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Database: PDB
Entry: 1G1A
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Original site: 1G1A 
HEADER    LYASE                                   11-OCT-00   1G1A              
TITLE     THE CRYSTAL STRUCTURE OF DTDP-D-GLUCOSE 4,6-DEHYDRATASE (RMLB)FROM    
TITLE    2 SALMONELLA ENTERICA SEROVAR TYPHIMURIUM                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DTDP-D-GLUCOSE 4,6-DEHYDRATASE;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 4.2.1.46;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR     
SOURCE   3 TYPHIMURIUM;                                                         
SOURCE   4 ORGANISM_TAXID: 90371;                                               
SOURCE   5 STRAIN: SUBSP. ENTERICA SEROVAR TYPHIMURIUM;                         
SOURCE   6 VARIANT: SEROVAR TYPHIMURIUM;                                        
SOURCE   7 GENE: RMLB;                                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    ROSSMANN FOLD, PROTEIN-NAD COMPLEX, SHORT CHAIN DEHYDROGENASE, LYASE  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.T.M.ALLARD,M.-F.GIRAUD,C.WHITFIELD,M.GRANINGER,P.MESSNER,           
AUTHOR   2 J.H.NAISMITH                                                         
REVDAT   4   03-OCT-18 1G1A    1       REMARK                                   
REVDAT   3   24-FEB-09 1G1A    1       VERSN                                    
REVDAT   2   01-APR-03 1G1A    1       JRNL                                     
REVDAT   1   21-MAR-01 1G1A    0                                                
JRNL        AUTH   S.T.ALLARD,M.F.GIRAUD,C.WHITFIELD,M.GRANINGER,P.MESSNER,     
JRNL        AUTH 2 J.H.NAISMITH                                                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF DTDP-D-GLUCOSE 4,6-DEHYDRATASE      
JRNL        TITL 2 (RMLB) FROM SALMONELLA ENTERICA SEROVAR TYPHIMURIUM, THE     
JRNL        TITL 3 SECOND ENZYME IN THE DTDP-L-RHAMNOSE PATHWAY.                
JRNL        REF    J.MOL.BIOL.                   V. 307   283 2001              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11243820                                                     
JRNL        DOI    10.1006/JMBI.2000.4470                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.T.M.ALLARD,M.-F.GIRAUD,C.WHITFIELD,P.MESSNER,J.H.NAISMITH  
REMARK   1  TITL   THE PURIFIACTION, CRYSTALLISATION AND STRUCTURAL ELUCIDATION 
REMARK   1  TITL 2 OF DTDP-D-GLUCOSE 4,6-DEHYDRATASE (RMLB), THE SECOND ENZYME  
REMARK   1  TITL 3 OF THE DTDP-L-RHAMNOSE SYNTHESIS PATHWAY FROM SALMONELLA     
REMARK   1  TITL 4 ENTERICA SEROVAR TYPHIMURIUM.                                
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  56   222 2000              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444999016200                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.47 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 2.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.80                          
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)   (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 67669                          
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) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3391                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11196                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 221                                     
REMARK   3   SOLVENT ATOMS            : 512                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.22                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1G1A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012108.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-JUL-99; 28-FEB-00               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SRS; ESRF                          
REMARK 200  BEAMLINE                       : PX7.2; BM14                        
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488; 0.934                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE; CCD                   
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; MARRESEARCH           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67669                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.470                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 1.5M LITHIUM SULFATE, PH       
REMARK 280  6.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.76650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 BIOLOGICAL UNIT IS A DIMER. THE ASSYMMMETRIC UNIT        
REMARK 300 CONTAINS TWO DIMERS.                                                 
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: 5870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 5700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27690 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ILE A   353                                                      
REMARK 465     GLU A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     TYR A   357                                                      
REMARK 465     GLU A   358                                                      
REMARK 465     GLY A   359                                                      
REMARK 465     ARG A   360                                                      
REMARK 465     GLN A   361                                                      
REMARK 465     ILE B   353                                                      
REMARK 465     GLU B   354                                                      
REMARK 465     GLN B   355                                                      
REMARK 465     ASN B   356                                                      
REMARK 465     TYR B   357                                                      
REMARK 465     GLU B   358                                                      
REMARK 465     GLY B   359                                                      
REMARK 465     ARG B   360                                                      
REMARK 465     GLN B   361                                                      
REMARK 465     ILE C   353                                                      
REMARK 465     GLU C   354                                                      
REMARK 465     GLN C   355                                                      
REMARK 465     ASN C   356                                                      
REMARK 465     TYR C   357                                                      
REMARK 465     GLU C   358                                                      
REMARK 465     GLY C   359                                                      
REMARK 465     ARG C   360                                                      
REMARK 465     GLN C   361                                                      
REMARK 465     ILE D   353                                                      
REMARK 465     GLU D   354                                                      
REMARK 465     GLN D   355                                                      
REMARK 465     ASN D   356                                                      
REMARK 465     TYR D   357                                                      
REMARK 465     GLU D   358                                                      
REMARK 465     GLY D   359                                                      
REMARK 465     ARG D   360                                                      
REMARK 465     GLN D   361                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     THR B    91                                                      
REMARK 475     PRO C   298                                                      
REMARK 475     GLY D   299                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ILE A    5   CD1                                                 
REMARK 480     ILE A   20   CG2                                                 
REMARK 480     ILE A   46   CD1                                                 
REMARK 480     ILE A   90   C    O    CG1  CG2  CD1                             
REMARK 480     THR A   91   N    CA   CG2                                       
REMARK 480     GLU A  120   CB                                                  
REMARK 480     ASP A  121   CG   OD1  OD2                                       
REMARK 480     VAL A  146   O    CG1  CG2                                       
REMARK 480     GLU A  147   CB   CG                                             
REMARK 480     SER A  149   C    CB   OG                                        
REMARK 480     LYS A  283   O                                                   
REMARK 480     THR A  285   OG1                                                 
REMARK 480     HIS A  300   C    O    CB   CG   ND1  CD2  CE1                   
REMARK 480     HIS A  300   NE2                                                 
REMARK 480     THR B   27   OG1                                                 
REMARK 480     GLU B   48   OE2                                                 
REMARK 480     SER B   89   O    CB   OG                                        
REMARK 480     HIS B  300   C    O    CB   CG   ND1  CD2  CE1                   
REMARK 480     HIS B  300   NE2                                                 
REMARK 480     GLN C   25   NE2                                                 
REMARK 480     ILE C   90   O                                                   
REMARK 480     THR C   91   CB   OG1  CG2                                       
REMARK 480     VAL C  146   CG1  CG2                                            
REMARK 480     GLU C  147   N                                                   
REMARK 480     VAL C  150   C    O    CB   CG1  CG2                             
REMARK 480     ALA C  284   CB                                                  
REMARK 480     ARG C  297   CB   CG   CD                                        
REMARK 480     GLY C  299   N    CA                                             
REMARK 480     HIS C  300   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLU C  332   C    O    CD   OE1  OE2                             
REMARK 480     LYS D    2   NZ                                                  
REMARK 480     VAL D  146   CG1                                                 
REMARK 480     GLU D  147   N    CA                                             
REMARK 480     SER D  149   OG                                                  
REMARK 480     VAL D  150   N                                                   
REMARK 480     LYS D  226   CE   NZ                                             
REMARK 480     ARG D  297   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     PRO D  298   CA   CB   CG                                        
REMARK 480     HIS D  300   CG   ND1  CD2  CE1  NE2                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU C   277     O    ILE C   280              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 153   C   -  N   -  CD  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    PRO A 163   CA  -  N   -  CD  ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    PRO A 188   C   -  N   -  CD  ANGL. DEV. = -12.7 DEGREES          
REMARK 500    PRO A 298   C   -  N   -  CD  ANGL. DEV. = -13.1 DEGREES          
REMARK 500    PRO B 141   CA  -  N   -  CD  ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    PRO B 163   C   -  N   -  CD  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    PRO B 188   C   -  N   -  CD  ANGL. DEV. = -14.4 DEGREES          
REMARK 500    PRO C 298   C   -  N   -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    PRO D 282   C   -  N   -  CD  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    PRO D 298   C   -  N   -  CD  ANGL. DEV. = -15.4 DEGREES          
REMARK 500    TRP D 352   CA  -  CB  -  CG  ANGL. DEV. = -30.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  45       32.44    -86.95                                   
REMARK 500    ILE A  46      -19.74   -149.12                                   
REMARK 500    GLN A  73       67.08     37.40                                   
REMARK 500    ILE A 101      -68.37    -94.44                                   
REMARK 500    LEU A 118      -99.61    -76.55                                   
REMARK 500    GLU A 120      -57.72    -10.65                                   
REMARK 500    ASN A 148      177.80     46.44                                   
REMARK 500    SER A 149       72.55    -56.28                                   
REMARK 500    VAL A 150      -72.32    -85.79                                   
REMARK 500    THR A 151      134.82    132.21                                   
REMARK 500    ALA A 162       61.86   -162.29                                   
REMARK 500    PRO A 188       73.32    -61.59                                   
REMARK 500    TYR A 224      -88.83    -76.11                                   
REMARK 500    GLN A 229      129.84    -36.70                                   
REMARK 500    VAL A 294     -143.76   -114.29                                   
REMARK 500    ASP B  45       31.64    -92.96                                   
REMARK 500    ILE B  46      -21.39   -146.24                                   
REMARK 500    GLN B  73       68.21     38.89                                   
REMARK 500    ILE B  90      -70.10    -72.71                                   
REMARK 500    THR B  91      -78.03    -46.45                                   
REMARK 500    ILE B 101      -65.48    -99.83                                   
REMARK 500    GLU B 120      -52.62    -17.53                                   
REMARK 500    ASN B 148      130.52      2.84                                   
REMARK 500    SER B 149       50.98     31.25                                   
REMARK 500    ALA B 162       70.90   -162.98                                   
REMARK 500    PRO B 188       68.27    -67.45                                   
REMARK 500    GLN B 229      127.89    -38.42                                   
REMARK 500    ALA B 295      148.56    -18.26                                   
REMARK 500    GLN B 350       30.73    -84.65                                   
REMARK 500    GLN C  73       66.00     39.62                                   
REMARK 500    THR C  91      -86.16    -80.87                                   
REMARK 500    ILE C 101      -68.01    -94.19                                   
REMARK 500    LEU C 118      -84.29    -85.67                                   
REMARK 500    GLU C 120      -53.87    -16.43                                   
REMARK 500    ASP C 121      -71.00    -57.68                                   
REMARK 500    ASN C 148       94.57     37.90                                   
REMARK 500    SER C 149       92.01     39.21                                   
REMARK 500    VAL C 150       70.75   -154.70                                   
REMARK 500    THR C 151      112.80    -13.00                                   
REMARK 500    ALA C 162       52.93   -158.50                                   
REMARK 500    LEU C 207      -70.25    -42.18                                   
REMARK 500    GLN C 229      125.27    -39.36                                   
REMARK 500    PRO C 298       35.97    -65.19                                   
REMARK 500    PHE D  11      -71.25    -50.55                                   
REMARK 500    ASP D  45       33.86    -93.85                                   
REMARK 500    ILE D  46      -23.70   -146.65                                   
REMARK 500    ILE D 101      -74.54    -91.49                                   
REMARK 500    GLU D 120      -49.06    -18.31                                   
REMARK 500    ASP D 121      -70.28    -59.22                                   
REMARK 500    GLU D 145      -50.44   -124.48                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 RAMACHANDRAN OUTLIERS.                        
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 SO4 A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 5007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 5008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 700                 
DBREF  1G1A A    1   361  UNP    P26391   RFBB_SALTY       1    361             
DBREF  1G1A B    1   361  UNP    P26391   RFBB_SALTY       1    361             
DBREF  1G1A C    1   361  UNP    P26391   RFBB_SALTY       1    361             
DBREF  1G1A D    1   361  UNP    P26391   RFBB_SALTY       1    361             
SEQRES   1 A  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 A  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 A  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 A  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 A  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 A  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 A  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 A  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 A  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 A  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 A  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 A  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 A  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 A  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 A  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 A  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 A  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 A  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 A  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 A  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 A  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 A  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 A  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 A  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 A  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 A  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 A  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 A  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
SEQRES   1 B  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 B  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 B  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 B  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 B  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 B  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 B  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 B  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 B  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 B  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 B  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 B  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 B  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 B  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 B  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 B  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 B  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 B  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 B  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 B  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 B  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 B  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 B  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 B  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 B  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 B  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 B  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 B  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
SEQRES   1 C  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 C  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 C  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 C  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 C  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 C  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 C  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 C  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 C  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 C  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 C  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 C  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 C  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 C  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 C  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 C  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 C  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 C  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 C  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 C  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 C  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 C  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 C  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 C  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 C  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 C  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 C  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 C  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
SEQRES   1 D  361  MET LYS ILE LEU ILE THR GLY GLY ALA GLY PHE ILE GLY          
SEQRES   2 D  361  SER ALA VAL VAL ARG HIS ILE ILE LYS ASN THR GLN ASP          
SEQRES   3 D  361  THR VAL VAL ASN ILE ASP LYS LEU THR TYR ALA GLY ASN          
SEQRES   4 D  361  LEU GLU SER LEU SER ASP ILE SER GLU SER ASN ARG TYR          
SEQRES   5 D  361  ASN PHE GLU HIS ALA ASP ILE CYS ASP SER ALA GLU ILE          
SEQRES   6 D  361  THR ARG ILE PHE GLU GLN TYR GLN PRO ASP ALA VAL MET          
SEQRES   7 D  361  HIS LEU ALA ALA GLU SER HIS VAL ASP ARG SER ILE THR          
SEQRES   8 D  361  GLY PRO ALA ALA PHE ILE GLU THR ASN ILE VAL GLY THR          
SEQRES   9 D  361  TYR ALA LEU LEU GLU VAL ALA ARG LYS TYR TRP SER ALA          
SEQRES  10 D  361  LEU GLY GLU ASP LYS LYS ASN ASN PHE ARG PHE HIS HIS          
SEQRES  11 D  361  ILE SER THR ASP GLU VAL TYR GLY ASP LEU PRO HIS PRO          
SEQRES  12 D  361  ASP GLU VAL GLU ASN SER VAL THR LEU PRO LEU PHE THR          
SEQRES  13 D  361  GLU THR THR ALA TYR ALA PRO SER SER PRO TYR SER ALA          
SEQRES  14 D  361  SER LYS ALA SER SER ASP HIS LEU VAL ARG ALA TRP ARG          
SEQRES  15 D  361  ARG THR TYR GLY LEU PRO THR ILE VAL THR ASN CYS SER          
SEQRES  16 D  361  ASN ASN TYR GLY PRO TYR HIS PHE PRO GLU LYS LEU ILE          
SEQRES  17 D  361  PRO LEU VAL ILE LEU ASN ALA LEU GLU GLY LYS PRO LEU          
SEQRES  18 D  361  PRO ILE TYR GLY LYS GLY ASP GLN ILE ARG ASP TRP LEU          
SEQRES  19 D  361  TYR VAL GLU ASP HIS ALA ARG ALA LEU HIS MET VAL VAL          
SEQRES  20 D  361  THR GLU GLY LYS ALA GLY GLU THR TYR ASN ILE GLY GLY          
SEQRES  21 D  361  HIS ASN GLU LYS LYS ASN LEU ASP VAL VAL PHE THR ILE          
SEQRES  22 D  361  CYS ASP LEU LEU ASP GLU ILE VAL PRO LYS ALA THR SER          
SEQRES  23 D  361  TYR ARG GLU GLN ILE THR TYR VAL ALA ASP ARG PRO GLY          
SEQRES  24 D  361  HIS ASP ARG ARG TYR ALA ILE ASP ALA GLY LYS ILE SER          
SEQRES  25 D  361  ARG GLU LEU GLY TRP LYS PRO LEU GLU THR PHE GLU SER          
SEQRES  26 D  361  GLY ILE ARG LYS THR VAL GLU TRP TYR LEU ALA ASN THR          
SEQRES  27 D  361  GLN TRP VAL ASN ASN VAL LYS SER GLY ALA TYR GLN SER          
SEQRES  28 D  361  TRP ILE GLU GLN ASN TYR GLU GLY ARG GLN                      
HET    SO4  A5001       5                                                       
HET    SO4  A5005       5                                                       
HET    NAD  A 400      44                                                       
HET    SO4  B5002       5                                                       
HET    SO4  B5006       5                                                       
HET    SO4  B5009       5                                                       
HET    NAD  B 500      44                                                       
HET    SO4  C5003       5                                                       
HET    SO4  C5007       5                                                       
HET    NAD  C 600      44                                                       
HET    SO4  D5004       5                                                       
HET    SO4  D5008       5                                                       
HET    NAD  D 700      44                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
FORMUL   5  SO4    9(O4 S 2-)                                                   
FORMUL   7  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL  18  HOH   *512(H2 O)                                                    
HELIX    1   1 GLY A   10  THR A   24  1                                  15    
HELIX    2   2 ASN A   39  SER A   44  5                                   6    
HELIX    3   3 ASP A   61  GLN A   73  1                                  13    
HELIX    4   4 ALA A   94  ILE A  101  1                                   8    
HELIX    5   5 ILE A  101  ALA A  117  1                                  17    
HELIX    6   6 GLY A  119  PHE A  126  1                                   8    
HELIX    7   7 GLU A  135  GLY A  138  5                                   4    
HELIX    8   8 SER A  165  GLY A  186  1                                  22    
HELIX    9   9 LYS A  206  GLU A  217  1                                  12    
HELIX   10  10 VAL A  236  GLY A  250  1                                  15    
HELIX   11  11 ASN A  266  ILE A  280  1                                  15    
HELIX   12  12 SER A  286  GLU A  289  5                                   4    
HELIX   13  13 ALA A  308  GLY A  316  1                                   9    
HELIX   14  14 THR A  322  ALA A  336  1                                  15    
HELIX   15  15 ASN A  337  GLY A  347  1                                  11    
HELIX   16  16 ALA A  348  TRP A  352  5                                   5    
HELIX   17  17 GLY B   10  THR B   24  1                                  15    
HELIX   18  18 ASN B   39  SER B   44  5                                   6    
HELIX   19  19 ASP B   61  GLN B   73  1                                  13    
HELIX   20  20 ALA B   94  ILE B  101  1                                   8    
HELIX   21  21 ILE B  101  ALA B  117  1                                  17    
HELIX   22  22 GLY B  119  PHE B  126  1                                   8    
HELIX   23  23 GLU B  135  GLY B  138  5                                   4    
HELIX   24  24 SER B  165  GLY B  186  1                                  22    
HELIX   25  25 LYS B  206  GLU B  217  1                                  12    
HELIX   26  26 VAL B  236  GLY B  250  1                                  15    
HELIX   27  27 ASN B  266  ILE B  280  1                                  15    
HELIX   28  28 SER B  286  GLU B  289  5                                   4    
HELIX   29  29 ALA B  308  GLY B  316  1                                   9    
HELIX   30  30 THR B  322  ASN B  337  1                                  16    
HELIX   31  31 ASN B  337  GLY B  347  1                                  11    
HELIX   32  32 ALA B  348  TRP B  352  5                                   5    
HELIX   33  33 GLY C   10  THR C   24  1                                  15    
HELIX   34  34 ASN C   39  SER C   44  5                                   6    
HELIX   35  35 ASP C   61  GLN C   73  1                                  13    
HELIX   36  36 ALA C   94  ILE C  101  1                                   8    
HELIX   37  37 ILE C  101  ALA C  117  1                                  17    
HELIX   38  38 GLY C  119  PHE C  126  1                                   8    
HELIX   39  39 GLU C  135  GLY C  138  5                                   4    
HELIX   40  40 SER C  165  GLY C  186  1                                  22    
HELIX   41  41 LYS C  206  GLY C  218  1                                  13    
HELIX   42  42 VAL C  236  GLY C  250  1                                  15    
HELIX   43  43 ASN C  266  ILE C  280  1                                  15    
HELIX   44  44 TYR C  287  GLU C  289  5                                   3    
HELIX   45  45 ALA C  308  GLY C  316  1                                   9    
HELIX   46  46 THR C  322  ASN C  337  1                                  16    
HELIX   47  47 ASN C  337  GLY C  347  1                                  11    
HELIX   48  48 ALA C  348  TRP C  352  5                                   5    
HELIX   49  49 GLY D   10  THR D   24  1                                  15    
HELIX   50  50 ASN D   39  SER D   44  5                                   6    
HELIX   51  51 ASP D   61  GLN D   73  1                                  13    
HELIX   52  52 ALA D   94  ILE D  101  1                                   8    
HELIX   53  53 ILE D  101  ALA D  117  1                                  17    
HELIX   54  54 GLY D  119  PHE D  126  1                                   8    
HELIX   55  55 GLU D  135  GLY D  138  5                                   4    
HELIX   56  56 HIS D  142  GLU D  147  1                                   6    
HELIX   57  57 SER D  165  GLY D  186  1                                  22    
HELIX   58  58 LYS D  206  GLU D  217  1                                  12    
HELIX   59  59 VAL D  236  GLY D  250  1                                  15    
HELIX   60  60 ASN D  266  ILE D  280  1                                  15    
HELIX   61  61 SER D  286  GLU D  289  5                                   4    
HELIX   62  62 ALA D  308  GLY D  316  1                                   9    
HELIX   63  63 THR D  322  ASN D  337  1                                  16    
HELIX   64  64 ASN D  337  GLY D  347  1                                  11    
HELIX   65  65 ALA D  348  SER D  351  5                                   4    
SHEET    1   A 7 TYR A  52  GLU A  55  0                                        
SHEET    2   A 7 THR A  27  ILE A  31  1  O  VAL A  28   N  ASN A  53           
SHEET    3   A 7 LYS A   2  THR A   6  1  N  ILE A   3   O  THR A  27           
SHEET    4   A 7 ALA A  76  HIS A  79  1  O  ALA A  76   N  LEU A   4           
SHEET    5   A 7 ARG A 127  THR A 133  1  O  ARG A 127   N  VAL A  77           
SHEET    6   A 7 THR A 189  CYS A 194  1  O  ILE A 190   N  HIS A 130           
SHEET    7   A 7 THR A 255  ILE A 258  1  N  TYR A 256   O  VAL A 191           
SHEET    1   B 2 ASN A 196  TYR A 198  0                                        
SHEET    2   B 2 TRP A 233  TYR A 235  1  N  LEU A 234   O  ASN A 196           
SHEET    1   C 2 LEU A 221  ILE A 223  0                                        
SHEET    2   C 2 ILE A 291  TYR A 293  1  N  THR A 292   O  LEU A 221           
SHEET    1   D 2 ILE A 230  ARG A 231  0                                        
SHEET    2   D 2 LYS A 264  LYS A 265 -1  O  LYS A 264   N  ARG A 231           
SHEET    1   E 7 TYR B  52  GLU B  55  0                                        
SHEET    2   E 7 THR B  27  ILE B  31  1  O  VAL B  28   N  ASN B  53           
SHEET    3   E 7 LYS B   2  THR B   6  1  N  ILE B   3   O  THR B  27           
SHEET    4   E 7 ALA B  76  HIS B  79  1  O  ALA B  76   N  LEU B   4           
SHEET    5   E 7 ARG B 127  THR B 133  1  O  ARG B 127   N  VAL B  77           
SHEET    6   E 7 THR B 189  CYS B 194  1  O  ILE B 190   N  HIS B 130           
SHEET    7   E 7 THR B 255  ILE B 258  1  N  TYR B 256   O  VAL B 191           
SHEET    1   F 2 ASN B 196  TYR B 198  0                                        
SHEET    2   F 2 TRP B 233  TYR B 235  1  N  LEU B 234   O  ASN B 196           
SHEET    1   G 2 LEU B 221  TYR B 224  0                                        
SHEET    2   G 2 ILE B 291  VAL B 294  1  N  THR B 292   O  LEU B 221           
SHEET    1   H 2 ILE B 230  ARG B 231  0                                        
SHEET    2   H 2 LYS B 264  LYS B 265 -1  N  LYS B 264   O  ARG B 231           
SHEET    1   I 7 TYR C  52  GLU C  55  0                                        
SHEET    2   I 7 THR C  27  ILE C  31  1  O  VAL C  28   N  ASN C  53           
SHEET    3   I 7 LYS C   2  THR C   6  1  N  ILE C   3   O  THR C  27           
SHEET    4   I 7 ALA C  76  HIS C  79  1  O  ALA C  76   N  LEU C   4           
SHEET    5   I 7 ARG C 127  THR C 133  1  O  ARG C 127   N  VAL C  77           
SHEET    6   I 7 THR C 189  CYS C 194  1  O  ILE C 190   N  HIS C 130           
SHEET    7   I 7 THR C 255  ILE C 258  1  N  TYR C 256   O  VAL C 191           
SHEET    1   J 2 ASN C 197  TYR C 198  0                                        
SHEET    2   J 2 LEU C 234  TYR C 235  1  O  LEU C 234   N  TYR C 198           
SHEET    1   K 2 LEU C 221  TYR C 224  0                                        
SHEET    2   K 2 ILE C 291  VAL C 294  1  N  THR C 292   O  LEU C 221           
SHEET    1   L 2 ILE C 230  ARG C 231  0                                        
SHEET    2   L 2 LYS C 264  LYS C 265 -1  N  LYS C 264   O  ARG C 231           
SHEET    1   M 7 TYR D  52  HIS D  56  0                                        
SHEET    2   M 7 THR D  27  ASP D  32  1  O  VAL D  28   N  ASN D  53           
SHEET    3   M 7 LYS D   2  THR D   6  1  N  ILE D   3   O  THR D  27           
SHEET    4   M 7 ALA D  76  HIS D  79  1  O  ALA D  76   N  LEU D   4           
SHEET    5   M 7 ARG D 127  THR D 133  1  O  ARG D 127   N  VAL D  77           
SHEET    6   M 7 THR D 189  CYS D 194  1  O  ILE D 190   N  HIS D 130           
SHEET    7   M 7 THR D 255  ILE D 258  1  N  TYR D 256   O  VAL D 191           
SHEET    1   N 2 ASN D 196  TYR D 198  0                                        
SHEET    2   N 2 TRP D 233  TYR D 235  1  N  LEU D 234   O  ASN D 196           
SHEET    1   O 2 LEU D 221  ILE D 223  0                                        
SHEET    2   O 2 ILE D 291  TYR D 293  1  O  THR D 292   N  ILE D 223           
SHEET    1   P 2 ILE D 230  ARG D 231  0                                        
SHEET    2   P 2 LYS D 264  LYS D 265 -1  N  LYS D 264   O  ARG D 231           
SITE     1 AC1  4 HIS A 202  LYS A 206  NAD A 400  HOH A5097                    
SITE     1 AC2  7 HIS B 202  LYS B 206  NAD B 500  HOH B5063                    
SITE     2 AC2  7 HOH B5066  HOH B5100  HOH B5171                               
SITE     1 AC3  4 HIS C 202  LYS C 206  NAD C 600  HOH C5094                    
SITE     1 AC4  6 HIS D 202  LYS D 206  NAD D 700  HOH D5093                    
SITE     2 AC4  6 HOH D5118  HOH D5124                                          
SITE     1 AC5  2 THR A 159  ALA A 160                                          
SITE     1 AC6  3 THR B 159  ALA B 160  HOH B5138                               
SITE     1 AC7  2 THR C 159  ALA C 160                                          
SITE     1 AC8  3 THR D 159  ALA D 160  HOH D5031                               
SITE     1 AC9  5 LYS B 264  THR B 322  PHE B 323  GLU B 324                    
SITE     2 AC9  5 HOH B5116                                                     
SITE     1 BC1 33 GLY A   7  ALA A   9  GLY A  10  PHE A  11                    
SITE     2 BC1 33 ILE A  12  ASP A  32  LYS A  33  LEU A  34                    
SITE     3 BC1 33 THR A  35  ALA A  37  GLY A  38  ALA A  57                    
SITE     4 BC1 33 ASP A  58  ILE A  59  LEU A  80  ALA A  82                    
SITE     5 BC1 33 THR A  99  ILE A 131  SER A 132  THR A 133                    
SITE     6 BC1 33 TYR A 167  LYS A 171  CYS A 194  SER A 195                    
SITE     7 BC1 33 ASN A 197  SO4 A5001  HOH A5010  HOH A5013                    
SITE     8 BC1 33 HOH A5014  HOH A5020  HOH A5031  HOH A5060                    
SITE     9 BC1 33 HOH A5098                                                     
SITE     1 BC2 33 GLY B   7  ALA B   9  GLY B  10  PHE B  11                    
SITE     2 BC2 33 ILE B  12  ASP B  32  LYS B  33  LEU B  34                    
SITE     3 BC2 33 THR B  35  ALA B  37  GLY B  38  ALA B  57                    
SITE     4 BC2 33 ASP B  58  ILE B  59  LEU B  80  ALA B  81                    
SITE     5 BC2 33 ALA B  82  THR B  99  ILE B 131  SER B 132                    
SITE     6 BC2 33 THR B 133  TYR B 167  LYS B 171  CYS B 194                    
SITE     7 BC2 33 SER B 195  ASN B 196  ASN B 197  SO4 B5002                    
SITE     8 BC2 33 HOH B5019  HOH B5025  HOH B5045  HOH B5063                    
SITE     9 BC2 33 HOH B5073                                                     
SITE     1 BC3 34 GLY C   7  ALA C   9  GLY C  10  PHE C  11                    
SITE     2 BC3 34 ILE C  12  ASP C  32  LYS C  33  LEU C  34                    
SITE     3 BC3 34 THR C  35  ALA C  37  GLY C  38  ALA C  57                    
SITE     4 BC3 34 ASP C  58  ILE C  59  LEU C  80  ALA C  81                    
SITE     5 BC3 34 ALA C  82  THR C  99  ILE C 131  SER C 132                    
SITE     6 BC3 34 THR C 133  TYR C 167  LYS C 171  CYS C 194                    
SITE     7 BC3 34 SER C 195  ASN C 197  SO4 C5003  HOH C5026                    
SITE     8 BC3 34 HOH C5034  HOH C5045  HOH C5052  HOH C5058                    
SITE     9 BC3 34 HOH C5081  HOH C5094                                          
SITE     1 BC4 35 GLY D   7  ALA D   9  GLY D  10  PHE D  11                    
SITE     2 BC4 35 ILE D  12  ASP D  32  LYS D  33  LEU D  34                    
SITE     3 BC4 35 THR D  35  ALA D  37  GLY D  38  ALA D  57                    
SITE     4 BC4 35 ASP D  58  ILE D  59  LEU D  80  ALA D  81                    
SITE     5 BC4 35 ALA D  82  THR D  99  ILE D 131  SER D 132                    
SITE     6 BC4 35 THR D 133  TYR D 167  LYS D 171  CYS D 194                    
SITE     7 BC4 35 SER D 195  ASN D 197  SO4 D5004  HOH D5012                    
SITE     8 BC4 35 HOH D5019  HOH D5025  HOH D5027  HOH D5049                    
SITE     9 BC4 35 HOH D5055  HOH D5093  HOH D5124                               
CRYST1  110.623   87.533  111.304  90.00  98.04  90.00 P 1 21 1      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      0.009040  0.000000  0.001277        0.00000                         
SCALE2      0.000000  0.011424  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009074        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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