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Database: PDB
Entry: 4Q0X
LinkDB: 4Q0X
Original site: 4Q0X 
HEADER    IMMUNE SYSTEM/VIRAL PROTEIN             02-APR-14   4Q0X              
TITLE     CRYSTAL STRUCTURE OF NON-NEUTRALIZING ANTIBODY IN COMPLEX WITH EPITOPE
TITLE    2 II OF HCV E2                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAB 12 HEAVY CHAIN;                                        
COMPND   3 CHAIN: H;                                                            
COMPND   4 FRAGMENT: FAB;                                                       
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MAB 12 LIGHT CHAIN;                                        
COMPND   7 CHAIN: L;                                                            
COMPND   8 FRAGMENT: FAB;                                                       
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ENVELOPE GLYCOPROTEIN E2;                                  
COMPND  11 CHAIN: E;                                                            
COMPND  12 FRAGMENT: EPITOPE II (UNP RESIDUES 421-446);                         
COMPND  13 SYNONYM: NS1, GP68, GP70                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   7 ORGANISM_COMMON: MOUSE;                                              
SOURCE   8 ORGANISM_TAXID: 10090;                                               
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS;                              
SOURCE  11 ORGANISM_COMMON: HCV;                                                
SOURCE  12 ORGANISM_TAXID: 11103                                                
KEYWDS    ANTIBODY, ANTI-HCV E2, HCV E2, IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DENG,P.ZHANG                                                        
REVDAT   3   06-AUG-14 4Q0X    1       JRNL                                     
REVDAT   2   23-JUL-14 4Q0X    1       JRNL                                     
REVDAT   1   09-JUL-14 4Q0X    0                                                
JRNL        AUTH   L.DENG,L.MA,M.L.VIRATA-THEIMER,L.ZHONG,H.YAN,Z.ZHAO,         
JRNL        AUTH 2 E.STRUBLE,S.FEINSTONE,H.ALTER,P.ZHANG                        
JRNL        TITL   DISCRETE CONFORMATIONS OF EPITOPE II ON THE HEPATITIS C      
JRNL        TITL 2 VIRUS E2 PROTEIN FOR ANTIBODY-MEDIATED NEUTRALIZATION AND    
JRNL        TITL 3 NONNEUTRALIZATION.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 111 10690 2014              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   25002515                                                     
JRNL        DOI    10.1073/PNAS.1411317111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11454                          
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) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.285                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 606                             
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 826                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.4360                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3398                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.45000                                              
REMARK   3    B22 (A**2) : 1.45000                                              
REMARK   3    B33 (A**2) : -2.90000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.459         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.379         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 44.623        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.887                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3489 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4756 ; 1.222 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   439 ;12.255 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;34.695 ;24.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   546 ;16.759 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;21.435 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   530 ; 0.071 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2633 ; 0.014 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1768 ; 0.981 ; 5.011       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2203 ; 1.797 ; 7.502       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1717 ; 0.657 ; 5.008       
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):  5049 ; 5.019 ;42.177       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H   117                          
REMARK   3    RESIDUE RANGE :   L     1        L   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.9876  13.4151  17.0542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4646 T22:   0.0564                                     
REMARK   3      T33:   0.0303 T12:  -0.0363                                     
REMARK   3      T13:  -0.0149 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8667 L22:   4.0824                                     
REMARK   3      L33:   2.7444 L12:   0.4699                                     
REMARK   3      L13:   0.8429 L23:  -0.5057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0658 S12:   0.1221 S13:   0.0434                       
REMARK   3      S21:  -0.6257 S22:   0.1024 S23:   0.2112                       
REMARK   3      S31:  -0.2303 S32:  -0.1706 S33:  -0.0366                       
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 :   H   123        H   218                          
REMARK   3    RESIDUE RANGE :   L   115        L   217                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9172  -5.9579  44.7724              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0727 T22:   0.0715                                     
REMARK   3      T33:   0.1716 T12:  -0.0320                                     
REMARK   3      T13:   0.0425 T23:  -0.0402                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4601 L22:   2.7127                                     
REMARK   3      L33:   2.5446 L12:   0.9980                                     
REMARK   3      L13:   1.1802 L23:   0.4889                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:  -0.2810 S13:  -0.1696                       
REMARK   3      S21:  -0.3743 S22:   0.0804 S23:  -0.1808                       
REMARK   3      S31:  -0.0786 S32:   0.1346 S33:  -0.0880                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4Q0X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085465.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12050                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 97.646                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE, 14% W/V PEG550 MME,     
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 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,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
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      195.29250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      292.93875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       97.64625            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      195.29250            
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       97.64625            
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      292.93875            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN H   137                                                      
REMARK 465     THR H   138                                                      
REMARK 465     ASN H   139                                                      
REMARK 465     HIS E   421                                                      
REMARK 465     ILE E   422                                                      
REMARK 465     ASN E   423                                                      
REMARK 465     SER E   424                                                      
REMARK 465     THR E   425                                                      
REMARK 465     ALA E   426                                                      
REMARK 465     LEU E   427                                                      
REMARK 465     ASN E   428                                                      
REMARK 465     CYS E   429                                                      
REMARK 465     ASN E   430                                                      
REMARK 465     GLU E   431                                                      
REMARK 465     SER E   432                                                      
REMARK 465     LEU E   433                                                      
REMARK 465     TYR E   443                                                      
REMARK 465     GLN E   444                                                      
REMARK 465     HIS E   445                                                      
REMARK 465     LYS E   446                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE H 152   C     PRO H 153   N       0.203                       
REMARK 500    GLU H 154   C     PRO H 155   N       0.124                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO H 153   C   -  N   -  CA  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    PRO H 155   C   -  N   -  CA  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    PRO H 195   C   -  N   -  CD  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    PRO L 146   C   -  N   -  CD  ANGL. DEV. =  18.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL H  56        7.18     54.50                                   
REMARK 500    SER H  84      -83.28   -104.01                                   
REMARK 500    ASP H 102       18.18     58.67                                   
REMARK 500    ALA H 135     -132.80   -102.55                                   
REMARK 500    SER H 162       10.23     59.61                                   
REMARK 500    SER H 178       67.34     61.68                                   
REMARK 500    VAL L  56      -58.28     70.41                                   
REMARK 500    ALA L  85      -51.12     66.44                                   
REMARK 500    LYS L 174      -61.76   -107.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PHE H  152     PRO H  153                  -67.15                    
REMARK 500 GLU H  154     PRO H  155                   62.88                    
REMARK 500 TRP H  194     PRO H  195                   32.72                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    PHE H 152        -15.10                                           
REMARK 500    GLU H 154         10.32                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HZL   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL EVIDENCE FOR A BIFURCATED MODE OF ACTION IN THE           
REMARK 900 ANTIBODY-MEDIATED NEUTRALIZATION OF HEPATITIS C VIRUS                
DBREF  4Q0X E  421   446  UNP    P27958   POLG_HCVH      421    446             
DBREF  4Q0X H    1   219  PDB    4Q0X     4Q0X             1    219             
DBREF  4Q0X L    1   218  PDB    4Q0X     4Q0X             1    218             
SEQRES   1 H  219  GLN VAL GLN LEU ARG GLN SER GLY PRO GLU LEU VAL LYS          
SEQRES   2 H  219  PRO GLY ALA SER VAL ARG ILE SER CYS LYS ALA SER GLY          
SEQRES   3 H  219  TYR THR PHE THR SER TYR TYR ILE HIS TRP VAL LYS GLN          
SEQRES   4 H  219  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TRP ILE TYR          
SEQRES   5 H  219  PRO GLY ASN VAL ASN THR LYS TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  219  GLY LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR          
SEQRES   7 H  219  ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  219  ALA VAL TYR PHE CYS ALA ARG ASP ASP TYR ASP GLY ALA          
SEQRES   9 H  219  TRP PHE ALA TYR TRP GLY GLN GLY THR LEU VAL THR VAL          
SEQRES  10 H  219  SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO LEU          
SEQRES  11 H  219  ALA PRO GLY SER ALA ALA GLN THR ASN SER MET VAL THR          
SEQRES  12 H  219  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  219  THR VAL THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  219  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  219  LEU SER SER SER VAL THR VAL PRO SER SER THR TRP PRO          
SEQRES  16 H  219  SER GLN THR VAL THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  219  SER THR LYS VAL ASP LYS LYS ILE VAL PRO ARG                  
SEQRES   1 L  218  ASP VAL LEU MET THR GLN THR PRO LEU SER LEU PRO VAL          
SEQRES   2 L  218  SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER          
SEQRES   3 L  218  GLN SER ILE VAL HIS ASN ASN GLY ASN THR TYR LEU ASP          
SEQRES   4 L  218  TRP SER LEU GLN LYS PRO GLY GLN SER PRO LYS LEU LEU          
SEQRES   5 L  218  ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP          
SEQRES   6 L  218  ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU          
SEQRES   7 L  218  LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR          
SEQRES   8 L  218  TYR CYS PHE GLN GLY SER HIS VAL PRO PRO THR PHE GLY          
SEQRES   9 L  218  GLY GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA          
SEQRES  10 L  218  PRO THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU          
SEQRES  11 L  218  THR SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN          
SEQRES  12 L  218  PHE TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP          
SEQRES  13 L  218  GLY SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR          
SEQRES  14 L  218  ASP GLN ASP SER LYS ASP SER THR TYR SER MET SER SER          
SEQRES  15 L  218  THR LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN          
SEQRES  16 L  218  SER TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER          
SEQRES  17 L  218  PRO ILE VAL LYS SER PHE ASN ARG ASN GLU                      
SEQRES   1 E   26  HIS ILE ASN SER THR ALA LEU ASN CYS ASN GLU SER LEU          
SEQRES   2 E   26  ASN THR GLY TRP LEU ALA GLY LEU PHE TYR GLN HIS LYS          
FORMUL   4  HOH   *23(H2 O)                                                     
HELIX    1   1 THR H   28  TYR H   32  5                                   5    
HELIX    2   2 GLU H   62  LYS H   65  5                                   4    
HELIX    3   3 THR H   87  SER H   91  5                                   5    
HELIX    4   4 SER H  162  SER H  164  5                                   3    
HELIX    5   5 SER L  126  THR L  131  1                                   6    
HELIX    6   6 LYS L  188  GLU L  192  1                                   5    
HELIX    7   7 GLY E  436  PHE E  442  1                                   7    
SHEET    1   A 4 GLN H   3  GLN H   6  0                                        
SHEET    2   A 4 VAL H  18  SER H  25 -1  O  LYS H  23   N  ARG H   5           
SHEET    3   A 4 THR H  78  LEU H  83 -1  O  ALA H  79   N  CYS H  22           
SHEET    4   A 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1   B 6 GLU H  10  VAL H  12  0                                        
SHEET    2   B 6 THR H 113  VAL H 117  1  O  LEU H 114   N  GLU H  10           
SHEET    3   B 6 ALA H  92  ASP H 100 -1  N  ALA H  92   O  VAL H 115           
SHEET    4   B 6 ILE H  34  ARG H  40 -1  N  HIS H  35   O  ALA H  97           
SHEET    5   B 6 GLY H  44  TYR H  52 -1  O  GLU H  46   N  LYS H  38           
SHEET    6   B 6 ASN H  57  TYR H  60 -1  O  ASN H  57   N  TYR H  52           
SHEET    1   C 4 GLU H  10  VAL H  12  0                                        
SHEET    2   C 4 THR H 113  VAL H 117  1  O  LEU H 114   N  GLU H  10           
SHEET    3   C 4 ALA H  92  ASP H 100 -1  N  ALA H  92   O  VAL H 115           
SHEET    4   C 4 ALA H 104  TRP H 109 -1  O  ALA H 107   N  ARG H  98           
SHEET    1   D 4 SER H 126  LEU H 130  0                                        
SHEET    2   D 4 MET H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3   D 4 TYR H 181  PRO H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4   D 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1   E 4 SER H 126  LEU H 130  0                                        
SHEET    2   E 4 MET H 141  TYR H 151 -1  O  GLY H 145   N  LEU H 130           
SHEET    3   E 4 TYR H 181  PRO H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4   E 4 VAL H 175  LEU H 176 -1  N  VAL H 175   O  THR H 182           
SHEET    1   F 3 THR H 157  TRP H 160  0                                        
SHEET    2   F 3 THR H 200  HIS H 205 -1  O  ALA H 204   N  THR H 157           
SHEET    3   F 3 THR H 210  LYS H 215 -1  O  VAL H 212   N  VAL H 203           
SHEET    1   G 4 MET L   4  THR L   5  0                                        
SHEET    2   G 4 ALA L  19  SER L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   G 4 ASP L  75  ILE L  80 -1  O  LEU L  78   N  ILE L  21           
SHEET    4   G 4 PHE L  67  SER L  72 -1  N  SER L  68   O  LYS L  79           
SHEET    1   H 6 SER L  10  VAL L  13  0                                        
SHEET    2   H 6 THR L 107  ILE L 111  1  O  LYS L 108   N  LEU L  11           
SHEET    3   H 6 GLY L  89  GLN L  95 -1  N  TYR L  91   O  THR L 107           
SHEET    4   H 6 LEU L  38  GLN L  43 -1  N  GLN L  43   O  VAL L  90           
SHEET    5   H 6 PRO L  49  TYR L  54 -1  O  LEU L  52   N  TRP L  40           
SHEET    6   H 6 ASN L  58  ARG L  59 -1  O  ASN L  58   N  TYR L  54           
SHEET    1   I 4 SER L  10  VAL L  13  0                                        
SHEET    2   I 4 THR L 107  ILE L 111  1  O  LYS L 108   N  LEU L  11           
SHEET    3   I 4 GLY L  89  GLN L  95 -1  N  TYR L  91   O  THR L 107           
SHEET    4   I 4 THR L 102  PHE L 103 -1  O  THR L 102   N  GLN L  95           
SHEET    1   J 4 THR L 119  PHE L 123  0                                        
SHEET    2   J 4 GLY L 134  PHE L 144 -1  O  VAL L 138   N  PHE L 123           
SHEET    3   J 4 TYR L 178  THR L 187 -1  O  MET L 180   N  LEU L 141           
SHEET    4   J 4 VAL L 164  TRP L 168 -1  N  SER L 167   O  SER L 181           
SHEET    1   K 4 SER L 158  ARG L 160  0                                        
SHEET    2   K 4 ASN L 150  ILE L 155 -1  N  ILE L 155   O  SER L 158           
SHEET    3   K 4 SER L 196  THR L 202 -1  O  THR L 198   N  LYS L 154           
SHEET    4   K 4 ILE L 210  ASN L 215 -1  O  LYS L 212   N  CYS L 199           
SSBOND   1 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND   2 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND   3 CYS L   23    CYS L   93                          1555   1555  2.04  
SSBOND   4 CYS L  139    CYS L  199                          1555   1555  2.03  
CISPEP   1 TYR L  145    PRO L  146          0        -9.91                     
CRYST1   49.991   49.991  390.585  90.00  90.00  90.00 P 43 2 2      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      0.020004  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002560        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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