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LongText Report for: 6gui-pdb

Name Class
6gui-pdb
HEADER    HYDROLASE                               19-JUN-18   6GUI              
TITLE     SIDEROPHORE HYDROLASE ESTB MUTANT H267N FROM ASPERGILLUS FUMIGATUS    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIDEROPHORE ESTERASE IROE-LIKE, PUTATIVE;                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS AF293;                    
SOURCE   3 ORGANISM_TAXID: 330879;                                              
SOURCE   4 GENE: AFUA_3G03660;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA-HYDROLASE, SIDEROPHORE, HYDROLYSIS, FUNGI, HYDROLASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.ECKER,H.HAAS,M.GROLL,E.M.HUBER                                      
REVDAT   1   15-AUG-18 6GUI    0                                                
JRNL        AUTH   F.ECKER,H.HAAS,M.GROLL,E.HUBER                               
JRNL        TITL   IRON SCAVENGING IN ASPERGILLUS SPECIES: STRUCTURAL AND       
JRNL        TITL 2 BIOCHEMICAL INSIGHTS INTO FUNGAL SIDEROPHORE ESTERASES.      
JRNL        REF    ANGEW. CHEM. INT. ED. ENGL.                2018              
JRNL        REFN                   ESSN 1521-3773                               
JRNL        PMID   30070018                                                     
JRNL        DOI    10.1002/ANIE.201807093                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 69245                          
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) : 0.160                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3644                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5049                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2540                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 266                          
REMARK   3   BIN FREE R VALUE                    : 0.2660                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4478                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 526                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.25                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.21000                                             
REMARK   3    B22 (A**2) : 2.33000                                              
REMARK   3    B33 (A**2) : -2.12000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.088         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.818         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.966                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4664 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4183 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6347 ; 1.053 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9690 ; 0.864 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   570 ; 5.045 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   215 ;37.942 ;22.744       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   704 ;10.783 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;15.974 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   669 ; 0.057 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5201 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1034 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2268 ; 0.761 ; 2.765       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2267 ; 0.761 ; 2.763       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2830 ; 0.890 ; 4.136       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2831 ; 0.890 ; 4.138       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2396 ; 0.736 ; 2.997       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2396 ; 0.736 ; 2.997       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3514 ; 0.816 ; 4.407       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5409 ; 2.001 ;33.689       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5268 ; 1.616 ;32.903       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  8847 ; 0.483 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   310 ;20.533 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  8931 ; 5.912 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6GUI 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_1200010577.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73016                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6GUD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE PH 4.5 0.9 M AMMONIUM      
REMARK 280  TARTRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       27.48500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.45000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       46.30500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.45000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.48500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       46.30500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     VAL A   195                                                      
REMARK 465     SER A   196                                                      
REMARK 465     HIS A   197                                                      
REMARK 465     ASP A   198                                                      
REMARK 465     GLY A   292                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     VAL B   195                                                      
REMARK 465     SER B   196                                                      
REMARK 465     HIS B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     GLY B   292                                                      
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 125      -50.14   -120.02                                   
REMARK 500    SER A 148     -114.28     64.39                                   
REMARK 500    ARG A 161       59.37   -143.28                                   
REMARK 500    SER B 125      -51.14   -122.12                                   
REMARK 500    SER B 148     -114.19     64.45                                   
REMARK 500    ARG B 161       59.96   -143.92                                   
REMARK 500    ASN B 178       79.86   -153.64                                   
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 GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 304                 
DBREF  6GUI A    3   292  UNP    Q4WF29   Q4WF29_ASPFU     3    292             
DBREF  6GUI B    3   292  UNP    Q4WF29   Q4WF29_ASPFU     3    292             
SEQADV 6GUI GLY A    1  UNP  Q4WF29              EXPRESSION TAG                 
SEQADV 6GUI SER A    2  UNP  Q4WF29              EXPRESSION TAG                 
SEQADV 6GUI ASN A  267  UNP  Q4WF29    HIS   267 ENGINEERED MUTATION            
SEQADV 6GUI GLY B    1  UNP  Q4WF29              EXPRESSION TAG                 
SEQADV 6GUI SER B    2  UNP  Q4WF29              EXPRESSION TAG                 
SEQADV 6GUI ASN B  267  UNP  Q4WF29    HIS   267 ENGINEERED MUTATION            
SEQRES   1 A  292  GLY SER ASP ARG PRO THR PRO VAL PRO LEU PRO ASN SER          
SEQRES   2 A  292  GLU GLN PHE TYR LEU GLU ASN ASP ARG GLY GLU PRO TYR          
SEQRES   3 A  292  LEU ILE GLN VAL SER TRP PRO LEU HIS TRP GLU ASP LYS          
SEQRES   4 A  292  GLN THR GLY ARG GLY PRO LEU PRO ILE ILE TYR ILE VAL          
SEQRES   5 A  292  ASP GLY ASN ALA LEU PHE LEU THR ALA THR GLU ALA ALA          
SEQRES   6 A  292  TRP ARG ARG ALA ALA ALA SER HIS PHE ALA GLY GLY GLY          
SEQRES   7 A  292  ILE ILE VAL ALA ILE GLY TYR PRO LEU LYS GLY LYS LEU          
SEQRES   8 A  292  TYR ASP ALA ARG ARG ARG SER PHE ASP LEU THR PRO PRO          
SEQRES   9 A  292  THR ALA CYS ALA PRO VAL GLY TYR GLY GLY ALA ASP VAL          
SEQRES  10 A  292  PHE LEU ASP PHE ILE GLU ASN SER VAL ARG PRO ALA VAL          
SEQRES  11 A  292  GLN ALA ARG PHE PRO GLN VAL SER LEU ALA ARG GLU ALA          
SEQRES  12 A  292  LEU TYR GLY HIS SER TYR GLY GLY LEU LEU ALA LEU HIS          
SEQRES  13 A  292  ALA LEU PHE THR ARG PRO GLN SER PHE ASP CYS TYR ILE          
SEQRES  14 A  292  ALA SER SER PRO SER ILE TRP TRP ASN SER LEU CYS ILE          
SEQRES  15 A  292  LEU HIS GLU ALA LYS ALA PHE VAL GLU THR LYS LYS VAL          
SEQRES  16 A  292  SER HIS ASP GLN SER PRO SER LEU MET VAL SER TRP GLY          
SEQRES  17 A  292  SER TRP GLU GLN HIS PRO PRO ARG TRP ALA ASP GLU LEU          
SEQRES  18 A  292  LEU ASP HIS TYR GLU ALA ARG LYS ARG THR ALA ALA GLU          
SEQRES  19 A  292  LEU ARG MET ALA ASP ASN ALA LEU ASP LEU CYS ALA MET          
SEQRES  20 A  292  LEU HIS GLY CYS SER ARG LEU HIS ALA LEU ILE LYS THR          
SEQRES  21 A  292  GLU TYR GLU GLY GLU ASP ASN THR SER VAL MET SER CYS          
SEQRES  22 A  292  SER VAL SER ARG GLY LEU THR MET PHE PHE GLU ASP TRP          
SEQRES  23 A  292  PRO PHE HIS GLN SER GLY                                      
SEQRES   1 B  292  GLY SER ASP ARG PRO THR PRO VAL PRO LEU PRO ASN SER          
SEQRES   2 B  292  GLU GLN PHE TYR LEU GLU ASN ASP ARG GLY GLU PRO TYR          
SEQRES   3 B  292  LEU ILE GLN VAL SER TRP PRO LEU HIS TRP GLU ASP LYS          
SEQRES   4 B  292  GLN THR GLY ARG GLY PRO LEU PRO ILE ILE TYR ILE VAL          
SEQRES   5 B  292  ASP GLY ASN ALA LEU PHE LEU THR ALA THR GLU ALA ALA          
SEQRES   6 B  292  TRP ARG ARG ALA ALA ALA SER HIS PHE ALA GLY GLY GLY          
SEQRES   7 B  292  ILE ILE VAL ALA ILE GLY TYR PRO LEU LYS GLY LYS LEU          
SEQRES   8 B  292  TYR ASP ALA ARG ARG ARG SER PHE ASP LEU THR PRO PRO          
SEQRES   9 B  292  THR ALA CYS ALA PRO VAL GLY TYR GLY GLY ALA ASP VAL          
SEQRES  10 B  292  PHE LEU ASP PHE ILE GLU ASN SER VAL ARG PRO ALA VAL          
SEQRES  11 B  292  GLN ALA ARG PHE PRO GLN VAL SER LEU ALA ARG GLU ALA          
SEQRES  12 B  292  LEU TYR GLY HIS SER TYR GLY GLY LEU LEU ALA LEU HIS          
SEQRES  13 B  292  ALA LEU PHE THR ARG PRO GLN SER PHE ASP CYS TYR ILE          
SEQRES  14 B  292  ALA SER SER PRO SER ILE TRP TRP ASN SER LEU CYS ILE          
SEQRES  15 B  292  LEU HIS GLU ALA LYS ALA PHE VAL GLU THR LYS LYS VAL          
SEQRES  16 B  292  SER HIS ASP GLN SER PRO SER LEU MET VAL SER TRP GLY          
SEQRES  17 B  292  SER TRP GLU GLN HIS PRO PRO ARG TRP ALA ASP GLU LEU          
SEQRES  18 B  292  LEU ASP HIS TYR GLU ALA ARG LYS ARG THR ALA ALA GLU          
SEQRES  19 B  292  LEU ARG MET ALA ASP ASN ALA LEU ASP LEU CYS ALA MET          
SEQRES  20 B  292  LEU HIS GLY CYS SER ARG LEU HIS ALA LEU ILE LYS THR          
SEQRES  21 B  292  GLU TYR GLU GLY GLU ASP ASN THR SER VAL MET SER CYS          
SEQRES  22 B  292  SER VAL SER ARG GLY LEU THR MET PHE PHE GLU ASP TRP          
SEQRES  23 B  292  PRO PHE HIS GLN SER GLY                                      
HET    GOL  A 301       6                                                       
HET    GOL  B 301       6                                                       
HET    GOL  B 302       6                                                       
HET    GOL  B 303       6                                                       
HET    GOL  B 304       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  GOL    5(C3 H8 O3)                                                  
FORMUL   8  HOH   *526(H2 O)                                                    
HELIX    1 AA1 ASP A   38  GLY A   42  5                                   5    
HELIX    2 AA2 ASP A   53  ARG A   68  1                                  16    
HELIX    3 AA3 ALA A   69  ALA A   71  5                                   3    
HELIX    4 AA4 ASP A   93  LEU A  101  1                                   9    
HELIX    5 AA5 GLY A  114  SER A  125  1                                  12    
HELIX    6 AA6 SER A  125  PHE A  134  1                                  10    
HELIX    7 AA7 SER A  148  ARG A  161  1                                  14    
HELIX    8 AA8 TRP A  176  CYS A  181  1                                   6    
HELIX    9 AA9 CYS A  181  THR A  192  1                                  12    
HELIX   10 AB1 LEU A  221  ARG A  236  1                                  16    
HELIX   11 AB2 ARG A  236  HIS A  249  1                                  14    
HELIX   12 AB3 SER A  269  ASP A  285  1                                  17    
HELIX   13 AB4 ASP B   38  GLY B   42  5                                   5    
HELIX   14 AB5 ASP B   53  ARG B   68  1                                  16    
HELIX   15 AB6 ALA B   69  ALA B   71  5                                   3    
HELIX   16 AB7 ASP B   93  LEU B  101  1                                   9    
HELIX   17 AB8 GLY B  114  SER B  125  1                                  12    
HELIX   18 AB9 SER B  125  PHE B  134  1                                  10    
HELIX   19 AC1 SER B  148  ARG B  161  1                                  14    
HELIX   20 AC2 PRO B  162  PHE B  165  5                                   4    
HELIX   21 AC3 SER B  174  TRP B  177  5                                   4    
HELIX   22 AC4 ASN B  178  THR B  192  1                                  15    
HELIX   23 AC5 LEU B  221  ARG B  236  1                                  16    
HELIX   24 AC6 ARG B  236  HIS B  249  1                                  14    
HELIX   25 AC7 SER B  269  ASP B  285  1                                  17    
SHEET    1 AA1 8 SER A  13  GLU A  19  0                                        
SHEET    2 AA1 8 PRO A  25  SER A  31 -1  O  ILE A  28   N  PHE A  16           
SHEET    3 AA1 8 ILE A  79  GLY A  84 -1  O  ALA A  82   N  GLN A  29           
SHEET    4 AA1 8 GLY A  44  VAL A  52  1  N  ILE A  51   O  ILE A  83           
SHEET    5 AA1 8 VAL A 137  HIS A 147  1  O  TYR A 145   N  TYR A  50           
SHEET    6 AA1 8 CYS A 167  SER A 171  1  O  ILE A 169   N  LEU A 144           
SHEET    7 AA1 8 SER A 202  GLY A 208  1  O  MET A 204   N  ALA A 170           
SHEET    8 AA1 8 ALA A 256  TYR A 262  1  O  ILE A 258   N  VAL A 205           
SHEET    1 AA2 8 SER B  13  GLU B  19  0                                        
SHEET    2 AA2 8 PRO B  25  SER B  31 -1  O  ILE B  28   N  PHE B  16           
SHEET    3 AA2 8 ILE B  79  GLY B  84 -1  O  GLY B  84   N  LEU B  27           
SHEET    4 AA2 8 GLY B  44  VAL B  52  1  N  ILE B  51   O  VAL B  81           
SHEET    5 AA2 8 VAL B 137  HIS B 147  1  O  ALA B 143   N  TYR B  50           
SHEET    6 AA2 8 CYS B 167  SER B 171  1  O  ILE B 169   N  LEU B 144           
SHEET    7 AA2 8 SER B 202  GLY B 208  1  O  MET B 204   N  ALA B 170           
SHEET    8 AA2 8 ALA B 256  TYR B 262  1  O  ILE B 258   N  VAL B 205           
CISPEP   1 TRP A  286    PRO A  287          0        -2.22                     
CISPEP   2 TRP B  286    PRO B  287          0        -3.35                     
SITE     1 AC1  7 ASN A  55  LEU A  87  LYS A  90  HOH A 403                    
SITE     2 AC1  7 HOH A 461  HOH A 469  PRO B  11                               
SITE     1 AC2  8 ALA B  75  ARG B 141  ASP B 223  PHE B 283                    
SITE     2 AC2  8 GLU B 284  ASP B 285  TRP B 286  HOH B 457                    
SITE     1 AC3  7 PRO A  11  ASN B  55  LYS B  90  HOH B 403                    
SITE     2 AC3  7 HOH B 416  HOH B 430  HOH B 459                               
SITE     1 AC4  7 ALA A  70  TYR B  92  ARG B  97  GOL B 304                    
SITE     2 AC4  7 HOH B 404  HOH B 510  HOH B 514                               
SITE     1 AC5  4 ARG B  97  SER B 148  TYR B 149  GOL B 303                    
CRYST1   54.970   92.610  130.900  90.00  90.00  90.00 P 21 21 21    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      0.018192  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010798  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007639        0.00000                         
TER    2251      SER A 291                                                      
TER    4497      SER B 291                                                      
MASTER      309    0    5   25   16    0    9    6 5034    2   30   46          
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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