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Database: PDB
Entry: 6MVP
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Original site: 6MVP 
HEADER    VIRAL PROTEIN                           26-OCT-18   6MVP              
TITLE     HCV NS5B 1B N316 BOUND TO COMPOUND 18                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GENOME POLYPROTEIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.22.-,3.4.21.98,3.6.1.15,3.6.4.13,2.7.7.48;                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS GENOTYPE 1B (ISOLATE BK);     
SOURCE   3 ORGANISM_COMMON: HCV;                                                
SOURCE   4 ORGANISM_TAXID: 11105;                                               
SOURCE   5 STRAIN: ISOLATE BK;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    HEPATITUS C, NS5B, VIRAL PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.P.WILLIAMS,K.KAHLER,D.J.PRICE,A.J.PEAT                              
REVDAT   2   13-MAR-24 6MVP    1       REMARK                                   
REVDAT   1   04-SEP-19 6MVP    0                                                
JRNL        AUTH   P.Y.CHONG,J.B.SHOTWELL,J.MILLER,D.J.PRICE,A.MAYNARD,         
JRNL        AUTH 2 C.VOITENLEITNER,A.MATHIS,S.WILLIAMS,J.J.POULIOT,K.CREECH,    
JRNL        AUTH 3 F.WANG,J.FANG,H.ZHANG,V.W.TAI,E.TURNER,K.M.KAHLER,R.CROSBY,  
JRNL        AUTH 4 A.J.PEAT                                                     
JRNL        TITL   DESIGN OF N-BENZOXABOROLE BENZOFURAN GSK8175-OPTIMIZATION OF 
JRNL        TITL 2 HUMAN PHARMACOKINETICS INSPIRED BY METABOLITES OF A FAILED   
JRNL        TITL 3 CLINICAL HCV INHIBITOR.                                      
JRNL        REF    J.MED.CHEM.                   V.  62  3254 2019              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   30763090                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B01719                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0081                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 72491                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5457                            
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) : 5425                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 401                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8356                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 74                                      
REMARK   3   SOLVENT ATOMS            : 528                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.26000                                             
REMARK   3    B22 (A**2) : 1.15000                                              
REMARK   3    B33 (A**2) : -0.89000                                             
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): 0.223         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.176         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.907         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.952                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8637 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8065 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11774 ; 1.200 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18530 ; 1.041 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1100 ; 5.328 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   335 ;33.003 ;23.164       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1377 ;11.855 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    57 ;13.577 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1345 ; 0.066 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9742 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1941 ; 0.002 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    563       B     1    563   64778 0.070 0.050     
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 :   A     1        A   563                          
REMARK   3    RESIDUE RANGE :   A   601        A   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):   11.581   46.034   47.082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0520 T22:   0.0480                                     
REMARK   3      T33:   0.0117 T12:  -0.0335                                     
REMARK   3      T13:  -0.0122 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3835 L22:   0.1418                                     
REMARK   3      L33:   0.8983 L12:  -0.1055                                     
REMARK   3      L13:   0.3422 L23:  -0.0804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0904 S12:  -0.0418 S13:   0.0164                       
REMARK   3      S21:   0.0000 S22:  -0.0552 S23:  -0.0234                       
REMARK   3      S31:   0.1091 S32:  -0.0310 S33:  -0.0352                       
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 :   B     1        B   563                          
REMARK   3    RESIDUE RANGE :   B   601        B   601                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.599   46.196   -7.851              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0304 T22:   0.0337                                     
REMARK   3      T33:   0.0081 T12:   0.0247                                     
REMARK   3      T13:  -0.0052 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4916 L22:   0.1710                                     
REMARK   3      L33:   0.6596 L12:   0.0877                                     
REMARK   3      L13:   0.1682 L23:   0.0697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0631 S12:   0.0504 S13:   0.0130                       
REMARK   3      S21:   0.0078 S22:  -0.0372 S23:   0.0283                       
REMARK   3      S31:   0.0484 S32:   0.0417 S33:  -0.0259                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: U VALUES : WITH TLS ADDED HYDROGENS       
REMARK   3  HAVE BEEN ADDED IN THE RIDING POSITIONS                             
REMARK   4                                                                      
REMARK   4 6MVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000237686.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAR-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79393                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE PH5.0, 10% GLYCEROL,     
REMARK 280  15% PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       43.19950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.12050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.65550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.12050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.19950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.65550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 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 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    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     GLU A   150                                                      
REMARK 465     LYS A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     ALA A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 465     ARG A   544                                                      
REMARK 465     LEU A   545                                                      
REMARK 465     ASP A   546                                                      
REMARK 465     LEU A   547                                                      
REMARK 465     SER A   548                                                      
REMARK 465     GLY A   549                                                      
REMARK 465     TRP A   550                                                      
REMARK 465     PHE A   551                                                      
REMARK 465     LEU A   564                                                      
REMARK 465     SER A   565                                                      
REMARK 465     ARG A   566                                                      
REMARK 465     ALA A   567                                                      
REMARK 465     ARG A   568                                                      
REMARK 465     PRO A   569                                                      
REMARK 465     ARG A   570                                                      
REMARK 465     LEU A   571                                                      
REMARK 465     GLU A   572                                                      
REMARK 465     HIS A   573                                                      
REMARK 465     HIS A   574                                                      
REMARK 465     HIS A   575                                                      
REMARK 465     HIS A   576                                                      
REMARK 465     HIS A   577                                                      
REMARK 465     HIS A   578                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     GLU B   150                                                      
REMARK 465     LYS B   151                                                      
REMARK 465     GLY B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     ALA B   541                                                      
REMARK 465     ALA B   542                                                      
REMARK 465     SER B   543                                                      
REMARK 465     ARG B   544                                                      
REMARK 465     LEU B   545                                                      
REMARK 465     ASP B   546                                                      
REMARK 465     LEU B   547                                                      
REMARK 465     SER B   548                                                      
REMARK 465     GLY B   549                                                      
REMARK 465     LEU B   564                                                      
REMARK 465     SER B   565                                                      
REMARK 465     ARG B   566                                                      
REMARK 465     ALA B   567                                                      
REMARK 465     ARG B   568                                                      
REMARK 465     PRO B   569                                                      
REMARK 465     ARG B   570                                                      
REMARK 465     LEU B   571                                                      
REMARK 465     GLU B   572                                                      
REMARK 465     HIS B   573                                                      
REMARK 465     HIS B   574                                                      
REMARK 465     HIS B   575                                                      
REMARK 465     HIS B   576                                                      
REMARK 465     HIS B   577                                                      
REMARK 465     HIS B   578                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  43    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A  47    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  50    CD   CE   NZ                                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     LYS A  81    CD   CE   NZ                                        
REMARK 470     GLU A  86    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  90    CG   CD   CE   NZ                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     LYS A 106    CD   CE   NZ                                        
REMARK 470     ARG A 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO A 149    CG   CD                                             
REMARK 470     ARG A 158    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
REMARK 470     ARG A 222    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 270    CE   NZ                                             
REMARK 470     LYS A 307    CD   CE   NZ                                        
REMARK 470     GLN A 309    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 380    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 440    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 461    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 498    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 501    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 523    CD   CE   NZ                                        
REMARK 470     LYS A 531    CD   CE   NZ                                        
REMARK 470     THR A 532    OG1  CG2                                            
REMARK 470     LEU A 534    CG   CD1  CD2                                       
REMARK 470     LYS A 535    CG   CD   CE   NZ                                   
REMARK 470     VAL A 552    CG1  CG2                                            
REMARK 470     SER A 563    OG                                                  
REMARK 470     ARG B  32    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 100    CG   CD   CE   NZ                                   
REMARK 470     ARG B 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 141    CE   NZ                                             
REMARK 470     GLN B 148    CG   CD   OE1  NE2                                  
REMARK 470     PRO B 149    CG   CD                                             
REMARK 470     ARG B 154    CZ   NH1  NH2                                       
REMARK 470     LYS B 155    CE   NZ                                             
REMARK 470     ARG B 158    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B 202    CD   OE1  OE2                                       
REMARK 470     LYS B 212    CG   CD   CE   NZ                                   
REMARK 470     ARG B 222    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 270    CE   NZ                                             
REMARK 470     LYS B 307    CE   NZ                                             
REMARK 470     GLN B 309    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 352    CG   OD1  OD2                                       
REMARK 470     ARG B 380    CZ   NH1  NH2                                       
REMARK 470     GLN B 461    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 501    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 505    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     LYS B 531    CG   CD   CE   NZ                                   
REMARK 470     THR B 532    OG1  CG2                                            
REMARK 470     LEU B 534    CG   CD1  CD2                                       
REMARK 470     LYS B 535    CG   CD   CE   NZ                                   
REMARK 470     TRP B 550    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 550    CZ3  CH2                                            
REMARK 470     SER B 563    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   NH1  ARG A   200     O    HOH A   701              1.85            
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    LEU A 260      -57.03   -125.95                                   
REMARK 500    SER A 347        5.59     92.48                                   
REMARK 500    ALA A 348       70.30   -116.45                                   
REMARK 500    LEU B 260      -56.51   -125.81                                   
REMARK 500    SER B 347        6.11     91.24                                   
REMARK 500    ALA B 348       70.26   -115.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 968        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A 969        DISTANCE =  6.05 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K4S A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K4S B 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6MVK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6MVQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6MVO   RELATED DB: PDB                                   
DBREF  6MVP A    1   570  UNP    P26663   POLG_HCVBK    2420   2989             
DBREF  6MVP B    1   570  UNP    P26663   POLG_HCVBK    2420   2989             
SEQADV 6MVP MET A   -1  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP ALA A    0  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP GLN A   47  UNP  P26663    LEU  2466 CONFLICT                       
SEQADV 6MVP TYR A  101  UNP  P26663    PHE  2520 CONFLICT                       
SEQADV 6MVP ARG A  114  UNP  P26663    LYS  2533 CONFLICT                       
SEQADV 6MVP VAL A  329  UNP  P26663    THR  2748 CONFLICT                       
SEQADV 6MVP LEU A  571  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP GLU A  572  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  573  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  574  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  575  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  576  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  577  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS A  578  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP MET B   -1  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP ALA B    0  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP GLN B   47  UNP  P26663    LEU  2466 CONFLICT                       
SEQADV 6MVP TYR B  101  UNP  P26663    PHE  2520 CONFLICT                       
SEQADV 6MVP ARG B  114  UNP  P26663    LYS  2533 CONFLICT                       
SEQADV 6MVP VAL B  329  UNP  P26663    THR  2748 CONFLICT                       
SEQADV 6MVP LEU B  571  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP GLU B  572  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  573  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  574  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  575  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  576  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  577  UNP  P26663              EXPRESSION TAG                 
SEQADV 6MVP HIS B  578  UNP  P26663              EXPRESSION TAG                 
SEQRES   1 A  580  MET ALA SER MET SER TYR THR TRP THR GLY ALA LEU ILE          
SEQRES   2 A  580  THR PRO CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN          
SEQRES   3 A  580  ALA LEU SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL          
SEQRES   4 A  580  TYR ALA THR THR SER ARG SER ALA GLY GLN ARG GLN LYS          
SEQRES   5 A  580  LYS VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS          
SEQRES   6 A  580  TYR ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER          
SEQRES   7 A  580  THR VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS          
SEQRES   8 A  580  LYS LEU THR PRO PRO HIS SER ALA LYS SER LYS TYR GLY          
SEQRES   9 A  580  TYR GLY ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA          
SEQRES  10 A  580  VAL ASN HIS ILE HIS SER VAL TRP LYS ASP LEU LEU GLU          
SEQRES  11 A  580  ASP THR VAL THR PRO ILE ASP THR THR ILE MET ALA LYS          
SEQRES  12 A  580  ASN GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG          
SEQRES  13 A  580  LYS PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL          
SEQRES  14 A  580  ARG VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER          
SEQRES  15 A  580  THR LEU PRO GLN VAL VAL MET GLY SER SER TYR GLY PHE          
SEQRES  16 A  580  GLN TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN          
SEQRES  17 A  580  THR TRP LYS SER LYS LYS ASN PRO MET GLY PHE SER TYR          
SEQRES  18 A  580  ASP THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP          
SEQRES  19 A  580  ILE ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU          
SEQRES  20 A  580  ALA PRO GLU ALA ARG GLN ALA ILE LYS SER LEU THR GLU          
SEQRES  21 A  580  ARG LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY          
SEQRES  22 A  580  GLN ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL          
SEQRES  23 A  580  LEU THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU          
SEQRES  24 A  580  LYS ALA SER ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP          
SEQRES  25 A  580  CYS THR MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE          
SEQRES  26 A  580  CYS GLU SER ALA GLY VAL GLN GLU ASP ALA ALA SER LEU          
SEQRES  27 A  580  ARG VAL PHE THR GLU ALA MET THR ARG TYR SER ALA PRO          
SEQRES  28 A  580  PRO GLY ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU          
SEQRES  29 A  580  ILE THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP          
SEQRES  30 A  580  ALA SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO          
SEQRES  31 A  580  THR THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG          
SEQRES  32 A  580  HIS THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET          
SEQRES  33 A  580  TYR ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR          
SEQRES  34 A  580  HIS PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU          
SEQRES  35 A  580  LYS ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER          
SEQRES  36 A  580  ILE GLU PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU          
SEQRES  37 A  580  HIS GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO          
SEQRES  38 A  580  GLY GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU          
SEQRES  39 A  580  GLY VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG          
SEQRES  40 A  580  SER VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA          
SEQRES  41 A  580  ALA THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL LYS          
SEQRES  42 A  580  THR LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER ARG          
SEQRES  43 A  580  LEU ASP LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY          
SEQRES  44 A  580  GLY ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG          
SEQRES  45 A  580  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  580  MET ALA SER MET SER TYR THR TRP THR GLY ALA LEU ILE          
SEQRES   2 B  580  THR PRO CYS ALA ALA GLU GLU SER LYS LEU PRO ILE ASN          
SEQRES   3 B  580  ALA LEU SER ASN SER LEU LEU ARG HIS HIS ASN MET VAL          
SEQRES   4 B  580  TYR ALA THR THR SER ARG SER ALA GLY GLN ARG GLN LYS          
SEQRES   5 B  580  LYS VAL THR PHE ASP ARG LEU GLN VAL LEU ASP ASP HIS          
SEQRES   6 B  580  TYR ARG ASP VAL LEU LYS GLU MET LYS ALA LYS ALA SER          
SEQRES   7 B  580  THR VAL LYS ALA LYS LEU LEU SER VAL GLU GLU ALA CYS          
SEQRES   8 B  580  LYS LEU THR PRO PRO HIS SER ALA LYS SER LYS TYR GLY          
SEQRES   9 B  580  TYR GLY ALA LYS ASP VAL ARG ASN LEU SER SER ARG ALA          
SEQRES  10 B  580  VAL ASN HIS ILE HIS SER VAL TRP LYS ASP LEU LEU GLU          
SEQRES  11 B  580  ASP THR VAL THR PRO ILE ASP THR THR ILE MET ALA LYS          
SEQRES  12 B  580  ASN GLU VAL PHE CYS VAL GLN PRO GLU LYS GLY GLY ARG          
SEQRES  13 B  580  LYS PRO ALA ARG LEU ILE VAL PHE PRO ASP LEU GLY VAL          
SEQRES  14 B  580  ARG VAL CYS GLU LYS MET ALA LEU TYR ASP VAL VAL SER          
SEQRES  15 B  580  THR LEU PRO GLN VAL VAL MET GLY SER SER TYR GLY PHE          
SEQRES  16 B  580  GLN TYR SER PRO GLY GLN ARG VAL GLU PHE LEU VAL ASN          
SEQRES  17 B  580  THR TRP LYS SER LYS LYS ASN PRO MET GLY PHE SER TYR          
SEQRES  18 B  580  ASP THR ARG CYS PHE ASP SER THR VAL THR GLU ASN ASP          
SEQRES  19 B  580  ILE ARG VAL GLU GLU SER ILE TYR GLN CYS CYS ASP LEU          
SEQRES  20 B  580  ALA PRO GLU ALA ARG GLN ALA ILE LYS SER LEU THR GLU          
SEQRES  21 B  580  ARG LEU TYR ILE GLY GLY PRO LEU THR ASN SER LYS GLY          
SEQRES  22 B  580  GLN ASN CYS GLY TYR ARG ARG CYS ARG ALA SER GLY VAL          
SEQRES  23 B  580  LEU THR THR SER CYS GLY ASN THR LEU THR CYS TYR LEU          
SEQRES  24 B  580  LYS ALA SER ALA ALA CYS ARG ALA ALA LYS LEU GLN ASP          
SEQRES  25 B  580  CYS THR MET LEU VAL ASN GLY ASP ASP LEU VAL VAL ILE          
SEQRES  26 B  580  CYS GLU SER ALA GLY VAL GLN GLU ASP ALA ALA SER LEU          
SEQRES  27 B  580  ARG VAL PHE THR GLU ALA MET THR ARG TYR SER ALA PRO          
SEQRES  28 B  580  PRO GLY ASP PRO PRO GLN PRO GLU TYR ASP LEU GLU LEU          
SEQRES  29 B  580  ILE THR SER CYS SER SER ASN VAL SER VAL ALA HIS ASP          
SEQRES  30 B  580  ALA SER GLY LYS ARG VAL TYR TYR LEU THR ARG ASP PRO          
SEQRES  31 B  580  THR THR PRO LEU ALA ARG ALA ALA TRP GLU THR ALA ARG          
SEQRES  32 B  580  HIS THR PRO VAL ASN SER TRP LEU GLY ASN ILE ILE MET          
SEQRES  33 B  580  TYR ALA PRO THR LEU TRP ALA ARG MET ILE LEU MET THR          
SEQRES  34 B  580  HIS PHE PHE SER ILE LEU LEU ALA GLN GLU GLN LEU GLU          
SEQRES  35 B  580  LYS ALA LEU ASP CYS GLN ILE TYR GLY ALA CYS TYR SER          
SEQRES  36 B  580  ILE GLU PRO LEU ASP LEU PRO GLN ILE ILE GLU ARG LEU          
SEQRES  37 B  580  HIS GLY LEU SER ALA PHE SER LEU HIS SER TYR SER PRO          
SEQRES  38 B  580  GLY GLU ILE ASN ARG VAL ALA SER CYS LEU ARG LYS LEU          
SEQRES  39 B  580  GLY VAL PRO PRO LEU ARG VAL TRP ARG HIS ARG ALA ARG          
SEQRES  40 B  580  SER VAL ARG ALA ARG LEU LEU SER GLN GLY GLY ARG ALA          
SEQRES  41 B  580  ALA THR CYS GLY LYS TYR LEU PHE ASN TRP ALA VAL LYS          
SEQRES  42 B  580  THR LYS LEU LYS LEU THR PRO ILE PRO ALA ALA SER ARG          
SEQRES  43 B  580  LEU ASP LEU SER GLY TRP PHE VAL ALA GLY TYR SER GLY          
SEQRES  44 B  580  GLY ASP ILE TYR HIS SER LEU SER ARG ALA ARG PRO ARG          
SEQRES  45 B  580  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET    K4S  A 601      37                                                       
HET    K4S  B 601      37                                                       
HETNAM     K4S (4-{[5-CYCLOPROPYL-2-(4-FLUOROPHENYL)-3-                         
HETNAM   2 K4S  (METHYLCARBAMOYL)-1-BENZOFURAN-6-YL](METHYLSULFONYL)            
HETNAM   3 K4S  AMINO}PHENYL)BORONIC ACID                                       
FORMUL   3  K4S    2(C26 H24 B F N2 O6 S)                                       
FORMUL   5  HOH   *528(H2 O)                                                    
HELIX    1 AA1 LEU A   26  LEU A   31  1                                   6    
HELIX    2 AA2 HIS A   33  ASN A   35  5                                   3    
HELIX    3 AA3 THR A   41  ARG A   43  5                                   3    
HELIX    4 AA4 SER A   44  THR A   53  1                                  10    
HELIX    5 AA5 ASP A   61  SER A   76  1                                  16    
HELIX    6 AA6 SER A   84  LEU A   91  1                                   8    
HELIX    7 AA7 GLY A  104  ASN A  110  1                                   7    
HELIX    8 AA8 SER A  112  ASP A  129  1                                  18    
HELIX    9 AA9 ASP A  164  GLY A  188  1                                  25    
HELIX   10 AB1 SER A  189  TYR A  195  5                                   7    
HELIX   11 AB2 SER A  196  SER A  210  1                                  15    
HELIX   12 AB3 CYS A  223  VAL A  228  1                                   6    
HELIX   13 AB4 THR A  229  CYS A  242  1                                  14    
HELIX   14 AB5 ALA A  246  LEU A  260  1                                  15    
HELIX   15 AB6 THR A  286  ALA A  306  1                                  21    
HELIX   16 AB7 GLY A  328  TYR A  346  1                                  19    
HELIX   17 AB8 ASP A  359  ILE A  363  5                                   5    
HELIX   18 AB9 PRO A  388  ARG A  401  1                                  14    
HELIX   19 AC1 ASN A  406  TYR A  415  1                                  10    
HELIX   20 AC2 THR A  418  ILE A  424  1                                   7    
HELIX   21 AC3 ILE A  424  GLU A  437  1                                  14    
HELIX   22 AC4 GLU A  455  LEU A  457  5                                   3    
HELIX   23 AC5 ASP A  458  GLY A  468  1                                  11    
HELIX   24 AC6 LEU A  469  SER A  473  5                                   5    
HELIX   25 AC7 SER A  478  GLY A  493  1                                  16    
HELIX   26 AC8 PRO A  496  GLY A  515  1                                  20    
HELIX   27 AC9 GLY A  515  PHE A  526  1                                  12    
HELIX   28 AD1 ASN A  527  VAL A  530  5                                   4    
HELIX   29 AD2 LEU B   26  LEU B   31  1                                   6    
HELIX   30 AD3 HIS B   33  ASN B   35  5                                   3    
HELIX   31 AD4 THR B   41  ARG B   43  5                                   3    
HELIX   32 AD5 SER B   44  THR B   53  1                                  10    
HELIX   33 AD6 ASP B   61  SER B   76  1                                  16    
HELIX   34 AD7 SER B   84  LEU B   91  1                                   8    
HELIX   35 AD8 GLY B  104  ASN B  110  1                                   7    
HELIX   36 AD9 SER B  112  ASP B  129  1                                  18    
HELIX   37 AE1 ASP B  164  GLY B  188  1                                  25    
HELIX   38 AE2 SER B  189  TYR B  195  5                                   7    
HELIX   39 AE3 SER B  196  SER B  210  1                                  15    
HELIX   40 AE4 CYS B  223  VAL B  228  1                                   6    
HELIX   41 AE5 THR B  229  CYS B  242  1                                  14    
HELIX   42 AE6 ALA B  246  LEU B  260  1                                  15    
HELIX   43 AE7 THR B  286  ALA B  306  1                                  21    
HELIX   44 AE8 GLY B  328  TYR B  346  1                                  19    
HELIX   45 AE9 ASP B  359  ILE B  363  5                                   5    
HELIX   46 AF1 PRO B  388  ARG B  401  1                                  14    
HELIX   47 AF2 ASN B  406  TYR B  415  1                                  10    
HELIX   48 AF3 THR B  418  ILE B  424  1                                   7    
HELIX   49 AF4 ILE B  424  GLU B  437  1                                  14    
HELIX   50 AF5 GLU B  455  LEU B  457  5                                   3    
HELIX   51 AF6 ASP B  458  GLY B  468  1                                  11    
HELIX   52 AF7 LEU B  469  SER B  473  5                                   5    
HELIX   53 AF8 SER B  478  GLY B  493  1                                  16    
HELIX   54 AF9 PRO B  496  GLY B  515  1                                  20    
HELIX   55 AG1 GLY B  515  PHE B  526  1                                  12    
HELIX   56 AG2 ASN B  527  VAL B  530  5                                   4    
SHEET    1 AA1 5 TYR A   4  TRP A   6  0                                        
SHEET    2 AA1 5 ASN A 273  ARG A 277 -1  O  TYR A 276   N  THR A   5           
SHEET    3 AA1 5 GLY A 264  THR A 267 -1  N  LEU A 266   O  CYS A 274           
SHEET    4 AA1 5 THR A 136  ALA A 140  1  N  THR A 136   O  THR A 267           
SHEET    5 AA1 5 LEU A 159  PHE A 162 -1  O  PHE A 162   N  THR A 137           
SHEET    1 AA2 2 VAL A  37  ALA A  39  0                                        
SHEET    2 AA2 2 VAL A 144  CYS A 146 -1  O  PHE A 145   N  TYR A  38           
SHEET    1 AA3 3 PRO A 214  ASP A 220  0                                        
SHEET    2 AA3 3 ASP A 319  GLU A 325 -1  O  CYS A 324   N  MET A 215           
SHEET    3 AA3 3 GLN A 309  ASN A 316 -1  N  THR A 312   O  ILE A 323           
SHEET    1 AA4 2 SER A 368  HIS A 374  0                                        
SHEET    2 AA4 2 ARG A 380  ARG A 386 -1  O  VAL A 381   N  ALA A 373           
SHEET    1 AA5 3 LEU A 443  ILE A 447  0                                        
SHEET    2 AA5 3 ALA A 450  ILE A 454 -1  O  TYR A 452   N  CYS A 445           
SHEET    3 AA5 3 TYR A 561  HIS A 562  1  O  HIS A 562   N  CYS A 451           
SHEET    1 AA6 5 TYR B   4  TRP B   6  0                                        
SHEET    2 AA6 5 ASN B 273  ARG B 277 -1  O  TYR B 276   N  THR B   5           
SHEET    3 AA6 5 GLY B 264  THR B 267 -1  N  LEU B 266   O  CYS B 274           
SHEET    4 AA6 5 THR B 136  ALA B 140  1  N  THR B 136   O  THR B 267           
SHEET    5 AA6 5 LEU B 159  PHE B 162 -1  O  PHE B 162   N  THR B 137           
SHEET    1 AA7 2 VAL B  37  ALA B  39  0                                        
SHEET    2 AA7 2 VAL B 144  CYS B 146 -1  O  PHE B 145   N  TYR B  38           
SHEET    1 AA8 3 PRO B 214  ASP B 220  0                                        
SHEET    2 AA8 3 ASP B 319  GLU B 325 -1  O  CYS B 324   N  MET B 215           
SHEET    3 AA8 3 GLN B 309  ASN B 316 -1  N  THR B 312   O  ILE B 323           
SHEET    1 AA9 2 SER B 368  HIS B 374  0                                        
SHEET    2 AA9 2 ARG B 380  ARG B 386 -1  O  VAL B 381   N  ALA B 373           
SHEET    1 AB1 3 LEU B 443  ILE B 447  0                                        
SHEET    2 AB1 3 ALA B 450  ILE B 454 -1  O  TYR B 452   N  CYS B 445           
SHEET    3 AB1 3 TYR B 561  HIS B 562  1  O  HIS B 562   N  CYS B 451           
SITE     1 AC1 18 PRO A 197  ARG A 200  LEU A 204  LEU A 314                    
SITE     2 AC1 18 ASN A 316  VAL A 321  LEU A 360  ILE A 363                    
SITE     3 AC1 18 SER A 365  CYS A 366  SER A 368  LEU A 384                    
SITE     4 AC1 18 MET A 414  TYR A 415  TYR A 448  HOH A 701                    
SITE     5 AC1 18 HOH A 702  HOH A 705                                          
SITE     1 AC2 16 PRO B 197  ARG B 200  LEU B 204  LEU B 314                    
SITE     2 AC2 16 ASN B 316  ASP B 319  LEU B 360  ILE B 363                    
SITE     3 AC2 16 SER B 365  CYS B 366  SER B 368  LEU B 384                    
SITE     4 AC2 16 MET B 414  TYR B 415  TYR B 448  HOH B 701                    
CRYST1   86.399  107.311  126.241  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011574  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007921        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system