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LongText Report for: 5D3K-pdb

Name Class
5D3K-pdb
HEADER    HYDROLASE                               06-AUG-15   5D3K              
TITLE     CRYSTAL STRUCTURE OF THE THIOESTERASE DOMAIN OF DEOXYERYTHRONOLIDE B  
TITLE    2 SYNTHASE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ERYTHRONOLIDE SYNTHASE, MODULES 5 AND 6;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2904-3172;                                    
COMPND   5 SYNONYM: 6-DEOXYERYTHRONOLIDE B SYNTHASE III,DEBS 3,ORF 3;           
COMPND   6 EC: 2.3.1.94;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;                    
SOURCE   3 ORGANISM_TAXID: 1836;                                                
SOURCE   4 GENE: ERYA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;                                  
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PBACP                                     
KEYWDS    THIOESTERASE DOMAINE ALPHA / BETA HYDROLASE FOLD DEOXYERYTHRONOLIDE B 
KEYWDS   2 SYNTHASE, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.BERGERET,P.ARGYROPOULOS,C.N.BODDY,T.M.SCHMEING                      
REVDAT   1   09-DEC-15 5D3K    0                                                
JRNL        AUTH   P.ARGYROPOULOS,F.BERGERET,C.PARDIN,J.M.REIMER,A.PINTO,       
JRNL        AUTH 2 C.N.BODDY,T.MARTIN SCHMEING                                  
JRNL        TITL   TOWARDS A CHARACTERIZATION OF THE STRUCTURAL DETERMINANTS OF 
JRNL        TITL 2 SPECIFICITY IN THE MACROCYCLIZING THIOESTERASE FOR           
JRNL        TITL 3 DEOXYERYTHRONOLIDE B BIOSYNTHESIS.                           
JRNL        REF    BIOCHIM.BIOPHYS.ACTA                       2015              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   26592346                                                     
JRNL        DOI    10.1016/J.BBAGEN.2015.11.007                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 32914                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1638                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2436                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 113                          
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2006                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
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): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.058         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.758         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
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):  2101 ; 0.021 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1929 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2865 ; 1.995 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4437 ; 0.964 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   272 ; 5.395 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;26.522 ;22.778       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   285 ;12.589 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.645 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   310 ; 0.132 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2422 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   478 ; 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):  1084 ; 1.765 ; 1.413       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1084 ; 1.759 ; 1.412       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1357 ; 2.577 ; 2.109       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5D3K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212609.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08B1-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97957                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX300HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.21                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34562                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : 0.12000                            
REMARK 200   FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.06900                            
REMARK 200   FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC 5.8.0073                                       
REMARK 200 STARTING MODEL: 1KEZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM NA-CACODYLATE, 35-38%             
REMARK 280  POLYETHYLENE GLYCOL , 0.18-0.24 M CA-ACETATE, PEG300, PH 6.5,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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 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 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     GLU A  67    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 134    CG   CD   CE   NZ                                   
REMARK 470     GLU A 185    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     SER A 283    O                                                   
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    HOH A   612     O    HOH A   613              1.69            
REMARK 500   O    HOH A   612     O    HOH A   615              1.87            
REMARK 500   O    HOH A   437     O    HOH A   570              1.89            
REMARK 500   O    HOH A   482     O    HOH A   603              1.99            
REMARK 500   O    HOH A   401     O    HOH A   529              2.03            
REMARK 500   O    HOH A   600     O    HOH A   609              2.07            
REMARK 500   O    HOH A   408     O    HOH A   425              2.12            
REMARK 500   O    HOH A   408     O    HOH A   491              2.18            
REMARK 500   O    HOH A   489     O    HOH A   497              2.18            
REMARK 500   O    HOH A   402     O    HOH A   536              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 184   CD    GLU A 184   OE1     0.082                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  49   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 158   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ASP A 199   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 211   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 211   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ASP A 258   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 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    SER A 142     -129.40     59.61                                   
REMARK 500    GLN A 264      -85.10   -123.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE A  302                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 303  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  49   OD2                                                    
REMARK 620 2 HOH A 411   O   105.8                                              
REMARK 620 3 HOH A 568   O    83.0  92.2                                        
REMARK 620 4 VAL A  27   O    41.0 141.3  99.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 304  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 108   OE2                                                    
REMARK 620 2 ASP A 199   OD2 108.1                                              
REMARK 620 3 HOH A 500   O    78.4 172.9                                        
REMARK 620 4 GLY A 279   O    84.4  39.5 141.2                                  
REMARK 620 5 GLY A 281   O    86.6  36.1 144.6   3.5                            
REMARK 620 6 HOH A 540   O    84.8  86.5  97.1 115.9 113.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 305  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 275   OD1                                                    
REMARK 620 2 HOH A 469   O    78.9                                              
REMARK 620 3 HOH A 446   O    68.6 147.0                                        
REMARK 620 4 HOH A 459   O    99.7  89.8  90.0                                  
REMARK 620 5 GLU A 107   OE1  56.2  74.2  82.9  44.5                            
REMARK 620 6 GLU A 107   OE2  53.9  74.3  81.8  46.6   2.3                      
REMARK 620 7 HOH A 575   O    93.4  94.6  92.9 166.8 148.7 146.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 303                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5D2R   RELATED DB: PDB                                   
DBREF  5D3K A   15   283  UNP    Q03133   ERYA3_SACER   2904   3172             
SEQRES   1 A  269  SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY VAL          
SEQRES   2 A  269  SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA GLY          
SEQRES   3 A  269  LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP GLY          
SEQRES   4 A  269  PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO GLY          
SEQRES   5 A  269  GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA ILE          
SEQRES   6 A  269  SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA LEU          
SEQRES   7 A  269  ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO GLY          
SEQRES   8 A  269  TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA ALA          
SEQRES   9 A  269  VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR GLN          
SEQRES  10 A  269  GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA GLY          
SEQRES  11 A  269  ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU ASP          
SEQRES  12 A  269  ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP VAL          
SEQRES  13 A  269  TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP LEU          
SEQRES  14 A  269  GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR VAL          
SEQRES  15 A  269  ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA TYR          
SEQRES  16 A  269  ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR GLY          
SEQRES  17 A  269  LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET GLY          
SEQRES  18 A  269  PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO PHE          
SEQRES  19 A  269  GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE THR          
SEQRES  20 A  269  MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS ILE          
SEQRES  21 A  269  ASP ALA TRP LEU GLY GLY GLY ASN SER                          
HET    1PE  A 301      16                                                       
HET    1PE  A 302      13                                                       
HET     CA  A 303       1                                                       
HET     CA  A 304       1                                                       
HET     CA  A 305       1                                                       
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      CA CALCIUM ION                                                      
HETSYN     1PE PEG400                                                           
FORMUL   2  1PE    2(C10 H22 O6)                                                
FORMUL   4   CA    3(CA 2+)                                                     
FORMUL   7  HOH   *224(H2 O)                                                    
HELIX    1 AA1 SER A   16  SER A   28  1                                  13    
HELIX    2 AA2 ARG A   30  ASP A   43  1                                  14    
HELIX    3 AA3 GLY A   81  GLU A   84  5                                   4    
HELIX    4 AA4 PHE A   85  ARG A   93  1                                   9    
HELIX    5 AA5 SER A  115  GLY A  132  1                                  18    
HELIX    6 AA6 SER A  142  ARG A  158  1                                  17    
HELIX    7 AA7 GLN A  176  TRP A  182  1                                   7    
HELIX    8 AA8 TRP A  182  ARG A  193  1                                  12    
HELIX    9 AA9 ASP A  199  TRP A  216  1                                  18    
HELIX   10 AB1 PHE A  260  GLN A  264  5                                   5    
HELIX   11 AB2 HIS A  266  GLY A  279  1                                  14    
SHEET    1 AA1 2 HIS A  47  PHE A  48  0                                        
SHEET    2 AA1 2 LEU A 112  PRO A 113  1  O  LEU A 112   N  PHE A  48           
SHEET    1 AA2 7 VAL A  59  ALA A  62  0                                        
SHEET    2 AA2 7 VAL A  98  VAL A 101 -1  O  ALA A 100   N  VAL A  59           
SHEET    3 AA2 7 THR A  69  CYS A  73  1  N  CYS A  72   O  ARG A  99           
SHEET    4 AA2 7 PHE A 136  HIS A 141  1  O  ALA A 139   N  CYS A  73           
SHEET    5 AA2 7 GLY A 164  ILE A 168  1  O  ILE A 168   N  GLY A 140           
SHEET    6 AA2 7 THR A 225  ALA A 230  1  O  LEU A 226   N  LEU A 167           
SHEET    7 AA2 7 ASP A 251  VAL A 255  1  O  ASP A 251   N  LEU A 227           
LINK         OD2 ASP A  49                CA    CA A 303     1555   1555  2.27  
LINK         OE2 GLU A 108                CA    CA A 304     1555   1555  2.08  
LINK         OD2 ASP A 199                CA    CA A 304     1555   1555  2.34  
LINK         OD1 ASP A 275                CA    CA A 305     1555   1555  2.36  
LINK        CA    CA A 303                 O   HOH A 411     1555   1555  2.44  
LINK        CA    CA A 303                 O   HOH A 568     1555   1555  2.34  
LINK        CA    CA A 304                 O   HOH A 500     1555   1555  2.37  
LINK        CA    CA A 305                 O   HOH A 469     1555   1555  2.34  
LINK        CA    CA A 305                 O   HOH A 446     1555   1555  2.45  
LINK        CA    CA A 305                 O   HOH A 459     1555   1555  2.33  
LINK         O   VAL A  27                CA    CA A 303     1555   1554  2.28  
LINK         OE1 GLU A 107                CA    CA A 305     1555   2865  2.44  
LINK         OE2 GLU A 107                CA    CA A 305     1555   2865  2.49  
LINK         O   GLY A 279                CA    CA A 304     1555   3785  2.36  
LINK         O   GLY A 281                CA    CA A 304     1555   3785  2.23  
LINK        CA    CA A 304                 O   HOH A 540     1555   2865  2.47  
LINK        CA    CA A 305                 O   HOH A 575     1555   3785  2.44  
SITE     1 AC1  8 HIS A  83  ARG A  87  HIS A 141  THR A 195                    
SITE     2 AC1  8 HOH A 406  HOH A 536  HOH A 550  HOH A 566                    
SITE     1 AC2  9 TYR A  22  VAL A  31  GLN A 176  MET A 179                    
SITE     2 AC2  9 LEU A 183  THR A 187  ASP A 210  THR A 213                    
SITE     3 AC2  9 GLY A 214                                                     
SITE     1 AC3  4 VAL A  27  ASP A  49  HOH A 411  HOH A 568                    
SITE     1 AC4  3 GLU A 108  ASP A 199  HOH A 500                               
SITE     1 AC5  4 ASP A 275  HOH A 446  HOH A 459  HOH A 469                    
CRYST1  112.920  112.920   42.970  90.00  90.00 120.00 P 3 2 1       6          
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      0.008856  0.005113  0.000000        0.00000                         
SCALE2      0.000000  0.010226  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023272        0.00000                         
TER    2019      SER A 283                                                      
MASTER      409    0    5   11    9    0    8    6 2262    1   42   21          
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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