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Database: PDB
Entry: 1Q2D
LinkDB: 1Q2D
Original site: 1Q2D 
HEADER    TRANSFERASE/STRUCTURAL PROTEIN          24-JUL-03   1Q2D              
TITLE     CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND A 19- 
TITLE    2 RESIDUE P53 PEPTIDE                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE ACETYLTRANSFERASE GCN5;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 49-209, CATALYTIC DOMAIN;                         
COMPND   5 SYNONYM: HAT A1;                                                     
COMPND   6 EC: 2.3.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 19-MER PEPTIDE FRAGMENT FROM P53 TUMOR SUPPRESSOR;         
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 311-329;                                          
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRAHYMENA THERMOPHILA;                        
SOURCE   3 ORGANISM_TAXID: 5911;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL-21;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PRSETA;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES                                                       
KEYWDS    TETRAHYMENA; GCN5; HISTONE H4; X-RAY STRUCTURE, TRANSFERASE-          
KEYWDS   2 STRUCTURAL PROTEIN COMPLEX                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.N.POUX,R.MARMORSTEIN                                                
REVDAT   3   16-AUG-23 1Q2D    1       REMARK SEQADV                            
REVDAT   2   24-FEB-09 1Q2D    1       VERSN                                    
REVDAT   1   03-AUG-04 1Q2D    0                                                
JRNL        AUTH   A.N.POUX,R.MARMORSTEIN                                       
JRNL        TITL   MOLECULAR BASIS FOR GCN5/PCAF HISTONE ACETYLTRANSFERASE      
JRNL        TITL 2 SELECTIVITY FOR HISTONE AND NONHISTONE SUBSTRATES            
JRNL        REF    BIOCHEMISTRY                  V.  42 14366 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   14661947                                                     
JRNL        DOI    10.1021/BI035632N                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 10902                          
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 SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1103                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.018                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.39                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1656                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5660                       
REMARK   3   BIN FREE R VALUE                    : 0.5520                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.30                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 190                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.040                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1388                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 48                                      
REMARK   3   SOLVENT ATOMS            : 62                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.93700                                             
REMARK   3    B22 (A**2) : -3.93700                                             
REMARK   3    B33 (A**2) : 7.87300                                              
REMARK   3    B12 (A**2) : -5.77400                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.57                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.515                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.84                                                 
REMARK   3   BSOL        : 49.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : COA_OLD.PAR                                    
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : COA_OLD.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Q2D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019828.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9213                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23773                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1QSN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, HEPES, SODIUM          
REMARK 280  CHLORIDE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K   
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       64.27533            
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       32.13767            
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       32.13767            
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       64.27533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9060 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   210                                                      
REMARK 465     ASN B   311                                                      
REMARK 465     THR B   312                                                      
REMARK 465     SER B   313                                                      
REMARK 465     SER B   314                                                      
REMARK 465     SER B   315                                                      
REMARK 465     PRO B   316                                                      
REMARK 465     GLN B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     LYS B   319                                                      
REMARK 465     GLU B   326                                                      
REMARK 465     TYR B   327                                                      
REMARK 465     PHE B   328                                                      
REMARK 465     THR B   329                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
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   OH   TYR A   205     O    LYS B   320     2664     2.15            
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  56       82.69    -64.55                                   
REMARK 500    ASN A 102       69.74     -4.14                                   
REMARK 500    LYS A 103       -5.92     57.43                                   
REMARK 500    GLN A 104       39.96   -149.83                                   
REMARK 500    TYR A 115       75.96   -119.99                                   
REMARK 500    ASN A 131        7.02    -69.77                                   
REMARK 500    ASN A 163     -120.69     48.60                                   
REMARK 500    TYR A 205       43.26   -142.09                                   
REMARK 500    PRO B 322       63.58      8.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QSN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QSR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QST   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1M1D   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1PU9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1PUA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Q2C   RELATED DB: PDB                                   
DBREF  1Q2D A   49   210  UNP    Q27198   Q27198_TETTH    49    210             
DBREF  1Q2D B  311   329  PDB    1Q2D     1Q2D           311    329             
SEQADV 1Q2D PHE A   90  UNP  Q27198    LEU    90 CLONING ARTIFACT               
SEQADV 1Q2D ARG A  210  UNP  Q27198    ASN   210 CLONING ARTIFACT               
SEQRES   1 A  162  LEU ASP PHE ASP ILE LEU THR ASN ASP GLY THR HIS ARG          
SEQRES   2 A  162  ASN MET LYS LEU LEU ILE ASP LEU LYS ASN ILE PHE SER          
SEQRES   3 A  162  ARG GLN LEU PRO LYS MET PRO LYS GLU TYR ILE VAL LYS          
SEQRES   4 A  162  LEU VAL PHE ASP ARG HIS HIS GLU SER MET VAL ILE LEU          
SEQRES   5 A  162  LYS ASN LYS GLN LYS VAL ILE GLY GLY ILE CYS PHE ARG          
SEQRES   6 A  162  GLN TYR LYS PRO GLN ARG PHE ALA GLU VAL ALA PHE LEU          
SEQRES   7 A  162  ALA VAL THR ALA ASN GLU GLN VAL ARG GLY TYR GLY THR          
SEQRES   8 A  162  ARG LEU MET ASN LYS PHE LYS ASP HIS MET GLN LYS GLN          
SEQRES   9 A  162  ASN ILE GLU TYR LEU LEU THR TYR ALA ASP ASN PHE ALA          
SEQRES  10 A  162  ILE GLY TYR PHE LYS LYS GLN GLY PHE THR LYS GLU HIS          
SEQRES  11 A  162  ARG MET PRO GLN GLU LYS TRP LYS GLY TYR ILE LYS ASP          
SEQRES  12 A  162  TYR ASP GLY GLY THR LEU MET GLU CYS TYR ILE HIS PRO          
SEQRES  13 A  162  TYR VAL ASP TYR GLY ARG                                      
SEQRES   1 B   19  ASN THR SER SER SER PRO GLN PRO LYS LYS LYS PRO LEU          
SEQRES   2 B   19  ASP GLY GLU TYR PHE THR                                      
HET    COA  A 401      48                                                       
HETNAM     COA COENZYME A                                                       
FORMUL   3  COA    C21 H36 N7 O16 P3 S                                          
FORMUL   4  HOH   *62(H2 O)                                                     
HELIX    1   1 THR A   59  LEU A   77  1                                  19    
HELIX    2   2 PRO A   81  PHE A   90  1                                  10    
HELIX    3   3 ALA A  130  GLN A  133  5                                   4    
HELIX    4   4 GLY A  136  GLN A  152  1                                  17    
HELIX    5   5 ASN A  163  GLN A  172  1                                  10    
HELIX    6   6 PRO A  181  LYS A  186  1                                   6    
SHEET    1   A 6 ASP A  50  LEU A  54  0                                        
SHEET    2   A 6 HIS A  94  LYS A 101 -1  O  SER A  96   N  LEU A  54           
SHEET    3   A 6 LYS A 105  TYR A 115 -1  O  PHE A 112   N  GLU A  95           
SHEET    4   A 6 PHE A 120  VAL A 128 -1  O  PHE A 125   N  CYS A 111           
SHEET    5   A 6 TYR A 156  ALA A 161  1  O  LEU A 158   N  ALA A 121           
SHEET    6   A 6 THR A 196  TYR A 201 -1  O  CYS A 200   N  LEU A 157           
SITE     1 AC1 15 GLN A  76  LEU A  77  LEU A 126  ALA A 127                    
SITE     2 AC1 15 VAL A 128  GLN A 133  VAL A 134  GLY A 136                    
SITE     3 AC1 15 GLY A 138  THR A 139  PHE A 164  LYS A 171                    
SITE     4 AC1 15 HOH A 502  LYS B 320  PRO B 322                               
CRYST1   64.740   64.740   96.413  90.00  90.00 120.00 P 32 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015446  0.008918  0.000000        0.00000                         
SCALE2      0.000000  0.017836  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010372        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system