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Database: PDB
Entry: 4HEC
LinkDB: 4HEC
Original site: 4HEC 
HEADER    UNKNOWN FUNCTION                        03-OCT-12   4HEC              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE UNCHARACTERIZED PROTEIN FROM          
TITLE    2 MYCOBACTERIUM TUBERCULOSIS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: MT2234.1, RV2179C;                                             
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, MYCOBACTERIUM TUBERCULOSIS, STRUCTURAL GENOMICS, SEATTLE      
KEYWDS   2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, UNKNOWN FUNCTION  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)    
REVDAT   5   28-FEB-24 4HEC    1       REMARK SEQADV LINK                       
REVDAT   4   20-SEP-17 4HEC    1       REMARK                                   
REVDAT   3   12-FEB-14 4HEC    1       JRNL                                     
REVDAT   2   18-DEC-13 4HEC    1       JRNL                                     
REVDAT   1   17-OCT-12 4HEC    0                                                
JRNL        AUTH   J.ABENDROTH,A.OLLODART,E.S.ANDREWS,P.J.MYLER,B.L.STAKER,     
JRNL        AUTH 2 T.E.EDWARDS,V.L.ARCUS,C.GRUNDNER                             
JRNL        TITL   MYCOBACTERIUM TUBERCULOSIS RV2179C PROTEIN ESTABLISHES A NEW 
JRNL        TITL 2 EXORIBONUCLEASE FAMILY WITH BROAD PHYLOGENETIC DISTRIBUTION. 
JRNL        REF    J.BIOL.CHEM.                  V. 289  2139 2014              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   24311791                                                     
JRNL        DOI    10.1074/JBC.M113.525683                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 31227                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1645                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2217                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.35                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2570                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 220                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.68000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.67000                                              
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): 0.131         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.126         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.087         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.611         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2692 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2475 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3686 ; 1.652 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5683 ; 0.860 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   329 ; 5.600 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   135 ;29.271 ;22.222       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   421 ;11.828 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;22.951 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   396 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3035 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   647 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   159                          
REMARK   3    RESIDUE RANGE :   A   301        A   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3990  17.0880  81.3230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0668 T22:   0.0145                                     
REMARK   3      T33:   0.0348 T12:   0.0045                                     
REMARK   3      T13:  -0.0116 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1551 L22:   1.2706                                     
REMARK   3      L33:   1.4490 L12:   0.1391                                     
REMARK   3      L13:  -0.3673 L23:  -0.4798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0486 S12:   0.0147 S13:   0.0073                       
REMARK   3      S21:  -0.1098 S22:  -0.0411 S23:   0.0195                       
REMARK   3      S31:  -0.0359 S32:  -0.1085 S33:  -0.0075                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     0        B   162                          
REMARK   3    RESIDUE RANGE :   B   301        B   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3850   2.0010  99.0070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0769 T22:   0.0501                                     
REMARK   3      T33:   0.0418 T12:  -0.0278                                     
REMARK   3      T13:   0.0066 T23:   0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9015 L22:   1.2827                                     
REMARK   3      L33:   1.3609 L12:  -0.1701                                     
REMARK   3      L13:  -0.1892 L23:  -0.1476                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:  -0.1742 S13:  -0.0551                       
REMARK   3      S21:   0.1035 S22:  -0.0455 S23:   0.0212                       
REMARK   3      S31:   0.0455 S32:  -0.0525 S33:   0.0296                       
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 RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 4HEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-OCT-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075359.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
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 : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
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     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.03600                            
REMARK 200  R SYM                      (I) : 0.03600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.2900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.440                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: DE NOVO PHASING WITH IODIDE IONS                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: EMBIO JCSG+ B4: 10% PEG 8000, 8%         
REMARK 280  ETHYLENE GLYCOL, 100MM HEPES PH 7.5; MYTUD.18400.A.A1.PS01434 AT    
REMARK 280  12.8MG/ML + 2.5MM AMPPNP AND MGCL2, CRYO: 20% EG; THE STRUCTURE     
REMARK 280  WAS SOLVED VIA IODIDE SAD: A CRYSTAL WAS SOAKED IN RESERVOIR        
REMARK 280  PLUS 20% ETHYLENE GLYCOL AND 750MM NAI, ANOMALOUS AMPLITUDES ARE    
REMARK 280  DEPOSITED, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.39000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.02000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.36000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       53.02000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.39000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.36000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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     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     ARG A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     ARG A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     VAL A   140                                                      
REMARK 465     THR A   160                                                      
REMARK 465     ASP A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     GLY A   164                                                      
REMARK 465     ARG A   165                                                      
REMARK 465     GLY A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     ARG A   169                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     ALA B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     MET B   -12                                                      
REMARK 465     GLY B   -11                                                      
REMARK 465     THR B   -10                                                      
REMARK 465     LEU B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ALA B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     THR B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     ARG B   165                                                      
REMARK 465     GLY B   166                                                      
REMARK 465     ALA B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     ARG B   169                                                      
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     GLU A  42    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  62    CG   CD   OE1  NE2                                  
REMARK 470     HIS A 141    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 152    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  62    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 132    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 136    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 138    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 139    CG   OD1  OD2                                       
REMARK 470     VAL B 140    CG1  CG2                                            
REMARK 470     ASP B 162    CG   OD1  OD2                                       
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    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG B  71   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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  15      -52.14   -129.31                                   
REMARK 500    ALA B  94     -103.89     31.97                                   
REMARK 500    ASP B 139       66.54   -106.21                                   
REMARK 500    THR B 160      159.68    -36.25                                   
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                              MG A 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   7   OD1                                                    
REMARK 620 2 HOH A 422   O    81.2                                              
REMARK 620 3 HOH A 437   O   102.2 103.3                                        
REMARK 620 4 HOH A 494   O    84.9 165.4  84.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B   7   OD1                                                    
REMARK 620 2 THR B   8   O    86.0                                              
REMARK 620 3 ASP B  96   OD1  86.4  86.3                                        
REMARK 620 4 HOH B 427   O   146.8  97.3 126.7                                  
REMARK 620 5 HOH B 432   O    82.5 167.6  88.4  94.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: SSGCID-MYTUD.18400.A   RELATED DB: TARGETTRACK           
DBREF  4HEC A    1   169  UNP    O53513   O53513_MYCTU     1    168             
DBREF  4HEC B    1   169  UNP    O53513   O53513_MYCTU     1    168             
SEQADV 4HEC MET A  -20  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC ALA A  -19  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -18  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -17  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -16  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -15  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -14  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS A  -13  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC MET A  -12  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY A  -11  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC THR A  -10  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC LEU A   -9  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLU A   -8  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC ALA A   -7  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLN A   -6  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC THR A   -5  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLN A   -4  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY A   -3  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC PRO A   -2  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY A   -1  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC SER A    0  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC VAL A    2  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC MET B  -20  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC ALA B  -19  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -18  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -17  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -16  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -15  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -14  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC HIS B  -13  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC MET B  -12  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY B  -11  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC THR B  -10  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC LEU B   -9  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLU B   -8  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC ALA B   -7  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLN B   -6  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC THR B   -5  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLN B   -4  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY B   -3  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC PRO B   -2  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC GLY B   -1  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC SER B    0  UNP  O53513              EXPRESSION TAG                 
SEQADV 4HEC VAL B    2  UNP  O53513              EXPRESSION TAG                 
SEQRES   1 A  190  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 A  190  ALA GLN THR GLN GLY PRO GLY SER MET VAL ARG TYR PHE          
SEQRES   3 A  190  TYR ASP THR GLU PHE ILE GLU ASP GLY HIS THR ILE GLU          
SEQRES   4 A  190  LEU ILE SER ILE GLY VAL VAL ALA GLU ASP GLY ARG GLU          
SEQRES   5 A  190  TYR TYR ALA VAL SER THR GLU PHE ASP PRO GLU ARG ALA          
SEQRES   6 A  190  GLY SER TRP VAL ARG THR HIS VAL LEU PRO LYS LEU PRO          
SEQRES   7 A  190  PRO PRO ALA SER GLN LEU TRP ARG SER ARG GLN GLN ILE          
SEQRES   8 A  190  ARG LEU ASP LEU GLU GLU PHE LEU ARG ILE ASP GLY THR          
SEQRES   9 A  190  ASP SER ILE GLU LEU TRP ALA TRP VAL GLY ALA TYR ASP          
SEQRES  10 A  190  HIS VAL ALA LEU CYS GLN LEU TRP GLY PRO MET THR ALA          
SEQRES  11 A  190  LEU PRO PRO THR VAL PRO ARG PHE THR ARG GLU LEU ARG          
SEQRES  12 A  190  GLN LEU TRP GLU ASP ARG GLY CYS PRO ARG MET PRO PRO          
SEQRES  13 A  190  ARG PRO ARG ASP VAL HIS ASP ALA LEU VAL ASP ALA ARG          
SEQRES  14 A  190  ASP GLN LEU ARG ARG PHE ARG LEU ILE THR SER THR ASP          
SEQRES  15 A  190  ASP ALA GLY ARG GLY ALA ALA ARG                              
SEQRES   1 B  190  MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU          
SEQRES   2 B  190  ALA GLN THR GLN GLY PRO GLY SER MET VAL ARG TYR PHE          
SEQRES   3 B  190  TYR ASP THR GLU PHE ILE GLU ASP GLY HIS THR ILE GLU          
SEQRES   4 B  190  LEU ILE SER ILE GLY VAL VAL ALA GLU ASP GLY ARG GLU          
SEQRES   5 B  190  TYR TYR ALA VAL SER THR GLU PHE ASP PRO GLU ARG ALA          
SEQRES   6 B  190  GLY SER TRP VAL ARG THR HIS VAL LEU PRO LYS LEU PRO          
SEQRES   7 B  190  PRO PRO ALA SER GLN LEU TRP ARG SER ARG GLN GLN ILE          
SEQRES   8 B  190  ARG LEU ASP LEU GLU GLU PHE LEU ARG ILE ASP GLY THR          
SEQRES   9 B  190  ASP SER ILE GLU LEU TRP ALA TRP VAL GLY ALA TYR ASP          
SEQRES  10 B  190  HIS VAL ALA LEU CYS GLN LEU TRP GLY PRO MET THR ALA          
SEQRES  11 B  190  LEU PRO PRO THR VAL PRO ARG PHE THR ARG GLU LEU ARG          
SEQRES  12 B  190  GLN LEU TRP GLU ASP ARG GLY CYS PRO ARG MET PRO PRO          
SEQRES  13 B  190  ARG PRO ARG ASP VAL HIS ASP ALA LEU VAL ASP ALA ARG          
SEQRES  14 B  190  ASP GLN LEU ARG ARG PHE ARG LEU ILE THR SER THR ASP          
SEQRES  15 B  190  ASP ALA GLY ARG GLY ALA ALA ARG                              
HET     MG  A 301       1                                                       
HET     MG  B 301       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  HOH   *220(H2 O)                                                    
HELIX    1   1 ASP A   40  ALA A   44  5                                   5    
HELIX    2   2 GLY A   45  VAL A   52  1                                   8    
HELIX    3   3 LEU A   53  LEU A   56  5                                   4    
HELIX    4   4 SER A   66  LEU A   78  1                                  13    
HELIX    5   5 GLY A   93  GLN A  102  1                                  10    
HELIX    6   6 PRO A  106  LEU A  110  5                                   5    
HELIX    7   7 LEU A  121  ARG A  128  1                                   8    
HELIX    8   8 ASP A  142  SER A  159  1                                  18    
HELIX    9   9 ASP B   40  ALA B   44  5                                   5    
HELIX   10  10 GLY B   45  VAL B   52  1                                   8    
HELIX   11  11 LEU B   53  LEU B   56  5                                   4    
HELIX   12  12 SER B   66  LEU B   78  1                                  13    
HELIX   13  13 ALA B   94  GLN B  102  1                                   9    
HELIX   14  14 LEU B  103  GLY B  105  5                                   3    
HELIX   15  15 PRO B  106  LEU B  110  5                                   5    
HELIX   16  16 LEU B  121  ARG B  128  1                                   8    
HELIX   17  17 ASP B  142  SER B  159  1                                  18    
SHEET    1   A 6 TRP A  64  ARG A  65  0                                        
SHEET    2   A 6 GLU A  31  SER A  36  1  N  VAL A  35   O  ARG A  65           
SHEET    3   A 6 ILE A  17  ALA A  26 -1  N  ILE A  20   O  SER A  36           
SHEET    4   A 6 MET A   1  GLU A  12 -1  N  ILE A  11   O  GLU A  18           
SHEET    5   A 6 SER A  85  ALA A  90  1  O  GLU A  87   N  TYR A   4           
SHEET    6   A 6 ARG A 119  GLU A 120  1  O  ARG A 119   N  LEU A  88           
SHEET    1   B 6 TRP B  64  ARG B  65  0                                        
SHEET    2   B 6 GLU B  31  SER B  36  1  N  VAL B  35   O  ARG B  65           
SHEET    3   B 6 ILE B  17  ALA B  26 -1  N  VAL B  24   O  TYR B  32           
SHEET    4   B 6 MET B   1  GLU B  12 -1  N  ILE B  11   O  GLU B  18           
SHEET    5   B 6 SER B  85  ALA B  90  1  O  TRP B  89   N  TYR B   4           
SHEET    6   B 6 ARG B 119  GLU B 120  1  O  ARG B 119   N  LEU B  88           
LINK         OD1 ASP A   7                MG    MG A 301     1555   1555  2.19  
LINK        MG    MG A 301                 O   HOH A 422     1555   1555  2.03  
LINK        MG    MG A 301                 O   HOH A 437     1555   1555  2.12  
LINK        MG    MG A 301                 O   HOH A 494     1555   1555  2.29  
LINK         OD1 ASP B   7                MG    MG B 301     1555   1555  2.60  
LINK         O   THR B   8                MG    MG B 301     1555   1555  2.29  
LINK         OD1 ASP B  96                MG    MG B 301     1555   1555  2.49  
LINK        MG    MG B 301                 O   HOH B 427     1555   1555  2.34  
LINK        MG    MG B 301                 O   HOH B 432     1555   1555  2.33  
SITE     1 AC1  5 ASP A   7  ASP A  96  HOH A 422  HOH A 437                    
SITE     2 AC1  5 HOH A 494                                                     
SITE     1 AC2  5 ASP B   7  THR B   8  ASP B  96  HOH B 427                    
SITE     2 AC2  5 HOH B 432                                                     
CRYST1   42.780   76.720  106.040  90.00  90.00  90.00 P 21 21 21    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      0.023375  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013034  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009430        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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