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Database: PDB
Entry: 4UNS
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HEADER    TRANSFERASE                             30-MAY-14   4UNS              
TITLE     MTB TMK IN COMPLEX WITH COMPOUND 40                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THYMIDYLATE KINASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-210;                                            
COMPND   5 SYNONYM: DTMP KINASE;                                                
COMPND   6 EC: 2.7.4.9;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE, ATP TMP PHOSPHOTRANSFERASE                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.READ,S.HUSSEIN,H.GINGELL,J.TUCKER                                 
REVDAT   4   10-JAN-24 4UNS    1       REMARK LINK                              
REVDAT   3   04-APR-18 4UNS    1       REMARK                                   
REVDAT   2   22-JUL-15 4UNS    1       JRNL                                     
REVDAT   1   17-JUN-15 4UNS    0                                                
JRNL        AUTH   M.NAIK,A.RAICHURKAR,B.S.BANDODKAR,B.V.VARUN,S.BHAT,          
JRNL        AUTH 2 R.KALKHAMBKAR,K.MURUGAN,R.MENON,J.BHAT,B.PAUL,H.IYER,        
JRNL        AUTH 3 S.HUSSEIN,J.A.TUCKER,M.VOGTHERR,K.J.EMBREY,H.MCMIKEN,        
JRNL        AUTH 4 S.PRASAD,A.GILL,B.G.UGARKAR,J.VENKATRAMAN,J.READ,M.PANDA     
JRNL        TITL   STRUCTURE GUIDED LEAD GENERATION FOR M. TUBERCULOSIS         
JRNL        TITL 2 THYMIDYLATE KINASE (MTB TMK): DISCOVERY OF 3-CYANOPYRIDONE   
JRNL        TITL 3 AND 1,6-NAPHTHYRIDIN-2-ONE AS POTENT INHIBITORS.             
JRNL        REF    J.MED.CHEM.                   V.  58   753 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25486447                                                     
JRNL        DOI    10.1021/JM5012947                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.18 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) : 2.18                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22586                          
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) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1217                            
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) : 2.18                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.24                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1676                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.2570                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2730                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 211                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.05                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.56000                                              
REMARK   3    B22 (A**2) : 0.56000                                              
REMARK   3    B33 (A**2) : -0.84000                                             
REMARK   3    B12 (A**2) : 0.28000                                              
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): 0.217         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.173         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.654        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2867 ; 0.011 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1825 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3910 ; 1.281 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4408 ; 0.860 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   376 ; 5.067 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   114 ;30.406 ;22.807       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   399 ;13.764 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;19.911 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   436 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3379 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   624 ; 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):  1862 ; 0.621 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   786 ; 0.116 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2903 ; 1.156 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1005 ; 1.822 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1007 ; 3.087 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   209                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5893  24.1394 -13.4736              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0234 T22:   0.0054                                     
REMARK   3      T33:   0.0260 T12:  -0.0103                                     
REMARK   3      T13:   0.0218 T23:  -0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1451 L22:   1.2466                                     
REMARK   3      L33:   1.3080 L12:   0.3138                                     
REMARK   3      L13:  -0.3695 L23:  -0.5749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0352 S12:   0.0001 S13:  -0.0336                       
REMARK   3      S21:   0.0153 S22:   0.0061 S23:   0.0088                       
REMARK   3      S31:  -0.0467 S32:   0.0021 S33:   0.0291                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   209                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1556  12.7815  13.9088              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0284 T22:   0.0444                                     
REMARK   3      T33:   0.0650 T12:   0.0079                                     
REMARK   3      T13:   0.0198 T23:   0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8098 L22:   0.9128                                     
REMARK   3      L33:   1.9156 L12:   0.7010                                     
REMARK   3      L13:  -1.3908 L23:  -0.2341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0719 S12:   0.0716 S13:   0.0901                       
REMARK   3      S21:  -0.0190 S22:   0.0245 S23:   0.0671                       
REMARK   3      S31:  -0.0530 S32:  -0.1639 S33:  -0.0964                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4UNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060814.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU CCD                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23875                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 72.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
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) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1G3U                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.87800            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       23.93900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     LEU A   145                                                      
REMARK 465     ALA A   146                                                      
REMARK 465     GLY A   147                                                      
REMARK 465     GLU A   148                                                      
REMARK 465     ARG A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     ARG A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ARG A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     GLN A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     ASP A   157                                                      
REMARK 465     PRO A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ARG A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     ASP A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     TYR A   165                                                      
REMARK 465     GLU A   166                                                      
REMARK 465     ARG A   167                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     GLY B   147                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     ARG B   149                                                      
REMARK 465     SER B   150                                                      
REMARK 465     ARG B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     ARG B   153                                                      
REMARK 465     ALA B   154                                                      
REMARK 465     GLN B   155                                                      
REMARK 465     ARG B   156                                                      
REMARK 465     ASP B   157                                                      
REMARK 465     PRO B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     ARG B   160                                                      
REMARK 465     ALA B   161                                                      
REMARK 465     ARG B   162                                                      
REMARK 465     ASP B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     TYR B   165                                                      
REMARK 465     GLU B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     PRO B   210                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  19    CE   NZ                                             
REMARK 470     LYS A 115    CD   CE   NZ                                        
REMARK 470     GLU A 144    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 170    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 202    CZ   NH1  NH2                                       
REMARK 470     ARG B  14    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 145    CG   CD1  CD2                                       
REMARK 470     ARG B 202    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B     9     O    HOH B  2005              2.11            
REMARK 500   O    HOH B  2005     O    HOH B  2008              2.16            
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    ARG A  95      140.76     72.99                                   
REMARK 500    TYR A  96     -151.28   -149.26                                   
REMARK 500    ARG B  95      143.72     75.97                                   
REMARK 500    TYR B  96     -147.35   -157.32                                   
REMARK 500    ALA B 208      130.92    -26.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2001        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH A2129        DISTANCE =  6.07 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1211  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LEU A 108   O                                                      
REMARK 620 2 HOH A2075   O    87.8                                              
REMARK 620 3 HOH A2076   O    93.1 173.7                                        
REMARK 620 4 HOH A2081   O    98.4  97.0  76.7                                  
REMARK 620 5 HOH B2035   O   178.4  93.8  85.3  81.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B1211  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2076   O                                                      
REMARK 620 2 LEU B 108   O   171.4                                              
REMARK 620 3 HOH B2035   O    92.5  93.5                                        
REMARK 620 4 HOH B2036   O    92.5  81.1 173.9                                  
REMARK 620 5 HOH B2040   O    87.6  99.2  82.6 100.9                            
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 QZ3 A 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QZ3 B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1211                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UNN   RELATED DB: PDB                                   
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 8                                   
REMARK 900 RELATED ID: 4UNP   RELATED DB: PDB                                   
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 34                                  
REMARK 900 RELATED ID: 4UNQ   RELATED DB: PDB                                   
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 36                                  
REMARK 900 RELATED ID: 4UNR   RELATED DB: PDB                                   
REMARK 900 MTB TMK IN COMPLEX WITH COMPOUND 23                                  
DBREF  4UNS A    1   210  UNP    F2GKC3   F2GKC3_MYCTX     1    210             
DBREF  4UNS B    1   210  UNP    F2GKC3   F2GKC3_MYCTX     1    210             
SEQRES   1 A  210  MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS          
SEQRES   2 A  210  ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA          
SEQRES   3 A  210  ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR          
SEQRES   4 A  210  GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU          
SEQRES   5 A  210  HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA          
SEQRES   6 A  210  MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL          
SEQRES   7 A  210  HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL          
SEQRES   8 A  210  ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER          
SEQRES   9 A  210  ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA          
SEQRES  10 A  210  ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU          
SEQRES  11 A  210  PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA          
SEQRES  12 A  210  GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG          
SEQRES  13 A  210  ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA          
SEQRES  14 A  210  GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU          
SEQRES  15 A  210  ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY          
SEQRES  16 A  210  ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA          
SEQRES  17 A  210  PRO PRO                                                      
SEQRES   1 B  210  MET LEU ILE ALA ILE GLU GLY VAL ASP GLY ALA GLY LYS          
SEQRES   2 B  210  ARG THR LEU VAL GLU LYS LEU SER GLY ALA PHE ARG ALA          
SEQRES   3 B  210  ALA GLY ARG SER VAL ALA THR LEU ALA PHE PRO ARG TYR          
SEQRES   4 B  210  GLY GLN SER VAL ALA ALA ASP ILE ALA ALA GLU ALA LEU          
SEQRES   5 B  210  HIS GLY GLU HIS GLY ASP LEU ALA SER SER VAL TYR ALA          
SEQRES   6 B  210  MET ALA THR LEU PHE ALA LEU ASP ARG ALA GLY ALA VAL          
SEQRES   7 B  210  HIS THR ILE GLN GLY LEU CYS ARG GLY TYR ASP VAL VAL          
SEQRES   8 B  210  ILE LEU ASP ARG TYR VAL ALA SER ASN ALA ALA TYR SER          
SEQRES   9 B  210  ALA ALA ARG LEU HIS GLU ASN ALA ALA GLY LYS ALA ALA          
SEQRES  10 B  210  ALA TRP VAL GLN ARG ILE GLU PHE ALA ARG LEU GLY LEU          
SEQRES  11 B  210  PRO LYS PRO ASP TRP GLN VAL LEU LEU ALA VAL SER ALA          
SEQRES  12 B  210  GLU LEU ALA GLY GLU ARG SER ARG GLY ARG ALA GLN ARG          
SEQRES  13 B  210  ASP PRO GLY ARG ALA ARG ASP ASN TYR GLU ARG ASP ALA          
SEQRES  14 B  210  GLU LEU GLN GLN ARG THR GLY ALA VAL TYR ALA GLU LEU          
SEQRES  15 B  210  ALA ALA GLN GLY TRP GLY GLY ARG TRP LEU VAL VAL GLY          
SEQRES  16 B  210  ALA ASP VAL ASP PRO GLY ARG LEU ALA ALA THR LEU ALA          
SEQRES  17 B  210  PRO PRO                                                      
HET    QZ3  A1210      27                                                       
HET     NA  A1211       1                                                       
HET    QZ3  B1210      27                                                       
HET     NA  B1211       1                                                       
HETNAM     QZ3 N-[4-(3-CYANO-7-ETHYL-5-METHYL-2-OXO-1H-1,6-                     
HETNAM   2 QZ3  NAPHTHYRIDIN-4-YL)PHENYL]METHANESULFONAMIDE                     
HETNAM      NA SODIUM ION                                                       
FORMUL   3  QZ3    2(C19 H18 N4 O3 S)                                           
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   7  HOH   *211(H2 O)                                                    
HELIX    1   1 GLY A   12  ALA A   27  1                                  16    
HELIX    2   2 SER A   42  HIS A   53  1                                  12    
HELIX    3   3 ASP A   58  SER A   61  5                                   4    
HELIX    4   4 SER A   62  ALA A   77  1                                  16    
HELIX    5   5 ALA A   77  TYR A   88  1                                  12    
HELIX    6   6 TYR A   96  LEU A  108  1                                  13    
HELIX    7   7 GLY A  114  PHE A  125  1                                  12    
HELIX    8   8 ASP A  168  GLY A  186  1                                  19    
HELIX    9   9 ASP A  199  ALA A  208  1                                  10    
HELIX   10  10 GLY B   12  ALA B   27  1                                  16    
HELIX   11  11 SER B   42  HIS B   53  1                                  12    
HELIX   12  12 ASP B   58  SER B   61  5                                   4    
HELIX   13  13 SER B   62  GLY B   76  1                                  15    
HELIX   14  14 ALA B   77  TYR B   88  1                                  12    
HELIX   15  15 TYR B   96  LEU B  108  1                                  13    
HELIX   16  16 GLY B  114  PHE B  125  1                                  12    
HELIX   17  17 ASP B  168  GLY B  186  1                                  19    
HELIX   18  18 ASP B  199  ALA B  208  1                                  10    
SHEET    1  AA 5 VAL A  31  ALA A  35  0                                        
SHEET    2  AA 5 VAL A  90  ASP A  94  1  O  VAL A  90   N  ALA A  32           
SHEET    3  AA 5 LEU A   2  GLU A   6  1  O  ILE A   3   N  LEU A  93           
SHEET    4  AA 5 TRP A 135  LEU A 139  1  O  TRP A 135   N  ALA A   4           
SHEET    5  AA 5 ARG A 190  VAL A 194  1  O  ARG A 190   N  GLN A 136           
SHEET    1  BA 5 VAL B  31  ALA B  35  0                                        
SHEET    2  BA 5 VAL B  90  ASP B  94  1  O  VAL B  90   N  ALA B  32           
SHEET    3  BA 5 LEU B   2  GLU B   6  1  O  ILE B   3   N  LEU B  93           
SHEET    4  BA 5 TRP B 135  LEU B 139  1  O  TRP B 135   N  ALA B   4           
SHEET    5  BA 5 ARG B 190  VAL B 194  1  O  ARG B 190   N  GLN B 136           
LINK         O   LEU A 108                NA    NA A1211     1555   1555  2.48  
LINK        NA    NA A1211                 O   HOH A2075     1555   1555  2.31  
LINK        NA    NA A1211                 O   HOH A2076     1555   1555  2.48  
LINK        NA    NA A1211                 O   HOH A2081     1555   1555  2.84  
LINK        NA    NA A1211                 O   HOH B2035     1555   2554  2.63  
LINK         O   HOH A2076                NA    NA B1211     3555   1555  2.47  
LINK         O   LEU B 108                NA    NA B1211     1555   1555  2.43  
LINK        NA    NA B1211                 O   HOH B2035     1555   1555  2.32  
LINK        NA    NA B1211                 O   HOH B2036     1555   1555  2.33  
LINK        NA    NA B1211                 O   HOH B2040     1555   1555  2.58  
CISPEP   1 PHE A   36    PRO A   37          0        -6.09                     
CISPEP   2 PHE B   36    PRO B   37          0        -2.50                     
SITE     1 AC1 14 ASP A   9  PRO A  37  TYR A  39  MET A  66                    
SITE     2 AC1 14 PHE A  70  ARG A  74  ARG A  95  ASN A 100                    
SITE     3 AC1 14 TYR A 103  ARG A 107  HOH A2014  HOH A2045                    
SITE     4 AC1 14 HOH A2127  HOH A2128                                          
SITE     1 AC2 10 ASP B   9  PRO B  37  TYR B  39  MET B  66                    
SITE     2 AC2 10 PHE B  70  ARG B  74  ARG B  95  ASN B 100                    
SITE     3 AC2 10 TYR B 103  HOH B2005                                          
SITE     1 AC3  6 LEU A 108  HOH A2075  HOH A2076  HOH A2081                    
SITE     2 AC3  6  NA B1211  HOH B2035                                          
SITE     1 AC4  6  NA A1211  HOH A2076  LEU B 108  HOH B2035                    
SITE     2 AC4  6 HOH B2036  HOH B2040                                          
CRYST1   75.513   75.513   71.817  90.00  90.00 120.00 P 32          6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013243  0.007646  0.000000        0.00000                         
SCALE2      0.000000  0.015291  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013924        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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