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Database: PDB
Entry: 5D6J
LinkDB: 5D6J
Original site: 5D6J 
HEADER    LIGASE/PROTEIN BINDING                  12-AUG-15   5D6J              
TITLE     CRYSTAL STRUCTURE OF A MYCOBACTERIAL PROTEIN                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-COA SYNTHASE;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FATTY-ACID-COA LIGASE FADD32;                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: UBIQUITIN-LIKE PROTEIN SMT3;                               
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 21-94;                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /   
SOURCE   3 MC(2)155);                                                           
SOURCE   4 ORGANISM_TAXID: 246196;                                              
SOURCE   5 STRAIN: ATCC 700084 / MC(2)155;                                      
SOURCE   6 GENE: FADD32, MSMEG_6393, MSMEI_6225;                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  11 S288C);                                                              
SOURCE  12 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  13 ORGANISM_TAXID: 559292;                                              
SOURCE  14 STRAIN: ATCC 204508 / S288C;                                         
SOURCE  15 GENE: SMT3, YDR510W, D9719.15;                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MYCOBACTERIUM SMEGMATIS, LIGASE-PROTEIN BINDING COMPLEX               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.J.LI,L.J.BI                                                         
REVDAT   1   02-MAR-16 5D6J    0                                                
JRNL        AUTH   W.LI,S.GU,J.FLEMING,L.BI                                     
JRNL        TITL   CRYSTAL STRUCTURE OF FADD32, AN ENZYME ESSENTIAL FOR MYCOLIC 
JRNL        TITL 2 ACID BIOSYNTHESIS IN MYCOBACTERIA.                           
JRNL        REF    SCI REP                       V.   5 15493 2015              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   26628098                                                     
JRNL        DOI    10.1038/SREP15493                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 51768                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.840                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1986                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9878 -  5.4130    1.00     3813   153  0.1519 0.1551        
REMARK   3     2  5.4130 -  4.3005    1.00     3638   144  0.1357 0.1550        
REMARK   3     3  4.3005 -  3.7581    1.00     3586   143  0.1432 0.1735        
REMARK   3     4  3.7581 -  3.4150    1.00     3575   143  0.1653 0.2064        
REMARK   3     5  3.4150 -  3.1705    1.00     3557   142  0.1826 0.2523        
REMARK   3     6  3.1705 -  2.9838    1.00     3517   140  0.1924 0.2201        
REMARK   3     7  2.9838 -  2.8345    1.00     3542   141  0.1941 0.2589        
REMARK   3     8  2.8345 -  2.7112    1.00     3527   141  0.1907 0.2347        
REMARK   3     9  2.7112 -  2.6068    1.00     3500   139  0.1886 0.2259        
REMARK   3    10  2.6068 -  2.5169    1.00     3538   142  0.1903 0.2639        
REMARK   3    11  2.5169 -  2.4383    1.00     3486   139  0.2026 0.2780        
REMARK   3    12  2.4383 -  2.3686    1.00     3500   139  0.2005 0.2737        
REMARK   3    13  2.3686 -  2.3063    1.00     3491   140  0.2062 0.2635        
REMARK   3    14  2.3063 -  2.2500    1.00     3512   140  0.2163 0.2941        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           5588                                  
REMARK   3   ANGLE     :  0.951           7610                                  
REMARK   3   CHIRALITY :  0.037            838                                  
REMARK   3   PLANARITY :  0.004           1010                                  
REMARK   3   DIHEDRAL  : 13.844           2049                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5D6J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000212744.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97928                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.30                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.55700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM MALONATE, 20% PEG 3350,     
REMARK 280  EVAPORATION, TEMPERATURE 281K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.29400            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       61.10550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       61.10550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      106.94100            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       61.10550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       61.10550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       35.64700            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       61.10550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.10550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      106.94100            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       61.10550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.10550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.64700            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       71.29400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ALA A 593    CB                                                  
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 A   287     O    HOH A   801              2.12            
REMARK 500   O    HOH A  1218     O    HOH A  1253              2.15            
REMARK 500   OD2  ASP B    82     O    HOH B   101              2.17            
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    ASN A  87     -167.85   -162.34                                   
REMARK 500    LEU A 107     -134.57   -119.54                                   
REMARK 500    HIS A 127       70.88     41.79                                   
REMARK 500    ARG A 192     -178.02   -173.26                                   
REMARK 500    ARG A 259       81.68   -150.92                                   
REMARK 500    SER A 314       -6.27     73.94                                   
REMARK 500    THR A 349      -66.01     70.45                                   
REMARK 500    LEU A 350      -65.39   -154.22                                   
REMARK 500    HIS A 560      116.01    -25.50                                   
REMARK 500    SER B  32      -64.92   -137.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  559     HIS A  560                  139.32                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 701  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 702   O1G                                                    
REMARK 620 2 ATP A 702   O2B  86.0                                              
REMARK 620 3 HOH A 827   O    90.2  92.5                                        
REMARK 620 4 HOH A 921   O    87.7  93.8 173.2                                  
REMARK 620 5 HOH A 926   O    96.9 176.4  85.3  88.5                            
REMARK 620 6 HOH A 835   O   173.5  91.3  95.9  86.5  86.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 701                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5D6N   RELATED DB: PDB                                   
DBREF  5D6J A    1   630  UNP    A0R618   A0R618_MYCS2     1    630             
DBREF  5D6J B   21    94  UNP    Q12306   SMT3_YEAST      21     94             
SEQRES   1 A  630  MET PRO PHE HIS ASN PRO PHE ILE LYS ASP GLY GLN ILE          
SEQRES   2 A  630  LYS PHE PRO ASP GLY SER SER ILE VAL ALA HIS VAL GLU          
SEQRES   3 A  630  ARG TRP ALA LYS VAL ARG GLY ASP LYS LEU ALA TYR ARG          
SEQRES   4 A  630  PHE LEU ASP PHE SER THR GLU ARG ASP GLY VAL PRO ARG          
SEQRES   5 A  630  ASP LEU THR TRP ALA GLN PHE SER ALA ARG ASN ARG ALA          
SEQRES   6 A  630  VAL ALA ALA ARG LEU GLN GLN VAL THR GLN PRO GLY ASP          
SEQRES   7 A  630  ARG VAL ALA ILE LEU CYS PRO GLN ASN LEU ASP TYR LEU          
SEQRES   8 A  630  VAL ALA PHE PHE GLY ALA LEU TYR ALA GLY ARG ILE ALA          
SEQRES   9 A  630  VAL PRO LEU PHE ASP PRO SER GLU PRO GLY HIS VAL GLY          
SEQRES  10 A  630  ARG LEU HIS ALA VAL LEU ASP ASN CYS HIS PRO SER ALA          
SEQRES  11 A  630  ILE LEU THR THR THR GLU ALA ALA GLU GLY VAL ARG LYS          
SEQRES  12 A  630  PHE PHE ARG THR ARG PRO ALA ASN GLN ARG PRO ARG VAL          
SEQRES  13 A  630  ILE ALA VAL ASP ALA VAL PRO ASP ASP VAL ALA SER THR          
SEQRES  14 A  630  TRP VAL ASN PRO ASP GLU PRO ASP GLU THR THR ILE ALA          
SEQRES  15 A  630  TYR LEU GLN TYR THR SER GLY SER THR ARG ILE PRO THR          
SEQRES  16 A  630  GLY VAL GLN ILE THR HIS LEU ASN LEU ALA THR ASN VAL          
SEQRES  17 A  630  VAL GLN VAL ILE GLU ALA LEU GLU GLY GLU GLU GLY ASP          
SEQRES  18 A  630  ARG GLY LEU SER TRP LEU PRO PHE PHE HIS ASP MET GLY          
SEQRES  19 A  630  LEU ILE THR ALA LEU LEU ALA PRO MET ILE GLY HIS TYR          
SEQRES  20 A  630  PHE THR PHE MET THR PRO ALA ALA PHE VAL ARG ARG PRO          
SEQRES  21 A  630  GLU ARG TRP ILE ARG GLU LEU ALA ARG LYS GLU GLY ASP          
SEQRES  22 A  630  THR GLY GLY THR ILE SER VAL ALA PRO ASN PHE ALA PHE          
SEQRES  23 A  630  ASP HIS ALA ALA ALA ARG GLY VAL PRO LYS PRO GLY SER          
SEQRES  24 A  630  PRO PRO LEU ASP LEU SER ASN VAL LYS ALA VAL LEU ASN          
SEQRES  25 A  630  GLY SER GLU PRO ILE SER ALA ALA THR VAL ARG ARG PHE          
SEQRES  26 A  630  ASN GLU ALA PHE GLY PRO PHE GLY PHE PRO PRO LYS ALA          
SEQRES  27 A  630  ILE LYS PRO SER TYR GLY LEU ALA GLU ALA THR LEU PHE          
SEQRES  28 A  630  VAL SER THR THR PRO SER ALA GLU GLU PRO LYS ILE ILE          
SEQRES  29 A  630  THR VAL ASP ARG ASP GLN LEU ASN SER GLY ARG ILE VAL          
SEQRES  30 A  630  GLU VAL ASP ALA ASP SER PRO LYS ALA VAL ALA GLN ALA          
SEQRES  31 A  630  SER ALA GLY LYS VAL GLY ILE ALA GLU TRP ALA VAL ILE          
SEQRES  32 A  630  VAL ASP ALA GLU SER ALA THR GLU LEU PRO ASP GLY GLN          
SEQRES  33 A  630  VAL GLY GLU ILE TRP ILE SER GLY GLN ASN MET GLY THR          
SEQRES  34 A  630  GLY TYR TRP GLY LYS PRO GLU GLU SER VAL ALA THR PHE          
SEQRES  35 A  630  GLN ASN ILE LEU LYS SER ARG THR ASN PRO SER HIS ALA          
SEQRES  36 A  630  GLU GLY ALA THR ASP ASP ALA THR TRP VAL ARG THR GLY          
SEQRES  37 A  630  ASP TYR GLY ALA PHE TYR ASP GLY ASP LEU TYR ILE THR          
SEQRES  38 A  630  GLY ARG VAL LYS ASP LEU VAL ILE ILE ASP GLY ARG ASN          
SEQRES  39 A  630  HIS TYR PRO GLN ASP LEU GLU TYR SER ALA GLN GLU ALA          
SEQRES  40 A  630  SER LYS ALA ILE ARG THR GLY TYR VAL ALA ALA PHE SER          
SEQRES  41 A  630  VAL PRO ALA ASN GLN LEU PRO ASP GLU VAL PHE GLU ASN          
SEQRES  42 A  630  ALA HIS SER GLY ILE LYS ARG ASP PRO ASP ASP THR SER          
SEQRES  43 A  630  GLU GLN LEU VAL ILE VAL ALA GLU ARG ALA PRO GLY ALA          
SEQRES  44 A  630  HIS LYS LEU ASP ILE GLY PRO ILE THR ASP ASP ILE ARG          
SEQRES  45 A  630  ALA ALA ILE ALA VAL ARG HIS GLY VAL THR VAL ARG ASP          
SEQRES  46 A  630  VAL LEU LEU THR ALA ALA GLY ALA ILE PRO ARG THR SER          
SEQRES  47 A  630  SER GLY LYS ILE GLY ARG ARG ALA CYS ARG ALA ALA TYR          
SEQRES  48 A  630  LEU ASP GLY SER LEU ARG ALA GLY LYS VAL ALA ASN ASP          
SEQRES  49 A  630  PHE PRO ASP ALA THR ASP                                      
SEQRES   1 B   74  GLU THR HIS ILE ASN LEU LYS VAL SER ASP GLY SER SER          
SEQRES   2 B   74  GLU ILE PHE PHE LYS ILE LYS LYS THR THR PRO LEU ARG          
SEQRES   3 B   74  ARG LEU MET GLU ALA PHE ALA LYS ARG GLN GLY LYS GLU          
SEQRES   4 B   74  MET ASP SER LEU ARG PHE LEU TYR ASP GLY ILE ARG ILE          
SEQRES   5 B   74  GLN ALA ASP GLN THR PRO GLU ASP LEU ASP MET GLU ASP          
SEQRES   6 B   74  ASN ASP ILE ILE GLU ALA HIS ARG GLU                          
HET     MG  A 701       1                                                       
HET    ATP  A 702      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
FORMUL   5  HOH   *482(H2 O)                                                    
HELIX    1 AA1 SER A   20  ARG A   32  1                                  13    
HELIX    2 AA2 TRP A   56  THR A   74  1                                  19    
HELIX    3 AA3 ASN A   87  ALA A  100  1                                  14    
HELIX    4 AA4 HIS A  115  HIS A  127  1                                  13    
HELIX    5 AA5 ALA A  137  ARG A  146  1                                  10    
HELIX    6 AA6 THR A  147  ARG A  148  5                                   2    
HELIX    7 AA7 PRO A  149  ARG A  153  5                                   5    
HELIX    8 AA8 ASP A  160  VAL A  162  5                                   3    
HELIX    9 AA9 PRO A  163  TRP A  170  5                                   8    
HELIX   10 AB1 HIS A  201  GLU A  216  1                                  16    
HELIX   11 AB2 HIS A  231  LEU A  239  1                                   9    
HELIX   12 AB3 LEU A  240  GLY A  245  1                                   6    
HELIX   13 AB4 THR A  252  ARG A  259  1                                   8    
HELIX   14 AB5 PRO A  260  ALA A  268  1                                   9    
HELIX   15 AB6 PRO A  282  GLY A  293  1                                  12    
HELIX   16 AB7 SER A  318  GLY A  330  1                                  13    
HELIX   17 AB8 PRO A  331  GLY A  333  5                                   3    
HELIX   18 AB9 PRO A  335  LYS A  337  5                                   3    
HELIX   19 AC1 ALA A  346  THR A  349  5                                   4    
HELIX   20 AC2 ARG A  368  SER A  373  1                                   6    
HELIX   21 AC3 LYS A  434  GLN A  443  1                                  10    
HELIX   22 AC4 LYS A  485  LEU A  487  5                                   3    
HELIX   23 AC5 TYR A  496  SER A  508  1                                  13    
HELIX   24 AC6 ASN A  524  LEU A  526  5                                   3    
HELIX   25 AC7 PRO A  527  ASN A  533  1                                   7    
HELIX   26 AC8 ALA A  534  GLY A  537  5                                   4    
HELIX   27 AC9 ASP A  563  GLY A  580  1                                  18    
HELIX   28 AD1 GLY A  603  LEU A  612  1                                  10    
HELIX   29 AD2 GLY A  614  GLY A  619  1                                   6    
HELIX   30 AD3 LEU B   45  GLN B   56  1                                  12    
HELIX   31 AD4 GLU B   59  ASP B   61  5                                   3    
SHEET    1 AA1 2 ILE A   8  LYS A   9  0                                        
SHEET    2 AA1 2 GLN A  12  ILE A  13 -1  O  GLN A  12   N  LYS A   9           
SHEET    1 AA2 4 VAL A  50  THR A  55  0                                        
SHEET    2 AA2 4 LEU A  36  ASP A  42 -1  N  PHE A  40   O  ARG A  52           
SHEET    3 AA2 4 PHE A 248  PHE A 250  1  O  PHE A 250   N  LEU A  41           
SHEET    4 AA2 4 GLY A 223  SER A 225  1  N  GLY A 223   O  THR A 249           
SHEET    1 AA3 4 ILE A 103  PRO A 106  0                                        
SHEET    2 AA3 4 ARG A  79  ILE A  82  1  N  VAL A  80   O  ILE A 103           
SHEET    3 AA3 4 ALA A 130  THR A 133  1  O  LEU A 132   N  ALA A  81           
SHEET    4 AA3 4 ARG A 155  ALA A 158  1  O  ILE A 157   N  ILE A 131           
SHEET    1 AA4 2 ILE A 181  TYR A 186  0                                        
SHEET    2 AA4 2 GLY A 196  THR A 200 -1  O  ILE A 199   N  ALA A 182           
SHEET    1 AA5 5 ILE A 278  VAL A 280  0                                        
SHEET    2 AA5 5 ALA A 309  ASN A 312  1  O  ALA A 309   N  SER A 279           
SHEET    3 AA5 5 ILE A 339  GLY A 344  1  O  LYS A 340   N  ASN A 312           
SHEET    4 AA5 5 PHE A 351  THR A 354 -1  O  VAL A 352   N  TYR A 343           
SHEET    5 AA5 5 LYS A 394  VAL A 395 -1  O  LYS A 394   N  THR A 354           
SHEET    1 AA6 2 ILE A 363  ASP A 367  0                                        
SHEET    2 AA6 2 ALA A 386  ALA A 390 -1  O  GLN A 389   N  ILE A 364           
SHEET    1 AA7 5 THR A 410  GLU A 411  0                                        
SHEET    2 AA7 5 GLU A 399  ASP A 405 -1  N  ASP A 405   O  THR A 410           
SHEET    3 AA7 5 GLY A 418  GLY A 424 -1  O  TRP A 421   N  VAL A 402           
SHEET    4 AA7 5 VAL A 465  TYR A 474 -1  O  VAL A 465   N  ILE A 422           
SHEET    5 AA7 5 ASP A 477  ARG A 483 -1  O  GLY A 482   N  TYR A 470           
SHEET    1 AA8 2 VAL A 488  ILE A 490  0                                        
SHEET    2 AA8 2 ARG A 493  HIS A 495 -1  O  HIS A 495   N  VAL A 488           
SHEET    1 AA9 3 VAL A 516  PRO A 522  0                                        
SHEET    2 AA9 3 GLU A 547  GLU A 554 -1  O  VAL A 552   N  ALA A 517           
SHEET    3 AA9 3 VAL A 583  THR A 589  1  O  LEU A 587   N  ILE A 551           
SHEET    1 AB1 5 GLU B  34  LYS B  40  0                                        
SHEET    2 AB1 5 HIS B  23  SER B  29 -1  N  VAL B  28   O  ILE B  35           
SHEET    3 AB1 5 ASP B  87  ARG B  93  1  O  ALA B  91   N  SER B  29           
SHEET    4 AB1 5 LEU B  63  TYR B  67 -1  N  LEU B  66   O  GLU B  90           
SHEET    5 AB1 5 ILE B  70  ARG B  71 -1  O  ILE B  70   N  TYR B  67           
LINK        MG    MG A 701                 O1G ATP A 702     1555   1555  2.01  
LINK        MG    MG A 701                 O2B ATP A 702     1555   1555  2.01  
LINK        MG    MG A 701                 O   HOH A 827     1555   1555  2.19  
LINK        MG    MG A 701                 O   HOH A 921     1555   1555  2.24  
LINK        MG    MG A 701                 O   HOH A 926     1555   1555  2.04  
LINK        MG    MG A 701                 O   HOH A 835     1555   1555  2.06  
CISPEP   1 ASN A  451    PRO A  452          0         0.90                     
CISPEP   2 HIS A  560    LYS A  561          0        10.11                     
CISPEP   3 ASP A  613    GLY A  614          0        -4.65                     
SITE     1 AC1  5 ATP A 702  HOH A 827  HOH A 835  HOH A 921                    
SITE     2 AC1  5 HOH A 926                                                     
SITE     1 AC2 26 THR A 187  SER A 188  GLY A 189  SER A 190                    
SITE     2 AC2 26 THR A 191  ARG A 192  SER A 314  GLU A 315                    
SITE     3 AC2 26 PRO A 316  SER A 342  GLY A 344  LEU A 345                    
SITE     4 AC2 26 ALA A 346  ASP A 469  ILE A 480  ARG A 483                    
SITE     5 AC2 26  MG A 701  HOH A 827  HOH A 835  HOH A 921                    
SITE     6 AC2 26 HOH A 924  HOH A 926  HOH A 973  HOH A 988                    
SITE     7 AC2 26 HOH A1060  HOH A1122                                          
CRYST1  122.211  122.211  142.588  90.00  90.00  90.00 P 43 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008183  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008183  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007013        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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