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Database: PDB
Entry: 4MWF
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Original site: 4MWF 
HEADER    IMMUNE SYSTEM                           24-SEP-13   4MWF              
TITLE     STRUCTURE OF HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 CORE BOUND TO 
TITLE    2 BROADLY NEUTRALIZING ANTIBODY AR3C                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAB AR3C HEAVY CHAIN;                                      
COMPND   3 CHAIN: A, H;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: FAB AR3C LIGHT CHAIN;                                      
COMPND   7 CHAIN: B, L;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ENVELOPE GLYCOPROTEIN E2;                                  
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS (ISOLATE H);                  
SOURCE  15 ORGANISM_COMMON: HCV;                                                
SOURCE  16 ORGANISM_TAXID: 11108;                                               
SOURCE  17 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  18 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: HEK 293 FREESTYLE                       
KEYWDS    IMMUNOGLOBULIN FOLD, HCV E2, IMMUNE SYSTEM                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.KONG,I.A.WILSON,M.LAW                                               
REVDAT   4   29-JUL-20 4MWF    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   02-AUG-17 4MWF    1       SOURCE REMARK                            
REVDAT   2   24-SEP-14 4MWF    1       KEYWDS                                   
REVDAT   1   11-DEC-13 4MWF    0                                                
JRNL        AUTH   L.KONG,E.GIANG,T.NIEUSMA,R.U.KADAM,K.E.COGBURN,Y.HUA,X.DAI,  
JRNL        AUTH 2 R.L.STANFIELD,D.R.BURTON,A.B.WARD,I.A.WILSON,M.LAW           
JRNL        TITL   HEPATITIS C VIRUS E2 ENVELOPE GLYCOPROTEIN CORE STRUCTURE.   
JRNL        REF    SCIENCE                       V. 342  1090 2013              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   24288331                                                     
JRNL        DOI    10.1126/SCIENCE.1243876                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45926                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2312                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 49.0860 -  6.7941    0.93     2784   151  0.2353 0.2658        
REMARK   3     2  6.7941 -  5.3949    0.96     2758   142  0.2175 0.2401        
REMARK   3     3  5.3949 -  4.7135    0.96     2681   148  0.1765 0.2182        
REMARK   3     4  4.7135 -  4.2829    0.97     2681   158  0.1766 0.2143        
REMARK   3     5  4.2829 -  3.9760    0.96     2666   155  0.2030 0.2203        
REMARK   3     6  3.9760 -  3.7417    0.96     2716   114  0.2179 0.2912        
REMARK   3     7  3.7417 -  3.5544    0.96     2641   142  0.2399 0.2859        
REMARK   3     8  3.5544 -  3.3997    0.97     2626   152  0.2579 0.2948        
REMARK   3     9  3.3997 -  3.2688    0.97     2687   147  0.2569 0.3084        
REMARK   3    10  3.2688 -  3.1561    0.97     2618   153  0.2622 0.2868        
REMARK   3    11  3.1561 -  3.0574    0.96     2661   158  0.2698 0.3228        
REMARK   3    12  3.0574 -  2.9700    0.96     2617   115  0.2757 0.3084        
REMARK   3    13  2.9700 -  2.8918    0.92     2531   126  0.2993 0.3217        
REMARK   3    14  2.8918 -  2.8213    0.90     2448   123  0.3197 0.4044        
REMARK   3    15  2.8213 -  2.7571    0.87     2338   131  0.3176 0.3715        
REMARK   3    16  2.7571 -  2.6985    0.82     2260   107  0.3185 0.4037        
REMARK   3    17  2.6985 -  2.6445    0.70     1901    90  0.3130 0.3948        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           9721                                  
REMARK   3   ANGLE     :  1.275          13227                                  
REMARK   3   CHIRALITY :  0.054           1512                                  
REMARK   3   PLANARITY :  0.014           1666                                  
REMARK   3   DIHEDRAL  : 17.670           3489                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4MWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000082450.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46174                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.4                               
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) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.5                               
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   (%): 57.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 4000, 10% (V/V)            
REMARK 280  ISOPROPANOL, AND 0.1 M HEPES PH 7.5, VAPOR DIFFUSION, SITTING       
REMARK 280  DROP, TEMPERATURE 293K                                              
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       23.56600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.98150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.27650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.98150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       23.56600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.27650            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, G                            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H, L, E, F                         
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     GLU A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     SER A   130                                                      
REMARK 465     THR A   131                                                      
REMARK 465     SER A   132                                                      
REMARK 465     SER A   215                                                      
REMARK 465     CYS A   216                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     SER A   218                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     CYS B   214                                                      
REMARK 465     GLN C   412                                                      
REMARK 465     LEU C   413                                                      
REMARK 465     ILE C   414                                                      
REMARK 465     ASN C   415                                                      
REMARK 465     THR C   416                                                      
REMARK 465     ASN C   417                                                      
REMARK 465     GLY C   418                                                      
REMARK 465     SER C   419                                                      
REMARK 465     TRP C   420                                                      
REMARK 465     PRO C   453                                                      
REMARK 465     GLU C   454                                                      
REMARK 465     ARG C   455                                                      
REMARK 465     LEU C   456                                                      
REMARK 465     ALA C   457                                                      
REMARK 465     SER C   458                                                      
REMARK 465     CYS C   459                                                      
REMARK 465     GLY C   482                                                      
REMARK 465     SER C   483                                                      
REMARK 465     SER C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     CYS C   486                                                      
REMARK 465     TRP C   487                                                      
REMARK 465     HIS C   488                                                      
REMARK 465     TYR C   489                                                      
REMARK 465     PRO C   490                                                      
REMARK 465     PRO C   491                                                      
REMARK 465     THR C   542                                                      
REMARK 465     ARG C   543                                                      
REMARK 465     PRO C   544                                                      
REMARK 465     PRO C   545                                                      
REMARK 465     LEU C   546                                                      
REMARK 465     GLY C   547                                                      
REMARK 465     PHE C   586                                                      
REMARK 465     ARG C   587                                                      
REMARK 465     LYS C   588                                                      
REMARK 465     HIS C   589                                                      
REMARK 465     PRO C   590                                                      
REMARK 465     GLU C   591                                                      
REMARK 465     ALA C   592                                                      
REMARK 465     THR C   593                                                      
REMARK 465     TYR C   594                                                      
REMARK 465     SER C   595                                                      
REMARK 465     ARG C   596                                                      
REMARK 465     GLN D   412                                                      
REMARK 465     LEU D   413                                                      
REMARK 465     ILE D   414                                                      
REMARK 465     ASN D   415                                                      
REMARK 465     THR D   416                                                      
REMARK 465     ASN D   417                                                      
REMARK 465     GLY D   418                                                      
REMARK 465     SER D   419                                                      
REMARK 465     TRP D   420                                                      
REMARK 465     PRO D   453                                                      
REMARK 465     GLU D   454                                                      
REMARK 465     ARG D   455                                                      
REMARK 465     LEU D   456                                                      
REMARK 465     ALA D   457                                                      
REMARK 465     SER D   458                                                      
REMARK 465     CYS D   459                                                      
REMARK 465     GLY D   482                                                      
REMARK 465     SER D   483                                                      
REMARK 465     SER D   484                                                      
REMARK 465     GLY D   485                                                      
REMARK 465     CYS D   486                                                      
REMARK 465     TRP D   487                                                      
REMARK 465     HIS D   488                                                      
REMARK 465     TYR D   489                                                      
REMARK 465     PRO D   490                                                      
REMARK 465     PRO D   491                                                      
REMARK 465     VAL D   574                                                      
REMARK 465     GLY D   575                                                      
REMARK 465     ASP D   576                                                      
REMARK 465     ASN D   577                                                      
REMARK 465     PHE D   586                                                      
REMARK 465     ARG D   587                                                      
REMARK 465     LYS D   588                                                      
REMARK 465     HIS D   589                                                      
REMARK 465     PRO D   590                                                      
REMARK 465     GLU D   591                                                      
REMARK 465     ALA D   592                                                      
REMARK 465     THR D   593                                                      
REMARK 465     TYR D   594                                                      
REMARK 465     SER D   595                                                      
REMARK 465     ARG D   596                                                      
REMARK 465     GLU H     0                                                      
REMARK 465     VAL H     1                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     GLY H   217                                                      
REMARK 465     SER H   218                                                      
REMARK 465     GLU L     1                                                      
REMARK 465     CYS L   214                                                      
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   SG   CYS C   452     SG   CYS C   620              1.65            
REMARK 500   SG   CYS C   429     SG   CYS C   503              1.67            
REMARK 500   O3   BMA E     3     O5   MAN E     4              2.01            
REMARK 500   OG1  THR C   578     O    CYS C   581              2.07            
REMARK 500   ND2  ASN D   556     C2   NAG G     1              2.11            
REMARK 500   ND2  ASN C   556     C2   NAG F     1              2.11            
REMARK 500   C6   MAN E     7     C1   MAN E     8              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  48      -60.03    -93.75                                   
REMARK 500    SER A  82B      61.11     61.29                                   
REMARK 500    THR A  97      101.13     90.30                                   
REMARK 500    SER B  30     -118.42     54.19                                   
REMARK 500    ALA B  51      -39.03     67.59                                   
REMARK 500    TYR B  92      -68.62   -130.70                                   
REMARK 500    SER C 599     -125.12     60.39                                   
REMARK 500    ALA D 531     -120.58     59.09                                   
REMARK 500    LEU D 539      -70.28   -100.52                                   
REMARK 500    PRO D 582      154.98    -47.99                                   
REMARK 500    LEU H  45      151.56    -48.32                                   
REMARK 500    THR H  97       72.76     58.04                                   
REMARK 500    SER L  30     -130.65     55.91                                   
REMARK 500    ALA L  51      -45.48     72.60                                   
REMARK 500    ASP L  82        0.28    -69.68                                   
REMARK 500    SER L  83       98.91    -69.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4MWF C  412   459  UNP    P27958   POLG_HCVH      412    459             
DBREF  4MWF C  486   645  UNP    P27958   POLG_HCVH      486    645             
DBREF  4MWF D  412   459  UNP    P27958   POLG_HCVH      412    459             
DBREF  4MWF D  486   645  UNP    P27958   POLG_HCVH      486    645             
DBREF  4MWF A    0   218  PDB    4MWF     4MWF             0    218             
DBREF  4MWF H    0   218  PDB    4MWF     4MWF             0    218             
DBREF  4MWF B    1   214  PDB    4MWF     4MWF             1    214             
DBREF  4MWF L    1   214  PDB    4MWF     4MWF             1    214             
SEQADV 4MWF ASP C  448  UNP  P27958    ASN   448 ENGINEERED MUTATION            
SEQADV 4MWF GLY C  482  UNP  P27958              LINKER                         
SEQADV 4MWF SER C  483  UNP  P27958              LINKER                         
SEQADV 4MWF SER C  484  UNP  P27958              LINKER                         
SEQADV 4MWF GLY C  485  UNP  P27958              LINKER                         
SEQADV 4MWF ASP C  576  UNP  P27958    ASN   576 ENGINEERED MUTATION            
SEQADV 4MWF HIS C  589  UNP  P27958    TYR   589 VARIANT                        
SEQADV 4MWF TRP C  602  UNP  P27958    ARG   602 VARIANT                        
SEQADV 4MWF ASP D  448  UNP  P27958    ASN   448 ENGINEERED MUTATION            
SEQADV 4MWF GLY D  482  UNP  P27958              LINKER                         
SEQADV 4MWF SER D  483  UNP  P27958              LINKER                         
SEQADV 4MWF SER D  484  UNP  P27958              LINKER                         
SEQADV 4MWF GLY D  485  UNP  P27958              LINKER                         
SEQADV 4MWF ASP D  576  UNP  P27958    ASN   576 ENGINEERED MUTATION            
SEQADV 4MWF HIS D  589  UNP  P27958    TYR   589 VARIANT                        
SEQADV 4MWF TRP D  602  UNP  P27958    ARG   602 VARIANT                        
SEQRES   1 A  233  GLU VAL GLN LEU LEU GLU GLN SER GLY ALA GLU VAL LYS          
SEQRES   2 A  233  LYS PRO GLY SER SER VAL LYS VAL SER CYS GLU THR SER          
SEQRES   3 A  233  GLY GLY THR PHE ASP ASN TYR ALA LEU ASN TRP VAL ARG          
SEQRES   4 A  233  GLN ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLY VAL          
SEQRES   5 A  233  VAL PRO LEU PHE GLY THR THR ARG ASN ALA GLN LYS PHE          
SEQRES   6 A  233  GLN GLY ARG VAL THR ILE SER ASP ASP LYS SER THR GLY          
SEQRES   7 A  233  THR GLY HIS MET GLU LEU ARG SER LEU ARG SER GLU ASP          
SEQRES   8 A  233  THR ALA VAL TYR TYR CYS VAL ARG SER VAL THR PRO ARG          
SEQRES   9 A  233  TYR CYS GLY GLY GLY PHE CYS TYR GLY GLU PHE ASP TYR          
SEQRES  10 A  233  TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER          
SEQRES  11 A  233  THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER          
SEQRES  12 A  233  LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU          
SEQRES  13 A  233  VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP          
SEQRES  14 A  233  ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO          
SEQRES  15 A  233  ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER          
SEQRES  16 A  233  VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR          
SEQRES  17 A  233  TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS          
SEQRES  18 A  233  VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER              
SEQRES   1 B  214  GLU ILE GLU LEU THR GLN SER PRO ALA THR LEU SER VAL          
SEQRES   2 B  214  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 B  214  GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 B  214  PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER          
SEQRES   5 B  214  THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER          
SEQRES   6 B  214  GLY SER GLY THR GLU PHE THR LEU THR VAL SER ARG LEU          
SEQRES   7 B  214  GLU PRO GLU ASP SER ALA VAL TYR PHE CYS GLN GLN TYR          
SEQRES   8 B  214  TYR ARG SER PRO LEU THR PHE GLY GLY GLY THR LYS VAL          
SEQRES   9 B  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 B  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 B  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 B  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 B  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 B  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 B  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 B  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 B  214  PHE ASN ARG GLY GLU CYS                                      
SEQRES   1 C  212  GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE ASN SER          
SEQRES   2 C  212  THR ALA LEU ASN CYS ASN GLU SER LEU ASN THR GLY TRP          
SEQRES   3 C  212  LEU ALA GLY LEU PHE TYR GLN HIS LYS PHE ASP SER SER          
SEQRES   4 C  212  GLY CYS PRO GLU ARG LEU ALA SER CYS GLY SER SER GLY          
SEQRES   5 C  212  CYS TRP HIS TYR PRO PRO ARG PRO CYS GLY ILE VAL PRO          
SEQRES   6 C  212  ALA LYS SER VAL CYS GLY PRO VAL TYR CYS PHE THR PRO          
SEQRES   7 C  212  SER PRO VAL VAL VAL GLY THR THR ASP ARG SER GLY ALA          
SEQRES   8 C  212  PRO THR TYR SER TRP GLY ALA ASN ASP THR ASP VAL PHE          
SEQRES   9 C  212  VAL LEU ASN ASN THR ARG PRO PRO LEU GLY ASN TRP PHE          
SEQRES  10 C  212  GLY CYS THR TRP MET ASN SER THR GLY PHE THR LYS VAL          
SEQRES  11 C  212  CYS GLY ALA PRO PRO CYS VAL ILE GLY GLY VAL GLY ASP          
SEQRES  12 C  212  ASN THR LEU LEU CYS PRO THR ASP CYS PHE ARG LYS HIS          
SEQRES  13 C  212  PRO GLU ALA THR TYR SER ARG CYS GLY SER GLY PRO TRP          
SEQRES  14 C  212  ILE THR PRO ARG CYS MET VAL ASP TYR PRO TYR ARG LEU          
SEQRES  15 C  212  TRP HIS TYR PRO CYS THR ILE ASN TYR THR ILE PHE LYS          
SEQRES  16 C  212  VAL ARG MET TYR VAL GLY GLY VAL GLU HIS ARG LEU GLU          
SEQRES  17 C  212  ALA ALA CYS ASN                                              
SEQRES   1 D  212  GLN LEU ILE ASN THR ASN GLY SER TRP HIS ILE ASN SER          
SEQRES   2 D  212  THR ALA LEU ASN CYS ASN GLU SER LEU ASN THR GLY TRP          
SEQRES   3 D  212  LEU ALA GLY LEU PHE TYR GLN HIS LYS PHE ASP SER SER          
SEQRES   4 D  212  GLY CYS PRO GLU ARG LEU ALA SER CYS GLY SER SER GLY          
SEQRES   5 D  212  CYS TRP HIS TYR PRO PRO ARG PRO CYS GLY ILE VAL PRO          
SEQRES   6 D  212  ALA LYS SER VAL CYS GLY PRO VAL TYR CYS PHE THR PRO          
SEQRES   7 D  212  SER PRO VAL VAL VAL GLY THR THR ASP ARG SER GLY ALA          
SEQRES   8 D  212  PRO THR TYR SER TRP GLY ALA ASN ASP THR ASP VAL PHE          
SEQRES   9 D  212  VAL LEU ASN ASN THR ARG PRO PRO LEU GLY ASN TRP PHE          
SEQRES  10 D  212  GLY CYS THR TRP MET ASN SER THR GLY PHE THR LYS VAL          
SEQRES  11 D  212  CYS GLY ALA PRO PRO CYS VAL ILE GLY GLY VAL GLY ASP          
SEQRES  12 D  212  ASN THR LEU LEU CYS PRO THR ASP CYS PHE ARG LYS HIS          
SEQRES  13 D  212  PRO GLU ALA THR TYR SER ARG CYS GLY SER GLY PRO TRP          
SEQRES  14 D  212  ILE THR PRO ARG CYS MET VAL ASP TYR PRO TYR ARG LEU          
SEQRES  15 D  212  TRP HIS TYR PRO CYS THR ILE ASN TYR THR ILE PHE LYS          
SEQRES  16 D  212  VAL ARG MET TYR VAL GLY GLY VAL GLU HIS ARG LEU GLU          
SEQRES  17 D  212  ALA ALA CYS ASN                                              
SEQRES   1 H  233  GLU VAL GLN LEU LEU GLU GLN SER GLY ALA GLU VAL LYS          
SEQRES   2 H  233  LYS PRO GLY SER SER VAL LYS VAL SER CYS GLU THR SER          
SEQRES   3 H  233  GLY GLY THR PHE ASP ASN TYR ALA LEU ASN TRP VAL ARG          
SEQRES   4 H  233  GLN ALA PRO GLY GLN GLY LEU GLU TRP ILE GLY GLY VAL          
SEQRES   5 H  233  VAL PRO LEU PHE GLY THR THR ARG ASN ALA GLN LYS PHE          
SEQRES   6 H  233  GLN GLY ARG VAL THR ILE SER ASP ASP LYS SER THR GLY          
SEQRES   7 H  233  THR GLY HIS MET GLU LEU ARG SER LEU ARG SER GLU ASP          
SEQRES   8 H  233  THR ALA VAL TYR TYR CYS VAL ARG SER VAL THR PRO ARG          
SEQRES   9 H  233  TYR CYS GLY GLY GLY PHE CYS TYR GLY GLU PHE ASP TYR          
SEQRES  10 H  233  TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER          
SEQRES  11 H  233  THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER          
SEQRES  12 H  233  LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU          
SEQRES  13 H  233  VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP          
SEQRES  14 H  233  ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO          
SEQRES  15 H  233  ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER          
SEQRES  16 H  233  VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR          
SEQRES  17 H  233  TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS          
SEQRES  18 H  233  VAL ASP LYS LYS VAL GLU PRO LYS SER CYS GLY SER              
SEQRES   1 L  214  GLU ILE GLU LEU THR GLN SER PRO ALA THR LEU SER VAL          
SEQRES   2 L  214  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 L  214  GLN SER VAL SER SER ASN LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER          
SEQRES   5 L  214  THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR GLU PHE THR LEU THR VAL SER ARG LEU          
SEQRES   7 L  214  GLU PRO GLU ASP SER ALA VAL TYR PHE CYS GLN GLN TYR          
SEQRES   8 L  214  TYR ARG SER PRO LEU THR PHE GLY GLY GLY THR LYS VAL          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU CYS                                      
MODRES 4MWF ASN D  556  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN D  532  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN D  430  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN C  430  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN C  532  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN D  623  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN D  540  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN C  556  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN C  623  ASN  GLYCOSYLATION SITE                                 
MODRES 4MWF ASN C  540  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    MAN  E   6      11                                                       
HET    MAN  E   7      11                                                       
HET    MAN  E   8      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  C 711      14                                                       
HET    NAG  C 712      14                                                       
HET    NAG  C 713      14                                                       
HET    NAG  D 701      14                                                       
HET    NAG  D 702      14                                                       
HET    NAG  D 703      14                                                       
HET    NAG  D 706      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
FORMUL   7  NAG    13(C8 H15 N O6)                                              
FORMUL   7  BMA    C6 H12 O6                                                    
FORMUL   7  MAN    5(C6 H12 O6)                                                 
HELIX    1   1 ARG A   83  THR A   87  5                                   5    
HELIX    2   2 SER A  156  ALA A  158  5                                   3    
HELIX    3   3 SER A  187  LEU A  189  5                                   3    
HELIX    4   4 LYS A  201  ASN A  204  5                                   4    
HELIX    5   5 GLU B   79  SER B   83  5                                   5    
HELIX    6   6 SER B  121  LYS B  126  1                                   6    
HELIX    7   7 LYS B  183  GLU B  187  1                                   5    
HELIX    8   8 HIS C  421  THR C  425  5                                   5    
HELIX    9   9 LEU C  438  TYR C  443  1                                   6    
HELIX   10  10 PRO C  567  GLY C  572  5                                   6    
HELIX   11  11 TYR C  613  TYR C  618  1                                   6    
HELIX   12  12 PRO C  619  ILE C  622  5                                   4    
HELIX   13  13 GLY D  436  PHE D  442  5                                   7    
HELIX   14  14 PRO D  567  GLY D  572  5                                   6    
HELIX   15  15 TYR D  613  TYR D  618  1                                   6    
HELIX   16  16 PRO D  619  TYR D  624  5                                   6    
HELIX   17  17 GLN H   61  GLN H   64  5                                   4    
HELIX   18  18 ARG H   83  THR H   87  5                                   5    
HELIX   19  19 SER H  156  ALA H  158  5                                   3    
HELIX   20  20 SER H  187  LEU H  189  5                                   3    
HELIX   21  21 LYS H  201  ASN H  204  5                                   4    
HELIX   22  22 GLU L   79  SER L   83  5                                   5    
HELIX   23  23 SER L  121  SER L  127  1                                   7    
HELIX   24  24 LYS L  183  HIS L  189  1                                   7    
SHEET    1   A 4 LEU A   4  GLN A   6  0                                        
SHEET    2   A 4 SER A  17  THR A  24 -1  O  GLU A  23   N  GLU A   5           
SHEET    3   A 4 THR A  77  ARG A  82A-1  O  MET A  80   N  VAL A  20           
SHEET    4   A 4 THR A  68  ASP A  72 -1  N  ASP A  72   O  THR A  77           
SHEET    1   B 6 GLU A  10  LYS A  12  0                                        
SHEET    2   B 6 THR A 107  VAL A 111  1  O  THR A 110   N  GLU A  10           
SHEET    3   B 6 ALA A  88  SER A  95 -1  N  ALA A  88   O  VAL A 109           
SHEET    4   B 6 ALA A  33  GLN A  39 -1  N  ASN A  35   O  VAL A  93           
SHEET    5   B 6 LEU A  45  VAL A  51 -1  O  VAL A  51   N  LEU A  34           
SHEET    6   B 6 THR A  57  ASN A  59 -1  O  ARG A  58   N  GLY A  50           
SHEET    1   C 4 GLU A  10  LYS A  12  0                                        
SHEET    2   C 4 THR A 107  VAL A 111  1  O  THR A 110   N  GLU A  10           
SHEET    3   C 4 ALA A  88  SER A  95 -1  N  ALA A  88   O  VAL A 109           
SHEET    4   C 4 TYR A 102  TRP A 103 -1  O  TYR A 102   N  ARG A  94           
SHEET    1   D 2 TYR A 100  CYS A 100A 0                                        
SHEET    2   D 2 CYS A 100F TYR A 100G-1  O  TYR A 100G  N  TYR A 100           
SHEET    1   E 4 SER A 120  LEU A 124  0                                        
SHEET    2   E 4 THR A 135  TYR A 145 -1  O  LYS A 143   N  SER A 120           
SHEET    3   E 4 TYR A 176  PRO A 185 -1  O  LEU A 178   N  VAL A 142           
SHEET    4   E 4 VAL A 163  THR A 165 -1  N  HIS A 164   O  VAL A 181           
SHEET    1   F 4 SER A 120  LEU A 124  0                                        
SHEET    2   F 4 THR A 135  TYR A 145 -1  O  LYS A 143   N  SER A 120           
SHEET    3   F 4 TYR A 176  PRO A 185 -1  O  LEU A 178   N  VAL A 142           
SHEET    4   F 4 VAL A 169  LEU A 170 -1  N  VAL A 169   O  SER A 177           
SHEET    1   G 3 THR A 151  TRP A 154  0                                        
SHEET    2   G 3 ILE A 195  HIS A 200 -1  O  ASN A 199   N  THR A 151           
SHEET    3   G 3 THR A 205  LYS A 210 -1  O  VAL A 207   N  VAL A 198           
SHEET    1   H 4 LEU B   4  SER B   7  0                                        
SHEET    2   H 4 ALA B  19  ALA B  25 -1  O  SER B  22   N  SER B   7           
SHEET    3   H 4 GLU B  70  VAL B  75 -1  O  LEU B  73   N  LEU B  21           
SHEET    4   H 4 PHE B  62  SER B  67 -1  N  SER B  67   O  GLU B  70           
SHEET    1   I 6 THR B  10  VAL B  13  0                                        
SHEET    2   I 6 THR B 102  ILE B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3   I 6 VAL B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   I 6 LEU B  33  GLN B  38 -1  N  TYR B  36   O  PHE B  87           
SHEET    5   I 6 ARG B  45  TYR B  49 -1  O  ARG B  45   N  GLN B  37           
SHEET    6   I 6 THR B  53  ARG B  54 -1  O  THR B  53   N  TYR B  49           
SHEET    1   J 4 THR B  10  VAL B  13  0                                        
SHEET    2   J 4 THR B 102  ILE B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3   J 4 VAL B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4   J 4 THR B  97  PHE B  98 -1  O  THR B  97   N  GLN B  90           
SHEET    1   K 4 SER B 114  PHE B 118  0                                        
SHEET    2   K 4 THR B 129  PHE B 139 -1  O  LEU B 135   N  PHE B 116           
SHEET    3   K 4 TYR B 173  SER B 182 -1  O  LEU B 175   N  LEU B 136           
SHEET    4   K 4 SER B 159  VAL B 163 -1  N  GLN B 160   O  THR B 178           
SHEET    1   L 4 ALA B 153  LEU B 154  0                                        
SHEET    2   L 4 LYS B 145  VAL B 150 -1  N  VAL B 150   O  ALA B 153           
SHEET    3   L 4 VAL B 191  THR B 197 -1  O  GLU B 195   N  GLN B 147           
SHEET    4   L 4 VAL B 205  ASN B 210 -1  O  VAL B 205   N  VAL B 196           
SHEET    1   M 2 ALA C 426  LEU C 427  0                                        
SHEET    2   M 2 CYS C 503  GLY C 504 -1  O  GLY C 504   N  ALA C 426           
SHEET    1   N 2 ILE C 496  PRO C 498  0                                        
SHEET    2   N 2 VAL C 536  VAL C 538 -1  O  PHE C 537   N  VAL C 497           
SHEET    1   O 4 PRO C 513  VAL C 515  0                                        
SHEET    2   O 4 TYR C 507  PHE C 509 -1  N  CYS C 508   O  VAL C 514           
SHEET    3   O 4 GLY C 551  MET C 555 -1  O  THR C 553   N  TYR C 507           
SHEET    4   O 4 THR C 561  GLY C 565 -1  O  LYS C 562   N  TRP C 554           
SHEET    1   P 4 TRP C 602  THR C 604  0                                        
SHEET    2   P 4 CYS C 607  VAL C 609 -1  O  CYS C 607   N  ILE C 603           
SHEET    3   P 4 VAL C 636  CYS C 644 -1  O  ALA C 643   N  MET C 608           
SHEET    4   P 4 THR C 625  VAL C 633 -1  N  THR C 625   O  CYS C 644           
SHEET    1   Q 2 ALA D 426  LEU D 427  0                                        
SHEET    2   Q 2 CYS D 503  GLY D 504 -1  O  GLY D 504   N  ALA D 426           
SHEET    1   R 2 ILE D 496  PRO D 498  0                                        
SHEET    2   R 2 VAL D 536  VAL D 538 -1  O  PHE D 537   N  VAL D 497           
SHEET    1   S 4 PRO D 513  VAL D 515  0                                        
SHEET    2   S 4 TYR D 507  PHE D 509 -1  N  CYS D 508   O  VAL D 514           
SHEET    3   S 4 GLY D 551  MET D 555 -1  O  THR D 553   N  TYR D 507           
SHEET    4   S 4 THR D 561  GLY D 565 -1  O  CYS D 564   N  CYS D 552           
SHEET    1   T 3 CYS D 607  VAL D 609  0                                        
SHEET    2   T 3 VAL D 636  CYS D 644 -1  O  ALA D 643   N  MET D 608           
SHEET    3   T 3 THR D 625  VAL D 633 -1  N  THR D 625   O  CYS D 644           
SHEET    1   U 4 GLU H   5  GLN H   6  0                                        
SHEET    2   U 4 VAL H  18  GLU H  23 -1  O  GLU H  23   N  GLU H   5           
SHEET    3   U 4 THR H  77  LEU H  82 -1  O  MET H  80   N  VAL H  20           
SHEET    4   U 4 VAL H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77           
SHEET    1   V 6 GLU H  10  LYS H  12  0                                        
SHEET    2   V 6 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3   V 6 ALA H  88  SER H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   V 6 ALA H  33  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5   V 6 GLU H  46  VAL H  52 -1  O  GLY H  49   N  TRP H  36           
SHEET    6   V 6 THR H  56  ASN H  59 -1  O  THR H  56   N  VAL H  52           
SHEET    1   W 4 GLU H  10  LYS H  12  0                                        
SHEET    2   W 4 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3   W 4 ALA H  88  SER H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4   W 4 TYR H 102  TRP H 103 -1  O  TYR H 102   N  ARG H  94           
SHEET    1   X 2 TYR H 100  GLY H 100B 0                                        
SHEET    2   X 2 PHE H 100E TYR H 100G-1  O  TYR H 100G  N  TYR H 100           
SHEET    1   Y 4 SER H 120  LEU H 124  0                                        
SHEET    2   Y 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   Y 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4   Y 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1   Z 4 SER H 120  LEU H 124  0                                        
SHEET    2   Z 4 THR H 135  TYR H 145 -1  O  LEU H 141   N  PHE H 122           
SHEET    3   Z 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4   Z 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  SER H 177           
SHEET    1  AA 3 THR H 151  TRP H 154  0                                        
SHEET    2  AA 3 TYR H 194  HIS H 200 -1  O  ASN H 199   N  THR H 151           
SHEET    3  AA 3 THR H 205  VAL H 211 -1  O  THR H 205   N  HIS H 200           
SHEET    1  AB 4 LEU L   4  THR L   5  0                                        
SHEET    2  AB 4 ALA L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3  AB 4 GLU L  70  VAL L  75 -1  O  LEU L  73   N  LEU L  21           
SHEET    4  AB 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1  AC 6 THR L  10  VAL L  13  0                                        
SHEET    2  AC 6 THR L 102  ILE L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3  AC 6 ALA L  84  GLN L  90 -1  N  ALA L  84   O  VAL L 104           
SHEET    4  AC 6 LEU L  33  GLN L  38 -1  N  TYR L  36   O  PHE L  87           
SHEET    5  AC 6 ARG L  45  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6  AC 6 THR L  53  ARG L  54 -1  O  THR L  53   N  TYR L  49           
SHEET    1  AD 4 THR L  10  VAL L  13  0                                        
SHEET    2  AD 4 THR L 102  ILE L 106  1  O  GLU L 105   N  LEU L  11           
SHEET    3  AD 4 ALA L  84  GLN L  90 -1  N  ALA L  84   O  VAL L 104           
SHEET    4  AD 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AE 4 SER L 114  PHE L 118  0                                        
SHEET    2  AE 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  AE 4 TYR L 173  SER L 182 -1  O  LEU L 175   N  LEU L 136           
SHEET    4  AE 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1  AF 4 ALA L 153  LEU L 154  0                                        
SHEET    2  AF 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3  AF 4 VAL L 191  THR L 197 -1  O  ALA L 193   N  LYS L 149           
SHEET    4  AF 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS A  100A   CYS A  100F                         1555   1555  2.03  
SSBOND   2 CYS B   23    CYS B   88                          1555   1555  2.04  
SSBOND   3 CYS B  134    CYS B  194                          1555   1555  2.03  
SSBOND   4 CYS C  494    CYS C  564                          1555   1555  2.05  
SSBOND   5 CYS C  508    CYS C  552                          1555   1555  2.05  
SSBOND   6 CYS C  569    CYS C  581                          1555   1555  2.03  
SSBOND   7 CYS C  585    CYS C  597                          1555   1555  2.04  
SSBOND   8 CYS C  607    CYS C  644                          1555   1555  2.05  
SSBOND   9 CYS D  429    CYS D  503                          1555   1555  2.02  
SSBOND  10 CYS D  452    CYS D  620                          1555   1555  2.04  
SSBOND  11 CYS D  494    CYS D  564                          1555   1555  2.03  
SSBOND  12 CYS D  508    CYS D  552                          1555   1555  2.03  
SSBOND  13 CYS D  569    CYS D  581                          1555   1555  2.04  
SSBOND  14 CYS D  585    CYS D  597                          1555   1555  2.03  
SSBOND  15 CYS D  607    CYS D  644                          1555   1555  2.05  
SSBOND  16 CYS H   22    CYS H   92                          1555   1555  2.04  
SSBOND  17 CYS H  100A   CYS H  100F                         1555   1555  2.03  
SSBOND  18 CYS H  140    CYS H  196                          1555   1555  2.03  
SSBOND  19 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND  20 CYS L  134    CYS L  194                          1555   1555  2.05  
LINK         ND2 ASN C 430                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN C 532                 C1  NAG C 711     1555   1555  1.45  
LINK         ND2 ASN C 540                 C1  NAG C 712     1555   1555  1.46  
LINK         ND2 ASN C 556                 C1  NAG F   1     1555   1555  1.45  
LINK         ND2 ASN C 623                 C1  NAG C 713     1555   1555  1.45  
LINK         ND2 ASN D 430                 C1  NAG D 701     1555   1555  1.44  
LINK         ND2 ASN D 532                 C1  NAG D 702     1555   1555  1.43  
LINK         ND2 ASN D 540                 C1  NAG D 703     1555   1555  1.45  
LINK         ND2 ASN D 556                 C1  NAG G   1     1555   1555  1.42  
LINK         ND2 ASN D 623                 C1  NAG D 706     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.43  
LINK         O3  BMA E   3                 C1  MAN E   4     1555   1555  1.58  
LINK         O6  BMA E   3                 C1  MAN E   7     1555   1555  1.53  
LINK         O2  MAN E   4                 C1  MAN E   5     1555   1555  1.43  
LINK         O2  MAN E   5                 C1  MAN E   6     1555   1555  1.43  
LINK         O6  MAN E   7                 C1  MAN E   8     1555   1555  1.46  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
CISPEP   1 SER A   25    GLY A   26          0         0.50                     
CISPEP   2 GLY A   27    THR A   28          0         0.09                     
CISPEP   3 GLY A  100C   GLY A  100D         0        -7.03                     
CISPEP   4 PHE A  146    PRO A  147          0       -10.46                     
CISPEP   5 GLU A  148    PRO A  149          0         0.05                     
CISPEP   6 SER B    7    PRO B    8          0        -0.40                     
CISPEP   7 TYR B  140    PRO B  141          0         1.80                     
CISPEP   8 CYS C  494    GLY C  495          0         0.52                     
CISPEP   9 CYS C  503    GLY C  504          0       -13.45                     
CISPEP  10 THR C  510    PRO C  511          0        13.87                     
CISPEP  11 ARG C  521    SER C  522          0        -0.69                     
CISPEP  12 SER C  522    GLY C  523          0         3.69                     
CISPEP  13 THR C  583    ASP C  584          0         8.17                     
CISPEP  14 ASN D  430    GLU D  431          0         1.40                     
CISPEP  15 SER D  449    SER D  450          0         2.11                     
CISPEP  16 CYS D  503    GLY D  504          0       -14.64                     
CISPEP  17 THR D  510    PRO D  511          0         1.24                     
CISPEP  18 ARG D  521    SER D  522          0        -5.01                     
CISPEP  19 SER D  522    GLY D  523          0        -9.22                     
CISPEP  20 GLY D  530    ALA D  531          0        22.12                     
CISPEP  21 PRO D  545    LEU D  546          0       -11.22                     
CISPEP  22 GLY D  572    GLY D  573          0        -0.93                     
CISPEP  23 GLN H    2    LEU H    3          0         1.88                     
CISPEP  24 GLY H   26    GLY H   27          0       -14.96                     
CISPEP  25 GLY H  100C   GLY H  100D         0        -5.89                     
CISPEP  26 PHE H  146    PRO H  147          0        -8.26                     
CISPEP  27 GLU H  148    PRO H  149          0         7.27                     
CISPEP  28 SER L    7    PRO L    8          0        -1.01                     
CISPEP  29 SER L   94    PRO L   95          0         1.03                     
CISPEP  30 TYR L  140    PRO L  141          0         2.46                     
CRYST1   47.132  166.553  209.963  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      0.021217  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006004  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004763        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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