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Database: PDB
Entry: 1ISI
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Original site: 1ISI 
HEADER    HYDROLASE                               05-DEC-01   1ISI              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF BST-1/CD157 COMPLEXED WITH ETHENONAD    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BONE MARROW STROMAL CELL ANTIGEN 1;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR REGION;                                      
COMPND   5 SYNONYM: BST-1/CD157, ADP-RIBOSYL CYCLASE 2;                         
COMPND   6 EC: 3.2.2.5;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: AUTOGRAPHA CALIFORNICA NUCLEAR             
SOURCE  11 POLYHEDROSIS VIRUS                                                   
KEYWDS    ADP RIBOSYL CYCLASE, NAD GLYCOHYDROLASE, CNS, ETHENONAD, HYDROLASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YAMAMOTO-KATAYAMA,M.ARIYOSHI,K.ISHIHARA,T.HIRANO,H.JINGAMI,         
AUTHOR   2 K.MORIKAWA                                                           
REVDAT   5   13-JUL-11 1ISI    1       VERSN                                    
REVDAT   4   29-DEC-09 1ISI    1       HETNAM FORMUL HETATM                     
REVDAT   3   24-FEB-09 1ISI    1       VERSN                                    
REVDAT   2   07-JAN-03 1ISI    1       REMARK                                   
REVDAT   1   13-MAR-02 1ISI    0                                                
JRNL        AUTH   S.YAMAMOTO-KATAYAMA,M.ARIYOSHI,K.ISHIHARA,T.HIRANO,          
JRNL        AUTH 2 H.JINGAMI,K.MORIKAWA                                         
JRNL        TITL   CRYSTALLOGRAPHIC STUDIES ON HUMAN BST-1/CD157 WITH           
JRNL        TITL 2 ADP-RIBOSYL CYCLASE AND NAD GLYCOHYDROLASE ACTIVITIES.       
JRNL        REF    J.MOL.BIOL.                   V. 316   711 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11866528                                                     
JRNL        DOI    10.1006/JMBI.2001.5386                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.YAMAMOTO-KATAYAMA,A.SATO,M.ARIYOSHI,M.SUYAMA,K.ISHIHARA,   
REMARK   1  AUTH 2 T.HIRANO,H.NAKAMURA,K.MORIKAWA,H.JINGAMI                     
REMARK   1  TITL   SITE-DIRECTED REMOVAL OF N-GLYCOSYLATION SITES IN            
REMARK   1  TITL 2 BST-1/CD157: EFFECTS ON MOLECULAR AND FUNCTIONAL             
REMARK   1  TITL 3 HETEROGENEITY.                                               
REMARK   1  REF    BIOCHEM.J.                    V. 357   385 2001              
REMARK   1  REFN                   ISSN 0264-6021                               
REMARK   1  DOI    10.1042/0264-6021:3570385                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.57                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1395327.100                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49401                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.219                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3759                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6907                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 601                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4010                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 150                                     
REMARK   3   SOLVENT ATOMS            : 262                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.30000                                             
REMARK   3    B22 (A**2) : -5.99000                                             
REMARK   3    B33 (A**2) : -8.31000                                             
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) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.24                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.72                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.190 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.880 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.730 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 55.37                                                
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  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER_REP2.PARAM                               
REMARK   3  PARAMETER FILE  4  : NCA.PARAM                                      
REMARK   3  PARAMETER FILE  5  : ETHENO.PARAM                                   
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER2.TOP                                     
REMARK   3  TOPOLOGY FILE  4   : NCA.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : ETHENO.TOP                                     
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ISI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB005235.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-00                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL24XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.836                              
REMARK 200  MONOCHROMATOR                  : SILICON CRYSTAL                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49467                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
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     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 30.000                             
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 30.300                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CITRATE, ETHENONAD,    
REMARK 280  PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.47250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.42550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.37000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.42550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.47250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.37000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 25.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ARG A     1                                                      
REMARK 465     SER A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     ALA A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     ALA A   256                                                      
REMARK 465     THR A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     ARG A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     SER A   263                                                      
REMARK 465     LEU A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 465     ARG B     1                                                      
REMARK 465     SER B   252                                                      
REMARK 465     ALA B   253                                                      
REMARK 465     ALA B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     ALA B   256                                                      
REMARK 465     THR B   257                                                      
REMARK 465     GLN B   258                                                      
REMARK 465     ARG B   259                                                      
REMARK 465     LYS B   260                                                      
REMARK 465     ALA B   261                                                      
REMARK 465     PRO B   262                                                      
REMARK 465     SER B   263                                                      
REMARK 465     LEU B   264                                                      
REMARK 465     TYR B   265                                                      
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    LYS A  43        2.52    -67.23                                   
REMARK 500    PRO A  50       -2.51    -57.41                                   
REMARK 500    SER A  80       29.03   -149.31                                   
REMARK 500    THR A  91       -6.10     77.41                                   
REMARK 500    PHE A 108      -10.36     73.64                                   
REMARK 500    CYS A 131      138.37   -175.80                                   
REMARK 500    ASN A 202       76.60   -100.86                                   
REMARK 500    HIS A 242       51.04   -145.46                                   
REMARK 500    PRO B  50       -1.09    -54.86                                   
REMARK 500    SER B  80       40.64   -159.38                                   
REMARK 500    THR B  91       -7.07     77.43                                   
REMARK 500    MET B  95       77.26   -119.44                                   
REMARK 500    PHE B 108      -12.19     75.60                                   
REMARK 500    CYS B 112      149.15    179.93                                   
REMARK 500    CYS B 131      141.89   -176.09                                   
REMARK 500    HIS B 242       45.88   -144.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2071        DISTANCE =  5.08 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCA A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENQ A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NCA B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ENQ B 2002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ISF   RELATED DB: PDB                                   
REMARK 900 1ISF CONTAINS THE SAME PROTEIN (LIGAND FREE FORM).                   
REMARK 900 RELATED ID: 1ISG   RELATED DB: PDB                                   
REMARK 900 1ISG CONTAINS THE SAME PROTEIN COMPLEXED WITH ATPGAMMAS.             
REMARK 900 RELATED ID: 1ISH   RELATED DB: PDB                                   
REMARK 900 1ISH CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHENONADP.            
REMARK 900 RELATED ID: 1ISJ   RELATED DB: PDB                                   
REMARK 900 1ISJ CONTAINS THE SAME PROTEIN COMPLEXED WITH NMN.                   
REMARK 900 RELATED ID: 1ISM   RELATED DB: PDB                                   
REMARK 900 1ISM CONTAINS THE SAME PROTEIN COMPLEXED WITH NICOTINAMIDE.          
DBREF  1ISI A    1   265  UNP    Q10588   BST1_HUMAN      33    297             
DBREF  1ISI B    1   265  UNP    Q10588   BST1_HUMAN      33    297             
SEQADV 1ISI ASP A   34  UNP  Q10588    ASN    66 ENGINEERED                     
SEQADV 1ISI THR A   63  UNP  Q10588    ASN    95 ENGINEERED                     
SEQADV 1ISI ALA A  116  UNP  Q10588    ASN   148 ENGINEERED                     
SEQADV 1ISI ASP B   34  UNP  Q10588    ASN    66 ENGINEERED                     
SEQADV 1ISI THR B   63  UNP  Q10588    ASN    95 ENGINEERED                     
SEQADV 1ISI ALA B  116  UNP  Q10588    ASN   148 ENGINEERED                     
SEQRES   1 A  265  ARG TRP ARG ALA GLU GLY THR SER ALA HIS LEU ARG ASP          
SEQRES   2 A  265  ILE PHE LEU GLY ARG CYS ALA GLU TYR ARG ALA LEU LEU          
SEQRES   3 A  265  SER PRO GLU GLN ARG ASN LYS ASP CYS THR ALA ILE TRP          
SEQRES   4 A  265  GLU ALA PHE LYS VAL ALA LEU ASP LYS ASP PRO CYS SER          
SEQRES   5 A  265  VAL LEU PRO SER ASP TYR ASP LEU PHE ILE THR LEU SER          
SEQRES   6 A  265  ARG HIS SER ILE PRO ARG ASP LYS SER LEU PHE TRP GLU          
SEQRES   7 A  265  ASN SER HIS LEU LEU VAL ASN SER PHE ALA ASP ASN THR          
SEQRES   8 A  265  ARG ARG PHE MET PRO LEU SER ASP VAL LEU TYR GLY ARG          
SEQRES   9 A  265  VAL ALA ASP PHE LEU SER TRP CYS ARG GLN LYS ALA ASP          
SEQRES  10 A  265  SER GLY LEU ASP TYR GLN SER CYS PRO THR SER GLU ASP          
SEQRES  11 A  265  CYS GLU ASN ASN PRO VAL ASP SER PHE TRP LYS ARG ALA          
SEQRES  12 A  265  SER ILE GLN TYR SER LYS ASP SER SER GLY VAL ILE HIS          
SEQRES  13 A  265  VAL MET LEU ASN GLY SER GLU PRO THR GLY ALA TYR PRO          
SEQRES  14 A  265  ILE LYS GLY PHE PHE ALA ASP TYR GLU ILE PRO ASN LEU          
SEQRES  15 A  265  GLN LYS GLU LYS ILE THR ARG ILE GLU ILE TRP VAL MET          
SEQRES  16 A  265  HIS GLU ILE GLY GLY PRO ASN VAL GLU SER CYS GLY GLU          
SEQRES  17 A  265  GLY SER MET LYS VAL LEU GLU LYS ARG LEU LYS ASP MET          
SEQRES  18 A  265  GLY PHE GLN TYR SER CYS ILE ASN ASP TYR ARG PRO VAL          
SEQRES  19 A  265  LYS LEU LEU GLN CYS VAL ASP HIS SER THR HIS PRO ASP          
SEQRES  20 A  265  CYS ALA LEU LYS SER ALA ALA ALA ALA THR GLN ARG LYS          
SEQRES  21 A  265  ALA PRO SER LEU TYR                                          
SEQRES   1 B  265  ARG TRP ARG ALA GLU GLY THR SER ALA HIS LEU ARG ASP          
SEQRES   2 B  265  ILE PHE LEU GLY ARG CYS ALA GLU TYR ARG ALA LEU LEU          
SEQRES   3 B  265  SER PRO GLU GLN ARG ASN LYS ASP CYS THR ALA ILE TRP          
SEQRES   4 B  265  GLU ALA PHE LYS VAL ALA LEU ASP LYS ASP PRO CYS SER          
SEQRES   5 B  265  VAL LEU PRO SER ASP TYR ASP LEU PHE ILE THR LEU SER          
SEQRES   6 B  265  ARG HIS SER ILE PRO ARG ASP LYS SER LEU PHE TRP GLU          
SEQRES   7 B  265  ASN SER HIS LEU LEU VAL ASN SER PHE ALA ASP ASN THR          
SEQRES   8 B  265  ARG ARG PHE MET PRO LEU SER ASP VAL LEU TYR GLY ARG          
SEQRES   9 B  265  VAL ALA ASP PHE LEU SER TRP CYS ARG GLN LYS ALA ASP          
SEQRES  10 B  265  SER GLY LEU ASP TYR GLN SER CYS PRO THR SER GLU ASP          
SEQRES  11 B  265  CYS GLU ASN ASN PRO VAL ASP SER PHE TRP LYS ARG ALA          
SEQRES  12 B  265  SER ILE GLN TYR SER LYS ASP SER SER GLY VAL ILE HIS          
SEQRES  13 B  265  VAL MET LEU ASN GLY SER GLU PRO THR GLY ALA TYR PRO          
SEQRES  14 B  265  ILE LYS GLY PHE PHE ALA ASP TYR GLU ILE PRO ASN LEU          
SEQRES  15 B  265  GLN LYS GLU LYS ILE THR ARG ILE GLU ILE TRP VAL MET          
SEQRES  16 B  265  HIS GLU ILE GLY GLY PRO ASN VAL GLU SER CYS GLY GLU          
SEQRES  17 B  265  GLY SER MET LYS VAL LEU GLU LYS ARG LEU LYS ASP MET          
SEQRES  18 B  265  GLY PHE GLN TYR SER CYS ILE ASN ASP TYR ARG PRO VAL          
SEQRES  19 B  265  LYS LEU LEU GLN CYS VAL ASP HIS SER THR HIS PRO ASP          
SEQRES  20 B  265  CYS ALA LEU LYS SER ALA ALA ALA ALA THR GLN ARG LYS          
SEQRES  21 B  265  ALA PRO SER LEU TYR                                          
MODRES 1ISI ASN B  160  ASN  GLYCOSYLATION SITE                                 
MODRES 1ISI ASN A  160  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 301      14                                                       
HET    NAG  A 302      14                                                       
HET    NCA  A1002       9                                                       
HET    ENQ  A2001      38                                                       
HET    NAG  B 303      14                                                       
HET    NAG  B 304      14                                                       
HET    NCA  B1001       9                                                       
HET    ENQ  B2002      38                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     NCA NICOTINAMIDE                                                     
HETNAM     ENQ [[(2R,3S,4R,5R)-3,4-DIHYDROXY-5-(9H-IMIDAZO[2,1-                 
HETNAM   2 ENQ  F]PURIN-6-IUM-3-YL)OXOLAN-2-YL]METHOXY-OXIDANIDYL-              
HETNAM   3 ENQ  PHOSPHORYL] [(2R,3S,4R,5R)-3,4-DIHYDROXY-5-OXIDANIDYL-          
HETNAM   4 ENQ  OXOLAN-2-YL]METHYL PHOSPHATE                                    
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4  NCA    2(C6 H6 N2 O)                                                
FORMUL   5  ENQ    2(C17 H22 N5 O14 P2 1-)                                      
FORMUL   9  HOH   *262(H2 O)                                                    
HELIX    1   1 HIS A   10  LEU A   26  1                                  17    
HELIX    2   2 SER A   27  ARG A   31  5                                   5    
HELIX    3   3 ASP A   34  LYS A   43  1                                  10    
HELIX    4   4 VAL A   44  ASP A   47  5                                   4    
HELIX    5   5 LEU A   54  ASP A   57  5                                   4    
HELIX    6   6 TYR A   58  ARG A   66  1                                   9    
HELIX    7   7 SER A   80  ASP A   89  1                                  10    
HELIX    8   8 VAL A  100  VAL A  105  1                                   6    
HELIX    9   9 ASN A  134  ASP A  150  1                                  17    
HELIX   10  10 GLY A  172  GLU A  178  1                                   7    
HELIX   11  11 ILE A  179  LEU A  182  5                                   4    
HELIX   12  12 GLN A  183  GLU A  185  5                                   3    
HELIX   13  13 GLY A  209  MET A  221  1                                  13    
HELIX   14  14 TYR A  231  VAL A  240  1                                  10    
HELIX   15  15 HIS A  245  ALA A  249  5                                   5    
HELIX   16  16 HIS B   10  ALA B   24  1                                  15    
HELIX   17  17 ASP B   34  ASP B   47  1                                  14    
HELIX   18  18 LEU B   54  ASP B   57  5                                   4    
HELIX   19  19 TYR B   58  ARG B   66  1                                   9    
HELIX   20  20 SER B   80  ASP B   89  1                                  10    
HELIX   21  21 PRO B   96  ASP B   99  5                                   4    
HELIX   22  22 VAL B  100  VAL B  105  1                                   6    
HELIX   23  23 ASN B  134  ASP B  150  1                                  17    
HELIX   24  24 GLY B  172  GLU B  178  1                                   7    
HELIX   25  25 ILE B  179  LEU B  182  5                                   4    
HELIX   26  26 GLN B  183  GLU B  185  5                                   3    
HELIX   27  27 GLY B  209  MET B  221  1                                  13    
HELIX   28  28 TYR B  231  VAL B  240  1                                  10    
HELIX   29  29 HIS B  245  ALA B  249  5                                   5    
SHEET    1   A 2 ALA A   4  GLU A   5  0                                        
SHEET    2   A 2 SER A 124  CYS A 125 -1  O  CYS A 125   N  ALA A   4           
SHEET    1   B 5 MET A  95  PRO A  96  0                                        
SHEET    2   B 5 SER A  74  TRP A  77  1  N  LEU A  75   O  MET A  95           
SHEET    3   B 5 GLY A 153  ASN A 160  1  O  HIS A 156   N  PHE A  76           
SHEET    4   B 5 ILE A 187  MET A 195  1  O  GLU A 191   N  ILE A 155           
SHEET    5   B 5 TYR A 225  ASN A 229  1  O  SER A 226   N  ILE A 192           
SHEET    1   C 2 ALA B   4  GLU B   5  0                                        
SHEET    2   C 2 SER B 124  CYS B 125 -1  O  CYS B 125   N  ALA B   4           
SHEET    1   D 4 LEU B  75  TRP B  77  0                                        
SHEET    2   D 4 GLY B 153  ASN B 160  1  O  HIS B 156   N  PHE B  76           
SHEET    3   D 4 ILE B 187  MET B 195  1  O  GLU B 191   N  ILE B 155           
SHEET    4   D 4 TYR B 225  ASN B 229  1  O  ILE B 228   N  ILE B 192           
SSBOND   1 CYS A   19    CYS A   35                          1555   1555  2.04  
SSBOND   2 CYS A   51    CYS A  131                          1555   1555  2.03  
SSBOND   3 CYS A  112    CYS A  125                          1555   1555  2.04  
SSBOND   4 CYS A  206    CYS A  227                          1555   1555  2.04  
SSBOND   5 CYS A  239    CYS A  248                          1555   1555  2.03  
SSBOND   6 CYS B   19    CYS B   35                          1555   1555  2.04  
SSBOND   7 CYS B   51    CYS B  131                          1555   1555  2.04  
SSBOND   8 CYS B  112    CYS B  125                          1555   1555  2.04  
SSBOND   9 CYS B  206    CYS B  227                          1555   1555  2.03  
SSBOND  10 CYS B  239    CYS B  248                          1555   1555  2.03  
LINK         O4  NAG B 303                 C1  NAG B 304     1555   1555  1.38  
LINK         O4  NAG A 301                 C1  NAG A 302     1555   1555  1.39  
LINK         ND2 ASN B 160                 C1  NAG B 303     1555   1555  1.44  
LINK         ND2 ASN A 160                 C1  NAG A 301     1555   1555  1.45  
SITE     1 AC1 12 ASN A  79  SER A  80  LEU A  83  ASN A 160                    
SITE     2 AC1 12 SER A 162  GLU A 163  PRO A 164  GLU A 197                    
SITE     3 AC1 12 NAG A 302  HOH A2050  HOH A2057  HOH A2104                    
SITE     1 AC2  2 PRO A 201  NAG A 301                                          
SITE     1 AC3  6 TRP A  77  GLU A  78  PHE A 173  GLU A 178                    
SITE     2 AC3  6 ENQ A2001  HOH A2133                                          
SITE     1 AC4 15 TRP A  77  HIS A  81  LEU A  97  ALA A 106                    
SITE     2 AC4 15 ASP A 107  PHE A 108  TRP A 140  SER A 144                    
SITE     3 AC4 15 PHE A 173  GLU A 178  NCA A1002  HOH A2059                    
SITE     4 AC4 15 HOH A2067  HOH A2130  HOH A2132                               
SITE     1 AC5 12 ASN B  79  SER B  80  LEU B  83  ASN B 160                    
SITE     2 AC5 12 SER B 162  GLU B 163  PRO B 164  GLU B 197                    
SITE     3 AC5 12 NAG B 304  HOH B2042  HOH B2043  HOH B2080                    
SITE     1 AC6  1 NAG B 303                                                     
SITE     1 AC7  6 TRP B  77  GLU B  78  PHE B 173  ENQ B2002                    
SITE     2 AC7  6 HOH B2024  HOH B2129                                          
SITE     1 AC8 17 GLU B   5  TRP B  77  HIS B  81  LEU B  97                    
SITE     2 AC8 17 ALA B 106  ASP B 107  PHE B 108  TRP B 140                    
SITE     3 AC8 17 SER B 144  PHE B 173  GLU B 178  NCA B1001                    
SITE     4 AC8 17 HOH B2061  HOH B2126  HOH B2128  HOH B2130                    
SITE     5 AC8 17 HOH B2131                                                     
CRYST1   58.945  112.740  130.851  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016965  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008870  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007642        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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