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LongText Report for: 6fj4-pdb

Name Class
6fj4-pdb
HEADER    HYDROLASE                               19-JAN-18   6FJ4              
TITLE     STRUCTURE OF FAE SOLVED BY SAD FROM DATA COLLECTED AT THE PEAK OF THE 
TITLE    2 SELENIUM ABSORPTION EDGE ON ID30B                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: XYLANASE Y,1,4-BETA-D-XYLAN XYLANOHYDROLASE Y,XYLY;         
COMPND   5 EC: 3.2.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM THERMOCELLUM;                       
SOURCE   3 ORGANISM_COMMON: RUMINICLOSTRIDIUM THERMOCELLUM;                     
SOURCE   4 ORGANISM_TAXID: 1515;                                                
SOURCE   5 GENE: XYNY;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693                                      
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.MCCARTHY,C.MUELLER-DIECKMANN                                      
REVDAT   1   07-FEB-18 6FJ4    0                                                
JRNL        AUTH   A.A.MCCARTHY,R.BARRETT,A.BETEVA,H.CASEROTTO,F.DOBIAS,        
JRNL        AUTH 2 F.FELISAZ,T.GIRAUD,M.GUIJARRO,A.KHADROUCHE,M.LENTINI,        
JRNL        AUTH 3 G.A.LEONARD,M.LOPEZ MARRERO,S.MALBET-MONACO,S.MCSWEENEY,     
JRNL        AUTH 4 D.NURIZZO,G.PAPP,C.ROSSI,J.SINOIR,C.SOREZ,J.SURR,O.SVENSSON, 
JRNL        AUTH 5 U.ZANDER,F.CIPRIANI,P.THEVENEAU,C.MUELLER-DIECKMANN          
JRNL        TITL   ID30B - A VERSATILE BEAMLINE FOR MACROMOLECULAR              
JRNL        TITL 2 CRYSTALLOGRAPHY EXPERIMENTS AT THE ESRF.                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
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) : 79.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 43496                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2487                            
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) : 3195                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2290                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : -0.73000                                             
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): 0.077         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.498         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2440 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2040 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3292 ; 1.695 ; 1.940       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4749 ; 1.026 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   292 ; 5.964 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;36.890 ;23.858       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   324 ;11.160 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;17.183 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   327 ; 0.109 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2750 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   554 ; 0.002 ; 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):  1141 ; 1.035 ; 1.905       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1140 ; 1.034 ; 1.905       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1427 ; 1.619 ; 2.851       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1428 ; 1.619 ; 2.851       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1291 ; 2.067 ; 2.160       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1287 ; 1.917 ; 2.145       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1855 ; 2.510 ; 3.120       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2657 ; 5.209 ;23.071       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2622 ; 5.160 ;22.599       
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   : 1.30                                          
REMARK   3   ION PROBE RADIUS   : 0.70                                          
REMARK   3   SHRINKAGE RADIUS   : 0.70                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200008426.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : BE CRL (VERTICAL) AND RH           
REMARK 200                                   ELLIPTICAL MIRROR (HORIZONTAL)     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46013                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.2000                            
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) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CRANK2                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, 50 MM CDSO4, 5% (V/V)       
REMARK 280  GLYCEROL, AND 1 M NA-ACETATE, PH 7.5, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       32.93250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       56.01150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       56.01150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       16.46625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       56.01150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       56.01150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       49.39875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       56.01150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.01150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       16.46625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       56.01150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.01150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       49.39875            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       32.93250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR A   819     OE2  GLU A   892              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1368     O    HOH A  1374     8664     1.92            
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 894   CG    GLU A 894   CD      0.092                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 828   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    GLU A 894   OE1 -  CD  -  OE2 ANGL. DEV. = -13.9 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    VAL A 878      -49.84   -130.45                                   
REMARK 500    SEP A 954     -118.55     65.43                                   
REMARK 500    TYR A 983       89.88   -163.26                                   
REMARK 500    THR A1040      149.65    176.60                                   
REMARK 500    ASN A1047       16.04   -151.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              CD A1101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 823   SG                                                     
REMARK 620 2 HIS A 886   ND1  93.2                                              
REMARK 620 3 GLU A1017   OE1 102.3  20.8                                        
REMARK 620 4 GLU A1017   OE2 105.8  21.3   3.7                                  
REMARK 620 5 HOH A1206   O   130.5  88.3  68.1  67.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 894   OE1                                                    
REMARK 620 2 GLU A 894   OE2  51.9                                              
REMARK 620 3 HIS A1076   ND1  90.3  89.1                                        
REMARK 620 4 GLU A1079   OE1  78.3 129.9  97.3                                  
REMARK 620 5 GLU A1079   OE2 135.7 167.2 100.4  57.8                            
REMARK 620 6 HIS A1083   ND1  86.5  83.4 172.2  89.0  86.7                      
REMARK 620 7 HIS A1085   NE2 135.9  84.5  81.7 145.6  88.4  95.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 947   NE2                                                    
REMARK 620 2 HIS A1080   NE2  95.0                                              
REMARK 620 3 HOH A1372   O    93.1 117.9                                        
REMARK 620 4 HOH A1214   O    86.7  85.2 156.8                                  
REMARK 620 5 HOH A1375   O    99.8 153.8  82.9  74.3                            
REMARK 620 6 HOH A1377   O   169.2  95.8  80.8  95.4  70.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A1007   OE1                                                    
REMARK 620 2 GLU A1007   OE2  54.3                                              
REMARK 620 3 HOH A1374   O    93.0 130.8                                        
REMARK 620 4 HIS A1082   NE2  83.8  31.6 152.4                                  
REMARK 620 5 HIS A1084   NE2  76.7  26.9 155.0   8.4                            
REMARK 620 6 HOH A1368   O    89.2  88.6  51.5 101.0 105.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CD A 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1108                
DBREF  6FJ4 A  803  1077  UNP    P51584   XYNY_CLOTM     803   1077             
SEQADV 6FJ4 GLU A 1017  UNP  P51584    ASP  1017 CONFLICT                       
SEQADV 6FJ4 ASP A 1018  UNP  P51584    HIS  1018 CONFLICT                       
SEQADV 6FJ4 LEU A 1078  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 GLU A 1079  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1080  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1081  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1082  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1083  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1084  UNP  P51584              EXPRESSION TAG                 
SEQADV 6FJ4 HIS A 1085  UNP  P51584              EXPRESSION TAG                 
SEQRES   1 A  283  SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO ALA          
SEQRES   2 A  283  PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY ARG          
SEQRES   3 A  283  ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR LYS          
SEQRES   4 A  283  SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO ASN          
SEQRES   5 A  283  LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY GLY          
SEQRES   6 A  283  GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS LEU          
SEQRES   7 A  283  GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU LEU          
SEQRES   8 A  283  GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY GLY          
SEQRES   9 A  283  ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG GLN          
SEQRES  10 A  283  ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR TYR          
SEQRES  11 A  283  ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER ARG          
SEQRES  12 A  283  MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY LEU          
SEQRES  13 A  283  THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR VAL          
SEQRES  14 A  283  ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR GLY          
SEQRES  15 A  283  ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU ALA          
SEQRES  16 A  283  ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE VAL          
SEQRES  17 A  283  PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA ASN          
SEQRES  18 A  283  MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO HIS          
SEQRES  19 A  283  PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE TYR          
SEQRES  20 A  283  PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY TYR          
SEQRES  21 A  283  VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE PHE          
SEQRES  22 A  283  HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS                      
MODRES 6FJ4 MSE A  863  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A  889  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A  946  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 SEP A  954  SER  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A  955  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A  964  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A  975  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A 1024  MET  MODIFIED RESIDUE                                   
MODRES 6FJ4 MSE A 1031  MET  MODIFIED RESIDUE                                   
HET    MSE  A 863       8                                                       
HET    MSE  A 889       8                                                       
HET    MSE  A 946       8                                                       
HET    SEP  A 954      10                                                       
HET    MSE  A 955      13                                                       
HET    MSE  A 964       8                                                       
HET    MSE  A 975       8                                                       
HET    MSE  A1024       8                                                       
HET    MSE  A1031       8                                                       
HET     CD  A1101       1                                                       
HET     CD  A1102       1                                                       
HET     CD  A1103       1                                                       
HET     CD  A1104       1                                                       
HET     CD  A1105       1                                                       
HET    GOL  A1106       6                                                       
HET    GOL  A1107       6                                                       
HET    SO4  A1108       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      CD CADMIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2   CD    5(CD 2+)                                                     
FORMUL   7  GOL    2(C3 H8 O3)                                                  
FORMUL   9  SO4    O4 S 2-                                                      
FORMUL  10  HOH   *194(H2 O)                                                    
HELIX    1 AA1 PRO A  816  ASN A  821  5                                   6    
HELIX    2 AA2 LYS A  879  ASN A  890  1                                  12    
HELIX    3 AA3 ASN A  912  ASN A  920  1                                   9    
HELIX    4 AA4 ASN A  920  TYR A  929  1                                  10    
HELIX    5 AA5 THR A  937  SER A  944  1                                   8    
HELIX    6 AA6 SEP A  954  LEU A  968  1                                  15    
HELIX    7 AA7 SER A  986  GLY A 1002  1                                  17    
HELIX    8 AA8 ALA A 1020  ALA A 1033  1                                  14    
HELIX    9 AA9 TRP A 1059  LEU A 1071  1                                  13    
HELIX   10 AB1 PRO A 1072  PHE A 1074  5                                   3    
SHEET    1 AA1 8 ARG A 828  GLY A 836  0                                        
SHEET    2 AA1 8 GLY A 839  LEU A 847 -1  O  LEU A 847   N  ARG A 828           
SHEET    3 AA1 8 ILE A 897  THR A 900 -1  O  VAL A 898   N  TYR A 846           
SHEET    4 AA1 8 ILE A 859  MSE A 863  1  N  LEU A 862   O  VAL A 899           
SHEET    5 AA1 8 ARG A 948  PHE A 953  1  O  GLY A 951   N  TYR A 861           
SHEET    6 AA1 8 TYR A 973  LEU A 977  1  O  LEU A 977   N  GLY A 952           
SHEET    7 AA1 8 PHE A1009  GLY A1015  1  O  PHE A1011   N  PHE A 974           
SHEET    8 AA1 8 PHE A1048  ALA A1053  1  O  TYR A1049   N  ALA A1012           
LINK         SG  CYS A 823                CD    CD A1101     1555   1555  2.64  
LINK         C   LEU A 862                 N   MSE A 863     1555   1555  1.35  
LINK         C   MSE A 863                 N   HIS A 864     1555   1555  1.34  
LINK         ND1 HIS A 886                CD    CD A1101     1555   1555  2.37  
LINK         C   ILE A 888                 N   MSE A 889     1555   1555  1.34  
LINK         C   MSE A 889                 N   ASN A 890     1555   1555  1.33  
LINK         OE1 GLU A 894                CD    CD A1102     1555   1555  2.39  
LINK         OE2 GLU A 894                CD    CD A1102     1555   1555  2.25  
LINK         C   ARG A 945                 N   MSE A 946     1555   1555  1.35  
LINK         C   MSE A 946                 N   HIS A 947     1555   1555  1.33  
LINK         NE2 HIS A 947                CD    CD A1104     1555   1555  2.30  
LINK         C   PHE A 953                 N   SEP A 954     1555   1555  1.34  
LINK         C   SEP A 954                 N   MSE A 955     1555   1555  1.34  
LINK         C   MSE A 955                 N   GLY A 956     1555   1555  1.34  
LINK         C   VAL A 963                 N   MSE A 964     1555   1555  1.33  
LINK         C   MSE A 964                 N   VAL A 965     1555   1555  1.32  
LINK         C   PHE A 974                 N   MSE A 975     1555   1555  1.33  
LINK         C   MSE A 975                 N   PRO A 976     1555   1555  1.35  
LINK         OE1 GLU A1007                CD    CD A1103     1555   1555  2.33  
LINK         OE2 GLU A1007                CD    CD A1103     1555   1555  2.27  
LINK         C   ASN A1023                 N   MSE A1024     1555   1555  1.33  
LINK         C   MSE A1024                 N   ASN A1025     1555   1555  1.34  
LINK         C   ALA A1030                 N   MSE A1031     1555   1555  1.34  
LINK         C   MSE A1031                 N   LYS A1032     1555   1555  1.34  
LINK         ND1 HIS A1076                CD    CD A1102     1555   1555  2.38  
LINK         OE1 GLU A1079                CD    CD A1102     1555   1555  2.20  
LINK         OE2 GLU A1079                CD    CD A1102     1555   1555  2.28  
LINK         NE2 HIS A1080                CD    CD A1104     1555   1555  2.23  
LINK         ND1 HIS A1081                CD    CD A1105     1555   1555  2.25  
LINK         ND1 HIS A1083                CD    CD A1102     1555   1555  2.36  
LINK         NE2 HIS A1085                CD    CD A1102     1555   1555  2.28  
LINK        CD    CD A1103                 O   HOH A1374     1555   1555  2.19  
LINK        CD    CD A1104                 O   HOH A1372     1555   1555  2.17  
LINK        CD    CD A1104                 O   HOH A1214     1555   1555  2.16  
LINK        CD    CD A1104                 O   HOH A1375     1555   1555  2.11  
LINK        CD    CD A1104                 O   HOH A1377     1555   1555  2.48  
LINK         OE1 GLU A1017                CD    CD A1101     1555   3545  2.28  
LINK         OE2 GLU A1017                CD    CD A1101     1555   3545  2.30  
LINK         NE2 HIS A1082                CD    CD A1103     1555   8664  2.26  
LINK         NE2 HIS A1084                CD    CD A1103     1555   8664  2.26  
LINK        CD    CD A1101                 O   HOH A1206     1555   4554  2.19  
LINK        CD    CD A1103                 O   HOH A1368     1555   8664  2.23  
SITE     1 AC1  5 CYS A 823  HIS A 886  MSE A 889  GLU A1017                    
SITE     2 AC1  5 HOH A1206                                                     
SITE     1 AC2  5 GLU A 894  HIS A1076  GLU A1079  HIS A1083                    
SITE     2 AC2  5 HIS A1085                                                     
SITE     1 AC3  5 GLU A1007  HIS A1082  HIS A1084  HOH A1368                    
SITE     2 AC3  5 HOH A1374                                                     
SITE     1 AC4  6 HIS A 947  HIS A1080  HOH A1214  HOH A1372                    
SITE     2 AC4  6 HOH A1375  HOH A1377                                          
SITE     1 AC5  3 HIS A1081  SO4 A1108  HOH A1279                               
SITE     1 AC6  8 ILE A 837  ASN A 838  ASN A 907  ASN A 912                    
SITE     2 AC6  8 GLN A 915  ARG A 918  ASN A 966  HOH A1204                    
SITE     1 AC7  6 GLU A 926  SER A 927  LYS A 928  TYR A 929                    
SITE     2 AC7  6 SER A 930  HOH A1208                                          
SITE     1 AC8  3 LYS A 855  HIS A1081   CD A1105                               
CRYST1  112.023  112.023   65.865  90.00  90.00  90.00 P 41 21 2     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      0.008927  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008927  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015183        0.00000                         
TER    2318      HIS A1085                                                      
MASTER      427    0   17   10    8    0   14    6 2506    1  138   22          
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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