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Database: PDB
Entry: 1LSU
LinkDB: 1LSU
Original site: 1LSU 
HEADER    TRANSPORT PROTEIN                       18-MAY-02   1LSU              
TITLE     KTN BSU222 CRYSTAL STRUCTURE IN COMPLEX WITH NADH                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CONSERVED HYPOTHETICAL PROTEIN YUAA;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KTN DOMAIN, RESIDUES 1-143;                                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: KTRA;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL-21;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PHIS8                                     
KEYWDS    KTN DOMAIN, NAD, RCK DOMAIN, POTASSIUM TRANSPORT, POTASSIUM CHANNEL,  
KEYWDS   2 KTRA, ROSSMANN FOLD, TRANSPORT PROTEIN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.ROOSILD,S.MILLER,I.R.BOOTH,S.CHOE                                 
REVDAT   3   12-NOV-14 1LSU    1       KEYWDS                                   
REVDAT   2   24-FEB-09 1LSU    1       VERSN                                    
REVDAT   1   03-JUL-02 1LSU    0                                                
JRNL        AUTH   T.P.ROOSILD,S.MILLER,I.R.BOOTH,S.CHOE                        
JRNL        TITL   A MECHANISM OF REGULATING TRANSMEMBRANE POTASSIUM FLUX       
JRNL        TITL 2 THROUGH A LIGAND-MEDIATED CONFORMATIONAL SWITCH.             
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 109   781 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12086676                                                     
JRNL        DOI    10.1016/S0092-8674(02)00768-7                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1669970.480                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 9590                           
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) : 0.279                           
REMARK   3   FREE R VALUE                     : 0.329                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 503                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.013                           
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) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.03                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1475                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4300                       
REMARK   3   BIN FREE R VALUE                    : 0.4670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.80                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 90                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.043                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2096                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 88                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.31000                                              
REMARK   3    B22 (A**2) : 5.31000                                              
REMARK   3    B33 (A**2) : -10.62000                                            
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) : 0.48                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.57                            
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) : 0.49                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.66                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.100                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.920                           
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) : 1.540 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.750 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.130 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.350 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 41.86                                                
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : NAD_XPLOR_PAR.TXT                              
REMARK   3  PARAMETER FILE  4  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016248.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-01; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SSRL; SSRL                         
REMARK 200  BEAMLINE                       : BL9-2; BL9-2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.071, 0.9794, 0.9252; 0.9198,     
REMARK 200                                   0.8611, 0.9196                     
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL; DOUBLE CRYSTAL     
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; NULL               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9635                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; MAD                                       
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD, MIR                     
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 6, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       49.35000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       49.35000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       49.35000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       49.35000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       49.35000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       49.35000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       63.30000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       49.35000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       63.30000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       63.30000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       49.35000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: THE KTN BIOLOGICAL UNIT CONSISTS OF TWO HELIX-SWAPPED        
REMARK 300 MONOMERS. THE ASYMMETRIC UNIT CONTAINS ONE BIOLOGICAL UNIT FORMED    
REMARK 300 BY CHAINS A & B                                                      
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     ASN A     6                                                      
REMARK 465     VAL A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     ASN B     6                                                      
REMARK 465     VAL B   141                                                      
REMARK 465     LEU B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG   SER B    47     OG   SER B    47     7556     1.69            
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    LEU A  14       52.61   -105.13                                   
REMARK 500    PHE A  17      -71.70    -72.52                                   
REMARK 500    HIS A  51      107.51   -170.66                                   
REMARK 500    ALA A  80       -4.21    -41.19                                   
REMARK 500    GLN A 105       -5.65   -142.41                                   
REMARK 500    GLU A 139       12.87    -64.07                                   
REMARK 500    LEU B  14       68.97   -119.58                                   
REMARK 500    ALA B  44       -6.25    -59.11                                   
REMARK 500    HIS B  51      102.01   -173.57                                   
REMARK 500    GLU B  60      -63.13    -28.06                                   
REMARK 500    ARG B  69       -8.70    -56.40                                   
REMARK 500    ALA B  80       -5.60    -41.45                                   
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 NAI A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1LSS   RELATED DB: PDB                                   
REMARK 900 KTN MJA218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+                    
REMARK 999                                                                      
REMARK 999 SEQUENCE AUTHORS STATE THE SEQUENCE PRESENT IN THE B. SUBTILIS LAB   
REMARK 999 STRAIN FROM WHICH THEY CLONED MAY BE A STRAIN TYPE POLYMORPHISM, OR  
REMARK 999 AN ERROR IN THE DATABASE ITSELF.                                     
DBREF  1LSU A    1   143  UNP    O32080   O32080_BACSU     1    143             
DBREF  1LSU B    1   143  UNP    O32080   O32080_BACSU     1    143             
SEQADV 1LSU GLY A   -3  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU SER A   -2  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU HIS A   -1  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU GLY A    0  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU VAL A   22  UNP  O32080    CYS    22 ENGINEERED                     
SEQADV 1LSU SER A  143  UNP  O32080    ASN   143 SEE REMARK 999                 
SEQADV 1LSU GLY B   -3  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU SER B   -2  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU HIS B   -1  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU GLY B    0  UNP  O32080              CLONING ARTIFACT               
SEQADV 1LSU VAL B   22  UNP  O32080    CYS    22 ENGINEERED                     
SEQADV 1LSU SER B  143  UNP  O32080    ASN   143 SEE REMARK 999                 
SEQRES   1 A  147  GLY SER HIS GLY MET GLY ARG ILE LYS ASN LYS GLN PHE          
SEQRES   2 A  147  ALA VAL ILE GLY LEU GLY ARG PHE GLY GLY SER ILE VAL          
SEQRES   3 A  147  LYS GLU LEU HIS ARG MET GLY HIS GLU VAL LEU ALA VAL          
SEQRES   4 A  147  ASP ILE ASN GLU GLU LYS VAL ASN ALA TYR ALA SER TYR          
SEQRES   5 A  147  ALA THR HIS ALA VAL ILE ALA ASN ALA THR GLU GLU ASN          
SEQRES   6 A  147  GLU LEU LEU SER LEU GLY ILE ARG ASN PHE GLU TYR VAL          
SEQRES   7 A  147  ILE VAL ALA ILE GLY ALA ASN ILE GLN ALA SER THR LEU          
SEQRES   8 A  147  THR THR LEU LEU LEU LYS GLU LEU ASP ILE PRO ASN ILE          
SEQRES   9 A  147  TRP VAL LYS ALA GLN ASN TYR TYR HIS HIS LYS VAL LEU          
SEQRES  10 A  147  GLU LYS ILE GLY ALA ASP ARG ILE ILE HIS PRO GLU LYS          
SEQRES  11 A  147  ASP MET GLY VAL LYS ILE ALA GLN SER LEU SER ASP GLU          
SEQRES  12 A  147  ASN VAL LEU SER                                              
SEQRES   1 B  147  GLY SER HIS GLY MET GLY ARG ILE LYS ASN LYS GLN PHE          
SEQRES   2 B  147  ALA VAL ILE GLY LEU GLY ARG PHE GLY GLY SER ILE VAL          
SEQRES   3 B  147  LYS GLU LEU HIS ARG MET GLY HIS GLU VAL LEU ALA VAL          
SEQRES   4 B  147  ASP ILE ASN GLU GLU LYS VAL ASN ALA TYR ALA SER TYR          
SEQRES   5 B  147  ALA THR HIS ALA VAL ILE ALA ASN ALA THR GLU GLU ASN          
SEQRES   6 B  147  GLU LEU LEU SER LEU GLY ILE ARG ASN PHE GLU TYR VAL          
SEQRES   7 B  147  ILE VAL ALA ILE GLY ALA ASN ILE GLN ALA SER THR LEU          
SEQRES   8 B  147  THR THR LEU LEU LEU LYS GLU LEU ASP ILE PRO ASN ILE          
SEQRES   9 B  147  TRP VAL LYS ALA GLN ASN TYR TYR HIS HIS LYS VAL LEU          
SEQRES  10 B  147  GLU LYS ILE GLY ALA ASP ARG ILE ILE HIS PRO GLU LYS          
SEQRES  11 B  147  ASP MET GLY VAL LYS ILE ALA GLN SER LEU SER ASP GLU          
SEQRES  12 B  147  ASN VAL LEU SER                                              
HET    NAI  A1001      44                                                       
HET    NAI  B1002      44                                                       
HETNAM     NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE                     
HETSYN     NAI NADH                                                             
FORMUL   3  NAI    2(C21 H29 N7 O14 P2)                                         
HELIX    1   1 GLY A   15  MET A   28  1                                  14    
HELIX    2   2 ASN A   38  TYR A   45  1                                   8    
HELIX    3   3 GLU A   59  SER A   65  1                                   7    
HELIX    4   4 GLY A   67  PHE A   71  5                                   5    
HELIX    5   5 ASN A   81  GLU A   94  1                                  14    
HELIX    6   6 ASN A  106  GLY A  117  1                                  12    
HELIX    7   7 HIS A  123  GLU A  139  1                                  17    
HELIX    8   8 GLY B   15  MET B   28  1                                  14    
HELIX    9   9 ASN B   38  ALA B   44  1                                   7    
HELIX   10  10 GLU B   59  LEU B   64  5                                   6    
HELIX   11  11 GLY B   67  PHE B   71  5                                   5    
HELIX   12  12 ASN B   81  LEU B   95  1                                  15    
HELIX   13  13 ASN B  106  GLY B  117  1                                  12    
HELIX   14  14 HIS B  123  GLU B  139  1                                  17    
SHEET    1   A 6 HIS A  51  ILE A  54  0                                        
SHEET    2   A 6 VAL A  32  ASP A  36  1  N  ALA A  34   O  HIS A  51           
SHEET    3   A 6 PHE A   9  ILE A  12  1  N  VAL A  11   O  LEU A  33           
SHEET    4   A 6 TYR A  73  VAL A  76  1  O  ILE A  75   N  ILE A  12           
SHEET    5   A 6 ASN A  99  LYS A 103  1  O  TRP A 101   N  VAL A  76           
SHEET    6   A 6 ARG A 120  ILE A 122  1  O  ARG A 120   N  VAL A 102           
SHEET    1   B 6 HIS B  51  ILE B  54  0                                        
SHEET    2   B 6 VAL B  32  ASP B  36  1  N  ALA B  34   O  HIS B  51           
SHEET    3   B 6 PHE B   9  ILE B  12  1  N  VAL B  11   O  LEU B  33           
SHEET    4   B 6 TYR B  73  VAL B  76  1  O  ILE B  75   N  ILE B  12           
SHEET    5   B 6 ASN B  99  LYS B 103  1  O  ASN B  99   N  VAL B  74           
SHEET    6   B 6 ARG B 120  ILE B 122  1  O  ARG B 120   N  VAL B 102           
SITE     1 AC1 17 GLY A  13  GLY A  15  ASP A  36  ILE A  37                    
SITE     2 AC1 17 ASN A  38  LYS A  41  ASN A  56  ALA A  57                    
SITE     3 AC1 17 ILE A  78  GLY A  79  ALA A  80  ILE A  82                    
SITE     4 AC1 17 ALA A  84  SER A  85  LYS A 103  GLN A 105                    
SITE     5 AC1 17 HIS A 109                                                     
SITE     1 AC2 20 GLU A 125  GLY B  13  LEU B  14  GLY B  15                    
SITE     2 AC2 20 ARG B  16  ASP B  36  ILE B  37  ASN B  38                    
SITE     3 AC2 20 LYS B  41  ASN B  56  ALA B  57  ILE B  78                    
SITE     4 AC2 20 GLY B  79  ALA B  80  ILE B  82  ALA B  84                    
SITE     5 AC2 20 SER B  85  LYS B 103  GLN B 105  HIS B 109                    
CRYST1  126.600  126.600   98.700  90.00  90.00  90.00 I 4 2 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      0.007899  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010132        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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