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Database: PDB
Entry: 2VD9
LinkDB: 2VD9
Original site: 2VD9 
HEADER    ISOMERASE                               01-OCT-07   2VD9              
TITLE     THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM BACILLUS               
TITLE    2 ANTHRACIS (BA0252) WITH BOUND L-ALA-P                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALANINE RACEMASE;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 5.1.1.1;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: ALL LYSINES DIMETHYLATED EXCEPT K41 AND K260          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 198094;                                              
SOURCE   4 STRAIN: AMES;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA PLYSS;                             
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: POPINB                                     
KEYWDS    PYRIDOXAL 5'-PHOSPHATE, PEPTIDOGLYCAN SYNTHESIS, PLP, OPPF,           
KEYWDS   2 L-ALANINE, ISOMERASE, D-ALANINE, PYRIDOXAL PHOSPHATE,                
KEYWDS   3 STRUCTURAL GENOMICS, ALANINE RACEMASE, SPORE GERMINATION,            
KEYWDS   4 OXFORD PROTEIN PRODUCTION FACILITY, STRUCTURAL PROTEOMICS            
KEYWDS   5 IN EUROPE (SPINE)                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.AU,J.REN,T.S.WALTER,K.HARLOS,J.E.NETTLESHIP,R.J.OWENS,              
AUTHOR   2 D.I.STUART,R.M.ESNOUF,                                               
AUTHOR   3 OXFORD PROTEIN PRODUCTION FACILITY (OPPF),                           
AUTHOR   4 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)                              
REVDAT   3   08-FEB-12 2VD9    1       REMARK VERSN  FORMUL LINK                
REVDAT   3 2                           SITE   CONECT                            
REVDAT   2   24-FEB-09 2VD9    1       VERSN                                    
REVDAT   1   20-MAY-08 2VD9    0                                                
JRNL        AUTH   K.AU,J.REN,T.S.WALTER,K.HARLOS,J.E.NETTLESHIP,               
JRNL        AUTH 2 R.J.OWENS,D.I.STUART,R.M.ESNOUF                              
JRNL        TITL   STRUCTURES OF AN ALANINE RACEMASE FROM BACILLUS              
JRNL        TITL 2 ANTHRACIS (BA0252) IN THE PRESENCE AND ABSENCE OF            
JRNL        TITL 3 (R)-1-AMINOETHYLPHOSPHONIC ACID (L-ALA-P).                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  64   327 2008              
JRNL        REFN                   ISSN 1744-3091                               
JRNL        PMID   18453697                                                     
JRNL        DOI    10.1107/S1744309108007252                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45596                          
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 + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2434                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3188                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2610                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5800                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 490                                     
REMARK   3   SOLVENT ATOMS            : 871                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03000                                              
REMARK   3    B22 (A**2) : -0.05000                                             
REMARK   3    B33 (A**2) : 0.02000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.261         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.203         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.555         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6431 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4237 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8767 ; 1.195 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10276 ; 0.912 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   770 ; 6.288 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   282 ;33.064 ;23.546       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   895 ;11.569 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    40 ;12.771 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   980 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7134 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1326 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1289 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4970 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3106 ; 0.175 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3177 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   636 ; 0.153 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.224 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    45 ; 0.231 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4970 ; 0.769 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6230 ; 0.914 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3039 ; 0.535 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2537 ; 0.859 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A     394      2                      
REMARK   3           1     B      4       B     394      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2264 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2929 ;  0.41 ;  0.50           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2264 ;  0.39 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2929 ;  0.58 ;  5.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-OCT-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-34020.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48124                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.23                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.10                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 9.0                                
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.88                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.20                               
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 2VD8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) POLYETHYLENE GLYCOL            
REMARK 280  3350, 0.1M BIS-TRIS PH6.5, SOAKED IN 10MM L-ALA-P FOR 45            
REMARK 280  MINUTES, CRYOPROTECTED IN 25% GLYCEROL                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       29.84600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.33000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.25200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.33000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.84600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.25200            
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: 10510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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     GLY A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLU B     3                                                      
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   OH   TYR A   270     O7   IN5 B  1392              2.16            
REMARK 500   OH   TYR B   270     O6   EPC A  1395              2.16            
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  48      123.81     92.90                                   
REMARK 500    PHE A 108       11.95   -151.53                                   
REMARK 500    ARG A 138      -79.93    -97.83                                   
REMARK 500    MLY A 202      -54.62     74.51                                   
REMARK 500    PHE A 220     -127.86     45.19                                   
REMARK 500    SER A 269     -170.08     72.77                                   
REMARK 500    VAL A 272       49.66     39.37                                   
REMARK 500    ASP B  48      122.68     92.85                                   
REMARK 500    PHE B 108       11.73   -152.40                                   
REMARK 500    SER B 123      -37.96   -131.33                                   
REMARK 500    ARG B 138      -80.34    -97.74                                   
REMARK 500    MLY B 202      -53.34     73.24                                   
REMARK 500    PHE B 220     -126.60     43.08                                   
REMARK 500    SER B 269     -173.29     73.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AB", "BB" IN EACH CHAIN ON SHEET RECORDS    
REMARK 700 BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1390                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1390                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1391                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1392                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1391                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1393                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IN5 B1392                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IN5 A1394                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPC B1393                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPC A1395                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VD8   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF ALANINE RACEMASE                           
REMARK 900  FROM BACILLUS ANTHRACIS (BA0252)                                    
DBREF  2VD9 A   -1     0  PDB    2VD9     2VD9            -1      0             
DBREF  2VD9 A    1   389  UNP    Q81VF6   Q81VF6_BACAN     1    389             
DBREF  2VD9 B   -1     0  PDB    2VD9     2VD9            -1      0             
DBREF  2VD9 B    1   389  UNP    Q81VF6   Q81VF6_BACAN     1    389             
SEQRES   1 A  391  GLY PRO MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP          
SEQRES   2 A  391  VAL GLU VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR          
SEQRES   3 A  391  HIS ILE MLY GLU PHE ILE PRO SER ASP VAL GLU ILE PHE          
SEQRES   4 A  391  ALA VAL VAL LYS GLY ASN ALA TYR GLY HIS ASP TYR VAL          
SEQRES   5 A  391  PRO VAL ALA MLY ILE ALA LEU GLU ALA GLY ALA THR ARG          
SEQRES   6 A  391  LEU ALA VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG          
SEQRES   7 A  391  ARG ALA GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO          
SEQRES   8 A  391  SER PRO PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP          
SEQRES   9 A  391  VAL ALA LEU THR VAL PHE GLN MLY GLU TRP VAL ASP GLU          
SEQRES  10 A  391  ALA ILE MLY LEU TRP ASP GLY SER SER THR MET MLY TYR          
SEQRES  11 A  391  HIS ILE ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE          
SEQRES  12 A  391  ARG GLU ARG MLY GLU LEU MLY GLY PHE LEU MLY SER LEU          
SEQRES  13 A  391  GLU GLY ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR          
SEQRES  14 A  391  HIS PHE ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE          
SEQRES  15 A  391  ASP MLY GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP          
SEQRES  16 A  391  LEU MLY GLU PHE GLY VAL ASP PRO MLY PHE VAL HIS THR          
SEQRES  17 A  391  ALA ASN SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR          
SEQRES  18 A  391  PHE ASN ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU          
SEQRES  19 A  391  SER PRO SER VAL GLU ILE ARG PRO PHE LEU PRO PHE MLY          
SEQRES  20 A  391  LEU GLU PRO ALA LEU SER LEU HIS THR MLY VAL ALA HIS          
SEQRES  21 A  391  ILE LYS GLN VAL ILE MLY GLY ASP GLY ILE SER TYR ASN          
SEQRES  22 A  391  VAL THR TYR ARG THR MLY THR GLU GLU TRP ILE ALA THR          
SEQRES  23 A  391  VAL ALA ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU          
SEQRES  24 A  391  GLN GLY PHE GLU VAL LEU VAL ASN GLY MLY ARG VAL PRO          
SEQRES  25 A  391  ILE VAL GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS          
SEQRES  26 A  391  LEU PRO CYS GLU VAL PRO LEU GLY THR MLY VAL THR LEU          
SEQRES  27 A  391  ILE GLY ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU          
SEQRES  28 A  391  VAL ALA GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE          
SEQRES  29 A  391  THR THR ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG          
SEQRES  30 A  391  ASN GLY MLY VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP          
SEQRES  31 A  391  ILE                                                          
SEQRES   1 B  391  GLY PRO MET GLU GLU ALA PRO PHE TYR ARG ASP THR TRP          
SEQRES   2 B  391  VAL GLU VAL ASP LEU ASP ALA ILE TYR ASN ASN VAL THR          
SEQRES   3 B  391  HIS ILE MLY GLU PHE ILE PRO SER ASP VAL GLU ILE PHE          
SEQRES   4 B  391  ALA VAL VAL LYS GLY ASN ALA TYR GLY HIS ASP TYR VAL          
SEQRES   5 B  391  PRO VAL ALA MLY ILE ALA LEU GLU ALA GLY ALA THR ARG          
SEQRES   6 B  391  LEU ALA VAL ALA PHE LEU ASP GLU ALA LEU VAL LEU ARG          
SEQRES   7 B  391  ARG ALA GLY ILE THR ALA PRO ILE LEU VAL LEU GLY PRO          
SEQRES   8 B  391  SER PRO PRO ARG ASP ILE ASN VAL ALA ALA GLU ASN ASP          
SEQRES   9 B  391  VAL ALA LEU THR VAL PHE GLN MLY GLU TRP VAL ASP GLU          
SEQRES  10 B  391  ALA ILE MLY LEU TRP ASP GLY SER SER THR MET MLY TYR          
SEQRES  11 B  391  HIS ILE ASN PHE ASP SER GLY MET GLY ARG ILE GLY ILE          
SEQRES  12 B  391  ARG GLU ARG MLY GLU LEU MLY GLY PHE LEU MLY SER LEU          
SEQRES  13 B  391  GLU GLY ALA PRO PHE LEU GLU LEU GLU GLY VAL TYR THR          
SEQRES  14 B  391  HIS PHE ALA THR ALA ASP GLU VAL GLU THR SER TYR PHE          
SEQRES  15 B  391  ASP MLY GLN TYR ASN THR PHE LEU GLU GLN LEU SER TRP          
SEQRES  16 B  391  LEU MLY GLU PHE GLY VAL ASP PRO MLY PHE VAL HIS THR          
SEQRES  17 B  391  ALA ASN SER ALA ALA THR LEU ARG PHE GLN GLY ILE THR          
SEQRES  18 B  391  PHE ASN ALA VAL ARG ILE GLY ILE ALA MET TYR GLY LEU          
SEQRES  19 B  391  SER PRO SER VAL GLU ILE ARG PRO PHE LEU PRO PHE MLY          
SEQRES  20 B  391  LEU GLU PRO ALA LEU SER LEU HIS THR MLY VAL ALA HIS          
SEQRES  21 B  391  ILE LYS GLN VAL ILE MLY GLY ASP GLY ILE SER TYR ASN          
SEQRES  22 B  391  VAL THR TYR ARG THR MLY THR GLU GLU TRP ILE ALA THR          
SEQRES  23 B  391  VAL ALA ILE GLY TYR ALA ASP GLY TRP LEU ARG ARG LEU          
SEQRES  24 B  391  GLN GLY PHE GLU VAL LEU VAL ASN GLY MLY ARG VAL PRO          
SEQRES  25 B  391  ILE VAL GLY ARG VAL THR MET ASP GLN PHE MET ILE HIS          
SEQRES  26 B  391  LEU PRO CYS GLU VAL PRO LEU GLY THR MLY VAL THR LEU          
SEQRES  27 B  391  ILE GLY ARG GLN GLY ASP GLU TYR ILE SER ALA THR GLU          
SEQRES  28 B  391  VAL ALA GLU TYR SER GLY THR ILE ASN TYR GLU ILE ILE          
SEQRES  29 B  391  THR THR ILE SER PHE ARG VAL PRO ARG ILE PHE ILE ARG          
SEQRES  30 B  391  ASN GLY MLY VAL VAL GLU VAL ILE ASN TYR LEU ASN ASP          
SEQRES  31 B  391  ILE                                                          
MODRES 2VD9 MLY A   27  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A   54  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  110  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  118  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  127  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  145  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  148  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  152  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  182  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  195  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  202  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  245  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  255  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  264  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  277  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  307  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  333  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY A  378  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B   27  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B   54  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  110  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  118  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  127  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  145  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  148  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  152  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  182  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  195  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  202  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  245  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  255  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  264  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  277  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  307  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  333  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD9 MLY B  378  LYS  N,N-DIMETHYLLYSINE                                 
HET    MLY  A  27      11                                                       
HET    MLY  A  54      11                                                       
HET    MLY  A 110      11                                                       
HET    MLY  A 118      11                                                       
HET    MLY  A 127      11                                                       
HET    MLY  A 145      11                                                       
HET    MLY  A 148      11                                                       
HET    MLY  A 152      11                                                       
HET    MLY  A 182      11                                                       
HET    MLY  A 195      11                                                       
HET    MLY  A 202      11                                                       
HET    MLY  A 245      11                                                       
HET    MLY  A 255      11                                                       
HET    MLY  A 264      11                                                       
HET    MLY  A 277      11                                                       
HET    MLY  A 307      11                                                       
HET    MLY  A 333      11                                                       
HET    MLY  A 378      11                                                       
HET    MLY  B  27      11                                                       
HET    MLY  B  54      11                                                       
HET    MLY  B 110      11                                                       
HET    MLY  B 118      11                                                       
HET    MLY  B 127      11                                                       
HET    MLY  B 145      11                                                       
HET    MLY  B 148      11                                                       
HET    MLY  B 152      11                                                       
HET    MLY  B 182      11                                                       
HET    MLY  B 195      11                                                       
HET    MLY  B 202      11                                                       
HET    MLY  B 245      11                                                       
HET    MLY  B 255      11                                                       
HET    MLY  B 264      11                                                       
HET    MLY  B 277      11                                                       
HET    MLY  B 307      11                                                       
HET    MLY  B 333      11                                                       
HET    MLY  B 378      11                                                       
HET     MG  B1390       1                                                       
HET     MG  A1390       1                                                       
HET     MG  A1391       1                                                       
HET     CL  A1392       1                                                       
HET     CL  B1391       1                                                       
HET     CL  A1393       1                                                       
HET    IN5  B1392      22                                                       
HET    IN5  A1394      22                                                       
HET    EPC  B1393      22                                                       
HET    EPC  A1395      22                                                       
HETNAM     EPC (1S)-1-[((1E)-{3-HYDROXY-2-METHYL-5-                             
HETNAM   2 EPC  [(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLENE)AMINO]             
HETNAM   3 EPC  ETHYLPHOSPHONIC ACID                                            
HETNAM     IN5 {1-[(3-HYDROXY-METHYL-5-PHOSPHONOOXY-METHYL-                     
HETNAM   2 IN5  PYRIDIN-4-YLMETHYL)-AMINO]-ETHYL}-PHOSPHONIC                    
HETNAM   3 IN5  ACID                                                            
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  EPC    2(C10 H16 N2 O8 P2)                                          
FORMUL   4  IN5    2(C10 H18 N2 O8 P2)                                          
FORMUL   5   CL    3(CL 1-)                                                     
FORMUL   6  MLY    36(C8 H18 N2 O2)                                             
FORMUL   7   MG    3(MG 2+)                                                     
FORMUL   8  HOH   *871(H2 O)                                                    
HELIX    1   1 LEU A   16  ILE A   30  1                                  15    
HELIX    2   2 VAL A   40  HIS A   47  1                                   8    
HELIX    3   3 ASP A   48  ALA A   59  1                                  12    
HELIX    4   4 PHE A   68  ALA A   78  1                                  11    
HELIX    5   5 PRO A   91  ARG A   93  5                                   3    
HELIX    6   6 ASP A   94  ASN A  101  1                                   8    
HELIX    7   7 GLN A  109  TRP A  120  1                                  12    
HELIX    8   8 GLU A  143  GLU A  155  1                                  13    
HELIX    9   9 THR A  177  PHE A  197  1                                  21    
HELIX   10  10 ASN A  208  PHE A  215  1                                   8    
HELIX   11  11 ILE A  238  LEU A  242  5                                   5    
HELIX   12  12 SER A  269  THR A  273  5                                   5    
HELIX   13  13 GLY A  288  GLY A  292  5                                   5    
HELIX   14  14 LEU A  294  GLN A  298  5                                   5    
HELIX   15  15 SER A  346  GLY A  355  1                                  10    
HELIX   16  16 ILE A  357  THR A  364  1                                   8    
HELIX   17  17 ASN A  384  ILE A  389  5                                   6    
HELIX   18  18 LEU B   16  ILE B   30  1                                  15    
HELIX   19  19 VAL B   40  GLY B   46  1                                   7    
HELIX   20  20 ASP B   48  ALA B   59  1                                  12    
HELIX   21  21 PHE B   68  ALA B   78  1                                  11    
HELIX   22  22 PRO B   91  ARG B   93  5                                   3    
HELIX   23  23 ASP B   94  ASN B  101  1                                   8    
HELIX   24  24 GLN B  109  TRP B  120  1                                  12    
HELIX   25  25 GLU B  143  GLU B  155  1                                  13    
HELIX   26  26 THR B  177  PHE B  197  1                                  21    
HELIX   27  27 ASN B  208  PHE B  215  1                                   8    
HELIX   28  28 ILE B  238  LEU B  242  5                                   5    
HELIX   29  29 SER B  269  THR B  273  5                                   5    
HELIX   30  30 GLY B  288  GLY B  292  5                                   5    
HELIX   31  31 LEU B  294  GLN B  298  5                                   5    
HELIX   32  32 SER B  346  GLY B  355  1                                  10    
HELIX   33  33 ILE B  357  THR B  364  1                                   8    
HELIX   34  34 ASN B  384  ASP B  388  5                                   5    
SHEET    1  AA 3 GLU A 343  ILE A 345  0                                        
SHEET    2  AA 3 MLY A 333  GLN A 340 -1  O  GLY A 338   N  ILE A 345           
SHEET    3  AA 3 LEU A 250  VAL A 262 -1  O  LEU A 252   N  LEU A 336           
SHEET    1  AB 7 GLU A 343  ILE A 345  0                                        
SHEET    2  AB 7 MLY A 333  GLN A 340 -1  O  GLY A 338   N  ILE A 345           
SHEET    3  AB 7 GLU A 301  VAL A 304 -1  O  LEU A 303   N  THR A 335           
SHEET    4  AB 7 MLY A 307  VAL A 312 -1  O  MLY A 307   N  VAL A 304           
SHEET    5  AB 7 PHE A 320  LEU A 324 -1  O  MET A 321   N  VAL A 312           
SHEET    6  AB 7 GLU A 280  VAL A 285 -1  O  TRP A 281   N  LEU A 324           
SHEET    7  AB 7 LEU A 250  VAL A 262 -1  N  ALA A 257   O  THR A 284           
SHEET    1  AC 9 GLU A  35  VAL A  39  0                                        
SHEET    2  AC 9 ALA A 222  ILE A 225  1  O  VAL A 223   N  PHE A  37           
SHEET    3  AC 9 VAL A 204  ALA A 207  1  N  THR A 206   O  ALA A 222           
SHEET    4  AC 9 LEU A 160  TYR A 166  1  O  VAL A 165   N  HIS A 205           
SHEET    5  AC 9 MET A 126  ASN A 131  1  O  MET A 126   N  GLU A 161           
SHEET    6  AC 9 VAL A 103  THR A 106  1  O  LEU A 105   N  HIS A 129           
SHEET    7  AC 9 ILE A  84  VAL A  86  1  O  ILE A  84   N  ALA A 104           
SHEET    8  AC 9 ARG A  63  VAL A  66  1  O  LEU A  64   N  LEU A  85           
SHEET    9  AC 9 GLU A  35  VAL A  39  1  O  ILE A  36   N  ARG A  63           
SHEET    1  AD 2 GLY A 267  ILE A 268  0                                        
SHEET    2  AD 2 TYR A 274  ARG A 275 -1  O  TYR A 274   N  ILE A 268           
SHEET    1  BA 6 GLU B 343  ILE B 345  0                                        
SHEET    2  BA 6 MLY B 333  GLN B 340 -1  O  GLY B 338   N  ILE B 345           
SHEET    3  BA 6 MLY B 378  ILE B 383                                           
SHEET    4  BA 6 ARG B 371  ARG B 375 -1  O  ARG B 371   N  ILE B 383           
SHEET    5  BA 6 TRP B  11  ASP B  15  1  O  VAL B  12   N  ILE B 372           
SHEET    6  BA 6 LEU B 250  VAL B 262 -1  O  SER B 251   N  GLU B  13           
SHEET    1  BB 9 GLU B  35  VAL B  39  0                                        
SHEET    2  BB 9 ALA B 222  ILE B 225  1  O  VAL B 223   N  PHE B  37           
SHEET    3  BB 9 VAL B 204  HIS B 205                                           
SHEET    4  BB 9 LEU B 160  TYR B 166  1  O  VAL B 165   N  HIS B 205           
SHEET    5  BB 9 MET B 126  ASN B 131  1  O  MET B 126   N  GLU B 161           
SHEET    6  BB 9 VAL B 103  THR B 106  1  O  LEU B 105   N  HIS B 129           
SHEET    7  BB 9 ILE B  84  VAL B  86  1  O  ILE B  84   N  ALA B 104           
SHEET    8  BB 9 ARG B  63  VAL B  66  1  O  LEU B  64   N  LEU B  85           
SHEET    9  BB 9 GLU B  35  VAL B  39  1  O  ALA B  38   N  ALA B  65           
SHEET    1  BC 2 GLY B 267  ILE B 268  0                                        
SHEET    2  BC 2 TYR B 274  ARG B 275 -1  O  TYR B 274   N  ILE B 268           
LINK         N   MLY A  27                 C   ILE A  26     1555   1555  1.33  
LINK         C   MLY A  27                 N   GLU A  28     1555   1555  1.33  
LINK         N   MLY A  54                 C   ALA A  53     1555   1555  1.33  
LINK         C   MLY A  54                 N   ILE A  55     1555   1555  1.33  
LINK         N   MLY A 110                 C   GLN A 109     1555   1555  1.33  
LINK         C   MLY A 110                 N   GLU A 111     1555   1555  1.33  
LINK         N   MLY A 118                 C   ILE A 117     1555   1555  1.33  
LINK         C   MLY A 118                 N   LEU A 119     1555   1555  1.33  
LINK         N   MLY A 127                 C   MET A 126     1555   1555  1.33  
LINK         C   MLY A 127                 N   TYR A 128     1555   1555  1.33  
LINK         N   MLY A 145                 C   ARG A 144     1555   1555  1.33  
LINK         C   MLY A 145                 N   GLU A 146     1555   1555  1.33  
LINK         N   MLY A 148                 C   LEU A 147     1555   1555  1.33  
LINK         C   MLY A 148                 N   GLY A 149     1555   1555  1.33  
LINK         N   MLY A 152                 C   LEU A 151     1555   1555  1.34  
LINK         C   MLY A 152                 N   SER A 153     1555   1555  1.33  
LINK         N   MLY A 182                 C   ASP A 181     1555   1555  1.33  
LINK         C   MLY A 182                 N   GLN A 183     1555   1555  1.34  
LINK         N   MLY A 195                 C   LEU A 194     1555   1555  1.33  
LINK         C   MLY A 195                 N   GLU A 196     1555   1555  1.33  
LINK         N   MLY A 202                 C   PRO A 201     1555   1555  1.34  
LINK         C   MLY A 202                 N   PHE A 203     1555   1555  1.33  
LINK         N   MLY A 245                 C   PHE A 244     1555   1555  1.33  
LINK         C   MLY A 245                 N   LEU A 246     1555   1555  1.33  
LINK         N   MLY A 255                 C   THR A 254     1555   1555  1.33  
LINK         C   MLY A 255                 N   VAL A 256     1555   1555  1.33  
LINK         N   MLY A 264                 C   ILE A 263     1555   1555  1.33  
LINK         C   MLY A 264                 N   GLY A 265     1555   1555  1.33  
LINK         N   MLY A 277                 C   THR A 276     1555   1555  1.33  
LINK         C   MLY A 277                 N   THR A 278     1555   1555  1.33  
LINK         N   MLY A 307                 C   GLY A 306     1555   1555  1.33  
LINK         C   MLY A 307                 N   ARG A 308     1555   1555  1.33  
LINK         N   MLY A 333                 C   THR A 332     1555   1555  1.33  
LINK         C   MLY A 333                 N   VAL A 334     1555   1555  1.33  
LINK         N   MLY A 378                 C   GLY A 377     1555   1555  1.34  
LINK         C   MLY A 378                 N   VAL A 379     1555   1555  1.33  
LINK        MG    MG A1390                 O   HOH A2336     1555   1555  2.89  
LINK         C   MLY B  27                 N   GLU B  28     1555   1555  1.33  
LINK         N   MLY B  27                 C   ILE B  26     1555   1555  1.33  
LINK         C   MLY B  54                 N   ILE B  55     1555   1555  1.33  
LINK         N   MLY B  54                 C   ALA B  53     1555   1555  1.33  
LINK         C   MLY B 110                 N   GLU B 111     1555   1555  1.33  
LINK         N   MLY B 110                 C   GLN B 109     1555   1555  1.33  
LINK         C   MLY B 118                 N   LEU B 119     1555   1555  1.33  
LINK         N   MLY B 118                 C   ILE B 117     1555   1555  1.33  
LINK         C   MLY B 127                 N   TYR B 128     1555   1555  1.33  
LINK         N   MLY B 127                 C   MET B 126     1555   1555  1.33  
LINK         C   MLY B 145                 N   GLU B 146     1555   1555  1.34  
LINK         N   MLY B 145                 C   ARG B 144     1555   1555  1.33  
LINK         C   MLY B 148                 N   GLY B 149     1555   1555  1.33  
LINK         N   MLY B 148                 C   LEU B 147     1555   1555  1.33  
LINK         C   MLY B 152                 N   SER B 153     1555   1555  1.33  
LINK         N   MLY B 152                 C   LEU B 151     1555   1555  1.33  
LINK         C   MLY B 182                 N   GLN B 183     1555   1555  1.34  
LINK         N   MLY B 182                 C   ASP B 181     1555   1555  1.33  
LINK         C   MLY B 195                 N   GLU B 196     1555   1555  1.32  
LINK         N   MLY B 195                 C   LEU B 194     1555   1555  1.33  
LINK         C   MLY B 202                 N   PHE B 203     1555   1555  1.33  
LINK         N   MLY B 202                 C   PRO B 201     1555   1555  1.33  
LINK         C   MLY B 245                 N   LEU B 246     1555   1555  1.33  
LINK         N   MLY B 245                 C   PHE B 244     1555   1555  1.33  
LINK         C   MLY B 255                 N   VAL B 256     1555   1555  1.33  
LINK         N   MLY B 255                 C   THR B 254     1555   1555  1.33  
LINK         C   MLY B 264                 N   GLY B 265     1555   1555  1.33  
LINK         N   MLY B 264                 C   ILE B 263     1555   1555  1.33  
LINK         C   MLY B 277                 N   THR B 278     1555   1555  1.33  
LINK         N   MLY B 277                 C   THR B 276     1555   1555  1.33  
LINK         C   MLY B 307                 N   ARG B 308     1555   1555  1.33  
LINK         N   MLY B 307                 C   GLY B 306     1555   1555  1.33  
LINK         C   MLY B 333                 N   VAL B 334     1555   1555  1.33  
LINK         N   MLY B 333                 C   THR B 332     1555   1555  1.32  
LINK         C   MLY B 378                 N   VAL B 379     1555   1555  1.33  
LINK         N   MLY B 378                 C   GLY B 377     1555   1555  1.33  
SITE     1 AC1  1 GLU B 155                                                     
SITE     1 AC2  3 MLY A 333  HOH A2167  HOH A2336                               
SITE     1 AC3  1 ILE A 263                                                     
SITE     1 AC4  2 ASN A 131  ARG A 138                                          
SITE     1 AC5  2 ASN B 131  ARG B 138                                          
SITE     1 AC6  5 ARG A 144  PHE A 215  GLN A 216  HOH A2183                    
SITE     2 AC6  5 HOH A2259                                                     
SITE     1 AC7 18 TYR A 270  THR A 316  MET A 317  LYS B  41                    
SITE     2 AC7 18 TYR B  45  ARG B 138  HIS B 168  ASN B 208                    
SITE     3 AC7 18 SER B 209  ARG B 224  GLY B 226  ILE B 227                    
SITE     4 AC7 18 TYR B 359  HOH B2443  HOH B2444  HOH B2445                    
SITE     5 AC7 18 HOH B2446  HOH B2447                                          
SITE     1 AC8 21 VAL A  39  LYS A  41  TYR A  45  ARG A 138                    
SITE     2 AC8 21 HIS A 168  ASN A 208  SER A 209  ARG A 224                    
SITE     3 AC8 21 GLY A 226  ILE A 227  TYR A 359  HOH A2421                    
SITE     4 AC8 21 HOH A2422  HOH A2423  HOH A2424  TYR B 270                    
SITE     5 AC8 21 TYR B 289  THR B 316  MET B 317  ASP B 318                    
SITE     6 AC8 21 HOH B2318                                                     
SITE     1 AC9 19 TYR A 270  TYR A 289  THR A 316  MET A 317                    
SITE     2 AC9 19 LYS B  41  TYR B  45  ARG B 138  HIS B 168                    
SITE     3 AC9 19 ASN B 208  SER B 209  ARG B 224  GLY B 226                    
SITE     4 AC9 19 ILE B 227  TYR B 359  HOH B2443  HOH B2444                    
SITE     5 AC9 19 HOH B2445  HOH B2446  HOH B2447                               
SITE     1 BC1 19 LYS A  41  TYR A  45  ARG A 138  HIS A 168                    
SITE     2 BC1 19 ASN A 208  SER A 209  ARG A 224  GLY A 226                    
SITE     3 BC1 19 ILE A 227  TYR A 359  HOH A2421  HOH A2422                    
SITE     4 BC1 19 HOH A2423  HOH A2424  TYR B 270  TYR B 289                    
SITE     5 BC1 19 THR B 316  MET B 317  ASP B 318                               
CRYST1   59.692   96.504  140.660  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      0.016753  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010362  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007109        0.00000                         
MTRIX1   1 -0.996620  0.082100  0.000060      -13.37200    1                    
MTRIX2   1  0.082070  0.996300  0.025690        1.46100    1                    
MTRIX3   1  0.002050  0.025610 -0.999670      -71.05700    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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