GenomeNet

Database: PDB
Entry: 2P8U
LinkDB: 2P8U
Original site: 2P8U 
HEADER    TRANSFERASE                             23-MAR-07   2P8U              
TITLE     CRYSTAL STRUCTURE OF HUMAN 3-HYDROXY-3-METHYLGLUTARYL COA SYNTHASE I  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROXYMETHYLGLUTARYL-COA SYNTHASE, CYTOPLASMIC;           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HMG-COA SYNTHASE, 3-HYDROXY-3-METHYLGLUTARYL COENZYME A     
COMPND   5 SYNTHASE;                                                            
COMPND   6 EC: 2.3.3.10;                                                        
COMPND   7 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: HMGCS1, HMGCS;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3/ROSETTA;                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    HYDROMETHYLGLUTARYL COA, MEVALONATE PATHWAY, STRUCTURAL GENOMICS,     
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.TURNBULL,N.SHAFQAT,E.SALAH,F.H.NIESEN,N.BURGESS,G.BUNKOCZI,         
AUTHOR   2 J.DEBRECZENI,A.C.W.PIKE,C.UMEANO,F.GORREC,F.VON DELFT,J.WEIGELT,     
AUTHOR   3 C.H.ARROWSMITH,M.SUNDSTROM,A.EDWARDS,U.OPPERMANN,STRUCTURAL GENOMICS 
AUTHOR   4 CONSORTIUM (SGC)                                                     
REVDAT   7   18-OCT-17 2P8U    1       REMARK                                   
REVDAT   6   13-JUL-11 2P8U    1       VERSN                                    
REVDAT   5   19-MAY-10 2P8U    1       JRNL                                     
REVDAT   4   24-NOV-09 2P8U    1       ATOM   DBREF  SEQADV REMARK              
REVDAT   4 2                   1       SITE                                     
REVDAT   3   24-FEB-09 2P8U    1       VERSN                                    
REVDAT   2   10-APR-07 2P8U    1       AUTHOR                                   
REVDAT   1   03-APR-07 2P8U    0                                                
JRNL        AUTH   N.SHAFQAT,A.TURNBULL,J.ZSCHOCKE,U.OPPERMANN,W.W.YUE          
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN HMG-COA SYNTHASE ISOFORMS        
JRNL        TITL 2 PROVIDE INSIGHTS INTO INHERITED KETOGENESIS DISORDERS AND    
JRNL        TITL 3 INHIBITOR DESIGN.                                            
JRNL        REF    J.MOL.BIOL.                   V. 398   497 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20346956                                                     
JRNL        DOI    10.1016/J.JMB.2010.03.034                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 63108                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3380                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4847                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.67                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.2630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7135                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 745                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : 0.22000                                              
REMARK   3    B33 (A**2) : -0.45000                                             
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): 0.168         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.149         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.328         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7399 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4861 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10045 ; 1.345 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11775 ; 1.378 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   930 ; 6.020 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   337 ;37.212 ;24.481       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1195 ;12.140 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;17.088 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1113 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8340 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1516 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1503 ; 0.205 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5174 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3621 ; 0.177 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3598 ; 0.093 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   638 ; 0.142 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     8 ; 0.172 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    20 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    21 ; 0.154 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4708 ; 2.520 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1906 ; 0.654 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7337 ; 3.463 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3099 ; 5.870 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2704 ; 7.182 ;11.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 7                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     46       A     276      2                      
REMARK   3           1     B     46       B     276      2                      
REMARK   3           2     A    277       A     288      5                      
REMARK   3           2     B    277       B     288      5                      
REMARK   3           3     A    289       A     320      2                      
REMARK   3           3     B    289       B     320      2                      
REMARK   3           4     A    321       A     329      5                      
REMARK   3           4     B    321       B     329      5                      
REMARK   3           5     A    330       A     423      2                      
REMARK   3           5     B    330       B     423      2                      
REMARK   3           6     A    424       A     436      5                      
REMARK   3           6     B    424       B     436      5                      
REMARK   3           7     A    437       A     505      2                      
REMARK   3           7     B    437       B     505      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2502 ;  0.05 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3181 ;  0.34 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    208 ;  0.48 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2502 ;  0.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3181 ;  1.12 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    208 ;  3.03 ; 10.00           
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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    46        A   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.3263  27.4953  63.9642              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0850 T22:  -0.0713                                     
REMARK   3      T33:  -0.0852 T12:   0.0097                                     
REMARK   3      T13:  -0.0155 T23:  -0.0096                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7117 L22:   0.7851                                     
REMARK   3      L33:   1.1780 L12:  -0.0410                                     
REMARK   3      L13:   0.1090 L23:  -0.0745                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0055 S12:   0.0137 S13:   0.0676                       
REMARK   3      S21:  -0.0163 S22:   0.0238 S23:   0.0943                       
REMARK   3      S31:  -0.0866 S32:  -0.1747 S33:  -0.0293                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    46        B   470                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7231  24.0404  84.0571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0860 T22:  -0.0932                                     
REMARK   3      T33:  -0.1031 T12:   0.0047                                     
REMARK   3      T13:  -0.0187 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6826 L22:   0.6309                                     
REMARK   3      L33:   1.3024 L12:   0.0087                                     
REMARK   3      L13:   0.2252 L23:  -0.0973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0028 S12:   0.0024 S13:  -0.0333                       
REMARK   3      S21:   0.0218 S22:  -0.0042 S23:  -0.0890                       
REMARK   3      S31:   0.0338 S32:   0.1426 S33:   0.0070                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 2P8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042111.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99999                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66668                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.12800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 2FA0,2F82,2FA3,2F9A,1XPL                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.20                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M (NH4)2SO4, 0.1M BIS-TRIS PH 6.5,    
REMARK 280  25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      117.76600            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.38100            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.38100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      176.64900            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.38100            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.38100            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.88300            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.38100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.38100            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      176.64900            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.38100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.38100            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       58.88300            
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      117.76600            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     MET B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     ASP B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     GLU B     8                                                      
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     ASN A   9    CG   OD1  ND2                                       
REMARK 470     LEU A  10    CG   CD1  CD2                                       
REMARK 470     TYR A  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A  13    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 238    CE   NZ                                             
REMARK 470     ASP A 290    CG   OD1  OD2                                       
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     LYS A 305    CE   NZ                                             
REMARK 470     ARG A 313    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 317    CG   CD   CE   NZ                                   
REMARK 470     LYS A 321    CD   CE   NZ                                        
REMARK 470     GLU A 325    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 363    CD   OE1  NE2                                       
REMARK 470     LYS A 400    NZ                                                  
REMARK 470     LYS A 428    CE   NZ                                             
REMARK 470     ASN B   9    CG   OD1  ND2                                       
REMARK 470     LEU B  10    CG   CD1  CD2                                       
REMARK 470     TYR B  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 245    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 246    CD   CE   NZ                                        
REMARK 470     ASP B 290    CG   OD1  OD2                                       
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     ILE B 294    CG1  CG2  CD1                                       
REMARK 470     LYS B 305    CG   CD   CE   NZ                                   
REMARK 470     ARG B 313    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 317    CD   CE   NZ                                        
REMARK 470     LYS B 321    CD   CE   NZ                                        
REMARK 470     LYS B 400    CE   NZ                                             
REMARK 470     LYS B 409    CE   NZ                                             
REMARK 470     LYS B 428    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1057     O    HOH A  1285              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A 123     -124.35   -137.04                                   
REMARK 500    ALA A 128     -134.88     49.44                                   
REMARK 500    VAL A 174      138.33   -170.01                                   
REMARK 500    LEU A 193       55.78   -116.41                                   
REMARK 500    TYR A 202       55.65   -113.40                                   
REMARK 500    THR A 331      -31.73   -130.65                                   
REMARK 500    TYR A 345     -115.58     52.19                                   
REMARK 500    THR A 389      151.34    -49.60                                   
REMARK 500    ILE B 123     -132.40   -136.43                                   
REMARK 500    ALA B 128     -130.56     48.51                                   
REMARK 500    VAL B 174      137.07   -171.42                                   
REMARK 500    LEU B 193       59.72   -117.01                                   
REMARK 500    TYR B 202       51.78   -111.99                                   
REMARK 500    ASN B 288       44.49   -106.93                                   
REMARK 500    THR B 331      -31.53   -130.53                                   
REMARK 500    TYR B 345     -114.08     54.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 981                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA B 601                 
DBREF  2P8U A   16   470  UNP    Q01581   HMCS1_HUMAN     16    470             
DBREF  2P8U B   16   470  UNP    Q01581   HMCS1_HUMAN     16    470             
SEQADV 2P8U MET A   -7  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -6  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -5  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -4  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -3  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -2  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS A   -1  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER A    0  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER A    1  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLY A    2  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U VAL A    3  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U ASP A    4  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U LEU A    5  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLY A    6  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U THR A    7  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLU A    8  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U ASN A    9  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U LEU A   10  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U TYR A   11  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U PHE A   12  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLN A   13  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER A   14  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U MET A   15  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SCY A  129  UNP  Q01581    CYS   129 MODIFIED RESIDUE               
SEQADV 2P8U MET B   -7  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -6  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -5  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -4  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -3  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -2  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U HIS B   -1  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER B    0  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER B    1  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLY B    2  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U VAL B    3  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U ASP B    4  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U LEU B    5  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLY B    6  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U THR B    7  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLU B    8  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U ASN B    9  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U LEU B   10  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U TYR B   11  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U PHE B   12  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U GLN B   13  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SER B   14  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U MET B   15  UNP  Q01581              EXPRESSION TAG                 
SEQADV 2P8U SCY B  129  UNP  Q01581    CYS   129 MODIFIED RESIDUE               
SEQRES   1 A  478  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  478  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP VAL GLY          
SEQRES   3 A  478  ILE VAL ALA LEU GLU ILE TYR PHE PRO SER GLN TYR VAL          
SEQRES   4 A  478  ASP GLN ALA GLU LEU GLU LYS TYR ASP GLY VAL ASP ALA          
SEQRES   5 A  478  GLY LYS TYR THR ILE GLY LEU GLY GLN ALA LYS MET GLY          
SEQRES   6 A  478  PHE CYS THR ASP ARG GLU ASP ILE ASN SER LEU CYS MET          
SEQRES   7 A  478  THR VAL VAL GLN ASN LEU MET GLU ARG ASN ASN LEU SER          
SEQRES   8 A  478  TYR ASP CYS ILE GLY ARG LEU GLU VAL GLY THR GLU THR          
SEQRES   9 A  478  ILE ILE ASP LYS SER LYS SER VAL LYS THR ASN LEU MET          
SEQRES  10 A  478  GLN LEU PHE GLU GLU SER GLY ASN THR ASP ILE GLU GLY          
SEQRES  11 A  478  ILE ASP THR THR ASN ALA SCY TYR GLY GLY THR ALA ALA          
SEQRES  12 A  478  VAL PHE ASN ALA VAL ASN TRP ILE GLU SER SER SER TRP          
SEQRES  13 A  478  ASP GLY ARG TYR ALA LEU VAL VAL ALA GLY ASP ILE ALA          
SEQRES  14 A  478  VAL TYR ALA THR GLY ASN ALA ARG PRO THR GLY GLY VAL          
SEQRES  15 A  478  GLY ALA VAL ALA LEU LEU ILE GLY PRO ASN ALA PRO LEU          
SEQRES  16 A  478  ILE PHE GLU ARG GLY LEU ARG GLY THR HIS MET GLN HIS          
SEQRES  17 A  478  ALA TYR ASP PHE TYR LYS PRO ASP MET LEU SER GLU TYR          
SEQRES  18 A  478  PRO ILE VAL ASP GLY LYS LEU SER ILE GLN CYS TYR LEU          
SEQRES  19 A  478  SER ALA LEU ASP ARG CYS TYR SER VAL TYR CYS LYS LYS          
SEQRES  20 A  478  ILE HIS ALA GLN TRP GLN LYS GLU GLY ASN ASP LYS ASP          
SEQRES  21 A  478  PHE THR LEU ASN ASP PHE GLY PHE MET ILE PHE HIS SER          
SEQRES  22 A  478  PRO TYR CYS LYS LEU VAL GLN LYS SER LEU ALA ARG MET          
SEQRES  23 A  478  LEU LEU ASN ASP PHE LEU ASN ASP GLN ASN ARG ASP LYS          
SEQRES  24 A  478  ASN SER ILE TYR SER GLY LEU GLU ALA PHE GLY ASP VAL          
SEQRES  25 A  478  LYS LEU GLU ASP THR TYR PHE ASP ARG ASP VAL GLU LYS          
SEQRES  26 A  478  ALA PHE MET LYS ALA SER SER GLU LEU PHE SER GLN LYS          
SEQRES  27 A  478  THR LYS ALA SER LEU LEU VAL SER ASN GLN ASN GLY ASN          
SEQRES  28 A  478  MET TYR THR SER SER VAL TYR GLY SER LEU ALA SER VAL          
SEQRES  29 A  478  LEU ALA GLN TYR SER PRO GLN GLN LEU ALA GLY LYS ARG          
SEQRES  30 A  478  ILE GLY VAL PHE SER TYR GLY SER GLY LEU ALA ALA THR          
SEQRES  31 A  478  LEU TYR SER LEU LYS VAL THR GLN ASP ALA THR PRO GLY          
SEQRES  32 A  478  SER ALA LEU ASP LYS ILE THR ALA SER LEU CYS ASP LEU          
SEQRES  33 A  478  LYS SER ARG LEU ASP SER ARG THR GLY VAL ALA PRO ASP          
SEQRES  34 A  478  VAL PHE ALA GLU ASN MET LYS LEU ARG GLU ASP THR HIS          
SEQRES  35 A  478  HIS LEU VAL ASN TYR ILE PRO GLN GLY SER ILE ASP SER          
SEQRES  36 A  478  LEU PHE GLU GLY THR TRP TYR LEU VAL ARG VAL ASP GLU          
SEQRES  37 A  478  LYS HIS ARG ARG THR TYR ALA ARG ARG PRO                      
SEQRES   1 B  478  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  478  GLY THR GLU ASN LEU TYR PHE GLN SER MET ASP VAL GLY          
SEQRES   3 B  478  ILE VAL ALA LEU GLU ILE TYR PHE PRO SER GLN TYR VAL          
SEQRES   4 B  478  ASP GLN ALA GLU LEU GLU LYS TYR ASP GLY VAL ASP ALA          
SEQRES   5 B  478  GLY LYS TYR THR ILE GLY LEU GLY GLN ALA LYS MET GLY          
SEQRES   6 B  478  PHE CYS THR ASP ARG GLU ASP ILE ASN SER LEU CYS MET          
SEQRES   7 B  478  THR VAL VAL GLN ASN LEU MET GLU ARG ASN ASN LEU SER          
SEQRES   8 B  478  TYR ASP CYS ILE GLY ARG LEU GLU VAL GLY THR GLU THR          
SEQRES   9 B  478  ILE ILE ASP LYS SER LYS SER VAL LYS THR ASN LEU MET          
SEQRES  10 B  478  GLN LEU PHE GLU GLU SER GLY ASN THR ASP ILE GLU GLY          
SEQRES  11 B  478  ILE ASP THR THR ASN ALA SCY TYR GLY GLY THR ALA ALA          
SEQRES  12 B  478  VAL PHE ASN ALA VAL ASN TRP ILE GLU SER SER SER TRP          
SEQRES  13 B  478  ASP GLY ARG TYR ALA LEU VAL VAL ALA GLY ASP ILE ALA          
SEQRES  14 B  478  VAL TYR ALA THR GLY ASN ALA ARG PRO THR GLY GLY VAL          
SEQRES  15 B  478  GLY ALA VAL ALA LEU LEU ILE GLY PRO ASN ALA PRO LEU          
SEQRES  16 B  478  ILE PHE GLU ARG GLY LEU ARG GLY THR HIS MET GLN HIS          
SEQRES  17 B  478  ALA TYR ASP PHE TYR LYS PRO ASP MET LEU SER GLU TYR          
SEQRES  18 B  478  PRO ILE VAL ASP GLY LYS LEU SER ILE GLN CYS TYR LEU          
SEQRES  19 B  478  SER ALA LEU ASP ARG CYS TYR SER VAL TYR CYS LYS LYS          
SEQRES  20 B  478  ILE HIS ALA GLN TRP GLN LYS GLU GLY ASN ASP LYS ASP          
SEQRES  21 B  478  PHE THR LEU ASN ASP PHE GLY PHE MET ILE PHE HIS SER          
SEQRES  22 B  478  PRO TYR CYS LYS LEU VAL GLN LYS SER LEU ALA ARG MET          
SEQRES  23 B  478  LEU LEU ASN ASP PHE LEU ASN ASP GLN ASN ARG ASP LYS          
SEQRES  24 B  478  ASN SER ILE TYR SER GLY LEU GLU ALA PHE GLY ASP VAL          
SEQRES  25 B  478  LYS LEU GLU ASP THR TYR PHE ASP ARG ASP VAL GLU LYS          
SEQRES  26 B  478  ALA PHE MET LYS ALA SER SER GLU LEU PHE SER GLN LYS          
SEQRES  27 B  478  THR LYS ALA SER LEU LEU VAL SER ASN GLN ASN GLY ASN          
SEQRES  28 B  478  MET TYR THR SER SER VAL TYR GLY SER LEU ALA SER VAL          
SEQRES  29 B  478  LEU ALA GLN TYR SER PRO GLN GLN LEU ALA GLY LYS ARG          
SEQRES  30 B  478  ILE GLY VAL PHE SER TYR GLY SER GLY LEU ALA ALA THR          
SEQRES  31 B  478  LEU TYR SER LEU LYS VAL THR GLN ASP ALA THR PRO GLY          
SEQRES  32 B  478  SER ALA LEU ASP LYS ILE THR ALA SER LEU CYS ASP LEU          
SEQRES  33 B  478  LYS SER ARG LEU ASP SER ARG THR GLY VAL ALA PRO ASP          
SEQRES  34 B  478  VAL PHE ALA GLU ASN MET LYS LEU ARG GLU ASP THR HIS          
SEQRES  35 B  478  HIS LEU VAL ASN TYR ILE PRO GLN GLY SER ILE ASP SER          
SEQRES  36 B  478  LEU PHE GLU GLY THR TRP TYR LEU VAL ARG VAL ASP GLU          
SEQRES  37 B  478  LYS HIS ARG ARG THR TYR ALA ARG ARG PRO                      
MODRES 2P8U SCY A  129  CYS  S-ACETYL-CYSTEINE                                  
MODRES 2P8U SCY B  129  CYS  S-ACETYL-CYSTEINE                                  
HET    SCY  A 129       9                                                       
HET    SCY  B 129       9                                                       
HET    COA  A 601      48                                                       
HET    GOL  A 981       6                                                       
HET    COA  B 601      48                                                       
HETNAM     SCY S-ACETYL-CYSTEINE                                                
HETNAM     COA COENZYME A                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  SCY    2(C5 H9 N O3 S)                                              
FORMUL   3  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   4  GOL    C3 H8 O3                                                     
FORMUL   6  HOH   *745(H2 O)                                                    
HELIX    1   1 ASN A    9  ASP A   16  1                                   8    
HELIX    2   2 GLN A   33  GLY A   41  1                                   9    
HELIX    3   3 ASP A   64  ASN A   80  1                                  17    
HELIX    4   4 SER A   83  ASP A   85  5                                   3    
HELIX    5   5 SER A  103  MET A  109  1                                   7    
HELIX    6   6 GLN A  110  PHE A  112  5                                   3    
HELIX    7   7 ASN A  127  SCY A  129  5                                   3    
HELIX    8   8 TYR A  130  GLU A  144  1                                  15    
HELIX    9   9 ALA A  168  GLY A  172  5                                   5    
HELIX   10  10 ASP A  217  GLY A  248  1                                  32    
HELIX   11  11 THR A  254  PHE A  258  5                                   5    
HELIX   12  12 TYR A  267  ASP A  286  1                                  20    
HELIX   13  13 ASN A  288  SER A  296  5                                   9    
HELIX   14  14 LEU A  298  GLY A  302  5                                   5    
HELIX   15  15 LYS A  305  THR A  309  5                                   5    
HELIX   16  16 ASP A  312  SER A  323  1                                  12    
HELIX   17  17 SER A  323  THR A  331  1                                   9    
HELIX   18  18 LYS A  332  SER A  334  5                                   3    
HELIX   19  19 LEU A  335  GLY A  342  1                                   8    
HELIX   20  20 MET A  344  THR A  346  5                                   3    
HELIX   21  21 SER A  347  TYR A  360  1                                  14    
HELIX   22  22 SER A  361  ALA A  366  1                                   6    
HELIX   23  23 SER A  396  SER A  404  1                                   9    
HELIX   24  24 ASP A  407  SER A  414  1                                   8    
HELIX   25  25 ALA A  419  HIS A  434  1                                  16    
HELIX   26  26 LEU B   10  ASP B   16  1                                   7    
HELIX   27  27 GLN B   33  GLY B   41  1                                   9    
HELIX   28  28 ASP B   64  ASN B   80  1                                  17    
HELIX   29  29 SER B   83  ASP B   85  5                                   3    
HELIX   30  30 SER B  103  MET B  109  1                                   7    
HELIX   31  31 GLN B  110  PHE B  112  5                                   3    
HELIX   32  32 ASN B  127  SCY B  129  5                                   3    
HELIX   33  33 TYR B  130  SER B  145  1                                  16    
HELIX   34  34 ALA B  168  GLY B  172  5                                   5    
HELIX   35  35 ASP B  217  GLU B  247  1                                  31    
HELIX   36  36 THR B  254  PHE B  258  5                                   5    
HELIX   37  37 TYR B  267  ASP B  286  1                                  20    
HELIX   38  38 ASN B  288  SER B  296  5                                   9    
HELIX   39  39 LEU B  298  GLY B  302  5                                   5    
HELIX   40  40 LYS B  305  THR B  309  5                                   5    
HELIX   41  41 ASP B  312  SER B  323  1                                  12    
HELIX   42  42 SER B  323  THR B  331  1                                   9    
HELIX   43  43 LYS B  332  SER B  334  5                                   3    
HELIX   44  44 LEU B  335  GLY B  342  1                                   8    
HELIX   45  45 MET B  344  THR B  346  5                                   3    
HELIX   46  46 SER B  347  TYR B  360  1                                  14    
HELIX   47  47 SER B  361  ALA B  366  1                                   6    
HELIX   48  48 SER B  396  SER B  404  1                                   9    
HELIX   49  49 ASP B  407  SER B  414  1                                   8    
HELIX   50  50 ALA B  419  HIS B  434  1                                  16    
SHEET    1   A16 GLY A 195  MET A 198  0                                        
SHEET    2   A16 ALA A 380  VAL A 388 -1  O  LEU A 383   N  GLY A 195           
SHEET    3   A16 LEU A 187  PHE A 189 -1  N  ILE A 188   O  LYS A 387           
SHEET    4   A16 GLY A  18  TYR A  25 -1  N  ILE A  19   O  LEU A 187           
SHEET    5   A16 GLY A 173  GLY A 182 -1  O  LEU A 180   N  VAL A  20           
SHEET    6   A16 TYR A 152  ALA A 161 -1  N  VAL A 155   O  LEU A 179           
SHEET    7   A16 ILE A  87  GLY A  93  1  N  GLY A  88   O  TYR A 152           
SHEET    8   A16 ASP A 124  THR A 126  1  O  THR A 125   N  VAL A  92           
SHEET    9   A16 ASP B 124  THR B 126 -1  O  ASP B 124   N  THR A 126           
SHEET   10   A16 ILE B  87  GLY B  93  1  N  VAL B  92   O  THR B 125           
SHEET   11   A16 TYR B 152  ALA B 161  1  O  TYR B 152   N  GLY B  88           
SHEET   12   A16 GLY B 173  GLY B 182 -1  O  LEU B 179   N  VAL B 155           
SHEET   13   A16 GLY B  18  TYR B  25 -1  N  TYR B  25   O  ALA B 176           
SHEET   14   A16 LEU B 187  PHE B 189 -1  O  LEU B 187   N  ILE B  19           
SHEET   15   A16 ALA B 380  VAL B 388 -1  O  LYS B 387   N  ILE B 188           
SHEET   16   A16 GLY B 195  MET B 198 -1  N  GLY B 195   O  LEU B 383           
SHEET    1   B18 PHE A 260  PHE A 263  0                                        
SHEET    2   B18 ARG A 369  GLY A 376  1  O  GLY A 371   N  PHE A 260           
SHEET    3   B18 ALA A 380  VAL A 388 -1  O  TYR A 384   N  VAL A 372           
SHEET    4   B18 LEU A 187  PHE A 189 -1  N  ILE A 188   O  LYS A 387           
SHEET    5   B18 GLY A  18  TYR A  25 -1  N  ILE A  19   O  LEU A 187           
SHEET    6   B18 GLY A 173  GLY A 182 -1  O  LEU A 180   N  VAL A  20           
SHEET    7   B18 TYR A 152  ALA A 161 -1  N  VAL A 155   O  LEU A 179           
SHEET    8   B18 ILE A  87  GLY A  93  1  N  GLY A  88   O  TYR A 152           
SHEET    9   B18 ASP A 124  THR A 126  1  O  THR A 125   N  VAL A  92           
SHEET   10   B18 ASP B 124  THR B 126 -1  O  ASP B 124   N  THR A 126           
SHEET   11   B18 ILE B  87  GLY B  93  1  N  VAL B  92   O  THR B 125           
SHEET   12   B18 TYR B 152  ALA B 161  1  O  TYR B 152   N  GLY B  88           
SHEET   13   B18 GLY B 173  GLY B 182 -1  O  LEU B 179   N  VAL B 155           
SHEET   14   B18 GLY B  18  TYR B  25 -1  N  TYR B  25   O  ALA B 176           
SHEET   15   B18 LEU B 187  PHE B 189 -1  O  LEU B 187   N  ILE B  19           
SHEET   16   B18 ALA B 380  VAL B 388 -1  O  LYS B 387   N  ILE B 188           
SHEET   17   B18 ARG B 369  GLY B 376 -1  N  VAL B 372   O  TYR B 384           
SHEET   18   B18 PHE B 260  PHE B 263  1  N  ILE B 262   O  GLY B 371           
SHEET    1   C 3 LYS A  55  GLY A  57  0                                        
SHEET    2   C 3 GLN A  29  ASP A  32 -1  N  VAL A  31   O  MET A  56           
SHEET    3   C 3 THR A 416  GLY A 417  1  O  THR A 416   N  TYR A  30           
SHEET    1   D 2 PHE A 204  TYR A 205  0                                        
SHEET    2   D 2 ILE A 215  VAL A 216 -1  O  ILE A 215   N  TYR A 205           
SHEET    1   E 2 TRP A 453  VAL A 458  0                                        
SHEET    2   E 2 ARG A 464  ARG A 468 -1  O  THR A 465   N  VAL A 456           
SHEET    1   F 3 LYS B  55  GLY B  57  0                                        
SHEET    2   F 3 GLN B  29  ASP B  32 -1  N  VAL B  31   O  MET B  56           
SHEET    3   F 3 THR B 416  GLY B 417  1  O  THR B 416   N  TYR B  30           
SHEET    1   G 2 PHE B 204  TYR B 205  0                                        
SHEET    2   G 2 ILE B 215  VAL B 216 -1  O  ILE B 215   N  TYR B 205           
SHEET    1   H 2 TRP B 453  VAL B 458  0                                        
SHEET    2   H 2 ARG B 464  ARG B 468 -1  O  THR B 465   N  VAL B 456           
LINK         C   ALA A 128                 N   SCY A 129     1555   1555  1.35  
LINK         C   SCY A 129                 N   TYR A 130     1555   1555  1.34  
LINK         C   ALA B 128                 N   SCY B 129     1555   1555  1.34  
LINK         C   SCY B 129                 N   TYR B 130     1555   1555  1.33  
CISPEP   1 GLY A  378    LEU A  379          0        -8.06                     
CISPEP   2 GLY B  378    LEU B  379          0        -6.92                     
SITE     1 AC1 17 ASP A  43  ALA A  44  GLY A  45  LYS A  46                    
SITE     2 AC1 17 GLY A  50  TYR A 163  ASN A 167  ALA A 168                    
SITE     3 AC1 17 THR A 171  SER A 221  PRO A 266  TYR A 267                    
SITE     4 AC1 17 LYS A 269  LEU A 270  LYS A 273  HOH A1097                    
SITE     5 AC1 17 HOH A1252                                                     
SITE     1 AC2  5 LYS A 461  ARG A 463  LYS B 461  ARG B 463                    
SITE     2 AC2  5 HOH B 795                                                     
SITE     1 AC3 25 ALA B  44  GLY B  45  LYS B  46  GLY B  50                    
SITE     2 AC3 25 TYR B 163  ASN B 167  ALA B 168  THR B 171                    
SITE     3 AC3 25 SER B 221  PRO B 266  TYR B 267  LYS B 269                    
SITE     4 AC3 25 LEU B 270  LYS B 273  HOH B 638  HOH B 698                    
SITE     5 AC3 25 HOH B 774  HOH B 776  HOH B 819  HOH B 866                    
SITE     6 AC3 25 HOH B 895  HOH B 909  HOH B 912  HOH B 936                    
SITE     7 AC3 25 HOH B 966                                                     
CRYST1   92.762   92.762  235.532  90.00  90.00  90.00 P 43 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      0.010780  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010780  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004246        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system