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Database: PDB
Entry: 4JKK
LinkDB: 4JKK
Original site: 4JKK 
HEADER    HYDROLASE                               09-MAR-13   4JKK              
TITLE     CRYSTAL STRUCTURE OF STREPTOCOCCUS AGALACTIAE BETA-GLUCURONIDASE IN   
TITLE    2 SPACE GROUP I222                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-GLUCURONIDASE;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.31;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS AGALACTIAE;                       
SOURCE   3 ORGANISM_TAXID: 208435;                                              
SOURCE   4 STRAIN: ATCC BAA-611 / 2603 V/R;                                     
SOURCE   5 GENE: SAG0698;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-AI (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    ALPHA/BETA BARREL, BETA-SANDWICH, SUGAR-BINDING DOMAIN, GLYCOSYL      
KEYWDS   2 HYDROLASE, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.D.WALLACE,M.R.REDINBO                                               
REVDAT   3   28-FEB-24 4JKK    1       REMARK SEQADV                            
REVDAT   2   21-OCT-15 4JKK    1       JRNL                                     
REVDAT   1   17-SEP-14 4JKK    0                                                
JRNL        AUTH   B.D.WALLACE,A.B.ROBERTS,R.M.POLLET,J.D.INGLE,K.A.BIERNAT,    
JRNL        AUTH 2 S.J.PELLOCK,M.K.VENKATESH,L.GUTHRIE,S.K.O'NEAL,S.J.ROBINSON, 
JRNL        AUTH 3 M.DOLLINGER,E.FIGUEROA,S.R.MCSHANE,R.D.COHEN,J.JIN,S.V.FRYE, 
JRNL        AUTH 4 W.C.ZAMBONI,C.PEPE-RANNEY,S.MANI,L.KELLY,M.R.REDINBO         
JRNL        TITL   STRUCTURE AND INHIBITION OF MICROBIOME BETA-GLUCURONIDASES   
JRNL        TITL 2 ESSENTIAL TO THE ALLEVIATION OF CANCER DRUG TOXICITY.        
JRNL        REF    CHEM.BIOL.                    V.  22  1238 2015              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   26364932                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2015.08.005                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18110                          
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) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 938                             
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) : 2.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1099                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1640                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.2680                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4780                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 295                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.24000                                             
REMARK   3    B22 (A**2) : 0.84000                                              
REMARK   3    B33 (A**2) : -0.60000                                             
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): 0.311         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.208         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.616         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4950 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6725 ; 1.436 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   600 ; 6.360 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   260 ;37.319 ;24.846       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   855 ;17.994 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.167 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   727 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3828 ; 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):  2952 ; 0.926 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4799 ; 1.820 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1998 ; 2.731 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1919 ; 4.531 ; 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 : BABINET MODEL WITH 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: U VALUES : REFINED INDIVIDUALLY           
REMARK   4                                                                      
REMARK   4 4JKK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078162.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-11                          
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               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL WITH K-B BIOMORPH   
REMARK 200                                   MIRRORS                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18183                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-28% PEG 3350, 0.1-0.3 M KSCN, 0.02%   
REMARK 280  SODIUM AZIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289.15K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       34.40700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.91450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       99.66600            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.40700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.91450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       99.66600            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.40700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       41.91450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       99.66600            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.40700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       41.91450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       99.66600            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 78440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 601  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 985  LIES ON A SPECIAL POSITION.                          
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     SER A    -2                                                      
REMARK 465     PHE A   360                                                      
REMARK 465     ASN A   361                                                      
REMARK 465     ALA A   362                                                      
REMARK 465     SER A   363                                                      
REMARK 465     LEU A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     LEU A   366                                                      
REMARK 465     SER A   367                                                      
REMARK 465     PRO A   368                                                      
REMARK 465     LYS A   369                                                      
REMARK 465     SER A   597                                                      
REMARK 465     VAL A   598                                                      
REMARK 465     LYS A   599                                                      
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     LYS A  70    CG   CD   CE   NZ                                   
REMARK 470     GLU A  73    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 189    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 208    CG   CD   CE   NZ                                   
REMARK 470     GLU A 211    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 213    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 257    CG   OD1  OD2                                       
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   CG   GLU A    36     O    HOH A   957              1.77            
REMARK 500   OE1  GLU A   552     O    HOH A   981              1.95            
REMARK 500   NZ   LYS A   425     O    HOH A   960              2.03            
REMARK 500   NE2  GLN A   358     O    HOH A   908              2.07            
REMARK 500   O    HOH A   944     O    HOH A   957              2.10            
REMARK 500   O    HOH A   864     O    HOH A   865              2.19            
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    THR A  42      154.08    174.20                                   
REMARK 500    SER A  83      155.64    172.59                                   
REMARK 500    GLU A 147       -4.28     71.16                                   
REMARK 500    ASN A 158       34.72    -96.64                                   
REMARK 500    ASP A 160       48.82   -100.92                                   
REMARK 500    SER A 230       -6.79     79.67                                   
REMARK 500    LEU A 243       13.97     54.85                                   
REMARK 500    ASP A 262      143.71   -171.17                                   
REMARK 500    ILE A 300      -66.88     72.65                                   
REMARK 500    HIS A 329       54.68   -118.98                                   
REMARK 500    PRO A 352       40.46    -77.12                                   
REMARK 500    ASN A 371     -157.16   -179.85                                   
REMARK 500    GLN A 378       48.03    -91.68                                   
REMARK 500    TRP A 467      -58.67   -121.18                                   
REMARK 500    TYR A 518      -22.07     93.96                                   
REMARK 500    LYS A 595       25.59    124.52                                   
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 MG A 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JKL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4JKM   RELATED DB: PDB                                   
DBREF  4JKK A    1   599  UNP    Q8E0N2   Q8E0N2_STRA5     1    599             
SEQADV 4JKK SER A   -2  UNP  Q8E0N2              EXPRESSION TAG                 
SEQADV 4JKK ASN A   -1  UNP  Q8E0N2              EXPRESSION TAG                 
SEQADV 4JKK ALA A    0  UNP  Q8E0N2              EXPRESSION TAG                 
SEQRES   1 A  602  SER ASN ALA MET LEU TYR PRO LEU LEU THR LYS THR ARG          
SEQRES   2 A  602  ASN THR TYR ASP LEU GLY GLY ILE TRP ASN PHE LYS LEU          
SEQRES   3 A  602  GLY GLU HIS ASN PRO ASN GLU LEU LEU PRO SER ASP GLU          
SEQRES   4 A  602  VAL MET VAL ILE PRO THR SER PHE ASN ASP LEU MET VAL          
SEQRES   5 A  602  SER LYS GLU LYS ARG ASP TYR ILE GLY ASP PHE TRP TYR          
SEQRES   6 A  602  GLU LYS VAL ILE GLU VAL PRO LYS VAL SER GLU ASP GLU          
SEQRES   7 A  602  GLU MET VAL LEU ARG PHE GLY SER VAL THR HIS GLN ALA          
SEQRES   8 A  602  LYS ILE TYR VAL ASP GLY VAL LEU VAL GLY GLU HIS LYS          
SEQRES   9 A  602  GLY GLY PHE THR PRO PHE GLU VAL LEU VAL PRO GLU CYS          
SEQRES  10 A  602  LYS TYR ASN ASN GLU LYS ILE LYS VAL SER ILE CYS ALA          
SEQRES  11 A  602  ASN ASN VAL LEU ASP TYR THR THR LEU PRO VAL GLY ASN          
SEQRES  12 A  602  TYR SER GLU ILE ILE GLN GLU ASP GLY SER ILE LYS LYS          
SEQRES  13 A  602  LYS VAL ARG GLU ASN PHE ASP PHE PHE ASN TYR ALA GLY          
SEQRES  14 A  602  VAL HIS ARG PRO LEU LYS LEU MET ILE ARG PRO LYS ASN          
SEQRES  15 A  602  HIS ILE PHE ASP ILE THR ILE THR SER ARG LEU SER ASP          
SEQRES  16 A  602  ASP LEU GLN SER ALA ASP LEU HIS PHE LEU VAL GLU THR          
SEQRES  17 A  602  ASN GLN LYS VAL ASP GLU VAL ARG ILE SER VAL PHE ASP          
SEQRES  18 A  602  GLU ASP ASN LYS LEU VAL GLY GLU THR LYS ASP SER ARG          
SEQRES  19 A  602  LEU PHE LEU SER ASP VAL HIS LEU TRP GLU VAL LEU ASN          
SEQRES  20 A  602  ALA TYR LEU TYR THR ALA ARG VAL GLU ILE PHE VAL ASP          
SEQRES  21 A  602  ASN GLN LEU GLN ASP VAL TYR GLU GLU ASN PHE GLY LEU          
SEQRES  22 A  602  ARG GLU ILE GLU VAL THR ASN GLY GLN PHE LEU LEU ASN          
SEQRES  23 A  602  ARG LYS PRO ILE TYR PHE LYS GLY PHE GLY LYS HIS GLU          
SEQRES  24 A  602  ASP THR PHE ILE ASN GLY ARG GLY LEU ASN GLU ALA ALA          
SEQRES  25 A  602  ASN LEU MET ASP LEU ASN LEU LEU LYS ASP MET GLY ALA          
SEQRES  26 A  602  ASN SER PHE ARG THR SER HIS TYR PRO TYR SER GLU GLU          
SEQRES  27 A  602  MET MET ARG LEU ALA ASP ARG MET GLY VAL LEU VAL ILE          
SEQRES  28 A  602  ASP GLU VAL PRO ALA VAL GLY LEU PHE GLN ASN PHE ASN          
SEQRES  29 A  602  ALA SER LEU ASP LEU SER PRO LYS ASP ASN GLY THR TRP          
SEQRES  30 A  602  ASN LEU MET GLN THR LYS ALA ALA HIS GLU GLN ALA ILE          
SEQRES  31 A  602  GLN GLU LEU VAL LYS ARG ASP LYS ASN HIS PRO SER VAL          
SEQRES  32 A  602  VAL MET TRP VAL VAL ALA ASN GLU PRO ALA SER HIS GLU          
SEQRES  33 A  602  ALA GLY ALA HIS ASP TYR PHE GLU PRO LEU VAL LYS LEU          
SEQRES  34 A  602  TYR LYS ASP LEU ASP PRO GLN LYS ARG PRO VAL THR LEU          
SEQRES  35 A  602  VAL ASN ILE LEU MET ALA THR PRO ASP ARG ASP GLN VAL          
SEQRES  36 A  602  MET ASP LEU VAL ASP VAL VAL CYS LEU ASN ARG TYR TYR          
SEQRES  37 A  602  GLY TRP TYR VAL ASP HIS GLY ASP LEU THR ASN ALA GLU          
SEQRES  38 A  602  VAL GLY ILE ARG LYS GLU LEU LEU GLU TRP GLN ASP LYS          
SEQRES  39 A  602  PHE PRO ASP LYS PRO ILE ILE ILE THR GLU TYR GLY ALA          
SEQRES  40 A  602  ASP THR LEU PRO GLY LEU HIS SER THR TRP ASN ILE PRO          
SEQRES  41 A  602  TYR THR GLU GLU PHE GLN CYS ASP PHE TYR GLU MET SER          
SEQRES  42 A  602  HIS ARG VAL PHE ASP GLY ILE PRO ASN LEU VAL GLY GLU          
SEQRES  43 A  602  GLN VAL TRP ASN PHE ALA ASP PHE GLU THR ASN LEU MET          
SEQRES  44 A  602  ILE LEU ARG VAL GLN GLY ASN HIS LYS GLY LEU PHE SER          
SEQRES  45 A  602  ARG ASN ARG GLN PRO LYS GLN VAL VAL LYS GLU PHE LYS          
SEQRES  46 A  602  LYS ARG TRP MET THR ILE PRO HIS TYR HIS ASN LYS LYS          
SEQRES  47 A  602  ASN SER VAL LYS                                              
HET     MG  A 601       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  HOH   *295(H2 O)                                                    
HELIX    1   1 ASN A   45  MET A   48  5                                   4    
HELIX    2   2 SER A   50  ASP A   55  1                                   6    
HELIX    3   3 PRO A  112  TYR A  116  5                                   5    
HELIX    4   4 ASN A  306  MET A  320  1                                  15    
HELIX    5   5 SER A  333  GLY A  344  1                                  12    
HELIX    6   6 THR A  379  LYS A  395  1                                  17    
HELIX    7   7 GLY A  415  ASP A  431  1                                  17    
HELIX    8   8 VAL A  452  VAL A  456  5                                   5    
HELIX    9   9 ASP A  473  PHE A  492  1                                  20    
HELIX   10  10 THR A  519  ASP A  535  1                                  17    
HELIX   11  11 GLN A  576  MET A  586  1                                  11    
SHEET    1   A 4 ASN A  11  ASP A  14  0                                        
SHEET    2   A 4 LEU A 171  PRO A 177 -1  O  LEU A 173   N  TYR A  13           
SHEET    3   A 4 GLU A  75  PHE A  81 -1  N  VAL A  78   O  MET A 174           
SHEET    4   A 4 PHE A 107  LEU A 110 -1  O  VAL A 109   N  LEU A  79           
SHEET    1   B 6 VAL A  37  ILE A  40  0                                        
SHEET    2   B 6 GLY A  17  LEU A  23 -1  N  TRP A  19   O  MET A  38           
SHEET    3   B 6 ASP A  59  GLU A  67 -1  O  TRP A  61   N  LYS A  22           
SHEET    4   B 6 LYS A 120  ASN A 128 -1  O  ILE A 121   N  ILE A  66           
SHEET    5   B 6 GLN A  87  VAL A  92 -1  N  TYR A  91   O  SER A 124           
SHEET    6   B 6 VAL A  95  LYS A 101 -1  O  VAL A  97   N  ILE A  90           
SHEET    1   C 2 THR A  42  SER A  43  0                                        
SHEET    2   C 2 GLY A 166  VAL A 167 -1  O  VAL A 167   N  THR A  42           
SHEET    1   D 2 GLY A 139  ILE A 145  0                                        
SHEET    2   D 2 ILE A 151  GLU A 157 -1  O  LYS A 152   N  ILE A 144           
SHEET    1   E 3 ILE A 181  LEU A 190  0                                        
SHEET    2   E 3 ALA A 197  THR A 205 -1  O  GLU A 204   N  ASP A 183           
SHEET    3   E 3 ARG A 231  LEU A 234 -1  O  LEU A 232   N  LEU A 199           
SHEET    1   F 4 LEU A 223  THR A 227  0                                        
SHEET    2   F 4 GLU A 211  PHE A 217 -1  N  ILE A 214   O  THR A 227           
SHEET    3   F 4 TYR A 248  PHE A 255 -1  O  ARG A 251   N  SER A 215           
SHEET    4   F 4 LEU A 260  PHE A 268 -1  O  GLU A 266   N  ALA A 250           
SHEET    1   G 3 ILE A 273  THR A 276  0                                        
SHEET    2   G 3 GLN A 279  LEU A 282 -1  O  LEU A 281   N  GLU A 274           
SHEET    3   G 3 LYS A 285  PRO A 286 -1  O  LYS A 285   N  LEU A 282           
SHEET    1   H 9 PHE A 289  GLY A 293  0                                        
SHEET    2   H 9 SER A 324  ARG A 326  1  N  SER A 324   O  LYS A 290           
SHEET    3   H 9 LEU A 346  GLU A 350  1  O  ILE A 348   N  PHE A 325           
SHEET    4   H 9 VAL A 400  ASN A 407  1  O  MET A 402   N  ASP A 349           
SHEET    5   H 9 VAL A 437  ASN A 441  1  O  THR A 438   N  TRP A 403           
SHEET    6   H 9 VAL A 458  ASN A 462  1  O  ASN A 462   N  ASN A 441           
SHEET    7   H 9 ILE A 497  GLU A 501  1  O  ILE A 498   N  VAL A 459           
SHEET    8   H 9 LEU A 540  VAL A 545  1  O  GLN A 544   N  ILE A 499           
SHEET    9   H 9 PHE A 289  GLY A 293  1  N  GLY A 293   O  VAL A 545           
CISPEP   1 ILE A   40    PRO A   41          0        -3.57                     
CISPEP   2 THR A   85    HIS A   86          0         2.62                     
CISPEP   3 LEU A  136    PRO A  137          0         3.11                     
CISPEP   4 ASP A  148    GLY A  149          0        -3.06                     
CISPEP   5 SER A  328    HIS A  329          0        -6.90                     
CISPEP   6 ASP A  370    ASN A  371          0         9.27                     
CISPEP   7 TRP A  546    ASN A  547          0         5.00                     
CISPEP   8 LYS A  595    ASN A  596          0         8.82                     
SITE     1 AC1  2 GLY A 372  TRP A 374                                          
CRYST1   68.814   83.829  199.332  90.00  90.00  90.00 I 2 2 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      0.014532  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011929  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005017        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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