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Database: PDB
Entry: 2OY1
LinkDB: 2OY1
Original site: 2OY1 
HEADER    MEMBRANE PROTEIN                        21-FEB-07   2OY1              
TITLE     THE CRYSTAL STRUCTURE OF OSPA MUTANT                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OUTER SURFACE PROTEIN A;                                   
COMPND   3 CHAIN: O;                                                            
COMPND   4 FRAGMENT: RESIDUES 27-273;                                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BORRELIA BURGDORFERI;                           
SOURCE   3 ORGANISM_COMMON: LYME DISEASE SPIROCHETE;                            
SOURCE   4 ORGANISM_TAXID: 139;                                                 
SOURCE   5 GENE: OSPA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 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 2OY1    1       VERSN                                    
REVDAT   1   11-DEC-07 2OY1    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.    1.86 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) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 20929                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1127                            
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) : 1.86                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1398                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 83                           
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.53000                                              
REMARK   3    B22 (A**2) : -1.30000                                             
REMARK   3    B33 (A**2) : -0.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.29000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.148         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.135         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.957         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1822 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1694 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2457 ; 1.971 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3995 ; 0.890 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   246 ;12.837 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    57 ;38.193 ;28.070       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   363 ;15.832 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     2 ;21.524 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   316 ; 0.126 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1985 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   284 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   247 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1587 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   895 ; 0.165 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1109 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    79 ; 0.157 ; 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):    12 ; 0.281 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    23 ; 0.287 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.242 ; 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):  1564 ; 2.384 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   516 ; 0.393 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1969 ; 2.276 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   676 ; 4.032 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   488 ; 5.798 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 2OY1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041725.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22098                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.850                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.610                              
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   (%): 51.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG3350, 0.1M IMIDAZOLE, PH 8,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       28.00250            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY O    23                                                      
REMARK 465     SER O    24                                                      
REMARK 465     HIS O    25                                                      
REMARK 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    SER O 217   CB    SER O 217   OG     -0.081                       
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    ASP O  93   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP O 233   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 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    ASN O  28     -101.37    115.83                                   
REMARK 500    SER O  29      114.65     38.66                                   
REMARK 500    SER O  37       -3.09     57.01                                   
REMARK 500    ASP O  59     -109.52     58.58                                   
REMARK 500    ALA O  83       -6.89     75.63                                   
REMARK 500    VAL O 110      -60.19   -105.71                                   
REMARK 500    SER O 116     -137.68   -134.94                                   
REMARK 500    SER O 119       70.93     88.18                                   
REMARK 500    SER O 228        2.26     59.70                                   
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 ASN O  117     GLY O  118                 -114.22                    
REMARK 500 SER O  119     SER O  120                  124.83                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OL6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OL7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OL8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OY5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OY7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OY8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2OYB   RELATED DB: PDB                                   
DBREF  2OY1 O   27   272  UNP    Q45040   Q45040_BORBU    27    273             
SEQADV 2OY1 GLY O   23  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OY1 SER O   24  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OY1 HIS O   25  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OY1 MET O   26  UNP  Q45040              EXPRESSION TAG                 
SEQADV 2OY1 SER O   37  UNP  Q45040    GLU    37 ENGINEERED                     
SEQADV 2OY1 SER O   45  UNP  Q45040    GLU    45 ENGINEERED                     
SEQADV 2OY1 SER O   46  UNP  Q45040    LYS    46 ENGINEERED                     
SEQADV 2OY1 ALA O   48  UNP  Q45040    LYS    48 ENGINEERED                     
SEQADV 2OY1 ALA O   60  UNP  Q45040    LYS    60 ENGINEERED                     
SEQADV 2OY1 SER O   64  UNP  Q45040    LYS    64 ENGINEERED                     
SEQADV 2OY1 ALA O   83  UNP  Q45040    LYS    83 ENGINEERED                     
SEQADV 2OY1 SER O  104  UNP  Q45040    GLU   104 ENGINEERED                     
SEQADV 2OY1 SER O  107  UNP  Q45040    LYS   107 ENGINEERED                     
SEQADV 2OY1 ASN O  117  UNP  Q45040    LYS   117 ENGINEERED                     
SEQADV 2OY1 GLY O  118  UNP  Q45040    ASP   118 ENGINEERED                     
SEQADV 2OY1     O       UNP  Q45040    LYS   119 DELETION                       
SEQADV 2OY1 ILE O  125  UNP  Q45040    PHE   126 ENGINEERED                     
SEQADV 2OY1 ILE O  126  UNP  Q45040    ASN   127 ENGINEERED                     
SEQADV 2OY1 ILE O  127  UNP  Q45040    GLU   128 ENGINEERED                     
SEQADV 2OY1 ASP O  128  UNP  Q45040    LYS   129 ENGINEERED                     
SEQADV 2OY1 ILE O  130  UNP  Q45040    GLU   131 ENGINEERED                     
SEQADV 2OY1 ILE O  131  UNP  Q45040    VAL   132 ENGINEERED                     
SEQADV 2OY1 ILE O  132  UNP  Q45040    SER   133 ENGINEERED                     
SEQADV 2OY1 SER O  238  UNP  Q45040    LYS   239 ENGINEERED                     
SEQADV 2OY1 SER O  239  UNP  Q45040    GLU   240 ENGINEERED                     
SEQADV 2OY1 SER O  253  UNP  Q45040    LYS   254 ENGINEERED                     
SEQRES   1 O  250  GLY SER HIS MET LYS ASN SER VAL SER VAL ASP LEU PRO          
SEQRES   2 O  250  GLY SER MET LYS VAL LEU VAL SER LYS SER SER ASN ALA          
SEQRES   3 O  250  ASP GLY LYS TYR ASP LEU ILE ALA THR VAL ASP ALA LEU          
SEQRES   4 O  250  GLU LEU SER GLY THR SER ASP LYS ASN ASN GLY SER GLY          
SEQRES   5 O  250  VAL LEU GLU GLY VAL LYS ALA ASP ALA SER LYS VAL LYS          
SEQRES   6 O  250  LEU THR ILE SER ASP ASP LEU GLY GLN THR THR LEU GLU          
SEQRES   7 O  250  VAL PHE LYS SER ASP GLY SER THR LEU VAL SER LYS LYS          
SEQRES   8 O  250  VAL THR SER ASN GLY SER SER THR GLU GLU LYS ILE ILE          
SEQRES   9 O  250  ILE ASP GLY ILE ILE ILE GLU LYS ILE ILE THR ARG ALA          
SEQRES  10 O  250  ASP GLY THR ARG LEU GLU TYR THR GLY ILE LYS SER ASP          
SEQRES  11 O  250  GLY SER GLY LYS ALA LYS GLU VAL LEU LYS GLY TYR VAL          
SEQRES  12 O  250  LEU GLU GLY THR LEU THR ALA GLU LYS THR THR LEU VAL          
SEQRES  13 O  250  VAL LYS GLU GLY THR VAL THR LEU SER LYS ASN ILE SER          
SEQRES  14 O  250  LYS SER GLY GLU VAL SER VAL GLU LEU ASN ASP THR ASP          
SEQRES  15 O  250  SER SER ALA ALA THR LYS LYS THR ALA ALA TRP ASN SER          
SEQRES  16 O  250  GLY THR SER THR LEU THR ILE THR VAL ASN SER LYS LYS          
SEQRES  17 O  250  THR LYS ASP LEU VAL PHE THR SER SER ASN THR ILE THR          
SEQRES  18 O  250  VAL GLN GLN TYR ASP SER ASN GLY THR SER LEU GLU GLY          
SEQRES  19 O  250  SER ALA VAL GLU ILE THR LYS LEU ASP GLU ILE LYS ASN          
SEQRES  20 O  250  ALA LEU LYS                                                  
FORMUL   2  HOH   *88(H2 O)                                                     
HELIX    1   1 LYS O  263  LEU O  271  1                                   9    
SHEET    1   A 4 VAL O  30  ASP O  33  0                                        
SHEET    2   A 4 LYS O  39  VAL O  42 -1  O  VAL O  40   N  VAL O  32           
SHEET    3   A 4 TYR O  52  VAL O  58 -1  O  ILE O  55   N  LEU O  41           
SHEET    4   A 4 LEU O  61  SER O  67 -1  O  LEU O  63   N  ALA O  56           
SHEET    1   B12 GLY O  74  VAL O  79  0                                        
SHEET    2   B12 LYS O  85  ILE O  90 -1  O  LEU O  88   N  LEU O  76           
SHEET    3   B12 THR O  97  PHE O 102 -1  O  PHE O 102   N  LYS O  85           
SHEET    4   B12 LEU O 109  THR O 115 -1  O  LYS O 113   N  LEU O  99           
SHEET    5   B12 THR O 121  ILE O 126 -1  O  LYS O 124   N  LYS O 112           
SHEET    6   B12 ILE O 131  THR O 137 -1  O  THR O 137   N  THR O 121           
SHEET    7   B12 ARG O 143  THR O 147 -1  O  TYR O 146   N  LYS O 134           
SHEET    8   B12 GLY O 155  VAL O 160 -1  O  LYS O 158   N  GLU O 145           
SHEET    9   B12 VAL O 165  LEU O 170 -1  O  LEU O 170   N  GLY O 155           
SHEET   10   B12 LYS O 174  GLU O 181 -1  O  THR O 176   N  THR O 169           
SHEET   11   B12 VAL O 184  SER O 191 -1  O  LYS O 188   N  LEU O 177           
SHEET   12   B12 VAL O 196  ASP O 202 -1  O  SER O 197   N  ASN O 189           
SHEET    1   C 5 LYS O 211  ASN O 216  0                                        
SHEET    2   C 5 THR O 221  VAL O 226 -1  O  THR O 223   N  ALA O 214           
SHEET    3   C 5 LYS O 229  PHE O 236 -1  O  THR O 231   N  ILE O 224           
SHEET    4   C 5 ILE O 242  GLN O 246 -1  O  GLN O 245   N  ASP O 233           
SHEET    5   C 5 VAL O 259  GLU O 260 -1  O  VAL O 259   N  VAL O 244           
CISPEP   1 ILE O  127    ASP O  128          0         1.86                     
CRYST1   36.046   56.005   66.204  90.00  97.09  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.027742  0.000000  0.003449        0.00000                         
SCALE2      0.000000  0.017856  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015221        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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