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Database: PDB
Entry: 3TDC
LinkDB: 3TDC
Original site: 3TDC 
HEADER    LIGASE/LIGASE INHIBITOR                 10-AUG-11   3TDC              
TITLE     CRYSTAL STRUCTURE OF HUMAN ACETYL-COA CARBOXYLASE 2                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE 2 VARIANT;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 921-1676;                                     
COMPND   5 EC: 6.4.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    BIOTIN, MALONYL-COA, CARBOXYLASE, LIGASE-LIGASE INHIBITOR COMPLEX     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.R.DOUGAN,C.D.MOL                                                    
REVDAT   2   16-NOV-11 3TDC    1       JRNL                                     
REVDAT   1   12-OCT-11 3TDC    0                                                
JRNL        AUTH   T.YAMASHITA,M.KAMATA,S.ENDO,M.YAMAMOTO,K.KAKEGAWA,           
JRNL        AUTH 2 H.WATANABE,K.MIWA,T.YAMANO,M.FUNATA,J.SAKAMOTO,A.TANI,       
JRNL        AUTH 3 C.D.MOL,H.ZOU,D.R.DOUGAN,B.SANG,G.SNELL,K.FUKATSU            
JRNL        TITL   DESIGN, SYNTHESIS, AND STRUCTURE-ACTIVITY RELATIONSHIPS OF   
JRNL        TITL 2 SPIROLACTONES BEARING 2-UREIDOBENZOTHIOPHENE AS ACETYL-COA   
JRNL        TITL 3 CARBOXYLASES INHIBITORS.                                     
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  21  6314 2011              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   21944854                                                     
JRNL        DOI    10.1016/J.BMCL.2011.08.117                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35745                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1874                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5762                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 456                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.89000                                              
REMARK   3    B22 (A**2) : 1.73000                                              
REMARK   3    B33 (A**2) : -2.62000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.226         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.949        
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
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  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3TDC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067342.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9764                             
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37827                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1UYT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6.8% PEG MME 2000, 0.0175M AMMONIUM      
REMARK 280  SULFATE, 0.1M MES , PH 6.0, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
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   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.01750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.01750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       56.96050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.87800            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       56.96050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.87800            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       73.01750            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       56.96050            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.87800            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       73.01750            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       56.96050            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.87800            
REMARK 290   SMTRY3   8  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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL                       
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   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      119.75600            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      146.03500            
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     MET A  1715                                                      
REMARK 465     LEU A  1716                                                      
REMARK 465     ILE A  1717                                                      
REMARK 465     ASN A  1718                                                      
REMARK 465     GLN A  2415                                                      
REMARK 465     ALA A  2416                                                      
REMARK 465     GLY A  2417                                                      
REMARK 465     ASP A  2418                                                      
REMARK 465     GLY A  2419                                                      
REMARK 465     PRO A  2420                                                      
REMARK 465     ARG A  2421                                                      
REMARK 465     SER A  2422                                                      
REMARK 465     THR A  2423                                                      
REMARK 465     ILE A  2424                                                      
REMARK 465     ARG A  2425                                                      
REMARK 465     GLU A  2426                                                      
REMARK 465     ASN A  2427                                                      
REMARK 465     VAL A  2452                                                      
REMARK 465     ASP A  2453                                                      
REMARK 465     CYS A  2454                                                      
REMARK 465     VAL A  2455                                                      
REMARK 465     ILE A  2456                                                      
REMARK 465     TYR A  2457                                                      
REMARK 465     LEU A  2458                                                      
REMARK 465     SER A  2459                                                      
REMARK 465     GLN A  2460                                                      
REMARK 465     HIS A  2461                                                      
REMARK 465     ILE A  2462                                                      
REMARK 465     SER A  2463                                                      
REMARK 465     PRO A  2464                                                      
REMARK 465     ALA A  2465                                                      
REMARK 465     GLU A  2466                                                      
REMARK 465     ARG A  2467                                                      
REMARK 465     ALA A  2468                                                      
REMARK 465     GLN A  2469                                                      
REMARK 465     VAL A  2470                                                      
REMARK 465     HIS A  2471                                                      
REMARK 465     HIS A  2472                                                      
REMARK 465     HIS A  2473                                                      
REMARK 465     HIS A  2474                                                      
REMARK 465     HIS A  2475                                                      
REMARK 465     HIS A  2476                                                      
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    LYS A1762       59.97   -142.47                                   
REMARK 500    ILE A1824       29.76     49.96                                   
REMARK 500    ASP A1879       77.68   -153.36                                   
REMARK 500    CYS A1958      -73.09     67.54                                   
REMARK 500    GLN A1972      -52.56     75.00                                   
REMARK 500    ASN A1979        3.60     82.32                                   
REMARK 500    LEU A1984      -79.71    -99.57                                   
REMARK 500    SER A2001      148.60   -172.71                                   
REMARK 500    LEU A2082       86.40    -68.41                                   
REMARK 500    ASN A2181       65.49   -163.06                                   
REMARK 500    ASN A2237       70.67   -155.06                                   
REMARK 500    LEU A2287        1.94    -69.22                                   
REMARK 500    ASP A2291        7.68    -65.35                                   
REMARK 500    SER A2372       82.37   -159.64                                   
REMARK 500    GLU A2449     -136.41    -72.39                                   
REMARK 500    VAL A2450      -52.34     69.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A4416        DISTANCE =  6.77 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0EU A 3000                
DBREF  3TDC A 1715  2470  UNP    Q59GJ9   Q59GJ9_HUMAN   921   1676             
SEQADV 3TDC HIS A 2471  UNP  Q59GJ9              EXPRESSION TAG                 
SEQADV 3TDC HIS A 2472  UNP  Q59GJ9              EXPRESSION TAG                 
SEQADV 3TDC HIS A 2473  UNP  Q59GJ9              EXPRESSION TAG                 
SEQADV 3TDC HIS A 2474  UNP  Q59GJ9              EXPRESSION TAG                 
SEQADV 3TDC HIS A 2475  UNP  Q59GJ9              EXPRESSION TAG                 
SEQADV 3TDC HIS A 2476  UNP  Q59GJ9              EXPRESSION TAG                 
SEQRES   1 A  762  MET LEU ILE ASN THR PRO TYR VAL THR LYS ASP LEU LEU          
SEQRES   2 A  762  GLN ALA LYS ARG PHE GLN ALA GLN THR LEU GLY THR THR          
SEQRES   3 A  762  TYR ILE TYR ASP PHE PRO GLU MET PHE ARG GLN ALA LEU          
SEQRES   4 A  762  PHE LYS LEU TRP GLY SER PRO ASP LYS TYR PRO LYS ASP          
SEQRES   5 A  762  ILE LEU THR TYR THR GLU LEU VAL LEU ASP SER GLN GLY          
SEQRES   6 A  762  GLN LEU VAL GLU MET ASN ARG LEU PRO GLY GLY ASN GLU          
SEQRES   7 A  762  VAL GLY MET VAL ALA PHE LYS MET ARG PHE LYS THR GLN          
SEQRES   8 A  762  GLU TYR PRO GLU GLY ARG ASP VAL ILE VAL ILE GLY ASN          
SEQRES   9 A  762  ASP ILE THR PHE ARG ILE GLY SER PHE GLY PRO GLY GLU          
SEQRES  10 A  762  ASP LEU LEU TYR LEU ARG ALA SER GLU MET ALA ARG ALA          
SEQRES  11 A  762  GLU GLY ILE PRO LYS ILE TYR VAL ALA ALA ASN SER GLY          
SEQRES  12 A  762  ALA ARG ILE GLY MET ALA GLU GLU ILE LYS HIS MET PHE          
SEQRES  13 A  762  HIS VAL ALA TRP VAL ASP PRO GLU ASP PRO HIS LYS GLY          
SEQRES  14 A  762  PHE LYS TYR LEU TYR LEU THR PRO GLN ASP TYR THR ARG          
SEQRES  15 A  762  ILE SER SER LEU ASN SER VAL HIS CYS LYS HIS ILE GLU          
SEQRES  16 A  762  GLU GLY GLY GLU SER ARG TYR MET ILE THR ASP ILE ILE          
SEQRES  17 A  762  GLY LYS ASP ASP GLY LEU GLY VAL GLU ASN LEU ARG GLY          
SEQRES  18 A  762  SER GLY MET ILE ALA GLY GLU SER SER LEU ALA TYR GLU          
SEQRES  19 A  762  GLU ILE VAL THR ILE SER LEU VAL THR CYS ARG ALA ILE          
SEQRES  20 A  762  GLY ILE GLY ALA TYR LEU VAL ARG LEU GLY GLN ARG VAL          
SEQRES  21 A  762  ILE GLN VAL GLU ASN SER HIS ILE ILE LEU THR GLY ALA          
SEQRES  22 A  762  SER ALA LEU ASN LYS VAL LEU GLY ARG GLU VAL TYR THR          
SEQRES  23 A  762  SER ASN ASN GLN LEU GLY GLY VAL GLN ILE MET HIS TYR          
SEQRES  24 A  762  ASN GLY VAL SER HIS ILE THR VAL PRO ASP ASP PHE GLU          
SEQRES  25 A  762  GLY VAL TYR THR ILE LEU GLU TRP LEU SER TYR MET PRO          
SEQRES  26 A  762  LYS ASP ASN HIS SER PRO VAL PRO ILE ILE THR PRO THR          
SEQRES  27 A  762  ASP PRO ILE ASP ARG GLU ILE GLU PHE LEU PRO SER ARG          
SEQRES  28 A  762  ALA PRO TYR ASP PRO ARG TRP MET LEU ALA GLY ARG PRO          
SEQRES  29 A  762  HIS PRO THR LEU LYS GLY THR TRP GLN SER GLY PHE PHE          
SEQRES  30 A  762  ASP HIS GLY SER PHE LYS GLU ILE MET ALA PRO TRP ALA          
SEQRES  31 A  762  GLN THR VAL VAL THR GLY ARG ALA ARG LEU GLY GLY ILE          
SEQRES  32 A  762  PRO VAL GLY VAL ILE ALA VAL GLU THR ARG THR VAL GLU          
SEQRES  33 A  762  VAL ALA VAL PRO ALA ASP PRO ALA ASN LEU ASP SER GLU          
SEQRES  34 A  762  ALA LYS ILE ILE GLN GLN ALA GLY GLN VAL TRP PHE PRO          
SEQRES  35 A  762  ASP SER ALA TYR LYS THR ALA GLN ALA ILE LYS ASP PHE          
SEQRES  36 A  762  ASN ARG GLU LYS LEU PRO LEU MET ILE PHE ALA ASN TRP          
SEQRES  37 A  762  ARG GLY PHE SER GLY GLY MET LYS ASP MET TYR ASP GLN          
SEQRES  38 A  762  VAL LEU LYS PHE GLY ALA TYR ILE VAL ASP GLY LEU ARG          
SEQRES  39 A  762  GLN TYR LYS GLN PRO ILE LEU ILE TYR ILE PRO PRO TYR          
SEQRES  40 A  762  ALA GLU LEU ARG GLY GLY SER TRP VAL VAL ILE ASP ALA          
SEQRES  41 A  762  THR ILE ASN PRO LEU CYS ILE GLU MET TYR ALA ASP LYS          
SEQRES  42 A  762  GLU SER ARG GLY GLY VAL LEU GLU PRO GLU GLY THR VAL          
SEQRES  43 A  762  GLU ILE LYS PHE ARG LYS LYS ASP LEU ILE LYS SER MET          
SEQRES  44 A  762  ARG ARG ILE ASP PRO ALA TYR LYS LYS LEU MET GLU GLN          
SEQRES  45 A  762  LEU GLY GLU PRO ASP LEU SER ASP LYS ASP ARG LYS ASP          
SEQRES  46 A  762  LEU GLU GLY ARG LEU LYS ALA ARG GLU ASP LEU LEU LEU          
SEQRES  47 A  762  PRO ILE TYR HIS GLN VAL ALA VAL GLN PHE ALA ASP PHE          
SEQRES  48 A  762  HIS ASP THR PRO GLY ARG MET LEU GLU LYS GLY VAL ILE          
SEQRES  49 A  762  SER ASP ILE LEU GLU TRP LYS THR ALA ARG THR PHE LEU          
SEQRES  50 A  762  TYR TRP ARG LEU ARG ARG LEU LEU LEU GLU ASP GLN VAL          
SEQRES  51 A  762  LYS GLN GLU ILE LEU GLN ALA SER GLY GLU LEU SER HIS          
SEQRES  52 A  762  VAL HIS ILE GLN SER MET LEU ARG ARG TRP PHE VAL GLU          
SEQRES  53 A  762  THR GLU GLY ALA VAL LYS ALA TYR LEU TRP ASP ASN ASN          
SEQRES  54 A  762  GLN VAL VAL VAL GLN TRP LEU GLU GLN HIS TRP GLN ALA          
SEQRES  55 A  762  GLY ASP GLY PRO ARG SER THR ILE ARG GLU ASN ILE THR          
SEQRES  56 A  762  TYR LEU LYS HIS ASP SER VAL LEU LYS THR ILE ARG GLY          
SEQRES  57 A  762  LEU VAL GLU GLU ASN PRO GLU VAL ALA VAL ASP CYS VAL          
SEQRES  58 A  762  ILE TYR LEU SER GLN HIS ILE SER PRO ALA GLU ARG ALA          
SEQRES  59 A  762  GLN VAL HIS HIS HIS HIS HIS HIS                              
HET    0EU  A3000      36                                                       
HETNAM     0EU 1-[3-({4-[(5S)-3,3-DIMETHYL-1-OXO-2-OXA-7-                       
HETNAM   2 0EU  AZASPIRO[4.5]DEC-7-YL]PIPERIDIN-1-YL}CARBONYL)-1-               
HETNAM   3 0EU  BENZOTHIOPHEN-2-YL]-3-ETHYLUREA                                 
FORMUL   2  0EU    C27 H36 N4 O4 S                                              
FORMUL   3  HOH   *456(H2 O)                                                    
HELIX    1   1 LEU A 1727  LEU A 1737  1                                  11    
HELIX    2   2 TYR A 1741  TYR A 1743  5                                   3    
HELIX    3   3 ASP A 1744  GLY A 1758  1                                  15    
HELIX    4   4 PHE A 1822  SER A 1826  5                                   5    
HELIX    5   5 GLY A 1828  GLY A 1846  1                                  19    
HELIX    6   6 ALA A 1863  HIS A 1868  1                                   6    
HELIX    7   7 ASP A 1879  LYS A 1882  5                                   4    
HELIX    8   8 THR A 1890  SER A 1898  1                                   9    
HELIX    9   9 GLY A 1929  ILE A 1950  1                                  22    
HELIX   10  10 GLY A 1962  GLN A 1972  1                                  11    
HELIX   11  11 GLY A 1986  GLY A 1995  1                                  10    
HELIX   12  12 SER A 2001  GLY A 2007  1                                   7    
HELIX   13  13 GLY A 2007  HIS A 2012  1                                   6    
HELIX   14  14 ASP A 2023  SER A 2036  1                                  14    
HELIX   15  15 ASP A 2069  GLY A 2076  1                                   8    
HELIX   16  16 PHE A 2155  LYS A 2173  1                                  19    
HELIX   17  17 GLY A 2188  ASP A 2194  1                                   7    
HELIX   18  18 GLN A 2195  GLN A 2209  1                                  15    
HELIX   19  19 GLY A 2226  VAL A 2231  1                                   6    
HELIX   20  20 ILE A 2232  ASN A 2237  5                                   6    
HELIX   21  21 GLU A 2255  PHE A 2264  1                                  10    
HELIX   22  22 ARG A 2265  ASP A 2277  1                                  13    
HELIX   23  23 ASP A 2277  LEU A 2287  1                                  11    
HELIX   24  24 SER A 2293  PHE A 2325  1                                  33    
HELIX   25  25 THR A 2328  LYS A 2335  1                                   8    
HELIX   26  26 GLU A 2343  LYS A 2345  5                                   3    
HELIX   27  27 THR A 2346  GLN A 2370  1                                  25    
HELIX   28  28 SER A 2376  THR A 2391  1                                  16    
HELIX   29  29 GLY A 2393  ASP A 2401  5                                   9    
HELIX   30  30 ASN A 2402  TRP A 2414  1                                  13    
HELIX   31  31 THR A 2429  GLU A 2446  1                                  18    
SHEET    1   A 8 LEU A1781  MET A1784  0                                        
SHEET    2   A 8 LEU A1768  LEU A1775 -1  N  GLU A1772   O  MET A1784           
SHEET    3   A 8 MET A1795  PHE A1802 -1  O  ARG A1801   N  THR A1769           
SHEET    4   A 8 ARG A1811  ASN A1818 -1  O  GLY A1817   N  VAL A1796           
SHEET    5   A 8 LYS A1849  ALA A1853  1  O  ILE A1850   N  ILE A1814           
SHEET    6   A 8 THR A1952  VAL A1956  1  O  LEU A1955   N  ALA A1853           
SHEET    7   A 8 ARG A1973  VAL A1977  1  O  ILE A1975   N  VAL A1956           
SHEET    8   A 8 ILE A2019  VAL A2021  1  O  ILE A2019   N  GLN A1976           
SHEET    1   B 4 HIS A1871  TRP A1874  0                                        
SHEET    2   B 4 PHE A1884  LEU A1889 -1  O  LYS A1885   N  ALA A1873           
SHEET    3   B 4 GLU A1913  ILE A1921 -1  O  TYR A1916   N  LEU A1889           
SHEET    4   B 4 VAL A1903  GLU A1910 -1  N  ILE A1908   O  ARG A1915           
SHEET    1   C 2 ARG A1959  ILE A1961  0                                        
SHEET    2   C 2 HIS A1981  ILE A1983  1  O  ILE A1983   N  ALA A1960           
SHEET    1   D 2 ARG A2077  PRO A2078  0                                        
SHEET    2   D 2 TRP A2086  GLN A2087 -1  O  GLN A2087   N  ARG A2077           
SHEET    1   E 7 LYS A2097  ILE A2099  0                                        
SHEET    2   E 7 VAL A2107  LEU A2114 -1  O  THR A2109   N  ILE A2099           
SHEET    3   E 7 ILE A2117  VAL A2124 -1  O  ALA A2123   N  VAL A2108           
SHEET    4   E 7 LEU A2176  PHE A2179  1  O  PHE A2179   N  ILE A2122           
SHEET    5   E 7 ILE A2214  ILE A2218  1  O  TYR A2217   N  ILE A2178           
SHEET    6   E 7 ILE A2241  ASP A2246  1  O  GLU A2242   N  ILE A2216           
SHEET    7   E 7 ASP A2340  LEU A2342  1  O  LEU A2342   N  ALA A2245           
SHEET    1   F 2 VAL A2129  VAL A2133  0                                        
SHEET    2   F 2 LYS A2145  GLN A2149 -1  O  GLN A2149   N  VAL A2129           
SHEET    1   G 2 VAL A2153  TRP A2154  0                                        
SHEET    2   G 2 GLY A2184  PHE A2185  1  O  GLY A2184   N  TRP A2154           
SHEET    1   H 2 GLU A2223  ARG A2225  0                                        
SHEET    2   H 2 ARG A2250  GLY A2252  1  O  ARG A2250   N  LEU A2224           
SITE     1 AC1 12 ALA A1989  LEU A1990  VAL A1993  ARG A2183                    
SITE     2 AC1 12 PHE A2185  SER A2186  GLY A2187  LEU A2254                    
SITE     3 AC1 12 GLU A2255  GLU A2257  GLY A2258  GLU A2261                    
CRYST1  113.921  119.756  146.035  90.00  90.00  90.00 C 2 2 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      0.008778  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008350  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006848        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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