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Database: PDB
Entry: 1BD0
LinkDB: 1BD0
Original site: 1BD0 
HEADER    ISOMERASE                               12-MAY-98   1BD0              
TITLE     ALANINE RACEMASE COMPLEXED WITH ALANINE PHOSPHONATE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;                 
SOURCE   3 ORGANISM_TAXID: 1422;                                                
SOURCE   4 STRAIN: XL-1 BLUE;                                                   
SOURCE   5 PLASMID: PMDALR3                                                     
KEYWDS    ALANINE, ISOMERASE, PYRIDOXAL PHOSPHATE, ALANINE PHOSPHONATE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.F.STAMPER,A.A.MOROLLO,D.RINGE                                       
REVDAT   3   24-FEB-09 1BD0    1       VERSN                                    
REVDAT   2   01-APR-03 1BD0    1       JRNL                                     
REVDAT   1   14-OCT-98 1BD0    0                                                
JRNL        AUTH   G.F.STAMPER,A.A.MOROLLO,D.RINGE,C.G.STAMPER                  
JRNL        TITL   REACTION OF ALANINE RACEMASE WITH                            
JRNL        TITL 2 1-AMINOETHYLPHOSPHONIC ACID FORMS A STABLE                   
JRNL        TITL 3 EXTERNAL ALDIMINE.                                           
JRNL        REF    BIOCHEMISTRY                  V.  37 10438 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9671513                                                      
JRNL        DOI    10.1021/BI980692S                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.P.SHAW,G.A.PETSKO,D.RINGE                                  
REMARK   1  TITL   DETERMINATION OF THE STRUCTURE OF ALANINE RACEMASE           
REMARK   1  TITL 2 FROM BACILLUS STEAROTHERMOPHILUS AT 1.9-A                    
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  36  1329 1997              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   D.J.NEIDHART,M.D.DISTEFANO,K.TANIZAWA,K.SODA,                
REMARK   1  AUTH 2 C.T.WALSH,G.A.PETSKO                                         
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES OF THE                        
REMARK   1  TITL 2 ALANINE-SPECIFIC RACEMASE FROM BACILLUS                      
REMARK   1  TITL 3 STEAROTHERMOPHILUS. OVERPRODUCTION,                          
REMARK   1  TITL 4 CRYSTALLIZATION, AND PRELIMINARY CHARACTERIZATION            
REMARK   1  REF    J.BIOL.CHEM.                  V. 262 15323 1987              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000.000                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 85.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 82763                          
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) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2505                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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            : 6043                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 387                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.24                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.75                            
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  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : INHIB.PAR                                      
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : INHIB2.TOP                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BD0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-96                          
REMARK 200  TEMPERATURE           (KELVIN) : 95                                 
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.15                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97731                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.851                                          
REMARK 200 STARTING MODEL: PDB ENTRY 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 100MM      
REMARK 280  TRIS BUFFER, PH 8.5, 200MM SODIUM ACETATE, 21% PEG 4000, AND        
REMARK 280  4MM 1-AMINOETHYL PHOSPHONIC ACID.                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.11350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.65250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.84500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       42.65250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.11350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       43.84500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 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     MET A     1                                                      
REMARK 465     ALA A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     ALA B   388                                                      
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    SER A 119       21.96   -147.72                                   
REMARK 500    ARG A 136      -82.40   -102.20                                   
REMARK 500    CYS A 201      -33.31   -149.46                                   
REMARK 500    ASN A 203     -159.46   -102.70                                   
REMARK 500    PHE A 215     -142.39     62.70                                   
REMARK 500    SER A 264     -174.67     64.16                                   
REMARK 500    PHE A 295     -169.93    -79.34                                   
REMARK 500    PHE B 106        5.77   -152.80                                   
REMARK 500    SER B 119       28.10   -145.38                                   
REMARK 500    ARG B 136      -79.30    -97.27                                   
REMARK 500    CYS B 201      -20.52   -161.93                                   
REMARK 500    ASN B 203     -160.02   -101.19                                   
REMARK 500    ARG B 213       59.77   -115.17                                   
REMARK 500    PHE B 215     -135.58     52.72                                   
REMARK 500    SER B 264     -174.41     65.58                                   
REMARK 500    HIS B 371       33.27     70.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 472        DISTANCE =  5.96 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CIC                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: LYS 39 AND TYR 265 (FROM THE OTHER SUBUNIT)        
REMARK 800  ARE PROPOSED CATALYTIC RESIDUES IN THE ACTIVE SITE OF THE           
REMARK 800  MOLECULE.                                                           
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IN5 A 389                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IN5 B 389                 
DBREF  1BD0 A    1   388  UNP    P10724   ALR_BACST        1    388             
DBREF  1BD0 B    1   388  UNP    P10724   ALR_BACST        1    388             
SEQADV 1BD0 ALA A  383  UNP  P10724    ARG   383 CONFLICT                       
SEQADV 1BD0 ALA B  383  UNP  P10724    ARG   383 CONFLICT                       
SEQRES   1 A  388  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 A  388  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 A  388  LEU LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS          
SEQRES   4 A  388  ALA ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 A  388  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 A  388  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 A  388  GLU ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA          
SEQRES   8 A  388  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 A  388  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 A  388  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU LYS MET          
SEQRES  11 A  388  ASP THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 A  388  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 A  388  HIS PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR          
SEQRES  14 A  388  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 A  388  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 A  388  PRO PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 A  388  ARG PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY          
SEQRES  18 A  388  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 A  388  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 A  388  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 A  388  GLU LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 A  388  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP          
SEQRES  23 A  388  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 A  388  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET          
SEQRES  25 A  388  ASP GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 A  388  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU          
SEQRES  27 A  388  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 A  388  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 A  388  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 A  388  ARG ASN ALA ILE GLY ALA GLY GLU SER SER ALA                  
SEQRES   1 B  388  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 B  388  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 B  388  LEU LEU PRO ASP ASP THR HIS ILE MET ALA VAL VAL LYS          
SEQRES   4 B  388  ALA ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 B  388  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 B  388  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 B  388  GLU ALA PRO ILE LEU VAL LEU GLY ALA SER ARG PRO ALA          
SEQRES   8 B  388  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 B  388  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 B  388  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU LYS MET          
SEQRES  11 B  388  ASP THR GLY MET GLY ARG LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 B  388  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 B  388  HIS PHE VAL LEU GLU GLY LEU TYR THR HIS PHE ALA THR          
SEQRES  14 B  388  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 B  388  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 B  388  PRO PRO LEU VAL HIS CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 B  388  ARG PHE PRO ASP ARG THR PHE ASN MET VAL ARG PHE GLY          
SEQRES  18 B  388  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 B  388  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 B  388  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 B  388  GLU LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 B  388  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR ALA ASP          
SEQRES  23 B  388  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 B  388  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE CYS MET          
SEQRES  25 B  388  ASP GLN CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 B  388  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP GLU          
SEQRES  27 B  388  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 B  388  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 B  388  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 B  388  ARG ASN ALA ILE GLY ALA GLY GLU SER SER ALA                  
HET    IN5  A 389      22                                                       
HET    IN5  B 389      22                                                       
HETNAM     IN5 {1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-PYRIDIN-4-           
HETNAM   2 IN5  YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC ACID                         
FORMUL   3  IN5    2(C10 H18 N2 O8 P2)                                          
FORMUL   5  HOH   *387(H2 O)                                                    
HELIX    1   1 LEU A   14  LEU A   27  1                                  14    
HELIX    2   2 LYS A   39  GLY A   44  1                                   6    
HELIX    3   3 ASP A   47  ALA A   57  1                                  11    
HELIX    4   4 LEU A   67  GLU A   75  1                                   9    
HELIX    5   5 PRO A   90  GLN A   98  5                                   9    
HELIX    6   6 SER A  108  SER A  115  1                                   8    
HELIX    7   7 GLU A  142  ARG A  154  1                                  13    
HELIX    8   8 ASP A  176  TRP A  191  1                                  16    
HELIX    9   9 SER A  204  ARG A  209  1                                   6    
HELIX   10  10 ILE A  222  TYR A  225  5                                   4    
HELIX   11  11 LYS A  234  LEU A  236  5                                   3    
HELIX   12  12 TYR A  265  ALA A  267  5                                   3    
HELIX   13  13 TYR A  284  ASP A  286  5                                   3    
HELIX   14  14 ARG A  290  HIS A  294  5                                   5    
HELIX   15  15 ILE A  342  LEU A  349  1                                   8    
HELIX   16  16 ASN A  353  THR A  359  5                                   7    
HELIX   17  17 LEU B   14  LEU B   27  1                                  14    
HELIX   18  18 LYS B   39  GLY B   44  1                                   6    
HELIX   19  19 ASP B   47  ALA B   57  1                                  11    
HELIX   20  20 LEU B   67  LYS B   76  1                                  10    
HELIX   21  21 PRO B   90  GLN B   98  5                                   9    
HELIX   22  22 SER B  108  LEU B  117  1                                  10    
HELIX   23  23 GLU B  142  GLU B  153  1                                  12    
HELIX   24  24 ASP B  176  GLU B  190  1                                  15    
HELIX   25  25 SER B  204  ARG B  209  1                                   6    
HELIX   26  26 ILE B  222  TYR B  225  5                                   4    
HELIX   27  27 LYS B  234  LEU B  236  5                                   3    
HELIX   28  28 TYR B  265  ALA B  267  5                                   3    
HELIX   29  29 TYR B  284  ASP B  286  5                                   3    
HELIX   30  30 ARG B  290  HIS B  294  5                                   5    
HELIX   31  31 ILE B  342  LEU B  349  1                                   8    
HELIX   32  32 ASN B  353  THR B  359  1                                   7    
SHEET    1   A 5 ARG A 373  ARG A 378  0                                        
SHEET    2   A 5 PRO A 365  ARG A 370 -1  N  ARG A 370   O  ARG A 373           
SHEET    3   A 5 THR A   8  ASP A  13  1  N  ALA A  10   O  PRO A 365           
SHEET    4   A 5 PHE A 245  ARG A 250 -1  N  HIS A 248   O  TRP A   9           
SHEET    5   A 5 LYS A 328  ILE A 332 -1  N  ILE A 332   O  LEU A 247           
SHEET    1   B 8 MET A 217  PHE A 220  0                                        
SHEET    2   B 8 HIS A  33  VAL A  37  1  N  HIS A  33   O  VAL A 218           
SHEET    3   B 8 ARG A  61  VAL A  64  1  N  ARG A  61   O  ALA A  36           
SHEET    4   B 8 PRO A  81  VAL A  84  1  N  PRO A  81   O  LEU A  62           
SHEET    5   B 8 ILE A 101  VAL A 105  1  N  ALA A 102   O  ILE A  82           
SHEET    6   B 8 ILE A 124  LYS A 129  1  N  HIS A 127   O  LEU A 103           
SHEET    7   B 8 PHE A 158  TYR A 164  1  N  VAL A 159   O  ILE A 124           
SHEET    8   B 8 LEU A 198  HIS A 200  1  N  LEU A 198   O  LEU A 163           
SHEET    1   C 3 CYS A 315  ARG A 318  0                                        
SHEET    2   C 3 GLU A 275  ILE A 280 -1  N  ILE A 280   O  CYS A 315           
SHEET    3   C 3 LEU A 251  LEU A 257 -1  N  LEU A 257   O  GLU A 275           
SHEET    1   D 2 HIS A 296  VAL A 299  0                                        
SHEET    2   D 2 GLN A 302  PRO A 305 -1  N  ALA A 304   O  VAL A 297           
SHEET    1   E 2 GLY A 333  GLN A 335  0                                        
SHEET    2   E 2 GLU A 338  ILE A 340 -1  N  ILE A 340   O  GLY A 333           
SHEET    1   F 5 ARG B 373  ARG B 378  0                                        
SHEET    2   F 5 PRO B 365  ARG B 370 -1  N  ARG B 370   O  ARG B 373           
SHEET    3   F 5 THR B   8  ASP B  13  1  N  ALA B  10   O  PRO B 365           
SHEET    4   F 5 PHE B 245  ARG B 250 -1  N  HIS B 248   O  TRP B   9           
SHEET    5   F 5 LYS B 328  ILE B 332 -1  N  ILE B 332   O  LEU B 247           
SHEET    1   G 8 MET B 217  PHE B 220  0                                        
SHEET    2   G 8 HIS B  33  VAL B  37  1  N  HIS B  33   O  VAL B 218           
SHEET    3   G 8 ARG B  61  VAL B  64  1  N  ARG B  61   O  ALA B  36           
SHEET    4   G 8 PRO B  81  VAL B  84  1  N  PRO B  81   O  LEU B  62           
SHEET    5   G 8 ILE B 101  VAL B 105  1  N  ALA B 102   O  ILE B  82           
SHEET    6   G 8 ILE B 124  LYS B 129  1  N  HIS B 127   O  LEU B 103           
SHEET    7   G 8 PHE B 158  TYR B 164  1  N  VAL B 159   O  ILE B 124           
SHEET    8   G 8 LEU B 198  HIS B 200  1  N  LEU B 198   O  LEU B 163           
SHEET    1   H 3 CYS B 315  ARG B 318  0                                        
SHEET    2   H 3 GLU B 275  ILE B 280 -1  N  ILE B 280   O  CYS B 315           
SHEET    3   H 3 LEU B 251  LEU B 257 -1  N  LEU B 257   O  GLU B 275           
SHEET    1   I 2 HIS B 296  VAL B 299  0                                        
SHEET    2   I 2 GLN B 302  PRO B 305 -1  N  ALA B 304   O  VAL B 297           
SHEET    1   J 2 GLY B 333  GLN B 335  0                                        
SHEET    2   J 2 GLU B 338  ILE B 340 -1  N  ILE B 340   O  GLY B 333           
CISPEP   1 GLY A  120    PRO A  121          0         0.23                     
CISPEP   2 GLY B  120    PRO B  121          0        -0.07                     
SITE     1 CIC  2 LYS A  39  TYR A 265                                          
SITE     1 AC1 19 LYS A  39  TYR A  43  ARG A 136  HIS A 166                    
SITE     2 AC1 19 ASN A 203  SER A 204  ARG A 219  GLY A 221                    
SITE     3 AC1 19 ILE A 222  TYR A 354  HOH A 433  HOH A 450                    
SITE     4 AC1 19 HOH A 459  HOH A 461  HOH A 490  TYR B 265                    
SITE     5 AC1 19 TYR B 284  CYS B 311  MET B 312                               
SITE     1 AC2 20 TYR A 265  TYR A 284  CYS A 311  MET A 312                    
SITE     2 AC2 20 ASP A 313  LYS B  39  TYR B  43  ARG B 136                    
SITE     3 AC2 20 HIS B 166  ASN B 203  SER B 204  ARG B 219                    
SITE     4 AC2 20 GLY B 221  ILE B 222  TYR B 354  HOH B 392                    
SITE     5 AC2 20 HOH B 402  HOH B 404  HOH B 446  HOH B 484                    
CRYST1   98.227   87.690   85.305  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010181  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011404  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011723        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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