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LongText Report for: 4G5X-pdb

Name Class
4G5X-pdb
HEADER    HYDROLASE                               18-JUL-12   4G5X              
TITLE     CRYSTAL STRUCTURES OF N-ACYL HOMOSERINE LACTONASE AIDH                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OCHROBACTRUM;                                   
SOURCE   3 ORGANISM_TAXID: 680275;                                              
SOURCE   4 STRAIN: T63;                                                         
SOURCE   5 GENE: AIDH;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA-HYDROLASE FOLD, CORE DOMAIN, EIGHT-STRANDED SHEET,         
KEYWDS   2 LACTONASE, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.LIANG,X.X.YAN,A.GAO                                               
REVDAT   1   16-JAN-13 4G5X    0                                                
JRNL        AUTH   A.GAO,G.Y.MEI,S.LIU,P.WANG,Q.TANG,Y.P.LIU,H.WEN,X.M.AN,      
JRNL        AUTH 2 L.Q.ZHANG,X.X.YAN,D.C.LIANG                                  
JRNL        TITL   HIGH-RESOLUTION STRUCTURES OF AIDH COMPLEXES PROVIDE         
JRNL        TITL 2 INSIGHTS INTO A NOVEL CATALYTIC MECHANISM FOR N-ACYL         
JRNL        TITL 3 HOMOSERINE LACTONASE                                         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  69    82 2013              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   23275166                                                     
JRNL        DOI    10.1107/S0907444912042369                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.29 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.29                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 83.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 93530                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.125                           
REMARK   3   R VALUE            (WORKING SET) : 0.123                           
REMARK   3   FREE R VALUE                     : 0.158                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4727                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.8720 -  2.7770    0.96    10374   522  0.1259 0.1475        
REMARK   3     2  2.7770 -  2.2051    0.96    10275   556  0.1217 0.1514        
REMARK   3     3  2.2051 -  1.9266    0.88     9429   489  0.1120 0.1434        
REMARK   3     4  1.9266 -  1.7506    0.81     8596   484  0.1030 0.1456        
REMARK   3     5  1.7506 -  1.6252    0.80     8614   419  0.0976 0.1429        
REMARK   3     6  1.6252 -  1.5294    0.80     8521   500  0.1008 0.1581        
REMARK   3     7  1.5294 -  1.4528    0.80     8468   473  0.1126 0.1784        
REMARK   3     8  1.4528 -  1.3896    0.77     8309   425  0.1439 0.2174        
REMARK   3     9  1.3896 -  1.3361    0.77     8144   419  0.1853 0.2447        
REMARK   3    10  1.3361 -  1.2900    0.76     8073   440  0.2185 0.2650        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.49                                          
REMARK   3   K_SOL              : 0.46                                          
REMARK   3   B_SOL              : 102.14                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.28130                                              
REMARK   3    B22 (A**2) : 0.51550                                              
REMARK   3    B33 (A**2) : -1.79680                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 1.27020                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           4562                                  
REMARK   3   ANGLE     :  1.064           6211                                  
REMARK   3   CHIRALITY :  0.073            648                                  
REMARK   3   PLANARITY :  0.005            845                                  
REMARK   3   DIHEDRAL  : 12.386           1737                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G5X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073778.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 180                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 124835                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.290                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 55.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 34.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       64.74500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     HIS A   277                                                      
REMARK 465     HIS A   278                                                      
REMARK 465     HIS A   279                                                      
REMARK 465     MET B     1                                                      
REMARK 465     HIS B   277                                                      
REMARK 465     HIS B   278                                                      
REMARK 465     HIS B   279                                                      
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     GLN A 271    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 155    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 273    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER A   153     O    ARG A   155              2.08            
REMARK 500   O    HOH B   315     O    HOH B   343              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 156   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  35     -158.17   -104.71                                   
REMARK 500    SER A 102     -116.82     63.92                                   
REMARK 500    ASP A 156       12.85     58.89                                   
REMARK 500    ASP A 181      108.65    -58.30                                   
REMARK 500    HIS A 275     -167.27   -124.85                                   
REMARK 500    SER B  35     -156.67   -107.50                                   
REMARK 500    SER B 102     -116.01     65.24                                   
REMARK 500    SER B 140       55.56   -115.21                                   
REMARK 500    ASN B 234       79.54   -156.72                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP A 156        -26.43                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 584        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH A 586        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH A 590        DISTANCE =  5.73 ANGSTROMS                       
REMARK 525    HOH A 602        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH A 618        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A 672        DISTANCE =  7.71 ANGSTROMS                       
REMARK 525    HOH A 687        DISTANCE =  8.88 ANGSTROMS                       
REMARK 525    HOH A 692        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 700        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH A 701        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH A 703        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH A 705        DISTANCE =  8.10 ANGSTROMS                       
REMARK 525    HOH A 707        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH A 708        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A 717        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH A 718        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH A 719        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH A 723        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH A 727        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH A 728        DISTANCE =  7.71 ANGSTROMS                       
REMARK 525    HOH A 729        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH A 730        DISTANCE =  9.81 ANGSTROMS                       
REMARK 525    HOH A 731        DISTANCE =  7.95 ANGSTROMS                       
REMARK 525    HOH A 735        DISTANCE =  9.40 ANGSTROMS                       
REMARK 525    HOH A 738        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH A 740        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH A 745        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A 746        DISTANCE =  9.46 ANGSTROMS                       
REMARK 525    HOH A 747        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH A 751        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH A 754        DISTANCE =  8.90 ANGSTROMS                       
REMARK 525    HOH A 755        DISTANCE =  8.36 ANGSTROMS                       
REMARK 525    HOH B 301        DISTANCE =  9.88 ANGSTROMS                       
REMARK 525    HOH B 611        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH B 653        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH B 669        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH B 670        DISTANCE =  7.31 ANGSTROMS                       
REMARK 525    HOH B 672        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH B 674        DISTANCE =  7.13 ANGSTROMS                       
REMARK 525    HOH B 675        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH B 676        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH B 679        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH B 680        DISTANCE =  9.94 ANGSTROMS                       
REMARK 525    HOH B 685        DISTANCE =  9.20 ANGSTROMS                       
REMARK 525    HOH B 687        DISTANCE =  6.82 ANGSTROMS                       
REMARK 525    HOH B 688        DISTANCE =  8.49 ANGSTROMS                       
REMARK 525    HOH B 692        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH B 696        DISTANCE =  9.69 ANGSTROMS                       
REMARK 525    HOH B 697        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH B 699        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B 703        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH B 704        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH B 709        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH B 711        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH B 717        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH B 720        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B 722        DISTANCE =  7.77 ANGSTROMS                       
REMARK 525    HOH B 726        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH B 727        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH B 728        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 731        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH B 735        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH B 737        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE =  8.62 ANGSTROMS                       
REMARK 525    HOH B 741        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH B 743        DISTANCE =  7.24 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4G8B   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G8C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G8D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G9E   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4G9G   RELATED DB: PDB                                   
DBREF  4G5X A    1   271  UNP    D2J2T6   D2J2T6_9RHIZ     1    271             
DBREF  4G5X B    1   271  UNP    D2J2T6   D2J2T6_9RHIZ     1    271             
SEQADV 4G5X LEU A  272  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X GLU A  273  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  274  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  275  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  276  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  277  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  278  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS A  279  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X LEU B  272  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X GLU B  273  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  274  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  275  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  276  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  277  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  278  UNP  D2J2T6              EXPRESSION TAG                 
SEQADV 4G5X HIS B  279  UNP  D2J2T6              EXPRESSION TAG                 
SEQRES   1 A  279  MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY          
SEQRES   2 A  279  ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO          
SEQRES   3 A  279  LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE          
SEQRES   4 A  279  PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP          
SEQRES   5 A  279  ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER          
SEQRES   6 A  279  THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU          
SEQRES   7 A  279  GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU          
SEQRES   8 A  279  GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP SER LEU GLY          
SEQRES   9 A  279  GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU          
SEQRES  10 A  279  MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA          
SEQRES  11 A  279  ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP          
SEQRES  12 A  279  MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP          
SEQRES  13 A  279  VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE          
SEQRES  14 A  279  GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY          
SEQRES  15 A  279  ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY          
SEQRES  16 A  279  THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN          
SEQRES  17 A  279  LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE          
SEQRES  18 A  279  VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN          
SEQRES  19 A  279  LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY          
SEQRES  20 A  279  HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA          
SEQRES  21 A  279  TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU          
SEQRES  22 A  279  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  279  MET THR ILE ASN TYR HIS GLU LEU GLU THR SER HIS GLY          
SEQRES   2 B  279  ARG ILE ALA VAL ARG GLU SER GLU GLY GLU GLY ALA PRO          
SEQRES   3 B  279  LEU LEU MET ILE HIS GLY ASN SER SER SER GLY ALA ILE          
SEQRES   4 B  279  PHE ALA PRO GLN LEU GLU GLY GLU ILE GLY LYS LYS TRP          
SEQRES   5 B  279  ARG VAL ILE ALA PRO ASP LEU PRO GLY HIS GLY LYS SER          
SEQRES   6 B  279  THR ASP ALA ILE ASP PRO ASP ARG SER TYR SER MET GLU          
SEQRES   7 B  279  GLY TYR ALA ASP ALA MET THR GLU VAL MET GLN GLN LEU          
SEQRES   8 B  279  GLY ILE ALA ASP ALA VAL VAL PHE GLY TRP SER LEU GLY          
SEQRES   9 B  279  GLY HIS ILE GLY ILE GLU MET ILE ALA ARG TYR PRO GLU          
SEQRES  10 B  279  MET ARG GLY LEU MET ILE THR GLY THR PRO PRO VAL ALA          
SEQRES  11 B  279  ARG GLU GLU VAL GLY GLN GLY PHE LYS SER GLY PRO ASP          
SEQRES  12 B  279  MET ALA LEU ALA GLY GLN GLU ILE PHE SER GLU ARG ASP          
SEQRES  13 B  279  VAL GLU SER TYR ALA ARG SER THR CYS GLY GLU PRO PHE          
SEQRES  14 B  279  GLU ALA SER LEU LEU ASP ILE VAL ALA ARG THR ASP GLY          
SEQRES  15 B  279  ARG ALA ARG ARG ILE MET PHE GLU LYS PHE GLY SER GLY          
SEQRES  16 B  279  THR GLY GLY ASN GLN ARG ASP ILE VAL ALA GLU ALA GLN          
SEQRES  17 B  279  LEU PRO ILE ALA VAL VAL ASN GLY ARG ASP GLU PRO PHE          
SEQRES  18 B  279  VAL GLU LEU ASP PHE VAL SER LYS VAL LYS PHE GLY ASN          
SEQRES  19 B  279  LEU TRP GLU GLY LYS THR HIS VAL ILE ASP ASN ALA GLY          
SEQRES  20 B  279  HIS ALA PRO PHE ARG GLU ALA PRO ALA GLU PHE ASP ALA          
SEQRES  21 B  279  TYR LEU ALA ARG PHE ILE ARG ASP CYS THR GLN LEU GLU          
SEQRES  22 B  279  HIS HIS HIS HIS HIS HIS                                      
FORMUL   3  HOH   *903(H2 O)                                                    
HELIX    1   1 SER A   36  ILE A   39  5                                   4    
HELIX    2   2 PHE A   40  GLY A   46  1                                   7    
HELIX    3   3 GLY A   46  LYS A   51  1                                   6    
HELIX    4   4 ASP A   70  TYR A   75  1                                   6    
HELIX    5   5 SER A   76  GLY A   92  1                                  17    
HELIX    6   6 SER A  102  TYR A  115  1                                  14    
HELIX    7   7 ALA A  130  GLU A  132  5                                   3    
HELIX    8   8 GLU A  133  PHE A  138  1                                   6    
HELIX    9   9 ASP A  143  GLN A  149  5                                   7    
HELIX   10  10 SER A  153  GLY A  166  1                                  14    
HELIX   11  11 ALA A  171  THR A  180  1                                  10    
HELIX   12  12 ASP A  181  GLY A  195  1                                  15    
HELIX   13  13 ASN A  199  ALA A  207  1                                   9    
HELIX   14  14 GLU A  223  SER A  228  1                                   6    
HELIX   15  15 LEU A  235  LYS A  239  5                                   5    
HELIX   16  16 ALA A  249  ALA A  254  1                                   6    
HELIX   17  17 ALA A  254  GLN A  271  1                                  18    
HELIX   18  18 SER B   36  ILE B   39  5                                   4    
HELIX   19  19 PHE B   40  GLY B   46  1                                   7    
HELIX   20  20 GLY B   46  LYS B   51  1                                   6    
HELIX   21  21 ASP B   70  TYR B   75  1                                   6    
HELIX   22  22 SER B   76  LEU B   91  1                                  16    
HELIX   23  23 SER B  102  TYR B  115  1                                  14    
HELIX   24  24 ALA B  130  GLU B  132  5                                   3    
HELIX   25  25 GLU B  133  PHE B  138  1                                   6    
HELIX   26  26 ASP B  143  GLN B  149  5                                   7    
HELIX   27  27 SER B  153  GLY B  166  1                                  14    
HELIX   28  28 GLU B  170  THR B  180  1                                  11    
HELIX   29  29 ASP B  181  GLY B  195  1                                  15    
HELIX   30  30 ASN B  199  ALA B  207  1                                   9    
HELIX   31  31 GLU B  223  SER B  228  1                                   6    
HELIX   32  32 LEU B  235  LYS B  239  5                                   5    
HELIX   33  33 ALA B  249  ALA B  254  1                                   6    
HELIX   34  34 ALA B  254  LEU B  272  1                                  19    
SHEET    1   A 8 ASN A   4  THR A  10  0                                        
SHEET    2   A 8 GLY A  13  GLU A  19 -1  O  GLU A  19   N  ASN A   4           
SHEET    3   A 8 TRP A  52  PRO A  57 -1  O  ALA A  56   N  ARG A  18           
SHEET    4   A 8 GLY A  24  ILE A  30  1  N  LEU A  27   O  ILE A  55           
SHEET    5   A 8 VAL A  97  TRP A 101  1  O  PHE A  99   N  LEU A  28           
SHEET    6   A 8 GLY A 120  THR A 124  1  O  MET A 122   N  VAL A  98           
SHEET    7   A 8 ILE A 211  GLY A 216  1  O  ALA A 212   N  ILE A 123           
SHEET    8   A 8 HIS A 241  ILE A 243  1  O  HIS A 241   N  VAL A 213           
SHEET    1   B 8 ASN B   4  THR B  10  0                                        
SHEET    2   B 8 GLY B  13  GLU B  19 -1  O  VAL B  17   N  HIS B   6           
SHEET    3   B 8 TRP B  52  PRO B  57 -1  O  ALA B  56   N  ARG B  18           
SHEET    4   B 8 GLY B  24  ILE B  30  1  N  LEU B  27   O  ILE B  55           
SHEET    5   B 8 VAL B  97  TRP B 101  1  O  PHE B  99   N  LEU B  28           
SHEET    6   B 8 GLY B 120  THR B 124  1  O  MET B 122   N  GLY B 100           
SHEET    7   B 8 ILE B 211  GLY B 216  1  O  ALA B 212   N  ILE B 123           
SHEET    8   B 8 HIS B 241  ILE B 243  1  O  HIS B 241   N  VAL B 213           
CISPEP   1 GLU A  167    PRO A  168          0         3.54                     
CISPEP   2 GLU B  167    PRO B  168          0         3.45                     
CRYST1   42.414  129.490   44.759  90.00 111.11  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023577  0.000000  0.009102        0.00000                         
SCALE2      0.000000  0.007723  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023949        0.00000                         
TER    2178      HIS A 276                                                      
TER    4432      HIS B 276                                                      
MASTER      379    0    0   34   16    0    0    6 5119    2    0   44          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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