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Database: PDB
Entry: 1VS0
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HEADER    LIGASE                                  27-JAN-06   1VS0              
TITLE     CRYSTAL STRUCTURE OF THE LIGASE DOMAIN FROM M. TUBERCULOSIS LIGD AT   
TITLE    2 2.4A                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN RV0938/MT0965;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGD LIGASE DOMAIN;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: ADENYLATED FORM                                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RV0938, MT0965;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PLYSS;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PAEB1120;                                 
SOURCE  11 OTHER_DETAILS: TEV CLEAVABLE HIS TAG                                 
KEYWDS    LIGASE; OB FOLD; NUCLEOTIDYL TRANSFERASE, STRUCTURAL GENOMICS, PSI,   
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM,     
KEYWDS   3 TBSGC, LIGASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.AKEY,A.MARTINS,J.ANIUKWU,M.S.GLICKMAN,S.SHUMAN,J.M.BERGER,TB        
AUTHOR   2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)                               
REVDAT   4   13-JUL-11 1VS0    1       VERSN                                    
REVDAT   3   24-FEB-09 1VS0    1       VERSN                                    
REVDAT   2   23-MAY-06 1VS0    1       JRNL                                     
REVDAT   1   28-FEB-06 1VS0    0                                                
JRNL        AUTH   D.AKEY,A.MARTINS,J.ANIUKWU,M.S.GLICKMAN,S.SHUMAN,J.M.BERGER  
JRNL        TITL   CRYSTAL STRUCTURE AND NONHOMOLOGOUS END-JOINING FUNCTION OF  
JRNL        TITL 2 THE LIGASE COMPONENT OF MYCOBACTERIUM DNA LIGASE D.          
JRNL        REF    J.BIOL.CHEM.                  V. 281 13412 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16476729                                                     
JRNL        DOI    10.1074/JBC.M513550200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 28487                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1453                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1894                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 111                          
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4777                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 407                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.01000                                              
REMARK   3    B22 (A**2) : 1.01000                                              
REMARK   3    B33 (A**2) : -1.52000                                             
REMARK   3    B12 (A**2) : 0.51000                                              
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): 0.414         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.264         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.811        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.942                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4881 ; 0.014 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6636 ; 1.600 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   616 ; 6.814 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;38.015 ;22.466       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   770 ;18.654 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;19.204 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   706 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3793 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2107 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3226 ; 0.311 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   366 ; 0.213 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     7 ; 0.309 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   131 ; 0.268 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    29 ; 0.352 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     7 ; 0.137 ; 0.200       
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):  3090 ; 2.497 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4836 ; 3.715 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2060 ; 2.281 ; 3.500       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1799 ; 3.070 ; 3.500       
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  : 4                                          
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   453        A   638                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6077  52.9960 125.3335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0623 T22:  -0.0758                                     
REMARK   3      T33:  -0.0200 T12:   0.0325                                     
REMARK   3      T13:   0.0163 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1221 L22:   0.7415                                     
REMARK   3      L33:   1.2200 L12:  -0.0542                                     
REMARK   3      L13:  -0.0150 L23:   0.3666                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0183 S12:   0.0440 S13:   0.0243                       
REMARK   3      S21:   0.0298 S22:  -0.0600 S23:   0.0111                       
REMARK   3      S31:   0.0060 S32:  -0.0271 S33:   0.0783                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   639        A   759                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.7849  75.2068 154.8358              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1044 T22:  -0.1325                                     
REMARK   3      T33:  -0.0717 T12:  -0.0521                                     
REMARK   3      T13:   0.0742 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0544 L22:   2.2426                                     
REMARK   3      L33:   1.9458 L12:  -0.3731                                     
REMARK   3      L13:  -0.2359 L23:   1.9652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0753 S12:   0.0073 S13:   0.0316                       
REMARK   3      S21:   0.4854 S22:  -0.1455 S23:   0.0148                       
REMARK   3      S31:   0.3277 S32:   0.0836 S33:   0.0702                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   453        B   638                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.6871  55.7937 188.1162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0798 T22:  -0.1107                                     
REMARK   3      T33:  -0.0869 T12:  -0.1443                                     
REMARK   3      T13:   0.0624 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8818 L22:   0.8552                                     
REMARK   3      L33:   1.1395 L12:   1.1439                                     
REMARK   3      L13:  -0.6549 L23:  -0.0163                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1567 S12:  -0.0956 S13:   0.0424                       
REMARK   3      S21:   0.1717 S22:  -0.0896 S23:   0.0762                       
REMARK   3      S31:   0.0074 S32:   0.1108 S33:  -0.0671                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   639        B   759                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9281  42.1284 214.3944              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0295 T22:  -0.0626                                     
REMARK   3      T33:  -0.0620 T12:  -0.0530                                     
REMARK   3      T13:   0.0234 T23:  -0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4184 L22:   1.0467                                     
REMARK   3      L33:   2.8564 L12:   0.3464                                     
REMARK   3      L13:   0.0470 L23:   0.0461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0112 S12:  -0.0464 S13:  -0.0930                       
REMARK   3      S21:  -0.1261 S22:   0.0697 S23:   0.0411                       
REMARK   3      S31:  -0.1768 S32:   0.0775 S33:  -0.0809                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1VS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036341.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796, 1.020, 0.9798              
REMARK 200  MONOCHROMATOR                  : ALS BEAMLINE 8.3.1                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : BLU-ICE                            
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28772                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.35000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3000, 25 MM ZNCL2, 100 MM         
REMARK 280  SODIUM ACETATE (PH 4.6), VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      245.97133            
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      122.98567            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      122.98567            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      245.97133            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER. THERE ARE TWO          
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.                                     
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 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 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     GLY A   450                                                      
REMARK 465     ALA A   451                                                      
REMARK 465     VAL A   452                                                      
REMARK 465     GLY A   652                                                      
REMARK 465     GLU A   653                                                      
REMARK 465     GLY A   654                                                      
REMARK 465     GLY A   655                                                      
REMARK 465     ARG A   656                                                      
REMARK 465     SER A   657                                                      
REMARK 465     SER A   658                                                      
REMARK 465     GLY A   659                                                      
REMARK 465     GLY B   450                                                      
REMARK 465     ALA B   451                                                      
REMARK 465     VAL B   452                                                      
REMARK 465     GLY B   655                                                      
REMARK 465     ARG B   656                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  472   CD   CE   NZ                                        
REMARK 480     ARG A  504   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG A  550   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG A  712   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  715   CD   CE   NZ                                        
REMARK 480     LYS A  721   CD   CE   NZ                                        
REMARK 480     GLU B  454   CD   OE1  OE2                                       
REMARK 480     LYS B  472   CE   NZ                                             
REMARK 480     ARG B  504   NE   CZ   NH1  NH2                                  
REMARK 480     ARG B  550   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG B  623   NE   CZ   NH1  NH2                                  
REMARK 480     ARG B  628   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU B  653   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU B  685   CG   CD   OE1  OE2                                  
REMARK 480     ARG B  686   NE   CZ   NH1  NH2                                  
REMARK 480     GLU B  693   CD   OE1  OE2                                       
REMARK 480     ARG B  712   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   OE2  GLU A   582     O    HOH A  9022              1.88            
REMARK 500   N    PHE B   453     O    HOH B  9083              2.08            
REMARK 500   ND1  HIS A   524     O    HOH A  9220              2.16            
REMARK 500   O    HOH A  9065     O    HOH A  9166              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OD2  ASP A   456     OD2  ASP B   701     2674     1.94            
REMARK 500  CL     CL B  9008     O    HOH B  9178     4456     1.99            
REMARK 500   OD2  ASP A   456     OD2  ASP A   750     6655     2.06            
REMARK 500   O    HOH B  9037     O    HOH B  9124     4566     2.16            
REMARK 500  CL     CL A  9007     O    HOH A  9220     6665     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 550   CB    ARG A 550   CG      0.262                       
REMARK 500    GLU B 454   CG    GLU B 454   CD     -0.136                       
REMARK 500    LYS B 472   CD    LYS B 472   CE     -0.444                       
REMARK 500    ARG B 504   CD    ARG B 504   NE     -0.530                       
REMARK 500    ARG B 628   CG    ARG B 628   CD     -0.210                       
REMARK 500    ARG B 686   CD    ARG B 686   NE      0.179                       
REMARK 500    GLU B 693   CG    GLU B 693   CD     -0.184                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS B 472   CG  -  CD  -  CE  ANGL. DEV. =  36.5 DEGREES          
REMARK 500    LYS B 472   CD  -  CE  -  NZ  ANGL. DEV. =  32.3 DEGREES          
REMARK 500    ARG B 504   CG  -  CD  -  NE  ANGL. DEV. =  40.6 DEGREES          
REMARK 500    ARG B 504   CD  -  NE  -  CZ  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    VAL B 679   CB  -  CA  -  C   ANGL. DEV. = -12.2 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    SER A 731      -75.13    -85.41                                   
REMARK 500    ALA B 473      -27.16    -39.28                                   
REMARK 500    ASP B 535      178.56    -36.19                                   
REMARK 500    ARG B 548      117.49    -36.49                                   
REMARK 500    ARG B 550       24.16    -74.64                                   
REMARK 500    SER B 731      -80.45   -100.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 480         19.66                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP A 456        24.6      L          L   OUTSIDE RANGE           
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 A9083        DISTANCE =  5.03 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                              ZN A9002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APK A 481   O1P                                                    
REMARK 620 2 ASP A 483   OD1  90.4                                              
REMARK 620 3 ASP A 483   OD2 145.3  55.8                                        
REMARK 620 4 GLU A 613   OE1 137.3 125.4  76.2                                  
REMARK 620 5 GLU A 613   OE2 101.1  99.3  92.9  55.4                            
REMARK 620 6 ASP A 522   OD2 103.4 101.1  78.5  92.4 147.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A9004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  CL A9007  CL                                                      
REMARK 620 2 GLU A 727   OE1 114.2                                              
REMARK 620 3 ASP A 492   OD1 114.0 102.3                                        
REMARK 620 4 HIS A 493   ND1 106.4 122.4  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A9009  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 454   OE2                                                    
REMARK 620 2 GLU A 454   OE1  58.3                                              
REMARK 620 3 ASP B 701   OD2  87.2 129.0                                        
REMARK 620 4 HIS B 699   NE2 143.7  87.2 126.7                                  
REMARK 620 5 ASP A 750   OD1 123.6 106.0  60.8  73.3                            
REMARK 620 6 ASP B 701   OD1  94.3 152.3  44.2 118.6  92.1                      
REMARK 620 7 ASP A 750   OD2  72.5  74.8  58.6 111.5  51.5 102.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 APK B 481   O1P                                                    
REMARK 620 2 GLU B 613   OE2  84.4                                              
REMARK 620 3 ASP B 483   OD2  99.4 105.1                                        
REMARK 620 4 ASP B 483   OD1 148.2 112.7  51.3                                  
REMARK 620 5 ASP B 522   OD2 106.0 137.2 113.6  80.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B9003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 727   OE2                                                    
REMARK 620 2 GLU B 727   OE1  53.9                                              
REMARK 620 3  CL B9008  CL    87.6 113.2                                        
REMARK 620 4 HIS B 493   ND1  90.4 124.3 104.9                                  
REMARK 620 5 ASP B 492   OD2 161.0 107.1 103.4 101.4                            
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 ZN B 9001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 9002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 9003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 9004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 9005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 9006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 9007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 9008                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 9009                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: RV0938   RELATED DB: TARGETDB                            
DBREF  1VS0 A  452   759  UNP    P71571   Y938_MYCTU     452    759             
DBREF  1VS0 B  452   759  UNP    P71571   Y938_MYCTU     452    759             
SEQADV 1VS0 GLY A  450  UNP  P71571              CLONING ARTIFACT               
SEQADV 1VS0 ALA A  451  UNP  P71571              CLONING ARTIFACT               
SEQADV 1VS0 MSE A  461  UNP  P71571    MET   461 MODIFIED RESIDUE               
SEQADV 1VS0 APK A  481  UNP  P71571    LYS   481 MODIFIED RESIDUE               
SEQADV 1VS0 MSE A  545  UNP  P71571    MET   545 MODIFIED RESIDUE               
SEQADV 1VS0 MSE A  665  UNP  P71571    MET   665 MODIFIED RESIDUE               
SEQADV 1VS0 MSE A  694  UNP  P71571    MET   694 MODIFIED RESIDUE               
SEQADV 1VS0 GLY B  450  UNP  P71571              CLONING ARTIFACT               
SEQADV 1VS0 ALA B  451  UNP  P71571              CLONING ARTIFACT               
SEQADV 1VS0 MSE B  461  UNP  P71571    MET   461 MODIFIED RESIDUE               
SEQADV 1VS0 APK B  481  UNP  P71571    LYS   481 MODIFIED RESIDUE               
SEQADV 1VS0 MSE B  545  UNP  P71571    MET   545 MODIFIED RESIDUE               
SEQADV 1VS0 MSE B  665  UNP  P71571    MET   665 MODIFIED RESIDUE               
SEQADV 1VS0 MSE B  694  UNP  P71571    MET   694 MODIFIED RESIDUE               
SEQRES   1 A  310  GLY ALA VAL PHE GLU PHE ASP ASN LEU ALA PRO MSE LEU          
SEQRES   2 A  310  ALA THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN          
SEQRES   3 A  310  TRP ALA PHE GLU GLY APK TRP ASP GLY TYR ARG LEU LEU          
SEQRES   4 A  310  VAL GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG          
SEQRES   5 A  310  SER GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG          
SEQRES   6 A  310  ALA LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU          
SEQRES   7 A  310  ASP GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO          
SEQRES   8 A  310  SER PHE SER GLN MSE GLN ASN ARG GLY ARG ASP THR ARG          
SEQRES   9 A  310  VAL GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY          
SEQRES  10 A  310  ARG ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS          
SEQRES  11 A  310  LEU LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL          
SEQRES  12 A  310  PRO GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA          
SEQRES  13 A  310  CYS SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS          
SEQRES  14 A  310  ARG ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA          
SEQRES  15 A  310  SER TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL          
SEQRES  16 A  310  VAL ILE GLY GLY TRP ARG ALA GLY GLU GLY GLY ARG SER          
SEQRES  17 A  310  SER GLY VAL GLY SER LEU LEU MSE GLY ILE PRO GLY PRO          
SEQRES  18 A  310  GLY GLY LEU GLN PHE ALA GLY ARG VAL GLY THR GLY LEU          
SEQRES  19 A  310  SER GLU ARG GLU LEU ALA ASN LEU LYS GLU MSE LEU ALA          
SEQRES  20 A  310  PRO LEU HIS THR ASP GLU SER PRO PHE ASP VAL PRO LEU          
SEQRES  21 A  310  PRO ALA ARG ASP ALA LYS GLY ILE THR TYR VAL LYS PRO          
SEQRES  22 A  310  ALA LEU VAL ALA GLU VAL ARG TYR SER GLU TRP THR PRO          
SEQRES  23 A  310  GLU GLY ARG LEU ARG GLN SER SER TRP ARG GLY LEU ARG          
SEQRES  24 A  310  PRO ASP LYS LYS PRO SER GLU VAL VAL ARG GLU                  
SEQRES   1 B  310  GLY ALA VAL PHE GLU PHE ASP ASN LEU ALA PRO MSE LEU          
SEQRES   2 B  310  ALA THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN          
SEQRES   3 B  310  TRP ALA PHE GLU GLY APK TRP ASP GLY TYR ARG LEU LEU          
SEQRES   4 B  310  VAL GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG          
SEQRES   5 B  310  SER GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG          
SEQRES   6 B  310  ALA LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU          
SEQRES   7 B  310  ASP GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO          
SEQRES   8 B  310  SER PHE SER GLN MSE GLN ASN ARG GLY ARG ASP THR ARG          
SEQRES   9 B  310  VAL GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY          
SEQRES  10 B  310  ARG ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS          
SEQRES  11 B  310  LEU LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL          
SEQRES  12 B  310  PRO GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA          
SEQRES  13 B  310  CYS SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS          
SEQRES  14 B  310  ARG ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA          
SEQRES  15 B  310  SER TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL          
SEQRES  16 B  310  VAL ILE GLY GLY TRP ARG ALA GLY GLU GLY GLY ARG SER          
SEQRES  17 B  310  SER GLY VAL GLY SER LEU LEU MSE GLY ILE PRO GLY PRO          
SEQRES  18 B  310  GLY GLY LEU GLN PHE ALA GLY ARG VAL GLY THR GLY LEU          
SEQRES  19 B  310  SER GLU ARG GLU LEU ALA ASN LEU LYS GLU MSE LEU ALA          
SEQRES  20 B  310  PRO LEU HIS THR ASP GLU SER PRO PHE ASP VAL PRO LEU          
SEQRES  21 B  310  PRO ALA ARG ASP ALA LYS GLY ILE THR TYR VAL LYS PRO          
SEQRES  22 B  310  ALA LEU VAL ALA GLU VAL ARG TYR SER GLU TRP THR PRO          
SEQRES  23 B  310  GLU GLY ARG LEU ARG GLN SER SER TRP ARG GLY LEU ARG          
SEQRES  24 B  310  PRO ASP LYS LYS PRO SER GLU VAL VAL ARG GLU                  
MODRES 1VS0 MSE A  461  MET  SELENOMETHIONINE                                   
MODRES 1VS0 APK A  481  LYS                                                     
MODRES 1VS0 MSE A  545  MET  SELENOMETHIONINE                                   
MODRES 1VS0 MSE A  665  MET  SELENOMETHIONINE                                   
MODRES 1VS0 MSE A  694  MET  SELENOMETHIONINE                                   
MODRES 1VS0 MSE B  461  MET  SELENOMETHIONINE                                   
MODRES 1VS0 APK B  481  LYS                                                     
MODRES 1VS0 MSE B  545  MET  SELENOMETHIONINE                                   
MODRES 1VS0 MSE B  665  MET  SELENOMETHIONINE                                   
MODRES 1VS0 MSE B  694  MET  SELENOMETHIONINE                                   
HET    MSE  A 461       8                                                       
HET    APK  A 481      31                                                       
HET    MSE  A 545       8                                                       
HET    MSE  A 665       8                                                       
HET    MSE  A 694       8                                                       
HET    MSE  B 461       8                                                       
HET    APK  B 481      31                                                       
HET    MSE  B 545       8                                                       
HET    MSE  B 665       8                                                       
HET    MSE  B 694      16                                                       
HET     ZN  B9001       1                                                       
HET     ZN  A9002       1                                                       
HET     ZN  B9003       1                                                       
HET     ZN  A9004       1                                                       
HET     CL  A9005       1                                                       
HET     CL  B9006       1                                                       
HET     CL  A9007       1                                                       
HET     CL  B9008       1                                                       
HET     MG  A9009       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     APK 5'-O-[(S)-{[(5S)-5-AMINO-6-OXOHEXYL]AMINO}(HYDROXY)              
HETNAM   2 APK  PHOSPHORYL]ADENOSINE                                            
HETNAM      ZN ZINC ION                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   1  APK    2(C16 H26 N7 O7 P)                                           
FORMUL   3   ZN    4(ZN 2+)                                                     
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  11   MG    MG 2+                                                        
FORMUL  12  HOH   *407(H2 O)                                                    
HELIX    1   1 GLU A  454  LEU A  458  5                                   5    
HELIX    2   2 VAL A  506  GLN A  512  5                                   7    
HELIX    3   3 LEU A  513  LEU A  520  1                                   8    
HELIX    4   4 SER A  541  ASN A  547  1                                   7    
HELIX    5   5 ARG A  573  THR A  588  1                                  16    
HELIX    6   6 ASP A  599  HIS A  610  1                                  12    
HELIX    7   7 SER A  684  ALA A  696  1                                  13    
HELIX    8   8 PRO A  697  HIS A  699  5                                   3    
HELIX    9   9 PRO A  710  LYS A  715  1                                   6    
HELIX   10  10 LYS A  752  VAL A  756  5                                   5    
HELIX   11  11 GLU B  454  LEU B  458  5                                   5    
HELIX   12  12 VAL B  506  GLN B  512  5                                   7    
HELIX   13  13 LEU B  513  LEU B  520  1                                   8    
HELIX   14  14 SER B  541  ASN B  547  1                                   7    
HELIX   15  15 ARG B  573  THR B  588  1                                  16    
HELIX   16  16 ASP B  599  GLY B  611  1                                  13    
HELIX   17  17 SER B  684  ALA B  696  1                                  13    
HELIX   18  18 PRO B  710  LYS B  715  1                                   6    
HELIX   19  19 LYS B  752  VAL B  756  5                                   5    
SHEET    1   A 4 LEU A 462  HIS A 465  0                                        
SHEET    2   A 4 ARG A 629  LYS A 637  1  O  TRP A 633   N  THR A 464           
SHEET    3   A 4 GLY A 614  ARG A 619 -1  N  ALA A 617   O  VAL A 634           
SHEET    4   A 4 TRP A 476  APK A 481 -1  N  GLU A 479   O  ILE A 616           
SHEET    1   B 5 ALA A 495  SER A 500  0                                        
SHEET    2   B 5 TYR A 485  ASP A 492 -1  N  GLU A 490   O  ARG A 497           
SHEET    3   B 5 HIS A 524  VAL A 532 -1  O  ALA A 531   N  TYR A 485           
SHEET    4   B 5 GLU A 555  LEU A 564 -1  O  LEU A 562   N  VAL A 526           
SHEET    5   B 5 ARG A 567  ALA A 568 -1  O  ARG A 567   N  LEU A 564           
SHEET    1   C 4 GLY A 672  VAL A 679  0                                        
SHEET    2   C 4 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3   C 4 ASN A 640  ARG A 650 -1  N  GLY A 647   O  LEU A 664           
SHEET    4   C 4 ILE A 717  TYR A 719 -1  O  THR A 718   N  TRP A 649           
SHEET    1   D 5 GLY A 672  VAL A 679  0                                        
SHEET    2   D 5 SER A 662  GLY A 669 -1  N  ILE A 667   O  GLN A 674           
SHEET    3   D 5 ASN A 640  ARG A 650 -1  N  GLY A 647   O  LEU A 664           
SHEET    4   D 5 VAL A 725  TYR A 730 -1  O  TYR A 730   N  ASN A 640           
SHEET    5   D 5 SER A 743  LEU A 747 -1  O  SER A 743   N  ARG A 729           
SHEET    1   E 4 LEU B 462  HIS B 465  0                                        
SHEET    2   E 4 ARG B 629  LYS B 637  1  O  LYS B 635   N  THR B 464           
SHEET    3   E 4 GLY B 614  ARG B 619 -1  N  ALA B 617   O  VAL B 634           
SHEET    4   E 4 TRP B 476  GLU B 479 -1  N  ALA B 477   O  LYS B 618           
SHEET    1   F 5 ALA B 495  SER B 500  0                                        
SHEET    2   F 5 TYR B 485  ASP B 492 -1  N  GLU B 490   O  ARG B 497           
SHEET    3   F 5 HIS B 524  VAL B 532 -1  O  ALA B 531   N  TYR B 485           
SHEET    4   F 5 GLU B 555  LEU B 564 -1  O  LEU B 562   N  VAL B 526           
SHEET    5   F 5 ARG B 567  ALA B 568 -1  O  ARG B 567   N  LEU B 564           
SHEET    1   G 5 GLY B 672  VAL B 679  0                                        
SHEET    2   G 5 VAL B 660  GLY B 669 -1  N  MSE B 665   O  ALA B 676           
SHEET    3   G 5 ASN B 640  ALA B 651 -1  N  VAL B 645   O  GLY B 666           
SHEET    4   G 5 ILE B 717  VAL B 720 -1  O  THR B 718   N  TRP B 649           
SHEET    5   G 5 HIS B 699  THR B 700 -1  N  THR B 700   O  TYR B 719           
SHEET    1   H 5 GLY B 672  VAL B 679  0                                        
SHEET    2   H 5 VAL B 660  GLY B 669 -1  N  MSE B 665   O  ALA B 676           
SHEET    3   H 5 ASN B 640  ALA B 651 -1  N  VAL B 645   O  GLY B 666           
SHEET    4   H 5 VAL B 725  TYR B 730 -1  O  TYR B 730   N  ASN B 640           
SHEET    5   H 5 SER B 743  LEU B 747 -1  O  GLY B 746   N  GLU B 727           
LINK         C   PRO A 460                 N   MSE A 461     1555   1555  1.33  
LINK         C   MSE A 461                 N   LEU A 462     1555   1555  1.33  
LINK         C   GLY A 480                 N   APK A 481     1555   1555  1.57  
LINK         C   APK A 481                 N   TRP A 482     1555   1555  1.75  
LINK         O1P APK A 481                ZN    ZN A9002     1555   1555  1.97  
LINK         C   GLN A 544                 N   MSE A 545     1555   1555  1.34  
LINK         C   MSE A 545                 N   GLN A 546     1555   1555  1.32  
LINK         C   LEU A 664                 N   MSE A 665     1555   1555  1.33  
LINK         C   MSE A 665                 N   GLY A 666     1555   1555  1.32  
LINK         C   GLU A 693                 N   MSE A 694     1555   1555  1.33  
LINK         C   MSE A 694                 N   LEU A 695     1555   1555  1.33  
LINK        ZN    ZN A9002                 OD1 ASP A 483     1555   1555  2.15  
LINK        ZN    ZN A9002                 OD2 ASP A 483     1555   1555  2.46  
LINK        ZN    ZN A9002                 OE1 GLU A 613     1555   1555  2.30  
LINK        ZN    ZN A9002                 OE2 GLU A 613     1555   1555  2.41  
LINK        ZN    ZN A9004                CL    CL A9007     1555   1555  2.24  
LINK        ZN    ZN A9004                 OE1 GLU A 727     1555   1555  1.91  
LINK        MG    MG A9009                 OE2 GLU A 454     1555   1555  2.26  
LINK        MG    MG A9009                 OE1 GLU A 454     1555   1555  2.23  
LINK         C   PRO B 460                 N   MSE B 461     1555   1555  1.33  
LINK         C   MSE B 461                 N   LEU B 462     1555   1555  1.33  
LINK         C   GLY B 480                 N   APK B 481     1555   1555  1.81  
LINK         O1P APK B 481                ZN    ZN B9001     1555   1555  1.90  
LINK         C   APK B 481                 N   TRP B 482     1555   1555  1.71  
LINK         C   GLN B 544                 N   MSE B 545     1555   1555  1.33  
LINK         C   MSE B 545                 N   GLN B 546     1555   1555  1.31  
LINK         C   LEU B 664                 N   MSE B 665     1555   1555  1.33  
LINK         C   MSE B 665                 N   GLY B 666     1555   1555  1.33  
LINK         C   GLU B 693                 N  BMSE B 694     1555   1555  1.33  
LINK         C   GLU B 693                 N  AMSE B 694     1555   1555  1.33  
LINK         C  AMSE B 694                 N   LEU B 695     1555   1555  1.33  
LINK         C  BMSE B 694                 N   LEU B 695     1555   1555  1.33  
LINK        ZN    ZN B9001                 OE2 GLU B 613     1555   1555  1.69  
LINK        ZN    ZN B9001                 OD2 ASP B 483     1555   1555  2.16  
LINK        ZN    ZN B9001                 OD1 ASP B 483     1555   1555  2.76  
LINK        ZN    ZN B9003                 OE2 GLU B 727     1555   1555  2.61  
LINK        ZN    ZN B9003                 OE1 GLU B 727     1555   1555  2.11  
LINK        ZN    ZN B9003                CL    CL B9008     1555   1555  1.89  
LINK        ZN    ZN A9002                 OD2 ASP A 522     1555   6665  2.00  
LINK        ZN    ZN A9004                 OD1 ASP A 492     1555   6665  1.91  
LINK        ZN    ZN A9004                 ND1 HIS A 493     1555   6665  2.02  
LINK        MG    MG A9009                 OD2 ASP B 701     1555   2674  3.11  
LINK        MG    MG A9009                 NE2 HIS B 699     1555   2674  1.97  
LINK        MG    MG A9009                 OD1 ASP A 750     1555   6655  2.57  
LINK        MG    MG A9009                 OD1 ASP B 701     1555   2674  1.91  
LINK        MG    MG A9009                 OD2 ASP A 750     1555   6655  2.43  
LINK        ZN    ZN B9001                 OD2 ASP B 522     1555   4456  1.94  
LINK        ZN    ZN B9003                 ND1 HIS B 493     1555   4456  2.12  
LINK        ZN    ZN B9003                 OD2 ASP B 492     1555   4456  1.93  
SITE     1 AC1  4 APK B 481  ASP B 483  ASP B 522  GLU B 613                    
SITE     1 AC2  4 APK A 481  ASP A 483  ASP A 522  GLU A 613                    
SITE     1 AC3  4 ASP B 492  HIS B 493  GLU B 727   CL B9008                    
SITE     1 AC4  4 ASP A 492  HIS A 493  GLU A 727   CL A9007                    
SITE     1 AC5  4 ALA A 463  APK A 481  LYS A 635  HOH A9163                    
SITE     1 AC6  4 ALA B 463  APK B 481  HOH B9118  HOH B9188                    
SITE     1 AC7  6 ASP A 492  HIS A 493  GLU A 727  ARG A 748                    
SITE     2 AC7  6  ZN A9004  HOH A9220                                          
SITE     1 AC8  7 ASP B 492  HIS B 493  HIS B 524  GLU B 727                    
SITE     2 AC8  7 ARG B 748   ZN B9003  HOH B9178                               
SITE     1 AC9  5 GLU A 454  ASP A 456  ASP A 750  HIS B 699                    
SITE     2 AC9  5 ASP B 701                                                     
CRYST1   57.102   57.102  368.957  90.00  90.00 120.00 P 32 2 1     12          
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      0.017510  0.010110  0.000000        0.00000                         
SCALE2      0.000000  0.020220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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