GenomeNet

Database: PDB
Entry: 4C7V
LinkDB: 4C7V
Original site: 4C7V 
HEADER    TRANSFERASE                             26-SEP-13   4C7V              
TITLE     APO TRANSKETOLASE FROM LACTOBACILLUS SALIVARIUS AT 2.2A RESOLUTION    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSKETOLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.2.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOBACILLUS SALIVARIUS;                       
SOURCE   3 ORGANISM_TAXID: 362948;                                              
SOURCE   4 STRAIN: UCC118;                                                      
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: ROSETTA PLYSS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: POPINF                                     
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.C.LOBLEY,P.LUKACIK,M.BUMANN,P.ALLER,A.DOUANGAMATH,P.W.O'TOOLE,    
AUTHOR   2 M.A.WALSH                                                            
REVDAT   3   21-OCT-15 4C7V    1       JRNL                                     
REVDAT   2   14-OCT-15 4C7V    1       TITLE  JRNL                              
REVDAT   1   08-OCT-14 4C7V    0                                                
JRNL        AUTH   P.LUKACIK,C.M.C.LOBLEY,M.BUMANN,V.ARENA DE SOUZA,R.J.OWENS,  
JRNL        AUTH 2 P.W.O'TOOLE,M.A.WALSH                                        
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURES OF LACTOBACILLUS          
JRNL        TITL 2 SALIVARIUS TRANSKETOLASE IN THE PRESENCE AND ABSENCE OF      
JRNL        TITL 3 THIAMINE PYROPHOSPHATE                                       
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  71  1327 2015              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   26457526                                                     
JRNL        DOI    10.1107/S2053230X1501657X                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.57                          
REMARK   3   NUMBER OF REFLECTIONS             : 32219                          
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) : 0.16524                         
REMARK   3   R VALUE            (WORKING SET) : 0.16236                         
REMARK   3   FREE R VALUE                     : 0.21917                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1720                            
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) : 2.200                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.257                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2360                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.238                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.273                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5117                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 246                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.117                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25                                                
REMARK   3    B22 (A**2) : -0.25                                                
REMARK   3    B33 (A**2) : 0.80                                                 
REMARK   3    B12 (A**2) : -0.25                                                
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.257         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.200         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.233        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
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):  5234 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4929 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7097 ; 1.780 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11390 ; 0.873 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   671 ; 6.509 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   234 ;36.725 ;25.128       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   884 ;15.831 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.150 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   772 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6007 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1157 ; 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):  2657 ; 2.539 ; 3.099       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2656 ; 2.537 ; 3.098       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3322 ; 3.499 ; 4.637       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2577 ; 3.220 ; 3.443       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   188                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.7510  54.4680 -10.4400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0254 T22:   0.1289                                     
REMARK   3      T33:   0.1719 T12:   0.0139                                     
REMARK   3      T13:  -0.0451 T23:  -0.0269                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7794 L22:   0.2795                                     
REMARK   3      L33:   0.4693 L12:  -0.0642                                     
REMARK   3      L13:   0.1382 L23:   0.0394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0014 S12:   0.0843 S13:  -0.2610                       
REMARK   3      S21:  -0.0773 S22:   0.0078 S23:   0.1702                       
REMARK   3      S31:  -0.0469 S32:  -0.2087 S33:  -0.0092                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   189        A   337                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9600  49.2120 -11.7830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0231 T22:   0.1424                                     
REMARK   3      T33:   0.2210 T12:  -0.0290                                     
REMARK   3      T13:  -0.0441 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6318 L22:   0.5618                                     
REMARK   3      L33:   0.5778 L12:  -0.1816                                     
REMARK   3      L13:   0.3180 L23:  -0.0793                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0264 S12:   0.0482 S13:  -0.2749                       
REMARK   3      S21:  -0.0624 S22:   0.0180 S23:   0.1810                       
REMARK   3      S31:   0.0446 S32:  -0.2080 S33:  -0.0445                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   338        A   528                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9320  62.2850  14.1250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0513 T22:   0.0845                                     
REMARK   3      T33:   0.0467 T12:   0.0394                                     
REMARK   3      T13:   0.0125 T23:   0.0363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4907 L22:   0.3302                                     
REMARK   3      L33:   0.9637 L12:  -0.0600                                     
REMARK   3      L13:  -0.0435 L23:   0.0116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0550 S12:  -0.1516 S13:  -0.1176                       
REMARK   3      S21:   0.0269 S22:   0.0588 S23:   0.0786                       
REMARK   3      S31:  -0.1625 S32:  -0.0666 S33:  -0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   529        A   637                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.2770  79.8550  13.5350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2236 T22:   0.0747                                     
REMARK   3      T33:   0.0340 T12:  -0.0741                                     
REMARK   3      T13:  -0.0223 T23:  -0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0997 L22:   1.0314                                     
REMARK   3      L33:   1.0204 L12:  -0.0080                                     
REMARK   3      L13:  -0.0429 L23:   0.2977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0467 S12:  -0.1546 S13:   0.1687                       
REMARK   3      S21:   0.0075 S22:   0.0779 S23:  -0.0585                       
REMARK   3      S31:  -0.3695 S32:   0.1622 S33:  -0.0312                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   638        A   661                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3300  67.8120  19.4190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1718 T22:   0.2875                                     
REMARK   3      T33:   0.0809 T12:  -0.0590                                     
REMARK   3      T13:  -0.0649 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3010 L22:   5.1223                                     
REMARK   3      L33:   0.1911 L12:   0.0278                                     
REMARK   3      L13:  -0.3262 L23:  -0.6004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0879 S12:  -0.2830 S13:   0.0021                       
REMARK   3      S21:   0.1590 S22:   0.0619 S23:  -0.2573                       
REMARK   3      S31:  -0.0334 S32:   0.1585 S33:   0.0261                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4C7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-58494.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-12                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.917                              
REMARK 200  MONOCHROMATOR                  : DCM SI(111)                        
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 2M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33992                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.14                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.6                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.8                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.62                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % W/V PEG3350, 0.2 M SODIUM           
REMARK 280  CHLORIDE                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.67333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.83667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.83667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      129.67333            
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: 8000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.4 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 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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      HOH A2162   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     MET A   -17                                                      
REMARK 465     ALA A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     LYS A   663                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU A   237     O    HOH A  2112              1.99            
REMARK 500   O    LYS A   574     N    GLY A   576              1.89            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  51   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A  60   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP A 469   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 492   NE  -  CZ  -  NH1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 492   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  54     -120.89     53.67                                   
REMARK 500    ALA A 114      149.91   -174.15                                   
REMARK 500    SER A 199      -12.36   -143.15                                   
REMARK 500    TYR A 322       58.96   -112.71                                   
REMARK 500    ASN A 335       31.64     72.65                                   
REMARK 500    ASP A 380       40.03     33.63                                   
REMARK 500    LYS A 386       63.84     78.37                                   
REMARK 500    ILE A 476      -54.46   -130.58                                   
REMARK 500    ASN A 549      -97.98   -107.20                                   
REMARK 500    LYS A 574     -104.68    -58.67                                   
REMARK 500    LYS A 575        2.58    -16.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE HIS TAG (THE FIRST 18 RESIDUES ABOVE) IS NOT VISIBLE             
REMARK 999 IN THE ELECTRON DENSITY MAP                                          
DBREF  4C7V A    2   663  UNP    Q1WQU8   Q1WQU8_LACS1     2    663             
SEQADV 4C7V MET A  -17  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V ALA A  -16  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -15  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -14  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -13  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -12  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -11  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V HIS A  -10  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V SER A   -9  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V SER A   -8  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V GLY A   -7  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V LEU A   -6  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V GLU A   -5  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V VAL A   -4  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V LEU A   -3  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V PHE A   -2  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V GLN A   -1  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V GLY A    0  UNP  Q1WQU8              EXPRESSION TAG                 
SEQADV 4C7V PRO A    1  UNP  Q1WQU8              EXPRESSION TAG                 
SEQRES   1 A  681  MET ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU          
SEQRES   2 A  681  VAL LEU PHE GLN GLY PRO TYR ASP GLN VAL ASP GLN LEU          
SEQRES   3 A  681  GLY VAL ASN THR LEU ARG THR LEU SER ILE ASP ALA ILE          
SEQRES   4 A  681  GLN ARG ALA ASN SER GLY HIS PRO GLY LEU PRO MET GLY          
SEQRES   5 A  681  ALA ALA PRO MET ALA TYR VAL LEU TRP THR ARG HIS LEU          
SEQRES   6 A  681  LYS ILE ASN PRO LYS THR HIS MET ASN TRP VAL ASN ARG          
SEQRES   7 A  681  ASP ARG PHE VAL LEU SER ALA GLY HIS GLY SER ALA LEU          
SEQRES   8 A  681  LEU TYR SER LEU ALA HIS LEU ALA GLY TYR ASP VAL SER          
SEQRES   9 A  681  MET ASP ASP LEU LYS ASN PHE ARG GLU TRP LYS SER ASN          
SEQRES  10 A  681  THR PRO GLY HIS PRO GLU TYR GLY CYS THR ASP GLY VAL          
SEQRES  11 A  681  GLU ALA THR THR GLY PRO LEU GLY GLN GLY ILE SER MET          
SEQRES  12 A  681  ALA VAL GLY MET ALA MET ALA GLU ALA HIS LEU GLY LYS          
SEQRES  13 A  681  LYS PHE ASN ARG GLU GLY TYR PRO VAL MET ASP HIS TYR          
SEQRES  14 A  681  THR TYR ALA LEU ILE GLY ASP GLY ASP LEU MET GLU GLY          
SEQRES  15 A  681  VAL ALA SER GLU ALA ALA SER LEU ALA GLY HIS LEU LYS          
SEQRES  16 A  681  LEU GLY LYS LEU ILE ALA LEU TYR ASP SER ASN GLY ILE          
SEQRES  17 A  681  SER LEU ASP GLY LYS THR SER ALA SER PHE THR GLU ASN          
SEQRES  18 A  681  VAL GLY ALA ARG PHE GLU ALA TYR GLY TRP GLN TYR ILE          
SEQRES  19 A  681  LEU VAL GLU ASP GLY PHE ASN LEU GLU GLU ILE ASP LYS          
SEQRES  20 A  681  ALA ILE VAL GLN ALA LYS ALA GLU SER ASP LYS PRO THR          
SEQRES  21 A  681  ILE ILE GLU ILE LYS THR THR ILE GLY TYR GLY SER GLU          
SEQRES  22 A  681  ASN GLN GLY THR HIS LYS VAL HIS GLY SER PRO LEU GLY          
SEQRES  23 A  681  GLU GLU GLY VAL ALA HIS ALA LYS GLU VAL TYR ASN TRP          
SEQRES  24 A  681  ASN TYR PRO PRO PHE THR VAL PRO GLU GLU VAL SER GLN          
SEQRES  25 A  681  ARG PHE LYS GLU CYS LEU GLN ASP LYS GLY VAL LYS ALA          
SEQRES  26 A  681  GLU ASN LYS TRP ASN GLU MET PHE GLU ALA TYR LYS LYS          
SEQRES  27 A  681  GLU TYR SER ASP LEU ALA GLN LYS PHE SER ASP GLY PHE          
SEQRES  28 A  681  SER ASN LYS VAL PRO ASN THR LEU GLY ASP ILE LEU PRO          
SEQRES  29 A  681  GLN TYR GLY GLU ASP ASP SER ILE ALA THR ARG ALA ALA          
SEQRES  30 A  681  SER GLN LYS ALA ILE ASN ALA LEU ALA LYS GLU VAL SER          
SEQRES  31 A  681  SER LEU TRP GLY GLY ALA ALA ASP LEU ALA SER SER ASN          
SEQRES  32 A  681  LYS THR VAL ILE ALA GLY GLU GLY ASP PHE GLN PRO GLU          
SEQRES  33 A  681  SER TYR GLU GLY ARG ASN ILE TRP PHE GLY VAL ARG GLU          
SEQRES  34 A  681  PHE GLY MET ALA CYS ALA MET ASN GLY ILE MET LEU HIS          
SEQRES  35 A  681  GLY GLY THR ARG ILE PHE GLY SER THR PHE PHE VAL PHE          
SEQRES  36 A  681  SER ASP TYR LEU LYS ALA ALA ILE ARG LEU SER ALA ILE          
SEQRES  37 A  681  GLN LYS LEU PRO VAL ILE TYR VAL LEU THR HIS ASP SER          
SEQRES  38 A  681  VAL ALA VAL GLY LYS ASP GLY PRO THR HIS GLU PRO ILE          
SEQRES  39 A  681  GLU GLN LEU ALA SER LEU ARG THR ILE PRO ASN VAL GLN          
SEQRES  40 A  681  VAL PHE ARG PRO ALA ASP GLY ASN GLU THR SER ALA ALA          
SEQRES  41 A  681  TRP LYS VAL ALA LEU GLU THR LEU ASP LYS PRO THR ILE          
SEQRES  42 A  681  LEU VAL LEU SER ARG GLN ASN LEU ASP THR LEU PRO ILE          
SEQRES  43 A  681  SER LYS GLU LYS VAL PHE ASP GLY VAL GLU LYS GLY GLY          
SEQRES  44 A  681  TYR VAL VAL GLN GLY ALA GLU ASN GLU ALA ASP GLY ILE          
SEQRES  45 A  681  LEU ILE ALA THR GLY SER GLU VAL GLY LEU ALA LEU LYS          
SEQRES  46 A  681  ALA LYS GLU GLU LEU GLN LYS LYS GLY LYS ASP VAL ILE          
SEQRES  47 A  681  VAL VAL SER LEU PRO SER TRP GLU ARG PHE GLU ALA GLN          
SEQRES  48 A  681  SER GLU GLU TYR LYS ASN THR VAL ILE PRO PRO GLU LEU          
SEQRES  49 A  681  LYS LYS ARG MET THR ILE GLU ALA GLY THR THR TYR GLY          
SEQRES  50 A  681  TRP ALA LYS TYR ALA GLY ASP HIS GLY VAL MET ILE GLY          
SEQRES  51 A  681  ILE ASP GLU PHE GLY MET SER ALA PRO SER ASP ILE VAL          
SEQRES  52 A  681  LEU ARG GLU LEU GLY MET SER VAL GLU ASN ILE VAL ASP          
SEQRES  53 A  681  LYS TYR LEU GLU LYS                                          
FORMUL   2  HOH   *246(H2 O)                                                    
HELIX    1   1 ASP A    3  ASN A   25  1                                  23    
HELIX    2   2 PRO A   29  HIS A   46  1                                  18    
HELIX    3   3 ASN A   50  HIS A   54  5                                   5    
HELIX    4   4 ALA A   67  HIS A   69  5                                   3    
HELIX    5   5 GLY A   70  GLY A   82  1                                  13    
HELIX    6   6 SER A   86  LYS A   91  1                                   6    
HELIX    7   7 GLY A  120  ASN A  141  1                                  22    
HELIX    8   8 GLY A  157  GLU A  163  1                                   7    
HELIX    9   9 GLU A  163  LEU A  176  1                                  14    
HELIX   10  10 SER A  197  SER A  199  5                                   3    
HELIX   11  11 ASN A  203  GLY A  212  1                                  10    
HELIX   12  12 ASN A  223  GLU A  237  1                                  15    
HELIX   13  13 THR A  259  HIS A  263  5                                   5    
HELIX   14  14 GLY A  268  TYR A  279  1                                  12    
HELIX   15  15 PRO A  289  LEU A  300  1                                  12    
HELIX   16  16 LEU A  300  TYR A  322  1                                  23    
HELIX   17  17 TYR A  322  ASN A  335  1                                  14    
HELIX   18  18 THR A  340  LEU A  345  1                                   6    
HELIX   19  19 THR A  356  VAL A  371  1                                  16    
HELIX   20  20 LEU A  381  LYS A  386  1                                   6    
HELIX   21  21 GLN A  396  TYR A  400  5                                   5    
HELIX   22  22 ARG A  410  GLY A  425  1                                  16    
HELIX   23  23 PHE A  437  GLN A  451  1                                  15    
HELIX   24  24 SER A  463  GLY A  467  5                                   5    
HELIX   25  25 GLY A  470  GLU A  474  5                                   5    
HELIX   26  26 GLU A  477  THR A  484  1                                   8    
HELIX   27  27 ASP A  495  THR A  509  1                                  15    
HELIX   28  28 SER A  529  LYS A  539  1                                  11    
HELIX   29  29 SER A  560  LYS A  575  1                                  16    
HELIX   30  30 SER A  586  ALA A  592  1                                   7    
HELIX   31  31 SER A  594  ILE A  602  1                                   9    
HELIX   32  32 TRP A  620  GLY A  625  1                                   6    
HELIX   33  33 PRO A  641  LEU A  649  1                                   9    
HELIX   34  34 SER A  652  GLU A  662  1                                  11    
SHEET    1  AA 5 ARG A  62  LEU A  65  0                                        
SHEET    2  AA 5 THR A 152  ILE A 156  1  O  TYR A 153   N  VAL A  64           
SHEET    3  AA 5 LEU A 181  SER A 187  1  O  ILE A 182   N  ALA A 154           
SHEET    4  AA 5 THR A 242  LYS A 247  1  O  THR A 242   N  ALA A 183           
SHEET    5  AA 5 GLN A 214  VAL A 218  1  O  GLN A 214   N  ILE A 243           
SHEET    1  AB 2 ILE A 190  SER A 191  0                                        
SHEET    2  AB 2 GLY A 194  LYS A 195 -1  O  GLY A 194   N  SER A 191           
SHEET    1  AC 2 SER A 353  ALA A 355  0                                        
SHEET    2  AC 2 ASN A 522  ASP A 524 -1  O  LEU A 523   N  ILE A 354           
SHEET    1  AD 6 ASN A 404  TRP A 406  0                                        
SHEET    2  AD 6 LEU A 374  ALA A 378  1  O  GLY A 376   N  ILE A 405           
SHEET    3  AD 6 ARG A 428  PHE A 434  1  O  ARG A 428   N  TRP A 375           
SHEET    4  AD 6 ILE A 456  THR A 460  1  O  ILE A 456   N  GLY A 431           
SHEET    5  AD 6 THR A 514  VAL A 517  1  O  THR A 514   N  TYR A 457           
SHEET    6  AD 6 GLN A 489  PHE A 491  1  O  GLN A 489   N  ILE A 515           
SHEET    1  AE 5 TYR A 542  GLN A 545  0                                        
SHEET    2  AE 5 VAL A 579  SER A 583 -1  O  VAL A 581   N  VAL A 544           
SHEET    3  AE 5 GLY A 553  ALA A 557  1  O  GLY A 553   N  ILE A 580           
SHEET    4  AE 5 ARG A 609  ILE A 612  1  O  MET A 610   N  ILE A 556           
SHEET    5  AE 5 VAL A 629  ILE A 631  1  O  VAL A 629   N  THR A 611           
CRYST1   76.150   76.150  194.510  90.00  90.00 120.00 P 32 2 1      6          
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      0.013132  0.007582  0.000000        0.00000                         
SCALE2      0.000000  0.015164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005141        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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