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Database: PDB
Entry: 1OSP
LinkDB: 1OSP
Original site: 1OSP 
HEADER    COMPLEX (IMMUNOGLOBULIN/LIPOPROTEIN)    23-NOV-96   1OSP              
TITLE     CRYSTAL STRUCTURE OF OUTER SURFACE PROTEIN A OF BORRELIA BURGDORFERI  
TITLE    2 COMPLEXED WITH A MURINE MONOCLONAL ANTIBODY FAB                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FAB 184.1;                                                 
COMPND   3 CHAIN: L;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: FAB 184.1;                                                 
COMPND   6 CHAIN: H;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: OUTER SURFACE PROTEIN A;                                   
COMPND   9 CHAIN: O;                                                            
COMPND  10 SYNONYM: OSPA;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   7 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   8 ORGANISM_TAXID: 10090;                                               
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;                           
SOURCE  11 ORGANISM_TAXID: 224326;                                              
SOURCE  12 STRAIN: B31;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PET9C                                     
KEYWDS    COMPLEX (IMMUNOGLOBULIN-LIPOPROTEIN), OUTER SURFACE PROTEIN A         
KEYWDS   2 COMPLEXED WITH FAB184.1, BORRELIA BURGDORFERI STRAIN B31, COMPLEX    
KEYWDS   3 (IMMUNOGLOBULIN-LIPOPROTEIN) COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LI,C.L.LAWSON                                                       
REVDAT   4   13-JUL-11 1OSP    1       VERSN                                    
REVDAT   3   24-FEB-09 1OSP    1       VERSN                                    
REVDAT   2   01-APR-03 1OSP    1       JRNL                                     
REVDAT   1   21-APR-97 1OSP    0                                                
JRNL        AUTH   H.LI,J.J.DUNN,B.J.LUFT,C.L.LAWSON                            
JRNL        TITL   CRYSTAL STRUCTURE OF LYME DISEASE ANTIGEN OUTER SURFACE      
JRNL        TITL 2 PROTEIN A COMPLEXED WITH AN FAB.                             
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  94  3584 1997              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   9108020                                                      
JRNL        DOI    10.1073/PNAS.94.8.3584                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 54404                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.295                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5209                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 328                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.61                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-95                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58870                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.04800                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.55000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.55000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.85000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, 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     ALA O    17                                                      
REMARK 465     LYS O    18                                                      
REMARK 465     GLN O    19                                                      
REMARK 465     ASN O    20                                                      
REMARK 465     VAL O    21                                                      
REMARK 465     SER O    22                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASN L  212                                                       
REMARK 475     GLU L  213                                                       
REMARK 475     CYS L  214                                                       
REMARK 475     GLY H  134                                                       
REMARK 475     CYS H  135                                                       
REMARK 475     GLY H  136                                                       
REMARK 475     ASP H  137                                                       
REMARK 475     THR H  138                                                       
REMARK 475     THR H  139                                                       
REMARK 475     GLY H  140                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HG1  THR H    90     H    VAL H   118              1.35            
REMARK 500   HZ3  LYS L   142     H2   HOH L   253              1.36            
REMARK 500  HH11  ARG O   139     HG1  THR O   143              1.45            
REMARK 500   HG1  THR L   182     H    GLU L   185              1.47            
REMARK 500   H    ASP H   100     HG   SER H   105              1.47            
REMARK 500   HZ1  LYS L   142     H1   HOH L   298              1.54            
REMARK 500   H    GLY L    50     HH   TYR L    91              1.54            
REMARK 500  HH21  ARG L    32     H2   HOH O   313              1.54            
REMARK 500   HZ1  LYS O    51     H2   HOH O   339              1.55            
REMARK 500   H    CYS H   135     H1   HOH H   300              1.56            
REMARK 500   HZ1  LYS O   117     H2   HOH O   307              1.57            
REMARK 500   HZ2  LYS O    69     H1   HOH O   289              1.57            
REMARK 500   HH   TYR H    59     H    ILE H    69              1.57            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   HZ3  LYS O   230     H1   HOH L   275     3446     0.65            
REMARK 500   HZ1  LYS O   254     H2   HOH L   258     3446     0.66            
REMARK 500  HH12  ARG L   188     H1   HOH L   281     4456     1.09            
REMARK 500  HH22  ARG L    61     H1   HOH H   306     4556     1.14            
REMARK 500   HZ1  LYS O   254     O    HOH L   258     3446     1.27            
REMARK 500  HH22  ARG L    61     H2   HOH H   306     4556     1.50            
REMARK 500   HZ3  LYS O   230     O    HOH L   275     3446     1.55            
REMARK 500   H    TRP L   163     OD1  ASN O   251     3456     1.57            
REMARK 500   NZ   LYS O   254     O    HOH L   258     3446     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG L 211   C     ASN L 212   N      -0.189                       
REMARK 500    ASN L 212   C     GLU L 213   N      -0.182                       
REMARK 500    PRO H 133   C     GLY H 134   N       0.252                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG L 211   O   -  C   -  N   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    LEU H   4   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    PRO H 133   CA  -  C   -  N   ANGL. DEV. = -27.2 DEGREES          
REMARK 500    PRO H 133   O   -  C   -  N   ANGL. DEV. =  26.7 DEGREES          
REMARK 500    GLY H 134   C   -  N   -  CA  ANGL. DEV. = -12.9 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 L  51      -31.20     70.59                                   
REMARK 500    SER L  67        2.19    -59.26                                   
REMARK 500    ASP L  70     -138.26   -126.76                                   
REMARK 500    LYS L 169      -62.99   -108.02                                   
REMARK 500    ASN L 190      -65.33   -107.25                                   
REMARK 500    THR L 200        9.37    -65.60                                   
REMARK 500    ASN L 212       68.68   -105.30                                   
REMARK 500    SER H  15      -17.51     82.33                                   
REMARK 500    GLU H  27      139.35   -173.80                                   
REMARK 500    ASN H  43       31.90     76.54                                   
REMARK 500    ARG H  52     -151.59   -137.47                                   
REMARK 500    CYS H 135     -178.75   -176.55                                   
REMARK 500    PHE H 153      -74.51   -108.14                                   
REMARK 500    SER H 156      103.05     89.54                                   
REMARK 500    SER H 193        2.46    -69.49                                   
REMARK 500    TRP H 195      -75.58    -87.27                                   
REMARK 500    LYS O  48       -7.30    -59.64                                   
REMARK 500    LYS O  83       -2.38     75.04                                   
REMARK 500    LYS O 107      -42.95   -133.12                                   
REMARK 500    LYS O 119       -4.87     76.99                                   
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 ANGLE, 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    ARG L 211        -16.20                                           
REMARK 500    ASN L 212         16.41                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE H 153        22.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1OSP H  121   218  UNP    P01867   GCBM_MOUSE       1     98             
DBREF  1OSP O   17   273  UNP    P14013   OSPA1_BORBU     16    273             
DBREF  1OSP L    1   214  PDB    1OSP     1OSP             1    214             
SEQADV 1OSP ALA O   17  UNP  P14013    CYS    17 CONFLICT                       
SEQADV 1OSP LYS O   39  UNP  P14013    ASN    39 VARIANT                        
SEQADV 1OSP CYS O   84  UNP  P14013    SER    84 ENGINEERED                     
SEQADV 1OSP GLY O  149  UNP  P14013    GLU   149 VARIANT                        
SEQADV 1OSP GLY O  164  UNP  P14013    SER   164 VARIANT                        
SEQRES   1 L  214  ASP ILE GLN MET SER GLN SER SER SER SER PHE SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP ARG VAL THR ILE THR CYS LYS ALA SER          
SEQRES   3 L  214  GLU ASP ILE TYR SER ARG LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY ASN ALA PRO ARG LEU LEU ILE SER GLY ALA THR          
SEQRES   5 L  214  SER LEU GLU THR TRP VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  ASP SER GLY LYS ASP TYR THR LEU SER ILE THR SER LEU          
SEQRES   7 L  214  GLN THR GLU ASP VAL ALA THR TYR PHE CYS GLN GLN TYR          
SEQRES   8 L  214  TRP SER PRO PRO PRO THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  218  GLU VAL GLN LEU GLN GLU SER GLY PRO SER LEU VAL LYS          
SEQRES   2 H  218  PRO SER GLN THR LEU SER LEU THR CYS SER VAL THR GLY          
SEQRES   3 H  218  GLU PRO ILE THR SER GLY PHE TRP ASP TRP ILE ARG LYS          
SEQRES   4 H  218  PHE PRO GLY ASN LYS LEU GLU PHE MET GLY TYR ILE ARG          
SEQRES   5 H  218  TYR GLY GLY GLY THR TYR TYR ASN PRO SER LEU LYS SER          
SEQRES   6 H  218  PRO ILE SER ILE THR ARG ASP THR SER LYS ASN HIS TYR          
SEQRES   7 H  218  TYR LEU GLN LEU ASN SER VAL VAL THR GLU ASP THR ALA          
SEQRES   8 H  218  THR TYR TYR CYS ALA ARG SER ARG ASP TYR TYR GLY SER          
SEQRES   9 H  218  SER GLY PHE ALA PHE TRP GLY GLU GLY THR LEU VAL THR          
SEQRES  10 H  218  VAL SER ALA ALA LYS THR THR PRO PRO SER VAL TYR PRO          
SEQRES  11 H  218  LEU ALA PRO GLY CYS GLY ASP THR THR GLY SER SER VAL          
SEQRES  12 H  218  THR LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU SER          
SEQRES  13 H  218  VAL THR VAL THR TRP ASN SER GLY SER LEU SER SER SER          
SEQRES  14 H  218  VAL HIS THR PHE PRO ALA LEU LEU GLN SER GLY LEU TYR          
SEQRES  15 H  218  THR MET SER SER SER VAL THR VAL PRO SER SER THR TRP          
SEQRES  16 H  218  PRO SER GLN THR VAL THR CYS SER VAL ALA HIS PRO ALA          
SEQRES  17 H  218  SER SER THR THR VAL ASP LYS LYS LEU GLU                      
SEQRES   1 O  257  ALA LYS GLN ASN VAL SER SER LEU ASP GLU LYS ASN SER          
SEQRES   2 O  257  VAL SER VAL ASP LEU PRO GLY GLU MET LYS VAL LEU VAL          
SEQRES   3 O  257  SER LYS GLU LYS ASN LYS ASP GLY LYS TYR ASP LEU ILE          
SEQRES   4 O  257  ALA THR VAL ASP LYS LEU GLU LEU LYS GLY THR SER ASP          
SEQRES   5 O  257  LYS ASN ASN GLY SER GLY VAL LEU GLU GLY VAL LYS ALA          
SEQRES   6 O  257  ASP LYS CYS LYS VAL LYS LEU THR ILE SER ASP ASP LEU          
SEQRES   7 O  257  GLY GLN THR THR LEU GLU VAL PHE LYS GLU ASP GLY LYS          
SEQRES   8 O  257  THR LEU VAL SER LYS LYS VAL THR SER LYS ASP LYS SER          
SEQRES   9 O  257  SER THR GLU GLU LYS PHE ASN GLU LYS GLY GLU VAL SER          
SEQRES  10 O  257  GLU LYS ILE ILE THR ARG ALA ASP GLY THR ARG LEU GLU          
SEQRES  11 O  257  TYR THR GLY ILE LYS SER ASP GLY SER GLY LYS ALA LYS          
SEQRES  12 O  257  GLU VAL LEU LYS GLY TYR VAL LEU GLU GLY THR LEU THR          
SEQRES  13 O  257  ALA GLU LYS THR THR LEU VAL VAL LYS GLU GLY THR VAL          
SEQRES  14 O  257  THR LEU SER LYS ASN ILE SER LYS SER GLY GLU VAL SER          
SEQRES  15 O  257  VAL GLU LEU ASN ASP THR ASP SER SER ALA ALA THR LYS          
SEQRES  16 O  257  LYS THR ALA ALA TRP ASN SER GLY THR SER THR LEU THR          
SEQRES  17 O  257  ILE THR VAL ASN SER LYS LYS THR LYS ASP LEU VAL PHE          
SEQRES  18 O  257  THR LYS GLU ASN THR ILE THR VAL GLN GLN TYR ASP SER          
SEQRES  19 O  257  ASN GLY THR LYS LEU GLU GLY SER ALA VAL GLU ILE THR          
SEQRES  20 O  257  LYS LEU ASP GLU ILE LYS ASN ALA LEU LYS                      
FORMUL   4  HOH   *328(H2 O)                                                    
HELIX    1   1 THR L   80  ASP L   82  5                                   3    
HELIX    2   2 SER L  122  THR L  126  1                                   5    
HELIX    3   3 LYS L  183  ARG L  188  1                                   6    
HELIX    4   4 TYR H   53  GLY H   55  5                                   3    
HELIX    5   5 THR H   87  ASP H   89  5                                   3    
HELIX    6   6 SER H  192  THR H  194  5                                   3    
HELIX    7   7 PRO H  207  SER H  209  5                                   3    
HELIX    8   8 GLU O   26  ASN O   28  5                                   3    
HELIX    9   9 PRO O   35  GLU O   37  5                                   3    
HELIX   10  10 SER O  218  THR O  220  5                                   3    
HELIX   11  11 LEU O  265  ALA O  271  1                                   7    
SHEET    1   A 2 SER L  10  VAL L  13  0                                        
SHEET    2   A 2 LYS L 103  ILE L 106  1  N  LYS L 103   O  PHE L  11           
SHEET    1   B 3 VAL L  19  CYS L  23  0                                        
SHEET    2   B 3 TYR L  71  ILE L  75 -1  N  ILE L  75   O  VAL L  19           
SHEET    3   B 3 PHE L  62  SER L  65 -1  N  SER L  65   O  THR L  72           
SHEET    1   C 3 THR L  85  GLN L  90  0                                        
SHEET    2   C 3 LEU L  33  GLN L  38 -1  N  GLN L  38   O  THR L  85           
SHEET    3   C 3 ARG L  45  ILE L  48 -1  N  ILE L  48   O  TRP L  35           
SHEET    1   D 4 THR L 114  PHE L 118  0                                        
SHEET    2   D 4 GLY L 129  ASN L 137 -1  N  ASN L 137   O  THR L 114           
SHEET    3   D 4 MET L 175  THR L 182 -1  N  LEU L 181   O  ALA L 130           
SHEET    4   D 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   E 4 SER L 153  ARG L 155  0                                        
SHEET    2   E 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3   E 4 SER L 191  THR L 197 -1  N  THR L 197   O  ASN L 145           
SHEET    4   E 4 ILE L 205  ASN L 210 -1  N  PHE L 209   O  TYR L 192           
SHEET    1   F 4 GLN H   3  SER H   7  0                                        
SHEET    2   F 4 LEU H  18  THR H  25 -1  N  THR H  25   O  GLN H   3           
SHEET    3   F 4 HIS H  77  LEU H  82 -1  N  LEU H  82   O  LEU H  18           
SHEET    4   F 4 ILE H  67  ASP H  72 -1  N  ASP H  72   O  HIS H  77           
SHEET    1   G 5 THR H 114  VAL H 116  0                                        
SHEET    2   G 5 ALA H  91  ARG H  97 -1  N  TYR H  93   O  THR H 114           
SHEET    3   G 5 TRP H  34  PHE H  40 -1  N  LYS H  39   O  THR H  92           
SHEET    4   G 5 LYS H  44  ILE H  51 -1  N  ILE H  51   O  TRP H  34           
SHEET    5   G 5 THR H  57  TYR H  59 -1  N  TYR H  58   O  TYR H  50           
SHEET    1   H 4 SER H 127  LEU H 131  0                                        
SHEET    2   H 4 SER H 142  TYR H 152 -1  N  LYS H 150   O  SER H 127           
SHEET    3   H 4 TYR H 182  PRO H 191 -1  N  VAL H 190   O  VAL H 143           
SHEET    4   H 4 SER H 169  PHE H 173 -1  N  PHE H 173   O  SER H 185           
SHEET    1   I 3 THR H 158  ASN H 162  0                                        
SHEET    2   I 3 THR H 201  HIS H 206 -1  N  ALA H 205   O  THR H 158           
SHEET    3   I 3 THR H 211  LYS H 216 -1  N  LYS H 215   O  CYS H 202           
SHEET    1   J 2 LEU H 176  GLN H 178  0                                        
SHEET    2   J 2 LEU H 181  THR H 183 -1  N  THR H 183   O  LEU H 176           
SHEET    1   K 2 SER O  29  ASP O  33  0                                        
SHEET    2   K 2 LYS O  39  SER O  43 -1  N  VAL O  42   O  VAL O  30           
SHEET    1   L 2 TYR O  52  VAL O  58  0                                        
SHEET    2   L 2 LEU O  61  SER O  67 -1  N  SER O  67   O  TYR O  52           
SHEET    1   M12 GLY O  74  VAL O  79  0                                        
SHEET    2   M12 LYS O  85  ILE O  90 -1  N  ILE O  90   O  GLY O  74           
SHEET    3   M12 GLN O  96  PHE O 102 -1  N  PHE O 102   O  LYS O  85           
SHEET    4   M12 LEU O 109  SER O 116 -1  N  THR O 115   O  THR O  97           
SHEET    5   M12 SER O 121  PHE O 126 -1  N  GLU O 124   O  LYS O 112           
SHEET    6   M12 VAL O 132  THR O 138 -1  N  THR O 138   O  SER O 121           
SHEET    7   M12 ARG O 144  THR O 148 -1  N  TYR O 147   O  LYS O 135           
SHEET    8   M12 GLY O 156  VAL O 161 -1  N  VAL O 161   O  ARG O 144           
SHEET    9   M12 VAL O 166  LEU O 171 -1  N  LEU O 171   O  GLY O 156           
SHEET   10   M12 LYS O 175  GLU O 182 -1  N  VAL O 179   O  GLU O 168           
SHEET   11   M12 VAL O 185  SER O 192 -1  N  ILE O 191   O  THR O 176           
SHEET   12   M12 VAL O 197  ASP O 203 -1  N  ASN O 202   O  THR O 186           
SHEET    1   N 4 LYS O 212  ASN O 217  0                                        
SHEET    2   N 4 THR O 222  VAL O 227 -1  N  THR O 226   O  THR O 213           
SHEET    3   N 4 LYS O 230  PHE O 237 -1  N  LEU O 235   O  LEU O 223           
SHEET    4   N 4 ILE O 243  GLN O 247 -1  N  GLN O 246   O  ASP O 234           
SHEET    1   O 2 ALA H  96  SER H  98  0                                        
SHEET    2   O 2 PHE H 107  TRP H 110 -1  N  PHE H 109   O  ARG H  97           
SSBOND   1 CYS L   23    CYS L   88                          1555   1555  2.55  
SSBOND   2 CYS L  134    CYS L  194                          1555   1555  2.41  
SSBOND   3 CYS H   22    CYS H   95                          1555   1555  2.54  
SSBOND   4 CYS H  147    CYS H  202                          1555   1555  2.42  
CISPEP   1 PRO L   94    PRO L   95          0        -0.44                     
CISPEP   2 TYR L  140    PRO L  141          0        -0.49                     
CRYST1   89.100   91.700  100.400  90.00  90.00  90.00 P 21 21 21    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      0.011223  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010905  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009960        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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