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LongText Report for: 6gu8-pdb

Name Class
6gu8-pdb
HEADER    HYDROLASE                               19-JUN-18   6GU8              
TITLE     GLUCURONOYL ESTERASE FROM SOLIBACTER USITATUS                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ACETYL XYLAN ESTERASE;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CANDIDATUS SOLIBACTER USITATUS ELLIN6076;       
SOURCE   3 ORGANISM_TAXID: 234267;                                              
SOURCE   4 GENE: ACID_4275;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    CARBOHYDRATE ESTERASE, HYDROLASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.LO LEGGIO,J.LARSBRINK,R.MELAND KNUDSEN,S.MAZURKEWICH,J.C.NAVARRO    
AUTHOR   2 POULSEN                                                              
REVDAT   1   15-AUG-18 6GU8    0                                                
JRNL        AUTH   J.ARNLING BAATH,S.MAZURKEWICH,R.M.KNUDSEN,J.N.POULSEN,       
JRNL        AUTH 2 L.OLSSON,L.LO LEGGIO,J.LARSBRINK                             
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL FEATURES OF DIVERSE BACTERIAL     
JRNL        TITL 2 GLUCURONOYL ESTERASES FACILITATING RECALCITRANT BIOMASS      
JRNL        TITL 3 CONVERSION.                                                  
JRNL        REF    BIOTECHNOL BIOFUELS           V.  11   213 2018              
JRNL        REFN                   ESSN 1754-6834                               
JRNL        PMID   30083226                                                     
JRNL        DOI    10.1186/S13068-018-1213-X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.29                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.354                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 29588                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.231                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 956                             
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 47.3010 -  3.8598    1.00     4398   147  0.1493 0.1967        
REMARK   3     2  3.8598 -  3.0638    1.00     4154   139  0.1609 0.2222        
REMARK   3     3  3.0638 -  2.6766    1.00     4074   135  0.1923 0.2948        
REMARK   3     4  2.6766 -  2.4319    1.00     4031   135  0.2164 0.3056        
REMARK   3     5  2.4319 -  2.2576    1.00     4001   133  0.2297 0.3083        
REMARK   3     6  2.2576 -  2.1245    1.00     4020   134  0.2503 0.3176        
REMARK   3     7  2.1245 -  2.0181    1.00     3954   133  0.2947 0.3474        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.302            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.838           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.012           3253                                  
REMARK   3   ANGLE     :  1.158           4393                                  
REMARK   3   CHIRALITY :  0.058            442                                  
REMARK   3   PLANARITY :  0.008            577                                  
REMARK   3   DIHEDRAL  : 16.253           1934                                  
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 6GU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-AUG-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, DESY                    
REMARK 200  BEAMLINE                       : P11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS BUILT=20180126                 
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59163                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.018                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.290                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.06910                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2700                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42610                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX 1.13_2998                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RESERVOIR COMPOSITION: 0.02 M D          
REMARK 280  -GLUCOSE, 0.02 M D-MANNOSE, 0.02 M D-GALACTOSE, 0.02 M L-FUCOSE,    
REMARK 280  0.02 M D-XYLOSE, 0.02 M N-ACETYL-D-GLUCOSAMINE, 0.05 M TRIS,        
REMARK 280  0.05 M BICINE, 20% V/V PEG500MME, 10% W/V PEG20000 DROP SIZE AND    
REMARK 280  COMPOSITION: SITTING DROPS OF 0.3 UL WERE MIXED IN A PROTEIN:       
REMARK 280  RESERVOIR VOLUME RATIO OF 1:1 USING 23.6 MG/ML OF SUCE15C-SEMET     
REMARK 280  IN 20 MM TRIS PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  293.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      142.05600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.28950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.28950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      213.08400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.28950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.28950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       71.02800            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.28950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.28950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      213.08400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.28950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.28950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       71.02800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      142.05600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 37.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     ILE A    23                                                      
REMARK 465     THR A    24                                                      
REMARK 465     ASP A    25                                                      
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     TRP A 348    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 348    CZ3  CH2                                            
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   H    GLY A   214     O    HOH A   618              1.50            
REMARK 500  HH12  ARG A   318     O    HOH A   604              1.55            
REMARK 500   OD1  ASN A   279     HH   TYR A   408              1.59            
REMARK 500   O    ALA A   121     O    HOH A   601              2.03            
REMARK 500   O    ASN A   301     O    HOH A   602              2.04            
REMARK 500   OE2  GLU A   321     O    HOH A   603              2.06            
REMARK 500   NH1  ARG A   318     O    HOH A   604              2.11            
REMARK 500   O    HOH A   674     O    HOH A   683              2.11            
REMARK 500   OE2  GLU A   280     O    HOH A   605              2.13            
REMARK 500   OE2  GLU A   383     O    HOH A   606              2.17            
REMARK 500   O    GLN A   347     O    HOH A   607              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   HO2  EDO A   501     HO2  EDO A   501     7556     0.98            
REMARK 500   O2   EDO A   501     HO2  EDO A   501     7556     1.59            
REMARK 500   O2   EDO A   501     O2   EDO A   501     7556     1.81            
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    ARG A 173   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    VAL A  68      -69.15   -128.78                                   
REMARK 500    PRO A 213      109.37    -54.40                                   
REMARK 500    SER A 257     -133.29     55.26                                   
REMARK 500    PRO A 323       38.70    -80.34                                   
REMARK 500    GLN A 347     -138.37     84.98                                   
REMARK 500    SER A 349      176.28    -57.54                                   
REMARK 500    ASP A 387      -84.88   -111.93                                   
REMARK 500    ASP A 399     -179.86   -175.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 511                 
DBREF  6GU8 A   23   417  UNP    Q01YM8   Q01YM8_SOLUE    23    417             
SEQADV 6GU8 GLY A   21  UNP  Q01YM8              EXPRESSION TAG                 
SEQADV 6GU8 HIS A   22  UNP  Q01YM8              EXPRESSION TAG                 
SEQRES   1 A  397  GLY HIS ILE THR ASP GLU ALA LYS VAL PRO ALA TYR THR          
SEQRES   2 A  397  LEU PRO ALA VAL LEU ALA LEU LYS SER GLY GLN PRO VAL          
SEQRES   3 A  397  THR ASP ALA LYS SER TRP THR THR LYS ARG ARG PRO GLU          
SEQRES   4 A  397  ILE LEU ALA ILE TYR GLU ALA GLU VAL TYR GLY LYS SER          
SEQRES   5 A  397  PRO ALA ARG PRO PRO LYS LEU ASN TYR GLU VAL LYS SER          
SEQRES   6 A  397  VAL GLU LYS GLN ALA LEU GLY GLY LYS ALA THR ARG LYS          
SEQRES   7 A  397  ILE VAL THR ILE PHE PHE SER ASP LYS PRO ASP ALA PRO          
SEQRES   8 A  397  LYS MSE ASP LEU LEU LEU TYR LEU PRO ALA ALA ALA ALA          
SEQRES   9 A  397  LYS PRO ALA PRO VAL ILE LEU GLY LEU SER PHE GLY GLY          
SEQRES  10 A  397  ILE HIS THR VAL ALA ASN ASP PRO GLY VAL PRO LEU ALA          
SEQRES  11 A  397  GLU GLN TRP THR ARG ASP ASN ARG LYS GLN PRO SER ALA          
SEQRES  12 A  397  GLU LYS SER ARG GLY GLY GLU ALA SER ARG TRP GLN VAL          
SEQRES  13 A  397  GLU LYS ILE LEU ALA ALA GLY TYR GLY LEU ALA THR VAL          
SEQRES  14 A  397  TYR TYR GLU GLN ILE GLU PRO ASP PHE ALA GLY GLY MSE          
SEQRES  15 A  397  LYS TYR GLY ILE ARG PRO LEU PHE PHE LYS PRO GLY GLN          
SEQRES  16 A  397  THR GLU PRO GLU PRO GLY ASP TRP GLY ALA VAL ALA ALA          
SEQRES  17 A  397  TRP ALA TRP GLY ALA SER ARG ALA MSE ASP TYR LEU GLU          
SEQRES  18 A  397  LYS ASP LYS ASP VAL ASP ALA ARG ARG VAL GLY LEU ILE          
SEQRES  19 A  397  GLY HIS SER ARG LEU GLY LYS ALA ALA ILE TRP ALA GLY          
SEQRES  20 A  397  ALA GLN ASP ALA ARG PHE THR PHE ILE ILE SER ASN GLU          
SEQRES  21 A  397  SER GLY GLU GLY GLY ALA ALA ILE SER ARG ARG ASP TYR          
SEQRES  22 A  397  GLY GLU ARG THR THR ALA LEU ASN THR ARG PHE PRO HIS          
SEQRES  23 A  397  TRP PHE ASP GLY ASN TYR LYS LYS TYR ASN ASP ARG GLU          
SEQRES  24 A  397  ASN GLU MSE PRO PHE ASP SER HIS MSE ALA LEU ALA LEU          
SEQRES  25 A  397  MSE ALA PRO ARG GLY LEU TYR VAL ALA SER ALA GLU GLY          
SEQRES  26 A  397  ASP GLN TRP SER ASP PRO LYS GLY GLU PHE LEU GLY ALA          
SEQRES  27 A  397  ALA ASN ALA SER PRO VAL TRP GLU LEU PHE GLY LYS LYS          
SEQRES  28 A  397  GLY ILE GLY THR MSE THR MSE PRO ASP LEU HIS GLU PRO          
SEQRES  29 A  397  VAL GLY ASP SER VAL ARG TYR HIS ILE ARG ALA GLY LYS          
SEQRES  30 A  397  HIS ASP VAL THR GLU TYR ASP TRP GLU GLN TYR LEU LYS          
SEQRES  31 A  397  PHE ALA LYS ALA GLN TRP GLY                                  
MODRES 6GU8 MSE A  113  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  202  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  237  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  322  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  328  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  333  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  376  MET  MODIFIED RESIDUE                                   
MODRES 6GU8 MSE A  378  MET  MODIFIED RESIDUE                                   
HET    MSE  A 113      17                                                       
HET    MSE  A 202      17                                                       
HET    MSE  A 237      17                                                       
HET    MSE  A 322      17                                                       
HET    MSE  A 328      17                                                       
HET    MSE  A 333      17                                                       
HET    MSE  A 376      34                                                       
HET    MSE  A 378      17                                                       
HET    EDO  A 501      10                                                       
HET    EDO  A 502      10                                                       
HET    EDO  A 503      10                                                       
HET    EDO  A 504      10                                                       
HET    EDO  A 505      10                                                       
HET    EDO  A 506      10                                                       
HET    EDO  A 507      10                                                       
HET    EDO  A 508      10                                                       
HET    PEG  A 509      17                                                       
HET    PEG  A 510      17                                                       
HET    PEG  A 511      17                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   2  EDO    8(C2 H6 O2)                                                  
FORMUL  10  PEG    3(C4 H10 O3)                                                 
FORMUL  13  HOH   *277(H2 O)                                                    
HELIX    1 AA1 ASP A   48  LYS A   55  1                                   8    
HELIX    2 AA2 LYS A   55  VAL A   68  1                                  14    
HELIX    3 AA3 GLY A  137  VAL A  141  5                                   5    
HELIX    4 AA4 ALA A  163  ARG A  167  5                                   5    
HELIX    5 AA5 GLU A  170  TRP A  174  5                                   5    
HELIX    6 AA6 GLN A  175  ALA A  182  1                                   8    
HELIX    7 AA7 GLU A  192  ILE A  194  5                                   3    
HELIX    8 AA8 GLY A  200  GLY A  205  5                                   6    
HELIX    9 AA9 ILE A  206  PHE A  211  5                                   6    
HELIX   10 AB1 GLY A  224  GLU A  241  1                                  18    
HELIX   11 AB2 SER A  257  ASP A  270  1                                  14    
HELIX   12 AB3 ILE A  288  ASP A  292  5                                   5    
HELIX   13 AB4 GLY A  294  PHE A  304  1                                  11    
HELIX   14 AB5 GLY A  310  GLU A  319  5                                  10    
HELIX   15 AB6 ASP A  325  LEU A  332  1                                   8    
HELIX   16 AB7 ASP A  350  SER A  362  1                                  13    
HELIX   17 AB8 SER A  362  PHE A  368  1                                   7    
HELIX   18 AB9 THR A  401  GLY A  417  1                                  17    
SHEET    1 AA110 ASN A  80  ALA A  90  0                                        
SHEET    2 AA110 ALA A  95  PHE A 103 -1  O  THR A 101   N  GLU A  82           
SHEET    3 AA110 LYS A 112  PRO A 120 -1  O  LEU A 115   N  VAL A 100           
SHEET    4 AA110 GLY A 185  TYR A 190 -1  O  THR A 188   N  LEU A 116           
SHEET    5 AA110 ALA A 127  SER A 134  1  N  SER A 134   O  VAL A 189           
SHEET    6 AA110 VAL A 246  HIS A 256  1  O  GLY A 252   N  LEU A 131           
SHEET    7 AA110 PHE A 273  ASN A 279  1  O  THR A 274   N  VAL A 251           
SHEET    8 AA110 GLY A 337  ALA A 343  1  O  TYR A 339   N  SER A 278           
SHEET    9 AA110 VAL A 389  ARG A 394  1  O  ARG A 390   N  VAL A 340           
SHEET   10 AA110 VAL A 385  GLY A 386 -1  N  VAL A 385   O  TYR A 391           
SHEET    1 AA2 2 GLU A 151  TRP A 153  0                                        
SHEET    2 AA2 2 LYS A 159  PRO A 161 -1  O  GLN A 160   N  GLN A 152           
LINK         C   LYS A 112                 N   MSE A 113     1555   1555  1.33  
LINK         C   MSE A 113                 N   ASP A 114     1555   1555  1.34  
LINK         C   GLY A 201                 N   MSE A 202     1555   1555  1.32  
LINK         C   MSE A 202                 N   LYS A 203     1555   1555  1.34  
LINK         C   ALA A 236                 N   MSE A 237     1555   1555  1.33  
LINK         C   MSE A 237                 N   ASP A 238     1555   1555  1.34  
LINK         C   GLU A 321                 N   MSE A 322     1555   1555  1.33  
LINK         C   MSE A 322                 N   PRO A 323     1555   1555  1.32  
LINK         C   HIS A 327                 N   MSE A 328     1555   1555  1.33  
LINK         C   MSE A 328                 N   ALA A 329     1555   1555  1.35  
LINK         C   LEU A 332                 N   MSE A 333     1555   1555  1.33  
LINK         C   MSE A 333                 N   ALA A 334     1555   1555  1.33  
LINK         C   THR A 375                 N  AMSE A 376     1555   1555  1.33  
LINK         C   THR A 375                 N  BMSE A 376     1555   1555  1.33  
LINK         C  AMSE A 376                 N   THR A 377     1555   1555  1.33  
LINK         C  BMSE A 376                 N   THR A 377     1555   1555  1.34  
LINK         C   THR A 377                 N   MSE A 378     1555   1555  1.32  
LINK         C   MSE A 378                 N   PRO A 379     1555   1555  1.33  
CISPEP   1 ALA A  334    PRO A  335          0         1.22                     
SITE     1 AC1  3 GLN A 415  TRP A 416  GLY A 417                               
SITE     1 AC2  2 LEU A  79  TYR A  81                                          
SITE     1 AC3  4 ARG A 258  GLN A 347  PEG A 509  PEG A 511                    
SITE     1 AC4  8 PHE A 135  ARG A 173  TRP A 174  HIS A 256                    
SITE     2 AC4  8 VAL A 400  HOH A 621  HOH A 699  HOH A 744                    
SITE     1 AC5  6 ASP A 114  ALA A 150  GLU A 151  GLN A 193                    
SITE     2 AC5  6 HOH A 682  HOH A 755                                          
SITE     1 AC6  3 ARG A 291  ARG A 296  ASP A 350                               
SITE     1 AC7  5 GLU A 192  ASP A 197  HOH A 608  HOH A 638                    
SITE     2 AC7  5 HOH A 681                                                     
SITE     1 AC8  6 PHE A 135  GLU A 170  ARG A 258  GLN A 347                    
SITE     2 AC8  6 EDO A 504  HOH A 612                                          
SITE     1 AC9  5 PRO A  73  ARG A 235  GLN A 269  ARG A 272                    
SITE     2 AC9  5 HOH A 695                                                     
SITE     1 AD1 10 SER A 257  ARG A 258  LYS A 261  GLY A 282                    
SITE     2 AD1 10 GLU A 283  LEU A 300  EDO A 504  HOH A 613                    
SITE     3 AD1 10 HOH A 639  HOH A 675                                          
CRYST1   54.579   54.579  284.112  90.00  90.00  90.00 P 43 21 2     8          
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      0.018322  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018322  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003520        0.00000                         
TER    6172      GLY A 417                                                      
MASTER      366    0   19   18   12    0   17    6 3382    1  300   31          
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:
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