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LongText Report for: 7ywp-pdb

Name Class
7ywp-pdb
HEADER    HYDROLASE                               14-FEB-22   7YWP              
TITLE     CLOSED CONFORMATION OF OLIGOPEPTIDASE B FROM SERRATIA PROTEOMACULANS  
TITLE    2 WITH COVALENTLY BOUND TCK                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OLIGOPEPTIDASE B;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.83;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SERRATIA PROTEAMACULANS;                        
SOURCE   3 ORGANISM_TAXID: 28151;                                               
SOURCE   4 GENE: OPDB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.PETRENKO,K.M.BOYKO,A.Y.NIKOLAEVA,A.V.VLASKINA,A.G.MIKHAILOVA,     
AUTHOR   2 V.I.TIMOFEEV,T.V.RAKITINA                                            
REVDAT   1   22-FEB-23 7YWP    0                                                
JRNL        AUTH   D.E.PETRENKO,D.M.KARLINSKY,V.D.GORDEEVA,G.P.ARAPIDI,         
JRNL        AUTH 2 E.V.BRITIKOVA,V.V.BRITIKOV,A.Y.NIKOLAEVA,K.M.BOYKO,          
JRNL        AUTH 3 V.I.TIMOFEEV,I.P.KURANOVA,A.G.MIKHAILOVA,E.V.BOCHAROV,       
JRNL        AUTH 4 T.V.RAKITINA                                                 
JRNL        TITL   CRYSTAL STRUCTURE OF INHIBITOR-BOUND BACTERIAL               
JRNL        TITL 2 OLIGOPEPTIDASE B IN THE CLOSED STATE: SIMILARITY AND         
JRNL        TITL 3 DIFFERENCE BETWEEN PROTOZOAN AND BACTERIAL ENZYMES           
JRNL        REF    INT J MOL SCI                              2023              
JRNL        REFN                   ESSN 1422-0067                               
JRNL        DOI    10.3390/IJMS24032286                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 35605                          
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1877                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2610                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 148                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5531                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 417                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.296         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.235         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.226         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.943                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.896                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5697 ; 0.008 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  5125 ; 0.001 ; 0.015       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7744 ; 1.566 ; 1.656       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11790 ; 1.257 ; 1.585       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   675 ; 7.807 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   351 ;33.703 ;22.422       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   922 ;16.747 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;18.611 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   704 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6555 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1404 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   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 U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 7YWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292121052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-MAY-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9677                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37524                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.140                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.6952                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.27                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.890                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 7OB1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM LITHIUM SULFATE, 100 MM BIS       
REMARK 280  -TRIS PH 5.5, 23% PEG 3350, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
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       37.76450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.32500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.83000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.32500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.76450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.83000            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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   OG   SER A   532     C    TCK A   701              1.88            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1120     O    HOH A  1188     4455     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG A 658   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 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    THR A   3      105.34     72.95                                   
REMARK 500    ARG A  33       76.29     91.10                                   
REMARK 500    THR A  34       24.54   -141.94                                   
REMARK 500    SER A 108      -42.40   -140.22                                   
REMARK 500    GLN A 123      -27.39     88.88                                   
REMARK 500    SER A 149        5.58    114.90                                   
REMARK 500    TYR A 199       -9.25   -141.74                                   
REMARK 500    PHE A 264      -81.82    -86.29                                   
REMARK 500    PHE A 293      150.36     72.96                                   
REMARK 500    ASP A 302      118.39    -39.45                                   
REMARK 500    ARG A 325      -61.91    -27.61                                   
REMARK 500    GLN A 346      -72.81    -87.38                                   
REMARK 500    THR A 359       58.61   -154.67                                   
REMARK 500    ASP A 396       -4.01     76.37                                   
REMARK 500    TYR A 452      -81.68   -129.53                                   
REMARK 500    LEU A 498     -129.12     52.20                                   
REMARK 500    SER A 532     -113.59     65.93                                   
REMARK 500    VAL A 556       55.48     29.54                                   
REMARK 500    ASP A 560       50.46    -91.01                                   
REMARK 500    LEU A 572       -7.48     85.34                                   
REMARK 500    GLU A 579      -68.57   -108.33                                   
REMARK 500    SER A 596      106.99    -50.28                                   
REMARK 500    ALA A 603       89.88    -68.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-            
REMARK 630 METHYLBENZENESULFONAMIDE                                             
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     TCK A   701                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    TSU LYS 0QE                                              
REMARK 630 DETAILS: NULL                                                        
DBREF  7YWP A    2   677  UNP    B3VI58   B3VI58_9GAMM     2    677             
SEQRES   1 A  676  MET THR PRO PRO LYS ALA GLU LYS ARG PRO TYR PRO ILE          
SEQRES   2 A  676  THR THR HIS GLY ASP THR ARG VAL ASP ASP TYR TYR TRP          
SEQRES   3 A  676  LEU ARG ASP ASP GLU ARG THR ASP PRO GLN VAL LEU ASP          
SEQRES   4 A  676  TYR LEU GLN ALA GLU ASN ALA PHE THR ASP ALA ALA LEU          
SEQRES   5 A  676  LYS PRO GLN GLN ALA LEU ARG GLU THR LEU TYR GLU GLU          
SEQRES   6 A  676  MET VAL ALA ARG ILE PRO GLN GLN GLU HIS SER VAL PRO          
SEQRES   7 A  676  TYR VAL ARG HIS GLY TYR ARG TYR GLN THR ARG PHE GLU          
SEQRES   8 A  676  PRO GLY ASN GLU TYR ALA ILE TYR VAL ARG GLN PRO GLN          
SEQRES   9 A  676  ALA GLU SER GLU HIS TRP ASP THR LEU ILE ASP GLY ASN          
SEQRES  10 A  676  GLN ARG ALA GLU GLN ARG GLU PHE TYR THR LEU GLY GLY          
SEQRES  11 A  676  LEU GLU VAL SER PRO ASP ASN GLN LYS LEU ALA VAL ALA          
SEQRES  12 A  676  GLU ASP PHE LEU SER ARG ARG GLN TYR ASP ILE ARG PHE          
SEQRES  13 A  676  LYS ASN LEU SER ASP ASP SER TRP THR ASP GLU VAL LEU          
SEQRES  14 A  676  GLU ASN THR SER GLY SER PHE GLU TRP ALA ASN ASP SER          
SEQRES  15 A  676  ALA THR VAL TYR TYR VAL ARG LYS HIS ALA LYS THR LEU          
SEQRES  16 A  676  LEU PRO TYR GLN VAL TYR ARG HIS VAL VAL GLY THR ASP          
SEQRES  17 A  676  PRO GLN LEU ASP GLU LEU ILE TYR GLU GLU GLN ASP ASP          
SEQRES  18 A  676  THR PHE TYR VAL GLY LEU GLU LYS THR THR SER ASP ARG          
SEQRES  19 A  676  PHE ILE LEU ILE HIS LEU SER SER THR THR THR SER GLU          
SEQRES  20 A  676  ILE LEU LEU LEU ASP ALA ASP ARG ALA ASP SER THR PRO          
SEQRES  21 A  676  GLN MET PHE VAL PRO ARG ARG LYS ASP HIS GLU TYR GLY          
SEQRES  22 A  676  ILE ASP HIS TYR HIS GLN HIS PHE TYR ILE ARG SER ASN          
SEQRES  23 A  676  LYS ASP GLY LYS ASN PHE GLY LEU TYR GLN SER GLU GLN          
SEQRES  24 A  676  ALA ASP GLU ALA GLN TRP GLN THR LEU ILE ALA PRO ARG          
SEQRES  25 A  676  ILE GLU VAL MET LEU GLU GLY PHE SER LEU PHE ARG ASP          
SEQRES  26 A  676  TRP LEU VAL VAL GLU GLU ARG SER GLU GLY LEU THR GLN          
SEQRES  27 A  676  LEU ARG GLN ILE HIS TRP GLN SER GLY GLU VAL LYS ARG          
SEQRES  28 A  676  ILE ALA PHE ASP ASP PRO THR TYR THR THR TRP LEU ALA          
SEQRES  29 A  676  TYR ASN PRO GLU PRO GLU THR GLU LEU LEU ARG TYR GLY          
SEQRES  30 A  676  TYR SER SER MET THR THR PRO THR THR LEU TYR GLU LEU          
SEQRES  31 A  676  ASN LEU ASP SER ASP GLU ARG VAL MET LEU LYS GLN GLN          
SEQRES  32 A  676  GLU VAL LYS ASN PHE THR PRO GLU ASN TYR ARG SER GLU          
SEQRES  33 A  676  ARG VAL TRP VAL LYS ALA ARG ASP GLY VAL GLU VAL PRO          
SEQRES  34 A  676  VAL SER LEU VAL TYR ARG HIS ASP SER PHE ALA ARG GLY          
SEQRES  35 A  676  THR ASN PRO LEU MET VAL TYR GLY TYR GLY SER TYR GLY          
SEQRES  36 A  676  SER SER MET ASP PRO ALA PHE SER ALA SER ARG LEU SER          
SEQRES  37 A  676  LEU LEU ASP ARG GLY PHE VAL PHE VAL LEU ALA HIS ILE          
SEQRES  38 A  676  ARG GLY GLY GLY GLU LEU GLY GLN LEU TRP TYR GLU ASP          
SEQRES  39 A  676  GLY LYS LEU PHE LYS LYS GLN ASN THR PHE ASN ASP PHE          
SEQRES  40 A  676  ILE ASP VAL THR GLU ALA LEU ILE ALA GLN GLY TYR GLY          
SEQRES  41 A  676  ASP ALA LYS ARG VAL PHE ALA MET GLY GLY SER ALA GLY          
SEQRES  42 A  676  GLY LEU LEU MET GLY ALA VAL ILE ASN GLN ALA PRO GLU          
SEQRES  43 A  676  LEU PHE ASN GLY ILE VAL ALA GLN VAL PRO PHE VAL ASP          
SEQRES  44 A  676  VAL VAL THR THR MET LEU ASP GLU SER ILE PRO LEU THR          
SEQRES  45 A  676  THR GLY GLU TYR ASP GLU TRP GLY ASN PRO ASN GLN GLN          
SEQRES  46 A  676  ALA TYR TYR ASP TYR ILE LEU GLN TYR SER PRO TYR ASP          
SEQRES  47 A  676  GLN VAL LYS ALA GLN ASP TYR PRO HIS MET LEU VAL THR          
SEQRES  48 A  676  THR GLY LEU HIS ASP SER GLN VAL GLN TYR TRP GLU PRO          
SEQRES  49 A  676  ALA LYS TRP VAL ALA LYS LEU ARG GLU LEU LYS THR ASP          
SEQRES  50 A  676  ASP ARG GLN LEU LEU LEU TYR THR ASP MET ASP SER GLY          
SEQRES  51 A  676  HIS GLY GLY LYS SER GLY ARG PHE LYS ALA TYR GLU ASP          
SEQRES  52 A  676  ILE ALA LEU GLU TYR ALA PHE ILE LEU ALA LEU ALA GLU          
HET    TCK  A 701      20                                                       
HETNAM     TCK N-[(1S)-5-AMINO-1-(CHLOROACETYL)PENTYL]-4-                       
HETNAM   2 TCK  METHYLBENZENESULFONAMIDE                                        
HETSYN     TCK TOS-LYS-CH2CL                                                    
FORMUL   2  TCK    C14 H21 CL N2 O3 S                                           
FORMUL   3  HOH   *417(H2 O)                                                    
HELIX    1 AA1 TYR A   25  ARG A   29  5                                   5    
HELIX    2 AA2 ASP A   35  LEU A   53  1                                  19    
HELIX    3 AA3 GLN A   56  ARG A   70  1                                  15    
HELIX    4 AA4 GLY A  117  GLU A  122  1                                   6    
HELIX    5 AA5 ASP A  209  ASP A  213  5                                   5    
HELIX    6 AA6 ASP A  302  TRP A  306  5                                   5    
HELIX    7 AA7 THR A  410  GLU A  412  5                                   3    
HELIX    8 AA8 ASP A  438  PHE A  440  5                                   3    
HELIX    9 AA9 ARG A  467  ASP A  472  1                                   6    
HELIX   10 AB1 GLY A  489  ASP A  495  1                                   7    
HELIX   11 AB2 GLY A  496  LYS A  500  5                                   5    
HELIX   12 AB3 LYS A  501  GLN A  518  1                                  18    
HELIX   13 AB4 SER A  532  ALA A  545  1                                  14    
HELIX   14 AB5 PRO A  546  PHE A  549  5                                   4    
HELIX   15 AB6 ASP A  560  LEU A  566  1                                   7    
HELIX   16 AB7 GLN A  585  GLN A  594  1                                  10    
HELIX   17 AB8 SER A  596  VAL A  601  1                                   6    
HELIX   18 AB9 TYR A  622  LYS A  636  1                                  15    
HELIX   19 AC1 LYS A  660  ALA A  676  1                                  17    
SHEET    1 AA1 2 TYR A  12  THR A  16  0                                        
SHEET    2 AA1 2 ASP A  19  ASP A  23 -1  O  ASP A  23   N  TYR A  12           
SHEET    1 AA2 3 GLU A  75  HIS A  76  0                                        
SHEET    2 AA2 3 TYR A  85  PHE A  91 -1  O  PHE A  91   N  GLU A  75           
SHEET    3 AA2 3 TYR A  80  ARG A  82 -1  N  TYR A  80   O  TYR A  87           
SHEET    1 AA3 4 GLU A  75  HIS A  76  0                                        
SHEET    2 AA3 4 TYR A  85  PHE A  91 -1  O  PHE A  91   N  GLU A  75           
SHEET    3 AA3 4 ILE A  99  PRO A 104 -1  O  ILE A  99   N  ARG A  90           
SHEET    4 AA3 4 ASP A 112  ASP A 116 -1  O  ASP A 112   N  ARG A 102           
SHEET    1 AA4 4 THR A 128  VAL A 134  0                                        
SHEET    2 AA4 4 LYS A 140  ASP A 146 -1  O  ASP A 146   N  THR A 128           
SHEET    3 AA4 4 TYR A 153  ASN A 159 -1  O  LYS A 158   N  LEU A 141           
SHEET    4 AA4 4 SER A 164  TRP A 165 -1  O  SER A 164   N  ASN A 159           
SHEET    1 AA5 7 THR A 128  VAL A 134  0                                        
SHEET    2 AA5 7 LYS A 140  ASP A 146 -1  O  ASP A 146   N  THR A 128           
SHEET    3 AA5 7 TYR A 153  ASN A 159 -1  O  LYS A 158   N  LEU A 141           
SHEET    4 AA5 7 LEU A 170  TRP A 179 -1  O  LEU A 170   N  ILE A 155           
SHEET    5 AA5 7 THR A 185  LYS A 191 -1  O  LYS A 191   N  ASN A 172           
SHEET    6 AA5 7 PRO A 198  VAL A 205 -1  O  HIS A 204   N  VAL A 186           
SHEET    7 AA5 7 GLU A 214  GLU A 218 -1  O  ILE A 216   N  VAL A 201           
SHEET    1 AA6 4 TYR A 225  LYS A 230  0                                        
SHEET    2 AA6 4 PHE A 236  SER A 242 -1  O  SER A 242   N  TYR A 225           
SHEET    3 AA6 4 SER A 247  ASP A 253 -1  O  GLU A 248   N  LEU A 241           
SHEET    4 AA6 4 GLN A 262  MET A 263 -1  O  GLN A 262   N  LEU A 251           
SHEET    1 AA7 4 TYR A 273  TYR A 278  0                                        
SHEET    2 AA7 4 HIS A 281  SER A 286 -1  O  HIS A 281   N  TYR A 278           
SHEET    3 AA7 4 GLY A 294  SER A 298 -1  O  TYR A 296   N  ILE A 284           
SHEET    4 AA7 4 GLN A 307  ILE A 310 -1  O  LEU A 309   N  LEU A 295           
SHEET    1 AA8 4 MET A 317  LEU A 323  0                                        
SHEET    2 AA8 4 TRP A 327  SER A 334 -1  O  GLU A 331   N  GLU A 319           
SHEET    3 AA8 4 LEU A 337  HIS A 344 -1  O  ARG A 341   N  VAL A 330           
SHEET    4 AA8 4 VAL A 350  ARG A 352 -1  O  LYS A 351   N  GLN A 342           
SHEET    1 AA9 4 TYR A 360  LEU A 364  0                                        
SHEET    2 AA9 4 LEU A 374  SER A 381 -1  O  SER A 380   N  THR A 361           
SHEET    3 AA9 4 THR A 387  ASN A 392 -1  O  THR A 387   N  TYR A 379           
SHEET    4 AA9 4 ARG A 398  GLN A 403 -1  O  LYS A 402   N  LEU A 388           
SHEET    1 AB1 8 TYR A 414  LYS A 422  0                                        
SHEET    2 AB1 8 GLU A 428  ARG A 436 -1  O  VAL A 429   N  VAL A 421           
SHEET    3 AB1 8 VAL A 476  ALA A 480 -1  O  LEU A 479   N  SER A 432           
SHEET    4 AB1 8 LEU A 447  TYR A 450  1  N  TYR A 450   O  VAL A 478           
SHEET    5 AB1 8 VAL A 526  GLY A 531  1  O  PHE A 527   N  VAL A 449           
SHEET    6 AB1 8 GLY A 551  GLN A 555  1  O  GLN A 555   N  GLY A 530           
SHEET    7 AB1 8 HIS A 608  GLY A 614  1  O  LEU A 610   N  ALA A 554           
SHEET    8 AB1 8 LEU A 642  ASP A 647  1  O  LEU A 643   N  VAL A 611           
LINK         NE2 HIS A 652                 CM  TCK A 701     1555   1555  1.47  
CRYST1   75.529   89.660  108.650  90.00  90.00  90.00 P 21 21 21    4          
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      0.013240  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011153  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009204        0.00000                         
TER    5532      GLU A 677                                                      
MASTER      338    0    1   19   44    0    0    6 5968    1   21   52          
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:
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