GenomeNet

Database: PDB
Entry: 2HIV
LinkDB: 2HIV
Original site: 2HIV 
HEADER    LIGASE                                  29-JUN-06   2HIV              
TITLE     ATP-DEPENDENT DNA LIGASE FROM S. SOLFATARICUS                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOSTABLE DNA LIGASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: POLYDEOXYRIBONUCLEOTIDE SYNTHASE;                           
COMPND   5 EC: 6.5.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;                        
SOURCE   3 ORGANISM_TAXID: 2287;                                                
SOURCE   4 GENE: LIG;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    DNA LIGASE, ATP-DEPENDENT, OPEN CONFORMATION, LIGASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.PASCAL,T.ELLENBERGER                                              
REVDAT   3   13-JUL-11 2HIV    1       VERSN                                    
REVDAT   2   24-FEB-09 2HIV    1       VERSN                                    
REVDAT   1   07-NOV-06 2HIV    0                                                
JRNL        AUTH   J.M.PASCAL,O.V.TSODIKOV,G.L.HURA,W.SONG,E.A.COTNER,          
JRNL        AUTH 2 S.CLASSEN,A.E.TOMKINSON,J.A.TAINER,T.ELLENBERGER             
JRNL        TITL   A FLEXIBLE INTERFACE BETWEEN DNA LIGASE AND PCNA SUPPORTS    
JRNL        TITL 2 CONFORMATIONAL SWITCHING AND EFFICIENT LIGATION OF DNA.      
JRNL        REF    MOL.CELL                      V.  24   279 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   17052461                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.08.015                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 48093                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2422                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2167                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 116                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4566                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.67000                                              
REMARK   3    B22 (A**2) : -1.47000                                             
REMARK   3    B33 (A**2) : 0.80000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.189         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.124         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.826         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4696 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6334 ; 1.493 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   587 ; 5.788 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   208 ;35.186 ;24.279       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   900 ;17.715 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    32 ;20.428 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   709 ; 0.114 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3470 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2549 ; 0.222 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3283 ; 0.315 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   344 ; 0.222 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   106 ; 0.262 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.295 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2950 ; 0.873 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4658 ; 1.459 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1956 ; 2.335 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1670 ; 3.610 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3816  19.0437  48.4902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0323 T22:  -0.0762                                     
REMARK   3      T33:  -0.0696 T12:  -0.0321                                     
REMARK   3      T13:  -0.0381 T23:  -0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8843 L22:   3.0174                                     
REMARK   3      L33:   2.9237 L12:   0.4426                                     
REMARK   3      L13:  -0.2544 L23:  -0.6564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1018 S12:  -0.2375 S13:  -0.1479                       
REMARK   3      S21:   0.5684 S22:  -0.0388 S23:  -0.0772                       
REMARK   3      S31:   0.2872 S32:   0.1526 S33:  -0.0629                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   231        A   440                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5470  23.5396  15.1577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2261 T22:  -0.1727                                     
REMARK   3      T33:  -0.1931 T12:  -0.0246                                     
REMARK   3      T13:   0.0029 T23:  -0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7558 L22:   3.8809                                     
REMARK   3      L33:   2.4066 L12:   0.2639                                     
REMARK   3      L13:   0.4045 L23:  -1.2926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0646 S12:   0.1436 S13:  -0.1050                       
REMARK   3      S21:  -0.1850 S22:   0.1344 S23:   0.3133                       
REMARK   3      S31:   0.1135 S32:  -0.0492 S33:  -0.1991                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   441        A   590                          
REMARK   3    ORIGIN FOR THE GROUP (A): -10.0316  38.3510  -2.2205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2004 T22:   0.0209                                     
REMARK   3      T33:  -0.1232 T12:  -0.0779                                     
REMARK   3      T13:   0.0465 T23:   0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7494 L22:   3.7437                                     
REMARK   3      L33:   4.9690 L12:  -0.1909                                     
REMARK   3      L13:   0.2821 L23:   0.5311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:   0.2478 S13:   0.1562                       
REMARK   3      S21:   0.0834 S22:  -0.0508 S23:  -0.3419                       
REMARK   3      S31:  -0.2851 S32:   0.6755 S33:   0.0546                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2HIV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038391.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.12                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48112                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 10.100                             
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6-8% PEG 3350, 100MM SODIUM ACETATE PH   
REMARK 280  4.5, 20-80MM SODIUM/POTASSIUM TARTRATE, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       38.65500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.65500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       59.60300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.88500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       59.60300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.88500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.65500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       59.60300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       84.88500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       38.65500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       59.60300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       84.88500            
REMARK 290   SMTRY3   8  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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     GLN A   103                                                      
REMARK 465     SER A   104                                                      
REMARK 465     THR A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     ILE A   107                                                      
REMARK 465     LEU A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     PHE A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     THR A   113                                                      
REMARK 465     THR A   114                                                      
REMARK 465     SER A   115                                                      
REMARK 465     LYS A   591                                                      
REMARK 465     ILE A   592                                                      
REMARK 465     GLU A   593                                                      
REMARK 465     SER A   594                                                      
REMARK 465     PRO A   595                                                      
REMARK 465     ALA A   596                                                      
REMARK 465     VAL A   597                                                      
REMARK 465     ASP A   598                                                      
REMARK 465     GLU A   599                                                      
REMARK 465     SER A   600                                                      
REMARK 465     VAL A   601                                                      
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     LYS A 116    CG   CD   CE   NZ                                   
REMARK 470     ARG A 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 437    CG   OD1  OD2                                       
REMARK 470     TYR A 438    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER A 440    OG                                                  
REMARK 470     GLU A 441    CG   CD   OE1  OE2                                  
REMARK 470     MET A 442    CG   SD   CE                                        
REMARK 470     LYS A 590    CG   CD   CE   NZ                                   
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   O    LEU A   170     O    HOH A   777              2.00            
REMARK 500   NE   ARG A   265     OE1  GLU A   308              2.15            
REMARK 500   OH   TYR A    43     O    HOH A   619              2.16            
REMARK 500   O    GLU A   137     O    HOH A   813              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A   506     O    HOH A   811     3555     1.79            
REMARK 500   OG   SER A    18     OD2  ASP A   419     6555     2.08            
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    GLU A 308   CB    GLU A 308   CG     -0.167                       
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    VAL A 345   CG1 -  CB  -  CG2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    LEU A 352   CA  -  CB  -  CG  ANGL. DEV. =  18.1 DEGREES          
REMARK 500    ARG A 369   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A 369   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 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    ARG A 171       71.55   -102.14                                   
REMARK 500    GLU A 239     -179.27    -68.30                                   
REMARK 500    GLU A 272      -71.28     37.75                                   
REMARK 500    PHE A 350       -8.33   -140.21                                   
REMARK 500    ALA A 385      134.06    -38.70                                   
REMARK 500    ARG A 436      -25.43    -38.93                                   
REMARK 500    ASP A 437        8.87    -58.81                                   
REMARK 500    SER A 440      -47.32   -130.41                                   
REMARK 500    GLU A 441      -87.57    -72.65                                   
REMARK 500    MET A 442       84.33    -68.05                                   
REMARK 500    SER A 465       18.15   -143.50                                   
REMARK 500    VAL A 526      -48.31   -132.71                                   
REMARK 500    ASP A 547       -4.29     70.57                                   
REMARK 500    LYS A 589       31.95    -80.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2HII   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HIK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2HIX   RELATED DB: PDB                                   
DBREF  2HIV A    1   601  UNP    Q980T8   DNLI_SULSO       1    601             
SEQADV 2HIV MET A  -19  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV GLY A  -18  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV SER A  -17  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV SER A  -16  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV HIS A  -15  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV HIS A  -14  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV HIS A  -13  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV HIS A  -12  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV HIS A  -11  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV HIS A  -10  UNP  Q980T8              EXPRESSION TAG                 
SEQADV 2HIV SER A   -9  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV SER A   -8  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV GLY A   -7  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV LEU A   -6  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV VAL A   -5  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV PRO A   -4  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV ARG A   -3  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV GLY A   -2  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV SER A   -1  UNP  Q980T8              CLONING ARTIFACT               
SEQADV 2HIV HIS A    0  UNP  Q980T8              CLONING ARTIFACT               
SEQRES   1 A  621  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  621  LEU VAL PRO ARG GLY SER HIS MET GLU PHE LYS VAL ILE          
SEQRES   3 A  621  ALA GLU TYR PHE ASP LYS LEU GLU LYS ILE SER SER ARG          
SEQRES   4 A  621  LEU GLN LEU THR ALA LEU LEU ALA ASP LEU LEU SER LYS          
SEQRES   5 A  621  SER ASP LYS THR ILE ILE ASP LYS VAL VAL TYR ILE ILE          
SEQRES   6 A  621  GLN GLY LYS LEU TRP PRO ASP PHE LEU GLY TYR PRO GLU          
SEQRES   7 A  621  LEU GLY ILE GLY GLU LYS PHE LEU ILE LYS ALA ILE SER          
SEQRES   8 A  621  ILE ALA THR ASN THR ASP GLU ASN SER VAL GLU ASN LEU          
SEQRES   9 A  621  TYR LYS THR ILE GLY ASP LEU GLY GLU VAL ALA ARG ARG          
SEQRES  10 A  621  LEU LYS SER LYS GLN GLN SER THR GLY ILE LEU GLY PHE          
SEQRES  11 A  621  LEU GLY THR THR SER LYS GLU SER LEU THR VAL ASP GLU          
SEQRES  12 A  621  VAL TYR SER THR LEU SER LYS VAL ALA LEU THR THR GLY          
SEQRES  13 A  621  GLU GLY SER ARG ASP LEU LYS ILE ARG LEU LEU ALA GLY          
SEQRES  14 A  621  LEU LEU LYS LYS ALA ASP PRO LEU GLU ALA LYS PHE LEU          
SEQRES  15 A  621  VAL ARG PHE VAL GLU GLY ARG LEU ARG VAL GLY ILE GLY          
SEQRES  16 A  621  ASP ALA THR VAL LEU ASP ALA MET ALA ILE ALA PHE GLY          
SEQRES  17 A  621  GLY GLY GLN SER ALA SER GLU ILE ILE GLU ARG ALA TYR          
SEQRES  18 A  621  ASN LEU ARG ALA ASP LEU GLY ASN ILE ALA LYS ILE ILE          
SEQRES  19 A  621  VAL GLU LYS GLY ILE GLU ALA LEU LYS THR LEU LYS PRO          
SEQRES  20 A  621  GLN VAL GLY ILE PRO ILE ARG PRO MET LEU ALA GLU ARG          
SEQRES  21 A  621  LEU SER ASN PRO GLU GLU ILE LEU LYS LYS MET GLY GLY          
SEQRES  22 A  621  ASN ALA ILE VAL ASP TYR LYS TYR ASP GLY GLU ARG ALA          
SEQRES  23 A  621  GLN ILE HIS LYS LYS GLU ASP LYS ILE PHE ILE PHE SER          
SEQRES  24 A  621  ARG ARG LEU GLU ASN ILE THR SER GLN TYR PRO ASP VAL          
SEQRES  25 A  621  VAL ASP TYR VAL SER LYS TYR ILE GLU GLY LYS GLU PHE          
SEQRES  26 A  621  ILE ILE GLU GLY GLU ILE VAL ALA ILE ASP PRO GLU SER          
SEQRES  27 A  621  GLY GLU MET ARG PRO PHE GLN GLU LEU MET HIS ARG LYS          
SEQRES  28 A  621  ARG LYS SER ASP ILE TYR GLU ALA ILE LYS GLU TYR PRO          
SEQRES  29 A  621  VAL ASN VAL PHE LEU PHE ASP LEU MET TYR TYR GLU ASP          
SEQRES  30 A  621  VAL ASP TYR THR THR LYS PRO LEU GLU ALA ARG ARG LYS          
SEQRES  31 A  621  LEU LEU GLU SER ILE VAL LYS PRO ASN ASP TYR VAL LYS          
SEQRES  32 A  621  ILE ALA HIS HIS ILE GLN ALA ASN ASN VAL GLU ASP LEU          
SEQRES  33 A  621  LYS SER PHE PHE TYR ARG ALA ILE SER GLU GLY GLY GLU          
SEQRES  34 A  621  GLY VAL MET VAL LYS ALA ILE GLY LYS ASP ALA ILE TYR          
SEQRES  35 A  621  GLN ALA GLY ALA ARG GLY TRP LEU TRP ILE LYS LEU LYS          
SEQRES  36 A  621  ARG ASP TYR GLN SER GLU MET ALA ASP THR VAL ASP LEU          
SEQRES  37 A  621  VAL VAL VAL GLY GLY PHE TYR GLY LYS GLY LYS ARG GLY          
SEQRES  38 A  621  GLY LYS ILE SER SER LEU LEU MET ALA ALA TYR ASN PRO          
SEQRES  39 A  621  LYS THR ASP SER PHE GLU SER VAL CYS LYS VAL ALA SER          
SEQRES  40 A  621  GLY PHE SER ASP GLU GLN LEU ASP GLU LEU GLN LYS LYS          
SEQRES  41 A  621  LEU MET GLU ILE LYS ARG ASP VAL LYS HIS PRO ARG VAL          
SEQRES  42 A  621  ASN SER LYS MET GLU PRO ASP ILE TRP VAL GLU PRO VAL          
SEQRES  43 A  621  TYR VAL ALA GLU ILE ILE GLY SER GLU ILE THR ILE SER          
SEQRES  44 A  621  PRO LEU HIS THR CYS CYS GLN ASP VAL VAL GLU LYS ASP          
SEQRES  45 A  621  ALA GLY LEU SER ILE ARG PHE PRO ARG PHE ILE ARG TRP          
SEQRES  46 A  621  ARG ASP ASP LYS SER PRO GLU ASP ALA THR THR THR ASP          
SEQRES  47 A  621  GLU ILE LEU GLU MET TYR ASN LYS GLN PRO LYS LYS LYS          
SEQRES  48 A  621  ILE GLU SER PRO ALA VAL ASP GLU SER VAL                      
FORMUL   2  HOH   *225(H2 O)                                                    
HELIX    1   1 PHE A    3  ILE A   16  1                                  14    
HELIX    2   2 SER A   18  LYS A   32  1                                  15    
HELIX    3   3 ASP A   34  THR A   36  5                                   3    
HELIX    4   4 ILE A   37  ILE A   45  1                                   9    
HELIX    5   5 PRO A   51  GLY A   55  5                                   5    
HELIX    6   6 GLY A   62  ASN A   75  1                                  14    
HELIX    7   7 ASP A   77  GLY A   89  1                                  13    
HELIX    8   8 ASP A   90  LYS A  101  1                                  12    
HELIX    9   9 THR A  120  THR A  134  1                                  15    
HELIX   10  10 GLY A  138  ALA A  154  1                                  17    
HELIX   11  11 ASP A  155  GLU A  167  1                                  13    
HELIX   12  12 GLY A  175  GLY A  188  1                                  14    
HELIX   13  13 GLY A  190  SER A  192  5                                   3    
HELIX   14  14 ALA A  193  ARG A  204  1                                  12    
HELIX   15  15 ASP A  206  GLY A  218  1                                  13    
HELIX   16  16 ILE A  219  LYS A  223  5                                   5    
HELIX   17  17 ASN A  243  MET A  251  1                                   9    
HELIX   18  18 ILE A  285  GLN A  288  5                                   4    
HELIX   19  19 TYR A  289  ILE A  300  1                                  12    
HELIX   20  20 PHE A  324  LYS A  333  1                                  10    
HELIX   21  21 ASP A  335  TYR A  343  1                                   9    
HELIX   22  22 PRO A  364  VAL A  376  1                                  13    
HELIX   23  23 ASN A  392  GLU A  406  1                                  15    
HELIX   24  24 LYS A  457  GLY A  461  5                                   5    
HELIX   25  25 SER A  490  GLU A  503  1                                  14    
HELIX   26  26 SER A  570  ALA A  574  5                                   5    
HELIX   27  27 THR A  576  GLN A  587  1                                  12    
SHEET    1   A 5 LEU A 237  ARG A 240  0                                        
SHEET    2   A 5 ARG A 427  LYS A 435  1  O  LYS A 433   N  GLU A 239           
SHEET    3   A 5 GLY A 410  LYS A 414 -1  N  VAL A 413   O  ILE A 432           
SHEET    4   A 5 ALA A 255  LYS A 260 -1  N  ILE A 256   O  LYS A 414           
SHEET    5   A 5 HIS A 387  ALA A 390 -1  O  ILE A 388   N  VAL A 257           
SHEET    1   B 5 LYS A 274  PHE A 278  0                                        
SHEET    2   B 5 GLU A 264  LYS A 271 -1  N  HIS A 269   O  PHE A 276           
SHEET    3   B 5 PHE A 305  ALA A 313 -1  O  GLY A 309   N  ALA A 266           
SHEET    4   B 5 VAL A 345  TYR A 355 -1  O  PHE A 348   N  GLU A 310           
SHEET    5   B 5 VAL A 358  ASP A 359 -1  O  VAL A 358   N  TYR A 355           
SHEET    1   C 5 LYS A 274  PHE A 278  0                                        
SHEET    2   C 5 GLU A 264  LYS A 271 -1  N  HIS A 269   O  PHE A 276           
SHEET    3   C 5 PHE A 305  ALA A 313 -1  O  GLY A 309   N  ALA A 266           
SHEET    4   C 5 VAL A 345  TYR A 355 -1  O  PHE A 348   N  GLU A 310           
SHEET    5   C 5 VAL A 382  ILE A 384  1  O  LYS A 383   N  LEU A 349           
SHEET    1   D 6 LYS A 505  ARG A 506  0                                        
SHEET    2   D 6 ILE A 521  VAL A 523 -1  O  TRP A 522   N  ARG A 506           
SHEET    3   D 6 ASP A 444  TYR A 455 -1  N  GLY A 453   O  ILE A 521           
SHEET    4   D 6 ILE A 464  ASN A 473 -1  O  ALA A 470   N  VAL A 449           
SHEET    5   D 6 SER A 478  VAL A 485 -1  O  SER A 478   N  ASN A 473           
SHEET    6   D 6 VAL A 513  ASN A 514  1  O  ASN A 514   N  PHE A 479           
SHEET    1   E 5 LYS A 505  ARG A 506  0                                        
SHEET    2   E 5 ILE A 521  VAL A 523 -1  O  TRP A 522   N  ARG A 506           
SHEET    3   E 5 ASP A 444  TYR A 455 -1  N  GLY A 453   O  ILE A 521           
SHEET    4   E 5 VAL A 528  GLY A 533 -1  O  ILE A 531   N  VAL A 446           
SHEET    5   E 5 ARG A 561  TRP A 565 -1  O  ILE A 563   N  GLU A 530           
SHEET    1   F 2 GLU A 535  SER A 539  0                                        
SHEET    2   F 2 GLY A 554  ARG A 558 -1  O  GLY A 554   N  SER A 539           
CRYST1  119.206  169.770   77.310  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008389  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005890  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012935        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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