B  645  5                                   5    
HELIX   29 AD2 ASP B  646  ASP B  655  1                                  10    
HELIX   30 AD3 LEU B  656  ALA B  659  5                                   4    
HELIX   31 AD4 ASN B  660  SER B  668  1                                   9    
HELIX   32 AD5 VAL B  669  ILE B  676  5                                   8    
HELIX   33 AD6 PHE B  694  GLY B  708  1                                  15    
HELIX   34 AD7 ARG B  724  LYS B  744  1                                  21    
SHEET    1 AA1 4 LEU A  41  ILE A  46  0                                        
SHEET    2 AA1 4 ARG A  52  GLY A  58 -1  O  LEU A  56   N  THR A  42           
SHEET    3 AA1 4 ARG A  65  ASP A  72 -1  O  TRP A  69   N  PHE A  55           
SHEET    4 AA1 4 THR A  78  VAL A  82 -1  O  LEU A  81   N  LEU A  68           
SHEET    1 AA2 4 LEU A  41  ILE A  46  0                                        
SHEET    2 AA2 4 ARG A  52  GLY A  58 -1  O  LEU A  56   N  THR A  42           
SHEET    3 AA2 4 ARG A  65  ASP A  72 -1  O  TRP A  69   N  PHE A  55           
SHEET    4 AA2 4 SER A 111  GLY A 112  1  O  SER A 111   N  LEU A  66           
SHEET    1 AA3 4 GLN A 117  TRP A 118  0                                        
SHEET    2 AA3 4 ALA A 124  LEU A 129 -1  O  LEU A 126   N  GLN A 117           
SHEET    3 AA3 4 GLU A 132  ASP A 137 -1  O  GLU A 132   N  LEU A 129           
SHEET    4 AA3 4 VAL A 146  LYS A 148 -1  O  ARG A 147   N  PHE A 135           
SHEET    1 AA4 4 THR A 157  ILE A 161  0                                        
SHEET    2 AA4 4 PHE A 167  ARG A 172 -1  O  SER A 169   N  LYS A 160           
SHEET    3 AA4 4 ASN A 175  ASP A 180 -1  O  ILE A 179   N  VAL A 168           
SHEET    4 AA4 4 LYS A 185  GLN A 188 -1  O  VAL A 187   N  ALA A 178           
SHEET    1 AA5 3 ILE A 197  ASN A 199  0                                        
SHEET    2 AA5 3 ILE A 225  ASP A 231 -1  O  ILE A 230   N  GLY A 198           
SHEET    3 AA5 3 TYR A 216  TRP A 218 -1  N  TRP A 217   O  ALA A 226           
SHEET    1 AA6 4 ILE A 197  ASN A 199  0                                        
SHEET    2 AA6 4 ILE A 225  ASP A 231 -1  O  ILE A 230   N  GLY A 198           
SHEET    3 AA6 4 ARG A 264  ILE A 270 -1  O  GLY A 268   N  PHE A 227           
SHEET    4 AA6 4 ARG A 279  TRP A 280 -1  O  ARG A 279   N  VAL A 269           
SHEET    1 AA7 2 VAL A 237  VAL A 243  0                                        
SHEET    2 AA7 2 THR A 248  ARG A 254 -1  O  VAL A 251   N  ARG A 240           
SHEET    1 AA8 4 ILE A 289  ASP A 298  0                                        
SHEET    2 AA8 4 ARG A 301  SER A 308 -1  O  THR A 303   N  ASP A 295           
SHEET    3 AA8 4 LYS A 313  THR A 320 -1  O  ILE A 317   N  PHE A 304           
SHEET    4 AA8 4 GLN A 326  THR A 333 -1  O  GLU A 332   N  ILE A 314           
SHEET    1 AA9 4 ARG A 345  PHE A 346  0                                        
SHEET    2 AA9 4 PHE A 352  SER A 356 -1  O  LEU A 353   N  ARG A 345           
SHEET    3 AA9 4 HIS A 363  ALA A 367 -1  O  TYR A 365   N  TRP A 354           
SHEET    4 AA9 4 LEU A 374  ALA A 376 -1  O  THR A 375   N  VAL A 366           
SHEET    1 AB1 4 VAL A 384  ASP A 391  0                                        
SHEET    2 AB1 4 LEU A 396  GLY A 401 -1  O  LEU A 396   N  ASP A 391           
SHEET    3 AB1 4 HIS A 410  PRO A 415 -1  O  VAL A 414   N  ALA A 397           
SHEET    4 AB1 4 ARG A 422  ARG A 423 -1  O  ARG A 422   N  ALA A 413           
SHEET    1 AB2 4 MET A 430  PHE A 435  0                                        
SHEET    2 AB2 4 VAL A 441  SER A 448 -1  O  VAL A 443   N  THR A 434           
SHEET    3 AB2 4 THR A 451  LYS A 459 -1  O  GLN A 454   N  TRP A 446           
SHEET    4 AB2 4 LYS A 464  THR A 467 -1  O  ALA A 466   N  LEU A 457           
SHEET    1 AB3 8 ALA A 491  THR A 496  0                                        
SHEET    2 AB3 8 PRO A 503  ILE A 509 -1  O  LEU A 504   N  LEU A 495           
SHEET    3 AB3 8 VAL A 557  LEU A 561 -1  O  VAL A 558   N  ILE A 509           
SHEET    4 AB3 8 TYR A 520  PHE A 525  1  N  PRO A 521   O  VAL A 557           
SHEET    5 AB3 8 VAL A 602  TRP A 612  1  O  GLY A 608   N  VAL A 522           
SHEET    6 AB3 8 CYS A 632  GLY A 636  1  O  GLY A 636   N  GLY A 611           
SHEET    7 AB3 8 LEU A 681  GLY A 686  1  O  LEU A 682   N  GLY A 633           
SHEET    8 AB3 8 GLU A 712  TYR A 716  1  O  GLU A 712   N  LEU A 681           
SHEET    1 AB4 4 LEU B  41  ILE B  46  0                                        
SHEET    2 AB4 4 ARG B  52  GLY B  58 -1  O  LEU B  56   N  THR B  42           
SHEET    3 AB4 4 ARG B  65  ASP B  72 -1  O  TRP B  69   N  PHE B  55           
SHEET    4 AB4 4 THR B  78  VAL B  82 -1  O  LEU B  81   N  LEU B  68           
SHEET    1 AB5 4 LEU B  41  ILE B  46  0                                        
SHEET    2 AB5 4 ARG B  52  GLY B  58 -1  O  LEU B  56   N  THR B  42           
SHEET    3 AB5 4 ARG B  65  ASP B  72 -1  O  TRP B  69   N  PHE B  55           
SHEET    4 AB5 4 SER B 111  GLY B 112  1  O  SER B 111   N  LEU B  66           
SHEET    1 AB6 4 GLN B 117  TRP B 118  0                                        
SHEET    2 AB6 4 ALA B 124  LEU B 129 -1  O  LEU B 126   N  GLN B 117           
SHEET    3 AB6 4 GLU B 132  ASP B 137 -1  O  TYR B 134   N  PHE B 127           
SHEET    4 AB6 4 VAL B 146  LYS B 148 -1  O  ARG B 147   N  PHE B 135           
SHEET    1 AB7 4 THR B 157  ILE B 161  0                                        
SHEET    2 AB7 4 PHE B 167  ARG B 172 -1  O  ILE B 171   N  THR B 157           
SHEET    3 AB7 4 ASN B 175  ASP B 180 -1  O  ILE B 179   N  VAL B 168           
SHEET    4 AB7 4 GLU B 186  GLN B 188 -1  O  VAL B 187   N  ALA B 178           
SHEET    1 AB8 3 ILE B 197  ASN B 199  0                                        
SHEET    2 AB8 3 ILE B 225  ASP B 231 -1  O  ILE B 230   N  GLY B 198           
SHEET    3 AB8 3 TYR B 216  TRP B 218 -1  N  TRP B 217   O  ALA B 226           
SHEET    1 AB9 4 ILE B 197  ASN B 199  0                                        
SHEET    2 AB9 4 ILE B 225  ASP B 231 -1  O  ILE B 230   N  GLY B 198           
SHEET    3 AB9 4 ARG B 264  ILE B 270 -1  O  GLY B 268   N  PHE B 227           
SHEET    4 AB9 4 ARG B 279  ILE B 281 -1  O  ILE B 281   N  LEU B 267           
SHEET    1 AC1 2 VAL B 237  VAL B 243  0                                        
SHEET    2 AC1 2 THR B 248  ARG B 254 -1  O  VAL B 251   N  ARG B 240           
SHEET    1 AC2 4 ILE B 289  ASP B 298  0                                        
SHEET    2 AC2 4 ARG B 301  SER B 308 -1  O  GLN B 307   N  TYR B 290           
SHEET    3 AC2 4 LYS B 313  THR B 320 -1  O  THR B 319   N  LEU B 302           
SHEET    4 AC2 4 THR B 325  THR B 333 -1  O  GLU B 332   N  ILE B 314           
SHEET    1 AC3 4 ARG B 345  PHE B 346  0                                        
SHEET    2 AC3 4 PHE B 352  SER B 356 -1  O  LEU B 353   N  ARG B 345           
SHEET    3 AC3 4 HIS B 363  ALA B 367 -1  O  ALA B 367   N  PHE B 352           
SHEET    4 AC3 4 LEU B 374  ALA B 376 -1  O  THR B 375   N  VAL B 366           
SHEET    1 AC4 4 VAL B 384  ASP B 391  0                                        
SHEET    2 AC4 4 LEU B 396  GLY B 401 -1  O  LEU B 396   N  ASP B 391           
SHEET    3 AC4 4 HIS B 410  PRO B 415 -1  O  TYR B 412   N  VAL B 399           
SHEET    4 AC4 4 ARG B 422  ARG B 423 -1  O  ARG B 422   N  ALA B 413           
SHEET    1 AC5 4 MET B 430  PHE B 435  0                                        
SHEET    2 AC5 4 VAL B 441  SER B 448 -1  O  VAL B 443   N  THR B 434           
SHEET    3 AC5 4 THR B 451  LYS B 459 -1  O  PHE B 458   N  PHE B 442           
SHEET    4 AC5 4 LYS B 464  THR B 467 -1  O  LEU B 465   N  LEU B 457           
SHEET    1 AC6 8 THR B 490  THR B 496  0                                        
SHEET    2 AC6 8 PRO B 503  ILE B 509 -1  O  LEU B 508   N  ALA B 491           
SHEET    3 AC6 8 VAL B 557  LEU B 561 -1  O  VAL B 558   N  ILE B 509           
SHEET    4 AC6 8 TYR B 520  PHE B 525  1  N  PRO B 521   O  VAL B 557           
SHEET    5 AC6 8 VAL B 602  TRP B 612  1  O  GLY B 608   N  VAL B 522           
SHEET    6 AC6 8 CYS B 632  GLY B 636  1  O  GLY B 636   N  GLY B 611           
SHEET    7 AC6 8 LEU B 681  GLY B 686  1  O  ILE B 684   N  ALA B 635           
SHEET    8 AC6 8 GLU B 712  TYR B 716  1  O  GLU B 712   N  LEU B 681           
LINK         OG  SER A 613                 C7  8YC A 801     1555   1555  1.43  
LINK         OG  SER B 613                 C7  8YC B 801     1555   1555  1.41  
SITE     1 AC1 12 ARG A 106  GLU A 208  GLU A 209  TYR A 527                    
SITE     2 AC1 12 SER A 613  ASN A 614  VAL A 639  TYR A 645                    
SITE     3 AC1 12 TYR A 649  ASN A 691  VAL A 692  HOH A 979                    
SITE     1 AC2  6 ARG A 106  ILE A 107  ALA A 108  ALA A 109                    
SITE     2 AC2  6 ARG A 724  HOH A 963                                          
SITE     1 AC3  6 SER A 543  ASP A 544  TRP A 612  GLY A 722                    
SITE     2 AC3  6 LEU A 723  ARG A 731                                          
SITE     1 AC4  6 ARG B 106  ILE B 107  ALA B 108  ALA B 109                    
SITE     2 AC4  6 HOH B 906  HOH B1006                                          
SITE     1 AC5 19 ARG B 106  GLU B 208  GLU B 209  TYR B 527                    
SITE     2 AC5 19 ALA B 531  TRP B 612  ASN B 614  GLY B 615                    
SITE     3 AC5 19 GLY B 616  TYR B 617  GLY B 636  ALA B 637                    
SITE     4 AC5 19 VAL B 639  TYR B 645  TYR B 649  ASN B 691                    
SITE     5 AC5 19 VAL B 692  HIS B 721  HOH B1012                               
CRYST1   59.880  120.220  231.890  90.00  90.00  90.00 P 21 21 21    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      0.016700  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008318  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004312        0.00000                         
TER    5661      PRO A 745                                                      
TER   11322      PRO B 745                                                      
MASTER      427    0    5   34   98    0   14    612078    2   60  116          
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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