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LongText Report for: 6tf5-pdb

Name Class
6tf5-pdb
HEADER    HYDROLASE                               13-NOV-19   6TF5              
TITLE     OLIGOPEPTIDASE B FROM S. PROTEOMACULANS WITH MODIFIED HINGE REGION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OLIGOPEPTIDASE B;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 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    PEPTIDASE, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.PETRENKO,A.Y.NIKOLAEVA,V.A.LAZARENKO,P.V.DOROVATOVSKIY,           
AUTHOR   2 A.V.VLASKINA,D.A.KORZHENEVSKIY,A.G.MIKHAILOVA,T.V.RAKITINA,          
AUTHOR   3 V.I.TIMOFEEV                                                         
REVDAT   1   25-NOV-20 6TF5    0                                                
JRNL        AUTH   D.E.PETRENKO,A.Y.NIKOLAEVA,V.A.LAZARENKO,P.V.DOROVATOVSKIY,  
JRNL        AUTH 2 A.V.VLASKINA,D.A.KORZHENEVSKIY,A.G.MIKHAILOVA,T.V.RAKITINA,  
JRNL        AUTH 3 V.I.TIMOFEEV                                                 
JRNL        TITL   OLIGOPEPTIDASE B FROM S. PROTEOMACULANS WITH MODIFIED HINGE  
JRNL        TITL 2 REGION                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0257                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 52370                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2760                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3799                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2360                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 200                          
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5545                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 216                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
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): 0.187         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.116         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.127         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5701 ; 0.010 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  4999 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7751 ; 1.632 ; 1.651       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11597 ; 1.346 ; 1.575       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   678 ; 7.673 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   354 ;33.362 ;22.429       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   925 ;16.822 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;19.542 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   703 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6490 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1289 ; 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 : NULL                                                 
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 6TF5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292105270.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-19                          
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               : KURCHATOV SNC                      
REMARK 200  BEAMLINE                       : K4.4                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.844                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 23.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.450                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 2XE4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
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       36.60500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.44500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.44500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.60500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.51000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 29030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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   O    PHE A   224     O    HOH A   701              2.17            
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  70   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 436   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 436   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 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    ARG A  33       32.67     70.10                                   
REMARK 500    ASP A 163       16.24     55.90                                   
REMARK 500    ALA A 193       74.18    -68.72                                   
REMARK 500    LYS A 194      -70.76    162.33                                   
REMARK 500    TYR A 199      -18.08   -140.96                                   
REMARK 500    PHE A 264      -84.56    -91.45                                   
REMARK 500    GLN A 280       17.91     59.51                                   
REMARK 500    PHE A 293      152.43     77.80                                   
REMARK 500    ALA A 365     -159.41    -94.21                                   
REMARK 500    TYR A 452      -81.78   -122.41                                   
REMARK 500    LEU A 498     -121.05     48.81                                   
REMARK 500    SER A 532     -114.49     58.58                                   
REMARK 500    VAL A 556       59.02     26.12                                   
REMARK 500    ASP A 560       56.70    -92.11                                   
REMARK 500    LEU A 572      -39.14     98.20                                   
REMARK 500    GLU A 579      -61.99   -101.13                                   
REMARK 500    SER A 596      107.26    -52.24                                   
REMARK 500    HIS A 616       57.73   -100.38                                   
REMARK 500    ASP A 617      140.71    141.21                                   
REMARK 500    ASP A 649      165.05    -43.36                                   
REMARK 500    HIS A 652     -143.46    -85.84                                   
REMARK 500    LYS A 655      -72.15     59.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6TF5 A    2   677  UNP    B3VI58   B3VI58_9GAMM     2    677             
SEQADV 6TF5 HIS A    1  UNP  B3VI58              EXPRESSION TAG                 
SEQADV 6TF5 GLU A   71  UNP  B3VI58    ILE    71 CONFLICT                       
SEQADV 6TF5 ASN A   72  UNP  B3VI58    PRO    72 CONFLICT                       
SEQADV 6TF5 LEU A   73  UNP  B3VI58    GLN    73 CONFLICT                       
SEQADV 6TF5 TYR A   74  UNP  B3VI58    GLN    74 CONFLICT                       
SEQADV 6TF5 PHE A   75  UNP  B3VI58    GLU    75 CONFLICT                       
SEQADV 6TF5 GLN A   76  UNP  B3VI58    HIS    76 CONFLICT                       
SEQRES   1 A  677  HIS MET THR PRO PRO LYS ALA GLU LYS ARG PRO TYR PRO          
SEQRES   2 A  677  ILE THR THR HIS GLY ASP THR ARG VAL ASP ASP TYR TYR          
SEQRES   3 A  677  TRP LEU ARG ASP ASP GLU ARG THR ASP PRO GLN VAL LEU          
SEQRES   4 A  677  ASP TYR LEU GLN ALA GLU ASN ALA PHE THR ASP ALA ALA          
SEQRES   5 A  677  LEU LYS PRO GLN GLN ALA LEU ARG GLU THR LEU TYR GLU          
SEQRES   6 A  677  GLU MET VAL ALA ARG GLU ASN LEU TYR PHE GLN SER VAL          
SEQRES   7 A  677  PRO TYR VAL ARG HIS GLY TYR ARG TYR GLN THR ARG PHE          
SEQRES   8 A  677  GLU PRO GLY ASN GLU TYR ALA ILE TYR VAL ARG GLN PRO          
SEQRES   9 A  677  GLN ALA GLU SER GLU HIS TRP ASP THR LEU ILE ASP GLY          
SEQRES  10 A  677  ASN GLN ARG ALA GLU GLN ARG GLU PHE TYR THR LEU GLY          
SEQRES  11 A  677  GLY LEU GLU VAL SER PRO ASP ASN GLN LYS LEU ALA VAL          
SEQRES  12 A  677  ALA GLU ASP PHE LEU SER ARG ARG GLN TYR ASP ILE ARG          
SEQRES  13 A  677  PHE LYS ASN LEU SER ASP ASP SER TRP THR ASP GLU VAL          
SEQRES  14 A  677  LEU GLU ASN THR SER GLY SER PHE GLU TRP ALA ASN ASP          
SEQRES  15 A  677  SER ALA THR VAL TYR TYR VAL ARG LYS HIS ALA LYS THR          
SEQRES  16 A  677  LEU LEU PRO TYR GLN VAL TYR ARG HIS VAL VAL GLY THR          
SEQRES  17 A  677  ASP PRO GLN LEU ASP GLU LEU ILE TYR GLU GLU GLN ASP          
SEQRES  18 A  677  ASP THR PHE TYR VAL GLY LEU GLU LYS THR THR SER ASP          
SEQRES  19 A  677  ARG PHE ILE LEU ILE HIS LEU SER SER THR THR THR SER          
SEQRES  20 A  677  GLU ILE LEU LEU LEU ASP ALA ASP ARG ALA ASP SER THR          
SEQRES  21 A  677  PRO GLN MET PHE VAL PRO ARG ARG LYS ASP HIS GLU TYR          
SEQRES  22 A  677  GLY ILE ASP HIS TYR HIS GLN HIS PHE TYR ILE ARG SER          
SEQRES  23 A  677  ASN LYS ASP GLY LYS ASN PHE GLY LEU TYR GLN SER GLU          
SEQRES  24 A  677  GLN ALA ASP GLU ALA GLN TRP GLN THR LEU ILE ALA PRO          
SEQRES  25 A  677  ARG ILE GLU VAL MET LEU GLU GLY PHE SER LEU PHE ARG          
SEQRES  26 A  677  ASP TRP LEU VAL VAL GLU GLU ARG SER GLU GLY LEU THR          
SEQRES  27 A  677  GLN LEU ARG GLN ILE HIS TRP GLN SER GLY GLU VAL LYS          
SEQRES  28 A  677  ARG ILE ALA PHE ASP ASP PRO THR TYR THR THR TRP LEU          
SEQRES  29 A  677  ALA TYR ASN PRO GLU PRO GLU THR GLU LEU LEU ARG TYR          
SEQRES  30 A  677  GLY TYR SER SER MET THR THR PRO THR THR LEU TYR GLU          
SEQRES  31 A  677  LEU ASN LEU ASP SER ASP GLU ARG VAL MET LEU LYS GLN          
SEQRES  32 A  677  GLN GLU VAL LYS ASN PHE THR PRO GLU ASN TYR ARG SER          
SEQRES  33 A  677  GLU ARG VAL TRP VAL LYS ALA ARG ASP GLY VAL GLU VAL          
SEQRES  34 A  677  PRO VAL SER LEU VAL TYR ARG HIS ASP SER PHE ALA ARG          
SEQRES  35 A  677  GLY THR ASN PRO LEU MET VAL TYR GLY TYR GLY SER TYR          
SEQRES  36 A  677  GLY SER SER MET ASP PRO ALA PHE SER ALA SER ARG LEU          
SEQRES  37 A  677  SER LEU LEU ASP ARG GLY PHE VAL PHE VAL LEU ALA HIS          
SEQRES  38 A  677  ILE ARG GLY GLY GLY GLU LEU GLY GLN LEU TRP TYR GLU          
SEQRES  39 A  677  ASP GLY LYS LEU PHE LYS LYS GLN ASN THR PHE ASN ASP          
SEQRES  40 A  677  PHE ILE ASP VAL THR GLU ALA LEU ILE ALA GLN GLY TYR          
SEQRES  41 A  677  GLY ASP ALA LYS ARG VAL PHE ALA MET GLY GLY SER ALA          
SEQRES  42 A  677  GLY GLY LEU LEU MET GLY ALA VAL ILE ASN GLN ALA PRO          
SEQRES  43 A  677  GLU LEU PHE ASN GLY ILE VAL ALA GLN VAL PRO PHE VAL          
SEQRES  44 A  677  ASP VAL VAL THR THR MET LEU ASP GLU SER ILE PRO LEU          
SEQRES  45 A  677  THR THR GLY GLU TYR ASP GLU TRP GLY ASN PRO ASN GLN          
SEQRES  46 A  677  GLN ALA TYR TYR ASP TYR ILE LEU GLN TYR SER PRO TYR          
SEQRES  47 A  677  ASP GLN VAL LYS ALA GLN ASP TYR PRO HIS MET LEU VAL          
SEQRES  48 A  677  THR THR GLY LEU HIS ASP SER GLN VAL GLN TYR TRP GLU          
SEQRES  49 A  677  PRO ALA LYS TRP VAL ALA LYS LEU ARG GLU LEU LYS THR          
SEQRES  50 A  677  ASP ASP ARG GLN LEU LEU LEU TYR THR ASP MET ASP SER          
SEQRES  51 A  677  GLY HIS GLY GLY LYS SER GLY ARG PHE LYS ALA TYR GLU          
SEQRES  52 A  677  ASP ILE ALA LEU GLU TYR ALA PHE ILE LEU ALA LEU ALA          
SEQRES  53 A  677  GLU                                                          
FORMUL   2  HOH   *216(H2 O)                                                    
HELIX    1 AA1 TYR A   25  ARG A   29  5                                   5    
HELIX    2 AA2 ASP A   35  LYS A   54  1                                  20    
HELIX    3 AA3 GLN A   56  GLU A   71  1                                  16    
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 ASP A  560  LEU A  566  1                                   7    
HELIX   15 AB6 THR A  573  TYR A  577  5                                   5    
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 GLY A  657  GLU A  677  1                                  21    
SHEET    1 AA1 2 TYR A  12  THR A  16  0                                        
SHEET    2 AA1 2 ASP A  19  ASP A  23 -1  O  ARG A  21   N  ILE A  14           
SHEET    1 AA2 3 PHE A  75  GLN A  76  0                                        
SHEET    2 AA2 3 TYR A  85  PHE A  91 -1  O  PHE A  91   N  PHE A  75           
SHEET    3 AA2 3 TYR A  80  ARG A  82 -1  N  ARG A  82   O  TYR A  85           
SHEET    1 AA3 4 PHE A  75  GLN A  76  0                                        
SHEET    2 AA3 4 TYR A  85  PHE A  91 -1  O  PHE A  91   N  PHE A  75           
SHEET    3 AA3 4 ILE A  99  PRO A 104 -1  O  GLN A 103   N  ARG A  86           
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  ALA A 144   N  GLY A 130           
SHEET    3 AA4 4 TYR A 153  ASN A 159 -1  O  ASP A 154   N  GLU A 145           
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  ALA A 144   N  GLY A 130           
SHEET    3 AA5 7 TYR A 153  ASN A 159 -1  O  ASP A 154   N  GLU A 145           
SHEET    4 AA5 7 LEU A 170  TRP A 179 -1  O  THR A 173   N  TYR A 153           
SHEET    5 AA5 7 THR A 185  LYS A 191 -1  O  TYR A 187   N  GLU A 178           
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  TYR A 217   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  HIS A 240   N  GLY A 227           
SHEET    3 AA6 4 SER A 247  ASP A 253 -1  O  LEU A 252   N  ILE A 237           
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  SER A 298   N  PHE A 282           
SHEET    4 AA7 4 GLN A 307  ILE A 310 -1  O  GLN A 307   N  GLN A 297           
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  GLY A 320           
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  LEU A 401   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  LEU A 447           
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           
CRYST1   73.210  101.020  108.890  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      0.013659  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009184        0.00000                         
TER    5555      GLU A 677                                                      
MASTER      310    0    0   19   44    0    0    6 5761    1    0   53          
END                                                                             

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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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