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LongText Report for: 4GEG-pdb

Name Class
4GEG-pdb
HEADER    LYASE                                   01-AUG-12   4GEG              
TITLE     CRYSTAL STRUCTURE OF E.COLI MENH Y85F 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_Y85FMUTANT, 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, MENH Y85F MUTANT, LYASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M JOHNSTON,E.N.BAKER,Z.GUO,M.JIANG                                  
REVDAT   2   15-MAY-13 4GEG    1       JRNL                                     
REVDAT   1   08-MAY-13 4GEG    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.    2.49 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) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 34093                          
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)  : 0.180                          
REMARK   3   R VALUE            (WORKING SET)  : 0.177                          
REMARK   3   FREE R VALUE                      : 0.249                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.050                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1723                           
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               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.49                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.57                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.77                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2838                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2158                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2679                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2117                   
REMARK   3   BIN FREE R VALUE                        : 0.2860                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.60                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 159                      
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            : 5959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 419                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.56280                                             
REMARK   3    B22 (A**2) : -2.23740                                             
REMARK   3    B33 (A**2) : 2.80010                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.29530                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.27                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.43                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.27                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.39                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.27                
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      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.843                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6164   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 8370   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2764   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 149    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 923    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6164   ; 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   : 745    ; 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   : 7428   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.07                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.92                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 3.08                     
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 4GEG 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 RCSB074080.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-11                          
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) : 0.953695                           
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   : 34116                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.489                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 124.587                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.32400                            
REMARK 200  R SYM                      (I) : 0.32400                            
REMARK 200   FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.62                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.95400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.95400                            
REMARK 200   FOR SHELL         : 2.000                              
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   (%): 54.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
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: 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      125.24950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.79450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      125.24950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.79450            
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, 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: 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: MONOMERIC                         
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     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     PHE B   252                                                      
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 465     GLY C    -6                                                      
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        0.04     82.69                                   
REMARK 500    PHE A  37       54.05   -100.47                                   
REMARK 500    SER A  86     -110.05     42.50                                   
REMARK 500    SER B  24       -1.69     80.50                                   
REMARK 500    SER B  86     -102.00     48.44                                   
REMARK 500    ALA B 221       41.20    -83.09                                   
REMARK 500    SER C  24       -8.76     93.29                                   
REMARK 500    PHE C  37       53.30   -105.05                                   
REMARK 500    SER C  86     -104.03     51.17                                   
REMARK 500    THR C 137      -36.58   -136.00                                   
REMARK 500    ASP C 223       73.90    -64.89                                   
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 B 474        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 475        DISTANCE =  5.77 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 306                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 307                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 309                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 310                  
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: 4GEC   RELATED DB: PDB                                   
REMARK 900 E. COLI MENH R124A MUTANT STRUCTURE                                  
DBREF  4GEG A    1   252  UNP    P37355   MENH_ECOLI       1    252             
DBREF  4GEG B    1   252  UNP    P37355   MENH_ECOLI       1    252             
DBREF  4GEG C    1   252  UNP    P37355   MENH_ECOLI       1    252             
SEQADV 4GEG MET A  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS A   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER A   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER A   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY A   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG LEU A   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG VAL A   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PRO A   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG ARG A   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY A   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER A    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PHE A   85  UNP  P37355    TYR    85 ENGINEERED MUTATION            
SEQADV 4GEG MET B  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS B   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER B   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER B   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY B   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG LEU B   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG VAL B   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PRO B   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG ARG B   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY B   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER B    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PHE B   85  UNP  P37355    TYR    85 ENGINEERED MUTATION            
SEQADV 4GEG MET C  -15  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C  -14  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C  -13  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C  -12  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C  -11  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C  -10  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG HIS C   -9  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER C   -8  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER C   -7  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY C   -6  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG LEU C   -5  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG VAL C   -4  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PRO C   -3  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG ARG C   -2  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG GLY C   -1  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG SER C    0  UNP  P37355              EXPRESSION TAG                 
SEQADV 4GEG PHE C   85  UNP  P37355    TYR    85 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 PHE 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 ARG 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 PHE 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 ARG 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 PHE 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 ARG 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    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET     CL  A 305       1                                                       
HET    EDO  A 306       4                                                       
HET    SO4  B 301       5                                                       
HET    SO4  B 302       5                                                       
HET    SO4  B 303       5                                                       
HET    SO4  B 304       5                                                       
HET     CL  B 305       1                                                       
HET    GOL  B 306       6                                                       
HET     CL  B 307       1                                                       
HET    SO4  C 301       5                                                       
HET    SO4  C 302       5                                                       
HET    SO4  C 303       5                                                       
HET    SO4  C 304       5                                                       
HET    SO4  C 305       5                                                       
HET     CL  C 306       1                                                       
HET     CL  C 307       1                                                       
HET    GOL  C 308       6                                                       
HET     CL  C 309       1                                                       
HET     CL  C 310       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  SO4    13(O4 S 2-)                                                  
FORMUL   8   CL    7(CL 1-)                                                     
FORMUL   9  EDO    C2 H6 O2                                                     
FORMUL  15  GOL    2(C3 H8 O3)                                                  
FORMUL  27  HOH   *419(H2 O)                                                    
HELIX    1   1 TRP A   30  GLU A   35  1                                   6    
HELIX    2   2 HIS A   50  ALA A   54  5                                   5    
HELIX    3   3 GLY A   60  TYR A   75  1                                  16    
HELIX    4   4 SER A   86  GLY A   99  1                                  14    
HELIX    5   5 ASN A  117  GLU A  138  1                                  22    
HELIX    6   6 PRO A  139  TYR A  148  1                                  10    
HELIX    7   7 GLN A  149  ALA A  154  5                                   6    
HELIX    8   8 ASN A  157  SER A  169  1                                  13    
HELIX    9   9 ASN A  172  THR A  183  1                                  12    
HELIX   10  10 LEU A  191  ALA A  197  1                                   7    
HELIX   11  11 ASP A  210  GLU A  219  1                                  10    
HELIX   12  12 ASN A  233  ASN A  238  1                                   6    
HELIX   13  13 ASN A  238  ARG A  251  1                                  14    
HELIX   14  14 TRP B   30  GLU B   35  1                                   6    
HELIX   15  15 HIS B   50  ALA B   54  5                                   5    
HELIX   16  16 GLY B   60  TYR B   75  1                                  16    
HELIX   17  17 SER B   86  CYS B   97  1                                  12    
HELIX   18  18 ASN B  117  LEU B  136  1                                  20    
HELIX   19  19 PRO B  139  TYR B  148  1                                  10    
HELIX   20  20 GLN B  149  ALA B  154  5                                   6    
HELIX   21  21 ASN B  157  SER B  169  1                                  13    
HELIX   22  22 ASN B  172  THR B  183  1                                  12    
HELIX   23  23 SER B  184  GLN B  188  5                                   5    
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  TYR C   75  1                                  16    
HELIX   31  31 SER C   86  GLY C   99  1                                  14    
HELIX   32  32 ASN C  117  LEU C  136  1                                  20    
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 LEU C  191  ALA C  197  1                                   7    
HELIX   38  38 ASP C  210  LEU C  220  1                                  11    
HELIX   39  39 ASN C  233  ASN C  238  1                                   6    
HELIX   40  40 ASN C  238  ARG C  251  1                                  14    
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  PHE A  85  1  O  VAL A  83   N  VAL A  18           
SHEET    5   A 7 LEU A 103  GLU A 109  1  O  ILE A 107   N  LEU A  82           
SHEET    6   A 7 ALA A 201  GLY A 207  1  O  LEU A 205   N  VAL A 108           
SHEET    7   A 7 CYS A 224  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  PHE B  85  1  O  TRP B  81   N  TRP B  16           
SHEET    5   B 7 LEU B 103  GLU B 109  1  O  CYS B 104   N  PHE B  80           
SHEET    6   B 7 PHE B 202  GLY B 207  1  O  TYR B 203   N  VAL B 108           
SHEET    7   B 7 ASP B 223  ILE B 227  1  O  ILE B 227   N  CYS B 206           
SHEET    1   C 7 ALA C   5  LYS C   8  0                                        
SHEET    2   C 7 SER C  41  VAL C  45 -1  O  ARG C  42   N  LYS C   8           
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  PHE C  85  1  O  TRP C  81   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 ALA C 201  GLY C 207  1  O  LEU C 205   N  VAL C 108           
SHEET    7   C 7 HIS C 225  ILE C 227  1  O  ILE C 227   N  CYS C 206           
SITE     1 AC1  8 SER A  86  LEU A  87  ARG A  90  EDO A 306                    
SITE     2 AC1  8 HOH A 452  HOH A 503  HOH A 526  HOH A 540                    
SITE     1 AC2  5 GLY A  60  PHE A  61  ASP A  62  HOH A 401                    
SITE     2 AC2  5 HOH A 529                                                     
SITE     1 AC3  5 ARG A 198  ALA A 201  PHE A 202  TYR A 203                    
SITE     2 AC3  5 HOH A 511                                                     
SITE     1 AC4  4 ALA A   7  LYS A   8  HIS A   9  HOH A 493                    
SITE     1 AC5  3 TYR A 148  ARG A 168  ASN A 233                               
SITE     1 AC6  5 ARG A 124  VAL A 152  PHE A 213  SO4 A 301                    
SITE     2 AC6  5 HOH A 418                                                     
SITE     1 AC7  7 SER B  86  LEU B  87  ARG B  90  ARG B 124                    
SITE     2 AC7  7 HOH B 437  HOH B 441  HOH B 534                               
SITE     1 AC8  2 ARG B 209  ARG B 229                                          
SITE     1 AC9  4 GLU B 163  LEU B 167  ARG B 236  HOH B 491                    
SITE     1 BC1  4 HOH A 493  ARG B 198  ALA B 201  PHE B 202                    
SITE     1 BC2  3 TYR B 148  ARG B 168  ASN B 233                               
SITE     1 BC3  5 HIS B   9  TYR B  75  PRO B 151  VAL B 152                    
SITE     2 BC3  5 LYS B 212                                                     
SITE     1 BC4  1 GLN B 160                                                     
SITE     1 BC5  8 SER C  86  ARG C  90  ARG C 124  HOH C 440                    
SITE     2 BC5  8 HOH C 443  HOH C 474  HOH C 478  HOH C 511                    
SITE     1 BC6  2 LYS C   8  HIS C   9                                          
SITE     1 BC7  2 ALA C 101  GLY C 102                                          
SITE     1 BC8  1 ARG C 236                                                     
SITE     1 BC9  4 SER C   0  MET C   1  ARG C 126  GLN C 130                    
SITE     1 CC1  3 GLY B 173  HOH B 429  GLY C 173                               
SITE     1 CC2  3 TYR C 148  ARG C 168  ASN C 233                               
SITE     1 CC3  6 ARG C  69  GLY C  99  LEU C 100  ALA C 101                    
SITE     2 CC3  6 HOH C 505  HOH C 512                                          
SITE     1 CC4  3 HOH C 491  HOH C 499  HOH C 533                               
SITE     1 CC5  2 LEU C  78  ASP C  79                                          
CRYST1  250.499   41.589   93.081  90.00  95.89  90.00 C 1 2 1      12          
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      0.003992  0.000000  0.000412        0.00000                         
SCALE2      0.000000  0.024045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010800        0.00000                         
TER    1990      PHE A 252                                                      
TER    3966      ARG B 251                                                      
TER    5962      PHE C 252                                                      
MASTER      415    0   23   40   21    0   31    6 6466    3   81   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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