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Database: PDB
Entry: 1SUW
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HEADER    TRANSFERASE                             26-MAR-04   1SUW              
TITLE     CRYSTAL STRUCTURE OF A NAD KINASE FROM ARCHAEOGLOBUS FULGIDUS IN      
TITLE    2 COMPLEX WITH ITS SUBSTRATE AND PRODUCT: INSIGHTS INTO THE CATALYSIS  
TITLE    3 OF NAD KINASE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE INORGANIC POLYPHOSPHATE/ATP-NAD KINASE;           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: POLY(P)/ATP NAD KINASE;                                     
COMPND   5 EC: 2.7.1.23;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;                         
SOURCE   3 ORGANISM_TAXID: 2234;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PSJS1244 STAR;                   
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PB4                                       
KEYWDS    ATP-NAD KINASE, NADK, NAD, NADP, STRUCTURAL GENOMICS, BSGC STRUCTURE  
KEYWDS   2 FUNDED BY NIH, PROTEIN STRUCTURE INITIATIVE, PSI, BERKELEY           
KEYWDS   3 STRUCTURAL GENOMICS CENTER, TRANSFERASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LIU,Y.LOU,H.YOKOTA,P.D.ADAMS,R.KIM,S.-H.KIM,BERKELEY STRUCTURAL     
AUTHOR   2 GENOMICS CENTER (BSGC)                                               
REVDAT   7   14-FEB-24 1SUW    1       REMARK                                   
REVDAT   6   11-OCT-17 1SUW    1       REMARK                                   
REVDAT   5   24-FEB-09 1SUW    1       VERSN                                    
REVDAT   4   07-MAR-06 1SUW    1       JRNL                                     
REVDAT   3   25-JAN-05 1SUW    1       AUTHOR KEYWDS REMARK                     
REVDAT   2   11-JAN-05 1SUW    1       AUTHOR JRNL   TITLE                      
REVDAT   1   24-AUG-04 1SUW    0                                                
JRNL        AUTH   J.LIU,Y.LOU,H.YOKOTA,P.D.ADAMS,R.KIM,S.-H.KIM                
JRNL        TITL   CRYSTAL STRUCTURES OF AN NAD KINASE FROM ARCHAEOGLOBUS       
JRNL        TITL 2 FULGIDUS IN COMPLEX WITH ATP, NAD, OR NADP                   
JRNL        REF    J.MOL.BIOL.                   V. 354   289 2005              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16242716                                                     
JRNL        DOI    10.1016/J.JMB.2005.09.026                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 46127                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : 5%                              
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2342                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7856                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 192                                     
REMARK   3   SOLVENT ATOMS            : 303                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.38000                                             
REMARK   3    B22 (A**2) : -4.38000                                             
REMARK   3    B33 (A**2) : 8.76000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SUW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022010.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796, 0.9798, 0.9600             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62750                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, 2M NACL, 10% PEG 6000, PH    
REMARK 280  7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.29750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       61.07050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       61.07050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       49.64875            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       61.07050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       61.07050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      148.94625            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       61.07050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       61.07050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       49.64875            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       61.07050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.07050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      148.94625            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       99.29750            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15160 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 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    GLY C  71   N   -  CA  -  C   ANGL. DEV. =  29.2 DEGREES          
REMARK 500    ARG C  72   N   -  CA  -  CB  ANGL. DEV. = -18.0 DEGREES          
REMARK 500    PRO C 109   C   -  N   -  CA  ANGL. DEV. =   9.6 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  22        3.67    -61.40                                   
REMARK 500    LYS A  60      -64.72    -91.80                                   
REMARK 500    ASN A  83       34.08   -145.80                                   
REMARK 500    PRO A 109      -37.53    -39.69                                   
REMARK 500    ASP A 209       26.51     44.09                                   
REMARK 500    ASP B  10        4.74    -68.81                                   
REMARK 500    ASN B  39       35.22    -90.42                                   
REMARK 500    LYS B  60      -70.28    -88.28                                   
REMARK 500    ASN B  83       19.22   -150.44                                   
REMARK 500    GLU B  85      -70.49    -53.87                                   
REMARK 500    ASP B 140      147.46   -171.67                                   
REMARK 500    ASP B 209       24.93     47.95                                   
REMARK 500    GLU C  18        0.80    -63.77                                   
REMARK 500    LYS C  60      -68.00    -97.65                                   
REMARK 500    ARG C  72      -80.85   -117.87                                   
REMARK 500    ASN C  83       28.97   -163.11                                   
REMARK 500    ASP C 209       22.66     44.62                                   
REMARK 500    VAL C 214      138.12   -179.02                                   
REMARK 500    ASN D  39       35.38    -87.46                                   
REMARK 500    ARG D  72      -72.15    -88.19                                   
REMARK 500    ASN D  83       15.25   -146.02                                   
REMARK 500    ALA D 125       16.23     58.46                                   
REMARK 500    ASP D 140      155.94    172.74                                   
REMARK 500    GLN D 211      -73.85    -99.02                                   
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 NAP A 3075                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 3076                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 3077                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 3078                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: BSGCAIR30424   RELATED DB: TARGETDB                      
DBREF  1SUW A    1   249  UNP    O30297   PPNK_ARCFU       1    249             
DBREF  1SUW B    1   249  UNP    O30297   PPNK_ARCFU       1    249             
DBREF  1SUW C    1   249  UNP    O30297   PPNK_ARCFU       1    249             
DBREF  1SUW D    1   249  UNP    O30297   PPNK_ARCFU       1    249             
SEQRES   1 A  249  MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL          
SEQRES   2 A  249  LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU          
SEQRES   3 A  249  VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN          
SEQRES   4 A  249  PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE          
SEQRES   5 A  249  LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE          
SEQRES   6 A  249  PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS          
SEQRES   7 A  249  ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA          
SEQRES   8 A  249  VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER          
SEQRES   9 A  249  CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE          
SEQRES  10 A  249  ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL          
SEQRES  11 A  249  ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG          
SEQRES  12 A  249  CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR          
SEQRES  13 A  249  GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO          
SEQRES  14 A  249  TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE          
SEQRES  15 A  249  ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG          
SEQRES  16 A  249  LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA          
SEQRES  17 A  249  ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR          
SEQRES  18 A  249  ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN          
SEQRES  19 A  249  GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER          
SEQRES  20 A  249  ILE GLY                                                      
SEQRES   1 B  249  MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL          
SEQRES   2 B  249  LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU          
SEQRES   3 B  249  VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN          
SEQRES   4 B  249  PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE          
SEQRES   5 B  249  LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE          
SEQRES   6 B  249  PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS          
SEQRES   7 B  249  ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA          
SEQRES   8 B  249  VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER          
SEQRES   9 B  249  CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE          
SEQRES  10 B  249  ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL          
SEQRES  11 B  249  ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG          
SEQRES  12 B  249  CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR          
SEQRES  13 B  249  GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO          
SEQRES  14 B  249  TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE          
SEQRES  15 B  249  ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG          
SEQRES  16 B  249  LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA          
SEQRES  17 B  249  ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR          
SEQRES  18 B  249  ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN          
SEQRES  19 B  249  GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER          
SEQRES  20 B  249  ILE GLY                                                      
SEQRES   1 C  249  MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL          
SEQRES   2 C  249  LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU          
SEQRES   3 C  249  VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN          
SEQRES   4 C  249  PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE          
SEQRES   5 C  249  LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE          
SEQRES   6 C  249  PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS          
SEQRES   7 C  249  ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA          
SEQRES   8 C  249  VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER          
SEQRES   9 C  249  CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE          
SEQRES  10 C  249  ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL          
SEQRES  11 C  249  ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG          
SEQRES  12 C  249  CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR          
SEQRES  13 C  249  GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO          
SEQRES  14 C  249  TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE          
SEQRES  15 C  249  ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG          
SEQRES  16 C  249  LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA          
SEQRES  17 C  249  ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR          
SEQRES  18 C  249  ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN          
SEQRES  19 C  249  GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER          
SEQRES  20 C  249  ILE GLY                                                      
SEQRES   1 D  249  MET ARG ALA ALA VAL VAL TYR LYS THR ASP GLY HIS VAL          
SEQRES   2 D  249  LYS ARG ILE GLU GLU ALA LEU LYS ARG LEU GLU VAL GLU          
SEQRES   3 D  249  VAL GLU LEU PHE ASN GLN PRO SER GLU GLU LEU GLU ASN          
SEQRES   4 D  249  PHE ASP PHE ILE VAL SER VAL GLY GLY ASP GLY THR ILE          
SEQRES   5 D  249  LEU ARG ILE LEU GLN LYS LEU LYS ARG CYS PRO PRO ILE          
SEQRES   6 D  249  PHE GLY ILE ASN THR GLY ARG VAL GLY LEU LEU THR HIS          
SEQRES   7 D  249  ALA SER PRO GLU ASN PHE GLU VAL GLU LEU LYS LYS ALA          
SEQRES   8 D  249  VAL GLU LYS PHE GLU VAL GLU ARG PHE PRO ARG VAL SER          
SEQRES   9 D  249  CYS SER ALA MET PRO ASP VAL LEU ALA LEU ASN GLU ILE          
SEQRES  10 D  249  ALA VAL LEU SER ARG LYS PRO ALA LYS MET ILE ASP VAL          
SEQRES  11 D  249  ALA LEU ARG VAL ASP GLY VAL GLU VAL ASP ARG ILE ARG          
SEQRES  12 D  249  CYS ASP GLY PHE ILE VAL ALA THR GLN ILE GLY SER THR          
SEQRES  13 D  249  GLY TYR ALA PHE SER ALA GLY GLY PRO VAL VAL GLU PRO          
SEQRES  14 D  249  TYR LEU GLU CYS PHE ILE LEU ILE PRO ILE ALA PRO PHE          
SEQRES  15 D  249  ARG PHE GLY TRP LYS PRO TYR VAL VAL SER MET GLU ARG          
SEQRES  16 D  249  LYS ILE GLU VAL ILE ALA GLU LYS ALA ILE VAL VAL ALA          
SEQRES  17 D  249  ASP GLY GLN LYS SER VAL ASP PHE ASP GLY GLU ILE THR          
SEQRES  18 D  249  ILE GLU LYS SER GLU PHE PRO ALA VAL PHE PHE LYS ASN          
SEQRES  19 D  249  GLU LYS ARG PHE ARG ASN LEU PHE GLY LYS VAL ARG SER          
SEQRES  20 D  249  ILE GLY                                                      
HET    NAP  A3075      48                                                       
HET    NAP  B3076      48                                                       
HET    NAP  C3077      48                                                       
HET    NAP  D3078      48                                                       
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   5  NAP    4(C21 H28 N7 O17 P3)                                         
FORMUL   9  HOH   *303(H2 O)                                                    
HELIX    1   1 HIS A   12  ARG A   22  1                                  11    
HELIX    2   2 SER A   34  PHE A   40  5                                   7    
HELIX    3   3 GLY A   48  GLN A   57  1                                  10    
HELIX    4   4 SER A   80  GLU A   82  5                                   3    
HELIX    5   5 ASN A   83  PHE A   95  1                                  13    
HELIX    6   6 ILE A  153  THR A  156  5                                   4    
HELIX    7   7 GLY A  157  ALA A  162  1                                   6    
HELIX    8   8 LYS A  236  ARG A  246  1                                  11    
HELIX    9   9 HIS B   12  LEU B   23  1                                  12    
HELIX   10  10 SER B   34  PHE B   40  5                                   7    
HELIX   11  11 GLY B   48  GLN B   57  1                                  10    
HELIX   12  12 ASN B   83  PHE B   95  1                                  13    
HELIX   13  13 ILE B  153  THR B  156  5                                   4    
HELIX   14  14 GLY B  157  ALA B  162  1                                   6    
HELIX   15  15 LYS B  236  SER B  247  1                                  12    
HELIX   16  16 HIS C   12  LYS C   21  1                                  10    
HELIX   17  17 SER C   34  PHE C   40  5                                   7    
HELIX   18  18 GLY C   48  GLN C   57  1                                  10    
HELIX   19  19 ASN C   83  PHE C   95  1                                  13    
HELIX   20  20 ILE C  153  THR C  156  5                                   4    
HELIX   21  21 GLY C  157  ALA C  162  1                                   6    
HELIX   22  22 LYS C  236  SER C  247  1                                  12    
HELIX   23  23 HIS D   12  LEU D   23  1                                  12    
HELIX   24  24 SER D   34  PHE D   40  5                                   7    
HELIX   25  25 GLY D   48  GLN D   57  1                                  10    
HELIX   26  26 ASN D   83  PHE D   95  1                                  13    
HELIX   27  27 ILE D  153  THR D  156  5                                   4    
HELIX   28  28 GLY D  157  ALA D  162  1                                   6    
HELIX   29  29 LYS D  236  SER D  247  1                                  12    
SHEET    1   A 4 GLU A  26  PHE A  30  0                                        
SHEET    2   A 4 ARG A   2  TYR A   7  1  N  ALA A   3   O  GLU A  26           
SHEET    3   A 4 PHE A  42  GLY A  47  1  O  VAL A  44   N  ALA A   4           
SHEET    4   A 4 ILE A  65  ASN A  69  1  O  PHE A  66   N  SER A  45           
SHEET    1   B 2 VAL A  97  PHE A 100  0                                        
SHEET    2   B 2 ALA A 229  PHE A 232 -1  O  ALA A 229   N  PHE A 100           
SHEET    1   C 5 VAL A 103  CYS A 105  0                                        
SHEET    2   C 5 LYS A 212  LYS A 224 -1  O  GLU A 223   N  SER A 104           
SHEET    3   C 5 ILE A 197  ALA A 208 -1  N  ILE A 197   O  ILE A 222           
SHEET    4   C 5 ILE A 128  VAL A 134 -1  N  ARG A 133   O  GLU A 198           
SHEET    5   C 5 VAL A 137  CYS A 144 -1  O  ASP A 140   N  LEU A 132           
SHEET    1   D 8 VAL A 103  CYS A 105  0                                        
SHEET    2   D 8 LYS A 212  LYS A 224 -1  O  GLU A 223   N  SER A 104           
SHEET    3   D 8 ILE A 197  ALA A 208 -1  N  ILE A 197   O  ILE A 222           
SHEET    4   D 8 GLU A 116  SER A 121 -1  N  ALA A 118   O  VAL A 207           
SHEET    5   D 8 GLY A 146  THR A 151 -1  O  PHE A 147   N  VAL A 119           
SHEET    6   D 8 PHE A 174  ILE A 179 -1  O  ILE A 177   N  ILE A 148           
SHEET    7   D 8 TYR A 189  VAL A 191 -1  O  VAL A 191   N  PHE A 174           
SHEET    8   D 8 VAL B 166  VAL B 167  1  O  VAL B 166   N  VAL A 190           
SHEET    1   E 9 VAL A 166  VAL A 167  0                                        
SHEET    2   E 9 TYR B 189  SER B 192  1  O  VAL B 190   N  VAL A 166           
SHEET    3   E 9 CYS B 173  ILE B 179 -1  N  PHE B 174   O  VAL B 191           
SHEET    4   E 9 GLY B 146  THR B 151 -1  N  ILE B 148   O  ILE B 177           
SHEET    5   E 9 GLU B 116  SER B 121 -1  N  VAL B 119   O  PHE B 147           
SHEET    6   E 9 ILE B 197  ALA B 208 -1  O  VAL B 207   N  ALA B 118           
SHEET    7   E 9 LYS B 212  LYS B 224 -1  O  ILE B 222   N  ILE B 197           
SHEET    8   E 9 VAL B 103  CYS B 105 -1  N  SER B 104   O  GLU B 223           
SHEET    9   E 9 MET B 108  ALA B 113 -1  O  ALA B 113   N  VAL B 103           
SHEET    1   F 8 VAL A 166  VAL A 167  0                                        
SHEET    2   F 8 TYR B 189  SER B 192  1  O  VAL B 190   N  VAL A 166           
SHEET    3   F 8 CYS B 173  ILE B 179 -1  N  PHE B 174   O  VAL B 191           
SHEET    4   F 8 GLY B 146  THR B 151 -1  N  ILE B 148   O  ILE B 177           
SHEET    5   F 8 GLU B 116  SER B 121 -1  N  VAL B 119   O  PHE B 147           
SHEET    6   F 8 ILE B 197  ALA B 208 -1  O  VAL B 207   N  ALA B 118           
SHEET    7   F 8 ILE B 128  VAL B 134 -1  N  ARG B 133   O  GLU B 198           
SHEET    8   F 8 VAL B 137  CYS B 144 -1  O  ILE B 142   N  VAL B 130           
SHEET    1   G 4 GLU B  26  PHE B  30  0                                        
SHEET    2   G 4 ARG B   2  TYR B   7  1  N  ALA B   3   O  GLU B  26           
SHEET    3   G 4 PHE B  42  GLY B  47  1  O  VAL B  44   N  ALA B   4           
SHEET    4   G 4 ILE B  65  ASN B  69  1  O  ILE B  68   N  GLY B  47           
SHEET    1   H 2 VAL B  97  PHE B 100  0                                        
SHEET    2   H 2 ALA B 229  PHE B 232 -1  O  PHE B 231   N  GLU B  98           
SHEET    1   I 4 GLU C  26  PHE C  30  0                                        
SHEET    2   I 4 ARG C   2  TYR C   7  1  N  VAL C   5   O  GLU C  28           
SHEET    3   I 4 PHE C  42  GLY C  47  1  O  VAL C  44   N  ALA C   4           
SHEET    4   I 4 ILE C  65  ASN C  69  1  O  ILE C  68   N  SER C  45           
SHEET    1   J 2 VAL C  97  PHE C 100  0                                        
SHEET    2   J 2 ALA C 229  PHE C 232 -1  O  ALA C 229   N  PHE C 100           
SHEET    1   K 5 VAL C 103  CYS C 105  0                                        
SHEET    2   K 5 LYS C 212  LYS C 224 -1  O  GLU C 223   N  SER C 104           
SHEET    3   K 5 ILE C 197  ALA C 208 -1  N  ILE C 197   O  ILE C 222           
SHEET    4   K 5 ILE C 128  VAL C 134 -1  N  ARG C 133   O  GLU C 198           
SHEET    5   K 5 VAL C 137  CYS C 144 -1  O  ASP C 140   N  LEU C 132           
SHEET    1   L 8 VAL C 103  CYS C 105  0                                        
SHEET    2   L 8 LYS C 212  LYS C 224 -1  O  GLU C 223   N  SER C 104           
SHEET    3   L 8 ILE C 197  ALA C 208 -1  N  ILE C 197   O  ILE C 222           
SHEET    4   L 8 GLU C 116  SER C 121 -1  N  ALA C 118   O  VAL C 207           
SHEET    5   L 8 GLY C 146  THR C 151 -1  O  PHE C 147   N  VAL C 119           
SHEET    6   L 8 PHE C 174  ILE C 179 -1  O  ILE C 177   N  ILE C 148           
SHEET    7   L 8 TYR C 189  VAL C 191 -1  O  TYR C 189   N  LEU C 176           
SHEET    8   L 8 VAL D 166  VAL D 167  1  O  VAL D 166   N  VAL C 190           
SHEET    1   M 9 VAL C 166  VAL C 167  0                                        
SHEET    2   M 9 TYR D 189  VAL D 191  1  O  VAL D 190   N  VAL C 166           
SHEET    3   M 9 PHE D 174  ILE D 179 -1  N  PHE D 174   O  VAL D 191           
SHEET    4   M 9 GLY D 146  ALA D 150 -1  N  ILE D 148   O  ILE D 177           
SHEET    5   M 9 GLU D 116  SER D 121 -1  N  VAL D 119   O  PHE D 147           
SHEET    6   M 9 ILE D 197  ALA D 208 -1  O  VAL D 207   N  ALA D 118           
SHEET    7   M 9 LYS D 212  LYS D 224 -1  O  ILE D 222   N  ILE D 197           
SHEET    8   M 9 VAL D 103  CYS D 105 -1  N  SER D 104   O  GLU D 223           
SHEET    9   M 9 MET D 108  ALA D 113 -1  O  ALA D 113   N  VAL D 103           
SHEET    1   N 8 VAL C 166  VAL C 167  0                                        
SHEET    2   N 8 TYR D 189  VAL D 191  1  O  VAL D 190   N  VAL C 166           
SHEET    3   N 8 PHE D 174  ILE D 179 -1  N  PHE D 174   O  VAL D 191           
SHEET    4   N 8 GLY D 146  ALA D 150 -1  N  ILE D 148   O  ILE D 177           
SHEET    5   N 8 GLU D 116  SER D 121 -1  N  VAL D 119   O  PHE D 147           
SHEET    6   N 8 ILE D 197  ALA D 208 -1  O  VAL D 207   N  ALA D 118           
SHEET    7   N 8 ILE D 128  VAL D 134 -1  N  ARG D 133   O  GLU D 198           
SHEET    8   N 8 VAL D 137  CYS D 144 -1  O  ASP D 140   N  LEU D 132           
SHEET    1   O 4 GLU D  26  PHE D  30  0                                        
SHEET    2   O 4 ARG D   2  TYR D   7  1  N  ALA D   3   O  GLU D  26           
SHEET    3   O 4 PHE D  42  GLY D  47  1  O  VAL D  44   N  ALA D   4           
SHEET    4   O 4 ILE D  65  ASN D  69  1  O  PHE D  66   N  ILE D  43           
SHEET    1   P 2 VAL D  97  PHE D 100  0                                        
SHEET    2   P 2 ALA D 229  PHE D 232 -1  O  PHE D 231   N  GLU D  98           
SITE     1 AC1 23 GLY A  48  ASP A  49  GLY A  50  ARG A  54                    
SITE     2 AC1 23 VAL A  73  ASN A 115  GLU A 116  ILE A 153                    
SITE     3 AC1 23 THR A 156  GLY A 157  TYR A 158  SER A 161                    
SITE     4 AC1 23 ASP A 209  GLY A 210  GLN A 211  HOH A3082                    
SITE     5 AC1 23 ALA D 125  LYS D 126  MET D 127  ARG D 143                    
SITE     6 AC1 23 ASP D 145  ALA D 180  PHE D 182                               
SITE     1 AC2 25 GLY B  48  ASP B  49  GLY B  50  LEU B  53                    
SITE     2 AC2 25 ARG B  54  VAL B  73  LEU B  75  ASN B 115                    
SITE     3 AC2 25 GLU B 116  ILE B 153  THR B 156  TYR B 158                    
SITE     4 AC2 25 SER B 161  ASP B 209  GLY B 210  GLN B 211                    
SITE     5 AC2 25 HOH B3079  HOH B3114  HOH B3134  ALA C 125                    
SITE     6 AC2 25 MET C 127  ARG C 143  ASP C 145  ALA C 180                    
SITE     7 AC2 25 PHE C 182                                                     
SITE     1 AC3 23 ALA B 125  LYS B 126  MET B 127  ARG B 143                    
SITE     2 AC3 23 ASP B 145  ALA B 180  PHE B 182  GLY C  48                    
SITE     3 AC3 23 ASP C  49  GLY C  50  ARG C  54  VAL C  73                    
SITE     4 AC3 23 LEU C  75  ASN C 115  GLU C 116  ILE C 153                    
SITE     5 AC3 23 THR C 156  GLY C 157  TYR C 158  SER C 161                    
SITE     6 AC3 23 ASP C 209  GLY C 210  GLN C 211                               
SITE     1 AC4 24 ALA A 125  MET A 127  ARG A 143  ASP A 145                    
SITE     2 AC4 24 ALA A 180  PHE A 182  GLY D  48  ASP D  49                    
SITE     3 AC4 24 GLY D  50  ARG D  54  VAL D  73  ASN D 115                    
SITE     4 AC4 24 GLU D 116  ILE D 153  THR D 156  GLY D 157                    
SITE     5 AC4 24 TYR D 158  SER D 161  ASP D 209  GLY D 210                    
SITE     6 AC4 24 GLN D 211  HOH D3087  HOH D3099  HOH D3103                    
CRYST1  122.141  122.141  198.595  90.00  90.00  90.00 P 41 21 2    32          
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      0.008187  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008187  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005035        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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