Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6u32-pdb

Name Class
6u32-pdb
HEADER    HYDROLASE                               21-AUG-19   6U32              
TITLE     CRYSTAL STRUCTURE OF HALOTAG BOUND TO TETRAMETHYLRHODAMINE-HALOTAG    
TITLE    2 LIGAND                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOTAG;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;                                
SOURCE   3 ORGANISM_TAXID: 1831;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HALOTAG, HALOALKANE DEHALOGENASE, TETRAMETHYRHODAMINE, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.BERRO,E.R.SCHREITER                                               
REVDAT   1   30-SEP-20 6U32    0                                                
JRNL        AUTH   A.J.BERRO,E.R.SCHREITER                                      
JRNL        TITL   CRYSTAL STRUCTURE OF HALOTAG BOUND TO                        
JRNL        TITL 2 TETRAMETHYLRHODAMINE-HALOTAG LIGAND                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 58.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 28449                          
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) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.157                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1545                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2084                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2345                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 177                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.62000                                              
REMARK   3    B22 (A**2) : 0.62000                                              
REMARK   3    B33 (A**2) : -1.23000                                             
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): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.108         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.637         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.959                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2514 ; 0.030 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2293 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3440 ; 2.537 ; 1.986       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5307 ; 1.366 ; 3.006       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   293 ; 6.227 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;30.697 ;23.448       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   371 ;13.524 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;23.779 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   354 ; 0.155 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2787 ; 0.017 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   535 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   295                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   86.862   59.990   10.573              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1376 T22:   0.0524                                     
REMARK   3      T33:   0.0060 T12:   0.0158                                     
REMARK   3      T13:   0.0127 T23:   0.0146                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1208 L22:   0.7338                                     
REMARK   3      L33:   2.4658 L12:   0.2896                                     
REMARK   3      L13:   0.3302 L23:   0.2352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0136 S12:   0.0319 S13:   0.0111                       
REMARK   3      S21:   0.0923 S22:   0.0069 S23:   0.0211                       
REMARK   3      S31:   0.2362 S32:   0.1386 S33:   0.0067                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6U32 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000243762.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30022                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.435                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200   FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.97700                            
REMARK 200   FOR SHELL         : 0.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5UY1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 0.1M TRIS PH 8.5, 20% PEG    
REMARK 280  8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.08450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.26500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.26500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      123.12675            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.26500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.26500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.04225            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.26500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.26500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      123.12675            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.26500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.26500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.04225            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       82.08450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     SER A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   539     O    HOH A   565              2.14            
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  99   CD    GLU A  99   OE2     0.075                       
REMARK 500    GLY A 125   C     GLY A 125   O       0.098                       
REMARK 500    THR A 154   C     THR A 154   O       0.121                       
REMARK 500    TRP A 289   CE3   TRP A 289   CZ3     0.114                       
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  21   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A  31   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP A  73   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP A  89   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 118   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    THR A 155   CA  -  CB  -  CG2 ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ASP A 156   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A 179   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG A 204   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG A 204   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    HIS A 230   CB  -  CA  -  C   ANGL. DEV. =  13.3 DEGREES          
REMARK 500    ARG A 254   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 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    PRO A   9       46.23    -84.86                                   
REMARK 500    PRO A  42       51.83   -113.55                                   
REMARK 500    THR A  43     -159.99   -102.16                                   
REMARK 500    GLU A  98      -88.95   -105.71                                   
REMARK 500    ASP A 106     -125.98     55.06                                   
REMARK 500    ARG A 153       36.33    -86.36                                   
REMARK 500    VAL A 245      -73.05   -134.03                                   
REMARK 500    LEU A 271      -95.64   -119.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    HIS A 188         0.09    SIDE CHAIN                              
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 PVY A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302                  
DBREF  6U32 A    1   297  PDB    6U32     6U32             1    297             
SEQRES   1 A  297  MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 A  297  TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP          
SEQRES   3 A  297  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 A  297  GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE          
SEQRES   5 A  297  PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 A  297  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY          
SEQRES   7 A  297  TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE          
SEQRES   8 A  297  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 A  297  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 A  297  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU          
SEQRES  11 A  297  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 A  297  PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP          
SEQRES  13 A  297  VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE          
SEQRES  14 A  297  GLU GLY THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR          
SEQRES  15 A  297  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN          
SEQRES  16 A  297  PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 A  297  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU          
SEQRES  18 A  297  VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 A  297  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 A  297  PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO          
SEQRES  21 A  297  ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU          
SEQRES  22 A  297  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 A  297  ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY                  
HET    PVY  A 301      76                                                       
HET     CL  A 302       1                                                       
HETNAM     PVY 9-[2-CARBOXY-5-({2-[2-(HEXYLOXY)                                 
HETNAM   2 PVY  ETHOXY]ETHYL}CARBAMOYL)PHENYL]-6-(DIMETHYLAMINO)-N,N-           
HETNAM   3 PVY  DIMETHYL-3H-XANTHEN-3-IMINIUM                                   
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  PVY    C35 H44 N3 O6 1+                                             
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  HOH   *177(H2 O)                                                    
HELIX    1 AA1 SER A   44  ARG A   49  5                                   6    
HELIX    2 AA2 ILE A   51  ALA A   56  1                                   6    
HELIX    3 AA3 PHE A   80  LEU A   95  1                                  16    
HELIX    4 AA4 ASP A  106  ASN A  119  1                                  14    
HELIX    5 AA5 THR A  137  TRP A  141  5                                   5    
HELIX    6 AA6 PRO A  142  PHE A  144  5                                   3    
HELIX    7 AA7 ALA A  145  ARG A  153  1                                   9    
HELIX    8 AA8 THR A  155  ILE A  163  1                                   9    
HELIX    9 AA9 ASN A  166  GLY A  171  1                                   6    
HELIX   10 AB1 LEU A  173  VAL A  177  5                                   5    
HELIX   11 AB2 THR A  182  GLU A  191  1                                  10    
HELIX   12 AB3 PRO A  192  LEU A  194  5                                   3    
HELIX   13 AB4 ASN A  195  ASP A  198  5                                   4    
HELIX   14 AB5 ARG A  199  LEU A  209  1                                  11    
HELIX   15 AB6 PRO A  215  SER A  232  1                                  18    
HELIX   16 AB7 PRO A  248  LEU A  259  1                                  12    
HELIX   17 AB8 LEU A  273  ASN A  278  1                                   6    
HELIX   18 AB9 ASN A  278  LEU A  293  1                                  16    
SHEET    1 AA1 8 HIS A  13  VAL A  17  0                                        
SHEET    2 AA1 8 GLU A  20  VAL A  27 -1  O  GLU A  20   N  VAL A  17           
SHEET    3 AA1 8 CYS A  61  PRO A  64 -1  O  CYS A  61   N  VAL A  27           
SHEET    4 AA1 8 VAL A  35  LEU A  38  1  N  PHE A  37   O  ILE A  62           
SHEET    5 AA1 8 VAL A 100  HIS A 105  1  O  VAL A 101   N  LEU A  36           
SHEET    6 AA1 8 VAL A 123  MET A 129  1  O  ALA A 127   N  LEU A 102           
SHEET    7 AA1 8 LYS A 236  PRO A 243  1  O  LEU A 237   N  PHE A 128           
SHEET    8 AA1 8 CYS A 262  GLY A 270  1  O  LYS A 263   N  LEU A 238           
LINK         OD1 ASP A 106                 CBO PVY A 301     1555   1555  1.44  
CISPEP   1 ASN A   41    PRO A   42          0         3.88                     
CISPEP   2 GLU A  214    PRO A  215          0        -4.30                     
CISPEP   3 THR A  242    PRO A  243          0         1.97                     
SITE     1 AC1 11 ASP A 106  ALA A 145  THR A 148  PHE A 149                    
SITE     2 AC1 11 LEU A 161  VAL A 167  GLU A 170  GLY A 171                    
SITE     3 AC1 11 THR A 172  PRO A 174  MET A 175                               
SITE     1 AC2  3 ASN A  41  TRP A 107  PRO A 206                               
CRYST1   62.530   62.530  164.169  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015992  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015992  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006091        0.00000                         
TER    2351      ILE A 295                                                      
MASTER      396    0    2   18    8    0    4    6 2567    1   77   23          
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer