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LongText Report for: 4GEC-pdb

Name Class
4GEC-pdb
HEADER    LYASE                                   01-AUG-12   4GEC              
TITLE     CRYSTAL STRUCTURE OF E.COLI MENH R124A MUTANT                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE      
COMPND   3 SYNTHASE;                                                            
COMPND   4 CHAIN: A, B, C;                                                      
COMPND   5 SYNONYM: SHCHC SYNTHASE;                                             
COMPND   6 EC: 4.2.99.20;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B2263, JW2258, MENH, MENH_R124AMUTANT, YFBB;                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETM                                      
KEYWDS    MENAQUINONE BIOSYNTHESIS, ALPHA BETA HYDROLASE, 2-SUCCINYL-6-HYDROXY- 
KEYWDS   2 2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE, MUTANT R124A, MENH MUTANT 
KEYWDS   3 R124A, LYASE                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M JOHNSTON,E.N.BAKER,Z.GUO,M.JIANG                                  
REVDAT   2   15-MAY-13 4GEC    1       JRNL                                     
REVDAT   1   08-MAY-13 4GEC    0                                                
JRNL        AUTH   J.M.JOHNSTON,M.JIANG,Z.GUO,E.N.BAKER                         
JRNL        TITL   CRYSTAL STRUCTURES OF E. COLI NATIVE MENH AND TWO ACTIVE     
JRNL        TITL 2 SITE MUTANTS.                                                
JRNL        REF    PLOS ONE                      V.   8 61325 2013              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   23637813                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0061325                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.0                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 54795                          
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)  : 0.195                          
REMARK   3   R VALUE            (WORKING SET)  : 0.194                          
REMARK   3   FREE R VALUE                      : 0.223                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2792                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.56                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.13                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3958                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2448                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3743                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2433                   
REMARK   3   BIN FREE R VALUE                        : 0.2708                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.43                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 215                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5923                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 232                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.48                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.71330                                             
REMARK   3    B22 (A**2) : -3.71330                                             
REMARK   3    B33 (A**2) : 7.42650                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.32                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.22                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.19                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.22                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.19                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6087   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8267   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2735   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 150    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 917    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6087   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 742    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7679   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.06                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.23                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.06                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4GEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074076.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.953692                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54795                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 117.444                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 14.900                             
REMARK 200  R MERGE                    (I) : 0.19000                            
REMARK 200  R SYM                      (I) : 0.19000                            
REMARK 200   FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 15.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.84700                            
REMARK 200  R SYM FOR SHELL            (I) : 1.84700                            
REMARK 200   FOR SHELL         : 1.800                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE, AMMONIUM SULFATE,        
REMARK 280  LITHIUM SULFATE, PH 5.5, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       57.57200            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      234.88750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      117.44375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       57.57200            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      352.33125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      352.33125            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.57200            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.44375            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       57.57200            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      234.88750            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       57.57200            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      234.88750            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       57.57200            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      352.33125            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      117.44375            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       57.57200            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      117.44375            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      352.33125            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       57.57200            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       57.57200            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      234.88750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     SER A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     MET B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     SER B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     VAL B    -4                                                      
REMARK 465     PRO B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     MET C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     SER C    -7                                                      
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     ARG A  -2    CG   CD   NE   CZ   NH1  NH2                        
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  24       -1.33     79.75                                   
REMARK 500    SER A  86     -106.88     47.48                                   
REMARK 500    ALA A 197       39.64    -79.90                                   
REMARK 500    SER B  24      -11.79     73.96                                   
REMARK 500    PHE B  37       56.81    -90.20                                   
REMARK 500    SER B  86     -107.43     46.78                                   
REMARK 500    SER C  24       -4.41     75.73                                   
REMARK 500    SER C  86     -102.36     51.46                                   
REMARK 500    ASP C 190       95.97    -65.71                                   
REMARK 500    ALA C 218       -3.05    -59.63                                   
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 GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 302                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4GDM   RELATED DB: PDB                                   
REMARK 900 NATIVE E. COLI MENH STRUCTURE                                        
REMARK 900 RELATED ID: 4GEG   RELATED DB: PDB                                   
REMARK 900 E. COLI MENH Y85F MUTANT STRUCTURE                                   
DBREF  4GEC A    1   252  UNP    P37355   MENH_ECOLI       1    252             
DBREF  4GEC B    1   252  UNP    P37355   MENH_ECOLI       1    252             
DBREF  4GEC C    1   252  UNP    P37355   MENH_ECOLI       1    252             
SEQADV 4GEC MET A  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS A   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER A   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER A   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY A   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC LEU A   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC VAL A   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC PRO A   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ARG A   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY A   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER A    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ALA A  124  UNP  P37355    ARG   124 ENGINEERED MUTATION            
SEQADV 4GEC MET B  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS B   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER B   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER B   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY B   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC LEU B   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC VAL B   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC PRO B   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ARG B   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY B   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER B    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ALA B  124  UNP  P37355    ARG   124 ENGINEERED MUTATION            
SEQADV 4GEC MET C  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC HIS C   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER C   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER C   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY C   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC LEU C   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC VAL C   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC PRO C   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ARG C   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC GLY C   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC SER C    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEC ALA C  124  UNP  P37355    ARG   124 ENGINEERED MUTATION            
SEQRES   1 A  268  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  268  ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY          
SEQRES   3 A  268  LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE          
SEQRES   4 A  268  SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA          
SEQRES   5 A  268  PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY          
SEQRES   6 A  268  HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP          
SEQRES   7 A  268  ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR          
SEQRES   8 A  268  ASN ILE LEU ASP PHE TRP LEU VAL GLY TYR SER LEU GLY          
SEQRES   9 A  268  GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA          
SEQRES  10 A  268  GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY          
SEQRES  11 A  268  LEU GLN ASN ALA GLU GLN ARG ALA GLU ALA GLN ARG SER          
SEQRES  12 A  268  ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU          
SEQRES  13 A  268  THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE          
SEQRES  14 A  268  ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA          
SEQRES  15 A  268  LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET          
SEQRES  16 A  268  LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG          
SEQRES  17 A  268  ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU          
SEQRES  18 A  268  CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA          
SEQRES  19 A  268  GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY          
SEQRES  20 A  268  HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA          
SEQRES  21 A  268  SER LEU ALA GLN ILE LEU ARG PHE                              
SEQRES   1 B  268  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  268  ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY          
SEQRES   3 B  268  LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE          
SEQRES   4 B  268  SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA          
SEQRES   5 B  268  PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY          
SEQRES   6 B  268  HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP          
SEQRES   7 B  268  ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR          
SEQRES   8 B  268  ASN ILE LEU ASP PHE TRP LEU VAL GLY TYR SER LEU GLY          
SEQRES   9 B  268  GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA          
SEQRES  10 B  268  GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY          
SEQRES  11 B  268  LEU GLN ASN ALA GLU GLN ARG ALA GLU ALA GLN ARG SER          
SEQRES  12 B  268  ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU          
SEQRES  13 B  268  THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE          
SEQRES  14 B  268  ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA          
SEQRES  15 B  268  LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET          
SEQRES  16 B  268  LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG          
SEQRES  17 B  268  ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU          
SEQRES  18 B  268  CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA          
SEQRES  19 B  268  GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY          
SEQRES  20 B  268  HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA          
SEQRES  21 B  268  SER LEU ALA GLN ILE LEU ARG PHE                              
SEQRES   1 C  268  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 C  268  ARG GLY SER MET ILE LEU HIS ALA GLN ALA LYS HIS GLY          
SEQRES   3 C  268  LYS PRO GLY LEU PRO TRP LEU VAL PHE LEU HIS GLY PHE          
SEQRES   4 C  268  SER GLY ASP CYS HIS GLU TRP GLN GLU VAL GLY GLU ALA          
SEQRES   5 C  268  PHE ALA ASP TYR SER ARG LEU TYR VAL ASP LEU PRO GLY          
SEQRES   6 C  268  HIS GLY GLY SER ALA ALA ILE SER VAL ASP GLY PHE ASP          
SEQRES   7 C  268  ASP VAL THR ASP LEU LEU ARG LYS THR LEU VAL SER TYR          
SEQRES   8 C  268  ASN ILE LEU ASP PHE TRP LEU VAL GLY TYR SER LEU GLY          
SEQRES   9 C  268  GLY ARG VAL ALA MET MET ALA ALA CYS GLN GLY LEU ALA          
SEQRES  10 C  268  GLY LEU CYS GLY VAL ILE VAL GLU GLY GLY HIS PRO GLY          
SEQRES  11 C  268  LEU GLN ASN ALA GLU GLN ARG ALA GLU ALA GLN ARG SER          
SEQRES  12 C  268  ASP ARG GLN TRP VAL GLN ARG PHE LEU THR GLU PRO LEU          
SEQRES  13 C  268  THR ALA VAL PHE ALA ASP TRP TYR GLN GLN PRO VAL PHE          
SEQRES  14 C  268  ALA SER LEU ASN ASP ASP GLN ARG ARG GLU LEU VAL ALA          
SEQRES  15 C  268  LEU ARG SER ASN ASN ASN GLY ALA THR LEU ALA ALA MET          
SEQRES  16 C  268  LEU GLU ALA THR SER LEU ALA VAL GLN PRO ASP LEU ARG          
SEQRES  17 C  268  ALA ASN LEU SER ALA ARG THR PHE ALA PHE TYR TYR LEU          
SEQRES  18 C  268  CYS GLY GLU ARG ASP SER LYS PHE ARG ALA LEU ALA ALA          
SEQRES  19 C  268  GLU LEU ALA ALA ASP CYS HIS VAL ILE PRO ARG ALA GLY          
SEQRES  20 C  268  HIS ASN ALA HIS ARG GLU ASN PRO ALA GLY VAL ILE ALA          
SEQRES  21 C  268  SER LEU ALA GLN ILE LEU ARG PHE                              
HET    SO4  A 301       5                                                       
HET    SO4  A 302       5                                                       
HET    GOL  A 303       6                                                       
HET     CL  A 304       1                                                       
HET    EDO  A 305       4                                                       
HET    SO4  B 301       5                                                       
HET     CL  B 302       1                                                       
HET    SO4  C 301       5                                                       
HET     CL  C 302       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7   CL    3(CL 1-)                                                     
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL  13  HOH   *232(H2 O)                                                    
HELIX    1   1 TRP A   30  GLU A   35  1                                   6    
HELIX    2   2 ALA A   36  ALA A   38  5                                   3    
HELIX    3   3 HIS A   50  ALA A   54  5                                   5    
HELIX    4   4 GLY A   60  TYR A   75  1                                  16    
HELIX    5   5 SER A   86  GLY A   99  1                                  14    
HELIX    6   6 ASN A  117  GLU A  138  1                                  22    
HELIX    7   7 PRO A  139  TYR A  148  1                                  10    
HELIX    8   8 GLN A  149  ALA A  154  5                                   6    
HELIX    9   9 ASN A  157  SER A  169  1                                  13    
HELIX   10  10 ASN A  172  THR A  183  1                                  12    
HELIX   11  11 LEU A  191  ALA A  197  1                                   7    
HELIX   12  12 ASP A  210  GLU A  219  1                                  10    
HELIX   13  13 ASN A  233  ASN A  238  1                                   6    
HELIX   14  14 ASN A  238  ARG A  251  1                                  14    
HELIX   15  15 TRP B   30  GLU B   35  1                                   6    
HELIX   16  16 HIS B   50  ALA B   54  5                                   5    
HELIX   17  17 GLY B   60  TYR B   75  1                                  16    
HELIX   18  18 SER B   86  GLY B   99  1                                  14    
HELIX   19  19 ASN B  117  GLU B  138  1                                  22    
HELIX   20  20 PRO B  139  TYR B  148  1                                  10    
HELIX   21  21 GLN B  149  ALA B  154  5                                   6    
HELIX   22  22 ASN B  157  SER B  169  1                                  13    
HELIX   23  23 ASN B  172  THR B  183  1                                  12    
HELIX   24  24 LEU B  191  ALA B  197  1                                   7    
HELIX   25  25 ASP B  210  ALA B  218  1                                   9    
HELIX   26  26 ASN B  233  ASN B  238  1                                   6    
HELIX   27  27 ASN B  238  ARG B  251  1                                  14    
HELIX   28  28 TRP C   30  GLU C   35  1                                   6    
HELIX   29  29 HIS C   50  ALA C   54  5                                   5    
HELIX   30  30 GLY C   60  ASN C   76  1                                  17    
HELIX   31  31 SER C   86  GLY C   99  1                                  14    
HELIX   32  32 ASN C  117  GLU C  138  1                                  22    
HELIX   33  33 PRO C  139  TYR C  148  1                                  10    
HELIX   34  34 GLN C  149  ALA C  154  5                                   6    
HELIX   35  35 ASN C  157  SER C  169  1                                  13    
HELIX   36  36 ASN C  172  THR C  183  1                                  12    
HELIX   37  37 SER C  184  GLN C  188  5                                   5    
HELIX   38  38 LEU C  191  ALA C  197  1                                   7    
HELIX   39  39 ASP C  210  ALA C  218  1                                   9    
HELIX   40  40 ASN C  233  ASN C  238  1                                   6    
HELIX   41  41 ASN C  238  PHE C  252  1                                  15    
SHEET    1   A 7 ALA A   5  LYS A   8  0                                        
SHEET    2   A 7 SER A  41  VAL A  45 -1  O  ARG A  42   N  LYS A   8           
SHEET    3   A 7 TRP A  16  LEU A  20  1  N  PHE A  19   O  LEU A  43           
SHEET    4   A 7 PHE A  80  TYR A  85  1  O  TRP A  81   N  VAL A  18           
SHEET    5   A 7 LEU A 103  GLU A 109  1  O  CYS A 104   N  PHE A  80           
SHEET    6   A 7 ALA A 201  GLY A 207  1  O  LEU A 205   N  VAL A 108           
SHEET    7   A 7 ASP A 223  ILE A 227  1  O  ILE A 227   N  CYS A 206           
SHEET    1   B 7 ALA B   5  LYS B   8  0                                        
SHEET    2   B 7 SER B  41  VAL B  45 -1  O  ARG B  42   N  LYS B   8           
SHEET    3   B 7 TRP B  16  LEU B  20  1  N  LEU B  17   O  LEU B  43           
SHEET    4   B 7 PHE B  80  TYR B  85  1  O  VAL B  83   N  VAL B  18           
SHEET    5   B 7 LEU B 103  GLU B 109  1  O  CYS B 104   N  PHE B  80           
SHEET    6   B 7 ALA B 201  GLY B 207  1  O  TYR B 203   N  VAL B 106           
SHEET    7   B 7 ASP B 223  ILE B 227  1  O  HIS B 225   N  TYR B 204           
SHEET    1   C 7 ALA C   5  LYS C   8  0                                        
SHEET    2   C 7 SER C  41  VAL C  45 -1  O  TYR C  44   N  GLN C   6           
SHEET    3   C 7 TRP C  16  LEU C  20  1  N  LEU C  17   O  SER C  41           
SHEET    4   C 7 PHE C  80  TYR C  85  1  O  VAL C  83   N  VAL C  18           
SHEET    5   C 7 LEU C 103  GLU C 109  1  O  CYS C 104   N  PHE C  80           
SHEET    6   C 7 PHE C 202  GLY C 207  1  O  LEU C 205   N  VAL C 108           
SHEET    7   C 7 ASP C 223  ILE C 227  1  O  HIS C 225   N  TYR C 204           
CISPEP   1 GLY C   -6    LEU C   -5          0         0.22                     
SITE     1 AC1  5 LYS A   8  HIS A   9  PRO C  15  TRP C  81                    
SITE     2 AC1  5 CYS C 104                                                     
SITE     1 AC2  6 SER A  86  LEU A  87  ARG A  90  HOH A 401                    
SITE     2 AC2  6 HOH A 408  HOH A 451                                          
SITE     1 AC3  6 ARG A 198  PHE A 200  ALA A 201  PHE A 202                    
SITE     2 AC3  6 HOH A 422  HIS B   9                                          
SITE     1 AC4  6 TYR A  85  TYR A 148  ARG A 168  ASN A 233                    
SITE     2 AC4  6 HOH A 434  HOH A 493                                          
SITE     1 AC5  7 ALA A  36  ALA A 247  ARG A 251  ALA B  36                    
SITE     2 AC5  7 PHE B  37  ALA B 247  ARG B 251                               
SITE     1 AC6  6 SER B  86  LEU B  87  ARG B  90  HOH B 437                    
SITE     2 AC6  6 HOH B 446  HOH B 449                                          
SITE     1 AC7  4 TYR B  85  TYR B 148  ARG B 168  ASN B 233                    
SITE     1 AC8  4 SER C  86  LEU C  87  ARG C  90  HOH C 401                    
SITE     1 AC9  4 TYR C  85  TYR C 148  ARG C 168  ASN C 233                    
CRYST1  115.144  115.144  469.775  90.00  90.00  90.00 I 41 2 2     48          
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      0.008685  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008685  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002129        0.00000                         
TER    1977      PHE A 252                                                      
TER    3931      PHE B 252                                                      
TER    5926      PHE C 252                                                      
MASTER      399    0    9   41   21    0   15    6 6188    3   30   63          
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
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