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Database: PDB
Entry: 1RJL
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HEADER    IMMUNE SYSTEM                           19-NOV-03   1RJL              
TITLE     STRUCTURE OF THE COMPLEX BETWEEN OSPB-CT AND BACTERICIDAL             
TITLE    2 FAB-H6831                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAB H6831 L-CHAIN;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: FAB H6831 H-CHAIN;                                         
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: OUTER SURFACE PROTEIN B;                                   
COMPND   9 CHAIN: C;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 4;                                                           
COMPND  12 MOLECULE: OUTER SURFACE PROTEIN B;                                   
COMPND  13 CHAIN: D;                                                            
COMPND  14 FRAGMENT: 5-RESIDUE POLYUNKNOWN FRAGMENT;                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: BALB-C;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   8 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   9 ORGANISM_TAXID: 10090;                                               
SOURCE  10 STRAIN: BALB-C;                                                      
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;                           
SOURCE  13 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;                            
SOURCE  14 ORGANISM_TAXID: 139;                                                 
SOURCE  15 GENE: OSPB, BBA16;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL2(DE3)/PLYSS;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET9C;                                    
SOURCE  21 MOL_ID: 4;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;                           
SOURCE  23 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;                            
SOURCE  24 ORGANISM_TAXID: 139;                                                 
SOURCE  25 GENE: OSPB, BBA16;                                                   
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL2(DE3)/PLYSS;                            
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET9C                                     
KEYWDS    BETA SHEET, ANTIBODY-PROTEIN COMPLEX, IMMUNE SYSTEM                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BECKER,J.BUNIKIS,B.D.LADE,J.J.DUNN,A.G.BARBOUR,C.L.LAWSON           
REVDAT   3   24-FEB-09 1RJL    1       VERSN                                    
REVDAT   2   03-MAY-05 1RJL    1       JRNL                                     
REVDAT   1   30-NOV-04 1RJL    0                                                
JRNL        AUTH   M.BECKER,J.BUNIKIS,B.D.LADE,J.J.DUNN,A.G.BARBOUR,            
JRNL        AUTH 2 C.L.LAWSON                                                   
JRNL        TITL   STRUCTURAL INVESTIGATION OF BORRELIA BURGDORFERI             
JRNL        TITL 2 OSPB, A BACTERICIDALFAB TARGET.                              
JRNL        REF    J.BIOL.CHEM.                  V. 280 17363 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15713683                                                     
JRNL        DOI    10.1074/JBC.M412842200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 17715                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1745                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.72                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1827                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE                    : 0.2430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 211                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.58000                                             
REMARK   3    B22 (A**2) : 10.27000                                             
REMARK   3    B33 (A**2) : -4.69000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.510 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.670 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.980 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.040 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS BULK SOLVENT MODEL USED                          
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 35.24                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PROTEIN.TOP                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1RJL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020807.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 288                                
REMARK 200  PH                             : 5.6; 5.6; 7.5                      
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : BRANDEIS                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17715                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: FAB PORTION OF PDB ENTRY 1OSP                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM CITRATE, PH 5.6,         
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K. PEG 3350,          
REMARK 280  SODIUM CITRATE, ISOPROPANOL, PH 5.6, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 277K. PEG 3350, PROPIONAMIDE, MOPS, AMMONIUM      
REMARK 280  SULFATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       93.14300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       18.63550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.14300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       18.63550            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY CONSISTS                             
REMARK 300 OF ONE FAB:OSPB-CT COMPLEX, WHICH                                    
REMARK 300 FORMS THE ASYMMETRIC UNIT.                                           
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CB   UNK D   3  LIES ON A SPECIAL POSITION.                          
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    ILE A  29   CA  -  C   -  N   ANGL. DEV. =  25.6 DEGREES          
REMARK 500    ILE A  29   O   -  C   -  N   ANGL. DEV. = -39.2 DEGREES          
REMARK 500    GLY B 140   C   -  N   -  CA  ANGL. DEV. = -18.3 DEGREES          
REMARK 500    SER B 141   N   -  CA  -  C   ANGL. DEV. = -20.7 DEGREES          
REMARK 500    GLU B 155   CA  -  C   -  N   ANGL. DEV. =  38.1 DEGREES          
REMARK 500    GLU B 155   O   -  C   -  N   ANGL. DEV. = -46.6 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                                                                      
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  51      -16.80     55.53                                   
REMARK 500    SER A 127       12.58   -144.77                                   
REMARK 500    ASN A 138       72.36     42.52                                   
REMARK 500    SER A 201      138.09   -174.78                                   
REMARK 500    ASN A 210      -88.28   -121.12                                   
REMARK 500    ARG A 211      -11.95   -164.55                                   
REMARK 500    GLU B  62      -36.66    -36.18                                   
REMARK 500    SER B  85       64.76     38.47                                   
REMARK 500    ALA B  92     -178.75    173.72                                   
REMARK 500    TYR B 101     -130.67    -90.43                                   
REMARK 500    TYR B 104      -63.01    -94.48                                   
REMARK 500    PRO B 133      171.70    -56.61                                   
REMARK 500    CYS B 135      123.39     -6.91                                   
REMARK 500    ASP B 137     -136.10   -135.65                                   
REMARK 500    THR B 138       80.22     50.90                                   
REMARK 500    PRO B 154       95.72    -55.82                                   
REMARK 500    SER B 163       18.45     52.81                                   
REMARK 500    GLN B 178      113.32   -170.14                                   
REMARK 500    GLU C 217       33.65    -84.70                                   
REMARK 500    LYS C 218       -3.20     46.61                                   
REMARK 500    THR C 255      -47.60   -135.55                                   
REMARK 500    ASP C 263      -13.93    -49.28                                   
REMARK 500    LYS C 286      -76.19    -88.37                                   
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 ILE A   29     ASN A   30                 -117.31                    
REMARK 500 GLY B  140     SER B  141                 -114.12                    
REMARK 500 GLU B  155     SER B  156                   84.75                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ILE A  29        -34.71                                           
REMARK 500    GLU B 155         34.19                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1P4P   RELATED DB: PDB                                   
REMARK 900 OSPB-CT ALONE                                                        
REMARK 900 RELATED ID: 1FJ1   RELATED DB: PDB                                   
REMARK 900 OSPA + FAB LA-2                                                      
REMARK 900 RELATED ID: 1OSP   RELATED DB: PDB                                   
REMARK 900 OSPA + AN N-TERM FAB                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 CHAINS A AND B:  NO SUITABLE SEQUENCE DATABASE REFERENCE             
REMARK 999 WAS FOUND AT THE TIME OF PROCESSING.                                 
REMARK 999                                                                      
REMARK 999 CHAIN C: THE SEQUENCE LISTED IN THE SEQRES FOR CHAIN C IS            
REMARK 999 THE PORTION OF THE FOLLOWING CONSTRUCT THAT WAS CLEARLY              
REMARK 999 OBSERVED IN THE DENSITY:                                             
REMARK 999                                                                      
REMARK 999 ANKLDSKKLTRSNGTTLEYSQITDADNATKAVETLKNSIKLEGSLVVGKTTVEIK              
REMARK 999 EGTVTLKREIEKDGKVKVFLNDTAGSNKKTGKWEDSTSTLTISADSKKTKDLVFL              
REMARK 999 TDGTITVQQYNTAGTSLEGSASEIKNLSELKNALK                                  
REMARK 999                                                                      
REMARK 999 THE AUTHORS DO NOT KNOW IF THE PORTION OF THE CONSTRUCT              
REMARK 999 THAT WAS NOT OBSERVED IN THE DENSITY WAS MISSING DUE TO              
REMARK 999 PROTEOLYSIS, OR WAS DISORDERED IN THE CRYSTAL.                       
REMARK 999                                                                      
REMARK 999 CHAIN D:  THE AUTHORS SAW AN EXTRA BETA STRAND                       
REMARK 999 OF DENSITY THAT WAS NOT CONTINUOUS WITH THE MAIN BODY OF             
REMARK 999 DENSITY (I.E. THERE WAS NO DENSITY FOR A CONNECTING                  
REMARK 999 LOOP) AND THAT DID NOT SHOW CLEAR SIDECHAIN DENSITY.                 
REMARK 999 THIS STRAND PRESUMABLY ARISES FROM SOME PORTION OR PORTIONS          
REMARK 999 OF THE REMAINING 'UNOBSERVED' SEQUENCE ABOVE, BUT SINCE              
REMARK 999 THE REGISTER WAS UNKNOWN, THE AUTHORS MODELLED IT AS A               
REMARK 999 POLYALANINE STRAND, LISTED IN THE SEQRES AND COORDINATES             
REMARK 999 AS UNK, UNKNOWN RESIDUE.                                             
DBREF  1RJL C  202   296  UNP    P17739   OSPB1_BORBU    202    296             
DBREF  1RJL A    1   212  PDB    1RJL     1RJL             1    212             
DBREF  1RJL B    1   221  PDB    1RJL     1RJL             1    221             
DBREF  1RJL D    1     5  PDB    1RJL     1RJL             1      5             
SEQRES   1 A  212  ASP ILE GLN MET ASN GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 A  212  SER LEU GLY ASP THR ILE THR ILE THR CYS HIS ALA SER          
SEQRES   3 A  212  GLN ASN ILE ASN VAL TRP LEU ASN TRP PHE GLN GLN LYS          
SEQRES   4 A  212  PRO GLY SER ILE PRO LYS LEU LEU ILE TYR MET ALA SER          
SEQRES   5 A  212  ASN LEU HIS THR GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 A  212  GLY SER GLY THR GLY PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 A  212  GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN GLY          
SEQRES   8 A  212  GLN SER PHE PRO LEU THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 A  212  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 A  212  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 A  212  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 A  212  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 A  212  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 A  212  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 A  212  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 A  212  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 A  212  PHE ASN ARG ASN                                              
SEQRES   1 B  221  GLN VAL GLN LEU GLN GLN PRO GLY SER VAL LEU VAL ARG          
SEQRES   2 B  221  PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER GLY          
SEQRES   3 B  221  PHE THR PHE THR SER SER TRP MET HIS TRP ALA LYS GLN          
SEQRES   4 B  221  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE HIS          
SEQRES   5 B  221  PRO ASN SER GLY ASN THR HIS TYR ASN GLU LYS PHE LYS          
SEQRES   6 B  221  GLY LYS ALA THR LEU THR VAL ASP THR SER SER SER THR          
SEQRES   7 B  221  ALA TYR VAL ASP LEU SER SER LEU THR SER GLU ASP SER          
SEQRES   8 B  221  ALA VAL TYR TYR CYS ALA ARG MET ARG TYR GLY ASP TYR          
SEQRES   9 B  221  TYR ALA MET ASP ASN TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 B  221  VAL SER SER ALA LYS THR THR ALA PRO PRO VAL TYR PRO          
SEQRES  11 B  221  LEU ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL          
SEQRES  12 B  221  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER          
SEQRES  13 B  221  VAL THR LEU LEU TRP ASN SER GLY SER LEU SER SER GLY          
SEQRES  14 B  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR          
SEQRES  15 B  221  THR LEU SER SER SER VAL THR VAL THR SER SER THR TRP          
SEQRES  16 B  221  PRO SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA          
SEQRES  17 B  221  SER SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY          
SEQRES   1 C   95  THR VAL GLU ILE LYS GLU GLY THR VAL THR LEU LYS ARG          
SEQRES   2 C   95  GLU ILE GLU LYS ASP GLY LYS VAL LYS VAL PHE LEU ASN          
SEQRES   3 C   95  ASP THR ALA GLY SER ASN LYS LYS THR GLY LYS TRP GLU          
SEQRES   4 C   95  ASP SER THR SER THR LEU THR ILE SER ALA ASP SER LYS          
SEQRES   5 C   95  LYS THR LYS ASP LEU VAL PHE LEU THR ASP GLY THR ILE          
SEQRES   6 C   95  THR VAL GLN GLN TYR ASN THR ALA GLY THR SER LEU GLU          
SEQRES   7 C   95  GLY SER ALA SER GLU ILE LYS ASN LEU SER GLU LEU LYS          
SEQRES   8 C   95  ASN ALA LEU LYS                                              
SEQRES   1 D    5  UNK UNK UNK UNK UNK                                          
FORMUL   5  HOH   *144(H2 O)                                                    
HELIX    1   1 SER A  121  THR A  126  1                                   6    
HELIX    2   2 LYS A  183  GLU A  187  1                                   5    
HELIX    3   3 ASN C  287  LYS C  296  1                                  10    
SHEET    1   A 4 MET A   4  SER A   7  0                                        
SHEET    2   A 4 ILE A  19  ALA A  25 -1  O  HIS A  24   N  ASN A   5           
SHEET    3   A 4 GLY A  70  ILE A  75 -1  O  PHE A  71   N  CYS A  23           
SHEET    4   A 4 PHE A  62  SER A  67 -1  N  SER A  63   O  THR A  74           
SHEET    1   B 6 SER A  10  ALA A  13  0                                        
SHEET    2   B 6 THR A 102  ILE A 106  1  O  GLU A 105   N  LEU A  11           
SHEET    3   B 6 THR A  85  GLN A  90 -1  N  TYR A  86   O  THR A 102           
SHEET    4   B 6 LEU A  33  GLN A  38 -1  N  PHE A  36   O  TYR A  87           
SHEET    5   B 6 LYS A  45  TYR A  49 -1  O  LEU A  47   N  TRP A  35           
SHEET    6   B 6 ASN A  53  LEU A  54 -1  O  ASN A  53   N  TYR A  49           
SHEET    1   C 4 SER A  10  ALA A  13  0                                        
SHEET    2   C 4 THR A 102  ILE A 106  1  O  GLU A 105   N  LEU A  11           
SHEET    3   C 4 THR A  85  GLN A  90 -1  N  TYR A  86   O  THR A 102           
SHEET    4   C 4 THR A  97  PHE A  98 -1  O  THR A  97   N  GLN A  90           
SHEET    1   D 4 THR A 114  PHE A 118  0                                        
SHEET    2   D 4 GLY A 129  PHE A 139 -1  O  VAL A 133   N  PHE A 118           
SHEET    3   D 4 TYR A 173  THR A 182 -1  O  LEU A 179   N  VAL A 132           
SHEET    4   D 4 VAL A 159  TRP A 163 -1  N  LEU A 160   O  THR A 178           
SHEET    1   E 4 SER A 153  ARG A 155  0                                        
SHEET    2   E 4 ASN A 145  ILE A 150 -1  N  ILE A 150   O  SER A 153           
SHEET    3   E 4 TYR A 192  THR A 197 -1  O  GLU A 195   N  LYS A 147           
SHEET    4   E 4 ILE A 205  PHE A 209 -1  O  PHE A 209   N  TYR A 192           
SHEET    1   F 4 GLN B   3  GLN B   5  0                                        
SHEET    2   F 4 VAL B  18  SER B  25 -1  O  SER B  25   N  GLN B   3           
SHEET    3   F 4 THR B  78  LEU B  83 -1  O  VAL B  81   N  LEU B  20           
SHEET    4   F 4 ALA B  68  ASP B  73 -1  N  THR B  71   O  TYR B  80           
SHEET    1   G 6 SER B   9  VAL B  12  0                                        
SHEET    2   G 6 THR B 114  VAL B 118  1  O  THR B 117   N  VAL B  10           
SHEET    3   G 6 ALA B  92  ARG B 100 -1  N  ALA B  92   O  VAL B 116           
SHEET    4   G 6 MET B  34  ARG B  40 -1  N  ALA B  37   O  TYR B  95           
SHEET    5   G 6 GLY B  44  ILE B  51 -1  O  GLU B  46   N  LYS B  38           
SHEET    6   G 6 THR B  58  TYR B  60 -1  O  HIS B  59   N  GLU B  50           
SHEET    1   H 4 SER B   9  VAL B  12  0                                        
SHEET    2   H 4 THR B 114  VAL B 118  1  O  THR B 117   N  VAL B  10           
SHEET    3   H 4 ALA B  92  ARG B 100 -1  N  ALA B  92   O  VAL B 116           
SHEET    4   H 4 ALA B 106  TRP B 110 -1  O  ASN B 109   N  ARG B  98           
SHEET    1   I 4 VAL B 128  LEU B 131  0                                        
SHEET    2   I 4 VAL B 143  TYR B 152 -1  O  GLY B 146   N  LEU B 131           
SHEET    3   I 4 TYR B 182  VAL B 190 -1  O  TYR B 182   N  TYR B 152           
SHEET    4   I 4 VAL B 170  THR B 172 -1  N  HIS B 171   O  SER B 187           
SHEET    1   J 4 VAL B 128  LEU B 131  0                                        
SHEET    2   J 4 VAL B 143  TYR B 152 -1  O  GLY B 146   N  LEU B 131           
SHEET    3   J 4 TYR B 182  VAL B 190 -1  O  TYR B 182   N  TYR B 152           
SHEET    4   J 4 VAL B 176  LEU B 177 -1  N  VAL B 176   O  THR B 183           
SHEET    1   K 3 THR B 158  TRP B 161  0                                        
SHEET    2   K 3 THR B 201  HIS B 206 -1  O  ASN B 203   N  LEU B 160           
SHEET    3   K 3 THR B 211  LYS B 216 -1  O  VAL B 213   N  VAL B 204           
SHEET    1   L 4 VAL C 222  ASP C 228  0                                        
SHEET    2   L 4 VAL C 210  ILE C 216 -1  N  THR C 211   O  ASN C 227           
SHEET    3   L 4 VAL C 203  GLU C 207 -1  N  ILE C 205   O  LEU C 212           
SHEET    1   M 5 LYS C 235  GLU C 240  0                                        
SHEET    2   M 5 THR C 245  ALA C 250 -1  O  THR C 245   N  GLU C 240           
SHEET    3   M 5 LYS C 253  PHE C 260 -1  O  LEU C 258   N  LEU C 246           
SHEET    4   M 5 ILE C 266  GLN C 270 -1  O  GLN C 269   N  ASP C 257           
SHEET    5   M 5 SER C 283  GLU C 284 -1  O  SER C 283   N  VAL C 268           
SSBOND   1 CYS A   23    CYS A   88                          1555   1555  2.03  
SSBOND   2 CYS A  134    CYS A  194                          1555   1555  2.03  
SSBOND   3 CYS B   22    CYS B   96                          1555   1555  2.03  
SSBOND   4 CYS B  147    CYS B  202                          1555   1555  2.04  
CISPEP   1 SER A    7    PRO A    8          0        -0.17                     
CISPEP   2 PHE A   94    PRO A   95          0        -0.04                     
CISPEP   3 TYR A  140    PRO A  141          0        -0.10                     
CISPEP   4 TRP B  195    PRO B  196          0        -0.05                     
CRYST1  186.286   37.271   87.939  90.00  90.66  90.00 C 1 2 1       4          
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      0.005368  0.000000  0.000062        0.00000                         
SCALE2      0.000000  0.026831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011372        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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