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LongText Report for: 6e6u-pdb

Name Class
6e6u-pdb
HEADER    BIOSYNTHETIC PROTEIN                    25-JUL-18   6E6U              
TITLE     VARIANT C89S OF DIECKMANN CYCLASE, NCMC                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIECKMANN CYCLASE, NCMC;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROTHRIX SYRINGAE;                         
SOURCE   3 ORGANISM_TAXID: 103733;                                              
SOURCE   4 ATCC: 51364;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    DIECKMANN CYCLASE, OFF-LOADING, DIECKMANN CONDENSATION, BIOSYNTHETIC  
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.P.COGAN,S.K.NAIR                                                    
REVDAT   3   21-OCT-20 6E6U    1       JRNL   REMARK                            
REVDAT   2   12-FEB-20 6E6U    1       JRNL                                     
REVDAT   1   31-JUL-19 6E6U    0                                                
JRNL        AUTH   D.P.COGAN,J.LY,S.K.NAIR                                      
JRNL        TITL   STRUCTURAL BASIS FOR ENZYMATIC OFF-LOADING OF HYBRID         
JRNL        TITL 2 POLYKETIDES BY DIECKMANN CONDENSATION.                       
JRNL        REF    ACS CHEM.BIOL.                             2020              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   33017142                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.0C00579                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.36                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 67900                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3570                            
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4997                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 296                          
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3936                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 519                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.98                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.41000                                              
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : -0.82000                                             
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): 0.082         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.629         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4022 ; 0.021 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3784 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5491 ; 2.084 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8663 ; 1.158 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   528 ; 5.916 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   170 ;34.390 ;22.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   569 ;12.879 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;20.231 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   633 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4620 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   882 ; 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):  2124 ; 2.322 ; 2.118       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2123 ; 2.320 ; 2.117       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2648 ; 3.240 ; 3.167       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2649 ; 3.241 ; 3.167       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1898 ; 3.477 ; 2.474       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1890 ; 3.461 ; 2.472       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2831 ; 5.092 ; 3.564       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4651 ; 8.421 ;27.885       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4448 ; 7.465 ;26.660       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6E6U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000235834.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71503                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.14100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6E6Y                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM SULFATE, 2.5% PEG 400,    
REMARK 280  0.1 M HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  282K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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       39.16150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       19.58075            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.74225            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     ALA B    16                                                      
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     ASP B 185    CG   OD1  OD2                                       
REMARK 470     GLU B 189    CB   CG   CD   OE1  OE2                             
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 A  73   CD    GLU A  73   OE1    -0.067                       
REMARK 500    ARG B  70   CZ    ARG B  70   NH1     0.090                       
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    LEU A  19   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 101   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG A 178   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 240   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    LEU B  19   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ASP B  24   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ARG B  70   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG B  81   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B  81   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B 108   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG B 108   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    GLU B 247   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG B 259   NE  -  CZ  -  NH1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 259   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B 265   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 269   NE  -  CZ  -  NH1 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    SER A  89     -131.54     57.72                                   
REMARK 500    ALA B  27       81.72   -152.86                                   
REMARK 500    ALA B  33      151.19    -48.18                                   
REMARK 500    SER B  89     -131.15     54.95                                   
REMARK 500    ALA B 183       13.49   -155.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 674        DISTANCE =  5.94 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 301                 
DBREF1 6E6U A    1   272  UNP                  A0A1X9WEN9_9PSEU                 
DBREF2 6E6U A     A0A1X9WEN9                          1         272             
DBREF1 6E6U B    1   272  UNP                  A0A1X9WEN9_9PSEU                 
DBREF2 6E6U B     A0A1X9WEN9                          1         272             
SEQADV 6E6U SER A   -2  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U ASN A   -1  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U ALA A    0  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U SER A   89  UNP  A0A1X9WEN CYS    89 ENGINEERED MUTATION            
SEQADV 6E6U SER B   -2  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U ASN B   -1  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U ALA B    0  UNP  A0A1X9WEN           EXPRESSION TAG                 
SEQADV 6E6U SER B   89  UNP  A0A1X9WEN CYS    89 ENGINEERED MUTATION            
SEQRES   1 A  275  SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE          
SEQRES   2 A  275  ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL          
SEQRES   3 A  275  ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA          
SEQRES   4 A  275  ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP          
SEQRES   5 A  275  GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET          
SEQRES   6 A  275  VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL          
SEQRES   7 A  275  ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE          
SEQRES   8 A  275  SER ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG          
SEQRES   9 A  275  LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL          
SEQRES  10 A  275  PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR          
SEQRES  11 A  275  GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU          
SEQRES  12 A  275  GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR          
SEQRES  13 A  275  ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY          
SEQRES  14 A  275  ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA          
SEQRES  15 A  275  ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP          
SEQRES  16 A  275  GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU          
SEQRES  17 A  275  VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER          
SEQRES  18 A  275  GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY          
SEQRES  19 A  275  LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL          
SEQRES  20 A  275  GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU          
SEQRES  21 A  275  LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU          
SEQRES  22 A  275  LEU ALA                                                      
SEQRES   1 B  275  SER ASN ALA MET THR ALA PRO ARG ALA TRP ARG PRO ILE          
SEQRES   2 B  275  ALA GLY GLY PRO PRO ALA GLY PRO LEU VAL LEU ALA VAL          
SEQRES   3 B  275  ASP PHE ALA ALA THR GLY ARG PRO GLU ALA ALA PHE ALA          
SEQRES   4 B  275  ASP LEU VAL ALA ARG LEU ASP PRO GLY THR GLU VAL TRP          
SEQRES   5 B  275  GLU SER LEU GLN PRO PRO LEU GLY THR GLU THR GLY MET          
SEQRES   6 B  275  VAL ALA GLU ASP TYR VAL THR ARG TRP GLU GLU GLU VAL          
SEQRES   7 B  275  ARG ALA SER GLY ARG ARG ILE GLY ALA VAL LEU GLY PHE          
SEQRES   8 B  275  SER ALA GLY SER ALA PHE ALA GLY GLU LEU ALA VAL ARG          
SEQRES   9 B  275  LEU ALA ARG SER GLN PRO ARG SER PRO ARG LEU VAL VAL          
SEQRES  10 B  275  PHE ASP PRO GLU SER PRO THR THR SER THR LEU TYR TYR          
SEQRES  11 B  275  GLN PHE ARG LYS VAL VAL GLU SER LEU ALA GLY VAL LEU          
SEQRES  12 B  275  GLY GLU GLN ALA ALA ARG GLU ALA LEU ALA GLU GLY THR          
SEQRES  13 B  275  ALA ALA ALA ASP ARG ILE GLY ASP VAL GLU GLY LEU GLY          
SEQRES  14 B  275  ALA GLU LEU VAL ARG VAL PHE THR ALA ALA GLY ARG ALA          
SEQRES  15 B  275  ALA CYS ALA ALA ALA ASP LEU ASP ASP GLU PHE ALA ASP          
SEQRES  16 B  275  GLU LEU THR ALA THR TYR ARG SER PHE VAL SER TYR LEU          
SEQRES  17 B  275  VAL ALA ALA ALA ALA VAL ASP HIS VAL LYS CYS TRP SER          
SEQRES  18 B  275  GLY ALA VAL ALA VAL SER SER ALA THR PRO THR SER GLY          
SEQRES  19 B  275  LEU ASN PRO LEU ASP PRO ALA ALA ARG ALA ALA LEU VAL          
SEQRES  20 B  275  GLU ARG GLU LEU THR PHE ASP VAL HIS HIS ALA ASP LEU          
SEQRES  21 B  275  LEU ARG ASP PRO GLY VAL ALA ARG ALA VAL ALA ARG LEU          
SEQRES  22 B  275  LEU ALA                                                      
HET    SO4  A 301       5                                                       
HET    SO4  B 301       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *519(H2 O)                                                    
HELIX    1 AA1 ALA A   34  ALA A   40  1                                   7    
HELIX    2 AA2 VAL A   63  GLY A   79  1                                  17    
HELIX    3 AA3 ALA A   90  GLN A  106  1                                  17    
HELIX    4 AA4 THR A  121  LEU A  136  1                                  16    
HELIX    5 AA5 LEU A  136  GLY A  141  1                                   6    
HELIX    6 AA6 GLY A  141  ILE A  159  1                                  19    
HELIX    7 AA7 ASP A  161  ALA A  183  1                                  23    
HELIX    8 AA8 ASP A  187  VAL A  211  1                                  25    
HELIX    9 AA9 ASP A  212  SER A  218  1                                   7    
HELIX   10 AB1 ASP A  236  VAL A  244  1                                   9    
HELIX   11 AB2 HIS A  253  ARG A  259  5                                   7    
HELIX   12 AB3 ASP A  260  ALA A  272  1                                  13    
HELIX   13 AB4 ALA B   34  ARG B   41  1                                   8    
HELIX   14 AB5 VAL B   63  GLY B   79  1                                  17    
HELIX   15 AB6 ALA B   90  GLN B  106  1                                  17    
HELIX   16 AB7 THR B  121  LEU B  136  1                                  16    
HELIX   17 AB8 LEU B  136  GLY B  141  1                                   6    
HELIX   18 AB9 GLY B  141  ILE B  159  1                                  19    
HELIX   19 AC1 ASP B  161  ASP B  185  1                                  25    
HELIX   20 AC2 ASP B  187  VAL B  211  1                                  25    
HELIX   21 AC3 ASP B  212  TRP B  217  1                                   6    
HELIX   22 AC4 ASP B  236  VAL B  244  1                                   9    
HELIX   23 AC5 HIS B  253  ARG B  259  5                                   7    
HELIX   24 AC6 ASP B  260  ALA B  272  1                                  13    
SHEET    1 AA1 7 TRP A   7  ALA A  11  0                                        
SHEET    2 AA1 7 GLU A  47  SER A  51 -1  O  GLU A  50   N  ARG A   8           
SHEET    3 AA1 7 LEU A  19  VAL A  23  1  N  VAL A  20   O  TRP A  49           
SHEET    4 AA1 7 ILE A  82  PHE A  88  1  O  LEU A  86   N  LEU A  21           
SHEET    5 AA1 7 ARG A 111  PHE A 115  1  O  PHE A 115   N  GLY A  87           
SHEET    6 AA1 7 VAL A 221  SER A 224  1  O  VAL A 223   N  VAL A 114           
SHEET    7 AA1 7 ARG A 246  THR A 249  1  O  ARG A 246   N  ALA A 222           
SHEET    1 AA2 7 TRP B   7  ALA B  11  0                                        
SHEET    2 AA2 7 VAL B  48  SER B  51 -1  O  VAL B  48   N  ILE B  10           
SHEET    3 AA2 7 LEU B  19  VAL B  23  1  N  ALA B  22   O  SER B  51           
SHEET    4 AA2 7 ILE B  82  PHE B  88  1  O  LEU B  86   N  LEU B  21           
SHEET    5 AA2 7 ARG B 111  PHE B 115  1  O  PHE B 115   N  GLY B  87           
SHEET    6 AA2 7 VAL B 221  SER B 224  1  O  VAL B 223   N  VAL B 114           
SHEET    7 AA2 7 ARG B 246  THR B 249  1  O  ARG B 246   N  ALA B 222           
SITE     1 AC1  6 ARG A  81  ARG A 108  PHE A 250  HOH A 485                    
SITE     2 AC1  6 HOH A 493  HOH A 547                                          
SITE     1 AC2  3 PHE B 250  HOH B 483  HOH B 556                               
CRYST1   80.361   80.361   78.323  90.00  90.00  90.00 P 41          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      0.012444  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012444  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012768        0.00000                         
TER    1973      ALA A 272                                                      
TER    3938      ALA B 272                                                      
MASTER      385    0    2   24   14    0    3    6 4465    2   10   44          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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