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Database: PDB
Entry: 3RD8
LinkDB: 3RD8
Original site: 3RD8 
HEADER    LYASE                                   01-APR-11   3RD8              
TITLE     CRYSTAL STRUCTURE OF FUMARATE HYDRATASE CLASS II MYCOBACTERIUM        
TITLE    2 SMEGMATIS                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUMARATE HYDRATASE CLASS II;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 4.2.1.2;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS;                        
SOURCE   3 ORGANISM_TAXID: 246196;                                              
SOURCE   4 STRAIN: ATCC 700084 / MC(2)155;                                      
SOURCE   5 GENE: MSMEG_5240;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: AVA0421                                   
KEYWDS    SSGCID, FUMARATE HYDRATASE CLASS II, HYDRATASE, LYASE, STRUCTURAL     
KEYWDS   2 GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   3   13-SEP-23 3RD8    1       SEQADV                                   
REVDAT   2   22-APR-15 3RD8    1       JRNL   VERSN                             
REVDAT   1   08-JUN-11 3RD8    0                                                
JRNL        AUTH   L.BAUGH,I.PHAN,D.W.BEGLEY,M.C.CLIFTON,B.ARMOUR,D.M.DRANOW,   
JRNL        AUTH 2 B.M.TAYLOR,M.M.MURUTHI,J.ABENDROTH,J.W.FAIRMAN,D.FOX,        
JRNL        AUTH 3 S.H.DIETERICH,B.L.STAKER,A.S.GARDBERG,R.CHOI,S.N.HEWITT,     
JRNL        AUTH 4 A.J.NAPULI,J.MYERS,L.K.BARRETT,Y.ZHANG,M.FERRELL,E.MUNDT,    
JRNL        AUTH 5 K.THOMPKINS,N.TRAN,S.LYONS-ABBOTT,A.ABRAMOV,A.SEKAR,         
JRNL        AUTH 6 D.SERBZHINSKIY,D.LORIMER,G.W.BUCHKO,R.STACY,L.J.STEWART,     
JRNL        AUTH 7 T.E.EDWARDS,W.C.VAN VOORHIS,P.J.MYLER                        
JRNL        TITL   INCREASING THE STRUCTURAL COVERAGE OF TUBERCULOSIS DRUG      
JRNL        TITL 2 TARGETS.                                                     
JRNL        REF    TUBERCULOSIS (EDINB)          V.  95   142 2015              
JRNL        REFN                   ISSN 1472-9792                               
JRNL        PMID   25613812                                                     
JRNL        DOI    10.1016/J.TUBE.2014.12.003                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 26630                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1332                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1855                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.84                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 111                          
REMARK   3   BIN FREE R VALUE                    : 0.2410                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3312                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 278                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.35000                                             
REMARK   3    B22 (A**2) : 1.64000                                              
REMARK   3    B33 (A**2) : -1.29000                                             
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): 0.225         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.155        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3374 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2178 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4595 ; 1.335 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5344 ; 0.965 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   459 ; 5.304 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;35.415 ;24.632       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   526 ;12.411 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;15.944 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   550 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3871 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   637 ; 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):  2271 ; 0.507 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   933 ; 0.134 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3605 ; 0.892 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1103 ; 1.743 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   988 ; 2.713 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
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     7        A   151                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7060  69.7330 -28.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1754 T22:   0.2569                                     
REMARK   3      T33:   0.0692 T12:  -0.0567                                     
REMARK   3      T13:  -0.0375 T23:   0.1247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7095 L22:   1.0661                                     
REMARK   3      L33:   0.7023 L12:  -0.3524                                     
REMARK   3      L13:  -0.0846 L23:  -0.0802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:   0.4095 S13:   0.1534                       
REMARK   3      S21:  -0.2868 S22:   0.0939 S23:   0.0622                       
REMARK   3      S31:  -0.1120 S32:  -0.0993 S33:  -0.0968                       
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   152        A   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0730  44.5260  -9.1610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0564 T22:   0.1429                                     
REMARK   3      T33:   0.0568 T12:  -0.0446                                     
REMARK   3      T13:  -0.0181 T23:   0.0368                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7416 L22:   0.8508                                     
REMARK   3      L33:   0.4940 L12:  -0.0720                                     
REMARK   3      L13:  -0.0097 L23:  -0.1051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:   0.1233 S13:  -0.1140                       
REMARK   3      S21:  -0.0618 S22:   0.1576 S23:   0.1532                       
REMARK   3      S31:   0.0747 S32:  -0.1268 S33:  -0.0924                       
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   394        A   465                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0570  12.4410  15.6870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3232 T22:   0.3346                                     
REMARK   3      T33:   0.9025 T12:  -0.0362                                     
REMARK   3      T13:  -0.0644 T23:   0.4714                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3704 L22:   3.8105                                     
REMARK   3      L33:   7.2816 L12:  -0.1343                                     
REMARK   3      L13:   1.9632 L23:   0.3761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3100 S12:  -0.3085 S13:  -0.6580                       
REMARK   3      S21:   0.3323 S22:   0.4604 S23:  -0.0995                       
REMARK   3      S31:   1.2400 S32:  -0.3474 S33:  -0.7704                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   4                                                                      
REMARK   4 3RD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064787.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
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 FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : RIGAKU VARIMAX                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944+                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26708                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1100                            
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     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3NO9, MODIFIED BY CHAINSAW                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MOLECULAR DIMENSIONS PACT SCREEN F9:     
REMARK 280  200MM NA/K TARTRATE, 100M BISTRISPROPANE PH 6.5, 20% PEG 3350;      
REMARK 280  MYSMA.01507.A.A1 PS00681 AT 67.55MG/ML, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 290K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.24500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       52.62500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.51000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.24500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       52.62500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.51000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.24500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       52.62500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.51000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.24500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       52.62500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       69.51000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 31420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 52350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -189.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       72.49000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      105.25000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       72.49000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000      105.25000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 669  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   -20                                                      
REMARK 465     ALA A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     MET A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     THR A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ALA A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     THR A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     LYS A   446                                                      
REMARK 465     ASP A   466                                                      
REMARK 465     GLY A   467                                                      
REMARK 465     GLU A   468                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 237    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 394    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 397    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 399    CG   CD1  CD2                                       
REMARK 470     SER A 402    OG                                                  
REMARK 470     ILE A 406    CG1  CG2  CD1                                       
REMARK 470     LYS A 424    CG   CD   CE   NZ                                   
REMARK 470     GLN A 425    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 427    CG   CD1  CD2                                       
REMARK 470     LYS A 430    CG   CD   CE   NZ                                   
REMARK 470     LYS A 431    CG   CD   CE   NZ                                   
REMARK 470     ILE A 433    CG1  CG2  CD1                                       
REMARK 470     ARG A 434    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 435    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 437    CG1  CG2                                            
REMARK 470     ILE A 438    CG1  CG2  CD1                                       
REMARK 470     ARG A 440    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 442    CG   CD1  CD2                                       
REMARK 470     ILE A 443    CG1  CG2  CD1                                       
REMARK 470     LEU A 449    CG   CD1  CD2                                       
REMARK 470     GLU A 450    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 452    CG   CD1  CD2                                       
REMARK 470     ARG A 454    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 465    CG   CD   CE   NZ                                   
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    ARG A  27     -149.60   -134.15                                   
REMARK 500    ILE A  39      -57.92   -123.57                                   
REMARK 500    ALA A 189     -168.97   -121.98                                   
REMARK 500    THR A 227     -129.67     48.18                                   
REMARK 500    PHE A 354     -119.08     46.18                                   
REMARK 500    VAL A 358       49.82   -106.78                                   
REMARK 500    CYS A 385      -68.50   -134.40                                   
REMARK 500    SER A 405        2.86    -69.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MYSMA.01507.A   RELATED DB: TARGETDB                     
DBREF  3RD8 A    1   468  UNP    A0R2U8   A0R2U8_MYCS2     1    468             
SEQADV 3RD8 MET A  -20  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 ALA A  -19  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -18  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -17  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -16  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -15  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -14  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 HIS A  -13  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 MET A  -12  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLY A  -11  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 THR A  -10  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 LEU A   -9  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLU A   -8  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 ALA A   -7  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLN A   -6  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 THR A   -5  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLN A   -4  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLY A   -3  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 PRO A   -2  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 GLY A   -1  UNP  A0R2U8              EXPRESSION TAG                 
SEQADV 3RD8 SER A    0  UNP  A0R2U8              EXPRESSION TAG                 
SEQRES   1 A  489  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 A  489  ALA GLN THR GLN GLY PRO GLY SER MET ALA ASP THR ASP          
SEQRES   3 A  489  VAL GLU TYR ARG ILE GLU HIS ASP THR MET GLY GLU VAL          
SEQRES   4 A  489  ARG VAL PRO LYS ASP ALA LEU TRP ARG ALA GLN THR GLN          
SEQRES   5 A  489  ARG ALA VAL GLU ASN PHE PRO ILE SER PHE ARG GLY LEU          
SEQRES   6 A  489  GLU ARG THR GLN ILE ARG ALA LEU GLY LEU LEU LYS ALA          
SEQRES   7 A  489  ALA CYS ALA GLN VAL ASN LYS ASP LEU GLY LEU LEU ASP          
SEQRES   8 A  489  PRO GLU LYS ALA ASP ALA ILE ILE ALA ALA ALA GLY GLU          
SEQRES   9 A  489  ILE ALA GLU GLY LYS HIS ASP ASP GLN PHE PRO ILE ASP          
SEQRES  10 A  489  VAL PHE GLN THR GLY SER GLY THR SER SER ASN MET ASN          
SEQRES  11 A  489  THR ASN GLU VAL ILE ALA SER ILE ALA ALA ALA ASN GLY          
SEQRES  12 A  489  VAL THR VAL HIS PRO ASN ASP HIS VAL ASN MET SER GLN          
SEQRES  13 A  489  SER SER ASN ASP THR PHE PRO THR ALA THR HIS ILE ALA          
SEQRES  14 A  489  ALA THR GLU ALA ALA VAL ARG HIS LEU ILE PRO ALA LEU          
SEQRES  15 A  489  GLU VAL LEU HIS ALA SER LEU ALA ALA LYS ALA LYS GLN          
SEQRES  16 A  489  TRP ARG THR VAL VAL LYS SER GLY ARG THR HIS LEU MET          
SEQRES  17 A  489  ASP ALA VAL PRO VAL THR LEU GLY GLN GLU PHE GLY GLY          
SEQRES  18 A  489  TYR ALA ARG GLN ILE GLU ALA GLY ILE GLU ARG VAL LYS          
SEQRES  19 A  489  ALA THR LEU PRO ARG LEU GLY GLU LEU ALA ILE GLY GLY          
SEQRES  20 A  489  THR ALA VAL GLY THR GLY LEU ASN ALA PRO GLU GLY PHE          
SEQRES  21 A  489  GLY ALA LYS VAL VAL GLU VAL LEU VAL ASN GLU THR GLY          
SEQRES  22 A  489  LEU ALA GLU LEU ARG THR ALA VAL ASP SER PHE GLU ALA          
SEQRES  23 A  489  GLN ALA ALA ARG ASP GLY LEU VAL GLU ALA SER GLY ALA          
SEQRES  24 A  489  LEU ARG THR ILE ALA VAL SER LEU THR LYS ILE ALA ASN          
SEQRES  25 A  489  ASP ILE ARG TRP MET GLY SER GLY PRO LEU THR GLY LEU          
SEQRES  26 A  489  ALA GLU ILE GLN LEU PRO ASP LEU GLN PRO GLY SER SER          
SEQRES  27 A  489  ILE MET PRO GLY LYS VAL ASN PRO VAL LEU PRO GLU ALA          
SEQRES  28 A  489  VAL THR GLN VAL ALA CYS GLN VAL VAL GLY ASN ASP ALA          
SEQRES  29 A  489  ALA ILE ALA PHE GLY GLY ALA SER GLY ALA PHE GLU LEU          
SEQRES  30 A  489  ASN VAL TYR ILE PRO MET MET ALA ARG ASN LEU LEU GLU          
SEQRES  31 A  489  SER PHE THR LEU LEU SER ASN VAL SER ARG LEU PHE ALA          
SEQRES  32 A  489  GLU ARG CYS ILE ASP GLY LEU VAL ALA ASN GLU GLU ARG          
SEQRES  33 A  489  LEU ARG GLU LEU ALA GLU SER SER PRO SER ILE VAL THR          
SEQRES  34 A  489  PRO LEU ASN SER ALA ILE GLY TYR GLU GLU ALA ALA LYS          
SEQRES  35 A  489  VAL ALA LYS GLN ALA LEU ALA GLU LYS LYS THR ILE ARG          
SEQRES  36 A  489  GLN THR VAL ILE ASP ARG GLY LEU ILE GLY ASP LYS LEU          
SEQRES  37 A  489  SER LEU GLU GLU LEU ASP ARG ARG LEU ASP VAL LEU ALA          
SEQRES  38 A  489  MET ALA ARG VAL LYS ASP GLY GLU                              
FORMUL   2  HOH   *278(H2 O)                                                    
HELIX    1   1 ARG A   27  PHE A   37  1                                  11    
HELIX    2   2 GLU A   45  LEU A   66  1                                  22    
HELIX    3   3 ASP A   70  GLY A   87  1                                  18    
HELIX    4   4 HIS A   89  PHE A   93  5                                   5    
HELIX    5   5 GLY A  103  ASN A  121  1                                  19    
HELIX    6   6 SER A  136  HIS A  156  1                                  21    
HELIX    7   7 HIS A  156  TRP A  175  1                                  20    
HELIX    8   8 LEU A  194  GLY A  220  1                                  27    
HELIX    9   9 GLY A  238  GLY A  252  1                                  15    
HELIX   10  10 PHE A  263  ALA A  268  1                                   6    
HELIX   11  11 ARG A  269  GLY A  297  1                                  29    
HELIX   12  12 PRO A  325  ALA A  350  1                                  26    
HELIX   13  13 TYR A  359  CYS A  385  1                                  27    
HELIX   14  14 ILE A  386  LEU A  389  5                                   4    
HELIX   15  15 ASN A  392  SER A  403  1                                  12    
HELIX   16  16 PRO A  404  PRO A  409  5                                   6    
HELIX   17  17 LEU A  410  LYS A  430  1                                  21    
HELIX   18  18 THR A  432  ARG A  440  1                                   9    
HELIX   19  19 SER A  448  ASP A  457  1                                  10    
HELIX   20  20 ASP A  457  ALA A  462  1                                   6    
SHEET    1   A 2 TYR A   8  ASP A  13  0                                        
SHEET    2   A 2 GLY A  16  PRO A  21 -1  O  VAL A  18   N  GLU A  11           
SHEET    1   B 2 VAL A 179  THR A 184  0                                        
SHEET    2   B 2 MET A 187  THR A 193 -1  O  VAL A 192   N  LYS A 180           
SHEET    1   C 2 GLU A 221  LEU A 222  0                                        
SHEET    2   C 2 ARG A 257  THR A 258  1  O  ARG A 257   N  LEU A 222           
SHEET    1   D 2 ILE A 307  GLN A 308  0                                        
SHEET    2   D 2 VAL A 390  ALA A 391 -1  O  VAL A 390   N  GLN A 308           
CISPEP   1 GLY A  299    PRO A  300          0         4.27                     
CRYST1   72.490  105.250  139.020  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013795  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009501  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007193        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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