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Entry: 1ISG
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HEADER    HYDROLASE                               05-DEC-01   1ISG              
TITLE     CRYSTAL STRUCTURE ANALYSIS OF BST-1/CD157 WITH ATPGAMMAS              
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 RIBOSYLCYCLASE, NAD GLYCOHYDROLASE, CNS, ATPGAMMAS, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YAMAMOTO-KATAYAMA,M.ARIYOSHI,K.ISHIHARA,T.HIRANO,H.JINGAMI,         
AUTHOR   2 K.MORIKAWA                                                           
REVDAT   5   15-FEB-12 1ISG    1       HET    HETATM                            
REVDAT   4   13-JUL-11 1ISG    1       VERSN                                    
REVDAT   3   24-FEB-09 1ISG    1       VERSN                                    
REVDAT   2   07-JAN-03 1ISG    1       REMARK                                   
REVDAT   1   13-MAR-02 1ISG    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  PMID   11439087                                                     
REMARK   1  DOI    10.1042/0264-6021:3570385                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.40                          
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)   (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 26500                          
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) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1958                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3693                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 287                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
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          : 118                                     
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 23.42000                                             
REMARK   3    B22 (A**2) : -8.99000                                             
REMARK   3    B33 (A**2) : -14.43000                                            
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) : 0.31                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
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) : 0.38                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.45                            
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) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.76                            
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) : 1.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.000 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.970 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.220 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 34.57                                                
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_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : ATS.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.TOP                                
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : ATS.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ISG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB005233.                                      
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   : 26538                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
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     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 31.200                             
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 33.600                             
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   (%): 65.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, CITRATE, ATPGAMMAS,    
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       29.28650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.26350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.42550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.26350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.28650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.42550            
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: 5150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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    ARG A   3       51.53    -95.25                                   
REMARK 500    PRO A  50       -4.49    -56.38                                   
REMARK 500    SER A  80       30.31   -152.09                                   
REMARK 500    PHE A 108       -3.12     74.29                                   
REMARK 500    CYS A 112      142.49    171.65                                   
REMARK 500    ALA A 116       60.03   -117.98                                   
REMARK 500    HIS A 242       47.62   -145.01                                   
REMARK 500    PRO B  50       -9.94    -47.81                                   
REMARK 500    SER B  80       35.70   -158.14                                   
REMARK 500    ASN B  90       70.48     51.00                                   
REMARK 500    THR B  91       -5.92     60.84                                   
REMARK 500    PHE B 108      -19.24     70.97                                   
REMARK 500    CYS B 112      150.08    173.04                                   
REMARK 500    ASP B 117      155.66    174.41                                   
REMARK 500    CYS B 131      148.93   -178.93                                   
REMARK 500    ASN B 202       66.39   -100.95                                   
REMARK 500    HIS B 242       46.93   -152.98                                   
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 NAG A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 267                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AGS A 1002                
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: 1ISH   RELATED DB: PDB                                   
REMARK 900 1ISH CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHENONADP.            
REMARK 900 RELATED ID: 1ISI   RELATED DB: PDB                                   
REMARK 900 1ISI CONTAINS THE SAME PROTEIN COMPLEXED WITH ETHENONAD.             
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  1ISG A    1   265  UNP    Q10588   BST1_HUMAN      33    297             
DBREF  1ISG B    1   265  UNP    Q10588   BST1_HUMAN      33    297             
SEQADV 1ISG ASP A   34  UNP  Q10588    ASN    66 ENGINEERED                     
SEQADV 1ISG THR A   63  UNP  Q10588    ASN    95 ENGINEERED                     
SEQADV 1ISG ALA A  116  UNP  Q10588    ASN   148 ENGINEERED                     
SEQADV 1ISG ASP B   34  UNP  Q10588    ASN    66 ENGINEERED                     
SEQADV 1ISG THR B   63  UNP  Q10588    ASN    95 ENGINEERED                     
SEQADV 1ISG 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 1ISG ASN A  160  ASN  GLYCOSYLATION SITE                                 
MODRES 1ISG ASN B  160  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 266      14                                                       
HET    NAG  A 267      14                                                       
HET    AGS  A1002      31                                                       
HET    NAG  B 266      14                                                       
HET    NAG  B 267      14                                                       
HET    AGS  B1001      31                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER                       
HETSYN     AGS ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE);                  
HETSYN   2 AGS  ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-            
HETSYN   3 AGS  DIPHOSPHATE MONOTHIOPHOSPHATE                                   
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   4  AGS    2(C10 H16 N5 O12 P3 S)                                       
FORMUL   7  HOH   *89(H2 O)                                                     
HELIX    1   1 HIS A   10  LEU A   26  1                                  17    
HELIX    2   2 ASP A   34  LYS A   43  1                                  10    
HELIX    3   3 VAL A   44  LYS A   48  5                                   5    
HELIX    4   4 LEU A   54  ASP A   57  5                                   4    
HELIX    5   5 TYR A   58  ARG A   66  1                                   9    
HELIX    6   6 SER A   80  ASP A   89  1                                  10    
HELIX    7   7 PRO A   96  ASP A   99  5                                   4    
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 GLN A  183  GLU A  185  5                                   3    
HELIX   12  12 GLY A  209  MET A  221  1                                  13    
HELIX   13  13 TYR A  231  VAL A  240  1                                  10    
HELIX   14  14 HIS A  245  ALA A  249  5                                   5    
HELIX   15  15 HIS B   10  LEU B   25  1                                  16    
HELIX   16  16 LEU B   26  LEU B   26  5                                   1    
HELIX   17  17 SER B   27  ARG B   31  5                                   5    
HELIX   18  18 ASP B   34  ASP B   47  1                                  14    
HELIX   19  19 LEU B   54  ASP B   57  5                                   4    
HELIX   20  20 TYR B   58  ARG B   66  1                                   9    
HELIX   21  21 SER B   80  ASP B   89  1                                  10    
HELIX   22  22 PRO B   96  ASP B   99  5                                   4    
HELIX   23  23 VAL B  100  VAL B  105  1                                   6    
HELIX   24  24 ASN B  134  ASP B  150  1                                  17    
HELIX   25  25 GLY B  172  GLU B  178  1                                   7    
HELIX   26  26 ILE B  179  LEU B  182  5                                   4    
HELIX   27  27 GLN B  183  GLU B  185  5                                   3    
HELIX   28  28 GLY B  209  GLY B  222  1                                  14    
HELIX   29  29 TYR B  231  VAL B  240  1                                  10    
HELIX   30  30 HIS B  245  ALA B  249  5                                   5    
SHEET    1   A 4 LEU A  75  TRP A  77  0                                        
SHEET    2   A 4 GLY A 153  ASN A 160  1  O  HIS A 156   N  PHE A  76           
SHEET    3   A 4 ILE A 187  MET A 195  1  O  GLU A 191   N  ILE A 155           
SHEET    4   A 4 TYR A 225  ASN A 229  1  O  SER A 226   N  ILE A 192           
SHEET    1   B 2 ALA B   4  GLU B   5  0                                        
SHEET    2   B 2 SER B 124  CYS B 125 -1  O  CYS B 125   N  ALA B   4           
SHEET    1   C 4 LEU B  75  TRP B  77  0                                        
SHEET    2   C 4 GLY B 153  ASN B 160  1  O  HIS B 156   N  PHE B  76           
SHEET    3   C 4 ILE B 187  MET B 195  1  O  TRP B 193   N  VAL B 157           
SHEET    4   C 4 TYR B 225  ASN B 229  1  O  ILE B 228   N  VAL B 194           
SSBOND   1 CYS A   19    CYS A   35                          1555   1555  2.03  
SSBOND   2 CYS A   51    CYS A  131                          1555   1555  2.04  
SSBOND   3 CYS A  112    CYS A  125                          1555   1555  2.03  
SSBOND   4 CYS A  206    CYS A  227                          1555   1555  2.04  
SSBOND   5 CYS A  239    CYS A  248                          1555   1555  2.04  
SSBOND   6 CYS B   19    CYS B   35                          1555   1555  2.05  
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  2.04  
SSBOND  10 CYS B  239    CYS B  248                          1555   1555  2.03  
LINK         ND2 ASN A 160                 C1  NAG A 266     1555   1555  1.45  
LINK         ND2 ASN B 160                 C1  NAG B 266     1555   1555  1.46  
LINK         O4  NAG A 266                 C1  NAG A 267     1555   1555  1.38  
LINK         O4  NAG B 266                 C1  NAG B 267     1555   1555  1.38  
SITE     1 AC1  8 ASN A  79  SER A  80  LEU A  83  ASN A 160                    
SITE     2 AC1  8 SER A 162  GLU A 163  GLU A 197  NAG A 267                    
SITE     1 AC2  2 PRO A 201  NAG A 266                                          
SITE     1 AC3  9 ASN B  79  SER B  80  LEU B  83  ASN B 160                    
SITE     2 AC3  9 SER B 162  GLU B 163  PRO B 164  GLU B 197                    
SITE     3 AC3  9 NAG B 267                                                     
SITE     1 AC4  1 NAG B 266                                                     
SITE     1 AC5 13 TRP B  77  ASN B  79  SER B  80  HIS B  81                    
SITE     2 AC5 13 LEU B  97  ASP B 107  PHE B 108  ASP B 137                    
SITE     3 AC5 13 TRP B 140  PHE B 173  HOH B1039  HOH B1041                    
SITE     4 AC5 13 HOH B1042                                                     
SITE     1 AC6 13 TRP A  77  ASN A  79  SER A  80  HIS A  81                    
SITE     2 AC6 13 LEU A  97  ASP A 107  PHE A 108  ASP A 137                    
SITE     3 AC6 13 TRP A 140  PHE A 173  HOH A1038  HOH A1047                    
SITE     4 AC6 13 HOH A1048                                                     
CRYST1   58.573  112.851  130.527  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      0.017073  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007661        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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