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Database: PDB
Entry: 2VD8
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Original site: 2VD8 
HEADER    ISOMERASE                               01-OCT-07   2VD8              
TITLE     THE CRYSTAL STRUCTURE OF ALANINE RACEMASE FROM BACILLUS               
TITLE    2 ANTHRACIS (BA0252)                                                   
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: PLP FORMS IMINO LINKAGE TO K41. ALL LYSINES           
COMPND   7  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   2   24-FEB-09 2VD8    1       VERSN                                    
REVDAT   1   20-MAY-08 2VD8    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.    1.47 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) : 1.47                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 110132                         
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5826                            
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) : 1.47                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.51                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6303                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 343                          
REMARK   3   BIN FREE R VALUE                    : 0.3670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5864                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 451                                     
REMARK   3   SOLVENT ATOMS            : 1020                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.077         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.078         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.051         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.320         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6467 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4272 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8826 ; 1.412 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10403 ; 1.024 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   791 ; 6.257 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   284 ;32.263 ;23.521       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   910 ;10.772 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;11.453 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   986 ; 0.219 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7270 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1351 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1384 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5057 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3245 ; 0.181 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3178 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   699 ; 0.151 ; 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):    34 ; 0.238 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    75 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    65 ; 0.165 ; 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):  5059 ; 1.826 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6355 ; 2.201 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2998 ; 1.987 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2471 ; 3.038 ; 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 : NULL                              
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 2VD8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-OCT-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-33940.                                       
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   : 116056                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.47                               
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     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 9.9                                
REMARK 200  R MERGE                    (I) : 0.11                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.60                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.47                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.95                               
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 1SFT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) POLYETHYLENE GLYCOL            
REMARK 280  3350, 0.1 M BIS-TRIS PH 6.5                                         
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       28.77600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.48400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.18250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.48400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.77600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.18250            
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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 8310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.5 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     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   N    GLU A     3  -  O    HOH A  2001              2.16            
REMARK 500   CH2  MLY A    27  -  O    VAL A    34              2.00            
REMARK 500   OH   TYR A   270  -  O    HOH A  2410              2.19            
REMARK 500   O    HOH A  2410  -  O    HOH A  2467              2.15            
REMARK 500   O    HOH B  2087  -  O    HOH B  2295              2.07            
REMARK 500   O    HOH B  2181  -  O    HOH A  2438              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR B 177   OG1 -  CB  -  CG2 ANGL. DEV. =  16.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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      123.35     96.81                                   
REMARK 500    PHE A 108       13.64   -158.38                                   
REMARK 500    SER A 123      -32.17   -136.29                                   
REMARK 500    ARG A 138      -78.59    -97.17                                   
REMARK 500    PHE A 220     -126.64     45.82                                   
REMARK 500    SER A 269     -176.73     72.64                                   
REMARK 500    THR A 356     -157.45   -143.35                                   
REMARK 500    ASP B  48      121.27     94.41                                   
REMARK 500    PHE B 108       12.28   -157.27                                   
REMARK 500    SER B 123      -37.52   -133.34                                   
REMARK 500    ARG B 138      -81.78    -97.14                                   
REMARK 500    PHE B 220     -126.13     45.59                                   
REMARK 500    SER B 269     -176.07     73.76                                   
REMARK 500    THR B 356     -157.36   -144.92                                   
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 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1390  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  17   OD2                                                    
REMARK 620 2 HOH A2539   O    90.4                                              
REMARK 620 3 HOH A2035   O    94.1  88.8                                        
REMARK 620 4 HOH A2033   O    90.7 159.1  70.2                                  
REMARK 620 5 HOH A2034   O    82.3 103.8 166.8  97.1                            
REMARK 620 6 HOH B2388   O   173.1  87.5  92.4  93.5  91.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2218   O                                                      
REMARK 620 2 HOH A2274   O    93.6                                              
REMARK 620 3 HOH B2221   O    94.5 170.7                                        
REMARK 620 4 HOH A2271   O    84.0  91.6  93.7                                  
REMARK 620 5 HOH A2273   O   104.3  83.4  90.3 170.5                            
REMARK 620 6 GLU A 161   OE1 160.9  97.0  76.5  79.9  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 342   OD1                                                    
REMARK 620 2 GLY B 306   O    89.4                                              
REMARK 620 3 GLU B 343   OE2  93.1  88.4                                        
REMARK 620 4 HOH A2455   O    86.7 173.4  86.5                                  
REMARK 620 5 HOH B2406   O    93.4  93.6 173.2  91.9                            
REMARK 620 6 HOH B2410   O   172.2  96.8  82.4  86.7  90.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1003  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2404   O                                                      
REMARK 620 2 HOH A2158   O    88.7                                              
REMARK 620 3 HOH A2160   O    91.6  76.6                                        
REMARK 620 4 HOH A2159   O    90.4 155.2  78.6                                  
REMARK 620 5 HOH A2405   O    87.4 101.6 178.0 103.1                            
REMARK 620 N                    1     2     3     4                             
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 B1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1390                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1391                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1392                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1390                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VD9   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF ALANINE RACEMASE                           
REMARK 900  FROM BACILLUS ANTHRACIS (BA0252) WITH BOUND                         
REMARK 900  L-ALA-P                                                             
DBREF  2VD8 A   -1     0  PDB    2VD8     2VD8            -1      0             
DBREF  2VD8 A    1   389  UNP    Q81VF6   Q81VF6_BACAN     1    389             
DBREF  2VD8 B   -1     0  PDB    2VD8     2VD8            -1      0             
DBREF  2VD8 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 LLP 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 LLP 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 2VD8 LLP A   41  LYS  LYSINE-PYRIDOXAL-5'-PHOSPHATE                      
MODRES 2VD8 LLP B   41  LYS  LYSINE-PYRIDOXAL-5'-PHOSPHATE                      
MODRES 2VD8 MLY A   27  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A   54  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  110  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  118  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  127  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  145  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  148  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  152  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  182  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  195  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  202  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  245  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  255  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  264  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  277  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  307  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  333  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY A  378  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B   27  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B   54  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  110  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  118  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  127  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  145  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  148  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  152  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  182  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  195  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  202  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  245  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  255  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  264  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  277  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  307  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  333  LYS  N,N-DIMETHYLLYSINE                                 
MODRES 2VD8 MLY B  378  LYS  N,N-DIMETHYLLYSINE                                 
HET    MLY  A  27      11                                                       
HET    LLP  A  41      24                                                       
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    LLP  B  41      24                                                       
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  B1001       1                                                       
HET     MG  B1002       1                                                       
HET     MG  B1003       1                                                       
HET     MG  A1390       1                                                       
HET     CL  A1391       1                                                       
HET     CL  A1392       1                                                       
HET     CL  B1390       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     LLP 2-LYSINE(3-HYDROXY-2-METHYL-5-                                   
HETNAM   2 LLP  PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)                         
FORMUL   3   CL    3(CL 1-)                                                     
FORMUL   4  MLY    36(C8 H18 N2 O2)                                             
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   6  LLP    2(C14 H24 N3 O7 P)                                           
FORMUL   7  HOH   *1020(H2 O1)                                                  
HELIX    1   1 LEU A   16  ILE A   30  1                                  15    
HELIX    2   2 VAL A   40  GLY A   46  1                                   7    
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  LEU A  213  1                                   6    
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  SER A  354  1                                   9    
HELIX   16  16 ILE A  357  THR A  364  1                                   8    
HELIX   17  17 ASN A  384  ASP A  388  5                                   5    
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  GLY B   60  1                                  13    
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  ILE B  389  1                                   6    
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  HIS A 205                                           
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  ALA A  38   N  ALA A  65           
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 ALA B 104  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         C   ILE A  26                 N   MLY A  27     1555   1555  1.34  
LINK         C   MLY A  27                 N   GLU A  28     1555   1555  1.33  
LINK         C   VAL A  40                 N   LLP A  41     1555   1555  1.34  
LINK         C   LLP A  41                 N   GLY A  42     1555   1555  1.33  
LINK         C   ALA A  53                 N   MLY A  54     1555   1555  1.33  
LINK         C   MLY A  54                 N   ILE A  55     1555   1555  1.33  
LINK         C   GLN A 109                 N   MLY A 110     1555   1555  1.34  
LINK         C   MLY A 110                 N   GLU A 111     1555   1555  1.33  
LINK         C   ILE A 117                 N   MLY A 118     1555   1555  1.33  
LINK         C   MLY A 118                 N   LEU A 119     1555   1555  1.33  
LINK         C   MET A 126                 N   MLY A 127     1555   1555  1.33  
LINK         C   MLY A 127                 N   TYR A 128     1555   1555  1.34  
LINK         C   ARG A 144                 N   MLY A 145     1555   1555  1.33  
LINK         C   MLY A 145                 N   GLU A 146     1555   1555  1.33  
LINK         C   LEU A 147                 N   MLY A 148     1555   1555  1.33  
LINK         C   MLY A 148                 N   GLY A 149     1555   1555  1.33  
LINK         C   LEU A 151                 N   MLY A 152     1555   1555  1.33  
LINK         C   MLY A 152                 N  ASER A 153     1555   1555  1.33  
LINK         C   MLY A 152                 N  BSER A 153     1555   1555  1.33  
LINK         C   ASP A 181                 N   MLY A 182     1555   1555  1.33  
LINK         C   MLY A 182                 N   GLN A 183     1555   1555  1.33  
LINK         C   LEU A 194                 N   MLY A 195     1555   1555  1.34  
LINK         C   MLY A 195                 N   GLU A 196     1555   1555  1.33  
LINK         C   PRO A 201                 N   MLY A 202     1555   1555  1.34  
LINK         C   MLY A 202                 N   PHE A 203     1555   1555  1.33  
LINK         C   PHE A 244                 N   MLY A 245     1555   1555  1.33  
LINK         C   MLY A 245                 N   LEU A 246     1555   1555  1.33  
LINK         C   THR A 254                 N   MLY A 255     1555   1555  1.32  
LINK         C   MLY A 255                 N   VAL A 256     1555   1555  1.33  
LINK         C   ILE A 263                 N   MLY A 264     1555   1555  1.33  
LINK         C   MLY A 264                 N   GLY A 265     1555   1555  1.33  
LINK         C   THR A 276                 N   MLY A 277     1555   1555  1.33  
LINK         C   MLY A 277                 N   THR A 278     1555   1555  1.33  
LINK         C   GLY A 306                 N   MLY A 307     1555   1555  1.34  
LINK         C   MLY A 307                 N   ARG A 308     1555   1555  1.33  
LINK         C   THR A 332                 N   MLY A 333     1555   1555  1.33  
LINK         C   MLY A 333                 N   VAL A 334     1555   1555  1.33  
LINK         C   GLY A 377                 N   MLY A 378     1555   1555  1.34  
LINK         C   MLY A 378                 N   VAL A 379     1555   1555  1.33  
LINK        MG    MG A1390                 OD2 ASP A  17     1555   1555  2.06  
LINK        MG    MG A1390                 O   HOH A2539     1555   1555  2.02  
LINK        MG    MG A1390                 O   HOH A2035     1555   1555  2.22  
LINK        MG    MG A1390                 O   HOH B2388     1555   1455  2.11  
LINK        MG    MG A1390                 O   HOH A2034     1555   1555  2.07  
LINK        MG    MG A1390                 O   HOH A2033     1555   1555  2.28  
LINK         C   ILE B  26                 N   MLY B  27     1555   1555  1.33  
LINK         C   MLY B  27                 N   GLU B  28     1555   1555  1.33  
LINK         C   VAL B  40                 N   LLP B  41     1555   1555  1.33  
LINK         C   LLP B  41                 N   GLY B  42     1555   1555  1.33  
LINK         C   ALA B  53                 N   MLY B  54     1555   1555  1.33  
LINK         C   MLY B  54                 N   ILE B  55     1555   1555  1.33  
LINK         C   GLN B 109                 N   MLY B 110     1555   1555  1.33  
LINK         C   MLY B 110                 N   GLU B 111     1555   1555  1.33  
LINK         C   ILE B 117                 N   MLY B 118     1555   1555  1.33  
LINK         C   MLY B 118                 N   LEU B 119     1555   1555  1.34  
LINK         C   MET B 126                 N   MLY B 127     1555   1555  1.33  
LINK         C   MLY B 127                 N   TYR B 128     1555   1555  1.32  
LINK         C   ARG B 144                 N   MLY B 145     1555   1555  1.33  
LINK         C   MLY B 145                 N   GLU B 146     1555   1555  1.33  
LINK         C   LEU B 147                 N   MLY B 148     1555   1555  1.33  
LINK         C   MLY B 148                 N   GLY B 149     1555   1555  1.33  
LINK         C   LEU B 151                 N   MLY B 152     1555   1555  1.33  
LINK         C   MLY B 152                 N   SER B 153     1555   1555  1.33  
LINK         C   ASP B 181                 N   MLY B 182     1555   1555  1.33  
LINK         C   MLY B 182                 N   GLN B 183     1555   1555  1.33  
LINK         C   LEU B 194                 N   MLY B 195     1555   1555  1.33  
LINK         C   MLY B 195                 N   GLU B 196     1555   1555  1.34  
LINK         C   PRO B 201                 N   MLY B 202     1555   1555  1.33  
LINK         C   MLY B 202                 N   PHE B 203     1555   1555  1.33  
LINK         C   PHE B 244                 N   MLY B 245     1555   1555  1.33  
LINK         C   MLY B 245                 N   LEU B 246     1555   1555  1.33  
LINK         C   THR B 254                 N   MLY B 255     1555   1555  1.32  
LINK         C   MLY B 255                 N   VAL B 256     1555   1555  1.34  
LINK         C   ILE B 263                 N   MLY B 264     1555   1555  1.32  
LINK         C   MLY B 264                 N   GLY B 265     1555   1555  1.32  
LINK         C   THR B 276                 N   MLY B 277     1555   1555  1.33  
LINK         C   MLY B 277                 N   THR B 278     1555   1555  1.33  
LINK         C   GLY B 306                 N   MLY B 307     1555   1555  1.33  
LINK         C   MLY B 307                 N   ARG B 308     1555   1555  1.33  
LINK         C   THR B 332                 N   MLY B 333     1555   1555  1.33  
LINK         C   MLY B 333                 N   VAL B 334     1555   1555  1.33  
LINK         C   GLY B 377                 N   MLY B 378     1555   1555  1.33  
LINK         C   MLY B 378                 N   VAL B 379     1555   1555  1.33  
LINK        MG    MG B1001                 OE1 GLU A 161     1555   2455  2.69  
LINK        MG    MG B1001                 O   HOH A2273     1555   2455  2.09  
LINK        MG    MG B1001                 O   HOH A2271     1555   2455  2.32  
LINK        MG    MG B1001                 O   HOH B2221     1555   1555  2.07  
LINK        MG    MG B1001                 O   HOH A2274     1555   2455  2.19  
LINK        MG    MG B1001                 O   HOH B2218     1555   1555  2.27  
LINK        MG    MG B1002                 O   HOH B2410     1555   1455  2.11  
LINK        MG    MG B1002                 O   HOH B2406     1555   1455  2.05  
LINK        MG    MG B1002                 O   HOH A2455     1555   1555  2.22  
LINK        MG    MG B1002                 OE2 GLU B 343     1555   1455  2.18  
LINK        MG    MG B1002                 O   GLY B 306     1555   1455  2.11  
LINK        MG    MG B1002                 OD1 ASP B 342     1555   1455  2.12  
LINK        MG    MG B1003                 O   HOH A2405     1555   1555  1.98  
LINK        MG    MG B1003                 O   HOH A2159     1555   1555  2.22  
LINK        MG    MG B1003                 O   HOH A2160     1555   1555  2.15  
LINK        MG    MG B1003                 O   HOH A2158     1555   1555  2.35  
LINK        MG    MG B1003                 O   HOH A2404     1555   1555  1.98  
SITE     1 AC1  6 GLU A 161  HOH A2271  HOH A2273  HOH A2274                    
SITE     2 AC1  6 HOH B2218  HOH B2221                                          
SITE     1 AC2  6 HOH A2455  GLY B 306  ASP B 342  GLU B 343                    
SITE     2 AC2  6 HOH B2406  HOH B2410                                          
SITE     1 AC3  5 HOH A2158  HOH A2159  HOH A2160  HOH A2404                    
SITE     2 AC3  5 HOH A2405                                                     
SITE     1 AC4  6 ASP A  17  HOH A2033  HOH A2034  HOH A2035                    
SITE     2 AC4  6 HOH A2539  HOH B2388                                          
SITE     1 AC5  4 ARG A 144  GLN A 216  HOH A2247  HOH A2249                    
SITE     1 AC6  2 ASN A 131  ARG A 138                                          
SITE     1 AC7  2 ASN B 131  ARG B 138                                          
CRYST1   57.552   88.365  138.968  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      0.017376  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007196        0.00000                         
MTRIX1   1 -0.925560  0.377050  0.034120      -18.88800    1                    
MTRIX2   1  0.377230  0.910860  0.167410       10.07700    1                    
MTRIX3   1  0.032040  0.167820 -0.985300      -73.03100    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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