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LongText Report for: 4P92-pdb

Name Class
4P92-pdb
HEADER    HYDROLASE                               02-APR-14   4P92              
TITLE     CRYSTAL STRUCTURE OF DIENELACTONE HYDROLASE C123S MUTANT AT 1.65 A    
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYMETHYLENEBUTENOLIDASE;                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DIENELACTONE HYDROLASE,DLH;                                 
COMPND   5 EC: 3.1.1.45;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 303;                                                 
SOURCE   4 GENE: CLCD;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];                      
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 668369                                      
KEYWDS    DIENELACTONE HYDROLASE, A/B HYDROLASE FOLD, HYDROLASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.L.PORTER,P.D.CARR,C.A.COLLYER,D.L.OLLIS                             
REVDAT   1   09-JUL-14 4P92    0                                                
JRNL        AUTH   J.L.PORTER,P.D.CARR,C.A.COLLYER,D.L.OLLIS                    
JRNL        TITL   CRYSTALLIZATION OF DIENELACTONE HYDROLASE IN TWO SPACE       
JRNL        TITL 2 GROUPS: STRUCTURAL CHANGES CAUSED BY CRYSTAL PACKING         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  70   884 2014              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        DOI    10.1107/S2053230X1401108X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.46                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 29557                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.172                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1578                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1894                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.1850                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1766                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 246                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.13000                                              
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): 0.083         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.077         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.041         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.161         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1836 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2505 ; 1.090 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   236 ; 6.260 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;32.016 ;24.048       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   263 ;11.866 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;14.481 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   268 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1443 ; 0.019 ; 0.021       
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 : BABINET MODEL WITH 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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4P92 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200587.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OTHER                              
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MUTILAYER OPTICS                   
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31176                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.460                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 7.230                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 50.5700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: 1ZI6                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM CITRATE         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.11500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.49000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.11500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.49000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 490 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
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     LYS A   234                                                      
REMARK 465     LYS A   235                                                      
REMARK 465     PRO A   236                                                      
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  25    CG   CD   CE   NZ                                   
REMARK 470     ARG A  79    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   113     O    HOH A   548              2.05            
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    GLU A  36     -159.95    -75.02                                   
REMARK 500    ASN A  41     -158.07   -128.41                                   
REMARK 500    ALA A  68      108.76   -169.93                                   
REMARK 500    ALA A  72       89.20   -150.27                                   
REMARK 500    SER A 123     -115.28     60.08                                   
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 SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DIN   RELATED DB: PDB                                   
REMARK 900 1DIN IS THE SAME PROTEIN ONLY WILD-TYPE (NO C123S MUTATION)          
REMARK 900 RELATED ID: 1ZI6   RELATED DB: PDB                                   
REMARK 900 1ZI6 IS THE SAME PROTEIN ONLY LOWER RESOLUTION STRUCTURE             
REMARK 900 RELATED ID: 4P93   RELATED DB: PDB                                   
DBREF  4P92 A    1   236  UNP    P0A114   CLCD_PSEPU       1    236             
SEQADV 4P92 SER A  123  UNP  P0A114    CYS   123 ENGINEERED MUTATION            
SEQADV 4P92 ASN A  154  UNP  P0A114    LYS   154 CONFLICT                       
SEQADV 4P92 THR A  224  UNP  P0A114    ARG   224 CONFLICT                       
SEQRES   1 A  236  MET LEU THR GLU GLY ILE SER ILE GLN SER TYR ASP GLY          
SEQRES   2 A  236  HIS THR PHE GLY ALA LEU VAL GLY SER PRO ALA LYS ALA          
SEQRES   3 A  236  PRO ALA PRO VAL ILE VAL ILE ALA GLN GLU ILE PHE GLY          
SEQRES   4 A  236  VAL ASN ALA PHE MET ARG GLU THR VAL SER TRP LEU VAL          
SEQRES   5 A  236  ASP GLN GLY TYR ALA ALA VAL CYS PRO ASP LEU TYR ALA          
SEQRES   6 A  236  ARG GLN ALA PRO GLY THR ALA LEU ASP PRO GLN ASP GLU          
SEQRES   7 A  236  ARG GLN ARG GLU GLN ALA TYR LYS LEU TRP GLN ALA PHE          
SEQRES   8 A  236  ASP MET GLU ALA GLY VAL GLY ASP LEU GLU ALA ALA ILE          
SEQRES   9 A  236  ARG TYR ALA ARG HIS GLN PRO TYR SER ASN GLY LYS VAL          
SEQRES  10 A  236  GLY LEU VAL GLY TYR SER LEU GLY GLY ALA LEU ALA PHE          
SEQRES  11 A  236  LEU VAL ALA ALA LYS GLY TYR VAL ASP ARG ALA VAL GLY          
SEQRES  12 A  236  TYR TYR GLY VAL GLY LEU GLU LYS GLN LEU ASN LYS VAL          
SEQRES  13 A  236  PRO GLU VAL LYS HIS PRO ALA LEU PHE HIS MET GLY GLY          
SEQRES  14 A  236  GLN ASP HIS PHE VAL PRO ALA PRO SER ARG GLN LEU ILE          
SEQRES  15 A  236  THR GLU GLY PHE GLY ALA ASN PRO LEU LEU GLN VAL HIS          
SEQRES  16 A  236  TRP TYR GLU GLU ALA GLY HIS SER PHE ALA ARG THR SER          
SEQRES  17 A  236  SER SER GLY TYR VAL ALA SER ALA ALA ALA LEU ALA ASN          
SEQRES  18 A  236  GLU ARG THR LEU ASP PHE LEU ALA PRO LEU GLN SER LYS          
SEQRES  19 A  236  LYS PRO                                                      
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  SO4    3(O4 S 2-)                                                   
FORMUL   5  HOH   *246(H2 O)                                                    
HELIX    1 AA1 ASN A   41  GLN A   54  1                                  14    
HELIX    2 AA2 LEU A   63  GLN A   67  5                                   5    
HELIX    3 AA3 ASP A   77  PHE A   91  1                                  15    
HELIX    4 AA4 ASP A   92  HIS A  109  1                                  18    
HELIX    5 AA5 SER A  123  GLY A  136  1                                  14    
HELIX    6 AA6 GLY A  148  VAL A  159  5                                  12    
HELIX    7 AA7 PRO A  175  GLY A  187  1                                  13    
HELIX    8 AA8 VAL A  213  ALA A  229  1                                  17    
HELIX    9 AA9 PRO A  230  GLN A  232  5                                   3    
SHEET    1 AA1 2 ILE A   8  GLN A   9  0                                        
SHEET    2 AA1 2 THR A  15  PHE A  16 -1  O  PHE A  16   N  ILE A   8           
SHEET    1 AA2 7 ALA A  18  GLY A  21  0                                        
SHEET    2 AA2 7 ALA A  57  PRO A  61 -1  O  CYS A  60   N  LEU A  19           
SHEET    3 AA2 7 ALA A  28  ALA A  34  1  N  ILE A  33   O  VAL A  59           
SHEET    4 AA2 7 SER A 113  TYR A 122  1  O  GLY A 118   N  VAL A  32           
SHEET    5 AA2 7 ARG A 140  TYR A 144  1  O  TYR A 144   N  GLY A 121           
SHEET    6 AA2 7 ALA A 163  GLY A 168  1  O  LEU A 164   N  GLY A 143           
SHEET    7 AA2 7 LEU A 192  TYR A 197  1  O  HIS A 195   N  MET A 167           
CISPEP   1 ALA A   26    PRO A   27          0         1.30                     
SITE     1 AC1  8 ARG A  45  SER A  49  PRO A 175  ALA A 176                    
SITE     2 AC1  8 HOH A 425  HOH A 432  HOH A 470  HOH A 594                    
SITE     1 AC2 10 ARG A  81  SER A 203  ARG A 206  SER A 209                    
SITE     2 AC2 10 HOH A 416  HOH A 449  HOH A 520  HOH A 522                    
SITE     3 AC2 10 HOH A 528  HOH A 592                                          
SITE     1 AC3  3 MET A   1  ALA A  72  HOH A 530                               
CRYST1   48.230   70.980   77.460  90.00  90.00  90.00 P 21 21 21    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      0.020734  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014088  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012910        0.00000                         
TER    1776      SER A 233                                                      
MASTER      306    0    3    9    9    0    6    6 2027    1   15   19          
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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