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LongText Report for: 6coh-pdb

Name Class
6coh-pdb
HEADER    LYASE                                   12-MAR-18   6COH              
TITLE     ATHNL ENANTIOSELECTIVITY MUTANT AT-A9-H7 APO, Y13C,Y121L,P126F,L128W, 
TITLE    2 C131T,A209I WITH BENZALDEHYDE, MANDELIC ACID NITRILE                 
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 6COH    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.    2.37 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) : 2.37                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 21683                          
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) : 0.155                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1178                            
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) : 2.37                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.43                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1486                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.2460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 159                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : 0.05000                                              
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): 0.367         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.228         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.180         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.771        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.939                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4289 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4077 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5792 ; 2.012 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9433 ; 1.083 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   524 ; 6.982 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   190 ;35.620 ;24.316       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   761 ;16.145 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;19.526 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   627 ; 0.111 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4759 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   975 ; 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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0489  90.0349 127.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0636 T22:   0.0402                                     
REMARK   3      T33:   0.0141 T12:   0.0031                                     
REMARK   3      T13:   0.0075 T23:  -0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6317 L22:   0.7664                                     
REMARK   3      L33:   1.0665 L12:   0.0400                                     
REMARK   3      L13:   0.0166 L23:  -0.1356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0308 S12:   0.2224 S13:  -0.1214                       
REMARK   3      S21:  -0.1164 S22:  -0.0230 S23:  -0.0319                       
REMARK   3      S31:   0.0958 S32:   0.0562 S33:   0.0538                       
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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6104  95.2603 157.5678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0522 T22:   0.0479                                     
REMARK   3      T33:   0.0088 T12:  -0.0007                                     
REMARK   3      T13:   0.0122 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9028 L22:   0.7134                                     
REMARK   3      L33:   0.6562 L12:   0.0124                                     
REMARK   3      L13:  -0.1982 L23:   0.0538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:  -0.2474 S13:  -0.0078                       
REMARK   3      S21:   0.0924 S22:  -0.0157 S23:   0.0333                       
REMARK   3      S31:   0.0026 S32:  -0.0052 S33:   0.0076                       
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 6COH 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_1000231848.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
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   : 22909                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.367                              
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                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 3.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67900                            
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: REFMAC                                                
REMARK 200 STARTING MODEL: PDBID 3DQZ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 20% PEG 3350, PH 6.4,    
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       25.13850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.99500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.73150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.99500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.13850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.73150            
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: 2160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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     LEU A   260                                                      
REMARK 465     LEU B   260                                                      
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  47   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    MET A 123   CG  -  SD  -  CE  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG A 157   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    MET A 172   CG  -  SD  -  CE  ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ASP B  92   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ARG B 217   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    HIS A  15     -164.45   -121.23                                   
REMARK 500    ASN A  72       -1.34     77.39                                   
REMARK 500    SER A  81     -121.37     54.91                                   
REMARK 500    ILE A 210      -53.09   -120.58                                   
REMARK 500    LYS A 227      135.06   -175.87                                   
REMARK 500    HIS B  15     -164.62   -121.04                                   
REMARK 500    SER B  81     -121.09     61.38                                   
REMARK 500    ASN B 105       50.13     33.99                                   
REMARK 500    ASP B 214      -65.61     -9.54                                   
REMARK 500    PHE B 223       97.95   -161.45                                   
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 MXN 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 HBX B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MXN B 302                 
DBREF  6COH A    1   258  UNP    Q9LFT6   HNL_ARATH        1    258             
DBREF  6COH B    1   258  UNP    Q9LFT6   HNL_ARATH        1    258             
SEQADV 6COH CYS A   14  UNP  Q9LFT6    TYR    14 ENGINEERED MUTATION            
SEQADV 6COH LEU A  122  UNP  Q9LFT6    TYR   122 ENGINEERED MUTATION            
SEQADV 6COH PHE A  126  UNP  Q9LFT6    PRO   126 ENGINEERED MUTATION            
SEQADV 6COH TRP A  129  UNP  Q9LFT6    LEU   129 ENGINEERED MUTATION            
SEQADV 6COH THR A  132  UNP  Q9LFT6    CYS   132 ENGINEERED MUTATION            
SEQADV 6COH ILE A  210  UNP  Q9LFT6    ALA   210 ENGINEERED MUTATION            
SEQADV 6COH GLY A  259  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COH LEU A  260  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COH CYS B   14  UNP  Q9LFT6    TYR    14 ENGINEERED MUTATION            
SEQADV 6COH LEU B  122  UNP  Q9LFT6    TYR   122 ENGINEERED MUTATION            
SEQADV 6COH PHE B  126  UNP  Q9LFT6    PRO   126 ENGINEERED MUTATION            
SEQADV 6COH TRP B  129  UNP  Q9LFT6    LEU   129 ENGINEERED MUTATION            
SEQADV 6COH THR B  132  UNP  Q9LFT6    CYS   132 ENGINEERED MUTATION            
SEQADV 6COH ILE B  210  UNP  Q9LFT6    ALA   210 ENGINEERED MUTATION            
SEQADV 6COH GLY B  259  UNP  Q9LFT6              EXPRESSION TAG                 
SEQADV 6COH 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 PHE 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 PHE 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    MXN  A 301      10                                                       
HET    GOL  A 302       6                                                       
HET    HBX  B 301       8                                                       
HET    MXN  B 302      10                                                       
HETNAM     MXN (2R)-HYDROXY(PHENYL)ETHANENITRILE                                
HETNAM     GOL GLYCEROL                                                         
HETNAM     HBX BENZALDEHYDE                                                     
HETSYN     MXN (R)-MANDELONITRILE                                               
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  MXN    2(C8 H7 N O)                                                 
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   5  HBX    C7 H6 O                                                      
FORMUL   7  HOH   *159(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  LEU A   69  1                                  16    
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  SER B   68  1                                  15    
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  186  1                                   7    
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  GLY A  79           
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  ILE A 231   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  VAL B  37  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  ILE B  76   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 GLN B 199  SER B 205  1  O  VAL B 201   N  LEU B 101           
SHEET    6 AA3 6 VAL B 228  ILE B 231  1  O  ILE B 231   N  MET B 204           
SHEET    1 AA4 3 GLU B 133  THR B 139  0                                        
SHEET    2 AA4 3 GLY B 142  LYS B 148 -1  O  MET B 144   N  HIS B 137           
SHEET    3 AA4 3 GLY B 177  SER B 178 -1  O  GLY B 177   N  LEU B 147           
SITE     1 AC1  7 ASN A  12  ALA A  13  SER A  81  PHE A  82                    
SITE     2 AC1  7 MET A 149  PHE A 179  HIS A 236                               
SITE     1 AC2  7 GLU A  53  THR A 139  ASN A 141  MET A 144                    
SITE     2 AC2  7 ASP A 183  LYS A 186  HOH A 406                               
SITE     1 AC3  4 PHE B 107  MET B 123  PHE B 179  MXN B 302                    
SITE     1 AC4  7 ASN B  12  ALA B  13  SER B  81  PHE B  82                    
SITE     2 AC4  7 MET B 149  HIS B 236  HBX B 301                               
CRYST1   50.277   87.463  123.990  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      0.019890  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011433  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008065        0.00000                         
TER    2074      GLY A 259                                                      
TER    4150      GLY B 259                                                      
MASTER      353    0    4   27   17    0    7    6 4315    2   34   40          
END                                                                             

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