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Database: PDB
Entry: 5KKN
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HEADER    LYASE                                   22-JUN-16   5KKN              
TITLE     CRYSTAL STRUCTURE OF HUMAN ACC2 BC DOMAIN IN COMPLEX WITH ND-646, THE 
TITLE    2 PRIMARY AMIDE OF ND-630                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYL-COA CARBOXYLASE 2;                                  
COMPND   3 CHAIN: B, C;                                                         
COMPND   4 SYNONYM: ACC-BETA;                                                   
COMPND   5 EC: 6.4.1.2,6.3.4.14;                                                
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 GENE: ACACB, ACC2, ACCB;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BIOTIN-DEPENDENT CARBOXYLASE, GRASP FOLD, LYASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.WANG,D.PAUL,L.TONG                                                  
REVDAT   2   01-NOV-17 5KKN    1       JRNL   REMARK                            
REVDAT   1   13-JUL-16 5KKN    0                                                
JRNL        AUTH   G.HARRIMAN,J.GREENWOOD,S.BHAT,X.HUANG,R.WANG,D.PAUL,L.TONG,  
JRNL        AUTH 2 A.K.SAHA,W.F.WESTLIN,R.KAPELLER,H.J.HARWOOD                  
JRNL        TITL   ACETYL-COA CARBOXYLASE INHIBITION BY ND-630 REDUCES HEPATIC  
JRNL        TITL 2 STEATOSIS, IMPROVES INSULIN SENSITIVITY, AND MODULATES       
JRNL        TITL 3 DYSLIPIDEMIA IN RATS.                                        
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 113 E1796 2016              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   26976583                                                     
JRNL        DOI    10.1073/PNAS.1520686113                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 45207                          
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) : 0.222                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2441                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6553                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 370                          
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7480                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 80                                      
REMARK   3   SOLVENT ATOMS            : 26                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : -0.34000                                             
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): 0.430         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.497        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.892                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7782 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10571 ; 1.633 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   943 ; 6.320 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   356 ;34.113 ;23.904       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1271 ;20.302 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    53 ;18.714 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1163 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5924 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  4758 ; 0.665 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7673 ; 1.314 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3024 ; 2.104 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2898 ; 3.598 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   241        B   760                          
REMARK   3    RESIDUE RANGE :   B   801        B   915                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.4974  54.2655  39.8771              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1072 T22:   0.1371                                     
REMARK   3      T33:   0.0664 T12:  -0.1036                                     
REMARK   3      T13:   0.0156 T23:   0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8497 L22:   0.7035                                     
REMARK   3      L33:   0.5253 L12:  -0.3320                                     
REMARK   3      L13:  -0.1177 L23:  -0.1590                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0403 S12:  -0.0323 S13:  -0.0155                       
REMARK   3      S21:   0.0105 S22:   0.0425 S23:  -0.0225                       
REMARK   3      S31:   0.0496 S32:  -0.0367 S33:  -0.0021                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   241        C   760                          
REMARK   3    RESIDUE RANGE :   C   801        C   911                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7689  82.7774   2.0853              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0491 T22:   0.1398                                     
REMARK   3      T33:   0.1231 T12:  -0.0768                                     
REMARK   3      T13:  -0.0064 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6944 L22:   0.7445                                     
REMARK   3      L33:   2.3666 L12:  -0.1100                                     
REMARK   3      L13:   0.1569 L23:   0.3344                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.0733 S13:  -0.0804                       
REMARK   3      S21:   0.0637 S22:   0.0035 S23:   0.1085                       
REMARK   3      S31:   0.2884 S32:  -0.4435 S33:  -0.0584                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5KKN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47726                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 7, 2.8 M SODIUM FORMATE,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       70.83550            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       70.83550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.59400            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       70.83550            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       70.83550            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       81.59400            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       70.83550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       70.83550            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       81.59400            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       70.83550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       70.83550            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       81.59400            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        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 300 REMARK: MONOMER CONFIRMED BY GEL FILTRATION                          
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 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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     MET B   221                                                      
REMARK 465     GLY B   222                                                      
REMARK 465     SER B   223                                                      
REMARK 465     SER B   224                                                      
REMARK 465     HIS B   225                                                      
REMARK 465     HIS B   226                                                      
REMARK 465     HIS B   227                                                      
REMARK 465     HIS B   228                                                      
REMARK 465     HIS B   229                                                      
REMARK 465     HIS B   230                                                      
REMARK 465     GLU B   231                                                      
REMARK 465     ASN B   232                                                      
REMARK 465     LEU B   233                                                      
REMARK 465     TYR B   234                                                      
REMARK 465     PHE B   235                                                      
REMARK 465     GLN B   236                                                      
REMARK 465     GLY B   237                                                      
REMARK 465     LEU B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     ARG B   240                                                      
REMARK 465     THR B   412                                                      
REMARK 465     GLU B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     ASP B   415                                                      
REMARK 465     LEU B   416                                                      
REMARK 465     GLN B   417                                                      
REMARK 465     GLN B   418                                                      
REMARK 465     GLY B   419                                                      
REMARK 465     GLY B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     GLY B   461                                                      
REMARK 465     GLU B   636                                                      
REMARK 465     THR B   637                                                      
REMARK 465     PRO B   638                                                      
REMARK 465     SER B   639                                                      
REMARK 465     GLU B   656                                                      
REMARK 465     ASN B   657                                                      
REMARK 465     PRO B   658                                                      
REMARK 465     ASP B   659                                                      
REMARK 465     GLU B   660                                                      
REMARK 465     GLY B   661                                                      
REMARK 465     PHE B   662                                                      
REMARK 465     LYS B   663                                                      
REMARK 465     PRO B   664                                                      
REMARK 465     SER B   665                                                      
REMARK 465     SER B   666                                                      
REMARK 465     GLY B   667                                                      
REMARK 465     ALA B   688                                                      
REMARK 465     THR B   689                                                      
REMARK 465     GLY B   690                                                      
REMARK 465     GLY B   691                                                      
REMARK 465     LEU B   692                                                      
REMARK 465     HIS B   693                                                      
REMARK 465     GLU B   694                                                      
REMARK 465     PHE B   695                                                      
REMARK 465     ALA B   696                                                      
REMARK 465     ASP B   697                                                      
REMARK 465     SER B   698                                                      
REMARK 465     MET C   221                                                      
REMARK 465     GLY C   222                                                      
REMARK 465     SER C   223                                                      
REMARK 465     SER C   224                                                      
REMARK 465     HIS C   225                                                      
REMARK 465     HIS C   226                                                      
REMARK 465     HIS C   227                                                      
REMARK 465     HIS C   228                                                      
REMARK 465     HIS C   229                                                      
REMARK 465     HIS C   230                                                      
REMARK 465     GLU C   231                                                      
REMARK 465     ASN C   232                                                      
REMARK 465     LEU C   233                                                      
REMARK 465     TYR C   234                                                      
REMARK 465     PHE C   235                                                      
REMARK 465     GLN C   236                                                      
REMARK 465     GLY C   237                                                      
REMARK 465     LEU C   238                                                      
REMARK 465     HIS C   239                                                      
REMARK 465     ARG C   240                                                      
REMARK 465     THR C   412                                                      
REMARK 465     GLU C   413                                                      
REMARK 465     ASP C   414                                                      
REMARK 465     ASP C   415                                                      
REMARK 465     LEU C   416                                                      
REMARK 465     GLN C   417                                                      
REMARK 465     GLN C   418                                                      
REMARK 465     GLY C   419                                                      
REMARK 465     LYS C   420                                                      
REMARK 465     ARG C   421                                                      
REMARK 465     GLY C   459                                                      
REMARK 465     GLY C   460                                                      
REMARK 465     GLY C   461                                                      
REMARK 465     PRO C   638                                                      
REMARK 465     SER C   639                                                      
REMARK 465     ASN C   640                                                      
REMARK 465     GLU C   656                                                      
REMARK 465     ASN C   657                                                      
REMARK 465     PRO C   658                                                      
REMARK 465     ASP C   659                                                      
REMARK 465     GLU C   660                                                      
REMARK 465     GLY C   661                                                      
REMARK 465     PHE C   662                                                      
REMARK 465     LYS C   663                                                      
REMARK 465     PRO C   664                                                      
REMARK 465     SER C   665                                                      
REMARK 465     SER C   666                                                      
REMARK 465     GLY C   667                                                      
REMARK 465     SER C   685                                                      
REMARK 465     VAL C   686                                                      
REMARK 465     ALA C   687                                                      
REMARK 465     ALA C   688                                                      
REMARK 465     THR C   689                                                      
REMARK 465     GLY C   690                                                      
REMARK 465     GLY C   691                                                      
REMARK 465     LEU C   692                                                      
REMARK 465     HIS C   693                                                      
REMARK 465     GLU C   694                                                      
REMARK 465     PHE C   695                                                      
REMARK 465     ALA C   696                                                      
REMARK 465     ASP C   697                                                      
REMARK 465     SER C   698                                                      
REMARK 465     GLN C   699                                                      
REMARK 465     ILE C   726                                                      
REMARK 465     ARG C   727                                                      
REMARK 465     GLY C   728                                                      
REMARK 465     ASP C   729                                                      
REMARK 465     PHE C   730                                                      
REMARK 465     ARG C   731                                                      
REMARK 465     THR C   732                                                      
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     SER B 403    OG                                                  
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    GLY C   458     NZ   LYS C   462              1.73            
REMARK 500   O    GLN B   496     O    GLY B   754              1.86            
REMARK 500   O    LYS C   462     OE1  GLU C   483              2.00            
REMARK 500   NH2  ARG B   499     OD1  ASN B   749              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS C 527   NE2   HIS C 527   CD2    -0.066                       
REMARK 500    TYR C 560   CZ    TYR C 560   CE2    -0.081                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 727   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    LEU C 581   CA  -  CB  -  CG  ANGL. DEV. =  15.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA B 266       51.35    -97.65                                   
REMARK 500    ASN B 268     -168.43   -128.55                                   
REMARK 500    ASN B 328     -132.39     58.32                                   
REMARK 500    HIS B 353     -121.71     53.88                                   
REMARK 500    ASP B 508     -161.41   -100.49                                   
REMARK 500    PHE B 517     -158.16     60.33                                   
REMARK 500    SER B 562     -161.87     79.03                                   
REMARK 500    VAL B 686      -71.03    -53.85                                   
REMARK 500    ARG B 731      -70.04    -48.20                                   
REMARK 500    ASN C 328     -126.87     48.54                                   
REMARK 500    HIS C 353     -124.24     56.26                                   
REMARK 500    ALA C 381      -33.58    -39.69                                   
REMARK 500    PHE C 517     -135.20     60.22                                   
REMARK 500    SER C 562     -176.61     82.03                                   
REMARK 500    GLN C 572      -37.84    -36.17                                   
REMARK 500    HIS C 614        0.55    -65.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B  668     VAL B  669                 -149.56                    
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 6U3 B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6U3 C 801                 
DBREF  5KKN B  238   760  UNP    O00763   ACACB_HUMAN     36    558             
DBREF  5KKN C  238   760  UNP    O00763   ACACB_HUMAN     36    558             
SEQADV 5KKN MET B  221  UNP  O00763              INITIATING METHIONINE          
SEQADV 5KKN GLY B  222  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN SER B  223  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN SER B  224  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  225  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  226  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  227  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  228  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  229  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS B  230  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLU B  231  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN ASN B  232  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN LEU B  233  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN TYR B  234  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN PHE B  235  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLN B  236  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLY B  237  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN MET C  221  UNP  O00763              INITIATING METHIONINE          
SEQADV 5KKN GLY C  222  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN SER C  223  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN SER C  224  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  225  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  226  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  227  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  228  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  229  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN HIS C  230  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLU C  231  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN ASN C  232  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN LEU C  233  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN TYR C  234  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN PHE C  235  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLN C  236  UNP  O00763              EXPRESSION TAG                 
SEQADV 5KKN GLY C  237  UNP  O00763              EXPRESSION TAG                 
SEQRES   1 B  540  MET GLY SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU          
SEQRES   2 B  540  TYR PHE GLN GLY LEU HIS ARG ASP PHE THR VAL ALA SER          
SEQRES   3 B  540  PRO ALA GLU PHE VAL THR ARG PHE GLY GLY ASP ARG VAL          
SEQRES   4 B  540  ILE GLU LYS VAL LEU ILE ALA ASN ASN GLY ILE ALA ALA          
SEQRES   5 B  540  VAL LYS CYS MET ARG SER ILE ARG ARG TRP ALA TYR GLU          
SEQRES   6 B  540  MET PHE ARG ASN GLU ARG ALA ILE ARG PHE VAL VAL MET          
SEQRES   7 B  540  VAL THR PRO GLU ASP LEU LYS ALA ASN ALA GLU TYR ILE          
SEQRES   8 B  540  LYS MET ALA ASP HIS TYR VAL PRO VAL PRO GLY GLY PRO          
SEQRES   9 B  540  ASN ASN ASN ASN TYR ALA ASN VAL GLU LEU ILE VAL ASP          
SEQRES  10 B  540  ILE ALA LYS ARG ILE PRO VAL GLN ALA VAL TRP ALA GLY          
SEQRES  11 B  540  TRP GLY HIS ALA SER GLU ASN PRO LYS LEU PRO GLU LEU          
SEQRES  12 B  540  LEU CYS LYS ASN GLY VAL ALA PHE LEU GLY PRO PRO SER          
SEQRES  13 B  540  GLU ALA MET TRP ALA LEU GLY ASP LYS ILE ALA SER THR          
SEQRES  14 B  540  VAL VAL ALA GLN THR LEU GLN VAL PRO THR LEU PRO TRP          
SEQRES  15 B  540  SER GLY SER GLY LEU THR VAL GLU TRP THR GLU ASP ASP          
SEQRES  16 B  540  LEU GLN GLN GLY LYS ARG ILE SER VAL PRO GLU ASP VAL          
SEQRES  17 B  540  TYR ASP LYS GLY CYS VAL LYS ASP VAL ASP GLU GLY LEU          
SEQRES  18 B  540  GLU ALA ALA GLU ARG ILE GLY PHE PRO LEU MET ILE LYS          
SEQRES  19 B  540  ALA SER GLU GLY GLY GLY GLY LYS GLY ILE ARG LYS ALA          
SEQRES  20 B  540  GLU SER ALA GLU ASP PHE PRO ILE LEU PHE ARG GLN VAL          
SEQRES  21 B  540  GLN SER GLU ILE PRO GLY SER PRO ILE PHE LEU MET LYS          
SEQRES  22 B  540  LEU ALA GLN HIS ALA ARG HIS LEU GLU VAL GLN ILE LEU          
SEQRES  23 B  540  ALA ASP GLN TYR GLY ASN ALA VAL SER LEU PHE GLY ARG          
SEQRES  24 B  540  ASP CYS SER ILE GLN ARG ARG HIS GLN LYS ILE VAL GLU          
SEQRES  25 B  540  GLU ALA PRO ALA THR ILE ALA PRO LEU ALA ILE PHE GLU          
SEQRES  26 B  540  PHE MET GLU GLN CYS ALA ILE ARG LEU ALA LYS THR VAL          
SEQRES  27 B  540  GLY TYR VAL SER ALA GLY THR VAL GLU TYR LEU TYR SER          
SEQRES  28 B  540  GLN ASP GLY SER PHE HIS PHE LEU GLU LEU ASN PRO ARG          
SEQRES  29 B  540  LEU GLN VAL GLU HIS PRO CYS THR GLU MET ILE ALA ASP          
SEQRES  30 B  540  VAL ASN LEU PRO ALA ALA GLN LEU GLN ILE ALA MET GLY          
SEQRES  31 B  540  VAL PRO LEU HIS ARG LEU LYS ASP ILE ARG LEU LEU TYR          
SEQRES  32 B  540  GLY GLU SER PRO TRP GLY VAL THR PRO ILE SER PHE GLU          
SEQRES  33 B  540  THR PRO SER ASN PRO PRO LEU ALA ARG GLY HIS VAL ILE          
SEQRES  34 B  540  ALA ALA ARG ILE THR SER GLU ASN PRO ASP GLU GLY PHE          
SEQRES  35 B  540  LYS PRO SER SER GLY THR VAL GLN GLU LEU ASN PHE ARG          
SEQRES  36 B  540  SER SER LYS ASN VAL TRP GLY TYR PHE SER VAL ALA ALA          
SEQRES  37 B  540  THR GLY GLY LEU HIS GLU PHE ALA ASP SER GLN PHE GLY          
SEQRES  38 B  540  HIS CYS PHE SER TRP GLY GLU ASN ARG GLU GLU ALA ILE          
SEQRES  39 B  540  SER ASN MET VAL VAL ALA LEU LYS GLU LEU SER ILE ARG          
SEQRES  40 B  540  GLY ASP PHE ARG THR THR VAL GLU TYR LEU ILE ASN LEU          
SEQRES  41 B  540  LEU GLU THR GLU SER PHE GLN ASN ASN ASP ILE ASP THR          
SEQRES  42 B  540  GLY TRP LEU ASP TYR LEU ILE                                  
SEQRES   1 C  540  MET GLY SER SER HIS HIS HIS HIS HIS HIS GLU ASN LEU          
SEQRES   2 C  540  TYR PHE GLN GLY LEU HIS ARG ASP PHE THR VAL ALA SER          
SEQRES   3 C  540  PRO ALA GLU PHE VAL THR ARG PHE GLY GLY ASP ARG VAL          
SEQRES   4 C  540  ILE GLU LYS VAL LEU ILE ALA ASN ASN GLY ILE ALA ALA          
SEQRES   5 C  540  VAL LYS CYS MET ARG SER ILE ARG ARG TRP ALA TYR GLU          
SEQRES   6 C  540  MET PHE ARG ASN GLU ARG ALA ILE ARG PHE VAL VAL MET          
SEQRES   7 C  540  VAL THR PRO GLU ASP LEU LYS ALA ASN ALA GLU TYR ILE          
SEQRES   8 C  540  LYS MET ALA ASP HIS TYR VAL PRO VAL PRO GLY GLY PRO          
SEQRES   9 C  540  ASN ASN ASN ASN TYR ALA ASN VAL GLU LEU ILE VAL ASP          
SEQRES  10 C  540  ILE ALA LYS ARG ILE PRO VAL GLN ALA VAL TRP ALA GLY          
SEQRES  11 C  540  TRP GLY HIS ALA SER GLU ASN PRO LYS LEU PRO GLU LEU          
SEQRES  12 C  540  LEU CYS LYS ASN GLY VAL ALA PHE LEU GLY PRO PRO SER          
SEQRES  13 C  540  GLU ALA MET TRP ALA LEU GLY ASP LYS ILE ALA SER THR          
SEQRES  14 C  540  VAL VAL ALA GLN THR LEU GLN VAL PRO THR LEU PRO TRP          
SEQRES  15 C  540  SER GLY SER GLY LEU THR VAL GLU TRP THR GLU ASP ASP          
SEQRES  16 C  540  LEU GLN GLN GLY LYS ARG ILE SER VAL PRO GLU ASP VAL          
SEQRES  17 C  540  TYR ASP LYS GLY CYS VAL LYS ASP VAL ASP GLU GLY LEU          
SEQRES  18 C  540  GLU ALA ALA GLU ARG ILE GLY PHE PRO LEU MET ILE LYS          
SEQRES  19 C  540  ALA SER GLU GLY GLY GLY GLY LYS GLY ILE ARG LYS ALA          
SEQRES  20 C  540  GLU SER ALA GLU ASP PHE PRO ILE LEU PHE ARG GLN VAL          
SEQRES  21 C  540  GLN SER GLU ILE PRO GLY SER PRO ILE PHE LEU MET LYS          
SEQRES  22 C  540  LEU ALA GLN HIS ALA ARG HIS LEU GLU VAL GLN ILE LEU          
SEQRES  23 C  540  ALA ASP GLN TYR GLY ASN ALA VAL SER LEU PHE GLY ARG          
SEQRES  24 C  540  ASP CYS SER ILE GLN ARG ARG HIS GLN LYS ILE VAL GLU          
SEQRES  25 C  540  GLU ALA PRO ALA THR ILE ALA PRO LEU ALA ILE PHE GLU          
SEQRES  26 C  540  PHE MET GLU GLN CYS ALA ILE ARG LEU ALA LYS THR VAL          
SEQRES  27 C  540  GLY TYR VAL SER ALA GLY THR VAL GLU TYR LEU TYR SER          
SEQRES  28 C  540  GLN ASP GLY SER PHE HIS PHE LEU GLU LEU ASN PRO ARG          
SEQRES  29 C  540  LEU GLN VAL GLU HIS PRO CYS THR GLU MET ILE ALA ASP          
SEQRES  30 C  540  VAL ASN LEU PRO ALA ALA GLN LEU GLN ILE ALA MET GLY          
SEQRES  31 C  540  VAL PRO LEU HIS ARG LEU LYS ASP ILE ARG LEU LEU TYR          
SEQRES  32 C  540  GLY GLU SER PRO TRP GLY VAL THR PRO ILE SER PHE GLU          
SEQRES  33 C  540  THR PRO SER ASN PRO PRO LEU ALA ARG GLY HIS VAL ILE          
SEQRES  34 C  540  ALA ALA ARG ILE THR SER GLU ASN PRO ASP GLU GLY PHE          
SEQRES  35 C  540  LYS PRO SER SER GLY THR VAL GLN GLU LEU ASN PHE ARG          
SEQRES  36 C  540  SER SER LYS ASN VAL TRP GLY TYR PHE SER VAL ALA ALA          
SEQRES  37 C  540  THR GLY GLY LEU HIS GLU PHE ALA ASP SER GLN PHE GLY          
SEQRES  38 C  540  HIS CYS PHE SER TRP GLY GLU ASN ARG GLU GLU ALA ILE          
SEQRES  39 C  540  SER ASN MET VAL VAL ALA LEU LYS GLU LEU SER ILE ARG          
SEQRES  40 C  540  GLY ASP PHE ARG THR THR VAL GLU TYR LEU ILE ASN LEU          
SEQRES  41 C  540  LEU GLU THR GLU SER PHE GLN ASN ASN ASP ILE ASP THR          
SEQRES  42 C  540  GLY TRP LEU ASP TYR LEU ILE                                  
HET    6U3  B 801      40                                                       
HET    6U3  C 801      40                                                       
HETNAM     6U3 2-[1-[(2~{R})-2-(2-METHOXYPHENYL)-2-(OXAN-4-YLOXY)               
HETNAM   2 6U3  ETHYL]-5-METHYL-6-(1,3-OXAZOL-2-YL)-2,4-                        
HETNAM   3 6U3  BIS(OXIDANYLIDENE)THIENO[2,3-D]PYRIMIDIN-3-YL]-2-               
HETNAM   4 6U3  METHYL-PROPANAMIDE                                              
FORMUL   3  6U3    2(C28 H32 N4 O7 S)                                           
FORMUL   5  HOH   *26(H2 O)                                                     
HELIX    1 AA1 SER B  246  PHE B  254  1                                   9    
HELIX    2 AA2 ASN B  268  ARG B  288  1                                  21    
HELIX    3 AA3 THR B  300  ALA B  306  1                                   7    
HELIX    4 AA4 ALA B  308  ALA B  314  1                                   7    
HELIX    5 AA5 ASN B  327  ALA B  330  5                                   4    
HELIX    6 AA6 ASN B  331  ILE B  342  1                                  12    
HELIX    7 AA7 PRO B  358  ASN B  367  1                                  10    
HELIX    8 AA8 PRO B  375  LEU B  382  1                                   8    
HELIX    9 AA9 ASP B  384  LEU B  395  1                                  12    
HELIX   10 AB1 PRO B  425  CYS B  433  1                                   9    
HELIX   11 AB2 ASP B  436  GLY B  448  1                                  13    
HELIX   12 AB3 ASP B  472  ILE B  484  1                                  13    
HELIX   13 AB4 PRO B  540  VAL B  558  1                                  19    
HELIX   14 AB5 HIS B  589  ASP B  597  1                                   9    
HELIX   15 AB6 ASN B  599  MET B  609  1                                  11    
HELIX   16 AB7 PRO B  612  ARG B  615  5                                   4    
HELIX   17 AB8 LEU B  616  TYR B  623  1                                   8    
HELIX   18 AB9 ASN B  709  SER B  725  1                                  17    
HELIX   19 AC1 PHE B  730  GLU B  742  1                                  13    
HELIX   20 AC2 THR B  743  ASN B  748  1                                   6    
HELIX   21 AC3 SER C  246  GLY C  255  1                                  10    
HELIX   22 AC4 ASN C  268  ARG C  288  1                                  21    
HELIX   23 AC5 THR C  300  ASN C  307  1                                   8    
HELIX   24 AC6 ALA C  308  ALA C  314  1                                   7    
HELIX   25 AC7 ASN C  327  ALA C  330  5                                   4    
HELIX   26 AC8 ASN C  331  ILE C  342  1                                  12    
HELIX   27 AC9 PRO C  358  ASN C  367  1                                  10    
HELIX   28 AD1 PRO C  375  ASP C  384  1                                  10    
HELIX   29 AD2 ASP C  384  LEU C  395  1                                  12    
HELIX   30 AD3 PRO C  425  CYS C  433  1                                   9    
HELIX   31 AD4 ASP C  436  GLY C  448  1                                  13    
HELIX   32 AD5 ASP C  472  ILE C  484  1                                  13    
HELIX   33 AD6 PRO C  540  VAL C  558  1                                  19    
HELIX   34 AD7 HIS C  589  ASP C  597  1                                   9    
HELIX   35 AD8 ASN C  599  MET C  609  1                                  11    
HELIX   36 AD9 PRO C  612  ARG C  615  5                                   4    
HELIX   37 AE1 LEU C  616  TYR C  623  1                                   8    
HELIX   38 AE2 ASN C  709  LEU C  724  1                                  16    
HELIX   39 AE3 VAL C  734  GLU C  742  1                                   9    
HELIX   40 AE4 THR C  743  ASN C  749  1                                   7    
SHEET    1 AA1 5 HIS B 316  PRO B 319  0                                        
SHEET    2 AA1 5 ARG B 294  VAL B 299  1  N  VAL B 297   O  VAL B 318           
SHEET    3 AA1 5 LYS B 262  ILE B 265  1  N  ILE B 265   O  VAL B 296           
SHEET    4 AA1 5 ALA B 346  TRP B 348  1  O  ALA B 346   N  LEU B 264           
SHEET    5 AA1 5 ALA B 370  PHE B 371  1  O  ALA B 370   N  VAL B 347           
SHEET    1 AA2 3 ILE B 464  ALA B 467  0                                        
SHEET    2 AA2 3 LEU B 451  ALA B 455 -1  N  LEU B 451   O  ALA B 467           
SHEET    3 AA2 3 ILE B 489  LYS B 493 -1  O  MET B 492   N  MET B 452           
SHEET    1 AA3 9 PHE B 576  ASN B 582  0                                        
SHEET    2 AA3 9 SER B 562  SER B 571 -1  N  GLU B 567   O  GLU B 580           
SHEET    3 AA3 9 ALA B 498  ALA B 507 -1  N  LEU B 501   O  TYR B 568           
SHEET    4 AA3 9 ALA B 513  ARG B 525 -1  O  LEU B 516   N  GLN B 504           
SHEET    5 AA3 9 GLN B 528  ALA B 534 -1  O  GLU B 533   N  ASP B 520           
SHEET    6 AA3 9 HIS B 647  ILE B 653 -1  O  ARG B 652   N  ILE B 530           
SHEET    7 AA3 9 PHE B 700  GLY B 707 -1  O  GLY B 701   N  ILE B 653           
SHEET    8 AA3 9 VAL B 680  SER B 685 -1  N  TRP B 681   O  PHE B 704           
SHEET    9 AA3 9 VAL B 669  ASN B 673 -1  N  GLN B 670   O  PHE B 684           
SHEET    1 AA4 5 HIS C 316  PRO C 319  0                                        
SHEET    2 AA4 5 ARG C 294  VAL C 299  1  N  VAL C 299   O  VAL C 318           
SHEET    3 AA4 5 LYS C 262  ILE C 265  1  N  ILE C 265   O  VAL C 296           
SHEET    4 AA4 5 ALA C 346  TRP C 348  1  O  TRP C 348   N  LEU C 264           
SHEET    5 AA4 5 ALA C 370  PHE C 371  1  O  ALA C 370   N  VAL C 347           
SHEET    1 AA5 3 ILE C 464  ALA C 467  0                                        
SHEET    2 AA5 3 LEU C 451  ALA C 455 -1  N  LEU C 451   O  ALA C 467           
SHEET    3 AA5 3 ILE C 489  LYS C 493 -1  O  PHE C 490   N  LYS C 454           
SHEET    1 AA6 9 PHE C 576  ASN C 582  0                                        
SHEET    2 AA6 9 SER C 562  SER C 571 -1  N  GLU C 567   O  GLU C 580           
SHEET    3 AA6 9 ALA C 498  ALA C 507 -1  N  ILE C 505   O  GLY C 564           
SHEET    4 AA6 9 ALA C 513  ARG C 525 -1  O  ARG C 519   N  GLU C 502           
SHEET    5 AA6 9 GLN C 528  ALA C 534 -1  O  GLU C 533   N  ASP C 520           
SHEET    6 AA6 9 HIS C 647  ILE C 653 -1  O  ARG C 652   N  ILE C 530           
SHEET    7 AA6 9 GLY C 701  GLY C 707 -1  O  SER C 705   N  ILE C 649           
SHEET    8 AA6 9 VAL C 680  TYR C 683 -1  N  TRP C 681   O  PHE C 704           
SHEET    9 AA6 9 GLU C 671  ASN C 673 -1  N  LEU C 672   O  GLY C 682           
CISPEP   1 ILE B  342    PRO B  343          0        -8.40                     
CISPEP   2 PHE B  449    PRO B  450          0        -2.45                     
CISPEP   3 ALA B  534    PRO B  535          0        -3.88                     
CISPEP   4 ILE C  342    PRO C  343          0       -10.31                     
CISPEP   5 PHE C  449    PRO C  450          0         3.57                     
CISPEP   6 ALA C  534    PRO C  535          0         1.94                     
SITE     1 AC1 12 ILE B 270  LYS B 274  ARG B 277  ARG B 281                    
SITE     2 AC1 12 VAL B 587  PRO B 590  GLU B 593  LYS B 678                    
SITE     3 AC1 12 ASN B 679  VAL B 680  TRP B 681  PHE B 704                    
SITE     1 AC2 10 ILE C 270  LYS C 274  ARG C 277  ARG C 281                    
SITE     2 AC2 10 VAL C 587  PRO C 590  GLU C 593  MET C 594                    
SITE     3 AC2 10 TRP C 681  PHE C 704                                          
CRYST1  141.671  141.671  163.188  90.00  90.00  90.00 P 42 21 2    16          
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      0.007059  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007059  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006128        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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