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Database: PDB
Entry: 3AUM
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Original site: 3AUM 
HEADER    MEMBRANE PROTEIN                        10-FEB-11   3AUM              
TITLE     CRYSTAL STRUCTURE OF OSPA MUTANT                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OUTER SURFACE PROTEIN A;                                   
COMPND   3 CHAIN: O;                                                            
COMPND   4 FRAGMENT: RESIDUES 27-273;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;                           
SOURCE   3 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;                            
SOURCE   4 ORGANISM_TAXID: 139;                                                 
SOURCE   5 GENE: OSPA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA-MENDER, MEMBRANE PROTEIN                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MAKABE                                                              
REVDAT   1   15-FEB-12 3AUM    0                                                
JRNL        AUTH   K.MAKABE                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF OSPA MUTANT                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 29294                          
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.199                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1566                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2050                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 119                          
REMARK   3   BIN FREE R VALUE                    : 0.2020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1863                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 314                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 12.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.64000                                              
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : -0.59000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.06000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.089         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.052         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.439         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1909 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1254 ; 0.020 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2586 ; 1.387 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3129 ; 0.970 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   256 ; 6.037 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    68 ;34.780 ;26.912       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   366 ;12.611 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;13.853 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   316 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2105 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   331 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1231 ; 0.826 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   517 ; 0.188 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1996 ; 1.528 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   678 ; 2.204 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   585 ; 3.609 ; 4.500       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3AUM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB029714.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NW12A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30877                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: 2OY5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24.4(MG/ML) PROTEIN, 17% PEG4000, 8.5%   
REMARK 280  ISOPROPANOL, 15% GLYCEROL, 0.1M TRIS-HCL, PH 8.0, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       26.51800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O                                     
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 O    23                                                      
REMARK 465     SER O    24                                                      
REMARK 465     HIS O    25                                                      
REMARK 465     MET O    26                                                      
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 O  59       60.66     36.86                                   
REMARK 500    ALA O  60      -12.96     80.54                                   
REMARK 500    ALA O  83        3.66     82.92                                   
REMARK 500    LYS O 119      -65.74   -133.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3AUM O   27   273  UNP    P0C926   OSPA1_BORBU     27    273             
SEQADV 3AUM GLY O   23  UNP  P0C926              EXPRESSION TAG                 
SEQADV 3AUM SER O   24  UNP  P0C926              EXPRESSION TAG                 
SEQADV 3AUM HIS O   25  UNP  P0C926              EXPRESSION TAG                 
SEQADV 3AUM MET O   26  UNP  P0C926              EXPRESSION TAG                 
SEQADV 3AUM SER O   37  UNP  P0C926    GLU    37 ENGINEERED MUTATION            
SEQADV 3AUM SER O   45  UNP  P0C926    GLU    45 ENGINEERED MUTATION            
SEQADV 3AUM SER O   46  UNP  P0C926    LYS    46 ENGINEERED MUTATION            
SEQADV 3AUM ALA O   48  UNP  P0C926    LYS    48 ENGINEERED MUTATION            
SEQADV 3AUM ALA O   60  UNP  P0C926    LYS    60 ENGINEERED MUTATION            
SEQADV 3AUM SER O   64  UNP  P0C926    LYS    64 ENGINEERED MUTATION            
SEQADV 3AUM ALA O   83  UNP  P0C926    LYS    83 ENGINEERED MUTATION            
SEQADV 3AUM SER O  104  UNP  P0C926    GLU   104 ENGINEERED MUTATION            
SEQADV 3AUM SER O  107  UNP  P0C926    LYS   107 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  111  UNP  P0C926    SER   111 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  113  UNP  P0C926    LYS   113 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  115  UNP  P0C926    THR   115 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  121  UNP  P0C926    SER   121 ENGINEERED MUTATION            
SEQADV 3AUM TRP O  123  UNP  P0C926    GLU   123 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  125  UNP  P0C926    LYS   125 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  134  UNP  P0C926    GLU   134 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  136  UNP  P0C926    ILE   136 ENGINEERED MUTATION            
SEQADV 3AUM TYR O  138  UNP  P0C926    THR   138 ENGINEERED MUTATION            
SEQADV 3AUM SER O  239  UNP  P0C926    LYS   239 ENGINEERED MUTATION            
SEQADV 3AUM SER O  240  UNP  P0C926    GLU   240 ENGINEERED MUTATION            
SEQADV 3AUM SER O  254  UNP  P0C926    LYS   254 ENGINEERED MUTATION            
SEQRES   1 O  251  GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO          
SEQRES   2 O  251  GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA          
SEQRES   3 O  251  ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU          
SEQRES   4 O  251  GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY          
SEQRES   5 O  251  VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS          
SEQRES   6 O  251  LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU          
SEQRES   7 O  251  VAL PHE LYS SER ASP GLY SER THR LEU VAL TYR LYS TYR          
SEQRES   8 O  251  VAL TYR SER LYS ASP LYS SER TYR THR TRP GLU TYR PHE          
SEQRES   9 O  251  ASN GLU LYS GLY GLU VAL SER TYR LYS TYR ILE TYR ARG          
SEQRES  10 O  251  ALA ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER          
SEQRES  11 O  251  ASP GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR          
SEQRES  12 O  251  VAL LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU          
SEQRES  13 O  251  VAL VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE          
SEQRES  14 O  251  SER LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR          
SEQRES  15 O  251  ASP SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN          
SEQRES  16 O  251  SER GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS          
SEQRES  17 O  251  LYS THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE          
SEQRES  18 O  251  THR VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU          
SEQRES  19 O  251  GLY SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS          
SEQRES  20 O  251  ASN ALA LEU LYS                                              
FORMUL   2  HOH   *314(H2 O)                                                    
HELIX    1   1 LYS O  264  LYS O  273  1                                  10    
SHEET    1   A 4 SER O  29  ASP O  33  0                                        
SHEET    2   A 4 LYS O  39  SER O  43 -1  O  VAL O  42   N  VAL O  30           
SHEET    3   A 4 TYR O  52  VAL O  58 -1  O  ILE O  55   N  LEU O  41           
SHEET    4   A 4 LEU O  61  SER O  67 -1  O  LEU O  63   N  ALA O  56           
SHEET    1   B12 GLY O  74  VAL O  79  0                                        
SHEET    2   B12 LYS O  85  ILE O  90 -1  O  ILE O  90   N  GLY O  74           
SHEET    3   B12 GLN O  96  PHE O 102 -1  O  PHE O 102   N  LYS O  85           
SHEET    4   B12 LEU O 109  SER O 116 -1  O  VAL O 110   N  VAL O 101           
SHEET    5   B12 SER O 120  PHE O 126 -1  O  SER O 120   N  SER O 116           
SHEET    6   B12 VAL O 132  ARG O 139 -1  O  SER O 133   N  TYR O 125           
SHEET    7   B12 ARG O 144  THR O 148 -1  O  LEU O 145   N  ILE O 137           
SHEET    8   B12 GLY O 156  LEU O 162 -1  O  LYS O 157   N  THR O 148           
SHEET    9   B12 TYR O 165  LEU O 171 -1  O  LEU O 167   N  GLU O 160           
SHEET   10   B12 LYS O 175  GLU O 182 -1  O  THR O 177   N  THR O 170           
SHEET   11   B12 VAL O 185  SER O 192 -1  O  LEU O 187   N  VAL O 180           
SHEET   12   B12 VAL O 197  ASP O 203 -1  O  SER O 198   N  ASN O 190           
SHEET    1   C 5 LYS O 212  ASN O 217  0                                        
SHEET    2   C 5 THR O 222  VAL O 227 -1  O  THR O 226   N  THR O 213           
SHEET    3   C 5 LYS O 230  PHE O 237 -1  O  LEU O 235   N  LEU O 223           
SHEET    4   C 5 ILE O 243  GLN O 247 -1  O  GLN O 246   N  ASP O 234           
SHEET    5   C 5 VAL O 260  GLU O 261 -1  O  VAL O 260   N  VAL O 245           
CRYST1   35.241   53.036   65.093  90.00  96.97  90.00 P 1 21 1      2          
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      0.028376  0.000000  0.003471        0.00000                         
SCALE2      0.000000  0.018855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015477        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system