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Database: PDB
Entry: 2W70
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HEADER    LIGASE                                  19-DEC-08   2W70              
TITLE     CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM E. COLI IN               
TITLE    2 COMPLEX WITH THE AMINO-THIAZOLE-PYRIMIDINE FRAGMENT                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BIOTIN CARBOXYLASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACC, ACETYL-COA CARBOXYLASE SUBUNIT A;                      
COMPND   5 EC: 6.3.4.14, 6.4.1.2;                                               
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LIGASE, ATP-BINDING, FATTY ACID BIOSYNTHESIS, NUCLEOTIDE-BINDING,     
KEYWDS   2 LIPID SYNTHESIS, ATP-GRASP DOMAIN, FRAGMENT SCREENING                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN,J.R.MILLER                                                
REVDAT   2   27-APR-11 2W70    1       KEYWDS JRNL   REMARK FORMUL              
REVDAT   1   19-MAY-09 2W70    0                                                
JRNL        AUTH   I.MOCHALKIN,J.R.MILLER,L.S.NARASIMHAN,V.THANABAL,            
JRNL        AUTH 2 P.ERDMAN,P.COX,J.V.PRASAD,S.LIGHTLE,M.HUBAND,                
JRNL        AUTH 3 K.STOVER                                                     
JRNL        TITL   DISCOVERY OF ANTIBACTERIAL BIOTIN CARBOXYLASE                
JRNL        TITL 2 INHIBITORS BY VIRTUAL SCREENING AND FRAGMENT-BASED           
JRNL        TITL 3 APPROACHES.                                                  
JRNL        REF    ACS CHEM.BIOL.                V.   4   473 2009              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   19413326                                                     
JRNL        DOI    10.1021/CB9000102                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 101581                         
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) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5319                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7298                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 367                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6893                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 942                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.23000                                             
REMARK   3    B22 (A**2) : 0.54000                                              
REMARK   3    B33 (A**2) : -0.31000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.105         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.898         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7048 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  6561 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9508 ; 1.118 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15242 ; 1.142 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   890 ; 4.956 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   318 ;33.748 ;23.648       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1243 ;12.971 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;18.796 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1040 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7905 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1424 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1324 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6567 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3379 ; 0.167 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3831 ; 0.081 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   666 ; 0.113 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    14 ; 0.119 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    56 ; 0.219 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    35 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5760 ; 0.683 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7095 ; 0.750 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3001 ; 1.467 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2413 ; 2.171 ; 4.500       
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  : NULL                                       
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2W70 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-38415.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 107085                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.77                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 80.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.94                               
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.54                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.54                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.35                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2J9G                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.11700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.31750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.10750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.31750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.11700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.10750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   447                                                      
REMARK 465     GLU A   448                                                      
REMARK 465     LYS A   449                                                      
REMARK 465     GLN B   447                                                      
REMARK 465     GLU B   448                                                      
REMARK 465     LYS B   449                                                      
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   O    HOH B  2067     O    HOH B  2068              1.62            
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  59      -88.30   -127.10                                   
REMARK 500    PHE A  84     -112.69     39.57                                   
REMARK 500    ASN A 206       59.98   -140.90                                   
REMARK 500    LEU A 225       61.32   -119.29                                   
REMARK 500    ALA A 226     -157.13     55.65                                   
REMARK 500    PHE A 347       17.13     59.52                                   
REMARK 500    ASN B   9     -168.92   -165.04                                   
REMARK 500    SER B  59      -89.19   -133.23                                   
REMARK 500    PHE B  84     -112.77     40.79                                   
REMARK 500    LEU B 225       61.65   -118.57                                   
REMARK 500    ALA B 226     -160.13     56.17                                   
REMARK 500    THR B 291       59.51    -96.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 4-(2-AMINO-THIAZOL-4-YL)-PYRIMIDIN-2-YLAMINE (LIG): INITIAL          
REMARK 600  FRAGMENT HIT 6                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L22 A1447                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE L22 B1447                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1448                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1448                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2J9G   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH AMPPNP AND ADP                              
REMARK 900 RELATED ID: 2VR1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH ATP ANALOG, ADPCF2P.                        
REMARK 900 RELATED ID: 2V5A   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E.COLI IN COMPLEX WITH POTENT INHIBITOR 3                           
REMARK 900 RELATED ID: 1K69   RELATED DB: PDB                                   
REMARK 900  MODEL INTERACTION BETWEEN BCCP AND ATP-BOUND                        
REMARK 900   CARBOXYLASESUBUNIT OF ACETYL COA CARBOXYLASE                       
REMARK 900 RELATED ID: 2GPW   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE                         
REMARK 900  SUBUNIT, F363AMUTANT, OF ACETYL-COA                                 
REMARK 900  CARBOXYLASE FROM ESCHERICHIA COLI.                                  
REMARK 900 RELATED ID: 2W6N   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH AMINO-OXAZOLE                               
REMARK 900  FRAGMENT SERIES                                                     
REMARK 900 RELATED ID: 2W6Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH THE TRIAZINE-2,4                            
REMARK 900  -DIAMINE FRAGMENT                                                   
REMARK 900 RELATED ID: 1BNC   RELATED DB: PDB                                   
REMARK 900  MOL_ID: 1; MOLECULE: BIOTIN CARBOXYLASE; CHAIN                      
REMARK 900  : A, B; EC: 6.3.4.14                                                
REMARK 900 RELATED ID: 2W71   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH THE IMIDAZOLE-                              
REMARK 900  PYRIMIDINE INHIBITOR                                                
REMARK 900 RELATED ID: 2V59   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E.COLI IN COMPLEX WITH POTENT INHIBITOR 2                           
REMARK 900 RELATED ID: 2W6P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH 5-METHYL-6-                                 
REMARK 900  PHENYL-QUINAZOLINE-2,4-DIAMINE                                      
REMARK 900 RELATED ID: 2W7C   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH THE 2-AMINO-                                
REMARK 900  PYRIMIDINE FRAGMENT                                                 
REMARK 900 RELATED ID: 2V58   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E.COLI IN COMPLEX WITH POTENT INHIBITOR 1                           
REMARK 900 RELATED ID: 2W6O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH 4-AMINO-7,7-                                
REMARK 900  DIMETHYL-7,8-DIHYDRO-QUINAZOLINONE FRAGMENT                         
REMARK 900 RELATED ID: 2W6Z   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH THE 3-(3-METHYL                             
REMARK 900  -BUT-2-ENYL)-3H-PURIN-6-YLAMINE FRAGMENT                            
REMARK 900 RELATED ID: 1DV1   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF BIOTIN CARBOXYLASE (APO)                               
REMARK 900 RELATED ID: 2W6M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF BIOTIN CARBOXYLASE FROM                        
REMARK 900  E. COLI IN COMPLEX WITH AMINO-OXAZOLE                               
REMARK 900  FRAGMENT SERIES                                                     
REMARK 900 RELATED ID: 2GPS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE BIOTIN CARBOXYLASE                         
REMARK 900  SUBUNIT, E23RMUTANT, OF ACETYL-COA CARBOXYLASE                      
REMARK 900   FROM ESCHERICHIA COLI.                                             
REMARK 900 RELATED ID: 1DV2   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF BIOTIN CARBOXYLASE, MUTANT                         
REMARK 900  E288K, COMPLEXED WITH ATP                                           
DBREF  2W70 A    1   449  UNP    P24182   ACCC_ECOLI       1    449             
DBREF  2W70 B    1   449  UNP    P24182   ACCC_ECOLI       1    449             
SEQRES   1 A  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 A  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 A  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 A  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 A  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 A  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 A  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 A  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 A  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 A  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 A  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 A  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 A  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 A  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 A  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 A  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 A  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 A  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 A  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 A  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 A  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 A  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 A  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 A  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 A  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 A  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 A  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 A  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 A  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 A  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 A  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 A  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 A  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 A  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 A  449  LYS LEU GLY LEU GLN GLU LYS                                  
SEQRES   1 B  449  MET LEU ASP LYS ILE VAL ILE ALA ASN ARG GLY GLU ILE          
SEQRES   2 B  449  ALA LEU ARG ILE LEU ARG ALA CYS LYS GLU LEU GLY ILE          
SEQRES   3 B  449  LYS THR VAL ALA VAL HIS SER SER ALA ASP ARG ASP LEU          
SEQRES   4 B  449  LYS HIS VAL LEU LEU ALA ASP GLU THR VAL CYS ILE GLY          
SEQRES   5 B  449  PRO ALA PRO SER VAL LYS SER TYR LEU ASN ILE PRO ALA          
SEQRES   6 B  449  ILE ILE SER ALA ALA GLU ILE THR GLY ALA VAL ALA ILE          
SEQRES   7 B  449  HIS PRO GLY TYR GLY PHE LEU SER GLU ASN ALA ASN PHE          
SEQRES   8 B  449  ALA GLU GLN VAL GLU ARG SER GLY PHE ILE PHE ILE GLY          
SEQRES   9 B  449  PRO LYS ALA GLU THR ILE ARG LEU MET GLY ASP LYS VAL          
SEQRES  10 B  449  SER ALA ILE ALA ALA MET LYS LYS ALA GLY VAL PRO CYS          
SEQRES  11 B  449  VAL PRO GLY SER ASP GLY PRO LEU GLY ASP ASP MET ASP          
SEQRES  12 B  449  LYS ASN ARG ALA ILE ALA LYS ARG ILE GLY TYR PRO VAL          
SEQRES  13 B  449  ILE ILE LYS ALA SER GLY GLY GLY GLY GLY ARG GLY MET          
SEQRES  14 B  449  ARG VAL VAL ARG GLY ASP ALA GLU LEU ALA GLN SER ILE          
SEQRES  15 B  449  SER MET THR ARG ALA GLU ALA LYS ALA ALA PHE SER ASN          
SEQRES  16 B  449  ASP MET VAL TYR MET GLU LYS TYR LEU GLU ASN PRO ARG          
SEQRES  17 B  449  HIS VAL GLU ILE GLN VAL LEU ALA ASP GLY GLN GLY ASN          
SEQRES  18 B  449  ALA ILE TYR LEU ALA GLU ARG ASP CYS SER MET GLN ARG          
SEQRES  19 B  449  ARG HIS GLN LYS VAL VAL GLU GLU ALA PRO ALA PRO GLY          
SEQRES  20 B  449  ILE THR PRO GLU LEU ARG ARG TYR ILE GLY GLU ARG CYS          
SEQRES  21 B  449  ALA LYS ALA CYS VAL ASP ILE GLY TYR ARG GLY ALA GLY          
SEQRES  22 B  449  THR PHE GLU PHE LEU PHE GLU ASN GLY GLU PHE TYR PHE          
SEQRES  23 B  449  ILE GLU MET ASN THR ARG ILE GLN VAL GLU HIS PRO VAL          
SEQRES  24 B  449  THR GLU MET ILE THR GLY VAL ASP LEU ILE LYS GLU GLN          
SEQRES  25 B  449  LEU ARG ILE ALA ALA GLY GLN PRO LEU SER ILE LYS GLN          
SEQRES  26 B  449  GLU GLU VAL HIS VAL ARG GLY HIS ALA VAL GLU CYS ARG          
SEQRES  27 B  449  ILE ASN ALA GLU ASP PRO ASN THR PHE LEU PRO SER PRO          
SEQRES  28 B  449  GLY LYS ILE THR ARG PHE HIS ALA PRO GLY GLY PHE GLY          
SEQRES  29 B  449  VAL ARG TRP GLU SER HIS ILE TYR ALA GLY TYR THR VAL          
SEQRES  30 B  449  PRO PRO TYR TYR ASP SER MET ILE GLY LYS LEU ILE CYS          
SEQRES  31 B  449  TYR GLY GLU ASN ARG ASP VAL ALA ILE ALA ARG MET LYS          
SEQRES  32 B  449  ASN ALA LEU GLN GLU LEU ILE ILE ASP GLY ILE LYS THR          
SEQRES  33 B  449  ASN VAL ASP LEU GLN ILE ARG ILE MET ASN ASP GLU ASN          
SEQRES  34 B  449  PHE GLN HIS GLY GLY THR ASN ILE HIS TYR LEU GLU LYS          
SEQRES  35 B  449  LYS LEU GLY LEU GLN GLU LYS                                  
HET    L22  A1447      13                                                       
HET    L22  B1447      13                                                       
HET     CL  A1448       1                                                       
HET     CL  B1448       1                                                       
HETNAM     L22 4-(2-AMINO-1,3-THIAZOL-4-YL)PYRIMIDIN-2-AMINE                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   3  L22    2(C7 H7 N5 S)                                                
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   5  HOH   *942(H2 O)                                                    
HELIX    1   1 ARG A   10  GLY A   25  1                                  16    
HELIX    2   2 ALA A   35  ARG A   37  5                                   3    
HELIX    3   3 LEU A   39  ALA A   45  1                                   7    
HELIX    4   4 PRO A   55  SER A   59  5                                   5    
HELIX    5   5 ASN A   62  GLY A   74  1                                  13    
HELIX    6   6 ASN A   88  SER A   98  1                                  11    
HELIX    7   7 LYS A  106  ASP A  115  1                                  10    
HELIX    8   8 ASP A  115  GLY A  127  1                                  13    
HELIX    9   9 ASP A  141  GLY A  153  1                                  13    
HELIX   10  10 GLY A  174  SER A  194  1                                  21    
HELIX   11  11 THR A  249  GLY A  268  1                                  20    
HELIX   12  12 GLU A  296  GLY A  305  1                                  10    
HELIX   13  13 ASP A  307  GLY A  318  1                                  12    
HELIX   14  14 LYS A  324  VAL A  328  5                                   5    
HELIX   15  15 ASN A  394  LEU A  409  1                                  16    
HELIX   16  16 ASN A  417  ASN A  426  1                                  10    
HELIX   17  17 ASP A  427  GLY A  433  1                                   7    
HELIX   18  18 HIS A  438  GLY A  445  1                                   8    
HELIX   19  19 ARG B   10  GLY B   25  1                                  16    
HELIX   20  20 ALA B   35  ARG B   37  5                                   3    
HELIX   21  21 LEU B   39  ALA B   45  1                                   7    
HELIX   22  22 PRO B   55  SER B   59  5                                   5    
HELIX   23  23 ASN B   62  THR B   73  1                                  12    
HELIX   24  24 ASN B   88  SER B   98  1                                  11    
HELIX   25  25 LYS B  106  ASP B  115  1                                  10    
HELIX   26  26 ASP B  115  GLY B  127  1                                  13    
HELIX   27  27 ASP B  141  GLY B  153  1                                  13    
HELIX   28  28 GLY B  174  SER B  194  1                                  21    
HELIX   29  29 THR B  249  GLY B  268  1                                  20    
HELIX   30  30 GLU B  296  GLY B  305  1                                  10    
HELIX   31  31 ASP B  307  ALA B  317  1                                  11    
HELIX   32  32 LYS B  324  VAL B  328  5                                   5    
HELIX   33  33 ASN B  394  LEU B  409  1                                  16    
HELIX   34  34 ASN B  417  ASN B  426  1                                  10    
HELIX   35  35 ASP B  427  GLY B  433  1                                   7    
HELIX   36  36 HIS B  438  GLY B  445  1                                   8    
SHEET    1  AA 5 GLU A  47  GLY A  52  0                                        
SHEET    2  AA 5 LYS A  27  SER A  33  1  O  THR A  28   N  GLU A  47           
SHEET    3  AA 5 LYS A   4  ILE A   7  1  O  ILE A   5   N  VAL A  29           
SHEET    4  AA 5 ALA A  77  HIS A  79  1  O  ALA A  77   N  VAL A   6           
SHEET    5  AA 5 ILE A 101  PHE A 102  1  O  ILE A 101   N  ILE A  78           
SHEET    1  AB 3 ARG A 170  VAL A 172  0                                        
SHEET    2  AB 3 VAL A 156  ALA A 160 -1  O  VAL A 156   N  VAL A 172           
SHEET    3  AB 3 VAL A 198  LYS A 202 -1  O  TYR A 199   N  LYS A 159           
SHEET    1  AC 8 GLU A 283  ASN A 290  0                                        
SHEET    2  AC 8 GLY A 271  GLU A 280 -1  O  THR A 274   N  ASN A 290           
SHEET    3  AC 8 ARG A 208  ALA A 216 -1  O  ARG A 208   N  PHE A 279           
SHEET    4  AC 8 ALA A 222  ARG A 234 -1  O  ILE A 223   N  LEU A 215           
SHEET    5  AC 8 GLN A 237  ALA A 243 -1  O  GLN A 237   N  ARG A 234           
SHEET    6  AC 8 HIS A 333  ASN A 340 -1  O  ALA A 334   N  ALA A 243           
SHEET    7  AC 8 MET A 384  GLY A 392 -1  N  ILE A 385   O  ILE A 339           
SHEET    8  AC 8 VAL A 365  GLU A 368 -1  O  ARG A 366   N  ILE A 389           
SHEET    1  AD 2 GLY A 352  LYS A 353  0                                        
SHEET    2  AD 2 THR A 376  VAL A 377 -1  O  VAL A 377   N  GLY A 352           
SHEET    1  AE 2 ARG A 356  HIS A 358  0                                        
SHEET    2  AE 2 ILE A 410  ASP A 412 -1  O  ILE A 410   N  HIS A 358           
SHEET    1  BA 5 GLU B  47  GLY B  52  0                                        
SHEET    2  BA 5 LYS B  27  SER B  33  1  O  THR B  28   N  GLU B  47           
SHEET    3  BA 5 LYS B   4  ILE B   7  1  O  ILE B   5   N  VAL B  29           
SHEET    4  BA 5 ALA B  77  HIS B  79  1  O  ALA B  77   N  VAL B   6           
SHEET    5  BA 5 ILE B 101  PHE B 102  1  O  ILE B 101   N  ILE B  78           
SHEET    1  BB 3 MET B 169  VAL B 172  0                                        
SHEET    2  BB 3 VAL B 156  ALA B 160 -1  O  VAL B 156   N  VAL B 172           
SHEET    3  BB 3 VAL B 198  LYS B 202 -1  O  TYR B 199   N  LYS B 159           
SHEET    1  BC 8 GLU B 283  ASN B 290  0                                        
SHEET    2  BC 8 ARG B 270  GLU B 280 -1  O  THR B 274   N  ASN B 290           
SHEET    3  BC 8 ARG B 208  ASP B 217 -1  O  ARG B 208   N  PHE B 279           
SHEET    4  BC 8 ALA B 222  ARG B 234 -1  O  ILE B 223   N  LEU B 215           
SHEET    5  BC 8 GLN B 237  ALA B 243 -1  O  GLN B 237   N  ARG B 234           
SHEET    6  BC 8 HIS B 333  ASN B 340 -1  O  ALA B 334   N  ALA B 243           
SHEET    7  BC 8 MET B 384  GLY B 392 -1  N  ILE B 385   O  ILE B 339           
SHEET    8  BC 8 VAL B 365  SER B 369 -1  O  ARG B 366   N  ILE B 389           
SHEET    1  BD 2 GLY B 352  LYS B 353  0                                        
SHEET    2  BD 2 THR B 376  VAL B 377 -1  O  VAL B 377   N  GLY B 352           
SHEET    1  BE 2 ARG B 356  HIS B 358  0                                        
SHEET    2  BE 2 ILE B 410  ASP B 412 -1  O  ILE B 410   N  HIS B 358           
CISPEP   1 TYR A  154    PRO A  155          0         1.98                     
CISPEP   2 ALA A  243    PRO A  244          0        -8.18                     
CISPEP   3 TYR B  154    PRO B  155          0        -0.80                     
CISPEP   4 ALA B  243    PRO B  244          0        -8.64                     
SITE     1 AC1 10 ILE A 157  LYS A 159  GLY A 166  GLU A 201                    
SITE     2 AC1 10 LYS A 202  TYR A 203  LEU A 204  LEU A 278                    
SITE     3 AC1 10 GLU A 288  HOH A2373                                          
SITE     1 AC2 10 ILE B 157  LYS B 159  GLY B 165  MET B 169                    
SITE     2 AC2 10 GLU B 201  LYS B 202  TYR B 203  LEU B 204                    
SITE     3 AC2 10 HIS B 236  LEU B 278                                          
SITE     1 AC3  4 ARG A 292  GLN A 294  VAL A 295  HOH A2185                    
SITE     1 AC4  5 ARG B 292  GLN B 294  VAL B 295  HOH B2073                    
SITE     2 AC4  5 HOH B2244                                                     
CRYST1   84.234  106.215  122.635  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011872  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009415  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008154        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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