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Database: PDB
Entry: 3AKH
LinkDB: 3AKH
Original site: 3AKH 
HEADER    HYDROLASE                               14-JUL-10   3AKH              
TITLE     CRYSTAL STRUCTURE OF EXO-1,5-ALPHA-L-ARABINOFURANOSIDASE COMPLEXED    
TITLE    2 WITH ALPHA-1,5-L-ARABINOFURANOTRIOSE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE SECRETED ALPHA L-ARABINOFURANOSIDASE II;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 28-481;                                       
COMPND   5 EC: 3.2.1.55;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES AVERMITILIS;                       
SOURCE   3 ORGANISM_TAXID: 227882;                                              
SOURCE   4 STRAIN: MA-4680;                                                     
SOURCE   5 GENE: ABFA, SAV1043, SAV_1043;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30                                     
KEYWDS    FIVE-BLADED BETA PROPELLER, BETA-TREFOIL, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.FUJIMOTO,H.ICHINOSE,S.KANEKO                                        
REVDAT   5   01-NOV-23 3AKH    1       HETSYN LINK                              
REVDAT   4   29-JUL-20 3AKH    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   11-OCT-17 3AKH    1       REMARK                                   
REVDAT   2   03-NOV-10 3AKH    1       JRNL                                     
REVDAT   1   25-AUG-10 3AKH    0                                                
JRNL        AUTH   Z.FUJIMOTO,H.ICHINOSE,T.MAEHARA,M.HONDA,M.KITAOKA,S.KANEKO   
JRNL        TITL   CRYSTAL STRUCTURE OF AN                                      
JRNL        TITL 2 EXO-1,5-{ALPHA}-L-ARABINOFURANOSIDASE FROM STREPTOMYCES      
JRNL        TITL 3 AVERMITILIS PROVIDES INSIGHTS INTO THE MECHANISM OF          
JRNL        TITL 4 SUBSTRATE DISCRIMINATION BETWEEN EXO- AND ENDO-TYPE ENZYMES  
JRNL        TITL 5 IN GLYCOSIDE HYDROLASE FAMILY 43.                            
JRNL        REF    J.BIOL.CHEM.                  V. 285 34134 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20739278                                                     
JRNL        DOI    10.1074/JBC.M110.164251                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Z.FUJIMOTO,H.ICHINOSE,S.KANEKO                               
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS OF 
REMARK   1  TITL 2 EXO-ALPHA-1,5-L-ARABINOFURANOSIDASE FROM STREPTOMYCES        
REMARK   1  TITL 3 AVERMITILIS NBRC14893.                                       
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.F      V.  64  1007 2008              
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   18997327                                                     
REMARK   1  DOI    10.1107/S1744309108029692                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   H.ICHINOSE,M.YOSHIDA,Z.FUJIMOTO,S.KANEKO                     
REMARK   1  TITL   CHARACTERIZATION OF A MODULAR ENZYME OF                      
REMARK   1  TITL 2 EXO-1,5-ALPHA-L-ARABINOFURANOSIDASE AND ARABINAN BINDING     
REMARK   1  TITL 3 MODULE FROM STREPTOMYCES AVERMITILIS NBRC14893.              
REMARK   1  REF    APPL.MICROBIOL.BIOTECHNOL.    V.  80   399 2008              
REMARK   1  REFN                   ISSN 0175-7598                               
REMARK   1  PMID   18665359                                                     
REMARK   1  DOI    10.1007/S00253-008-1551-X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.47                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53483                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2877                            
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) : 3815                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 230                          
REMARK   3   BIN FREE R VALUE                    : 0.2940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3518                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 578                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.05000                                             
REMARK   3    B22 (A**2) : 0.22000                                              
REMARK   3    B33 (A**2) : -0.17000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.107         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.109         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3701 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5054 ; 1.244 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   446 ; 5.878 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;28.278 ;23.276       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   529 ;11.879 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;15.570 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   554 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2853 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2225 ; 0.657 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3583 ; 1.189 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1476 ; 1.727 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1471 ; 2.774 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3AKH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000029363.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 7.0                                
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) : 0.97000                            
REMARK 200  MONOCHROMATOR                  : NUMERICAL LINK TYPE SI(111)        
REMARK 200                                   DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56484                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.470                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 14.60                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : 0.05500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 53.7000                            
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) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.25700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 9.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3AKF                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM CITRATE, 0.2M SODIUM         
REMARK 280  CHLORIDE, 0.1M TRIS, PH 7.0, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  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       20.61850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.98100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.67050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.98100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.61850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.67050            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     VAL A     8                                                      
REMARK 465     LEU A   456                                                      
REMARK 465     ALA A   457                                                      
REMARK 465     ALA A   458                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     LEU A   460                                                      
REMARK 465     GLU A   461                                                      
REMARK 465     HIS A   462                                                      
REMARK 465     HIS A   463                                                      
REMARK 465     HIS A   464                                                      
REMARK 465     HIS A   465                                                      
REMARK 465     HIS A   466                                                      
REMARK 465     HIS A   467                                                      
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    ASN A 159      -63.26    -95.44                                   
REMARK 500    SER A 214     -179.19     62.61                                   
REMARK 500    THR A 216       31.84    -80.95                                   
REMARK 500    ASP A 217     -153.13   -104.34                                   
REMARK 500    HIS A 260       70.83     37.67                                   
REMARK 500    ASN A 433      -12.95     73.36                                   
REMARK 500    SER A 441      -30.17   -134.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 502  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  79   OE2                                                    
REMARK 620 2 HOH A 682   O    96.6                                              
REMARK 620 3 HOH A 690   O    96.0  95.0                                        
REMARK 620 4 HOH A 779   O   126.5  81.6 137.5                                  
REMARK 620 5 HOH A 827   O    85.0 173.1  91.5  92.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3AKF   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITHOUT LIGAND                                      
REMARK 900 RELATED ID: 3AKG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3AKI   RELATED DB: PDB                                   
DBREF  3AKH A    1   454  UNP    Q82P90   Q82P90_STRAW    28    481             
SEQADV 3AKH MET A    0  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH LYS A  455  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH LEU A  456  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH ALA A  457  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH ALA A  458  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH ALA A  459  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH LEU A  460  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH GLU A  461  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  462  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  463  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  464  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  465  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  466  UNP  Q82P90              EXPRESSION TAG                 
SEQADV 3AKH HIS A  467  UNP  Q82P90              EXPRESSION TAG                 
SEQRES   1 A  468  MET THR ALA PRO ALA SER PRO SER VAL THR PHE THR ASN          
SEQRES   2 A  468  PRO LEU ALA GLU LYS ARG ALA ASP PRO HIS ILE PHE LYS          
SEQRES   3 A  468  HIS THR ASP GLY TYR TYR TYR PHE THR ALA THR VAL PRO          
SEQRES   4 A  468  GLU TYR ASP ARG ILE VAL LEU ARG ARG ALA THR THR LEU          
SEQRES   5 A  468  GLN GLY LEU ALA THR ALA PRO GLU THR THR ILE TRP THR          
SEQRES   6 A  468  LYS HIS ALA SER GLY VAL MET GLY ALA HIS ILE TRP ALA          
SEQRES   7 A  468  PRO GLU ILE HIS PHE ILE ASP GLY LYS TRP TYR VAL TYR          
SEQRES   8 A  468  PHE ALA ALA GLY SER THR SER ASP VAL TRP ALA ILE ARG          
SEQRES   9 A  468  MET TYR VAL LEU GLU SER GLY ALA ALA ASN PRO LEU THR          
SEQRES  10 A  468  GLY SER TRP THR GLU LYS GLY GLN ILE ALA THR PRO VAL          
SEQRES  11 A  468  SER SER PHE SER LEU ASP ALA THR THR PHE VAL VAL ASN          
SEQRES  12 A  468  GLY VAL ARG HIS LEU ALA TRP ALA GLN ARG ASN PRO ALA          
SEQRES  13 A  468  GLU ASP ASN ASN THR SER LEU PHE ILE ALA LYS MET ALA          
SEQRES  14 A  468  ASN PRO TRP THR ILE SER GLY THR PRO THR GLU ILE SER          
SEQRES  15 A  468  GLN PRO THR LEU SER TRP GLU THR VAL GLY TYR LYS VAL          
SEQRES  16 A  468  ASN GLU GLY PRO ALA VAL ILE GLN HIS GLY GLY LYS VAL          
SEQRES  17 A  468  PHE LEU THR TYR SER ALA SER ALA THR ASP ALA ASN TYR          
SEQRES  18 A  468  CYS LEU GLY MET LEU SER ALA SER ALA SER ALA ASP LEU          
SEQRES  19 A  468  LEU ASN ALA ALA SER TRP THR LYS SER SER GLN PRO VAL          
SEQRES  20 A  468  PHE LYS THR SER GLU ALA THR GLY GLN TYR GLY PRO GLY          
SEQRES  21 A  468  HIS ASN SER PHE THR VAL SER GLU ASP GLY LYS SER ASP          
SEQRES  22 A  468  ILE LEU VAL TYR HIS ASP ARG ASN TYR LYS ASP ILE SER          
SEQRES  23 A  468  GLY ASP PRO LEU ASN ASP PRO ASN ARG ARG THR ARG LEU          
SEQRES  24 A  468  GLN LYS VAL TYR TRP ASN ALA ASP GLY THR PRO ASN PHE          
SEQRES  25 A  468  GLY ILE PRO VAL ALA ASP GLY VAL THR PRO VAL ARG PHE          
SEQRES  26 A  468  SER SER TYR ASN TYR PRO ASP ARG TYR ILE ARG HIS TRP          
SEQRES  27 A  468  ASP PHE ARG ALA ARG ILE GLU ALA ASN VAL THR ASN LEU          
SEQRES  28 A  468  ALA ASP SER GLN PHE ARG VAL VAL THR GLY LEU ALA GLY          
SEQRES  29 A  468  SER GLY THR ILE SER LEU GLU SER ALA ASN TYR PRO GLY          
SEQRES  30 A  468  TYR TYR LEU ARG HIS LYS ASN TYR GLU VAL TRP VAL GLU          
SEQRES  31 A  468  LYS ASN ASP GLY SER SER ALA PHE LYS ASN ASP ALA SER          
SEQRES  32 A  468  PHE SER ARG ARG ALA GLY LEU ALA ASP SER ALA ASP GLY          
SEQRES  33 A  468  ILE ALA PHE GLU SER TYR ASN TYR PRO GLY ARG TYR LEU          
SEQRES  34 A  468  ARG HIS TYR GLU ASN LEU LEU ARG ILE GLN PRO VAL SER          
SEQRES  35 A  468  THR ALA LEU ASP ARG GLN ASP ALA THR PHE TYR ALA GLU          
SEQRES  36 A  468  LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS          
HET    AHR  B   1      10                                                       
HET    AHR  B   2       9                                                       
HET    AHR  C   1      10                                                       
HET    AHR  C   2       9                                                       
HET    AHR  D   1      10                                                       
HET    AHR  D   2       9                                                       
HET     CL  A 501       1                                                       
HET     NA  A 502       1                                                       
HET    AHR  A 541      10                                                       
HET    GOL  A 597       6                                                       
HET    GOL  A 599       6                                                       
HETNAM     AHR ALPHA-L-ARABINOFURANOSE                                          
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     AHR ALPHA-L-ARABINOSE; L-ARABINOSE; ARABINOSE                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  AHR    7(C5 H10 O5)                                                 
FORMUL   5   CL    CL 1-                                                        
FORMUL   6   NA    NA 1+                                                        
FORMUL   8  GOL    2(C3 H8 O3)                                                  
FORMUL  10  HOH   *578(H2 O)                                                    
HELIX    1   1 LEU A   51  ALA A   57  5                                   7    
HELIX    2   2 LEU A  185  THR A  189  5                                   5    
HELIX    3   3 ASN A  235  TRP A  239  5                                   5    
HELIX    4   4 ASP A  287  ASP A  291  5                                   5    
HELIX    5   5 ASN A  349  SER A  353  5                                   5    
HELIX    6   6 SER A  394  ALA A  401  1                                   8    
HELIX    7   7 THR A  442  ALA A  449  1                                   8    
SHEET    1   A 2 THR A  11  ASN A  12  0                                        
SHEET    2   A 2 GLY A 318  VAL A 319 -1  O  GLY A 318   N  ASN A  12           
SHEET    1   B 4 ALA A  19  LYS A  25  0                                        
SHEET    2   B 4 TYR A  31  THR A  36 -1  O  THR A  36   N  ALA A  19           
SHEET    3   B 4 ARG A  42  ALA A  48 -1  O  ALA A  48   N  TYR A  31           
SHEET    4   B 4 THR A  60  THR A  64 -1  O  THR A  60   N  LEU A  45           
SHEET    1   C 4 ALA A  73  ILE A  83  0                                        
SHEET    2   C 4 LYS A  86  GLY A  94 -1  O  LYS A  86   N  ILE A  83           
SHEET    3   C 4 ARG A 103  SER A 109 -1  O  SER A 109   N  TRP A  87           
SHEET    4   C 4 THR A 120  GLN A 124 -1  O  LYS A 122   N  VAL A 106           
SHEET    1   D 4 SER A 133  VAL A 141  0                                        
SHEET    2   D 4 VAL A 144  GLN A 151 -1  O  HIS A 146   N  PHE A 139           
SHEET    3   D 4 SER A 161  ASN A 169 -1  O  PHE A 163   N  TRP A 149           
SHEET    4   D 4 THR A 172  SER A 181 -1  O  ILE A 180   N  LEU A 162           
SHEET    1   E 4 ASN A 195  HIS A 203  0                                        
SHEET    2   E 4 LYS A 206  ALA A 213 -1  O  PHE A 208   N  ILE A 201           
SHEET    3   E 4 CYS A 221  SER A 228 -1  O  ALA A 227   N  VAL A 207           
SHEET    4   E 4 THR A 240  LYS A 241 -1  O  THR A 240   N  SER A 226           
SHEET    1   F 3 TYR A 256  VAL A 265  0                                        
SHEET    2   F 3 ASP A 272  ARG A 279 -1  O  ARG A 279   N  TYR A 256           
SHEET    3   F 3 ARG A 295  LYS A 300 -1  O  ARG A 297   N  TYR A 276           
SHEET    1   G 2 TYR A 302  TRP A 303  0                                        
SHEET    2   G 2 PRO A 309  ASN A 310 -1  O  ASN A 310   N  TYR A 302           
SHEET    1   H 2 PHE A 324  SER A 326  0                                        
SHEET    2   H 2 PHE A 451  ALA A 453 -1  O  TYR A 452   N  SER A 325           
SHEET    1   I 2 TYR A 333  TRP A 337  0                                        
SHEET    2   I 2 ARG A 340  GLU A 344 -1  O  GLU A 344   N  TYR A 333           
SHEET    1   J 2 PHE A 355  THR A 359  0                                        
SHEET    2   J 2 ILE A 367  SER A 371 -1  O  GLU A 370   N  ARG A 356           
SHEET    1   K 2 TYR A 377  LYS A 382  0                                        
SHEET    2   K 2 GLU A 385  LYS A 390 -1  O  TRP A 387   N  ARG A 380           
SHEET    1   L 2 PHE A 403  ALA A 407  0                                        
SHEET    2   L 2 ILE A 416  SER A 420 -1  O  GLU A 419   N  SER A 404           
SHEET    1   M 2 ARG A 426  TYR A 431  0                                        
SHEET    2   M 2 LEU A 434  PRO A 439 -1  O  GLN A 438   N  TYR A 427           
LINK         O5  AHR B   1                 C1  AHR B   2     1555   1555  1.45  
LINK         O5  AHR C   1                 C1  AHR C   2     1555   1555  1.42  
LINK         O5  AHR D   1                 C1  AHR D   2     1555   1555  1.45  
LINK         OE2 GLU A  79                NA    NA A 502     1555   1555  2.21  
LINK        NA    NA A 502                 O   HOH A 682     1555   1555  2.29  
LINK        NA    NA A 502                 O   HOH A 690     1555   1555  2.19  
LINK        NA    NA A 502                 O   HOH A 779     1555   1555  2.44  
LINK        NA    NA A 502                 O   HOH A 827     1555   1555  2.27  
CISPEP   1 ASN A   12    PRO A   13          0         4.18                     
CRYST1   41.237   91.341  135.962  90.00  90.00  90.00 P 21 21 21    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      0.024250  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010948  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007355        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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