GenomeNet

Database: PDB
Entry: 1HRV
LinkDB: 1HRV
Original site: 1HRV 
HEADER    VIRUS                                   02-MAR-95   1HRV              
TITLE     HRV14/SDZ 35-682 COMPLEX                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP1);            
COMPND   3 CHAIN: 1;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP2);            
COMPND   7 CHAIN: 2;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP3);            
COMPND  11 CHAIN: 3;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: HUMAN RHINOVIRUS 14 COAT PROTEIN (SUBUNIT VP4);            
COMPND  15 CHAIN: 4;                                                            
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;                            
SOURCE   3 ORGANISM_TAXID: 12131;                                               
SOURCE   4 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   5 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;                             
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;                            
SOURCE  10 ORGANISM_TAXID: 12131;                                               
SOURCE  11 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  12 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;                             
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;                            
SOURCE  17 ORGANISM_TAXID: 12131;                                               
SOURCE  18 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  19 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS;                             
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HUMAN RHINOVIRUS 14;                            
SOURCE  24 ORGANISM_TAXID: 12131;                                               
SOURCE  25 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  26 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  28 EXPRESSION_SYSTEM_CELL_LINE: HELA CELLS                              
KEYWDS    ANTIVIRAL AGENTS, ICOSAHEDRAL VIRUS, VIRUS                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.OREN,A.ZHANG,E.ARNOLD                                             
REVDAT   4   15-MAR-23 1HRV    1       REMARK                                   
REVDAT   3   18-JAN-23 1HRV    1       REMARK SEQADV CRYST1 MTRIX               
REVDAT   3 2                   1       ATOM                                     
REVDAT   2   24-FEB-09 1HRV    1       VERSN                                    
REVDAT   1   03-JUN-95 1HRV    0                                                
JRNL        AUTH   B.ROSENWIRTH,D.A.OREN,E.ARNOLD,Z.L.KIS,H.J.EGGERS            
JRNL        TITL   SDZ 35-682, A NEW PICORNAVIRUS CAPSID-BINDING AGENT WITH     
JRNL        TITL 2 POTENT ANTIVIRAL ACTIVITY.                                   
JRNL        REF    ANTIVIRAL RES.                V.  26    65 1995              
JRNL        REFN                   ISSN 0166-3542                               
JRNL        PMID   7741522                                                      
JRNL        DOI    10.1016/0166-3542(94)00066-H                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.ZHANG,R.G.NANNI,T.LI,G.F.ARNOLD,D.A.OREN,A.JACOBO-MOLINA,  
REMARK   1  AUTH 2 R.L.WILLIAMS,G.KAMER,D.A.RUBENSTEIN,Y.LI,E.ROZHON,S.COX,     
REMARK   1  AUTH 3 P.BUONTEMPO,J.O'CONNELL,J.SCHWARTZ,G.MILLER,B.BAUER,         
REMARK   1  AUTH 4 R.VERSACE,P.PINTO,A.GANGULY,V.GIRIJAVALLABHAN,E.ARNOLD       
REMARK   1  TITL   STRUCTURE DETERMINATION OF ANTIVIRAL COMPOUND SCH 38057      
REMARK   1  TITL 2 COMPLEXED WITH HUMAN RHINOVIRUS 14                           
REMARK   1  REF    J.MOL.BIOL.                   V. 230   857 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.ZHANG,R.G.NANNI,D.A.OREN,E.J.ROZHON,E.ARNOLD               
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE-ACTIVITY RELATIONSHIPS FOR       
REMARK   1  TITL 2 ANTIVIRAL AGENTS THAT INTERACT WITH PICORNAVIRUS CAPSIDS     
REMARK   1  REF    SEMIN.VIROL.                  V.   3   453 1992              
REMARK   1  REFN                   ISSN 1044-5773                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   E.ARNOLD,M.G.ROSSMANN                                        
REMARK   1  TITL   ANALYSIS OF THE STRUCTURE OF A COMMON COLD VIRUS, HUMAN      
REMARK   1  TITL 2 RHINOVIRUS 14, REFINED AT A RESOLUTION OF 3.0 ANGSTROMS      
REMARK   1  REF    J.MOL.BIOL.                   V. 211   763 1990              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   E.ARNOLD,M.G.ROSSMANN                                        
REMARK   1  TITL   THE USE OF MOLECULAR-REPLACEMENT PHASES FOR THE REFINEMENT   
REMARK   1  TITL 2 OF THE HUMAN RHINOVIRUS 14 STRUCTURE                         
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  44   270 1988              
REMARK   1  REFN                   ISSN 0108-7673                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.G.ROSSMANN,E.ARNOLD,J.W.ERICKSON,E.A.FRANKENBERGER,        
REMARK   1  AUTH 2 J.P.GRIFFITH,H.-J.HECHT,J.E.JOHNSON,G.KAMER,M.LUO,           
REMARK   1  AUTH 3 A.G.MOSSER,R.R.RUECKERT,B.SHERRY,G.VRIEND                    
REMARK   1  TITL   STRUCTURE OF A HUMAN COMMON COLD VIRUS AND FUNCTIONAL        
REMARK   1  TITL 2 RELATIONSHIP TO OTHER PICORNAVIRUSES                         
REMARK   1  REF    NATURE                        V. 317   145 1985              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFI IN O                                            
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000173986.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUN-90; JAN-91                     
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : CHESS; CHESS                       
REMARK 200  BEAMLINE                       : A1; F1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL; NULL                         
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL; NULL                         
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : FILM; FILM                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PURDUE DATA PROCESSING PACKAGE     
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12300                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL; NULL                                     
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OSCILLATION RANGE 0.3 DEGREES, DISTANCE=100 AND 168 MM       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3-4 CRYSTALS SOAKED IN 200 MICROLITER    
REMARK 280  DROPS OF SDZ 35-682 (5 MICROGRAM/ML).                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
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       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000      222.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      222.55000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      222.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      222.55000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      222.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      222.55000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000      222.55000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000      222.55000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000      222.55000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000      222.55000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000      222.55000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000      222.55000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000      222.55000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000      222.55000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000      222.55000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000      222.55000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000      222.55000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000      222.55000            
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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).                 
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 APPLY THE FOLLOWING TO CHAINS: 1, 2, 3, 4                            
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   BIOMT1   2  0.464282 -0.829905  0.309355        0.18336            
REMARK 350   BIOMT2   2  0.844397  0.309355 -0.437372        0.04923            
REMARK 350   BIOMT3   2  0.267276  0.464282  0.844397       -0.09998            
REMARK 350   BIOMT1   3 -0.402527 -0.498417  0.767823        0.19670            
REMARK 350   BIOMT2   3  0.536358 -0.808132 -0.243400        0.26302            
REMARK 350   BIOMT3   3  0.741817  0.313853  0.592625       -0.11254            
REMARK 350   BIOMT1   4 -0.402527  0.536358  0.741817        0.02159            
REMARK 350   BIOMT2   4 -0.498417 -0.808132  0.313853        0.34591            
REMARK 350   BIOMT3   4  0.767823 -0.243400  0.592625       -0.02032            
REMARK 350   BIOMT1   5  0.464282  0.844397  0.267276       -0.09998            
REMARK 350   BIOMT2   5 -0.829905  0.309355  0.464282        0.18336            
REMARK 350   BIOMT3   5  0.309355 -0.437372  0.844397        0.04923            
REMARK 350   BIOMT1   6 -0.829905  0.309355  0.464282        0.18336            
REMARK 350   BIOMT2   6  0.309355 -0.437372  0.844397        0.04923            
REMARK 350   BIOMT3   6  0.464282  0.844397  0.267276       -0.09998            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1   8  0.844397  0.309355 -0.437372        0.04923            
REMARK 350   BIOMT2   8  0.267276  0.464282  0.844397       -0.09998            
REMARK 350   BIOMT3   8  0.464282 -0.829905  0.309355        0.18336            
REMARK 350   BIOMT1   9  0.536358 -0.808132 -0.243400        0.26302            
REMARK 350   BIOMT2   9  0.741817  0.313853  0.592625       -0.11254            
REMARK 350   BIOMT3   9 -0.402527 -0.498417  0.767823        0.19670            
REMARK 350   BIOMT1  10 -0.498417 -0.808132  0.313853        0.34591            
REMARK 350   BIOMT2  10  0.767823 -0.243400  0.592625       -0.02032            
REMARK 350   BIOMT3  10 -0.402527  0.536358  0.741817        0.02159            
REMARK 350   BIOMT1  11 -0.630565 -0.701509  0.332074        0.34718            
REMARK 350   BIOMT2  11 -0.701509  0.332074 -0.630565        0.34718            
REMARK 350   BIOMT3  11  0.332074 -0.630565 -0.701509        0.34718            
REMARK 350   BIOMT1  12 -0.796357  0.460470  0.392154        0.16382            
REMARK 350   BIOMT2  12 -0.213831  0.392154 -0.894702        0.29795            
REMARK 350   BIOMT3  12 -0.565768 -0.796357 -0.213831        0.44716            
REMARK 350   BIOMT1  13  0.123898  0.985418 -0.116620        0.00127            
REMARK 350   BIOMT2  13 -0.007277 -0.116620 -0.993150        0.36750            
REMARK 350   BIOMT3  13 -0.992269  0.123898 -0.007277        0.32559            
REMARK 350   BIOMT1  14  0.858438  0.147876 -0.491140        0.08416            
REMARK 350   BIOMT2  14 -0.367298 -0.491140 -0.789857        0.45972            
REMARK 350   BIOMT3  14 -0.358019  0.858438 -0.367298        0.15048            
REMARK 350   BIOMT1  15  0.392154 -0.894702 -0.213831        0.29795            
REMARK 350   BIOMT2  15 -0.796357 -0.213831 -0.565768        0.44716            
REMARK 350   BIOMT3  15  0.460470  0.392154 -0.796357        0.16382            
REMARK 350   BIOMT1  16  0.460470  0.392154 -0.796357        0.16382            
REMARK 350   BIOMT2  16  0.392154 -0.894702 -0.213831        0.29795            
REMARK 350   BIOMT3  16 -0.796357 -0.213831 -0.565768        0.44716            
REMARK 350   BIOMT1  17  0.332074 -0.630565 -0.701509        0.34718            
REMARK 350   BIOMT2  17 -0.630565 -0.701509  0.332074        0.34718            
REMARK 350   BIOMT3  17 -0.701509  0.332074 -0.630565        0.34718            
REMARK 350   BIOMT1  18 -0.565768 -0.796357 -0.213831        0.44716            
REMARK 350   BIOMT2  18 -0.796357  0.460470  0.392154        0.16382            
REMARK 350   BIOMT3  18 -0.213831  0.392154 -0.894702        0.29795            
REMARK 350   BIOMT1  19 -0.992269  0.123898 -0.007277        0.32559            
REMARK 350   BIOMT2  19  0.123898  0.985418 -0.116620        0.00127            
REMARK 350   BIOMT3  19 -0.007277 -0.116620 -0.993150        0.36750            
REMARK 350   BIOMT1  20 -0.358019  0.858438 -0.367298        0.15048            
REMARK 350   BIOMT2  20  0.858438  0.147876 -0.491140        0.08416            
REMARK 350   BIOMT3  20 -0.367298 -0.491140 -0.789857        0.45972            
REMARK 350   BIOMT1  21 -0.491140 -0.789857 -0.367298        0.45972            
REMARK 350   BIOMT2  21  0.858438 -0.367298 -0.358019        0.15048            
REMARK 350   BIOMT3  21  0.147876 -0.491140  0.858438        0.08416            
REMARK 350   BIOMT1  22 -0.993150 -0.007277 -0.116620        0.36750            
REMARK 350   BIOMT2  22 -0.007277 -0.992269  0.123898        0.32559            
REMARK 350   BIOMT3  22 -0.116620  0.123898  0.985418        0.00127            
REMARK 350   BIOMT1  23 -0.498417  0.767823 -0.402527        0.19670            
REMARK 350   BIOMT2  23 -0.808132 -0.243400  0.536358        0.26302            
REMARK 350   BIOMT3  23  0.313853  0.592625  0.741817       -0.11254            
REMARK 350   BIOMT1  24  0.309355  0.464282 -0.829905        0.18336            
REMARK 350   BIOMT2  24 -0.437372  0.844397  0.309355        0.04923            
REMARK 350   BIOMT3  24  0.844397  0.267276  0.464282       -0.09998            
REMARK 350   BIOMT1  25  0.313853 -0.498417 -0.808132        0.34591            
REMARK 350   BIOMT2  25  0.592625  0.767823 -0.243400       -0.02032            
REMARK 350   BIOMT3  25  0.741817 -0.402527  0.536358        0.02159            
REMARK 350   BIOMT1  26 -0.007277 -0.116620 -0.993150        0.36750            
REMARK 350   BIOMT2  26 -0.992269  0.123898 -0.007277        0.32559            
REMARK 350   BIOMT3  26  0.123898  0.985418 -0.116620        0.00127            
REMARK 350   BIOMT1  27 -0.367298 -0.491140 -0.789857        0.45972            
REMARK 350   BIOMT2  27 -0.358019  0.858438 -0.367298        0.15048            
REMARK 350   BIOMT3  27  0.858438  0.147876 -0.491140        0.08416            
REMARK 350   BIOMT1  28 -0.796357 -0.213831 -0.565768        0.44716            
REMARK 350   BIOMT2  28  0.460470  0.392154 -0.796357        0.16382            
REMARK 350   BIOMT3  28  0.392154 -0.894702 -0.213831        0.29795            
REMARK 350   BIOMT1  29 -0.701509  0.332074 -0.630565        0.34718            
REMARK 350   BIOMT2  29  0.332074 -0.630565 -0.701509        0.34718            
REMARK 350   BIOMT3  29 -0.630565 -0.701509  0.332074        0.34718            
REMARK 350   BIOMT1  30 -0.213831  0.392154 -0.894702        0.29795            
REMARK 350   BIOMT2  30 -0.565768 -0.796357 -0.213831        0.44716            
REMARK 350   BIOMT3  30 -0.796357  0.460470  0.392154        0.16382            
REMARK 350   BIOMT1  31  0.741817  0.313853  0.592625       -0.11254            
REMARK 350   BIOMT2  31 -0.402527 -0.498417  0.767823        0.19670            
REMARK 350   BIOMT3  31  0.536358 -0.808132 -0.243400        0.26302            
REMARK 350   BIOMT1  32  0.767823 -0.243400  0.592625       -0.02032            
REMARK 350   BIOMT2  32 -0.402527  0.536358  0.741817        0.02159            
REMARK 350   BIOMT3  32 -0.498417 -0.808132  0.313853        0.34591            
REMARK 350   BIOMT1  33  0.309355 -0.437372  0.844397        0.04923            
REMARK 350   BIOMT2  33  0.464282  0.844397  0.267276       -0.09998            
REMARK 350   BIOMT3  33 -0.829905  0.309355  0.464282        0.18336            
REMARK 350   BIOMT1  34  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  34  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  34  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  35  0.267276  0.464282  0.844397       -0.09998            
REMARK 350   BIOMT2  35  0.464282 -0.829905  0.309355        0.18336            
REMARK 350   BIOMT3  35  0.844397  0.309355 -0.437372        0.04923            
REMARK 350   BIOMT1  36 -0.243400  0.592625  0.767823       -0.02032            
REMARK 350   BIOMT2  36  0.536358  0.741817 -0.402527        0.02159            
REMARK 350   BIOMT3  36 -0.808132  0.313853 -0.498417        0.34591            
REMARK 350   BIOMT1  37  0.592625  0.741817  0.313853       -0.11254            
REMARK 350   BIOMT2  37  0.767823 -0.402527 -0.498417        0.19670            
REMARK 350   BIOMT3  37 -0.243400  0.536358 -0.808132        0.26302            
REMARK 350   BIOMT1  38  0.985418 -0.116620  0.123898        0.00127            
REMARK 350   BIOMT2  38 -0.116620 -0.993150 -0.007277        0.36750            
REMARK 350   BIOMT3  38  0.123898 -0.007277 -0.992269        0.32559            
REMARK 350   BIOMT1  39  0.392154 -0.796357  0.460470        0.16382            
REMARK 350   BIOMT2  39 -0.894702 -0.213831  0.392154        0.29795            
REMARK 350   BIOMT3  39 -0.213831 -0.565768 -0.796357        0.44716            
REMARK 350   BIOMT1  40 -0.367298 -0.358019  0.858438        0.15048            
REMARK 350   BIOMT2  40 -0.491140  0.858438  0.147876        0.08416            
REMARK 350   BIOMT3  40 -0.789857 -0.367298 -0.491140        0.45972            
REMARK 350   BIOMT1  41 -0.491140  0.858438  0.147876        0.08416            
REMARK 350   BIOMT2  41 -0.789857 -0.367298 -0.491140        0.45972            
REMARK 350   BIOMT3  41 -0.367298 -0.358019  0.858438        0.15048            
REMARK 350   BIOMT1  42  0.536358  0.741817 -0.402527        0.02159            
REMARK 350   BIOMT2  42 -0.808132  0.313853 -0.498417        0.34591            
REMARK 350   BIOMT3  42 -0.243400  0.592625  0.767823       -0.02032            
REMARK 350   BIOMT1  43  0.767823 -0.402527 -0.498417        0.19670            
REMARK 350   BIOMT2  43 -0.243400  0.536358 -0.808132        0.26302            
REMARK 350   BIOMT3  43  0.592625  0.741817  0.313853       -0.11254            
REMARK 350   BIOMT1  44 -0.116620 -0.993150 -0.007277        0.36750            
REMARK 350   BIOMT2  44  0.123898 -0.007277 -0.992269        0.32559            
REMARK 350   BIOMT3  44  0.985418 -0.116620  0.123898        0.00127            
REMARK 350   BIOMT1  45 -0.894702 -0.213831  0.392154        0.29795            
REMARK 350   BIOMT2  45 -0.213831 -0.565768 -0.796357        0.44716            
REMARK 350   BIOMT3  45  0.392154 -0.796357  0.460470        0.16382            
REMARK 350   BIOMT1  46  0.741817 -0.402527  0.536358        0.02159            
REMARK 350   BIOMT2  46  0.313853 -0.498417 -0.808132        0.34591            
REMARK 350   BIOMT3  46  0.592625  0.767823 -0.243400       -0.02032            
REMARK 350   BIOMT1  47  0.147876 -0.491140  0.858438        0.08416            
REMARK 350   BIOMT2  47 -0.491140 -0.789857 -0.367298        0.45972            
REMARK 350   BIOMT3  47  0.858438 -0.367298 -0.358019        0.15048            
REMARK 350   BIOMT1  48 -0.116620  0.123898  0.985418        0.00127            
REMARK 350   BIOMT2  48 -0.993150 -0.007277 -0.116620        0.36750            
REMARK 350   BIOMT3  48 -0.007277 -0.992269  0.123898        0.32559            
REMARK 350   BIOMT1  49  0.313853  0.592625  0.741817       -0.11254            
REMARK 350   BIOMT2  49 -0.498417  0.767823 -0.402527        0.19670            
REMARK 350   BIOMT3  49 -0.808132 -0.243400  0.536358        0.26302            
REMARK 350   BIOMT1  50  0.844397  0.267276  0.464282       -0.09998            
REMARK 350   BIOMT2  50  0.309355  0.464282 -0.829905        0.18336            
REMARK 350   BIOMT3  50 -0.437372  0.844397  0.309355        0.04923            
REMARK 350   BIOMT1  51 -0.243400  0.536358 -0.808132        0.26302            
REMARK 350   BIOMT2  51  0.592625  0.741817  0.313853       -0.11254            
REMARK 350   BIOMT3  51  0.767823 -0.402527 -0.498417        0.19670            
REMARK 350   BIOMT1  52  0.123898 -0.007277 -0.992269        0.32559            
REMARK 350   BIOMT2  52  0.985418 -0.116620  0.123898        0.00127            
REMARK 350   BIOMT3  52 -0.116620 -0.993150 -0.007277        0.36750            
REMARK 350   BIOMT1  53 -0.213831 -0.565768 -0.796357        0.44716            
REMARK 350   BIOMT2  53  0.392154 -0.796357  0.460470        0.16382            
REMARK 350   BIOMT3  53 -0.894702 -0.213831  0.392154        0.29795            
REMARK 350   BIOMT1  54 -0.789857 -0.367298 -0.491140        0.45972            
REMARK 350   BIOMT2  54 -0.367298 -0.358019  0.858438        0.15048            
REMARK 350   BIOMT3  54 -0.491140  0.858438  0.147876        0.08416            
REMARK 350   BIOMT1  55 -0.808132  0.313853 -0.498417        0.34591            
REMARK 350   BIOMT2  55 -0.243400  0.592625  0.767823       -0.02032            
REMARK 350   BIOMT3  55  0.536358  0.741817 -0.402527        0.02159            
REMARK 350   BIOMT1  56 -0.007277 -0.992269  0.123898        0.32559            
REMARK 350   BIOMT2  56 -0.116620  0.123898  0.985418        0.00127            
REMARK 350   BIOMT3  56 -0.993150 -0.007277 -0.116620        0.36750            
REMARK 350   BIOMT1  57 -0.808132 -0.243400  0.536358        0.26302            
REMARK 350   BIOMT2  57  0.313853  0.592625  0.741817       -0.11254            
REMARK 350   BIOMT3  57 -0.498417  0.767823 -0.402527        0.19670            
REMARK 350   BIOMT1  58 -0.437372  0.844397  0.309355        0.04923            
REMARK 350   BIOMT2  58  0.844397  0.267276  0.464282       -0.09998            
REMARK 350   BIOMT3  58  0.309355  0.464282 -0.829905        0.18336            
REMARK 350   BIOMT1  59  0.592625  0.767823 -0.243400       -0.02032            
REMARK 350   BIOMT2  59  0.741817 -0.402527  0.536358        0.02159            
REMARK 350   BIOMT3  59  0.313853 -0.498417 -0.808132        0.34591            
REMARK 350   BIOMT1  60  0.858438 -0.367298 -0.358019        0.15048            
REMARK 350   BIOMT2  60  0.147876 -0.491140  0.858438        0.08416            
REMARK 350   BIOMT3  60 -0.491140 -0.789857 -0.367298        0.45972            
REMARK 450                                                                      
REMARK 450 SOURCE                                                               
REMARK 450 MOLECULE_NAME: HRV14. GROWN IN HELA CELLS.                           
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     GLY 1     1                                                      
REMARK 465     LEU 1     2                                                      
REMARK 465     GLY 1     3                                                      
REMARK 465     ASP 1     4                                                      
REMARK 465     GLU 1     5                                                      
REMARK 465     LEU 1     6                                                      
REMARK 465     GLU 1     7                                                      
REMARK 465     GLU 1     8                                                      
REMARK 465     VAL 1     9                                                      
REMARK 465     ILE 1    10                                                      
REMARK 465     VAL 1    11                                                      
REMARK 465     GLU 1    12                                                      
REMARK 465     LYS 1    13                                                      
REMARK 465     THR 1    14                                                      
REMARK 465     LYS 1    15                                                      
REMARK 465     GLN 1    16                                                      
REMARK 465     SER 2     1                                                      
REMARK 465     PRO 2     2                                                      
REMARK 465     ASN 2     3                                                      
REMARK 465     VAL 2     4                                                      
REMARK 465     GLU 2     5                                                      
REMARK 465     ALA 2     6                                                      
REMARK 465     CYS 2     7                                                      
REMARK 465     GLY 4     1                                                      
REMARK 465     ALA 4     2                                                      
REMARK 465     GLN 4     3                                                      
REMARK 465     VAL 4     4                                                      
REMARK 465     SER 4     5                                                      
REMARK 465     THR 4     6                                                      
REMARK 465     GLN 4     7                                                      
REMARK 465     LYS 4     8                                                      
REMARK 465     SER 4     9                                                      
REMARK 465     GLY 4    10                                                      
REMARK 465     SER 4    11                                                      
REMARK 465     HIS 4    12                                                      
REMARK 465     GLU 4    13                                                      
REMARK 465     ASN 4    14                                                      
REMARK 465     GLN 4    15                                                      
REMARK 465     ASN 4    16                                                      
REMARK 465     ILE 4    17                                                      
REMARK 465     LEU 4    18                                                      
REMARK 465     THR 4    19                                                      
REMARK 465     ASN 4    20                                                      
REMARK 465     GLY 4    21                                                      
REMARK 465     SER 4    22                                                      
REMARK 465     ASN 4    23                                                      
REMARK 465     GLN 4    24                                                      
REMARK 465     THR 4    25                                                      
REMARK 465     PHE 4    26                                                      
REMARK 465     THR 4    27                                                      
REMARK 465     VAL 4    28                                                      
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   OG1  THR 1   129     NH1  ARG 1   185              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS 1  30   CD    LYS 1  30   CE      0.157                       
REMARK 500    LYS 1  30   CE    LYS 1  30   NZ      0.162                       
REMARK 500    GLU 1  38   CB    GLU 1  38   CG     -0.172                       
REMARK 500    GLU 1  52   C     GLU 1  52   O       0.120                       
REMARK 500    SER 1  63   CB    SER 1  63   OG     -0.114                       
REMARK 500    GLY 1  72   C     GLY 1  72   O       0.104                       
REMARK 500    GLU 1  81   CD    GLU 1  81   OE1     0.071                       
REMARK 500    GLU 1  95   CB    GLU 1  95   CG      0.193                       
REMARK 500    GLU 1 117   CD    GLU 1 117   OE1     0.103                       
REMARK 500    SER 1 139   CB    SER 1 139   OG      0.094                       
REMARK 500    SER 1 143   CB    SER 1 143   OG      0.088                       
REMARK 500    SER 1 144   N     SER 1 144   CA      0.120                       
REMARK 500    LYS 1 161   CE    LYS 1 161   NZ      0.165                       
REMARK 500    SER 1 170   CB    SER 1 170   OG     -0.186                       
REMARK 500    SER 1 175   CB    SER 1 175   OG     -0.119                       
REMARK 500    GLU 1 234   CD    GLU 1 234   OE1     0.081                       
REMARK 500    ARG 1 282   CD    ARG 1 282   NE      0.126                       
REMARK 500    LYS 1 283   N     LYS 1 283   CA      0.153                       
REMARK 500    LYS 1 283   CE    LYS 1 283   NZ      0.159                       
REMARK 500    ASP 1 285   CA    ASP 1 285   CB      0.260                       
REMARK 500    SER 1 288   CA    SER 1 288   CB      0.121                       
REMARK 500    GLY 2   8   N     GLY 2   8   CA      0.096                       
REMARK 500    ARG 2  12   NE    ARG 2  12   CZ      0.083                       
REMARK 500    GLU 2  40   CD    GLU 2  40   OE1     0.090                       
REMARK 500    LYS 2  52   CE    LYS 2  52   NZ      0.198                       
REMARK 500    LYS 2  87   CB    LYS 2  87   CG     -0.170                       
REMARK 500    HIS 2 135   CE1   HIS 2 135   NE2    -0.073                       
REMARK 500    GLU 2 136   CB    GLU 2 136   CG      0.144                       
REMARK 500    ARG 2 152   CD    ARG 2 152   NE      0.122                       
REMARK 500    ARG 2 152   CZ    ARG 2 152   NH2     0.091                       
REMARK 500    ASN 2 194   CA    ASN 2 194   CB      0.181                       
REMARK 500    SER 2 219   CA    SER 2 219   CB     -0.115                       
REMARK 500    CYS 2 248   CB    CYS 2 248   SG     -0.141                       
REMARK 500    SER 2 256   CB    SER 2 256   OG      0.132                       
REMARK 500    SER 2 256   C     SER 2 256   O       0.127                       
REMARK 500    GLY 3   1   N     GLY 3   1   CA      0.117                       
REMARK 500    SER 3  21   CA    SER 3  21   CB      0.131                       
REMARK 500    ASP 3  50   CA    ASP 3  50   CB     -0.134                       
REMARK 500    ASN 3  57   CA    ASN 3  57   CB      0.219                       
REMARK 500    LYS 3  61   CE    LYS 3  61   NZ      0.168                       
REMARK 500    GLU 3  63   CD    GLU 3  63   OE1     0.085                       
REMARK 500    SER 3 108   CB    SER 3 108   OG      0.097                       
REMARK 500    GLY 3 138   N     GLY 3 138   CA      0.094                       
REMARK 500    THR 3 164   C     THR 3 164   O       0.130                       
REMARK 500    SER 3 194   CB    SER 3 194   OG     -0.080                       
REMARK 500    LYS 4  33   CD    LYS 4  33   CE      0.153                       
REMARK 500    LYS 4  33   CE    LYS 4  33   NZ      0.185                       
REMARK 500    SER 4  40   CB    SER 4  40   OG      0.140                       
REMARK 500    ALA 4  41   C     ALA 4  41   O       0.179                       
REMARK 500    GLY 4  42   N     GLY 4  42   CA      0.176                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 BOND DEVIATIONS.                              
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    SER 1  22   N   -  CA  -  CB  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    LYS 1  26   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    THR 1  28   CB  -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    GLU 1  38   CA  -  CB  -  CG  ANGL. DEV. =  19.5 DEGREES          
REMARK 500    GLU 1  38   CB  -  CG  -  CD  ANGL. DEV. =  21.6 DEGREES          
REMARK 500    THR 1  42   CA  -  CB  -  CG2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    THR 1  53   CA  -  CB  -  OG1 ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG 1  54   CD  -  NE  -  CZ  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    SER 1  63   CB  -  CA  -  C   ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ASP 1  66   CB  -  CG  -  OD2 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    GLU 1  68   CG  -  CD  -  OE1 ANGL. DEV. = -13.1 DEGREES          
REMARK 500    GLU 1  68   CG  -  CD  -  OE2 ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ASP 1  86   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG 1  94   CD  -  NE  -  CZ  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ARG 1  94   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG 1  94   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    GLU 1  95   CB  -  CG  -  CD  ANGL. DEV. = -16.9 DEGREES          
REMARK 500    GLU 1  95   OE1 -  CD  -  OE2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    LYS 1  97   CD  -  CE  -  NZ  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ARG 1 113   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG 1 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    GLU 1 117   CG  -  CD  -  OE1 ANGL. DEV. = -12.2 DEGREES          
REMARK 500    GLU 1 117   CG  -  CD  -  OE2 ANGL. DEV. =  14.5 DEGREES          
REMARK 500    LEU 1 118   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES          
REMARK 500    TYR 1 121   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    VAL 1 122   N   -  CA  -  CB  ANGL. DEV. = -13.6 DEGREES          
REMARK 500    ASP 1 138   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    SER 1 144   N   -  CA  -  CB  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ASN 1 145   CA  -  CB  -  CG  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ASN 1 145   OD1 -  CG  -  ND2 ANGL. DEV. =  17.9 DEGREES          
REMARK 500    MET 1 151   CG  -  SD  -  CE  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    ASP 1 165   C   -  N   -  CA  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ASP 1 165   CB  -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ASP 1 165   CB  -  CG  -  OD1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ASP 1 165   CB  -  CG  -  OD2 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    SER 1 170   CA  -  CB  -  OG  ANGL. DEV. =  30.0 DEGREES          
REMARK 500    ASN 1 173   N   -  CA  -  CB  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    SER 1 175   CB  -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    VAL 1 176   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP 1 182   CB  -  CG  -  OD1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    TYR 1 197   CB  -  CA  -  C   ANGL. DEV. =  14.1 DEGREES          
REMARK 500    TYR 1 197   N   -  CA  -  CB  ANGL. DEV. = -23.3 DEGREES          
REMARK 500    TYR 1 197   CA  -  CB  -  CG  ANGL. DEV. =  20.1 DEGREES          
REMARK 500    ASP 1 208   CB  -  CG  -  OD1 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    MET 1 224   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG 1 242   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ARG 1 246   CD  -  NE  -  CZ  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ARG 1 246   NE  -  CZ  -  NH1 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG 1 246   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    GLU 1 251   CA  -  CB  -  CG  ANGL. DEV. =  18.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     167 ANGLE DEVIATIONS.                             
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    HIS 1  78      134.95   -171.82                                   
REMARK 500    ILE 1 104      125.25    -27.70                                   
REMARK 500    SER 1 139      102.44     24.61                                   
REMARK 500    PRO 1 154      171.64    -58.81                                   
REMARK 500    PRO 1 155       96.60    -67.85                                   
REMARK 500    ASP 1 165      168.76    -46.13                                   
REMARK 500    ALA 1 194     -155.62    -93.95                                   
REMARK 500    HIS 1 249       52.31     70.90                                   
REMARK 500    ILE 1 254       89.12     56.72                                   
REMARK 500    ASN 1 274       78.18     42.79                                   
REMARK 500    ASP 1 285      171.37    -59.45                                   
REMARK 500    GLU 2  27       54.19   -148.92                                   
REMARK 500    ASN 2  30     -157.54     58.08                                   
REMARK 500    SER 2  48      -60.14   -131.62                                   
REMARK 500    ASP 2  57     -126.64     58.08                                   
REMARK 500    ALA 2 114     -134.64   -145.97                                   
REMARK 500    LEU 2 170       -8.63    -57.39                                   
REMARK 500    ASN 2 174       16.35   -156.09                                   
REMARK 500    PRO 2 227      150.31    -48.89                                   
REMARK 500    PRO 2 236       42.45    -79.60                                   
REMARK 500    ARG 2 255     -134.24   -173.03                                   
REMARK 500    LYS 2 257      100.70    104.05                                   
REMARK 500    LEU 3  25       75.33   -106.43                                   
REMARK 500    ILE 3  47        0.39    -68.13                                   
REMARK 500    ASN 3  56       34.86    -81.15                                   
REMARK 500    ASN 3  57       -7.17    -31.01                                   
REMARK 500    ASN 3  74       23.12     48.10                                   
REMARK 500    ASN 3  77      -14.35     38.75                                   
REMARK 500    LEU 3  85       61.06   -112.41                                   
REMARK 500    THR 3 193      -82.97   -124.71                                   
REMARK 500    SER 3 194      158.46    173.32                                   
REMARK 500    LEU 3 221       82.57     62.23                                   
REMARK 500    SER 4  46      -74.50    -96.88                                   
REMARK 500    MET 4  47       94.73     60.34                                   
REMARK 500    GLU 4  54       58.67   -143.73                                   
REMARK 500    PRO 4  55       38.49    -82.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG 1 259         0.12    SIDE CHAIN                              
REMARK 500    ARG 1 268         0.12    SIDE CHAIN                              
REMARK 500    ARG 2  12         0.10    SIDE CHAIN                              
REMARK 500    ARG 2 255         0.10    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SDZ 1 682                 
DBREF  1HRV 1    1   289  UNP    P03303   POLG_HRV14     567    855             
DBREF  1HRV 2    1   262  UNP    P03303   POLG_HRV14      69    330             
DBREF  1HRV 3    1   236  UNP    P03303   POLG_HRV14     331    566             
DBREF  1HRV 4    1    68  UNP    P03303   POLG_HRV14       1     68             
SEQADV 1HRV LEU 2  170  UNP  P03303    ILE   239 CONFLICT                       
SEQRES   1 1  289  GLY LEU GLY ASP GLU LEU GLU GLU VAL ILE VAL GLU LYS          
SEQRES   2 1  289  THR LYS GLN THR VAL ALA SER ILE SER SER GLY PRO LYS          
SEQRES   3 1  289  HIS THR GLN LYS VAL PRO ILE LEU THR ALA ASN GLU THR          
SEQRES   4 1  289  GLY ALA THR MET PRO VAL LEU PRO SER ASP SER ILE GLU          
SEQRES   5 1  289  THR ARG THR THR TYR MET HIS PHE ASN GLY SER GLU THR          
SEQRES   6 1  289  ASP VAL GLU CYS PHE LEU GLY ARG ALA ALA CYS VAL HIS          
SEQRES   7 1  289  VAL THR GLU ILE GLN ASN LYS ASP ALA THR GLY ILE ASP          
SEQRES   8 1  289  ASN HIS ARG GLU ALA LYS LEU PHE ASN ASP TRP LYS ILE          
SEQRES   9 1  289  ASN LEU SER SER LEU VAL GLN LEU ARG LYS LYS LEU GLU          
SEQRES  10 1  289  LEU PHE THR TYR VAL ARG PHE ASP SER GLU TYR THR ILE          
SEQRES  11 1  289  LEU ALA THR ALA SER GLN PRO ASP SER ALA ASN TYR SER          
SEQRES  12 1  289  SER ASN LEU VAL VAL GLN ALA MET TYR VAL PRO PRO GLY          
SEQRES  13 1  289  ALA PRO ASN PRO LYS GLU TRP ASP ASP TYR THR TRP GLN          
SEQRES  14 1  289  SER ALA SER ASN PRO SER VAL PHE PHE LYS VAL GLY ASP          
SEQRES  15 1  289  THR SER ARG PHE SER VAL PRO TYR VAL GLY LEU ALA SER          
SEQRES  16 1  289  ALA TYR ASN CYS PHE TYR ASP GLY TYR SER HIS ASP ASP          
SEQRES  17 1  289  ALA GLU THR GLN TYR GLY ILE THR VAL LEU ASN HIS MET          
SEQRES  18 1  289  GLY SER MET ALA PHE ARG ILE VAL ASN GLU HIS ASP GLU          
SEQRES  19 1  289  HIS LYS THR LEU VAL LYS ILE ARG VAL TYR HIS ARG ALA          
SEQRES  20 1  289  LYS HIS VAL GLU ALA TRP ILE PRO ARG ALA PRO ARG ALA          
SEQRES  21 1  289  LEU PRO TYR THR SER ILE GLY ARG THR ASN TYR PRO LYS          
SEQRES  22 1  289  ASN THR GLU PRO VAL ILE LYS LYS ARG LYS GLY ASP ILE          
SEQRES  23 1  289  LYS SER TYR                                                  
SEQRES   1 2  262  SER PRO ASN VAL GLU ALA CYS GLY TYR SER ASP ARG VAL          
SEQRES   2 2  262  GLN GLN ILE THR LEU GLY ASN SER THR ILE THR THR GLN          
SEQRES   3 2  262  GLU ALA ALA ASN ALA VAL VAL CYS TYR ALA GLU TRP PRO          
SEQRES   4 2  262  GLU TYR LEU PRO ASP VAL ASP ALA SER ASP VAL ASN LYS          
SEQRES   5 2  262  THR SER LYS PRO ASP THR SER VAL CYS ARG PHE TYR THR          
SEQRES   6 2  262  LEU ASP SER LYS THR TRP THR THR GLY SER LYS GLY TRP          
SEQRES   7 2  262  CYS TRP LYS LEU PRO ASP ALA LEU LYS ASP MET GLY VAL          
SEQRES   8 2  262  PHE GLY GLN ASN MET PHE PHE HIS SER LEU GLY ARG SER          
SEQRES   9 2  262  GLY TYR THR VAL HIS VAL GLN CYS ASN ALA THR LYS PHE          
SEQRES  10 2  262  HIS SER GLY CYS LEU LEU VAL VAL VAL ILE PRO GLU HIS          
SEQRES  11 2  262  GLN LEU ALA SER HIS GLU GLY GLY ASN VAL SER VAL LYS          
SEQRES  12 2  262  TYR THR PHE THR HIS PRO GLY GLU ARG GLY ILE ASP LEU          
SEQRES  13 2  262  SER SER ALA ASN GLU VAL GLY GLY PRO VAL LYS ASP VAL          
SEQRES  14 2  262  LEU TYR ASN MET ASN GLY THR LEU LEU GLY ASN LEU LEU          
SEQRES  15 2  262  ILE PHE PRO HIS GLN PHE ILE ASN LEU ARG THR ASN ASN          
SEQRES  16 2  262  THR ALA THR ILE VAL ILE PRO TYR ILE ASN SER VAL PRO          
SEQRES  17 2  262  ILE ASP SER MET THR ARG HIS ASN ASN VAL SER LEU MET          
SEQRES  18 2  262  VAL ILE PRO ILE ALA PRO LEU THR VAL PRO THR GLY ALA          
SEQRES  19 2  262  THR PRO SER LEU PRO ILE THR VAL THR ILE ALA PRO MET          
SEQRES  20 2  262  CYS THR GLU PHE SER GLY ILE ARG SER LYS SER ILE VAL          
SEQRES  21 2  262  PRO GLN                                                      
SEQRES   1 3  236  GLY LEU PRO THR THR THR LEU PRO GLY SER GLY GLN PHE          
SEQRES   2 3  236  LEU THR THR ASP ASP ARG GLN SER PRO SER ALA LEU PRO          
SEQRES   3 3  236  ASN TYR GLU PRO THR PRO ARG ILE HIS ILE PRO GLY LYS          
SEQRES   4 3  236  VAL HIS ASN LEU LEU GLU ILE ILE GLN VAL ASP THR LEU          
SEQRES   5 3  236  ILE PRO MET ASN ASN THR HIS THR LYS ASP GLU VAL ASN          
SEQRES   6 3  236  SER TYR LEU ILE PRO LEU ASN ALA ASN ARG GLN ASN GLU          
SEQRES   7 3  236  GLN VAL PHE GLY THR ASN LEU PHE ILE GLY ASP GLY VAL          
SEQRES   8 3  236  PHE LYS THR THR LEU LEU GLY GLU ILE VAL GLN TYR TYR          
SEQRES   9 3  236  THR HIS TRP SER GLY SER LEU ARG PHE SER LEU MET TYR          
SEQRES  10 3  236  THR GLY PRO ALA LEU SER SER ALA LYS LEU ILE LEU ALA          
SEQRES  11 3  236  TYR THR PRO PRO GLY ALA ARG GLY PRO GLN ASP ARG ARG          
SEQRES  12 3  236  GLU ALA MET LEU GLY THR HIS VAL VAL TRP ASP ILE GLY          
SEQRES  13 3  236  LEU GLN SER THR ILE VAL MET THR ILE PRO TRP THR SER          
SEQRES  14 3  236  GLY VAL GLN PHE ARG TYR THR ASP PRO ASP THR TYR THR          
SEQRES  15 3  236  SER ALA GLY PHE LEU SER CYS TRP TYR GLN THR SER LEU          
SEQRES  16 3  236  ILE LEU PRO PRO GLU THR THR GLY GLN VAL TYR LEU LEU          
SEQRES  17 3  236  SER PHE ILE SER ALA CYS PRO ASP PHE LYS LEU ARG LEU          
SEQRES  18 3  236  MET LYS ASP THR GLN THR ILE SER GLN THR VAL ALA LEU          
SEQRES  19 3  236  THR GLU                                                      
SEQRES   1 4   68  GLY ALA GLN VAL SER THR GLN LYS SER GLY SER HIS GLU          
SEQRES   2 4   68  ASN GLN ASN ILE LEU THR ASN GLY SER ASN GLN THR PHE          
SEQRES   3 4   68  THR VAL ILE ASN TYR TYR LYS ASP ALA ALA SER THR SER          
SEQRES   4 4   68  SER ALA GLY GLN SER LEU SER MET ASP PRO SER LYS PHE          
SEQRES   5 4   68  THR GLU PRO VAL LYS ASP LEU MET LEU LYS GLY ALA PRO          
SEQRES   6 4   68  ALA LEU ASN                                                  
HET    SDZ  1 682      58                                                       
HETNAM     SDZ 1-[2-HYDROXY-3-(4-CYCLOHEXYL-PHENOXY)-PROPYL]-4-(2-              
HETNAM   2 SDZ  PYRIDYL)-PIPERAZINE                                             
FORMUL   5  SDZ    C24 H33 N3 O2                                                
HELIX    1   1 ASN 1   37  THR 1   39  5                                   3    
HELIX    2   2 PRO 1   47  ASP 1   49  5                                   3    
HELIX    3   3 SER 1   63  THR 1   65  5                                   3    
HELIX    4   4 VAL 1   67  PHE 1   70  1                                   4    
HELIX    5   5 VAL 1  110  LEU 1  118  1                                   9    
HELIX    6   6 TYR 1  166  GLN 1  169  5                                   4    
HELIX    7   7 CYS 2   34  ALA 2   36  5                                   3    
HELIX    8   8 ASP 2   44  ASP 2   46  5                                   3    
HELIX    9   9 ASP 2   57  SER 2   59  5                                   3    
HELIX   10  10 ASP 2   84  LEU 2   86  5                                   3    
HELIX   11  11 GLY 2   90  PHE 2   98  1                                   9    
HELIX   12  12 TYR 2  144  THR 2  147  5                                   4    
HELIX   13  13 GLY 2  150  ARG 2  152  5                                   3    
HELIX   14  14 VAL 2  169  TYR 2  171  5                                   3    
HELIX   15  15 LEU 2  178  ILE 2  183  5                                   6    
HELIX   16  16 LEU 3   43  GLN 3   48  1                                   6    
HELIX   17  17 VAL 3   64  SER 3   66  5                                   3    
HELIX   18  18 GLY 3   90  THR 3   94  5                                   5    
HELIX   19  19 LEU 3   96  TYR 3  103  1                                   8    
HELIX   20  20 ARG 3  142  LEU 3  147  1                                   6    
HELIX   21  21 ALA 4   35  SER 4   37  5                                   3    
HELIX   22  22 PRO 4   49  THR 4   53  5                                   5    
SHEET    1   A 4 PHE 1  99  TRP 1 102  0                                        
SHEET    2   A 4 SER 1 223  ILE 1 228 -1  N  PHE 1 226   O  ASN 1 100           
SHEET    3   A 4 VAL 1 147  VAL 1 153 -1  N  VAL 1 153   O  SER 1 223           
SHEET    4   A 4 SER 1 175  LYS 1 179 -1  N  PHE 1 178   O  VAL 1 148           
SHEET    1   B 2 TYR 1 121  ARG 1 123  0                                        
SHEET    2   B 2 GLU 1 251  TRP 1 253 -1  N  TRP 1 253   O  TYR 1 121           
SHEET    1   C 4 THR 1 183  VAL 1 188  0                                        
SHEET    2   C 4 ASP 1 125  SER 1 135 -1  N  ILE 1 130   O  SER 1 184           
SHEET    3   C 4 THR 1 237  LYS 1 248 -1  N  LYS 1 248   O  ASP 1 125           
SHEET    4   C 4 ALA 1  75  ASN 1  84 -1  N  ASN 1  84   O  THR 1 237           
SHEET    1   D 2 GLN 2  14  LEU 2  18  0                                        
SHEET    2   D 2 SER 2  21  THR 2  25 -1  N  THR 2  25   O  GLN 2  14           
SHEET    1   E 4 PHE 2  63  THR 2  65  0                                        
SHEET    2   E 4 THR 2 241  MET 2 247 -1  N  ILE 2 244   O  TYR 2  64           
SHEET    3   E 4 GLY 2 105  GLN 2 111 -1  N  GLN 2 111   O  THR 2 241           
SHEET    4   E 4 THR 2 196  ILE 2 201 -1  N  ILE 2 201   O  TYR 2 106           
SHEET    1   F 2 LYS 2  69  THR 2  72  0                                        
SHEET    2   F 2 SER 2 237  ILE 2 240 -1  N  ILE 2 240   O  LYS 2  69           
SHEET    1   G 4 TRP 2  78  LEU 2  82  0                                        
SHEET    2   G 4 VAL 2 218  ALA 2 226 -1  N  VAL 2 222   O  TRP 2  78           
SHEET    3   G 4 CYS 2 121  PRO 2 128 -1  N  ILE 2 127   O  SER 2 219           
SHEET    4   G 4 HIS 2 186  ASN 2 190 -1  N  ILE 2 189   O  LEU 2 122           
SHEET    1   H 2 LEU 2 101  ARG 2 103  0                                        
SHEET    2   H 2 GLU 2 250  SER 2 252 -1  N  SER 2 252   O  LEU 2 101           
SHEET    1   I 4 LEU 3  68  ASN 3  72  0                                        
SHEET    2   I 4 GLN 3 204  ALA 3 213 -1  N  LEU 3 207   O  ILE 3  69           
SHEET    3   I 4 LEU 3 111  TYR 3 117 -1  N  MET 3 116   O  LEU 3 208           
SHEET    4   I 4 THR 3 160  ILE 3 165 -1  N  ILE 3 165   O  LEU 3 111           
SHEET    1   J 2 HIS 3 106  SER 3 108  0                                        
SHEET    2   J 2 LYS 3 218  ARG 3 220 -1  N  ARG 3 220   O  HIS 3 106           
SHEET    1   K 4 THR 3 149  ASP 3 154  0                                        
SHEET    2   K 4 LYS 3 126  THR 3 132 -1  N  TYR 3 131   O  THR 3 149           
SHEET    3   K 4 PHE 3 186  TYR 3 191 -1  N  TRP 3 190   O  ILE 3 128           
SHEET    4   K 4 GLN 3  79  ASN 3  84 -1  N  THR 3  83   O  LEU 3 187           
CISPEP   1 LEU 2   82    PRO 2   83          0         2.69                     
SITE     1 AC1 15 ILE 1 104  LEU 1 106  SER 1 107  LEU 1 116                    
SITE     2 AC1 15 PHE 1 124  SER 1 126  TYR 1 128  TYR 1 152                    
SITE     3 AC1 15 PRO 1 174  PHE 1 186  VAL 1 188  TYR 1 197                    
SITE     4 AC1 15 ILE 1 215  MET 1 224  ALA 3  24                               
CRYST1  445.100  445.100  445.100  90.00  90.00  90.00 P 21 3      240          
ORIGX1      0.996348 -0.058524  0.062176       -0.17359                         
ORIGX2      0.062176  0.996348 -0.058524       -0.17359                         
ORIGX3     -0.058524  0.062176  0.996348       -0.17359                         
SCALE1      0.002247  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002247  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002247        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.464282 -0.829905  0.309355        0.18336                         
MTRIX2   2  0.844397  0.309355 -0.437372        0.04923                         
MTRIX3   2  0.267276  0.464282  0.844397       -0.09998                         
MTRIX1   3 -0.402527 -0.498417  0.767824        0.19670                         
MTRIX2   3  0.536358 -0.808132 -0.243400        0.26302                         
MTRIX3   3  0.741817  0.313853  0.592625       -0.11254                         
MTRIX1   4 -0.402527  0.536358  0.741817        0.02159                         
MTRIX2   4 -0.498417 -0.808132  0.313853        0.34591                         
MTRIX3   4  0.767824 -0.243400  0.592625       -0.02032                         
MTRIX1   5  0.464282  0.844397  0.267276       -0.09998                         
MTRIX2   5 -0.829905  0.309355  0.464282        0.18336                         
MTRIX3   5  0.309355 -0.437372  0.844397        0.04923                         
MTRIX1   6 -0.630565 -0.701509  0.332074        0.34718                         
MTRIX2   6 -0.701509  0.332074 -0.630565        0.34718                         
MTRIX3   6  0.332074 -0.630565 -0.701509        0.34718                         
MTRIX1   7 -0.796357  0.460470  0.392154        0.16382                         
MTRIX2   7 -0.213831  0.392154 -0.894702        0.29795                         
MTRIX3   7 -0.565768 -0.796357 -0.213831        0.44716                         
MTRIX1   8  0.123898  0.985418 -0.116620        0.00127                         
MTRIX2   8 -0.007277 -0.116620 -0.993150        0.36750                         
MTRIX3   8 -0.992269  0.123898 -0.007277        0.32559                         
MTRIX1   9  0.858438  0.147876 -0.491140        0.08416                         
MTRIX2   9 -0.367298 -0.491140 -0.789857        0.45972                         
MTRIX3   9 -0.358019  0.858438 -0.367298        0.15048                         
MTRIX1  10  0.392154 -0.894702 -0.213831        0.29795                         
MTRIX2  10 -0.796357 -0.213831 -0.565768        0.44716                         
MTRIX3  10  0.460470  0.392154 -0.796357        0.16382                         
MTRIX1  11 -0.491140 -0.789857 -0.367298        0.45972                         
MTRIX2  11  0.858438 -0.367298 -0.358019        0.15048                         
MTRIX3  11  0.147876 -0.491140  0.858438        0.08416                         
MTRIX1  12 -0.993150 -0.007277 -0.116620        0.36750                         
MTRIX2  12 -0.007277 -0.992269  0.123898        0.32559                         
MTRIX3  12 -0.116620  0.123898  0.985418        0.00127                         
MTRIX1  13 -0.498417  0.767824 -0.402527        0.19670                         
MTRIX2  13 -0.808132 -0.243400  0.536358        0.26302                         
MTRIX3  13  0.313853  0.592625  0.741817       -0.11254                         
MTRIX1  14  0.309355  0.464282 -0.829905        0.18336                         
MTRIX2  14 -0.437372  0.844397  0.309355        0.04923                         
MTRIX3  14  0.844397  0.267276  0.464282       -0.09998                         
MTRIX1  15  0.313853 -0.498417 -0.808132        0.34591                         
MTRIX2  15  0.592625  0.767824 -0.243400       -0.02032                         
MTRIX3  15  0.741817 -0.402527  0.536358        0.02159                         
MTRIX1  16 -0.243400  0.592625  0.767824       -0.02032                         
MTRIX2  16  0.536358  0.741817 -0.402527        0.02159                         
MTRIX3  16 -0.808132  0.313853 -0.498417        0.34591                         
MTRIX1  17  0.592625  0.741817  0.313853       -0.11254                         
MTRIX2  17  0.767824 -0.402527 -0.498417        0.19670                         
MTRIX3  17 -0.243400  0.536358 -0.808132        0.26302                         
MTRIX1  18  0.985418 -0.116620  0.123898        0.00127                         
MTRIX2  18 -0.116620 -0.993150 -0.007277        0.36750                         
MTRIX3  18  0.123898 -0.007277 -0.992269        0.32559                         
MTRIX1  19  0.392154 -0.796357  0.460470        0.16382                         
MTRIX2  19 -0.894702 -0.213831  0.392154        0.29795                         
MTRIX3  19 -0.213831 -0.565768 -0.796357        0.44716                         
MTRIX1  20 -0.367298 -0.358019  0.858438        0.15048                         
MTRIX2  20 -0.491140  0.858438  0.147876        0.08416                         
MTRIX3  20 -0.789857 -0.367298 -0.491140        0.45972                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system