GenomeNet

Database: PDB
Entry: 2B4M
LinkDB: 2B4M
Original site: 2B4M 
HEADER    TRANSPORT PROTEIN                       26-SEP-05   2B4M              
TITLE     CRYSTAL STRUCTURE OF THE BINDING PROTEIN OPUAC IN COMPLEX WITH PROLINE
TITLE    2 BETAINE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCINE BETAINE-BINDING PROTEIN;                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: OPUAC;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PBKB76                                     
KEYWDS    SUBSTRATE-BINDING PROTEIN, CLOSED LIGANDED, ABC-TRANSPORTER,          
KEYWDS   2 COMPATIBLE SOLUTES, TRANSPORT PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.HORN,L.SOHN-BOESSER,J.BREED,W.WELTE,L.SCHMITT,E.BREMER              
REVDAT   3   13-JUL-11 2B4M    1       VERSN                                    
REVDAT   2   24-FEB-09 2B4M    1       VERSN                                    
REVDAT   1   21-MAR-06 2B4M    0                                                
JRNL        AUTH   C.HORN,L.SOHN-BOESSER,J.BREED,W.WELTE,L.SCHMITT,E.BREMER     
JRNL        TITL   MOLECULAR DETERMINANTS FOR SUBSTRATE SPECIFICITY OF THE      
JRNL        TITL 2 LIGAND-BINDING PROTEIN OPUAC FROM BACILLUS SUBTILIS FOR THE  
JRNL        TITL 3 COMPATIBLE SOLUTES GLYCINE BETAINE AND PROLINE BETAINE.      
JRNL        REF    J.MOL.BIOL.                   V. 357   592 2006              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   16445940                                                     
JRNL        DOI    10.1016/J.JMB.2005.12.085                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0000                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 10300                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 546                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 671                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 25                           
REMARK   3   BIN FREE R VALUE                    : 0.4100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4122                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -1.16000                                             
REMARK   3    B33 (A**2) : 2.16000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 5.49000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.544         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.405         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 47.945        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.909                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.865                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4212 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5702 ; 1.133 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   526 ; 5.759 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   162 ;39.522 ;25.926       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   770 ;19.143 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ; 9.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   634 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3072 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1807 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   136 ; 0.140 ; 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):    45 ; 0.240 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.185 ; 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):  2704 ; 0.226 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4242 ; 0.378 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1771 ; 0.549 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1460 ; 0.919 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      9       A     272      1                      
REMARK   3           1     B      9       B     272      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2053 ;  0.02 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2053 ;  0.04 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     9        A   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9030   0.0370   7.1210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2829 T22:   0.1465                                     
REMARK   3      T33:   0.1333 T12:   0.0282                                     
REMARK   3      T13:  -0.1086 T23:  -0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6778 L22:   1.1662                                     
REMARK   3      L33:   0.9594 L12:   0.6295                                     
REMARK   3      L13:   0.7075 L23:   0.2023                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.1177 S13:  -0.0278                       
REMARK   3      S21:  -0.0270 S22:   0.0321 S23:  -0.0972                       
REMARK   3      S31:  -0.0155 S32:   0.0710 S33:  -0.0453                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     9        B   272                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.7690   7.4510  46.7190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1903 T22:   0.3373                                     
REMARK   3      T33:   0.1750 T12:  -0.0293                                     
REMARK   3      T13:  -0.0970 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4809 L22:   1.5881                                     
REMARK   3      L33:   2.2104 L12:  -0.3098                                     
REMARK   3      L13:   1.1193 L23:  -0.3955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0960 S12:  -0.2940 S13:   0.0279                       
REMARK   3      S21:   0.0598 S22:  -0.0501 S23:  -0.1686                       
REMARK   3      S31:   0.0410 S32:   0.1448 S33:  -0.0459                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 2B4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB034668.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.25                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10846                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.31200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
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: 2B4L                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, AMMONIUM ACETATE, PEG 4000, PH     
REMARK 280  8.25, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 274K               
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       14.15900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ALA B     8                                                      
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   NH2  ARG B   104     OE1  GLU B   110              1.78            
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   CD   LYS A   140     OE2  GLU A   158     1565     1.89            
REMARK 500   NH1  ARG B    63     OE2  GLU B   137     2556     2.05            
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 A  39   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 243   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A 269   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B  39   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B 179   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B 243   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP B 269   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 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    ILE A  21     -147.25   -108.63                                   
REMARK 500    ALA A  48     -116.15   -148.06                                   
REMARK 500    PRO A  74       80.01    -52.73                                   
REMARK 500    ASP A  88       75.32   -115.13                                   
REMARK 500    ALA A  96       42.51     36.20                                   
REMARK 500    ALA A 177       41.49    -79.79                                   
REMARK 500    ILE B  21     -146.69   -108.79                                   
REMARK 500    ALA B  48     -114.85   -150.88                                   
REMARK 500    PRO B  74       78.29    -55.16                                   
REMARK 500    ASP B  88       77.36   -116.19                                   
REMARK 500    ALA B  96       40.11     38.68                                   
REMARK 500    ALA B 177       40.74    -78.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBE B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PBE A 311                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2B4L   RELATED DB: PDB                                   
DBREF  2B4M A    5   272  UNP    P46922   OPUAC_BACSU     26    293             
DBREF  2B4M B    5   272  UNP    P46922   OPUAC_BACSU     26    293             
SEQRES   1 A  268  ASP GLU ASN ALA SER ALA ALA GLU GLN VAL ASN LYS THR          
SEQRES   2 A  268  ILE ILE GLY ILE ASP PRO GLY SER GLY ILE MET SER LEU          
SEQRES   3 A  268  THR ASP LYS ALA MET LYS ASP TYR ASP LEU ASN ASP TRP          
SEQRES   4 A  268  THR LEU ILE SER ALA SER SER ALA ALA MET THR ALA THR          
SEQRES   5 A  268  LEU LYS LYS SER TYR ASP ARG LYS LYS PRO ILE ILE ILE          
SEQRES   6 A  268  THR GLY TRP THR PRO HIS TRP MET PHE SER ARG TYR LYS          
SEQRES   7 A  268  LEU LYS TYR LEU ASP ASP PRO LYS GLN SER TYR GLY SER          
SEQRES   8 A  268  ALA GLU GLU ILE HIS THR ILE THR ARG LYS GLY PHE SER          
SEQRES   9 A  268  LYS GLU GLN PRO ASN ALA ALA LYS LEU LEU SER GLN PHE          
SEQRES  10 A  268  LYS TRP THR GLN ASP GLU MET GLY GLU ILE MET ILE LYS          
SEQRES  11 A  268  VAL GLU GLU GLY GLU LYS PRO ALA LYS VAL ALA ALA GLU          
SEQRES  12 A  268  TYR VAL ASN LYS HIS LYS ASP GLN ILE ALA GLU TRP THR          
SEQRES  13 A  268  LYS GLY VAL GLN LYS VAL LYS GLY ASP LYS ILE ASN LEU          
SEQRES  14 A  268  ALA TYR VAL ALA TRP ASP SER GLU ILE ALA SER THR ASN          
SEQRES  15 A  268  VAL ILE GLY LYS VAL LEU GLU ASP LEU GLY TYR GLU VAL          
SEQRES  16 A  268  THR LEU THR GLN VAL GLU ALA GLY PRO MET TRP THR ALA          
SEQRES  17 A  268  ILE ALA THR GLY SER ALA ASP ALA SER LEU SER ALA TRP          
SEQRES  18 A  268  LEU PRO ASN THR HIS LYS ALA TYR ALA ALA LYS TYR LYS          
SEQRES  19 A  268  GLY LYS TYR ASP ASP ILE GLY THR SER MET THR GLY VAL          
SEQRES  20 A  268  LYS MET GLY LEU VAL VAL PRO GLN TYR MET LYS ASN VAL          
SEQRES  21 A  268  ASN SER ILE GLU ASP LEU LYS LYS                              
SEQRES   1 B  268  ASP GLU ASN ALA SER ALA ALA GLU GLN VAL ASN LYS THR          
SEQRES   2 B  268  ILE ILE GLY ILE ASP PRO GLY SER GLY ILE MET SER LEU          
SEQRES   3 B  268  THR ASP LYS ALA MET LYS ASP TYR ASP LEU ASN ASP TRP          
SEQRES   4 B  268  THR LEU ILE SER ALA SER SER ALA ALA MET THR ALA THR          
SEQRES   5 B  268  LEU LYS LYS SER TYR ASP ARG LYS LYS PRO ILE ILE ILE          
SEQRES   6 B  268  THR GLY TRP THR PRO HIS TRP MET PHE SER ARG TYR LYS          
SEQRES   7 B  268  LEU LYS TYR LEU ASP ASP PRO LYS GLN SER TYR GLY SER          
SEQRES   8 B  268  ALA GLU GLU ILE HIS THR ILE THR ARG LYS GLY PHE SER          
SEQRES   9 B  268  LYS GLU GLN PRO ASN ALA ALA LYS LEU LEU SER GLN PHE          
SEQRES  10 B  268  LYS TRP THR GLN ASP GLU MET GLY GLU ILE MET ILE LYS          
SEQRES  11 B  268  VAL GLU GLU GLY GLU LYS PRO ALA LYS VAL ALA ALA GLU          
SEQRES  12 B  268  TYR VAL ASN LYS HIS LYS ASP GLN ILE ALA GLU TRP THR          
SEQRES  13 B  268  LYS GLY VAL GLN LYS VAL LYS GLY ASP LYS ILE ASN LEU          
SEQRES  14 B  268  ALA TYR VAL ALA TRP ASP SER GLU ILE ALA SER THR ASN          
SEQRES  15 B  268  VAL ILE GLY LYS VAL LEU GLU ASP LEU GLY TYR GLU VAL          
SEQRES  16 B  268  THR LEU THR GLN VAL GLU ALA GLY PRO MET TRP THR ALA          
SEQRES  17 B  268  ILE ALA THR GLY SER ALA ASP ALA SER LEU SER ALA TRP          
SEQRES  18 B  268  LEU PRO ASN THR HIS LYS ALA TYR ALA ALA LYS TYR LYS          
SEQRES  19 B  268  GLY LYS TYR ASP ASP ILE GLY THR SER MET THR GLY VAL          
SEQRES  20 B  268  LYS MET GLY LEU VAL VAL PRO GLN TYR MET LYS ASN VAL          
SEQRES  21 B  268  ASN SER ILE GLU ASP LEU LYS LYS                              
HET    PBE  B 310      10                                                       
HET    PBE  A 311      10                                                       
HETNAM     PBE 1,1-DIMETHYL-PROLINIUM                                           
HETSYN     PBE PROLINE BETAINE                                                  
FORMUL   3  PBE    2(C7 H14 N O2 1+)                                            
HELIX    1   1 SER A    9  ASN A   15  1                                   7    
HELIX    2   2 SER A   25  TYR A   38  1                                  14    
HELIX    3   3 SER A   49  LYS A   64  1                                  16    
HELIX    4   4 TRP A   76  TYR A   81  1                                   6    
HELIX    5   5 GLY A  106  GLN A  111  1                                   6    
HELIX    6   6 GLN A  111  PHE A  121  1                                  11    
HELIX    7   7 THR A  124  GLU A  137  1                                  14    
HELIX    8   8 LYS A  140  ASN A  150  1                                  11    
HELIX    9   9 HIS A  152  THR A  160  1                                   9    
HELIX   10  10 TRP A  178  LEU A  195  1                                  18    
HELIX   11  11 GLY A  207  THR A  215  1                                   9    
HELIX   12  12 HIS A  230  TYR A  237  1                                   8    
HELIX   13  13 SER A  266  LYS A  271  5                                   6    
HELIX   14  14 SER B    9  ASN B   15  1                                   7    
HELIX   15  15 SER B   25  TYR B   38  1                                  14    
HELIX   16  16 SER B   49  ARG B   63  1                                  15    
HELIX   17  17 TRP B   76  TYR B   81  1                                   6    
HELIX   18  18 GLY B  106  GLN B  111  1                                   6    
HELIX   19  19 GLN B  111  PHE B  121  1                                  11    
HELIX   20  20 THR B  124  GLU B  137  1                                  14    
HELIX   21  21 LYS B  140  ASN B  150  1                                  11    
HELIX   22  22 HIS B  152  THR B  160  1                                   9    
HELIX   23  23 TRP B  178  LEU B  195  1                                  18    
HELIX   24  24 GLY B  207  THR B  215  1                                   9    
HELIX   25  25 HIS B  230  TYR B  237  1                                   8    
HELIX   26  26 SER B  266  LYS B  271  5                                   6    
SHEET    1   A 2 THR A  17  ILE A  19  0                                        
SHEET    2   A 2 THR A  44  ILE A  46  1  O  ILE A  46   N  ILE A  18           
SHEET    1   B 3 ILE A  69  TRP A  72  0                                        
SHEET    2   B 3 MET A 253  PRO A 258 -1  O  GLY A 254   N  GLY A  71           
SHEET    3   B 3 LEU A  83  TYR A  85 -1  N  LYS A  84   O  VAL A 257           
SHEET    1   C 5 GLU A 198  VAL A 204  0                                        
SHEET    2   C 5 LYS A 170  VAL A 176  1  N  LEU A 173   O  THR A 200           
SHEET    3   C 5 ALA A 220  LEU A 226  1  O  ALA A 220   N  ALA A 174           
SHEET    4   C 5 GLU A  97  ARG A 104 -1  N  HIS A 100   O  ALA A 224           
SHEET    5   C 5 TYR A 241  VAL A 251 -1  O  GLY A 245   N  THR A 101           
SHEET    1   D 2 THR B  17  ILE B  19  0                                        
SHEET    2   D 2 THR B  44  ILE B  46  1  O  THR B  44   N  ILE B  18           
SHEET    1   E 3 ILE B  69  TRP B  72  0                                        
SHEET    2   E 3 MET B 253  PRO B 258 -1  O  VAL B 256   N  ILE B  69           
SHEET    3   E 3 LEU B  83  TYR B  85 -1  N  LYS B  84   O  VAL B 257           
SHEET    1   F 5 GLU B 198  GLN B 203  0                                        
SHEET    2   F 5 LYS B 170  TYR B 175  1  N  LEU B 173   O  THR B 200           
SHEET    3   F 5 ALA B 220  LEU B 226  1  O  ALA B 220   N  ALA B 174           
SHEET    4   F 5 GLU B  97  ARG B 104 -1  N  HIS B 100   O  ALA B 224           
SHEET    5   F 5 TYR B 241  VAL B 251 -1  O  GLY B 245   N  THR B 101           
CISPEP   1 LEU A  226    PRO A  227          0         1.80                     
CISPEP   2 LEU B  226    PRO B  227          0         0.37                     
SITE     1 AC1  8 ILE B  21  SER B  25  GLY B  26  ILE B  27                    
SITE     2 AC1  8 TRP B  72  TRP B 178  TRP B 225  THR B 229                    
SITE     1 AC2  7 SER A  25  GLY A  26  ILE A  27  TRP A  72                    
SITE     2 AC2  7 TRP A 178  TRP A 225  THR A 229                               
CRYST1   88.562   28.318  102.826  90.00  93.87  90.00 P 1 21 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      0.011292  0.000000  0.000764        0.00000                         
SCALE2      0.000000  0.035313  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009747        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system