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LongText Report for: 6zl7-pdb

Name Class
6zl7-pdb
HEADER    HYDROLASE                               30-JUN-20   6ZL7              
TITLE     CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE FROM        
TITLE    2 PERMAFROST METAGENOMIC LIBRARY                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PMGL2;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.3;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PMGL2, ESTERASE, PERMAFROST, METAGENOMIC LIBRARY, LIPASE, MUTANT,     
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.GORYAYNOVA,K.M.BOYKO,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,             
AUTHOR   2 M.V.KRYUKOVA,L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,E.M.RIVKINA,   
AUTHOR   3 D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV                               
REVDAT   1   08-JUL-20 6ZL7    0                                                
JRNL        AUTH   D.A.GORYAYNOVA,K.M.BOYKO,A.Y.NIKOLAEVA,D.A.KORZHENEVSKIY,    
JRNL        AUTH 2 M.V.KRYUKOVA,L.E.PETROVSKAYA,K.A.NOVOTOTSKAYA-VLASOVA,       
JRNL        AUTH 3 E.M.RIVKINA,D.A.DOLGIKH,M.P.KIRPICHNIKOV,V.O.POPOV           
JRNL        TITL   CRYSTAL STRUCTURE OF C173S MUTATION IN THE PMGL2 ESTERASE    
JRNL        TITL 2 FROM PERMAFROST METAGENOMIC LIBRARY                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0258                                      
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 90444                          
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4737                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6558                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 335                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4751                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 453                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.08000                                              
REMARK   3    B22 (A**2) : 0.25000                                              
REMARK   3    B33 (A**2) : -0.51000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.44000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.072         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.302         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4960 ; 0.012 ; 0.012       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6783 ; 1.891 ; 1.634       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   652 ; 6.455 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;26.241 ;20.120       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   682 ;12.810 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;19.077 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   629 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3952 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 6ZL7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292109711.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.31                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95216                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.540                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 6QIN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 250MM MAGNESIUM CHLORIDE, 12-18%         
REMARK 280  PEG3350, 100MM HEPES PH 7.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 288K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       46.26500            
REMARK 290   SMTRY3   2  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: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLN A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ILE A   336                                                      
REMARK 465     PRO A   337                                                      
REMARK 465     THR A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     ARG A   340                                                      
REMARK 465     SER A   341                                                      
REMARK 465     PRO A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     HIS A   346                                                      
REMARK 465     HIS A   347                                                      
REMARK 465     HIS A   348                                                      
REMARK 465     HIS A   349                                                      
REMARK 465     HIS A   350                                                      
REMARK 465     HIS A   351                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     SER B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     GLN B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     PRO B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     SER B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     ILE B   336                                                      
REMARK 465     PRO B   337                                                      
REMARK 465     THR B   338                                                      
REMARK 465     PRO B   339                                                      
REMARK 465     ARG B   340                                                      
REMARK 465     SER B   341                                                      
REMARK 465     PRO B   342                                                      
REMARK 465     SER B   343                                                      
REMARK 465     LEU B   344                                                      
REMARK 465     GLU B   345                                                      
REMARK 465     HIS B   346                                                      
REMARK 465     HIS B   347                                                      
REMARK 465     HIS B   348                                                      
REMARK 465     HIS B   349                                                      
REMARK 465     HIS B   350                                                      
REMARK 465     HIS B   351                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  39    CG   CD   CE   NZ                                   
REMARK 470     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  44    CG   OD1  ND2                                       
REMARK 470     ARG A  49    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  72    CZ   NH1  NH2                                       
REMARK 470     ARG A 144    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 221    CG1  CG2                                            
REMARK 470     GLU A 240    CD   OE1  OE2                                       
REMARK 470     ALA A 256    CB                                                  
REMARK 470     SER A 333    C    O    CB   OG                                   
REMARK 470     LEU B  14    CG   CD1  CD2                                       
REMARK 470     LYS B  39    CD   CE   NZ                                        
REMARK 470     ARG B  67    CZ   NH1  NH2                                       
REMARK 470     ARG B  97    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 157    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 162    CD   NE   CZ   NH1  NH2                             
REMARK 470     PRO B 220    CG   CD                                             
REMARK 470     SER B 333    CA   C    O    CB   OG                              
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  34   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    TYR A 208   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 283   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  66   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 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    SER A 174     -123.99     64.74                                   
REMARK 500    SER A 174     -123.99     57.18                                   
REMARK 500    SER B 174     -124.12     62.98                                   
REMARK 500    SER B 174     -124.12     58.70                                   
REMARK 500    VAL B 221      -50.94   -124.14                                   
REMARK 500    PRO B 223      111.67    -32.00                                   
REMARK 500    ASP B 309       57.63    -90.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO B  220     VAL B  221                 -138.35                    
REMARK 500 VAL B  221     GLY B  222                 -147.29                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PG6 A  402                                                       
REMARK 610     PG6 B  401                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG6 B 401                 
DBREF1 6ZL7 A    1   343  UNP                  A0A142J6I6_9BACT                 
DBREF2 6ZL7 A     A0A142J6I6                          1         343             
DBREF1 6ZL7 B    1   343  UNP                  A0A142J6I6_9BACT                 
DBREF2 6ZL7 B     A0A142J6I6                          1         343             
SEQADV 6ZL7 SER A  173  UNP  A0A142J6I CYS   173 ENGINEERED MUTATION            
SEQADV 6ZL7 LEU A  344  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 GLU A  345  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  346  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  347  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  348  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  349  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  350  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS A  351  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 SER B  173  UNP  A0A142J6I CYS   173 ENGINEERED MUTATION            
SEQADV 6ZL7 LEU B  344  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 GLU B  345  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  346  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  347  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  348  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  349  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  350  UNP  A0A142J6I           EXPRESSION TAG                 
SEQADV 6ZL7 HIS B  351  UNP  A0A142J6I           EXPRESSION TAG                 
SEQRES   1 A  351  MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY          
SEQRES   2 A  351  LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO          
SEQRES   3 A  351  GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS          
SEQRES   4 A  351  ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA          
SEQRES   5 A  351  PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET          
SEQRES   6 A  351  ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU          
SEQRES   7 A  351  ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY          
SEQRES   8 A  351  VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL          
SEQRES   9 A  351  HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA          
SEQRES  10 A  351  LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL          
SEQRES  11 A  351  SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN          
SEQRES  12 A  351  ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR          
SEQRES  13 A  351  ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY          
SEQRES  14 A  351  ILE PHE GLY SER SER ALA GLY GLY VAL ILE THR ALA GLN          
SEQRES  15 A  351  ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO          
SEQRES  16 A  351  GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR          
SEQRES  17 A  351  SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL          
SEQRES  18 A  351  GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU          
SEQRES  19 A  351  PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA          
SEQRES  20 A  351  ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE          
SEQRES  21 A  351  MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE          
SEQRES  22 A  351  ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA          
SEQRES  23 A  351  ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY          
SEQRES  24 A  351  LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU          
SEQRES  25 A  351  SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP          
SEQRES  26 A  351  SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR          
SEQRES  27 A  351  PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  351  MET ALA SER GLY SER ALA SER SER ALA GLN THR PRO GLY          
SEQRES   2 B  351  LEU MET SER TRP LEU PRO PRO SER ASN GLN LEU SER PRO          
SEQRES   3 B  351  GLU ALA ARG SER VAL LEU ASP ARG MET ASP ALA ALA LYS          
SEQRES   4 B  351  ALA PRO GLU PHE ASN GLY ASP LEU VAL ARG GLN ARG ALA          
SEQRES   5 B  351  PHE TYR GLN GLN PHE ASN ASP ASP ARG LEU VAL GLU MET          
SEQRES   6 B  351  ARG ARG VAL PHE ARG THR ARG GLU ARG HIS GLU THR LEU          
SEQRES   7 B  351  ASN ALA VAL HIS VAL GLN VAL VAL GLU PRO ALA ASP GLY          
SEQRES   8 B  351  VAL SER ALA ARG ASN ARG ASP ARG VAL LEU ILE ASN VAL          
SEQRES   9 B  351  HIS GLY GLY ALA PHE MET TRP GLY ALA GLY SER GLY ALA          
SEQRES  10 B  351  LEU VAL GLU ALA ILE PRO ILE ALA ALA THR MET GLY VAL          
SEQRES  11 B  351  SER VAL VAL THR VAL ASP TYR ARG LEU ALA PRO GLU ASN          
SEQRES  12 B  351  ARG TYR PRO ALA ALA SER GLU ASP VAL THR ALA VAL TYR          
SEQRES  13 B  351  ARG ALA LEU LEU GLU ARG TYR PRO ALA ALA ASN ILE GLY          
SEQRES  14 B  351  ILE PHE GLY SER SER ALA GLY GLY VAL ILE THR ALA GLN          
SEQRES  15 B  351  ALA VAL THR TRP ILE ARG ARG GLU GLY LEU PRO ARG PRO          
SEQRES  16 B  351  GLY ALA ILE GLY THR LEU CYS GLY THR GLY ALA PRO TYR          
SEQRES  17 B  351  SER GLY ASP SER PRO TYR LEU ALA GLY VAL VAL PRO VAL          
SEQRES  18 B  351  GLY PRO GLY VAL LYS ALA PRO PRO LEU PRO GLY LEU LEU          
SEQRES  19 B  351  PRO THR ALA TYR MET GLU GLY VAL GLY ALA ASP ASP ALA          
SEQRES  20 B  351  ARG ALA TYR PRO LEU THR SER ASP ALA GLU THR VAL PHE          
SEQRES  21 B  351  MET PRO PRO THR LEU LEU LEU ALA GLY GLY ARG ASP PHE          
SEQRES  22 B  351  ALA VAL SER ALA LEU SER LEU ALA HIS ARG ARG LEU ALA          
SEQRES  23 B  351  ARG ALA GLY VAL ASP SER GLU LEU HIS LEU PHE ASP GLY          
SEQRES  24 B  351  LEU PRO HIS ALA PHE PHE VAL TRP PRO ASP MET PRO GLU          
SEQRES  25 B  351  SER LEU GLU ALA TYR ALA LEU ILE ALA GLY PHE PHE ASP          
SEQRES  26 B  351  SER ARG LEU GLY LEU THR PRO SER SER SER ILE PRO THR          
SEQRES  27 B  351  PRO ARG SER PRO SER LEU GLU HIS HIS HIS HIS HIS HIS          
HET     MG  A 401       1                                                       
HET    PG6  A 402      13                                                       
HET    PG6  B 401      11                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PG6 1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-                 
HETNAM   2 PG6  ETHOXY}-ETHANE                                                  
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  PG6    2(C12 H26 O6)                                                
FORMUL   6  HOH   *453(H2 O)                                                    
HELIX    1 AA1 SER A   25  ALA A   38  1                                  14    
HELIX    2 AA2 ASP A   46  PHE A   69  1                                  24    
HELIX    3 AA3 SER A   93  ARG A   97  5                                   5    
HELIX    4 AA4 GLY A  114  GLY A  129  1                                  16    
HELIX    5 AA5 PRO A  146  LEU A  160  1                                  15    
HELIX    6 AA6 PRO A  164  ALA A  166  5                                   3    
HELIX    7 AA7 SER A  174  GLU A  190  1                                  17    
HELIX    8 AA8 ASP A  211  ALA A  216  1                                   6    
HELIX    9 AA9 THR A  236  GLU A  240  5                                   5    
HELIX   10 AB1 TYR A  250  THR A  253  5                                   4    
HELIX   11 AB2 SER A  254  PHE A  260  1                                   7    
HELIX   12 AB3 ALA A  274  ALA A  288  1                                  15    
HELIX   13 AB4 ALA A  303  TRP A  307  5                                   5    
HELIX   14 AB5 MET A  310  LEU A  328  1                                  19    
HELIX   15 AB6 LEU B   14  LEU B   18  5                                   5    
HELIX   16 AB7 SER B   25  ALA B   38  1                                  14    
HELIX   17 AB8 ASP B   46  PHE B   69  1                                  24    
HELIX   18 AB9 SER B   93  ARG B   97  5                                   5    
HELIX   19 AC1 GLY B  114  GLY B  129  1                                  16    
HELIX   20 AC2 PRO B  146  LEU B  160  1                                  15    
HELIX   21 AC3 PRO B  164  ALA B  166  5                                   3    
HELIX   22 AC4 SER B  174  GLU B  190  1                                  17    
HELIX   23 AC5 ASP B  211  ALA B  216  1                                   6    
HELIX   24 AC6 THR B  236  GLU B  240  5                                   5    
HELIX   25 AC7 TYR B  250  THR B  253  5                                   4    
HELIX   26 AC8 SER B  254  PHE B  260  1                                   7    
HELIX   27 AC9 ALA B  274  ALA B  288  1                                  15    
HELIX   28 AD1 ALA B  303  TRP B  307  5                                   5    
HELIX   29 AD2 MET B  310  LEU B  328  1                                  19    
SHEET    1 AA1 8 THR A  71  LEU A  78  0                                        
SHEET    2 AA1 8 VAL A  81  PRO A  88 -1  O  VAL A  85   N  ARG A  74           
SHEET    3 AA1 8 VAL A 132  VAL A 135 -1  O  VAL A 132   N  VAL A  86           
SHEET    4 AA1 8 VAL A 100  VAL A 104  1  N  LEU A 101   O  VAL A 133           
SHEET    5 AA1 8 ILE A 168  SER A 173  1  O  PHE A 171   N  ILE A 102           
SHEET    6 AA1 8 ALA A 197  LEU A 201  1  O  LEU A 201   N  GLY A 172           
SHEET    7 AA1 8 THR A 264  GLY A 269  1  O  LEU A 265   N  ILE A 198           
SHEET    8 AA1 8 SER A 292  PHE A 297  1  O  GLU A 293   N  LEU A 266           
SHEET    1 AA2 8 THR B  71  LEU B  78  0                                        
SHEET    2 AA2 8 VAL B  81  PRO B  88 -1  O  VAL B  85   N  ARG B  74           
SHEET    3 AA2 8 VAL B 132  VAL B 135 -1  O  VAL B 132   N  VAL B  86           
SHEET    4 AA2 8 VAL B 100  VAL B 104  1  N  LEU B 101   O  VAL B 133           
SHEET    5 AA2 8 ILE B 168  SER B 173  1  O  GLY B 169   N  ILE B 102           
SHEET    6 AA2 8 ALA B 197  LEU B 201  1  O  LEU B 201   N  GLY B 172           
SHEET    7 AA2 8 THR B 264  GLY B 269  1  O  LEU B 265   N  ILE B 198           
SHEET    8 AA2 8 SER B 292  PHE B 297  1  O  GLU B 293   N  LEU B 266           
LINK        MG    MG A 401                 O   HOH A 667     1555   1555  2.99  
CISPEP   1 ALA A  140    PRO A  141          0        -2.38                     
CISPEP   2 TYR A  145    PRO A  146          0         2.63                     
CISPEP   3 ALA B  140    PRO B  141          0        -2.54                     
CISPEP   4 TYR B  145    PRO B  146          0         5.56                     
SITE     1 AC1  7 HIS A 282  GLU A 293  LEU A 294  HOH A 667                    
SITE     2 AC1  7 HIS B 282  GLU B 293  LEU B 294                               
SITE     1 AC2  9 SER A 174  ALA A 175  GLY A 203  THR A 204                    
SITE     2 AC2  9 ALA A 206  TYR A 208  PHE A 273  ALA A 274                    
SITE     3 AC2  9 ALA A 277                                                     
SITE     1 AC3  9 SER B 174  ALA B 175  CYS B 202  GLY B 203                    
SITE     2 AC3  9 THR B 204  ALA B 206  PHE B 273  ALA B 274                    
SITE     3 AC3  9 ALA B 277                                                     
CRYST1   47.149   92.530   74.410  90.00 106.61  90.00 P 1 21 1      4          
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      0.021209  0.000000  0.006327        0.00000                         
SCALE2      0.000000  0.010807  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014024        0.00000                         
TER    2381      SER A 333                                                      
TER    4808      SER B 333                                                      
MASTER      407    0    3   29   16    0    8    6 5229    2   26   54          
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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