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Database: PDB
Entry: 3MIX
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Original site: 3MIX 
HEADER    PROTEIN TRANSPORT                       12-APR-10   3MIX              
TITLE     CRYSTAL STRUCTURE OF THE CYTOSOLIC DOMAIN OF B. SUBTILIS FLHA         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLAGELLAR BIOSYNTHESIS PROTEIN FLHA;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CYTOSOLIC DOMAIN (UNP RESIDUES 303-677);                   
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: BSU16390, FLHA;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
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: PET24D                                    
KEYWDS    FLAGELLA BIOSYNTHESIS, PROTEIN TRANSPORT, TYPE III SECRETION          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BANGE,N.KUEMMERER,G.BOZKURT,K.WILD,I.SINNING                        
REVDAT   2   07-JUL-10 3MIX    1       JRNL                                     
REVDAT   1   23-JUN-10 3MIX    0                                                
JRNL        AUTH   G.BANGE,N.KUMMERER,C.ENGEL,G.BOZKURT,K.WILD,I.SINNING        
JRNL        TITL   FLHA PROVIDES THE ADAPTOR FOR COORDINATED DELIVERY OF LATE   
JRNL        TITL 2 FLAGELLA BUILDING BLOCKS TO THE TYPE III SECRETION SYSTEM.   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107 11295 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20534509                                                     
JRNL        DOI    10.1073/PNAS.1001383107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19891                          
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) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1056                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1350                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2340                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 75                           
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2468                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 120                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : -0.06000                                             
REMARK   3    B33 (A**2) : 0.10000                                              
REMARK   3    B12 (A**2) : -0.03000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.265         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.228         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.524        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.914                         
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):  2500 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3391 ; 1.288 ; 2.001       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   310 ; 5.555 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   111 ;39.029 ;25.586       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   471 ;18.475 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    14 ;23.145 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   414 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1821 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  1563 ; 0.644 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2547 ; 1.235 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   937 ; 1.900 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   844 ; 3.285 ; 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  : 1                                          
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   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.7860  27.1900   7.3050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0975 T22:   0.0778                                     
REMARK   3      T33:   0.1437 T12:   0.0007                                     
REMARK   3      T13:  -0.0584 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1734 L22:   1.9758                                     
REMARK   3      L33:   2.6015 L12:  -0.1528                                     
REMARK   3      L13:   1.0131 L23:   0.4470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0832 S12:   0.1710 S13:   0.3329                       
REMARK   3      S21:  -0.1245 S22:  -0.1249 S23:  -0.2794                       
REMARK   3      S31:  -0.2863 S32:   0.2842 S33:   0.2080                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3MIX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058601.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-09; 15-MAR-09               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ESRF; ESRF                         
REMARK 200  BEAMLINE                       : ID14-4; ID14-2                     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9330; 0.9330                     
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R; ADSC QUANTUM 4  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20948                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : 0.07500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 6.5, 25 % W/V         
REMARK 280  PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.77333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.38667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       59.08000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       19.69333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       98.46667            
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 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 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     MET A   296                                                      
REMARK 465     GLY A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 465     HIS A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     ALA A   303                                                      
REMARK 465     TYR A   304                                                      
REMARK 465     THR A   305                                                      
REMARK 465     LEU A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     LYS A   308                                                      
REMARK 465     SER A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     LYS A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     LYS A   313                                                      
REMARK 465     GLU A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     VAL A   316                                                      
REMARK 465     ASP A   317                                                      
REMARK 465     MET A   421                                                      
REMARK 465     SER A   422                                                      
REMARK 465     PRO A   423                                                      
REMARK 465     THR A   424                                                      
REMARK 465     PRO A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     ASP A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     ILE A   430                                                      
REMARK 465     GLU A   431                                                      
REMARK 465     GLY A   432                                                      
REMARK 465     ILE A   433                                                      
REMARK 465     GLU A   434                                                      
REMARK 465     THR A   435                                                      
REMARK 465     VAL A   436                                                      
REMARK 465     GLU A   437                                                      
REMARK 465     PRO A   438                                                      
REMARK 465     SER A   439                                                      
REMARK 465     PHE A   440                                                      
REMARK 465     GLY A   441                                                      
REMARK 465     LEU A   442                                                      
REMARK 465     PRO A   443                                                      
REMARK 465     ALA A   444                                                      
REMARK 465     LYS A   445                                                      
REMARK 465     TRP A   446                                                      
REMARK 465     ILE A   447                                                      
REMARK 465     SER A   448                                                      
REMARK 465     GLU A   449                                                      
REMARK 465     ALA A   450                                                      
REMARK 465     VAL A   451                                                      
REMARK 465     LYS A   452                                                      
REMARK 465     ASP A   453                                                      
REMARK 465     GLU A   454                                                      
REMARK 465     ALA A   455                                                      
REMARK 465     ASP A   456                                                      
REMARK 465     MET A   457                                                      
REMARK 465     LEU A   458                                                      
REMARK 465     GLY A   459                                                      
REMARK 465     TYR A   460                                                      
REMARK 465     GLN A   597                                                      
REMARK 465     THR A   598                                                      
REMARK 465     GLU A   599                                                      
REMARK 465     HIS A   600                                                      
REMARK 465     GLY A   601                                                      
REMARK 465     ASN A   602                                                      
REMARK 465     ILE A   677                                                      
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   O    HOH A   115     O    ILE A   341     6554     2.07            
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 A 641   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 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    LEU A 329       98.86    -51.77                                   
REMARK 500    LYS A 330      -41.83   -134.79                                   
REMARK 500    GLN A 360       44.69   -107.42                                   
REMARK 500    ASN A 575       11.76     54.58                                   
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    THR A 474        24.6      L          L   OUTSIDE RANGE           
REMARK 500    THR A 556        21.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3MIX A  303   677  UNP    P35620   FLHA_BACSU     303    677             
SEQADV 3MIX MET A  296  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX GLY A  297  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX HIS A  298  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX HIS A  299  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX HIS A  300  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX HIS A  301  UNP  P35620              EXPRESSION TAG                 
SEQADV 3MIX HIS A  302  UNP  P35620              EXPRESSION TAG                 
SEQRES   1 A  382  MET GLY HIS HIS HIS HIS HIS ALA TYR THR LEU SER LYS          
SEQRES   2 A  382  SER GLY LYS GLU LYS GLU GLU VAL ASP GLU ILE LEU GLU          
SEQRES   3 A  382  GLU GLU ALA GLU VAL ASP GLU LEU LYS SER PRO GLU SER          
SEQRES   4 A  382  VAL VAL GLN LEU LEU HIS ILE ASP PRO ILE GLU PHE GLU          
SEQRES   5 A  382  PHE GLY TYR GLY LEU ILE PRO LEU ALA ASP ALA ASN GLN          
SEQRES   6 A  382  GLY GLY ASP LEU LEU ASP ARG ILE VAL MET ILE ARG ARG          
SEQRES   7 A  382  GLN LEU ALA LEU GLU LEU GLY LEU VAL ILE PRO VAL VAL          
SEQRES   8 A  382  ARG ILE ARG ASP ASN ILE ALA LEU GLN PRO ASN GLU TYR          
SEQRES   9 A  382  ARG LEU LYS ILE LYS GLY ASN GLU VAL ALA LYS GLY GLU          
SEQRES  10 A  382  LEU LEU LEU ASP HIS TYR LEU ALA MET SER PRO THR PRO          
SEQRES  11 A  382  GLU ASP ASP LEU ILE GLU GLY ILE GLU THR VAL GLU PRO          
SEQRES  12 A  382  SER PHE GLY LEU PRO ALA LYS TRP ILE SER GLU ALA VAL          
SEQRES  13 A  382  LYS ASP GLU ALA ASP MET LEU GLY TYR THR VAL VAL ASP          
SEQRES  14 A  382  PRO ALA SER VAL VAL SER THR HIS ILE THR GLU LYS ILE          
SEQRES  15 A  382  LYS GLN HIS ALA HIS GLU LEU ILE GLY ARG GLN GLU THR          
SEQRES  16 A  382  LYS GLN LEU ILE ASP HIS LEU LYS GLU SER TYR PRO VAL          
SEQRES  17 A  382  LEU VAL GLU GLU VAL THR PRO ASN PRO LEU SER VAL GLY          
SEQRES  18 A  382  ASP ILE GLN LYS VAL LEU ALA LYS LEU LEU LYS GLU LYS          
SEQRES  19 A  382  VAL SER ILE ARG ASN LEU VAL THR ILE PHE GLU THR LEU          
SEQRES  20 A  382  ALA ASP TYR GLY LYS LEU THR THR ASP SER ASP LEU LEU          
SEQRES  21 A  382  THR GLU TYR THR ARG GLN ALA LEU ALA LYS GLN ILE THR          
SEQRES  22 A  382  ALA GLN PHE ALA LYS GLU ASN GLU VAL LEU LYS VAL VAL          
SEQRES  23 A  382  THR CYS SER GLY ARG VAL GLU LYS ALA ILE ALA ASP GLY          
SEQRES  24 A  382  VAL GLN GLN THR GLU HIS GLY ASN TYR LEU SER LEU GLU          
SEQRES  25 A  382  PRO ASP ILE SER GLU SER ILE VAL ARG SER VAL ALA LYS          
SEQRES  26 A  382  GLU ALA GLU GLN LEU SER LEU ARG GLN GLU THR ALA ILE          
SEQRES  27 A  382  LEU LEU CYS SER PRO PRO VAL ARG MET TYR VAL LYS GLN          
SEQRES  28 A  382  LEU LEU GLU ARG TYR PHE PRO ASP LEU PRO VAL LEU SER          
SEQRES  29 A  382  TYR ASN GLU LEU GLU ALA ASN VAL GLU VAL GLN SER ILE          
SEQRES  30 A  382  GLY VAL VAL ASP ILE                                          
FORMUL   2  HOH   *120(H2 O)                                                    
HELIX    1   1 GLU A  318  ASP A  327  1                                  10    
HELIX    2   2 SER A  331  VAL A  336  1                                   6    
HELIX    3   3 GLN A  337  LEU A  339  5                                   3    
HELIX    4   4 LEU A  352  ALA A  358  1                                   7    
HELIX    5   5 ASP A  363  GLY A  380  1                                  18    
HELIX    6   6 ASP A  464  ILE A  485  1                                  22    
HELIX    7   7 GLY A  486  TYR A  501  1                                  16    
HELIX    8   8 TYR A  501  THR A  509  1                                   9    
HELIX    9   9 SER A  514  GLU A  528  1                                  15    
HELIX   10  10 ASN A  534  GLY A  546  1                                  13    
HELIX   11  11 ASP A  551  LEU A  563  1                                  13    
HELIX   12  12 LEU A  563  ALA A  572  1                                  10    
HELIX   13  13 SER A  584  VAL A  595  1                                  12    
HELIX   14  14 GLU A  607  ARG A  628  1                                  22    
HELIX   15  15 SER A  637  GLU A  649  1                                  13    
HELIX   16  16 ASN A  661  LEU A  663  5                                   3    
SHEET    1   A 4 ARG A 387  ASP A 390  0                                        
SHEET    2   A 4 ILE A 344  PHE A 348  1  N  PHE A 346   O  ARG A 387           
SHEET    3   A 4 GLU A 398  ILE A 403 -1  O  ARG A 400   N  GLU A 347           
SHEET    4   A 4 ASN A 406  GLU A 412 -1  O  ALA A 409   N  LEU A 401           
SHEET    1   B 2 LEU A 578  LYS A 579  0                                        
SHEET    2   B 2 VAL A 669  GLN A 670  1  O  GLN A 670   N  LEU A 578           
SHEET    1   C 2 THR A 582  CYS A 583  0                                        
SHEET    2   C 2 VAL A 674  VAL A 675  1  O  VAL A 675   N  THR A 582           
SHEET    1   D 2 LEU A 634  CYS A 636  0                                        
SHEET    2   D 2 VAL A 657  SER A 659  1  O  LEU A 658   N  LEU A 634           
CISPEP   1 THR A  509    PRO A  510          0        -0.63                     
CISPEP   2 ASN A  511    PRO A  512          0        12.54                     
CRYST1   84.177   84.177  118.160  90.00  90.00 120.00 P 65          6          
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      0.011880  0.006859  0.000000        0.00000                         
SCALE2      0.000000  0.013717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008463        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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