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Database: PDB
Entry: 1UWB
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HEADER    ASPARTYL PROTEASE                       21-NOV-96   1UWB              
TITLE     TYR 181 CYS HIV-1 RT/8-CL TIBO                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: REVERSE TRANSCRIPTASE;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.7.49;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: REVERSE TRANSCRIPTASE;                                     
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 2.7.7.49;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 STRAIN: BH10;                                                        
SOURCE   5 CELL_LINE: 293;                                                      
SOURCE   6 ATCC: 1065288;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: 293;                                       
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  12 ORGANISM_TAXID: 11676;                                               
SOURCE  13 STRAIN: BH10;                                                        
SOURCE  14 CELL_LINE: 293;                                                      
SOURCE  15 ATCC: 1065288;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: 293                                        
KEYWDS    AIDS, POLYPROTEIN, HYDROLASE, ASPARTYL PROTEASE, ENDONUCLEASE, RNA-   
KEYWDS   2 DIRECTED DNA POLYMERASE, TYR181CYS HIV-1 RT/8-CL TIBO, DRUG-         
KEYWDS   3 RESISTANT MUTANT                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.DAS,J.DING,Y.HSIOU,E.ARNOLD                                         
REVDAT   5   14-FEB-24 1UWB    1       REMARK                                   
REVDAT   4   03-NOV-21 1UWB    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1UWB    1       VERSN                                    
REVDAT   2   01-APR-03 1UWB    1       JRNL                                     
REVDAT   1   15-MAY-97 1UWB    0                                                
JRNL        AUTH   K.DAS,J.DING,Y.HSIOU,A.D.CLARK JR.,H.MOEREELS,L.KOYMANS,     
JRNL        AUTH 2 K.ANDRIES,R.PAUWELS,P.A.JANSSEN,P.L.BOYER,P.CLARK,           
JRNL        AUTH 3 R.H.SMITH JR.,M.B.KROEGER SMITH,C.J.MICHEJDA,S.H.HUGHES,     
JRNL        AUTH 4 E.ARNOLD                                                     
JRNL        TITL   CRYSTAL STRUCTURES OF 8-CL AND 9-CL TIBO COMPLEXED WITH      
JRNL        TITL 2 WILD-TYPE HIV-1 RT AND 8-CL TIBO COMPLEXED WITH THE          
JRNL        TITL 3 TYR181CYS HIV-1 RT DRUG-RESISTANT MUTANT.                    
JRNL        REF    J.MOL.BIOL.                   V. 264  1085 1996              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9000632                                                      
JRNL        DOI    10.1006/JMBI.1996.0698                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.ARNOLD,K.DAS,J.DING,P.N.YADAV,Y.HSIOU,P.L.BOYER,S.H.HUGHES 
REMARK   1  TITL   TARGETING HIV REVERSE TRANSCRIPTASE FOR ANTI-AIDS DRUG       
REMARK   1  TITL 2 DESIGN: STRUCTURAL AND BIOLOGICAL CONSIDERATIONS FOR         
REMARK   1  TITL 3 CHEMOTHERAPEUTIC STRATEGIES                                  
REMARK   1  REF    DRUG DES.DISCOVERY            V.  13    29 1996              
REMARK   1  REFN                   ISSN 1055-9612                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.HSIOU,J.DING,K.DAS,A.D.CLARK JUNIOR,S.H.HUGHES,E.ARNOLD    
REMARK   1  TITL   STRUCTURE OF UNLIGANDED HIV-1 REVERSE TRANSCRIPTASE AT 2.7 A 
REMARK   1  TITL 2 RESOLUTION: IMPLICATIONS OF CONFORMATIONAL CHANGES FOR       
REMARK   1  TITL 3 POLYMERIZATION AND INHIBITION MECHANISMS                     
REMARK   1  REF    STRUCTURE                     V.   4   853 1996              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   P.H.PATEL,A.JACOBO-MOLINA,J.DING,C.TANTILLO,                 
REMARK   1  AUTH 2 A.D.CLARK JUNIOR,R.RAAG,R.G.NANNI,S.H.HUGHES,E.ARNOLD        
REMARK   1  TITL   INSIGHTS INTO DNA POLYMERIZATION MECHANISMS FROM STRUCTURE   
REMARK   1  TITL 2 AND FUNCTION ANALYSIS OF HIV-1 REVERSE TRANSCRIPTASE         
REMARK   1  REF    BIOCHEMISTRY                  V.  34  5351 1995              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.DING,K.DAS,C.TANTILLO,W.ZHANG,A.D.CLARK JUNIOR,S.JESSEN,   
REMARK   1  AUTH 2 X.LU,Y.HSIOU,A.JACOBO-MOLINA,K.ANDRIES,ET AL.                
REMARK   1  TITL   STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE IN A COMPLEX WITH   
REMARK   1  TITL 2 THE NON-NUCLEOSIDE INHIBITOR ALPHA-APA R 95845 AT 2.8 A      
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    STRUCTURE                     V.   3   365 1995              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   J.DING,K.DAS,H.MOEREELS,L.KOYMANS,K.ANDRIES,P.A.JANSSEN,     
REMARK   1  AUTH 2 S.H.HUGHES,E.ARNOLD                                          
REMARK   1  TITL   STRUCTURE OF HIV-1 RT/TIBO R 86183 COMPLEX REVEALS           
REMARK   1  TITL 2 SIMILARITY IN THE BINDING OF DIVERSE NONNUCLEOSIDE           
REMARK   1  TITL 3 INHIBITORS                                                   
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   2   407 1995              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   C.TANTILLO,J.DING,A.JACOBO-MOLINA,R.G.NANNI,P.L.BOYER,       
REMARK   1  AUTH 2 S.H.HUGHES,R.PAUWELS,K.ANDRIES,P.A.JANSSEN,E.ARNOLD          
REMARK   1  TITL   LOCATIONS OF ANTI-AIDS DRUG BINDING SITES AND RESISTANCE     
REMARK   1  TITL 2 MUTATIONS IN THE THREE-DIMENSIONAL STRUCTURE OF HIV-1        
REMARK   1  TITL 3 REVERSE TRANSCRIPTASE. IMPLICATIONS FOR MECHANISMS OF DRUG   
REMARK   1  TITL 4 INHIBITION AND RESISTANCE                                    
REMARK   1  REF    J.MOL.BIOL.                   V. 243   369 1994              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   A.JACOBO-MOLINA,J.DING,R.G.NANNI,A.D.CLARK JUNIOR,X.LU,      
REMARK   1  AUTH 2 C.TANTILLO,R.L.WILLIAMS,G.KAMER,A.L.FERRIS,P.CLARK,ET AL.    
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1     
REMARK   1  TITL 2 REVERSE TRANSCRIPTASE COMPLEXED WITH DOUBLE-STRANDED DNA AT  
REMARK   1  TITL 3 3.0 A RESOLUTION SHOWS BENT DNA                              
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  90  6320 1993              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 10.0000                        
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 21825                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.274                           
REMARK   3   FREE R VALUE                     : 0.360                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1059                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1944                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3870                       
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 94                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.037                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7801                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.60                          
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) : 0.51                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 10.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.71                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.68                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.800                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.600                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.570 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.820 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.640 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.680 ; 2.500                
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : TBO.PAR                                        
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TBO.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED                   
REMARK   4                                                                      
REMARK   4 1UWB 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_1000176990.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAR-96                             
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
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                : 2.620                              
REMARK 200  R MERGE                    (I) : 0.10500                            
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                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      112.85000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.60000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      112.85000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       34.60000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5620 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 48890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  36    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  66    CG   CD   CE   NZ                                   
REMARK 470     TRP A  71    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A  71    CZ3  CH2                                            
REMARK 470     ARG A  72    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 134    OG                                                  
REMARK 470     ILE A 135    CG1  CG2  CD1                                       
REMARK 470     ASN A 136    CG   OD1  ND2                                       
REMARK 470     ASN A 137    CG   OD1  ND2                                       
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     THR A 139    OG1  CG2                                            
REMARK 470     CYS A 181    SG                                                  
REMARK 470     ASP A 218    CG   OD1  OD2                                       
REMARK 470     LYS A 219    CG   CD   CE   NZ                                   
REMARK 470     LYS A 220    CG   CD   CE   NZ                                   
REMARK 470     HIS A 221    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 222    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     LEU A 282    CG   CD1  CD2                                       
REMARK 470     LEU A 283    CG   CD1  CD2                                       
REMARK 470     ARG A 284    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 286    OG1  CG2                                            
REMARK 470     LYS A 287    CG   CD   CE   NZ                                   
REMARK 470     LEU A 289    CG   CD1  CD2                                       
REMARK 470     THR A 290    OG1  CG2                                            
REMARK 470     GLU A 291    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 292    CG1  CG2                                            
REMARK 470     ILE A 293    CG1  CG2  CD1                                       
REMARK 470     GLU A 297    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 298    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 300    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 301    CG   CD1  CD2                                       
REMARK 470     GLU A 302    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 311    CG   CD   CE   NZ                                   
REMARK 470     GLU A 312    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 323    CG   CD   CE   NZ                                   
REMARK 470     ARG A 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET A 357    CG   SD   CE                                        
REMARK 470     ARG A 358    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 366    CG   CD   CE   NZ                                   
REMARK 470     LYS A 451    CG   CD   CE   NZ                                   
REMARK 470     ILE A 556    CG1  CG2  CD1                                       
REMARK 470     ARG A 557    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 558    CG   CD   CE   NZ                                   
REMARK 470     LYS B  13    CG   CD   CE   NZ                                   
REMARK 470     ASP B 121    CG   OD1  OD2                                       
REMARK 470     GLN B 197    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 199    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 220    CG   CD   CE   NZ                                   
REMARK 470     GLN B 222    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 223    CG   CD   CE   NZ                                   
REMARK 470     GLU B 224    CG   CD   OE1  OE2                                  
REMARK 470     PRO B 225    CG   CD                                             
REMARK 470     PRO B 226    CG   CD                                             
REMARK 470     PHE B 227    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 228    CG   CD1  CD2                                       
REMARK 470     TRP B 229    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 229    CZ3  CH2                                            
REMARK 470     MET B 230    CG   SD   CE                                        
REMARK 470     ILE B 270    CG1  CG2  CD1                                       
REMARK 470     GLN B 278    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 281    CG   CD   CE   NZ                                   
REMARK 470     MET B 357    CG   SD   CE                                        
REMARK 470     ARG B 358    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B 361    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B 362    OG1  CG2                                            
REMARK 470     ASN B 363    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 176   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    LYS A 287   N   -  CA  -  C   ANGL. DEV. =  18.7 DEGREES          
REMARK 500    PRO B  52   C   -  N   -  CA  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    PRO B  97   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    PRO B 133   C   -  N   -  CA  ANGL. DEV. =  12.8 DEGREES          
REMARK 500    PRO B 345   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A   4       27.35    -76.76                                   
REMARK 500    GLU A   6      101.74    -59.12                                   
REMARK 500    GLU A  28      -19.72    -47.43                                   
REMARK 500    PRO A  52      -85.10    -51.95                                   
REMARK 500    ASN A  54      105.70   -165.75                                   
REMARK 500    TYR A  56      118.10    -39.30                                   
REMARK 500    ILE A  63     -168.51   -165.25                                   
REMARK 500    LYS A  65      -67.64   -104.18                                   
REMARK 500    LYS A  66     -160.81   -105.48                                   
REMARK 500    ASP A  67       -2.94    -45.07                                   
REMARK 500    VAL A  75      116.03   -162.09                                   
REMARK 500    PHE A  77       33.04    -98.68                                   
REMARK 500    PHE A  87     -162.77   -107.85                                   
REMARK 500    VAL A  90      -65.96    -29.73                                   
REMARK 500    LEU A 100      171.39    -54.32                                   
REMARK 500    THR A 107      161.27    175.08                                   
REMARK 500    VAL A 111       46.40    -78.02                                   
REMARK 500    ALA A 114      -70.64    -24.08                                   
REMARK 500    SER A 134      -88.05    -70.01                                   
REMARK 500    ILE A 135     -140.54   -104.35                                   
REMARK 500    ASN A 137      -54.24   -139.18                                   
REMARK 500    GLU A 138       93.90    -61.23                                   
REMARK 500    SER A 156      -60.37    -21.40                                   
REMARK 500    GLU A 169      -75.74    -24.60                                   
REMARK 500    ASN A 175       70.30   -115.35                                   
REMARK 500    MET A 184     -141.02     56.92                                   
REMARK 500    ASP A 185       45.93    -94.31                                   
REMARK 500    ASP A 192       58.92   -100.45                                   
REMARK 500    ILE A 195      -62.40    -10.28                                   
REMARK 500    HIS A 221       63.61     63.57                                   
REMARK 500    PRO A 225      -35.17    -36.01                                   
REMARK 500    MET A 230       48.14     39.73                                   
REMARK 500    PRO A 236       -1.17    -48.28                                   
REMARK 500    ASP A 237      -13.75   -143.61                                   
REMARK 500    PRO A 243       95.46    -63.02                                   
REMARK 500    SER A 251       49.97    -73.16                                   
REMARK 500    ILE A 274      133.56    -22.54                                   
REMARK 500    VAL A 276       -1.30   -150.15                                   
REMARK 500    ARG A 284      -17.01    -38.22                                   
REMARK 500    LYS A 287      -35.90      5.76                                   
REMARK 500    PRO A 294       69.51    -60.07                                   
REMARK 500    LEU A 295      101.25    -53.14                                   
REMARK 500    PRO A 345      117.71    -35.24                                   
REMARK 500    ILE A 382      -71.93   -100.51                                   
REMARK 500    TYR A 405      151.95    -40.79                                   
REMARK 500    PRO A 412     -169.15    -65.73                                   
REMARK 500    PRO A 420      -87.05    -58.82                                   
REMARK 500    TRP A 426      -80.95    -71.98                                   
REMARK 500    GLN A 428      104.82   -168.65                                   
REMARK 500    LEU A 429      175.19    -51.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     116 RAMACHANDRAN OUTLIERS.                        
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 TBO A 559                 
DBREF  1UWB A    1   558  UNP    P03366   POL_HV1B1      599   1156             
DBREF  1UWB B    1   427  UNP    P03366   POL_HV1B1      599   1025             
SEQADV 1UWB CYS A  181  UNP  P03366    TYR   348 ENGINEERED MUTATION            
SEQADV 1UWB SER A  280  UNP  P03366    CYS   447 ENGINEERED MUTATION            
SEQADV 1UWB CYS B  181  UNP  P03366    TYR   348 ENGINEERED MUTATION            
SEQADV 1UWB SER B  280  UNP  P03366    CYS   447 ENGINEERED MUTATION            
SEQRES   1 A  558  PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS          
SEQRES   2 A  558  PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU          
SEQRES   3 A  558  THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR          
SEQRES   4 A  558  GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO          
SEQRES   5 A  558  GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS          
SEQRES   6 A  558  LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG          
SEQRES   7 A  558  GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN          
SEQRES   8 A  558  LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS          
SEQRES   9 A  558  SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER          
SEQRES  10 A  558  VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE          
SEQRES  11 A  558  THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG          
SEQRES  12 A  558  TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER          
SEQRES  13 A  558  PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU          
SEQRES  14 A  558  PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE CYS GLN          
SEQRES  15 A  558  TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE          
SEQRES  16 A  558  GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS          
SEQRES  17 A  558  LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS          
SEQRES  18 A  558  GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU          
SEQRES  19 A  558  HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO          
SEQRES  20 A  558  GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU          
SEQRES  21 A  558  VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY          
SEQRES  22 A  558  ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR          
SEQRES  23 A  558  LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA          
SEQRES  24 A  558  GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU          
SEQRES  25 A  558  PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU          
SEQRES  26 A  558  ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR          
SEQRES  27 A  558  TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR          
SEQRES  28 A  558  GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP          
SEQRES  29 A  558  VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR          
SEQRES  30 A  558  GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS          
SEQRES  31 A  558  LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR          
SEQRES  32 A  558  GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE          
SEQRES  33 A  558  VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR GLN LEU          
SEQRES  34 A  558  GLU LYS GLU PRO ILE VAL GLY ALA GLU THR PHE TYR VAL          
SEQRES  35 A  558  ASP GLY ALA ALA ASN ARG GLU THR LYS LEU GLY LYS ALA          
SEQRES  36 A  558  GLY TYR VAL THR ASN LYS GLY ARG GLN LYS VAL VAL PRO          
SEQRES  37 A  558  LEU THR ASN THR THR ASN GLN LYS THR GLU LEU GLN ALA          
SEQRES  38 A  558  ILE TYR LEU ALA LEU GLN ASP SER GLY LEU GLU VAL ASN          
SEQRES  39 A  558  ILE VAL THR ASP SER GLN TYR ALA LEU GLY ILE ILE GLN          
SEQRES  40 A  558  ALA GLN PRO ASP LYS SER GLU SER GLU LEU VAL ASN GLN          
SEQRES  41 A  558  ILE ILE GLU GLN LEU ILE LYS LYS GLU LYS VAL TYR LEU          
SEQRES  42 A  558  ALA TRP VAL PRO ALA HIS LYS GLY ILE GLY GLY ASN GLU          
SEQRES  43 A  558  GLN VAL ASP LYS LEU VAL SER ALA GLY ILE ARG LYS              
SEQRES   1 B  427  PRO ILE SER PRO ILE GLU THR VAL PRO VAL LYS LEU LYS          
SEQRES   2 B  427  PRO GLY MET ASP GLY PRO LYS VAL LYS GLN TRP PRO LEU          
SEQRES   3 B  427  THR GLU GLU LYS ILE LYS ALA LEU VAL GLU ILE CYS THR          
SEQRES   4 B  427  GLU MET GLU LYS GLU GLY LYS ILE SER LYS ILE GLY PRO          
SEQRES   5 B  427  GLU ASN PRO TYR ASN THR PRO VAL PHE ALA ILE LYS LYS          
SEQRES   6 B  427  LYS ASP SER THR LYS TRP ARG LYS LEU VAL ASP PHE ARG          
SEQRES   7 B  427  GLU LEU ASN LYS ARG THR GLN ASP PHE TRP GLU VAL GLN          
SEQRES   8 B  427  LEU GLY ILE PRO HIS PRO ALA GLY LEU LYS LYS LYS LYS          
SEQRES   9 B  427  SER VAL THR VAL LEU ASP VAL GLY ASP ALA TYR PHE SER          
SEQRES  10 B  427  VAL PRO LEU ASP GLU ASP PHE ARG LYS TYR THR ALA PHE          
SEQRES  11 B  427  THR ILE PRO SER ILE ASN ASN GLU THR PRO GLY ILE ARG          
SEQRES  12 B  427  TYR GLN TYR ASN VAL LEU PRO GLN GLY TRP LYS GLY SER          
SEQRES  13 B  427  PRO ALA ILE PHE GLN SER SER MET THR LYS ILE LEU GLU          
SEQRES  14 B  427  PRO PHE LYS LYS GLN ASN PRO ASP ILE VAL ILE CYS GLN          
SEQRES  15 B  427  TYR MET ASP ASP LEU TYR VAL GLY SER ASP LEU GLU ILE          
SEQRES  16 B  427  GLY GLN HIS ARG THR LYS ILE GLU GLU LEU ARG GLN HIS          
SEQRES  17 B  427  LEU LEU ARG TRP GLY LEU THR THR PRO ASP LYS LYS HIS          
SEQRES  18 B  427  GLN LYS GLU PRO PRO PHE LEU TRP MET GLY TYR GLU LEU          
SEQRES  19 B  427  HIS PRO ASP LYS TRP THR VAL GLN PRO ILE VAL LEU PRO          
SEQRES  20 B  427  GLU LYS ASP SER TRP THR VAL ASN ASP ILE GLN LYS LEU          
SEQRES  21 B  427  VAL GLY LYS LEU ASN TRP ALA SER GLN ILE TYR PRO GLY          
SEQRES  22 B  427  ILE LYS VAL ARG GLN LEU SER LYS LEU LEU ARG GLY THR          
SEQRES  23 B  427  LYS ALA LEU THR GLU VAL ILE PRO LEU THR GLU GLU ALA          
SEQRES  24 B  427  GLU LEU GLU LEU ALA GLU ASN ARG GLU ILE LEU LYS GLU          
SEQRES  25 B  427  PRO VAL HIS GLY VAL TYR TYR ASP PRO SER LYS ASP LEU          
SEQRES  26 B  427  ILE ALA GLU ILE GLN LYS GLN GLY GLN GLY GLN TRP THR          
SEQRES  27 B  427  TYR GLN ILE TYR GLN GLU PRO PHE LYS ASN LEU LYS THR          
SEQRES  28 B  427  GLY LYS TYR ALA ARG MET ARG GLY ALA HIS THR ASN ASP          
SEQRES  29 B  427  VAL LYS GLN LEU THR GLU ALA VAL GLN LYS ILE THR THR          
SEQRES  30 B  427  GLU SER ILE VAL ILE TRP GLY LYS THR PRO LYS PHE LYS          
SEQRES  31 B  427  LEU PRO ILE GLN LYS GLU THR TRP GLU THR TRP TRP THR          
SEQRES  32 B  427  GLU TYR TRP GLN ALA THR TRP ILE PRO GLU TRP GLU PHE          
SEQRES  33 B  427  VAL ASN THR PRO PRO LEU VAL LYS LEU TRP TYR                  
HET    TBO  A 559      21                                                       
HETNAM     TBO 5-CHLORO-8-METHYL-7-(3-METHYL-BUT-2-ENYL)-6,7,8,9-               
HETNAM   2 TBO  TETRAHYDRO-2H-2,7,9A-TRIAZA-BENZO[CD]AZULENE-1-THIONE           
HETSYN     TBO TBO 8; TIBO R86183                                               
FORMUL   3  TBO    C16 H20 CL N3 S                                              
HELIX    1  AA GLU A   28  GLU A   44  1                                  17    
HELIX    2  AB ARG A   78  ARG A   83  1                                   6    
HELIX    3  AC ALA A  114  SER A  117  1                                   4    
HELIX    4  AD GLU A  122  TYR A  127  1                                   6    
HELIX    5  AE LYS A  154  GLN A  174  1                                  21    
HELIX    6  AF ILE A  195  TRP A  212  1                                  18    
HELIX    7  AH VAL A  254  GLN A  269  1                                  16    
HELIX    8  AI ARG A  277  LEU A  283  1                                   7    
HELIX    9  AJ GLU A  297  LYS A  311  1                                  15    
HELIX   10  AK ASP A  364  TRP A  383  1                                  20    
HELIX   11  AL LYS A  395  GLU A  404  1                                  10    
HELIX   12  A' ASN A  474  ASP A  488  1                                  15    
HELIX   13  B' GLN A  500  ALA A  508  1                                   9    
HELIX   14  D' GLU A  516  LYS A  527  1                                  12    
HELIX   15  E' GLY A  544  ALA A  554  1                                  11    
HELIX   16  BA GLU B   28  GLU B   44  1                                  17    
HELIX   17  BB ARG B   78  VAL B   90  1                                  13    
HELIX   18  BC GLY B  112  SER B  117  1                                   6    
HELIX   19  BD GLU B  122  THR B  128  1                                   7    
HELIX   20  BE LYS B  154  GLN B  174  1                                  21    
HELIX   21  BF ILE B  195  TRP B  212  1                                  18    
HELIX   22  BH VAL B  254  ILE B  270  1                                  17    
HELIX   23  BI ARG B  277  LEU B  283  1                                   7    
HELIX   24  BJ GLU B  297  LYS B  311  1                                  15    
HELIX   25  BK ASP B  364  TRP B  383  1                                  20    
HELIX   26  BL LYS B  395  TYR B  405  1                                  11    
SHEET    1  S1 3 ILE A  47  ILE A  50  0                                        
SHEET    2  S1 3 ILE A 142  TYR A 146 -1                                        
SHEET    3  S1 3 THR A 128  ILE A 132 -1                                        
SHEET    1  S2 2 ASN A  57  LYS A  64  0                                        
SHEET    2  S2 2 ARG A  72  PHE A  77 -1                                        
SHEET    1  S3 3 SER A 105  VAL A 111  0                                        
SHEET    2  S3 3 ASP A 186  SER A 191 -1                                        
SHEET    3  S3 3 ILE A 178  TYR A 183 -1                                        
SHEET    1  S4 4 PHE A 227  TRP A 229  0                                        
SHEET    2  S4 4 TYR A 232  HIS A 235 -1                                        
SHEET    3  S4 4 LYS A 238  VAL A 241 -1                                        
SHEET    4  S4 4 VAL A 314  ASP A 320 -1                                        
SHEET    1  S5 5 LYS A 347  ARG A 356  0                                        
SHEET    2  S5 5 GLN A 336  TYR A 342 -1                                        
SHEET    3  S5 5 LEU A 325  GLN A 332 -1                                        
SHEET    4  S5 5 PRO A 387  LEU A 391  1                                        
SHEET    5  S5 5 GLU A 413  THR A 419  1                                        
SHEET    1  S6 5 GLY A 462  THR A 470  0                                        
SHEET    2  S6 5 LEU A 452  THR A 459 -1                                        
SHEET    3  S6 5 GLU A 438  ASN A 447 -1                                        
SHEET    4  S6 5 GLU A 492  THR A 497  1                                        
SHEET    5  S6 5 LYS A 530  VAL A 536  1                                        
SHEET    1  S7 3 ILE B  47  GLY B  51  0                                        
SHEET    2  S7 3 ILE B 142  TYR B 146 -1                                        
SHEET    3  S7 3 ALA B 129  ILE B 132 -1                                        
SHEET    1  S8 2 TYR B  56  LYS B  64  0                                        
SHEET    2  S8 2 TRP B  71  ASP B  76 -1                                        
SHEET    1  S9 3 SER B 105  ASP B 110  0                                        
SHEET    2  S9 3 ASP B 186  SER B 191 -1                                        
SHEET    3  S9 3 ILE B 178  TYR B 183 -1                                        
SHEET    1 S10 5 LYS B 347  ARG B 356  0                                        
SHEET    2 S10 5 GLN B 336  TYR B 342 -1                                        
SHEET    3 S10 5 LEU B 325  LYS B 331 -1                                        
SHEET    4 S10 5 PRO B 387  LEU B 391  1                                        
SHEET    5 S10 5 GLU B 413  VAL B 417  1                                        
SITE     1 AC1  6 LEU A 100  LYS A 101  LYS A 103  TYR A 188                    
SITE     2 AC1  6 TRP A 229  TYR A 318                                          
CRYST1  225.700   69.200  104.900  90.00 106.60  90.00 C 1 2 1       4          
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      0.004431  0.000000  0.001321        0.00000                         
SCALE2      0.000000  0.014451  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009947        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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