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LongText Report for: 2WTN-pdb

Name Class
2WTN-pdb
HEADER    HYDROLASE                               17-SEP-09   2WTN              
TITLE     FERULIC ACID BOUND TO EST1E FROM BUTYRIVIBRIO                         
TITLE    2 PROTEOCLASTICUS                                                      
CAVEAT     2WTN    ASN B   20  C-ALPHA IS PLANAR                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EST1E;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PROTEOCLASTICUM;                    
SOURCE   3 ORGANISM_TAXID: 43305;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    ESTERASE, HYDROLASE, FERULIC ACID ESTERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.GOLDSTONE,V.L.ARCUS                                               
REVDAT   1   19-JAN-10 2WTN    0                                                
JRNL        AUTH   D.C.GOLDSTONE,S.G.VILLAS-BOAS,M.TILL,W.J.KELLY,              
JRNL        AUTH 2 G.T.ATTWOOD,V.L.ARCUS                                        
JRNL        TITL   STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A              
JRNL        TITL 2 PROMISCUOUS FERULOYL ESTERASE (EST1E) FROM THE               
JRNL        TITL 3 RUMEN BACTERIUM BUTYRIVIBRIO PROTEOCLASTICUS.                
JRNL        REF    PROTEINS                                   2009              
JRNL        REFN                   ESSN 1097-0134                               
JRNL        PMID   20058325                                                     
JRNL        DOI    10.1002/PROT.22662                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.81                          
REMARK   3   NUMBER OF REFLECTIONS             : 28338                          
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) : 0.16676                         
REMARK   3   R VALUE            (WORKING SET) : 0.16369                         
REMARK   3   FREE R VALUE                     : 0.22491                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1479                            
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) : 2.100                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.155                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1731                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.255                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.364                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3920                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 202                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33                             
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.085                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.70                                                
REMARK   3    B22 (A**2) : -1.60                                                
REMARK   3    B33 (A**2) : 0.53                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -1.44                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.214         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.187         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.133         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.981         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4073 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3717 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5516 ; 1.965 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8649 ; 1.066 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   505 ; 7.619 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   179 ;36.974 ;24.860       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   698 ;14.787 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;16.987 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   614 ; 0.156 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4487 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   763 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   830 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3783 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1934 ; 0.182 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2317 ; 0.090 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   210 ; 0.182 ; 0.200       
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):     9 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    36 ; 0.189 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.166 ; 0.200       
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):  3179 ; 1.517 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1017 ; 0.321 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4028 ; 1.851 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1821 ; 2.922 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1484 ; 4.183 ; 4.500       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2WTN COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41176.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU-300R                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28338                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 2                                  
REMARK 200  R MERGE                    (I) : 0.05                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.10                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 45.45                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       72.13950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.08850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       72.13950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.08850            
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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2081   LIES ON A SPECIAL POSITION.                         
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     SER A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER B    -2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     ASN A  20    CG   OD1  ND2                                       
REMARK 470     LYS A 213    CE   NZ                                             
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     ASN B  19    CG   OD1  ND2                                       
REMARK 470     ASN B  20    OD1  ND2                                            
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     LYS B 213    CD   CE   NZ                                        
REMARK 470     LYS B 239    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 136   CG    GLU B 136   CD      0.127                       
REMARK 500    GLU B 198   CB    GLU B 198   CG      0.124                       
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    PRO A 127   C   -  N   -  CD  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASP A 155   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 177   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASN B  20   N   -  CA  -  C   ANGL. DEV. =  18.5 DEGREES          
REMARK 500    PRO B  25   C   -  N   -  CD  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG B  40   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B  40   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PHE B  77   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    PHE B  77   CB  -  CG  -  CD2 ANGL. DEV. =  -4.7 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    ASN A  19       -7.28    -58.51                                   
REMARK 500    ASN A  20       72.32     38.13                                   
REMARK 500    THR A  97      -94.89    -88.92                                   
REMARK 500    SER A 105     -121.13     59.58                                   
REMARK 500    SER A 129       61.97     38.55                                   
REMARK 500    ALA A 159     -164.12   -167.76                                   
REMARK 500    HIS A 230       55.77   -144.50                                   
REMARK 500    ASN B  19     -143.17     15.35                                   
REMARK 500    ASN B  20      -81.37    -46.20                                   
REMARK 500    THR B  97      -84.84    -88.71                                   
REMARK 500    SER B 105     -117.87     68.06                                   
REMARK 500    SER B 129       60.82     39.80                                   
REMARK 500    ALA B 159     -163.80   -115.71                                   
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 LYS B   18     ASN B   19                   43.81                    
REMARK 500 ASN B   19     ASN B   20                   66.62                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN B  19        19.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN B  20         1.9      L          L   EXPECTING SP3           
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 GOL A1249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER B1249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FER A1250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1252                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1253                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WTM   RELATED DB: PDB                                   
REMARK 900  EST1E FROM BUTYRIVIBRIO PROTEOCLASTICUS                             
DBREF  2WTN A   -2   248  PDB    2WTN     2WTN            -2    248             
DBREF  2WTN B   -2   248  PDB    2WTN     2WTN            -2    248             
SEQRES   1 A  251  SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU          
SEQRES   2 A  251  ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS          
SEQRES   3 A  251  CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS          
SEQRES   4 A  251  SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU          
SEQRES   5 A  251  ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR          
SEQRES   6 A  251  GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR          
SEQRES   7 A  251  LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP          
SEQRES   8 A  251  TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET          
SEQRES   9 A  251  ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA          
SEQRES  10 A  251  ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO          
SEQRES  11 A  251  LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR          
SEQRES  12 A  251  GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE          
SEQRES  13 A  251  PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS          
SEQRES  14 A  251  GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU          
SEQRES  15 A  251  ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL          
SEQRES  16 A  251  HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER          
SEQRES  17 A  251  VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL          
SEQRES  18 A  251  THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU          
SEQRES  19 A  251  GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU          
SEQRES  20 A  251  GLN ILE ALA LYS                                              
SEQRES   1 B  251  SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU          
SEQRES   2 B  251  ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS          
SEQRES   3 B  251  CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS          
SEQRES   4 B  251  SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU          
SEQRES   5 B  251  ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR          
SEQRES   6 B  251  GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR          
SEQRES   7 B  251  LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP          
SEQRES   8 B  251  TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET          
SEQRES   9 B  251  ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA          
SEQRES  10 B  251  ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO          
SEQRES  11 B  251  LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR          
SEQRES  12 B  251  GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE          
SEQRES  13 B  251  PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS          
SEQRES  14 B  251  GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU          
SEQRES  15 B  251  ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL          
SEQRES  16 B  251  HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER          
SEQRES  17 B  251  VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL          
SEQRES  18 B  251  THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU          
SEQRES  19 B  251  GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU          
SEQRES  20 B  251  GLN ILE ALA LYS                                              
HET    GOL  A1249       6                                                       
HET    FER  B1249      14                                                       
HET    FER  A1250      14                                                       
HET    GOL  B1250       6                                                       
HET    GOL  A1251       6                                                       
HET    GOL  B1251       6                                                       
HET    GOL  B1252       6                                                       
HET    GOL  A1252       6                                                       
HET    PO4  A1253       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     FER 3-(4-HYDROXY-3-METHOXYPHENYL)-2-PROPENOIC                        
HETNAM   2 FER  ACID                                                            
HETSYN     FER FERULIC ACID                                                     
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4  GOL    6(C3 H8 O3)                                                  
FORMUL   5  FER    2(C10 H10 O4)                                                
FORMUL   6  HOH   *202(H2 O)                                                    
HELIX    1   1 GLU A   39  ILE A   52  1                                  14    
HELIX    2   2 LYS A   70  HIS A   74  5                                   5    
HELIX    3   3 THR A   75  LYS A   91  1                                  17    
HELIX    4   4 LEU A  109  GLU A  118  1                                  10    
HELIX    5   5 MET A  133  THR A  140  1                                   8    
HELIX    6   6 ASN A  168  GLN A  174  1                                   7    
HELIX    7   7 ARG A  177  TYR A  185  1                                   9    
HELIX    8   8 PRO A  201  TYR A  212  1                                  12    
HELIX    9   9 HIS A  230  ALA A  247  1                                  18    
HELIX   10  10 GLU B   39  ILE B   52  1                                  14    
HELIX   11  11 LYS B   70  HIS B   74  5                                   5    
HELIX   12  12 THR B   75  LYS B   91  1                                  17    
HELIX   13  13 LEU B  109  GLU B  118  1                                  10    
HELIX   14  14 MET B  133  THR B  140  1                                   8    
HELIX   15  15 ASN B  168  GLN B  174  1                                   7    
HELIX   16  16 ARG B  177  TYR B  185  1                                   9    
HELIX   17  17 PRO B  201  TYR B  212  1                                  12    
HELIX   18  18 HIS B  230  ALA B  247  1                                  18    
SHEET    1  AA 6 MET A   1  ASP A   4  0                                        
SHEET    2  AA 6 LYS A   9  ASP A  15 -1  O  LEU A  10   N  ILE A   3           
SHEET    3  AA 6 ALA A  55  ALA A  59 -1  O  THR A  56   N  ASP A  15           
SHEET    4  AA 6 CYS A  24  ILE A  30  1  O  PRO A  25   N  ALA A  55           
SHEET    5  AA 6 VAL A  96  ALA A 102  1  N  THR A  97   O  CYS A  24           
SHEET    6  AA 6 ILE A 122  LEU A 125  1  N  LYS A 123   O  ILE A  99           
SHEET    1  AB 2 LEU A 157  ASP A 158  0                                        
SHEET    2  AB 2 LYS A 164  LEU A 165 -1  O  LEU A 165   N  LEU A 157           
SHEET    1  AC 2 VAL A 189  HIS A 193  0                                        
SHEET    2  AC 2 CYS A 215  THR A 219  1  O  LYS A 216   N  ILE A 191           
SHEET    1  BA 6 MET B   1  ASP B   4  0                                        
SHEET    2  BA 6 LYS B   9  ASP B  15 -1  O  LEU B  10   N  ILE B   3           
SHEET    3  BA 6 ALA B  55  ALA B  59 -1  O  THR B  56   N  ASP B  15           
SHEET    4  BA 6 CYS B  24  ILE B  30  1  O  PRO B  25   N  ALA B  55           
SHEET    5  BA 6 VAL B  96  ALA B 102  1  N  THR B  97   O  CYS B  24           
SHEET    6  BA 6 ILE B 122  LEU B 125  1  N  LYS B 123   O  ILE B  99           
SHEET    1  BB 2 LEU B 157  ASP B 158  0                                        
SHEET    2  BB 2 LYS B 164  LEU B 165 -1  O  LEU B 165   N  LEU B 157           
SHEET    1  BC 2 VAL B 189  HIS B 193  0                                        
SHEET    2  BC 2 CYS B 215  THR B 219  1  O  LYS B 216   N  ILE B 191           
CISPEP   1 ASN B   20    PRO B   21          0       -15.09                     
SITE     1 AC1  7 HIS A  31  GLY A  32  GLU A  39  HIS A  41                    
SITE     2 AC1  7 HIS A 104  SER A 105  FER A1250                               
SITE     1 AC2 12 GLY B  32  PHE B  33  SER B 105  GLN B 106                    
SITE     2 AC2 12 MET B 133  LEU B 143  LEU B 144  TRP B 160                    
SITE     3 AC2 12 TYR B 169  HIS B 225  HOH B2089  HOH B2090                    
SITE     1 AC3  7 GLY A  32  PHE A  33  THR A  34  SER A 105                    
SITE     2 AC3  7 GLN A 106  TRP A 160  GOL A1249                               
SITE     1 AC4  8 GLN A 174  THR A 175  HOH A2068  HOH A2069                    
SITE     2 AC4  8 ARG B 119  ASP B 180  PHE B 181  HOH B2091                    
SITE     1 AC5  9 ASP A 155  LYS A 166  GLY A 167  ASN A 168                    
SITE     2 AC5  9 HOH A2105  HOH A2106  ASP B  88  LYS B  91                    
SITE     3 AC5  9 HOH B2034                                                     
SITE     1 AC6  7 ASP A  88  LYS A  91  ASP B 155  LYS B 166                    
SITE     2 AC6  7 GLY B 167  ASN B 168  HOH B2092                               
SITE     1 AC7  7 HOH A2027  ASP B   4  ASP B   6  ALA B  85                    
SITE     2 AC7  7 HOH B2033  HOH B2093  HOH B2094                               
SITE     1 AC8  8 ARG A 119  ASP A 180  PHE A 181  HOH A2107                    
SITE     2 AC8  8 HOH A2108  GLN B 174  THR B 175  HOH B2061                    
SITE     1 AC9  6 GLY A 145  LEU A 146  LYS A 147  LYS B 147                    
SITE     2 AC9  6 ASP B 149  PRO B 150                                          
CRYST1  144.279   48.177   97.035  90.00 127.74  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006931  0.000000  0.005365        0.00000                         
SCALE2      0.000000  0.020757  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013032        0.00000                         
TER    1964      LYS A 248                                                      
TER    3922      LYS B 248                                                      
MASTER      414    0    9   18   20    0   20    6 4191    2   69   40          
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.
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