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LongText Report for: 5iq3-pdb

Name Class
5iq3-pdb
HEADER    HYDROLASE                               10-MAR-16   5IQ3              
TITLE     CRYSTAL STRUCTURE OF ESTERASE MUTANT - F72G/L255W                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ESTERASE;                                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 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    ESTERASE, EST25, HORMONE-SENSITIVE LIPASE, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-H.SEOK,M.-D.SEO,J.KIM,Y.RYU                                        
REVDAT   1   22-MAR-17 5IQ3    0                                                
JRNL        AUTH   S.-H.SEOK,M.-D.SEO,J.KIM,Y.RYU                               
JRNL        TITL   CRYSTAL STRUCTURE OF ESTERASE MUTANT - F72G                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 182176                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.183                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 25.5150 -  4.2065    0.99    13030   145  0.1522 0.1608        
REMARK   3     2  4.2065 -  3.3412    1.00    12974   143  0.1378 0.1552        
REMARK   3     3  3.3412 -  2.9195    1.00    12943   144  0.1658 0.1669        
REMARK   3     4  2.9195 -  2.6529    1.00    12892   144  0.1870 0.1640        
REMARK   3     5  2.6529 -  2.4629    1.00    12893   143  0.1813 0.2111        
REMARK   3     6  2.4629 -  2.3178    1.00    12910   143  0.1760 0.2086        
REMARK   3     7  2.3178 -  2.2018    1.00    12896   143  0.1722 0.1984        
REMARK   3     8  2.2018 -  2.1060    1.00    12885   143  0.1741 0.1756        
REMARK   3     9  2.1060 -  2.0250    1.00    12879   143  0.1825 0.2349        
REMARK   3    10  2.0250 -  1.9551    1.00    12847   143  0.1888 0.2291        
REMARK   3    11  1.9551 -  1.8940    1.00    12841   142  0.1924 0.2131        
REMARK   3    12  1.8940 -  1.8399    1.00    12882   143  0.2036 0.2296        
REMARK   3    13  1.8399 -  1.7915    1.00    12848   143  0.2187 0.2496        
REMARK   3    14  1.7915 -  1.7478    0.97    12456   138  0.2372 0.2645        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010          10776                                  
REMARK   3   ANGLE     :  1.109          14716                                  
REMARK   3   CHIRALITY :  0.065           1640                                  
REMARK   3   PLANARITY :  0.007           1948                                  
REMARK   3   DIHEDRAL  : 11.943           6396                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IQ3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219254.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 7A (6B, 6C1)                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00004                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 182179                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.360                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 33.6700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M SODIUM MALONATE (PH 7.0),          
REMARK 280  MICROBATCH, TEMPERATURE 299K                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       97.76050            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.93850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       97.76050            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       47.93850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 2990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 406  LIES ON A SPECIAL POSITION.                          
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     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     ALA B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     LEU C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     GLN C     8                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     LEU D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     GLN D     8                                                      
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     THR A   5    OG1  CG2                                            
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    LYS A  93   CA  -  CB  -  CG  ANGL. DEV. = -30.9 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    ALA A   4     -166.96   -114.17                                   
REMARK 500    LEU A 131      160.09     78.83                                   
REMARK 500    SER A 201     -117.76     59.03                                   
REMARK 500    CYS A 230       61.29     24.46                                   
REMARK 500    PHE A 254      -54.33     76.27                                   
REMARK 500    ALA A 334       18.57     59.94                                   
REMARK 500    SER A 338      -40.57   -138.98                                   
REMARK 500    LEU B 131      161.71     79.75                                   
REMARK 500    SER B 201     -118.58     60.14                                   
REMARK 500    CYS B 230       60.33     24.66                                   
REMARK 500    PHE B 254      -53.10     78.38                                   
REMARK 500    HIS B 333      119.72    -40.00                                   
REMARK 500    SER B 338      -41.27   -139.08                                   
REMARK 500    LEU C 131      160.09     79.00                                   
REMARK 500    SER C 201     -120.79     60.53                                   
REMARK 500    CYS C 230       61.04     23.22                                   
REMARK 500    PHE C 254      -54.99     79.80                                   
REMARK 500    LEU C 302       40.34   -100.23                                   
REMARK 500    SER C 338      -38.71   -140.31                                   
REMARK 500    LEU D 131      159.29     78.49                                   
REMARK 500    SER D 201     -118.49     60.68                                   
REMARK 500    CYS D 230       60.67     22.64                                   
REMARK 500    PHE D 254      -55.15     75.16                                   
REMARK 500    LEU D 302       40.56   -101.19                                   
REMARK 500    SER D 338      -39.88   -139.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 746        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A 747        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH C 706        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH D 679        DISTANCE =  5.86 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IQ2   RELATED DB: PDB                                   
REMARK 900 ANOTHER MUTANT OF EST25                                              
REMARK 900 RELATED ID: 5IQ0   RELATED DB: PDB                                   
REMARK 900 ANOTHER MUTANT OF EST25                                              
DBREF  5IQ3 A    1   362  UNP    Q4TZQ3   Q4TZQ3_9BACT     1    362             
DBREF  5IQ3 B    1   362  UNP    Q4TZQ3   Q4TZQ3_9BACT     1    362             
DBREF  5IQ3 C    1   362  UNP    Q4TZQ3   Q4TZQ3_9BACT     1    362             
DBREF  5IQ3 D    1   362  UNP    Q4TZQ3   Q4TZQ3_9BACT     1    362             
SEQADV 5IQ3 GLY A   72  UNP  Q4TZQ3    PHE    72 ENGINEERED MUTATION            
SEQADV 5IQ3 TRP A  255  UNP  Q4TZQ3    LEU   255 ENGINEERED MUTATION            
SEQADV 5IQ3 GLY B   72  UNP  Q4TZQ3    PHE    72 ENGINEERED MUTATION            
SEQADV 5IQ3 TRP B  255  UNP  Q4TZQ3    LEU   255 ENGINEERED MUTATION            
SEQADV 5IQ3 GLY C   72  UNP  Q4TZQ3    PHE    72 ENGINEERED MUTATION            
SEQADV 5IQ3 TRP C  255  UNP  Q4TZQ3    LEU   255 ENGINEERED MUTATION            
SEQADV 5IQ3 GLY D   72  UNP  Q4TZQ3    PHE    72 ENGINEERED MUTATION            
SEQADV 5IQ3 TRP D  255  UNP  Q4TZQ3    LEU   255 ENGINEERED MUTATION            
SEQRES   1 A  362  MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU          
SEQRES   2 A  362  GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR          
SEQRES   3 A  362  ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU          
SEQRES   4 A  362  ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER          
SEQRES   5 A  362  GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU          
SEQRES   6 A  362  GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN          
SEQRES   7 A  362  GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR          
SEQRES   8 A  362  ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE          
SEQRES   9 A  362  HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU          
SEQRES  10 A  362  PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE          
SEQRES  11 A  362  LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER          
SEQRES  12 A  362  GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU          
SEQRES  13 A  362  PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE          
SEQRES  14 A  362  PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP          
SEQRES  15 A  362  VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU          
SEQRES  16 A  362  ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU          
SEQRES  17 A  362  ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU          
SEQRES  18 A  362  GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER          
SEQRES  19 A  362  GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU          
SEQRES  20 A  362  LEU GLU ASN ASP ALA TYR PHE TRP ASP MET LYS THR MET          
SEQRES  21 A  362  GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN          
SEQRES  22 A  362  ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU          
SEQRES  23 A  362  GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL          
SEQRES  24 A  362  ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS          
SEQRES  25 A  362  TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY          
SEQRES  26 A  362  ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER          
SEQRES  27 A  362  PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL          
SEQRES  28 A  362  ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA                  
SEQRES   1 B  362  MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU          
SEQRES   2 B  362  GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR          
SEQRES   3 B  362  ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU          
SEQRES   4 B  362  ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER          
SEQRES   5 B  362  GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU          
SEQRES   6 B  362  GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN          
SEQRES   7 B  362  GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR          
SEQRES   8 B  362  ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE          
SEQRES   9 B  362  HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU          
SEQRES  10 B  362  PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE          
SEQRES  11 B  362  LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER          
SEQRES  12 B  362  GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU          
SEQRES  13 B  362  PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE          
SEQRES  14 B  362  PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP          
SEQRES  15 B  362  VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU          
SEQRES  16 B  362  ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU          
SEQRES  17 B  362  ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU          
SEQRES  18 B  362  GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER          
SEQRES  19 B  362  GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU          
SEQRES  20 B  362  LEU GLU ASN ASP ALA TYR PHE TRP ASP MET LYS THR MET          
SEQRES  21 B  362  GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN          
SEQRES  22 B  362  ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU          
SEQRES  23 B  362  GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL          
SEQRES  24 B  362  ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS          
SEQRES  25 B  362  TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY          
SEQRES  26 B  362  ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER          
SEQRES  27 B  362  PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL          
SEQRES  28 B  362  ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA                  
SEQRES   1 C  362  MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU          
SEQRES   2 C  362  GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR          
SEQRES   3 C  362  ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU          
SEQRES   4 C  362  ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER          
SEQRES   5 C  362  GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU          
SEQRES   6 C  362  GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN          
SEQRES   7 C  362  GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR          
SEQRES   8 C  362  ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE          
SEQRES   9 C  362  HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU          
SEQRES  10 C  362  PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE          
SEQRES  11 C  362  LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER          
SEQRES  12 C  362  GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU          
SEQRES  13 C  362  PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE          
SEQRES  14 C  362  PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP          
SEQRES  15 C  362  VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU          
SEQRES  16 C  362  ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU          
SEQRES  17 C  362  ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU          
SEQRES  18 C  362  GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER          
SEQRES  19 C  362  GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU          
SEQRES  20 C  362  LEU GLU ASN ASP ALA TYR PHE TRP ASP MET LYS THR MET          
SEQRES  21 C  362  GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN          
SEQRES  22 C  362  ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU          
SEQRES  23 C  362  GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL          
SEQRES  24 C  362  ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS          
SEQRES  25 C  362  TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY          
SEQRES  26 C  362  ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER          
SEQRES  27 C  362  PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL          
SEQRES  28 C  362  ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA                  
SEQRES   1 D  362  MET SER ASN ALA THR LEU ASN GLN LEU PRO GLY ARG LEU          
SEQRES   2 D  362  GLY ASP PRO SER MET SER LEU GLY THR ASP PRO ARG THR          
SEQRES   3 D  362  ASP PRO ARG LEU ALA ALA ALA LEU THR GLN LEU GLY LEU          
SEQRES   4 D  362  ALA ASP GLN ALA ALA GLU PRO PRO VAL ASN ALA ASN SER          
SEQRES   5 D  362  GLU VAL ALA ASP CYS ILE ALA TYR SER THR ALA ALA GLU          
SEQRES   6 D  362  GLN ALA TRP GLN THR LEU GLY ALA MET LEU GLY SER GLN          
SEQRES   7 D  362  GLY GLU PRO SER ASN PRO VAL ASP VAL ARG GLU GLU THR          
SEQRES   8 D  362  ILE LYS GLY ARG GLY GLY ASN GLU ILE LYS LEU TYR ILE          
SEQRES   9 D  362  HIS SER PRO THR GLY HIS THR SER ASP SER ASP PRO LEU          
SEQRES  10 D  362  PRO CYS VAL VAL HIS THR HIS GLY GLY GLY MET VAL ILE          
SEQRES  11 D  362  LEU THR ALA ALA ASP ALA ASN TYR SER ARG TRP ARG SER          
SEQRES  12 D  362  GLU LEU ALA ALA THR GLY LEU VAL VAL VAL GLY VAL GLU          
SEQRES  13 D  362  PHE ARG ASN ALA ALA GLY ALA LEU GLY ASN HIS PRO PHE          
SEQRES  14 D  362  PRO ALA GLY LEU HIS ASP CYS ALA ASP ALA ALA LYS TRP          
SEQRES  15 D  362  VAL ALA SER ASN ARG GLU ALA LEU GLY ILE SER THR LEU          
SEQRES  16 D  362  ILE MET SER GLY GLU SER GLY GLY GLY ASN LEU SER LEU          
SEQRES  17 D  362  ALA THR THR MET LEU ALA LYS LYS GLU GLY TRP LEU GLU          
SEQRES  18 D  362  GLU ILE ALA GLY VAL TYR ALA GLN CYS PRO TYR ILE SER          
SEQRES  19 D  362  GLY LEU TYR ALA SER LYS PRO GLU GLU LEU PRO SER LEU          
SEQRES  20 D  362  LEU GLU ASN ASP ALA TYR PHE TRP ASP MET LYS THR MET          
SEQRES  21 D  362  GLY ALA MET VAL LYS PRO TYR ASP PRO THR GLY GLU ASN          
SEQRES  22 D  362  ALA SER ASN PRO LEU ALA TRP PRO TYR HIS ALA SER LEU          
SEQRES  23 D  362  GLU ASP LEU ALA GLY LEU PRO PRO HIS VAL ILE SER VAL          
SEQRES  24 D  362  ASN GLU LEU ASP PRO LEU ARG ASP GLU GLY LEU ALA HIS          
SEQRES  25 D  362  TYR ARG LYS LEU LEU LYS ALA GLY VAL SER THR VAL GLY          
SEQRES  26 D  362  ARG THR VAL HIS GLY THR CYS HIS ALA ALA ASP CYS SER          
SEQRES  27 D  362  PHE VAL ASP VAL ILE PRO ASP VAL TYR PHE ALA THR VAL          
SEQRES  28 D  362  ARG ASP ILE SER ALA PHE ALA TYR SER ARG ALA                  
FORMUL   5  HOH   *1204(H2 O)                                                   
HELIX    1 AA1 PRO A   10  ASP A   15  1                                   6    
HELIX    2 AA2 ASP A   27  LEU A   37  1                                  11    
HELIX    3 AA3 GLU A   53  SER A   77  1                                  25    
HELIX    4 AA4 ASP A  135  THR A  148  1                                  14    
HELIX    5 AA5 ALA A  161  GLY A  165  5                                   5    
HELIX    6 AA6 PRO A  170  ASN A  186  1                                  17    
HELIX    7 AA7 ASN A  186  GLY A  191  1                                   6    
HELIX    8 AA8 SER A  201  GLU A  217  1                                  17    
HELIX    9 AA9 TRP A  219  ILE A  223  5                                   5    
HELIX   10 AB1 PRO A  245  ASN A  250  1                                   6    
HELIX   11 AB2 ASP A  256  ASP A  268  1                                  13    
HELIX   12 AB3 TRP A  280  ALA A  284  5                                   5    
HELIX   13 AB4 SER A  285  ALA A  290  1                                   6    
HELIX   14 AB5 LEU A  305  ALA A  319  1                                  15    
HELIX   15 AB6 ALA A  334  SER A  338  5                                   5    
HELIX   16 AB7 ILE A  343  ARG A  361  1                                  19    
HELIX   17 AB8 PRO B   10  ASP B   15  1                                   6    
HELIX   18 AB9 ASP B   27  LEU B   37  1                                  11    
HELIX   19 AC1 GLU B   53  SER B   77  1                                  25    
HELIX   20 AC2 ASP B  135  THR B  148  1                                  14    
HELIX   21 AC3 ALA B  161  GLY B  165  5                                   5    
HELIX   22 AC4 PRO B  170  SER B  185  1                                  16    
HELIX   23 AC5 ASN B  186  GLY B  191  1                                   6    
HELIX   24 AC6 SER B  201  GLU B  217  1                                  17    
HELIX   25 AC7 TRP B  219  ILE B  223  5                                   5    
HELIX   26 AC8 PRO B  245  ASN B  250  1                                   6    
HELIX   27 AC9 ASP B  256  ASP B  268  1                                  13    
HELIX   28 AD1 TRP B  280  ALA B  284  5                                   5    
HELIX   29 AD2 SER B  285  ALA B  290  1                                   6    
HELIX   30 AD3 LEU B  305  ALA B  319  1                                  15    
HELIX   31 AD4 ALA B  334  SER B  338  5                                   5    
HELIX   32 AD5 ILE B  343  ARG B  361  1                                  19    
HELIX   33 AD6 PRO C   10  ASP C   15  1                                   6    
HELIX   34 AD7 ASP C   27  LEU C   37  1                                  11    
HELIX   35 AD8 GLU C   53  SER C   77  1                                  25    
HELIX   36 AD9 ASP C  135  ALA C  147  1                                  13    
HELIX   37 AE1 ALA C  161  GLY C  165  5                                   5    
HELIX   38 AE2 PRO C  170  SER C  185  1                                  16    
HELIX   39 AE3 ASN C  186  GLY C  191  1                                   6    
HELIX   40 AE4 SER C  201  GLY C  218  1                                  18    
HELIX   41 AE5 TRP C  219  ILE C  223  5                                   5    
HELIX   42 AE6 PRO C  245  ASN C  250  1                                   6    
HELIX   43 AE7 ASP C  256  ASP C  268  1                                  13    
HELIX   44 AE8 TRP C  280  ALA C  284  5                                   5    
HELIX   45 AE9 SER C  285  ALA C  290  1                                   6    
HELIX   46 AF1 LEU C  305  ALA C  319  1                                  15    
HELIX   47 AF2 ALA C  334  SER C  338  5                                   5    
HELIX   48 AF3 ILE C  343  ARG C  361  1                                  19    
HELIX   49 AF4 PRO D   10  ASP D   15  1                                   6    
HELIX   50 AF5 ASP D   27  LEU D   37  1                                  11    
HELIX   51 AF6 GLU D   53  SER D   77  1                                  25    
HELIX   52 AF7 ASP D  135  THR D  148  1                                  14    
HELIX   53 AF8 ALA D  161  GLY D  165  5                                   5    
HELIX   54 AF9 PRO D  170  SER D  185  1                                  16    
HELIX   55 AG1 ASN D  186  GLY D  191  1                                   6    
HELIX   56 AG2 SER D  201  GLU D  217  1                                  17    
HELIX   57 AG3 TRP D  219  ILE D  223  5                                   5    
HELIX   58 AG4 PRO D  245  ASN D  250  1                                   6    
HELIX   59 AG5 ASP D  256  ASP D  268  1                                  13    
HELIX   60 AG6 TRP D  280  ALA D  284  5                                   5    
HELIX   61 AG7 SER D  285  ALA D  290  1                                   6    
HELIX   62 AG8 LEU D  305  ALA D  319  1                                  15    
HELIX   63 AG9 ALA D  334  SER D  338  5                                   5    
HELIX   64 AH1 ILE D  343  ALA D  362  1                                  20    
SHEET    1 AA116 VAL A  85  LYS A  93  0                                        
SHEET    2 AA116 GLU A  99  PRO A 107 -1  O  ILE A 104   N  ARG A  88           
SHEET    3 AA116 VAL A 151  GLU A 156 -1  O  GLY A 154   N  TYR A 103           
SHEET    4 AA116 LEU A 117  HIS A 122  1  N  VAL A 120   O  VAL A 153           
SHEET    5 AA116 ILE A 192  GLU A 200  1  O  ILE A 196   N  VAL A 121           
SHEET    6 AA116 GLY A 225  GLN A 229  1  O  GLN A 229   N  GLY A 199           
SHEET    7 AA116 HIS A 295  LEU A 302  1  O  VAL A 296   N  ALA A 228           
SHEET    8 AA116 THR A 323  CYS A 332  1  O  VAL A 328   N  VAL A 299           
SHEET    9 AA116 THR B 323  CYS B 332 -1  O  GLY B 325   N  HIS A 329           
SHEET   10 AA116 HIS B 295  LEU B 302  1  N  VAL B 299   O  VAL B 328           
SHEET   11 AA116 GLY B 225  GLN B 229  1  N  ALA B 228   O  VAL B 296           
SHEET   12 AA116 ILE B 192  GLU B 200  1  N  GLY B 199   O  GLN B 229           
SHEET   13 AA116 LEU B 117  HIS B 122  1  N  VAL B 121   O  ILE B 196           
SHEET   14 AA116 VAL B 151  GLU B 156  1  O  VAL B 153   N  VAL B 120           
SHEET   15 AA116 GLU B  99  PRO B 107 -1  N  TYR B 103   O  GLY B 154           
SHEET   16 AA116 VAL B  85  LYS B  93 -1  N  ARG B  88   O  ILE B 104           
SHEET    1 AA216 VAL C  85  LYS C  93  0                                        
SHEET    2 AA216 GLU C  99  PRO C 107 -1  O  ILE C 100   N  ILE C  92           
SHEET    3 AA216 VAL C 151  GLU C 156 -1  O  GLY C 154   N  TYR C 103           
SHEET    4 AA216 LEU C 117  THR C 123  1  N  VAL C 120   O  VAL C 153           
SHEET    5 AA216 ILE C 192  GLU C 200  1  O  ILE C 196   N  VAL C 121           
SHEET    6 AA216 GLY C 225  GLN C 229  1  O  GLN C 229   N  GLY C 199           
SHEET    7 AA216 HIS C 295  LEU C 302  1  O  VAL C 296   N  ALA C 228           
SHEET    8 AA216 THR C 323  CYS C 332  1  O  VAL C 324   N  ILE C 297           
SHEET    9 AA216 THR D 323  CYS D 332 -1  O  GLY D 325   N  HIS C 329           
SHEET   10 AA216 HIS D 295  LEU D 302  1  N  VAL D 299   O  VAL D 328           
SHEET   11 AA216 GLY D 225  GLN D 229  1  N  ALA D 228   O  VAL D 296           
SHEET   12 AA216 ILE D 192  GLU D 200  1  N  GLY D 199   O  GLN D 229           
SHEET   13 AA216 LEU D 117  THR D 123  1  N  VAL D 121   O  ILE D 196           
SHEET   14 AA216 VAL D 151  GLU D 156  1  O  VAL D 153   N  VAL D 120           
SHEET   15 AA216 GLU D  99  PRO D 107 -1  N  TYR D 103   O  GLY D 154           
SHEET   16 AA216 VAL D  85  LYS D  93 -1  N  ARG D  88   O  ILE D 104           
CISPEP   1 GLY A  165    ASN A  166          0        -0.12                     
CISPEP   2 PHE A  169    PRO A  170          0         5.77                     
CISPEP   3 GLY B  165    ASN B  166          0        -1.92                     
CISPEP   4 PHE B  169    PRO B  170          0         5.57                     
CISPEP   5 GLY C  165    ASN C  166          0        -1.37                     
CISPEP   6 PHE C  169    PRO C  170          0         6.00                     
CISPEP   7 GLY D  165    ASN D  166          0        -0.93                     
CISPEP   8 PHE D  169    PRO D  170          0         6.06                     
CRYST1  195.521   95.877   98.527  90.00  95.48  90.00 C 1 2 1      16          
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      0.005115  0.000000  0.000490        0.00000                         
SCALE2      0.000000  0.010430  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010196        0.00000                         
TER    2680      ALA A 362                                                      
TER    5311      ALA B 362                                                      
TER    7942      ALA C 362                                                      
TER   10573      ALA D 362                                                      
MASTER      347    0    0   64   32    0    0    611773    4    0  112          
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
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