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Database: PDB
Entry: 2OL7
LinkDB: 2OL7
Original site: 2OL7 
HEADER    MEMBRANE PROTEIN                        18-JAN-07   2OL7              
TITLE     THE CRYSTAL STRUCTURE OF OSPA MUTANT                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OUTER SURFACE PROTEIN A;                                   
COMPND   3 CHAIN: A, B;                                                         
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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24A                                    
KEYWDS    BETA-SHEET, MEMBRANE PROTEIN                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MAKABE,V.TERECHKO,S.KOIDE                                           
REVDAT   2   24-FEB-09 2OL7    1       VERSN                                    
REVDAT   1   11-DEC-07 2OL7    0                                                
JRNL        AUTH   K.MAKABE,S.YAN,V.TERESHKO,G.GAWLAK,S.KOIDE                   
JRNL        TITL   BETA-STRAND FLIPPING AND SLIPPING TRIGGERED BY               
JRNL        TITL 2 TURN REPLACEMENT REVEAL THE OPPORTUNISTIC NATURE             
JRNL        TITL 3 OF BETA-STRAND PAIRING                                       
JRNL        REF    J.AM.CHEM.SOC.                V. 129 14661 2007              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   17985889                                                     
JRNL        DOI    10.1021/JA074252C                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 97870                          
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) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5139                            
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) : 1.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6713                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 354                          
REMARK   3   BIN FREE R VALUE                    : 0.2470                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3767                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 568                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.91000                                              
REMARK   3    B22 (A**2) : -0.31000                                             
REMARK   3    B33 (A**2) : -0.49000                                             
REMARK   3    B12 (A**2) : 0.22000                                              
REMARK   3    B13 (A**2) : -0.18000                                             
REMARK   3    B23 (A**2) : -0.20000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.070         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.064         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.036         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.902         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.941                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3806 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3561 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5158 ; 1.479 ; 1.994       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8448 ; 0.749 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   536 ; 7.118 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   120 ;39.637 ;28.083       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   792 ;11.997 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ;20.900 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   661 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4164 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   594 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   615 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3355 ; 0.200 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1902 ; 0.159 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2238 ; 0.083 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   367 ; 0.158 ; 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):    14 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    56 ; 0.245 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    45 ; 0.176 ; 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):  3278 ; 2.043 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1056 ; 0.678 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4093 ; 2.168 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1452 ; 3.469 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1043 ; 4.414 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  8455 ; 2.142 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   568 ; 7.202 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  7328 ; 2.475 ; 3.000       
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   : 1.20                                          
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 2OL7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041274.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 103051                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.8700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.340                              
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 2G8C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 6% ISOPROPANOL, 200MM       
REMARK 280  NACL, AND 100 MM HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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    23                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     LYS B    27                                                      
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    ALA A  83      -13.38     90.15                                   
REMARK 500    ALA B  83        1.61     84.74                                   
REMARK 500    SER B 107      -38.57   -130.08                                   
REMARK 500    ASP B 118     -120.48   -135.50                                   
REMARK 500    SER B 120      -47.49    169.99                                   
REMARK 500    ILE B 137       64.84   -114.96                                   
REMARK 500    THR B 138      133.53    -23.38                                   
REMARK 500    ARG B 139      -55.87   -130.48                                   
REMARK 500    ALA B 140      -34.77    151.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  119     SER B  120                  -64.41                    
REMARK 500 ILE B  137     THR B  138                  125.00                    
REMARK 500 THR B  138     ARG B  139                 -141.19                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OL6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OL8   RELATED DB: PDB                                   
DBREF  2OL7 A   27   273  UNP    Q45040   Q45040_BORBU    27    273             
DBREF  2OL7 B   27   273  UNP    Q45040   Q45040_BORBU    27    273             
SEQADV 2OL7 GLY A   23  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 SER A   24  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 HIS A   25  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 MET A   26  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 SER A   37  UNP  Q45040    GLU    37 ENGINEERED                     
SEQADV 2OL7 SER A   45  UNP  Q45040    GLU    45 ENGINEERED                     
SEQADV 2OL7 SER A   46  UNP  Q45040    LYS    46 ENGINEERED                     
SEQADV 2OL7 ALA A   48  UNP  Q45040    LYS    48 ENGINEERED                     
SEQADV 2OL7 ALA A   60  UNP  Q45040    LYS    60 ENGINEERED                     
SEQADV 2OL7 SER A   64  UNP  Q45040    LYS    64 ENGINEERED                     
SEQADV 2OL7 ALA A   83  UNP  Q45040    LYS    83 ENGINEERED                     
SEQADV 2OL7 SER A  104  UNP  Q45040    GLU   104 ENGINEERED                     
SEQADV 2OL7 SER A  107  UNP  Q45040    LYS   107 ENGINEERED                     
SEQADV 2OL7 ILE A  126  UNP  Q45040    PHE   126 ENGINEERED                     
SEQADV 2OL7 ILE A  127  UNP  Q45040    ASN   127 ENGINEERED                     
SEQADV 2OL7 ILE A  128  UNP  Q45040    GLU   128 ENGINEERED                     
SEQADV 2OL7 ASP A  129  UNP  Q45040    LYS   129 ENGINEERED                     
SEQADV 2OL7 ILE A  131  UNP  Q45040    GLU   131 ENGINEERED                     
SEQADV 2OL7 ILE A  132  UNP  Q45040    VAL   132 ENGINEERED                     
SEQADV 2OL7 ILE A  133  UNP  Q45040    SER   133 ENGINEERED                     
SEQADV 2OL7 SER A  239  UNP  Q45040    LYS   239 ENGINEERED                     
SEQADV 2OL7 SER A  240  UNP  Q45040    GLU   240 ENGINEERED                     
SEQADV 2OL7 SER A  254  UNP  Q45040    LYS   254 ENGINEERED                     
SEQADV 2OL7 GLY B   23  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 SER B   24  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 HIS B   25  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 MET B   26  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OL7 SER B   37  UNP  Q45040    GLU    37 ENGINEERED                     
SEQADV 2OL7 SER B   45  UNP  Q45040    GLU    45 ENGINEERED                     
SEQADV 2OL7 SER B   46  UNP  Q45040    LYS    46 ENGINEERED                     
SEQADV 2OL7 ALA B   48  UNP  Q45040    LYS    48 ENGINEERED                     
SEQADV 2OL7 ALA B   60  UNP  Q45040    LYS    60 ENGINEERED                     
SEQADV 2OL7 SER B   64  UNP  Q45040    LYS    64 ENGINEERED                     
SEQADV 2OL7 ALA B   83  UNP  Q45040    LYS    83 ENGINEERED                     
SEQADV 2OL7 SER B  104  UNP  Q45040    GLU   104 ENGINEERED                     
SEQADV 2OL7 SER B  107  UNP  Q45040    LYS   107 ENGINEERED                     
SEQADV 2OL7 ILE B  126  UNP  Q45040    PHE   126 ENGINEERED                     
SEQADV 2OL7 ILE B  127  UNP  Q45040    ASN   127 ENGINEERED                     
SEQADV 2OL7 ILE B  128  UNP  Q45040    GLU   128 ENGINEERED                     
SEQADV 2OL7 ASP B  129  UNP  Q45040    LYS   129 ENGINEERED                     
SEQADV 2OL7 ILE B  131  UNP  Q45040    GLU   131 ENGINEERED                     
SEQADV 2OL7 ILE B  132  UNP  Q45040    VAL   132 ENGINEERED                     
SEQADV 2OL7 ILE B  133  UNP  Q45040    SER   133 ENGINEERED                     
SEQADV 2OL7 SER B  239  UNP  Q45040    LYS   239 ENGINEERED                     
SEQADV 2OL7 SER B  240  UNP  Q45040    GLU   240 ENGINEERED                     
SEQADV 2OL7 SER B  254  UNP  Q45040    LYS   254 ENGINEERED                     
SEQRES   1 A  251  GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO          
SEQRES   2 A  251  GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA          
SEQRES   3 A  251  ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU          
SEQRES   4 A  251  GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY          
SEQRES   5 A  251  VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS          
SEQRES   6 A  251  LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU          
SEQRES   7 A  251  VAL PHE LYS SER ASP GLY SER THR LEU VAL SER LYS LYS          
SEQRES   8 A  251  VAL THR SER LYS ASP LYS SER SER THR GLU GLU LYS ILE          
SEQRES   9 A  251  ILE ILE ASP GLY ILE ILE ILE GLU LYS ILE ILE THR ARG          
SEQRES  10 A  251  ALA ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER          
SEQRES  11 A  251  ASP GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR          
SEQRES  12 A  251  VAL LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU          
SEQRES  13 A  251  VAL VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE          
SEQRES  14 A  251  SER LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR          
SEQRES  15 A  251  ASP SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN          
SEQRES  16 A  251  SER GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS          
SEQRES  17 A  251  LYS THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE          
SEQRES  18 A  251  THR VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU          
SEQRES  19 A  251  GLY SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS          
SEQRES  20 A  251  ASN ALA LEU LYS                                              
SEQRES   1 B  251  GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO          
SEQRES   2 B  251  GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA          
SEQRES   3 B  251  ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU          
SEQRES   4 B  251  GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY          
SEQRES   5 B  251  VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS          
SEQRES   6 B  251  LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU          
SEQRES   7 B  251  VAL PHE LYS SER ASP GLY SER THR LEU VAL SER LYS LYS          
SEQRES   8 B  251  VAL THR SER LYS ASP LYS SER SER THR GLU GLU LYS ILE          
SEQRES   9 B  251  ILE ILE ASP GLY ILE ILE ILE GLU LYS ILE ILE THR ARG          
SEQRES  10 B  251  ALA ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER          
SEQRES  11 B  251  ASP GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR          
SEQRES  12 B  251  VAL LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU          
SEQRES  13 B  251  VAL VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE          
SEQRES  14 B  251  SER LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR          
SEQRES  15 B  251  ASP SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN          
SEQRES  16 B  251  SER GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS          
SEQRES  17 B  251  LYS THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE          
SEQRES  18 B  251  THR VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU          
SEQRES  19 B  251  GLY SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS          
SEQRES  20 B  251  ASN ALA LEU LYS                                              
FORMUL   3  HOH   *568(H2 O)                                                    
HELIX    1   1 LYS A  264  LYS A  273  1                                  10    
HELIX    2   2 LYS B  264  LEU B  272  1                                   9    
SHEET    1   A 4 SER A  29  ASP A  33  0                                        
SHEET    2   A 4 LYS A  39  SER A  43 -1  O  VAL A  40   N  VAL A  32           
SHEET    3   A 4 TYR A  52  VAL A  58 -1  O  ILE A  55   N  LEU A  41           
SHEET    4   A 4 LEU A  61  SER A  67 -1  O  LEU A  63   N  ALA A  56           
SHEET    1   B12 GLY A  74  VAL A  79  0                                        
SHEET    2   B12 LYS A  85  ILE A  90 -1  O  ILE A  90   N  GLY A  74           
SHEET    3   B12 GLN A  96  PHE A 102 -1  O  PHE A 102   N  LYS A  85           
SHEET    4   B12 LEU A 109  LYS A 117 -1  O  VAL A 110   N  VAL A 101           
SHEET    5   B12 SER A 121  ILE A 128 -1  O  ILE A 127   N  LYS A 112           
SHEET    6   B12 ILE A 131  ARG A 139 -1  O  THR A 138   N  THR A 122           
SHEET    7   B12 ARG A 144  THR A 148 -1  O  LEU A 145   N  ILE A 137           
SHEET    8   B12 GLY A 156  VAL A 161 -1  O  LYS A 159   N  GLU A 146           
SHEET    9   B12 VAL A 166  LEU A 171 -1  O  LEU A 167   N  GLU A 160           
SHEET   10   B12 LYS A 175  GLU A 182 -1  O  THR A 177   N  THR A 170           
SHEET   11   B12 VAL A 185  SER A 192 -1  O  LYS A 189   N  LEU A 178           
SHEET   12   B12 VAL A 197  ASP A 203 -1  O  SER A 198   N  ASN A 190           
SHEET    1   C 5 LYS A 212  ASN A 217  0                                        
SHEET    2   C 5 THR A 222  VAL A 227 -1  O  THR A 224   N  ALA A 215           
SHEET    3   C 5 LYS A 230  PHE A 237 -1  O  THR A 232   N  ILE A 225           
SHEET    4   C 5 ILE A 243  GLN A 247 -1  O  GLN A 246   N  ASP A 234           
SHEET    5   C 5 VAL A 260  GLU A 261 -1  O  VAL A 260   N  VAL A 245           
SHEET    1   D 4 VAL B  30  ASP B  33  0                                        
SHEET    2   D 4 LYS B  39  VAL B  42 -1  O  VAL B  42   N  VAL B  30           
SHEET    3   D 4 TYR B  52  VAL B  58 -1  O  ILE B  55   N  LEU B  41           
SHEET    4   D 4 LEU B  61  SER B  67 -1  O  LEU B  63   N  ALA B  56           
SHEET    1   E12 GLY B  74  VAL B  79  0                                        
SHEET    2   E12 LYS B  85  ILE B  90 -1  O  ILE B  90   N  GLY B  74           
SHEET    3   E12 GLN B  96  PHE B 102 -1  O  PHE B 102   N  LYS B  85           
SHEET    4   E12 LEU B 109  LYS B 117 -1  O  VAL B 110   N  VAL B 101           
SHEET    5   E12 THR B 122  ILE B 128 -1  O  GLU B 123   N  SER B 116           
SHEET    6   E12 ILE B 131  THR B 138 -1  O  ILE B 136   N  GLU B 124           
SHEET    7   E12 ARG B 144  THR B 148 -1  O  LEU B 145   N  ILE B 137           
SHEET    8   E12 GLY B 156  VAL B 161 -1  O  LYS B 159   N  GLU B 146           
SHEET    9   E12 VAL B 166  LEU B 171 -1  O  LEU B 171   N  GLY B 156           
SHEET   10   E12 THR B 176  GLU B 182 -1  O  THR B 177   N  THR B 170           
SHEET   11   E12 VAL B 185  ILE B 191 -1  O  LYS B 189   N  LEU B 178           
SHEET   12   E12 VAL B 197  ASP B 203 -1  O  SER B 198   N  ASN B 190           
SHEET    1   F 5 LYS B 212  ASN B 217  0                                        
SHEET    2   F 5 THR B 222  VAL B 227 -1  O  THR B 224   N  ALA B 215           
SHEET    3   F 5 LYS B 230  PHE B 237 -1  O  THR B 232   N  ILE B 225           
SHEET    4   F 5 ILE B 243  GLN B 247 -1  O  GLN B 246   N  ASP B 234           
SHEET    5   F 5 VAL B 260  GLU B 261 -1  O  VAL B 260   N  VAL B 245           
CRYST1   37.127   55.333   64.789  85.68  74.05  86.45 P 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      0.026935 -0.001671 -0.007608        0.00000                         
SCALE2      0.000000  0.018107 -0.001101        0.00000                         
SCALE3      0.000000  0.000000  0.016082        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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