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LongText Report for: 5dnu-pdb

Name Class
5dnu-pdb
HEADER    HYDROLASE                               10-SEP-15   5DNU              
TITLE     CRYSTAL STRUCTURE OF STRIGA KAI2-LIKE PROTEIN IN COMPLEX WITH KARRIKIN
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SHKAI2IB;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;                             
SOURCE   3 ORGANISM_TAXID: 68872;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    KAI2 KARRIKIN STRIGA, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA                                 
REVDAT   1   17-AUG-16 5DNU    0                                                
JRNL        AUTH   Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA                        
JRNL        TITL   STRUCTURAL BASIS OF UNIQUE LIGAND SPECIFICITY OF KAI2-LIKE   
JRNL        TITL 2 PROTEIN FROM PARASITIC WEED STRIGA HERMONTHICA               
JRNL        REF    TO BE PUBLISHED                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0124                                      
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) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 91454                          
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) : 0.141                           
REMARK   3   R VALUE            (WORKING SET) : 0.140                           
REMARK   3   FREE R VALUE                     : 0.155                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4887                            
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) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6607                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.58                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1930                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 350                          
REMARK   3   BIN FREE R VALUE                    : 0.2290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2076                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.07                          
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) : -0.03000                                             
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): 0.032         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.031         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.018         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.862         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.978                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.975                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2210 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2089 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2987 ; 1.692 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4777 ; 1.057 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   276 ; 6.256 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   100 ;30.709 ;22.800       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   341 ;12.698 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;18.496 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   333 ; 0.102 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2523 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   542 ; 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):  1077 ; 2.239 ; 2.017       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1078 ; 2.240 ; 2.018       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1347 ; 2.666 ; 3.035       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1348 ; 2.673 ; 3.039       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1133 ; 2.274 ; 2.281       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1134 ; 2.273 ; 2.280       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1636 ; 2.665 ; 3.310       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2712 ; 3.501 ;17.817       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2713 ; 3.500 ;17.815       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4298 ; 2.143 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    57 ;30.658 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4413 ;12.863 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5DNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 96642                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 20.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 97.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.22                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5DNW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, TRIS, PH 7.5, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 278K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       60.42200            
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      120.84400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       90.63300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      151.05500            
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       30.21100            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       60.42200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      120.84400            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      151.05500            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       90.63300            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       30.21100            
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 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -4                                                      
REMARK 465     PRO A    -3                                                      
REMARK 465     LEU A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     SER A   270                                                      
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   OG   SER A    68     O    HOH A   401              2.15            
REMARK 500   O    HOH A   445     O    HOH A   575              2.18            
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    THR A  28     -165.38   -110.79                                   
REMARK 500    SER A  88       72.17   -164.53                                   
REMARK 500    SER A  95     -131.86     53.82                                   
REMARK 500    ARG A 123      125.18   -175.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 609        DISTANCE =  6.92 ANGSTROMS                       
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                              NA A 313  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A  64   O                                                      
REMARK 620 2 SER A  68   OG  114.2                                              
REMARK 620 3 HOH A 401   O   151.8  45.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 312  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  83   OE2                                                    
REMARK 620 2 EDO A 316   O2  126.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 311  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 267   OD1                                                    
REMARK 620 2 FMT A 302   O2  112.6                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KKN A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 311                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 312                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 313                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 319                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DNV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DNW   RELATED DB: PDB                                   
DBREF  5DNU A   -4   270  PDB    5DNU     5DNU            -4    270             
SEQRES   1 A  275  GLY PRO LEU GLY SER MET ASN ARG VAL GLU ALA ALA ARG          
SEQRES   2 A  275  ASN VAL HIS ILE VAL GLY SER GLY ASP THR THR VAL VAL          
SEQRES   3 A  275  LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS          
SEQRES   4 A  275  HIS LEU VAL PRO TYR LEU VAL ASP SER TYR ARG VAL LEU          
SEQRES   5 A  275  LEU TYR ASP ASN MET GLY ALA GLY SER THR ASN PRO GLU          
SEQRES   6 A  275  TYR PHE HIS PHE GLU ARG TYR SER THR LEU GLN GLY TYR          
SEQRES   7 A  275  ALA HIS ASP LEU LEU VAL ILE LEU HIS GLU PHE ASN ILE          
SEQRES   8 A  275  ARG SER CYS ILE PHE VAL GLY HIS SER LEU SER ALA MET          
SEQRES   9 A  275  THR GLY ALA ILE ALA SER ILE ILE ARG PRO ASP LEU PHE          
SEQRES  10 A  275  GLN LYS ILE VAL MET LEU SER ALA SER PRO ARG PHE LEU          
SEQRES  11 A  275  ASN THR ALA ASP TYR LEU GLY GLY PHE GLU PRO ALA ASP          
SEQRES  12 A  275  VAL GLU GLN LEU ALA GLY ALA ILE GLU ALA ASN TYR LYS          
SEQRES  13 A  275  SER TRP VAL SER GLY PHE ALA PRO MET VAL VAL GLY GLY          
SEQRES  14 A  275  ASP MET ASP SER VAL ALA VAL GLN GLU PHE SER ARG THR          
SEQRES  15 A  275  LEU PHE ASN MET ARG PRO ASP ILE ALA ARG SER VAL PHE          
SEQRES  16 A  275  ARG THR ILE PHE THR SER ASP LEU ARG ASP TYR LEU GLY          
SEQRES  17 A  275  ARG VAL THR VAL PRO CYS HIS ILE ILE GLN SER SER ARG          
SEQRES  18 A  275  ASP MET ALA VAL PRO VAL SER VAL ALA GLY TYR ILE HIS          
SEQRES  19 A  275  ASN ARG VAL GLY GLY ARG SER VAL VAL GLU VAL MET ASN          
SEQRES  20 A  275  THR GLU GLY HIS LEU PRO GLN LEU SER ALA PRO GLU VAL          
SEQRES  21 A  275  ALA ILE PRO VAL LEU LEU ARG HIS ILE LYS ASN ASP ILE          
SEQRES  22 A  275  ASP SER                                                      
HET    KKN  A 301      11                                                       
HET    FMT  A 302       3                                                       
HET    FMT  A 303       3                                                       
HET    FMT  A 304       3                                                       
HET    FMT  A 305       3                                                       
HET    FMT  A 306       3                                                       
HET    FMT  A 307       3                                                       
HET    FMT  A 308       3                                                       
HET    FMT  A 309       3                                                       
HET    FMT  A 310       3                                                       
HET     NA  A 311       1                                                       
HET     NA  A 312       1                                                       
HET     NA  A 313       1                                                       
HET    EDO  A 314       4                                                       
HET    EDO  A 315       4                                                       
HET    EDO  A 316       4                                                       
HET    EDO  A 317       4                                                       
HET    EDO  A 318       4                                                       
HET    BEZ  A 319       9                                                       
HETNAM     KKN 3-METHYL-2H-FURO[2,3-C]PYRAN-2-ONE                               
HETNAM     FMT FORMIC ACID                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     BEZ BENZOIC ACID                                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  KKN    C8 H6 O3                                                     
FORMUL   3  FMT    9(C H2 O2)                                                   
FORMUL  12   NA    3(NA 1+)                                                     
FORMUL  15  EDO    5(C2 H6 O2)                                                  
FORMUL  20  BEZ    C7 H6 O2                                                     
FORMUL  21  HOH   *209(H2 O)                                                    
HELIX    1 AA1 ARG A    3  ASN A    9  1                                   7    
HELIX    2 AA2 ASP A   29  LYS A   34  5                                   6    
HELIX    3 AA3 LEU A   36  LEU A   40  5                                   5    
HELIX    4 AA4 PHE A   64  SER A   68  5                                   5    
HELIX    5 AA5 THR A   69  PHE A   84  1                                  16    
HELIX    6 AA6 SER A   95  ARG A  108  1                                  14    
HELIX    7 AA7 GLU A  135  GLY A  144  1                                  10    
HELIX    8 AA8 ASN A  149  GLY A  163  1                                  15    
HELIX    9 AA9 SER A  168  PHE A  179  1                                  12    
HELIX   10 AB1 ARG A  182  THR A  195  1                                  14    
HELIX   11 AB2 LEU A  198  VAL A  205  5                                   8    
HELIX   12 AB3 VAL A  222  VAL A  232  1                                  11    
HELIX   13 AB4 LEU A  247  ALA A  252  1                                   6    
HELIX   14 AB5 ALA A  252  ASN A  266  1                                  15    
SHEET    1 AA1 7 HIS A  11  GLY A  14  0                                        
SHEET    2 AA1 7 ARG A  45  LEU A  48 -1  O  VAL A  46   N  VAL A  13           
SHEET    3 AA1 7 THR A  19  GLY A  23  1  N  VAL A  20   O  ARG A  45           
SHEET    4 AA1 7 CYS A  89  HIS A  94  1  O  VAL A  92   N  VAL A  21           
SHEET    5 AA1 7 PHE A 112  LEU A 118  1  O  VAL A 116   N  PHE A  91           
SHEET    6 AA1 7 CYS A 209  ARG A 216  1  O  HIS A 210   N  MET A 117           
SHEET    7 AA1 7 SER A 236  GLU A 244  1  O  VAL A 237   N  ILE A 211           
LINK         O   PHE A  64                NA    NA A 313     1555   1555  2.86  
LINK         OG  SER A  68                NA    NA A 313     1555   1555  2.99  
LINK         OE2 GLU A  83                NA    NA A 312     1555   1555  2.56  
LINK         OD1 ASP A 267                NA    NA A 311     1555   1555  2.48  
LINK         O2  FMT A 302                NA    NA A 311     1555   1555  2.76  
LINK        NA    NA A 313                 O   HOH A 401     1555   1555  2.25  
LINK        NA    NA A 312                 O2  EDO A 316     1555  12545  2.74  
CISPEP   1 ILE A  268    ASP A  269          0       -13.27                     
SITE     1 AC1 10 PHE A  26  SER A  95  LEU A  96  PHE A 124                    
SITE     2 AC1 10 LEU A 142  ILE A 193  PHE A 194  ALA A 219                    
SITE     3 AC1 10 HIS A 246  HOH A 424                                          
SITE     1 AC2  6 TYR A  44  ILE A  90  GLN A 113  ILE A 264                    
SITE     2 AC2  6 LYS A 265   NA A 311                                          
SITE     1 AC3  9 SER A  15  ASP A 129  TYR A 130  ARG A 199                    
SITE     2 AC3  9 TYR A 227  ARG A 231  FMT A 309  HOH A 442                    
SITE     3 AC3  9 HOH A 547                                                     
SITE     1 AC4  6 PHE A  64  GLU A  65  ARG A  66  ARG A 108                    
SITE     2 AC4  6 ASP A 110  HOH A 497                                          
SITE     1 AC5  7 PRO A 109  PHE A 112  GLN A 113  VAL A 207                    
SITE     2 AC5  7 EDO A 317  HOH A 405  HOH A 408                               
SITE     1 AC6  5 GLU A  65  SER A  68  PRO A 109  HOH A 444                    
SITE     2 AC6  5 HOH A 604                                                     
SITE     1 AC7  5 PRO A 258  VAL A 259  ARG A 262  HOH A 455                    
SITE     2 AC7  5 HOH A 462                                                     
SITE     1 AC8  5 GLN A  71  SER A 196  ASP A 197  LEU A 198                    
SITE     2 AC8  5 ARG A 204                                                     
SITE     1 AC9  8 GLY A  14  SER A  15  ARG A 199  ASP A 200                    
SITE     2 AC9  8 ARG A 231  FMT A 303  HOH A 413  HOH A 421                    
SITE     1 AD1  5 ARG A 262  HIS A 263  ASN A 266  ASP A 267                    
SITE     2 AD1  5 HOH A 500                                                     
SITE     1 AD2  5 GLN A 113  LYS A 114  ASN A 266  ASP A 267                    
SITE     2 AD2  5 FMT A 302                                                     
SITE     1 AD3  5 VAL A   4  ARG A   8  VAL A  79  GLU A  83                    
SITE     2 AD3  5 EDO A 316                                                     
SITE     1 AD4  5 HIS A  63  PHE A  64  GLU A  65  SER A  68                    
SITE     2 AD4  5 HOH A 401                                                     
SITE     1 AD5  8 PRO A  38  ARG A 123  LEU A 125  THR A 195                    
SITE     2 AD5  8 SER A 196  ASP A 197  HOH A 425  HOH A 473                    
SITE     1 AD6  7 ILE A  12  ARG A  45  TYR A 227  ASN A 230                    
SITE     2 AD6  7 ARG A 231  HOH A 493  HOH A 510                               
SITE     1 AD7  6 ARG A   8  ARG A  66  VAL A  79  HIS A  82                    
SITE     2 AD7  6  NA A 312  HOH A 543                                          
SITE     1 AD8  5 THR A 206  VAL A 207  FMT A 305  HOH A 405                    
SITE     2 AD8  5 HOH A 565                                                     
SITE     1 AD9  4 TYR A 130  LEU A 131  SER A 223  HOH A 510                    
SITE     1 AE1  5 GLN A  71  ILE A 103  ILE A 107  TYR A 201                    
SITE     2 AE1  5 HOH A 553                                                     
CRYST1   75.757   75.757  181.266  90.00  90.00 120.00 P 61 2 2     12          
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      0.013200  0.007621  0.000000        0.00000                         
SCALE2      0.000000  0.015242  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005517        0.00000                         
TER    2103      ASP A 269                                                      
MASTER      432    0   19   14    7    0   39    6 2355    1   75   22          
END                                                                             

Send your questions or comments to :
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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