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Database: PDB
Entry: 4K2M
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Original site: 4K2M 
HEADER    TRANSFERASE                             09-APR-13   4K2M              
TITLE     CRYSTAL STRUCTURE OF NTDA FROM BACILLUS SUBTILIS IN COMPLEX WITH THE  
TITLE    2 PLP EXTERNAL ALDIMINE ADDUCT WITH KANOSAMINE-6-PHOSPHATE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NTD BIOSYNTHESIS OPERON PROTEIN NTDA;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: 939788, BSU10550, NP_388936.1, NTDA, YHJL;                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    SUGAR AMINOTRANSFERASE, ASPERTATE AMINOTRANSFERASE FOLD, HOMO-DIMER,  
KEYWDS   2 ADDITIONAL N-TERNINAL DOMAIN, 3-KETO-GLUCOSE-6-PHOSPHATE             
KEYWDS   3 AMINITRANSFERASE, KANOSAMINE-6-PHOSPHATE, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.E.VAN STRAATEN,D.R.J.PALMER,D.A.R.SANDERS                           
REVDAT   4   29-JUL-20 4K2M    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   01-JAN-14 4K2M    1       JRNL                                     
REVDAT   2   23-OCT-13 4K2M    1       JRNL                                     
REVDAT   1   16-OCT-13 4K2M    0                                                
JRNL        AUTH   K.E.VAN STRAATEN,J.B.KO,R.JAGDHANE,S.ANJUM,D.R.PALMER,       
JRNL        AUTH 2 D.A.SANDERS                                                  
JRNL        TITL   THE STRUCTURE OF NTDA, A SUGAR AMINOTRANSFERASE INVOLVED IN  
JRNL        TITL 2 THE KANOSAMINE BIOSYNTHETIC PATHWAY IN BACILLUS SUBTILIS,    
JRNL        TITL 3 REVEALS A NEW SUBCLASS OF AMINOTRANSFERASES.                 
JRNL        REF    J.BIOL.CHEM.                  V. 288 34121 2013              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   24097983                                                     
JRNL        DOI    10.1074/JBC.M113.500637                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.73                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 108734                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.186                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5437                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.7450 -  5.3107    0.99     3542   187  0.1700 0.2065        
REMARK   3     2  5.3107 -  4.2161    1.00     3485   184  0.1358 0.1666        
REMARK   3     3  4.2161 -  3.6834    1.00     3487   183  0.1267 0.1530        
REMARK   3     4  3.6834 -  3.3468    1.00     3457   182  0.1430 0.1657        
REMARK   3     5  3.3468 -  3.1069    1.00     3457   182  0.1454 0.1868        
REMARK   3     6  3.1069 -  2.9238    1.00     3461   182  0.1467 0.1705        
REMARK   3     7  2.9238 -  2.7774    1.00     3475   183  0.1476 0.1693        
REMARK   3     8  2.7774 -  2.6565    1.00     3474   183  0.1396 0.1810        
REMARK   3     9  2.6565 -  2.5542    1.00     3463   182  0.1469 0.1756        
REMARK   3    10  2.5542 -  2.4661    1.00     3445   181  0.1464 0.1725        
REMARK   3    11  2.4661 -  2.3890    1.00     3462   183  0.1497 0.2052        
REMARK   3    12  2.3890 -  2.3207    1.00     3459   182  0.1476 0.1816        
REMARK   3    13  2.3207 -  2.2596    1.00     3386   178  0.1449 0.1823        
REMARK   3    14  2.2596 -  2.2045    1.00     3514   185  0.1467 0.1841        
REMARK   3    15  2.2045 -  2.1544    1.00     3425   180  0.1455 0.1836        
REMARK   3    16  2.1544 -  2.1085    0.99     3453   182  0.1477 0.1937        
REMARK   3    17  2.1085 -  2.0663    0.99     3406   179  0.1487 0.1924        
REMARK   3    18  2.0663 -  2.0273    0.99     3477   183  0.1516 0.1894        
REMARK   3    19  2.0273 -  1.9911    0.99     3375   178  0.1502 0.1786        
REMARK   3    20  1.9911 -  1.9574    0.99     3475   183  0.1525 0.1892        
REMARK   3    21  1.9574 -  1.9258    0.99     3388   178  0.1701 0.2120        
REMARK   3    22  1.9258 -  1.8962    0.99     3444   181  0.1642 0.2164        
REMARK   3    23  1.8962 -  1.8683    0.99     3421   180  0.1704 0.1985        
REMARK   3    24  1.8683 -  1.8420    0.99     3393   179  0.1714 0.2139        
REMARK   3    25  1.8420 -  1.8171    0.99     3465   182  0.1916 0.2178        
REMARK   3    26  1.8171 -  1.7935    0.99     3417   180  0.1990 0.2595        
REMARK   3    27  1.7935 -  1.7711    0.99     3382   178  0.2093 0.2628        
REMARK   3    28  1.7711 -  1.7497    0.99     3418   180  0.2141 0.2552        
REMARK   3    29  1.7497 -  1.7294    0.98     3394   179  0.2233 0.2389        
REMARK   3    30  1.7294 -  1.7099    0.98     3397   178  0.2391 0.2726        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 60.24                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.42                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.64990                                              
REMARK   3    B22 (A**2) : -5.94020                                             
REMARK   3    B33 (A**2) : 2.29030                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.90370                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           7420                                  
REMARK   3   ANGLE     :  1.130          10041                                  
REMARK   3   CHIRALITY :  0.079           1122                                  
REMARK   3   PLANARITY :  0.005           1287                                  
REMARK   3   DIHEDRAL  : 13.902           2809                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4K2M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-APR-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000078812.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : DCM                                
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108740                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.2800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.75500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.140                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4K2B                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRI-SODIUM CITRATE PH 5.6, 0.2M     
REMARK 280  AMMONIUM ACETATE, 10-30% PEG3350, MICROBATCH, TEMPERATURE 295K      
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       53.22000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMO-DIMER                      
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: 7420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   441                                                      
REMARK 465     ALA B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     VAL B   441                                                      
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  70       79.95   -153.90                                   
REMARK 500    THR A  98      -85.03   -101.78                                   
REMARK 500    THR A  98      -83.01   -101.78                                   
REMARK 500    VAL A 251     -153.36   -104.73                                   
REMARK 500    CYS A 252       52.41   -117.87                                   
REMARK 500    ASN A 283       -4.85     78.05                                   
REMARK 500    ASN A 292       77.27   -105.01                                   
REMARK 500    ASP A 345       48.09   -107.37                                   
REMARK 500    LEU A 415      113.73   -161.07                                   
REMARK 500    ASP B  24       78.68   -104.08                                   
REMARK 500    LEU B  70       76.44   -154.20                                   
REMARK 500    THR B  98      -81.84   -102.70                                   
REMARK 500    THR B  98      -81.06   -102.70                                   
REMARK 500    VAL B 251     -150.63   -101.60                                   
REMARK 500    CYS B 252       51.89   -119.18                                   
REMARK 500    ASN B 280       19.29     58.48                                   
REMARK 500    ASN B 283       -3.63     79.41                                   
REMARK 500    ASN B 292       77.57   -106.49                                   
REMARK 500    ASP B 345       47.99    -99.66                                   
REMARK 500    LEU B 415      115.33   -164.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4K2B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NTDA FROM BACILLUS SUBTILIS IN COMPLEX WITH     
REMARK 900 THE INTERNAL ALDIMINE                                                
REMARK 900 RELATED ID: 4K2I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF NTDA FROM BACILLUS SUBTILIS WITH BOUND          
REMARK 900 COFACTOR PMP                                                         
DBREF  4K2M A    1   441  UNP    O07566   NTDA_BACSU       1    441             
DBREF  4K2M B    1   441  UNP    O07566   NTDA_BACSU       1    441             
SEQADV 4K2M ALA A   -1  UNP  O07566              EXPRESSION TAG                 
SEQADV 4K2M GLY A    0  UNP  O07566              EXPRESSION TAG                 
SEQADV 4K2M ALA B   -1  UNP  O07566              EXPRESSION TAG                 
SEQADV 4K2M GLY B    0  UNP  O07566              EXPRESSION TAG                 
SEQRES   1 A  443  ALA GLY MET GLN LYS GLN VAL LYS ILE SER GLY LYS SER          
SEQRES   2 A  443  LYS GLU ASN MET SER LEU LEU LYS HIS LEU LYS GLY ASP          
SEQRES   3 A  443  VAL GLN GLY LYS GLU LEU VAL ILE GLU ASP SER ILE VAL          
SEQRES   4 A  443  ASN GLU ARG TRP LYS GLN VAL LEU LYS GLU LYS ILE ASP          
SEQRES   5 A  443  ILE GLU HIS ASP LEU PHE ASN TYR GLN LYS ASN ARG GLU          
SEQRES   6 A  443  ILE SER LYS VAL PRO PHE LEU PRO VAL ASP ARG LEU ILE          
SEQRES   7 A  443  THR ASN ASP GLU VAL GLU ASP ILE LEU ASN THR LEU THR          
SEQRES   8 A  443  GLU VAL LEU PRO THR GLY LYS PHE THR SER GLY PRO TYR          
SEQRES   9 A  443  LEU GLU GLN PHE GLU LYS VAL LEU SER THR TYR LEU HIS          
SEQRES  10 A  443  LYS ARG TYR VAL ILE ALA THR SER SER GLY THR ASP ALA          
SEQRES  11 A  443  ILE MET ILE GLY LEU LEU ALA LEU GLY LEU ASN PRO GLY          
SEQRES  12 A  443  ASP GLU VAL ILE MET PRO ALA ASN SER PHE SER ALA THR          
SEQRES  13 A  443  GLU ASN ALA VAL LEU ALA SER GLY GLY VAL PRO ILE TYR          
SEQRES  14 A  443  VAL ASP ILE ASN PRO GLN THR PHE CYS ILE ASP PRO ASP          
SEQRES  15 A  443  LYS ILE GLU GLU ALA ILE THR PRO TYR THR LYS PHE ILE          
SEQRES  16 A  443  LEU PRO VAL HIS LEU TYR GLY LYS HIS SER ASP MET GLN          
SEQRES  17 A  443  HIS ILE ARG GLN ILE ALA ASN ARG TYR LYS LEU LYS VAL          
SEQRES  18 A  443  ILE GLU ASP ALA CYS GLN GLY ILE GLY LEU THR ASP LEU          
SEQRES  19 A  443  GLY LYS TYR ALA ASP ILE THR THR LEU SER PHE ASN PRO          
SEQRES  20 A  443  TYR LYS ASN PHE GLY VAL CYS GLY LYS ALA GLY ALA ILE          
SEQRES  21 A  443  ALA THR ASP ASN GLU GLU LEU ALA LYS LYS CYS ILE GLN          
SEQRES  22 A  443  PHE SER TYR HIS GLY PHE GLU VAL ASN VAL LYS ASN LYS          
SEQRES  23 A  443  LYS VAL ILE ASN PHE GLY PHE ASN SER LYS MET ASP ASN          
SEQRES  24 A  443  LEU GLN ALA ALA ILE GLY LEU GLU ARG MET LYS TYR LEU          
SEQRES  25 A  443  SER LEU ASN ASN PHE LYS ARG LEU PHE LEU ALA ASP ARG          
SEQRES  26 A  443  TYR ILE THR GLN LEU ALA GLU LEU GLN ASN LYS GLY TYR          
SEQRES  27 A  443  ILE GLU LEU PRO GLU LEU SER GLU ASP HIS VAL TRP HIS          
SEQRES  28 A  443  LEU PHE PRO ILE LYS VAL ARG THR GLU ASP ARG ALA ASP          
SEQRES  29 A  443  ILE MET THR LYS LEU ASN GLU ASP PHE GLY VAL GLN THR          
SEQRES  30 A  443  ASP VAL TYR TYR PRO ILE LEU SER HIS MET GLN LYS THR          
SEQRES  31 A  443  PRO LEU VAL GLN ASP LYS TYR ALA GLY LEU GLN LEU VAL          
SEQRES  32 A  443  HIS THR GLU LYS ALA HIS SER GLN VAL LEU HIS LEU PRO          
SEQRES  33 A  443  LEU TYR PRO SER PHE THR LEU GLU GLU GLN ASP ARG VAL          
SEQRES  34 A  443  MET GLU GLY LEU PHE HIS VAL ILE LYS GLN GLU ILE GLY          
SEQRES  35 A  443  VAL                                                          
SEQRES   1 B  443  ALA GLY MET GLN LYS GLN VAL LYS ILE SER GLY LYS SER          
SEQRES   2 B  443  LYS GLU ASN MET SER LEU LEU LYS HIS LEU LYS GLY ASP          
SEQRES   3 B  443  VAL GLN GLY LYS GLU LEU VAL ILE GLU ASP SER ILE VAL          
SEQRES   4 B  443  ASN GLU ARG TRP LYS GLN VAL LEU LYS GLU LYS ILE ASP          
SEQRES   5 B  443  ILE GLU HIS ASP LEU PHE ASN TYR GLN LYS ASN ARG GLU          
SEQRES   6 B  443  ILE SER LYS VAL PRO PHE LEU PRO VAL ASP ARG LEU ILE          
SEQRES   7 B  443  THR ASN ASP GLU VAL GLU ASP ILE LEU ASN THR LEU THR          
SEQRES   8 B  443  GLU VAL LEU PRO THR GLY LYS PHE THR SER GLY PRO TYR          
SEQRES   9 B  443  LEU GLU GLN PHE GLU LYS VAL LEU SER THR TYR LEU HIS          
SEQRES  10 B  443  LYS ARG TYR VAL ILE ALA THR SER SER GLY THR ASP ALA          
SEQRES  11 B  443  ILE MET ILE GLY LEU LEU ALA LEU GLY LEU ASN PRO GLY          
SEQRES  12 B  443  ASP GLU VAL ILE MET PRO ALA ASN SER PHE SER ALA THR          
SEQRES  13 B  443  GLU ASN ALA VAL LEU ALA SER GLY GLY VAL PRO ILE TYR          
SEQRES  14 B  443  VAL ASP ILE ASN PRO GLN THR PHE CYS ILE ASP PRO ASP          
SEQRES  15 B  443  LYS ILE GLU GLU ALA ILE THR PRO TYR THR LYS PHE ILE          
SEQRES  16 B  443  LEU PRO VAL HIS LEU TYR GLY LYS HIS SER ASP MET GLN          
SEQRES  17 B  443  HIS ILE ARG GLN ILE ALA ASN ARG TYR LYS LEU LYS VAL          
SEQRES  18 B  443  ILE GLU ASP ALA CYS GLN GLY ILE GLY LEU THR ASP LEU          
SEQRES  19 B  443  GLY LYS TYR ALA ASP ILE THR THR LEU SER PHE ASN PRO          
SEQRES  20 B  443  TYR LYS ASN PHE GLY VAL CYS GLY LYS ALA GLY ALA ILE          
SEQRES  21 B  443  ALA THR ASP ASN GLU GLU LEU ALA LYS LYS CYS ILE GLN          
SEQRES  22 B  443  PHE SER TYR HIS GLY PHE GLU VAL ASN VAL LYS ASN LYS          
SEQRES  23 B  443  LYS VAL ILE ASN PHE GLY PHE ASN SER LYS MET ASP ASN          
SEQRES  24 B  443  LEU GLN ALA ALA ILE GLY LEU GLU ARG MET LYS TYR LEU          
SEQRES  25 B  443  SER LEU ASN ASN PHE LYS ARG LEU PHE LEU ALA ASP ARG          
SEQRES  26 B  443  TYR ILE THR GLN LEU ALA GLU LEU GLN ASN LYS GLY TYR          
SEQRES  27 B  443  ILE GLU LEU PRO GLU LEU SER GLU ASP HIS VAL TRP HIS          
SEQRES  28 B  443  LEU PHE PRO ILE LYS VAL ARG THR GLU ASP ARG ALA ASP          
SEQRES  29 B  443  ILE MET THR LYS LEU ASN GLU ASP PHE GLY VAL GLN THR          
SEQRES  30 B  443  ASP VAL TYR TYR PRO ILE LEU SER HIS MET GLN LYS THR          
SEQRES  31 B  443  PRO LEU VAL GLN ASP LYS TYR ALA GLY LEU GLN LEU VAL          
SEQRES  32 B  443  HIS THR GLU LYS ALA HIS SER GLN VAL LEU HIS LEU PRO          
SEQRES  33 B  443  LEU TYR PRO SER PHE THR LEU GLU GLU GLN ASP ARG VAL          
SEQRES  34 B  443  MET GLU GLY LEU PHE HIS VAL ILE LYS GLN GLU ILE GLY          
SEQRES  35 B  443  VAL                                                          
HET    O1G  A 501      31                                                       
HET    EDO  A 502       4                                                       
HET    EDO  A 503       4                                                       
HET    ACT  A 504       4                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET    O1G  B 501      31                                                       
HET    EDO  B 502       4                                                       
HET    ACT  B 503       4                                                       
HET    ACT  B 504       4                                                       
HET    EDO  B 505       4                                                       
HET    EDO  B 506       4                                                       
HETNAM     O1G 3-DEOXY-3-[(E)-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)            
HETNAM   2 O1G  METHYL]PYRIDIN-4-YL}METHYLIDENE)AMINO]-6-O-PHOSPHONO-           
HETNAM   3 O1G  ALPHA-D-GLUCO PYRANOSE                                          
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ACT ACETATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  O1G    2(C14 H22 N2 O13 P2)                                         
FORMUL   4  EDO    7(C2 H6 O2)                                                  
FORMUL   6  ACT    3(C2 H3 O2 1-)                                               
FORMUL  15  HOH   *935(H2 O)                                                    
HELIX    1   1 LYS A   10  GLY A   23  1                                  14    
HELIX    2   2 SER A   35  VAL A   37  5                                   3    
HELIX    3   3 ASN A   38  LEU A   45  1                                   8    
HELIX    4   4 ASP A   50  LEU A   55  1                                   6    
HELIX    5   5 PRO A   71  ILE A   76  5                                   6    
HELIX    6   6 THR A   77  LEU A   92  1                                  16    
HELIX    7   7 PRO A   93  GLY A   95  5                                   3    
HELIX    8   8 GLY A  100  HIS A  115  1                                  16    
HELIX    9   9 SER A  124  LEU A  136  1                                  13    
HELIX   10  10 SER A  152  GLY A  162  1                                  11    
HELIX   11  11 ASP A  178  ILE A  186  5                                   9    
HELIX   12  12 HIS A  197  LYS A  201  5                                   5    
HELIX   13  13 ASP A  204  LYS A  216  1                                  13    
HELIX   14  14 ASN A  262  TYR A  274  1                                  13    
HELIX   15  15 ASP A  296  MET A  307  1                                  12    
HELIX   16  16 TYR A  309  LEU A  328  1                                  20    
HELIX   17  17 LEU A  328  LYS A  334  1                                   7    
HELIX   18  18 ASP A  359  GLY A  372  1                                  14    
HELIX   19  19 LEU A  382  GLN A  386  5                                   5    
HELIX   20  20 THR A  388  TYR A  395  1                                   8    
HELIX   21  21 LEU A  400  GLN A  409  1                                  10    
HELIX   22  22 THR A  420  GLY A  440  1                                  21    
HELIX   23  23 LYS B   10  LYS B   22  1                                  13    
HELIX   24  24 SER B   35  GLU B   39  5                                   5    
HELIX   25  25 ARG B   40  LEU B   45  1                                   6    
HELIX   26  26 ASP B   50  LEU B   55  1                                   6    
HELIX   27  27 PRO B   71  LEU B   75  5                                   5    
HELIX   28  28 THR B   77  LEU B   92  1                                  16    
HELIX   29  29 PRO B   93  GLY B   95  5                                   3    
HELIX   30  30 GLY B  100  HIS B  115  1                                  16    
HELIX   31  31 SER B  124  LEU B  136  1                                  13    
HELIX   32  32 SER B  152  SER B  161  1                                  10    
HELIX   33  33 ASP B  178  ILE B  186  5                                   9    
HELIX   34  34 HIS B  197  LYS B  201  5                                   5    
HELIX   35  35 ASP B  204  TYR B  215  1                                  12    
HELIX   36  36 ASN B  262  TYR B  274  1                                  13    
HELIX   37  37 ASP B  296  MET B  307  1                                  12    
HELIX   38  38 TYR B  309  LEU B  328  1                                  20    
HELIX   39  39 LEU B  328  LYS B  334  1                                   7    
HELIX   40  40 ASP B  359  GLY B  372  1                                  14    
HELIX   41  41 LEU B  382  GLN B  386  5                                   5    
HELIX   42  42 THR B  388  TYR B  395  1                                   8    
HELIX   43  43 LEU B  400  GLN B  409  1                                  10    
HELIX   44  44 THR B  420  ILE B  439  1                                  20    
SHEET    1   A 2 VAL A   5  ILE A   7  0                                        
SHEET    2   A 2 LEU A  30  ILE A  32  1  O  VAL A  31   N  ILE A   7           
SHEET    1   B 7 TYR A 118  THR A 122  0                                        
SHEET    2   B 7 GLY A 256  THR A 260 -1  O  ILE A 258   N  ILE A 120           
SHEET    3   B 7 ILE A 238  SER A 242 -1  N  THR A 239   O  ALA A 259           
SHEET    4   B 7 LYS A 218  ASP A 222  1  N  GLU A 221   O  ILE A 238           
SHEET    5   B 7 THR A 190  ILE A 193  1  N  LYS A 191   O  LYS A 218           
SHEET    6   B 7 GLU A 143  MET A 146  1  N  ILE A 145   O  PHE A 192           
SHEET    7   B 7 VAL A 164  TYR A 167  1  O  ILE A 166   N  VAL A 144           
SHEET    1   C 2 PHE A 351  LYS A 354  0                                        
SHEET    2   C 2 VAL A 410  LEU A 413 -1  O  LEU A 411   N  ILE A 353           
SHEET    1   D 2 GLN B   4  ILE B   7  0                                        
SHEET    2   D 2 GLU B  29  ILE B  32  1  O  VAL B  31   N  ILE B   7           
SHEET    1   E 7 TYR B 118  THR B 122  0                                        
SHEET    2   E 7 GLY B 256  THR B 260 -1  O  ILE B 258   N  ILE B 120           
SHEET    3   E 7 ILE B 238  SER B 242 -1  N  THR B 239   O  ALA B 259           
SHEET    4   E 7 LYS B 218  ASP B 222  1  N  GLU B 221   O  ILE B 238           
SHEET    5   E 7 THR B 190  ILE B 193  1  N  LYS B 191   O  LYS B 218           
SHEET    6   E 7 GLU B 143  MET B 146  1  N  ILE B 145   O  PHE B 192           
SHEET    7   E 7 VAL B 164  TYR B 167  1  O  ILE B 166   N  VAL B 144           
SHEET    1   F 2 PHE B 351  LYS B 354  0                                        
SHEET    2   F 2 VAL B 410  LEU B 413 -1  O  LEU B 411   N  ILE B 353           
CISPEP   1 TYR A  378    TYR A  379          0         5.42                     
CISPEP   2 TYR B  378    TYR B  379          0         7.14                     
CRYST1   49.700  106.440   98.240  90.00  96.42  90.00 P 1 21 1      4          
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      0.020121  0.000000  0.002264        0.00000                         
SCALE2      0.000000  0.009395  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010243        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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