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Database: PDB
Entry: 3M9Y
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Original site: 3M9Y 
HEADER    ISOMERASE                               23-MAR-10   3M9Y              
TITLE     CRYSTAL STRUCTURE OF TRIOSEPHOSPHATE ISOMERASE FROM METHICILLIN       
TITLE    2 RESISTANT STAPHYLOCOCCUS AUREUS AT 1.9 ANGSTROM RESOLUTION           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRIOSEPHOSPHATE ISOMERASE;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TIM, TRIOSE-PHOSPHATE ISOMERASE;                            
COMPND   5 EC: 5.3.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 282458;                                              
SOURCE   4 STRAIN: MRSA252;                                                     
SOURCE   5 GENE: SAR0830, TPI, TPIA;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE30                                     
KEYWDS    TIM BARREL, GLYCOLYSIS, GLUCONEOGENESIS, ISOMERASE, PENTOSE SHUNT     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MUKHERJEE,D.DUTTA,B.SAHA,A.K.DAS                                    
REVDAT   5   01-NOV-23 3M9Y    1       REMARK SEQADV LINK                       
REVDAT   4   26-JUN-13 3M9Y    1       JRNL                                     
REVDAT   3   17-OCT-12 3M9Y    1       JRNL   VERSN  REMARK                     
REVDAT   2   13-APR-11 3M9Y    1       ATOM                                     
REVDAT   1   06-APR-11 3M9Y    0                                                
JRNL        AUTH   S.MUKHERJEE,A.ROYCHOWDHURY,D.DUTTA,A.K.DAS                   
JRNL        TITL   CRYSTAL STRUCTURES OF TRIOSEPHOSPHATE ISOMERASE FROM         
JRNL        TITL 2 METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS MRSA252 PROVIDE  
JRNL        TITL 3 STRUCTURAL INSIGHTS INTO NOVEL MODES OF LIGAND BINDING AND   
JRNL        TITL 4 UNIQUE CONFORMATIONS OF CATALYTIC LOOP                       
JRNL        REF    BIOCHIMIE                     V.  94  2532 2012              
JRNL        REFN                   ISSN 0300-9084                               
JRNL        PMID   22813930                                                     
JRNL        DOI    10.1016/J.BIOCHI.2012.07.001                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 44825                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2258                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2972                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 171                          
REMARK   3   BIN FREE R VALUE                    : 0.2530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3825                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 481                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 24.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.10000                                              
REMARK   3    B22 (A**2) : 1.10000                                              
REMARK   3    B33 (A**2) : -2.21000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.128         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.083         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.189         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3916 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5298 ; 1.842 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   511 ; 5.822 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   171 ;38.137 ;26.374       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   702 ;13.790 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;11.336 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   608 ; 0.150 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2923 ; 0.010 ; 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):  2514 ; 1.275 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4043 ; 2.174 ; 2.500       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1402 ; 5.316 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1251 ; 8.335 ;10.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      3       A     107      2                      
REMARK   3           1     B      3       B     107      2                      
REMARK   3           2     A    110       A     156      2                      
REMARK   3           2     B    110       B     156      2                      
REMARK   3           3     A    160       A     172      2                      
REMARK   3           3     B    160       B     172      2                      
REMARK   3           4     A    186       A     242      2                      
REMARK   3           4     B    186       B     242      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    884 ; 0.100 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    776 ; 0.130 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    884 ; 1.210 ; 1.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    776 ; 1.450 ; 2.500           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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     0        A   253                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2495  13.0326  -8.0317              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0272 T22:   0.1290                                     
REMARK   3      T33:   0.0744 T12:  -0.0176                                     
REMARK   3      T13:   0.0360 T23:  -0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5165 L22:   0.5929                                     
REMARK   3      L33:   1.3815 L12:  -0.0339                                     
REMARK   3      L13:   0.0149 L23:   0.2821                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0338 S12:   0.2816 S13:   0.1546                       
REMARK   3      S21:  -0.1188 S22:   0.0555 S23:  -0.1667                       
REMARK   3      S31:  -0.1101 S32:   0.2647 S33:  -0.0893                       
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 :   B     0        B   253                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7112  19.6611  17.4992              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0125 T22:   0.0251                                     
REMARK   3      T33:   0.0429 T12:   0.0053                                     
REMARK   3      T13:  -0.0055 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6811 L22:   0.9265                                     
REMARK   3      L33:   2.0168 L12:  -0.1842                                     
REMARK   3      L13:   0.1097 L23:   0.5453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:  -0.0670 S13:   0.0931                       
REMARK   3      S21:   0.0033 S22:  -0.0201 S23:   0.0436                       
REMARK   3      S31:  -0.1309 S32:  -0.1127 S33:   0.0408                       
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: RESIDUAL ONLY                   
REMARK   4                                                                      
REMARK   4 3M9Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000058293.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : VARIMAX MIRRORS                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.9                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44961                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.365                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 13.50                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 29.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.43300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
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 2BTM                                       
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: 1.6M TRISODIUM CITRATE DIHYDRATE, PH     
REMARK 280  6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.50300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       39.73900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       39.73900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      131.25450            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       39.73900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       39.73900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.75150            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       39.73900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       39.73900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      131.25450            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       39.73900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       39.73900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.75150            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       87.50300            
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: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   176                                                      
REMARK 465     GLY A   177                                                      
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 B   250     O    HOH B   342              2.16            
REMARK 500   CE   LYS B   120     O    HOH B   511              2.16            
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    ASP A  21   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    GLY B 175   N   -  CA  -  C   ANGL. DEV. = -16.0 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    LYS A  11     -149.31     53.91                                   
REMARK 500    LYS A  14      141.78     87.85                                   
REMARK 500    SER A 200      -99.18   -144.97                                   
REMARK 500    LYS B  11     -139.61     53.75                                   
REMARK 500    MET B  12       76.51   -101.19                                   
REMARK 500    LYS B  14      145.60     83.54                                   
REMARK 500    THR B 176      138.48     73.40                                   
REMARK 500    SER B 200      -99.87   -145.06                                   
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 B 254  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 MET B 225   O                                                      
REMARK 620 2 GLN B 227   O    98.1                                              
REMARK 620 3 ILE B 230   O   105.3  95.4                                        
REMARK 620 4 HOH B 305   O    87.3 171.6  89.3                                  
REMARK 620 5 HOH B 327   O    89.7  87.3 164.2  86.4                            
REMARK 620 6 HOH B 359   O   167.8  90.2  82.7  83.5  81.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 254                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 255                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 256                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UWU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UWV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UWW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UWY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UWZ   RELATED DB: PDB                                   
DBREF  3M9Y A    1   253  UNP    Q6GIL6   TPIS_STAAR       1    253             
DBREF  3M9Y B    1   253  UNP    Q6GIL6   TPIS_STAAR       1    253             
SEQADV 3M9Y SER A    0  UNP  Q6GIL6              EXPRESSION TAG                 
SEQADV 3M9Y SER B    0  UNP  Q6GIL6              EXPRESSION TAG                 
SEQRES   1 A  254  SER MET ARG THR PRO ILE ILE ALA GLY ASN TRP LYS MET          
SEQRES   2 A  254  ASN LYS THR VAL GLN GLU ALA LYS ASP PHE VAL ASN ALA          
SEQRES   3 A  254  LEU PRO THR LEU PRO ASP SER LYS GLU VAL GLU SER VAL          
SEQRES   4 A  254  ILE CYS ALA PRO ALA ILE GLN LEU ASP ALA LEU THR THR          
SEQRES   5 A  254  ALA VAL LYS GLU GLY LYS ALA GLN GLY LEU GLU ILE GLY          
SEQRES   6 A  254  ALA GLN ASN THR TYR PHE GLU ASP ASN GLY ALA PHE THR          
SEQRES   7 A  254  GLY GLU THR SER PRO VAL ALA LEU ALA ASP LEU GLY VAL          
SEQRES   8 A  254  LYS TYR VAL VAL ILE GLY HIS SER GLU ARG ARG GLU LEU          
SEQRES   9 A  254  PHE HIS GLU THR ASP GLU GLU ILE ASN LYS LYS ALA HIS          
SEQRES  10 A  254  ALA ILE PHE LYS HIS GLY MET THR PRO ILE ILE CYS VAL          
SEQRES  11 A  254  GLY GLU THR ASP GLU GLU ARG GLU SER GLY LYS ALA ASN          
SEQRES  12 A  254  ASP VAL VAL GLY GLU GLN VAL LYS LYS ALA VAL ALA GLY          
SEQRES  13 A  254  LEU SER GLU ASP GLN LEU LYS SER VAL VAL ILE ALA TYR          
SEQRES  14 A  254  GLU PRO ILE TRP ALA ILE GLY THR GLY LYS SER SER THR          
SEQRES  15 A  254  SER GLU ASP ALA ASN GLU MET CYS ALA PHE VAL ARG GLN          
SEQRES  16 A  254  THR ILE ALA ASP LEU SER SER LYS GLU VAL SER GLU ALA          
SEQRES  17 A  254  THR ARG ILE GLN TYR GLY GLY SER VAL LYS PRO ASN ASN          
SEQRES  18 A  254  ILE LYS GLU TYR MET ALA GLN THR ASP ILE ASP GLY ALA          
SEQRES  19 A  254  LEU VAL GLY GLY ALA SER LEU LYS VAL GLU ASP PHE VAL          
SEQRES  20 A  254  GLN LEU LEU GLU GLY ALA LYS                                  
SEQRES   1 B  254  SER MET ARG THR PRO ILE ILE ALA GLY ASN TRP LYS MET          
SEQRES   2 B  254  ASN LYS THR VAL GLN GLU ALA LYS ASP PHE VAL ASN ALA          
SEQRES   3 B  254  LEU PRO THR LEU PRO ASP SER LYS GLU VAL GLU SER VAL          
SEQRES   4 B  254  ILE CYS ALA PRO ALA ILE GLN LEU ASP ALA LEU THR THR          
SEQRES   5 B  254  ALA VAL LYS GLU GLY LYS ALA GLN GLY LEU GLU ILE GLY          
SEQRES   6 B  254  ALA GLN ASN THR TYR PHE GLU ASP ASN GLY ALA PHE THR          
SEQRES   7 B  254  GLY GLU THR SER PRO VAL ALA LEU ALA ASP LEU GLY VAL          
SEQRES   8 B  254  LYS TYR VAL VAL ILE GLY HIS SER GLU ARG ARG GLU LEU          
SEQRES   9 B  254  PHE HIS GLU THR ASP GLU GLU ILE ASN LYS LYS ALA HIS          
SEQRES  10 B  254  ALA ILE PHE LYS HIS GLY MET THR PRO ILE ILE CYS VAL          
SEQRES  11 B  254  GLY GLU THR ASP GLU GLU ARG GLU SER GLY LYS ALA ASN          
SEQRES  12 B  254  ASP VAL VAL GLY GLU GLN VAL LYS LYS ALA VAL ALA GLY          
SEQRES  13 B  254  LEU SER GLU ASP GLN LEU LYS SER VAL VAL ILE ALA TYR          
SEQRES  14 B  254  GLU PRO ILE TRP ALA ILE GLY THR GLY LYS SER SER THR          
SEQRES  15 B  254  SER GLU ASP ALA ASN GLU MET CYS ALA PHE VAL ARG GLN          
SEQRES  16 B  254  THR ILE ALA ASP LEU SER SER LYS GLU VAL SER GLU ALA          
SEQRES  17 B  254  THR ARG ILE GLN TYR GLY GLY SER VAL LYS PRO ASN ASN          
SEQRES  18 B  254  ILE LYS GLU TYR MET ALA GLN THR ASP ILE ASP GLY ALA          
SEQRES  19 B  254  LEU VAL GLY GLY ALA SER LEU LYS VAL GLU ASP PHE VAL          
SEQRES  20 B  254  GLN LEU LEU GLU GLY ALA LYS                                  
HET     NA  B 254       1                                                       
HET     NA  B 255       1                                                       
HET    CIT  B 256      13                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  CIT    C6 H8 O7                                                     
FORMUL   6  HOH   *481(H2 O)                                                    
HELIX    1   1 THR A   15  LEU A   26  1                                  12    
HELIX    2   2 PRO A   42  ILE A   44  5                                   3    
HELIX    3   3 GLN A   45  GLU A   55  1                                  11    
HELIX    4   4 SER A   81  LEU A   88  1                                   8    
HELIX    5   5 HIS A   97  PHE A  104  1                                   8    
HELIX    6   6 THR A  107  HIS A  121  1                                  15    
HELIX    7   7 THR A  132  SER A  138  1                                   7    
HELIX    8   8 LYS A  140  ALA A  154  1                                  15    
HELIX    9   9 SER A  157  VAL A  164  1                                   8    
HELIX   10  10 PRO A  170  ILE A  174  5                                   5    
HELIX   11  11 THR A  181  SER A  200  1                                  20    
HELIX   12  12 SER A  201  GLU A  206  1                                   6    
HELIX   13  13 ASN A  220  ALA A  226  1                                   7    
HELIX   14  14 GLY A  236  LEU A  240  5                                   5    
HELIX   15  15 LYS A  241  LYS A  253  1                                  13    
HELIX   16  16 THR B   15  LEU B   26  1                                  12    
HELIX   17  17 PRO B   42  ILE B   44  5                                   3    
HELIX   18  18 GLN B   45  GLU B   55  1                                  11    
HELIX   19  19 SER B   81  LEU B   88  1                                   8    
HELIX   20  20 HIS B   97  PHE B  104  1                                   8    
HELIX   21  21 THR B  107  HIS B  121  1                                  15    
HELIX   22  22 THR B  132  SER B  138  1                                   7    
HELIX   23  23 LYS B  140  VAL B  153  1                                  14    
HELIX   24  24 SER B  157  VAL B  164  1                                   8    
HELIX   25  25 PRO B  170  ILE B  174  5                                   5    
HELIX   26  26 THR B  181  SER B  200  1                                  20    
HELIX   27  27 SER B  201  GLU B  206  1                                   6    
HELIX   28  28 ASN B  220  ALA B  226  1                                   7    
HELIX   29  29 GLY B  236  LEU B  240  5                                   5    
HELIX   30  30 LYS B  241  GLY B  251  1                                  11    
SHEET    1   A 9 ILE A   5  ASN A   9  0                                        
SHEET    2   A 9 GLU A  36  ALA A  41  1  O  VAL A  38   N  GLY A   8           
SHEET    3   A 9 GLU A  62  ALA A  65  1  O  GLY A  64   N  ILE A  39           
SHEET    4   A 9 TYR A  92  ILE A  95  1  O  VAL A  94   N  ALA A  65           
SHEET    5   A 9 THR A 124  VAL A 129  1  O  CYS A 128   N  ILE A  95           
SHEET    6   A 9 VAL A 165  TYR A 168  1  O  VAL A 165   N  ILE A 127           
SHEET    7   A 9 ARG A 209  TYR A 212  1  O  GLN A 211   N  TYR A 168           
SHEET    8   A 9 GLY A 232  VAL A 235  1  O  GLY A 232   N  TYR A 212           
SHEET    9   A 9 ILE A   5  ASN A   9  1  N  ASN A   9   O  VAL A 235           
SHEET    1   B 9 ILE B   5  ASN B   9  0                                        
SHEET    2   B 9 GLU B  36  CYS B  40  1  O  CYS B  40   N  GLY B   8           
SHEET    3   B 9 GLU B  62  ALA B  65  1  O  GLY B  64   N  ILE B  39           
SHEET    4   B 9 TYR B  92  ILE B  95  1  O  VAL B  94   N  ALA B  65           
SHEET    5   B 9 THR B 124  VAL B 129  1  O  ILE B 126   N  ILE B  95           
SHEET    6   B 9 VAL B 165  TYR B 168  1  O  VAL B 165   N  ILE B 127           
SHEET    7   B 9 ARG B 209  TYR B 212  1  O  GLN B 211   N  ILE B 166           
SHEET    8   B 9 GLY B 232  VAL B 235  1  O  GLY B 232   N  TYR B 212           
SHEET    9   B 9 ILE B   5  ASN B   9  1  N  ASN B   9   O  VAL B 235           
LINK         OG1 THR A  80                NA    NA B 255     1555   1555  2.82  
LINK         O   MET B 225                NA    NA B 254     1555   1555  2.28  
LINK         O   GLN B 227                NA    NA B 254     1555   1555  2.54  
LINK         O   ILE B 230                NA    NA B 254     1555   1555  2.42  
LINK        NA    NA B 254                 O   HOH B 305     1555   1555  2.42  
LINK        NA    NA B 254                 O   HOH B 327     1555   1555  2.43  
LINK        NA    NA B 254                 O   HOH B 359     1555   1555  2.58  
SITE     1 AC1  6 MET B 225  GLN B 227  ILE B 230  HOH B 305                    
SITE     2 AC1  6 HOH B 327  HOH B 359                                          
SITE     1 AC2  4 THR A  80  PRO B  42  ALA B  43  ILE B  44                    
SITE     1 AC3 12 LYS B  11  SER B 215  LYS B 217  GLY B 236                    
SITE     2 AC3 12 GLY B 237  HOH B 285  HOH B 301  HOH B 306                    
SITE     3 AC3 12 HOH B 354  HOH B 355  HOH B 365  HOH B 475                    
CRYST1   79.478   79.478  175.006  90.00  90.00  90.00 P 43 21 2    16          
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      0.012582  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012582  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005714        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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