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LongText Report for: 6cob-pdb

Name Class
6cob-pdb
HEADER    LYASE                                   12-MAR-18   6COB              
TITLE     ATHNL ENANTIOSELECTIVITY MUTANT AT-A9-H7 APO, Y13C,Y121L,P126F,L128W, 
TITLE    2 C131T,F179L,A209I                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-HYDROXYNITRILE LYASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ATHNL;                                                     
COMPND   5 SYNONYM: ATHNL,(R)-HYDROXYNITRILE LYASE,(R)-OXYNITRILASE,            
COMPND   6 METHYLESTERASE 5,ATMES5;                                             
COMPND   7 EC: 4.1.2.10;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: HNL, MES5, AT5G10300, F18D22_70;                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ALPHA BETA HYDROLASE GLOBULAR HYDROXYNITRILE LYASE, LYASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.J.JONES,R.J.KAZLAUSKAS,R.DESROULEAUX                                
REVDAT   1   20-MAR-19 6COB    0                                                
JRNL        AUTH   B.J.JONES,R.DESROULEAUX,R.J.KAZLAUSKAS                       
JRNL        TITL   ATHNL ENANTIOSELECTIVITY MUTANTS                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0155                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 46522                          
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) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2375                            
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) : 1.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3342                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 173                          
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4108                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 245                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : -0.07000                                             
REMARK   3    B33 (A**2) : -0.21000                                             
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): 0.112         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.129         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4366 ; 0.028 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4156 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5914 ; 2.443 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9627 ; 1.226 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   544 ; 6.411 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   192 ;34.515 ;24.167       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   785 ;15.831 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;17.198 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   640 ; 0.164 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4910 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   982 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0105   2.6807  -3.0914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0273 T22:   0.0548                                     
REMARK   3      T33:   0.0116 T12:   0.0094                                     
REMARK   3      T13:   0.0128 T23:   0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2344 L22:   0.7313                                     
REMARK   3      L33:   0.9833 L12:  -0.0359                                     
REMARK   3      L13:  -0.0313 L23:   0.3012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0656 S12:  -0.2365 S13:  -0.0871                       
REMARK   3      S21:   0.1294 S22:   0.0016 S23:   0.0352                       
REMARK   3      S31:   0.0869 S32:  -0.0697 S33:   0.0640                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   258                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.6278   7.0764 -33.1264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0191 T22:   0.0347                                     
REMARK   3      T33:   0.0374 T12:  -0.0013                                     
REMARK   3      T13:   0.0172 T23:  -0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2544 L22:   0.6533                                     
REMARK   3      L33:   0.5187 L12:  -0.1620                                     
REMARK   3      L13:  -0.1453 L23:  -0.0340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.1537 S13:   0.0269                       
REMARK   3      S21:  -0.0814 S22:   0.0040 S23:  -0.0653                       
REMARK   3      S31:  -0.0040 S32:   0.0239 S33:  -0.0121                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6COB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000223852.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97741                            
REMARK 200  MONOCHROMATOR                  : SI (111) ROSENBAUM-ROCK DOUBLE     
REMARK 200                                   -CRYSTAL MONOCHROMATOR             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48970                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.11300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.98500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.1                                          
REMARK 200 STARTING MODEL: PDBID 3DQZ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 17% PEG 3350, PH 6.2,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.99100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.67800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.55500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.67800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.99100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.55500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   259                                                      
REMARK 465     LEU A   260                                                      
REMARK 465     GLY B   259                                                      
REMARK 465     LEU B   260                                                      
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   OE1  GLU B    57     O    HOH B   401              2.02            
REMARK 500   O    HOH A   518     O    HOH A   521              2.04            
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   506     O    HOH A   514     4555     2.13            
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  38   CD    GLU A  38   OE1    -0.110                       
REMARK 500    ASP A  45   CB    ASP A  45   CG      0.135                       
REMARK 500    GLU A  57   CD    GLU A  57   OE1     0.069                       
REMARK 500    GLU A  57   CD    GLU A  57   OE2    -0.070                       
REMARK 500    SER A  59   CB    SER A  59   OG     -0.098                       
REMARK 500    GLU A  73   CD    GLU A  73   OE1     0.080                       
REMARK 500    SER A 136   CB    SER A 136   OG     -0.091                       
REMARK 500    GLU A 192   CD    GLU A 192   OE1     0.083                       
REMARK 500    SER B  29   CB    SER B  29   OG     -0.094                       
REMARK 500    SER B  59   CB    SER B  59   OG     -0.080                       
REMARK 500    TYR B 167   CG    TYR B 167   CD2    -0.084                       
REMARK 500    GLU B 182   CD    GLU B 182   OE1     0.067                       
REMARK 500    GLU B 192   CG    GLU B 192   CD      0.093                       
REMARK 500    GLU B 192   CD    GLU B 192   OE1     0.077                       
REMARK 500    SER B 205   CB    SER B 205   OG     -0.127                       
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  33   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A  33   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ASP A  56   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    SER A 136   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ARG A 157   CG  -  CD  -  NE  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    CYS A 213   CB  -  CA  -  C   ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG B  33   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG B  33   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP B  92   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    MET B 144   CG  -  SD  -  CE  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG B 157   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B 157   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG B 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    CYS B 213   CB  -  CA  -  C   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    LYS B 245   CD  -  CE  -  NZ  ANGL. DEV. = -14.4 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    CYS A  14       -4.93     77.83                                   
REMARK 500    HIS A  15     -157.86   -116.37                                   
REMARK 500    SER A  81     -124.95     59.55                                   
REMARK 500    PHE A 223       96.81   -165.97                                   
REMARK 500    CYS B  14       -7.36     73.73                                   
REMARK 500    HIS B  15     -162.78   -117.99                                   
REMARK 500    SER B  81     -118.39     64.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303                 
DBREF  6COB A    1   258  UNP    Q9LFT6   HNL_ARATH        1    258             
DBREF  6COB B    1   258  UNP    Q9LFT6   HNL_ARATH        1    258             
SEQADV 6COB CYS A   14  UNP  Q9LFT6    TYR    14 ENGINEERED MUTATION            
SEQADV 6COB LEU A  122  UNP  Q9LFT6    TYR   122 ENGINEERED MUTATION            
SEQADV 6COB PHE A  126  UNP  Q9LFT6    PRO   126 ENGINEERED MUTATION            
SEQADV 6COB TRP A  129  UNP  Q9LFT6    LEU   129 ENGINEERED MUTATION            
SEQADV 6COB THR A  132  UNP  Q9LFT6    CYS   132 ENGINEERED MUTATION            
SEQADV 6COB LEU A  179  UNP  Q9LFT6    PHE   179 ENGINEERED MUTATION            
SEQADV 6COB ILE A  210  UNP  Q9LFT6    ALA   210 ENGINEERED MUTATION            
SEQADV 6COB GLY A  259  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COB LEU A  260  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COB CYS B   14  UNP  Q9LFT6    TYR    14 ENGINEERED MUTATION            
SEQADV 6COB LEU B  122  UNP  Q9LFT6    TYR   122 ENGINEERED MUTATION            
SEQADV 6COB PHE B  126  UNP  Q9LFT6    PRO   126 ENGINEERED MUTATION            
SEQADV 6COB TRP B  129  UNP  Q9LFT6    LEU   129 ENGINEERED MUTATION            
SEQADV 6COB THR B  132  UNP  Q9LFT6    CYS   132 ENGINEERED MUTATION            
SEQADV 6COB LEU B  179  UNP  Q9LFT6    PHE   179 ENGINEERED MUTATION            
SEQADV 6COB ILE B  210  UNP  Q9LFT6    ALA   210 ENGINEERED MUTATION            
SEQADV 6COB GLY B  259  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COB LEU B  260  UNP  Q9LFT6              EXPRESSION TAG                 
SEQRES   1 A  260  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 A  260  CYS HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 A  260  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 A  260  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 A  260  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 A  260  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 A  260  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 A  260  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 A  260  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 A  260  VAL LEU ASP LYS LEU MET GLU MET PHE GLY GLY TRP GLY          
SEQRES  11 A  260  ASP THR GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 A  260  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 A  260  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 A  260  ALA LYS MET LEU HIS ARG GLN GLY SER LEU PHE THR GLU          
SEQRES  15 A  260  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 A  260  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 A  260  LYS ILE ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 A  260  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 A  260  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 A  260  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET GLY LEU          
SEQRES   1 B  260  MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA          
SEQRES   2 B  260  CYS HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU          
SEQRES   3 B  260  LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU          
SEQRES   4 B  260  ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL          
SEQRES   5 B  260  GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR          
SEQRES   6 B  260  LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL          
SEQRES   7 B  260  GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA          
SEQRES   8 B  260  ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU          
SEQRES   9 B  260  ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS          
SEQRES  10 B  260  VAL LEU ASP LYS LEU MET GLU MET PHE GLY GLY TRP GLY          
SEQRES  11 B  260  ASP THR GLU PHE SER SER HIS GLU THR ARG ASN GLY THR          
SEQRES  12 B  260  MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA          
SEQRES  13 B  260  ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU          
SEQRES  14 B  260  ALA LYS MET LEU HIS ARG GLN GLY SER LEU PHE THR GLU          
SEQRES  15 B  260  ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR          
SEQRES  16 B  260  GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP          
SEQRES  17 B  260  LYS ILE ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP          
SEQRES  18 B  260  ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY          
SEQRES  19 B  260  ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE          
SEQRES  20 B  260  ASP SER LEU SER ALA ILE ALA THR ASP TYR MET GLY LEU          
HET     CL  A 301       1                                                       
HET    GOL  A 302       6                                                       
HET     CL  B 301       1                                                       
HET    GOL  B 302       6                                                       
HET    GOL  B 303       6                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  GOL    3(C3 H8 O3)                                                  
FORMUL   8  HOH   *245(H2 O)                                                    
HELIX    1 AA1 GLY A   16  TYR A   21  5                                   6    
HELIX    2 AA2 LYS A   22  ALA A   30  1                                   9    
HELIX    3 AA3 PRO A   48  VAL A   52  5                                   5    
HELIX    4 AA4 THR A   54  SER A   68  1                                  15    
HELIX    5 AA5 PHE A   82  PHE A   94  1                                  13    
HELIX    6 AA6 SER A  116  PHE A  126  1                                  11    
HELIX    7 AA7 GLY A  150  LEU A  158  1                                   9    
HELIX    8 AA8 PRO A  163  HIS A  174  1                                  12    
HELIX    9 AA9 PHE A  180  LYS A  186  1                                   7    
HELIX   10 AB1 GLY A  194  VAL A  198  5                                   5    
HELIX   11 AB2 PRO A  212  PHE A  223  1                                  12    
HELIX   12 AB3 MET A  237  LYS A  242  1                                   6    
HELIX   13 AB4 LYS A  242  TYR A  257  1                                  16    
HELIX   14 AB5 GLY B   16  TYR B   21  5                                   6    
HELIX   15 AB6 LYS B   22  ALA B   30  1                                   9    
HELIX   16 AB7 PRO B   48  VAL B   52  5                                   5    
HELIX   17 AB8 THR B   54  LEU B   69  1                                  16    
HELIX   18 AB9 PHE B   82  ASP B   92  1                                  11    
HELIX   19 AC1 PHE B   94  ALA B   96  5                                   3    
HELIX   20 AC2 SER B  116  PHE B  126  1                                  11    
HELIX   21 AC3 GLY B  150  LEU B  158  1                                   9    
HELIX   22 AC4 PRO B  163  HIS B  174  1                                  12    
HELIX   23 AC5 PHE B  180  LYS B  187  1                                   8    
HELIX   24 AC6 GLY B  194  VAL B  198  5                                   5    
HELIX   25 AC7 PRO B  212  PHE B  223  1                                  12    
HELIX   26 AC8 MET B  237  LYS B  242  1                                   6    
HELIX   27 AC9 LYS B  242  TYR B  257  1                                  16    
SHEET    1 AA1 6 ARG A  33  VAL A  37  0                                        
SHEET    2 AA1 6 HIS A   6  VAL A  10  1  N  PHE A   7   O  ARG A  33           
SHEET    3 AA1 6 VAL A  75  PHE A  80  1  O  VAL A  78   N  VAL A   8           
SHEET    4 AA1 6 ILE A  98  LEU A 104  1  O  VAL A 102   N  LEU A  77           
SHEET    5 AA1 6 ARG A 200  SER A 205  1  O  VAL A 203   N  PHE A 103           
SHEET    6 AA1 6 VAL A 228  ILE A 231  1  O  TYR A 229   N  MET A 204           
SHEET    1 AA2 2 GLU A 133  THR A 139  0                                        
SHEET    2 AA2 2 GLY A 142  LYS A 148 -1  O  LEU A 146   N  SER A 135           
SHEET    1 AA3 6 ARG B  33  ALA B  36  0                                        
SHEET    2 AA3 6 HIS B   6  VAL B  10  1  N  PHE B   7   O  ARG B  33           
SHEET    3 AA3 6 VAL B  75  PHE B  80  1  O  VAL B  78   N  VAL B   8           
SHEET    4 AA3 6 ILE B  98  LEU B 104  1  O  VAL B 102   N  LEU B  77           
SHEET    5 AA3 6 ARG B 200  SER B 205  1  O  VAL B 203   N  PHE B 103           
SHEET    6 AA3 6 VAL B 228  ILE B 231  1  O  TYR B 229   N  MET B 204           
SHEET    1 AA4 2 GLU B 133  THR B 139  0                                        
SHEET    2 AA4 2 GLY B 142  LYS B 148 -1  O  LEU B 146   N  SER B 135           
SITE     1 AC1  4 ASN A  12  ALA A  13  SER A  81  PHE A  82                    
SITE     1 AC2  8 GLU A  53  ASN A 141  THR A 143  MET A 144                    
SITE     2 AC2  8 ASP A 183  LYS A 186  HOH A 407  HOH A 435                    
SITE     1 AC3  6 ASN B  12  ALA B  13  SER B  81  PHE B  82                    
SITE     2 AC3  6 GOL B 303  HOH B 423                                          
SITE     1 AC4  7 GLU B  53  THR B 139  ARG B 140  ASN B 161                    
SITE     2 AC4  7 GLY B 233  LYS B 242  HOH B 402                               
SITE     1 AC5  3 ALA B  13   CL B 301  HOH B 423                               
CRYST1   49.982   87.110  123.356  90.00  90.00  90.00 P 21 21 21    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      0.020007  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008107        0.00000                         
TER    2106      MET A 258                                                      
TER    4236      MET B 258                                                      
MASTER      430    0    5   27   16    0    8    6 4373    2   18   40          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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