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Database: PDB
Entry: 3HXP
LinkDB: 3HXP
Original site: 3HXP 
HEADER    TRANSPORT PROTEIN                       21-JUN-09   3HXP              
TITLE     CRYSTAL STRUCTURE OF THE FHUD FOLD-FAMILY BSU3320, A PERIPLASMIC      
TITLE    2 BINDING PROTEIN COMPONENT OF A FEP/FEC-LIKE FERRICHROME ABC          
TITLE    3 TRANSPORTER FROM BACILLUS SUBTILIS. NORTHEAST STRUCTURAL GENOMICS    
TITLE    4 CONSORTIUM TARGET SR577                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON(3+)-HYDROXAMATE-BINDING PROTEIN FHUD;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: IRON(III)-HYDROXAMATE-BINDING PROTEIN FHUD, FERRICHROME-    
COMPND   5 BINDING PROTEIN, FERRIC HYDROXAMATE UPTAKE PROTEIN D;                
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: BSU33320, FHUD;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+ MAGIC;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    ALPHA-BETA PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE     
KEYWDS   2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, CELL     
KEYWDS   3 MEMBRANE, ION TRANSPORT, IRON, IRON TRANSPORT, LIPOPROTEIN,          
KEYWDS   4 MEMBRANE, PALMITATE, TRANSPORT, TRANSPORT PROTEIN                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FOROUHAR,H.NEELY,J.SEETHARAMAN,F.FANG,R.XIAO,K.CUNNINGHAM,L.MA,     
AUTHOR   2 C.X.CHEN,J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,G.T.MONTELIONE,L.TONG,  
AUTHOR   3 J.F.HUNT,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)             
REVDAT   3   24-JUL-19 3HXP    1       REMARK LINK                              
REVDAT   2   01-NOV-17 3HXP    1       REMARK                                   
REVDAT   1   07-JUL-09 3HXP    0                                                
JRNL        AUTH   F.FOROUHAR,H.NEELY,J.SEETHARAMAN,F.FANG,R.XIAO,K.CUNNINGHAM, 
JRNL        AUTH 2 L.MA,C.X.CHEN,J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,           
JRNL        AUTH 3 G.T.MONTELIONE,L.TONG,J.F.HUNT                               
JRNL        TITL   NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET SR577        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2 & XTALVIEW                                   
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 375966.906                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 69.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 7749                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.272                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 776                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.31                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 48.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 491                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE                    : 0.3730                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 47                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.054                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2123                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 14                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 83.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -26.68000                                            
REMARK   3    B22 (A**2) : 49.92000                                             
REMARK   3    B33 (A**2) : -23.24000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.69                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.59                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.02                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.820                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.25                                                 
REMARK   3   BSOL        : 2.23                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3HXP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053710.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10255                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.21500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SNB THEN SOLVE/RESOLVE                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,   
REMARK 280  0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION: 50 MM      
REMARK 280  TAPS (PH 9), 20% PEG 8K, AND 25MM KCL. , VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       35.72650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.47750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.72650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.47750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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     MSE A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     GLU A    29                                                      
REMARK 465     SER A    30                                                      
REMARK 465     LYS A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     GLU A    41                                                      
REMARK 465     THR A    42                                                      
REMARK 465     PHE A    43                                                      
REMARK 465     THR A    44                                                      
REMARK 465     GLU A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
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    LYS A   134     O    LYS A   134     2665     1.82            
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 A  49       54.74   -117.48                                   
REMARK 500    ASN A  51       94.93    -66.69                                   
REMARK 500    LYS A  53      122.79    -27.77                                   
REMARK 500    HIS A  57       57.29     70.19                                   
REMARK 500    PRO A  58     -177.05    -63.72                                   
REMARK 500    LYS A  59       -1.50   -149.66                                   
REMARK 500    ARG A  60       85.70   -155.47                                   
REMARK 500    GLU A  84      -83.90    -34.60                                   
REMARK 500    ASN A  85      -42.46    -28.40                                   
REMARK 500    TYR A  92      -89.67    -92.57                                   
REMARK 500    LYS A  95       17.26   -154.93                                   
REMARK 500    ASN A  97       48.90    160.90                                   
REMARK 500    ILE A 102     -157.93   -105.92                                   
REMARK 500    ASP A 104      -19.76    -47.61                                   
REMARK 500    SER A 107       92.98    -42.49                                   
REMARK 500    ILE A 135      -42.35   -132.30                                   
REMARK 500    ASP A 144       11.24     44.25                                   
REMARK 500    ASP A 147     -153.56    -84.30                                   
REMARK 500    PHE A 155       -1.13    -59.04                                   
REMARK 500    THR A 159      -88.88    -88.50                                   
REMARK 500    LYS A 190     -175.69    -67.37                                   
REMARK 500    ASP A 208       69.00   -116.53                                   
REMARK 500    PHE A 209       11.63   -174.00                                   
REMARK 500    LYS A 218      -81.98    -90.39                                   
REMARK 500    ILE A 233      -66.70   -124.14                                   
REMARK 500    ASP A 234       37.63    -72.94                                   
REMARK 500    GLN A 235      -81.48    179.71                                   
REMARK 500    ILE A 242     -149.07   -142.65                                   
REMARK 500    LEU A 247      -47.95   -134.88                                   
REMARK 500    PRO A 248       16.26    -68.13                                   
REMARK 500    ALA A 251       99.29    -40.39                                   
REMARK 500    PHE A 256       64.72   -108.46                                   
REMARK 500    HIS A 285       48.30    -97.30                                   
REMARK 500    LEU A 313       12.06   -143.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G9Q   RELATED DB: PDB                                   
REMARK 900 THE CURRENT STRUCTURE IS FULL-LENGTH PROTEIN WITHOUT THE             
REMARK 900 TRANSMEMBRANE PART.                                                  
REMARK 900 RELATED ID: SR577   RELATED DB: TARGETDB                             
DBREF  3HXP A   25   315  UNP    P37580   FHUD_BACSU      25    315             
SEQADV 3HXP MSE A   24  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP LEU A  316  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP GLU A  317  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  318  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  319  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  320  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  321  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  322  UNP  P37580              EXPRESSION TAG                 
SEQADV 3HXP HIS A  323  UNP  P37580              EXPRESSION TAG                 
SEQRES   1 A  300  MSE GLY ASN ASN SER GLU SER LYS GLY SER ALA SER ASP          
SEQRES   2 A  300  SER LYS GLY ALA GLU THR PHE THR TYR LYS ALA GLU ASN          
SEQRES   3 A  300  GLY ASN VAL LYS ILE PRO LYS HIS PRO LYS ARG VAL VAL          
SEQRES   4 A  300  VAL MSE ALA ASP GLY TYR TYR GLY TYR PHE LYS THR LEU          
SEQRES   5 A  300  GLY ILE ASN VAL VAL GLY ALA PRO GLU ASN VAL PHE LYS          
SEQRES   6 A  300  ASN PRO TYR TYR LYS GLY LYS THR ASN GLY VAL GLU ASN          
SEQRES   7 A  300  ILE GLY ASP GLY THR SER VAL GLU LYS VAL ILE ASP LEU          
SEQRES   8 A  300  ASN PRO ASP LEU ILE ILE VAL TRP THR THR GLN GLY ALA          
SEQRES   9 A  300  ASP ILE LYS LYS LEU GLU LYS ILE ALA PRO THR VAL ALA          
SEQRES  10 A  300  VAL LYS TYR ASP LYS LEU ASP ASN ILE GLU GLN LEU LYS          
SEQRES  11 A  300  GLU PHE ALA LYS MSE THR GLY THR GLU ASP LYS ALA GLU          
SEQRES  12 A  300  LYS TRP LEU ALA LYS TRP ASP LYS LYS VAL ALA ALA ALA          
SEQRES  13 A  300  LYS THR LYS ILE LYS LYS ALA VAL GLY ASP LYS THR ILE          
SEQRES  14 A  300  SER ILE MSE GLN THR ASN GLY LYS ASP ILE TYR VAL PHE          
SEQRES  15 A  300  GLY LYS ASP PHE GLY ARG GLY GLY SER ILE ILE TYR LYS          
SEQRES  16 A  300  ASP LEU GLY LEU GLN ALA THR LYS LEU THR LYS GLU LYS          
SEQRES  17 A  300  ALA ILE ASP GLN GLY PRO GLY TYR THR SER ILE SER LEU          
SEQRES  18 A  300  GLU LYS LEU PRO ASP PHE ALA GLY ASP TYR ILE PHE ALA          
SEQRES  19 A  300  GLY PRO TRP GLN SER GLY GLY ASP ASP GLY GLY VAL PHE          
SEQRES  20 A  300  GLU SER SER ILE TRP LYS ASN LEU ASN ALA VAL LYS ASN          
SEQRES  21 A  300  GLY HIS VAL TYR LYS MSE ASP PRO ILE GLY PHE TYR PHE          
SEQRES  22 A  300  THR ASP PRO ILE SER LEU GLU GLY GLN LEU GLU PHE ILE          
SEQRES  23 A  300  THR GLU SER LEU THR LYS LEU GLU HIS HIS HIS HIS HIS          
SEQRES  24 A  300  HIS                                                          
MODRES 3HXP MSE A   64  MET  SELENOMETHIONINE                                   
MODRES 3HXP MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 3HXP MSE A  195  MET  SELENOMETHIONINE                                   
MODRES 3HXP MSE A  289  MET  SELENOMETHIONINE                                   
HET    MSE  A  64       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 195       8                                                       
HET    MSE  A 289       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *14(H2 O)                                                     
HELIX    1   1 ALA A   65  GLY A   67  5                                   3    
HELIX    2   2 TYR A   68  GLY A   76  1                                   9    
HELIX    3   3 PRO A   83  ASN A   89  1                                   7    
HELIX    4   4 ASN A   89  GLY A   94  1                                   6    
HELIX    5   5 GLU A  109  LEU A  114  1                                   6    
HELIX    6   6 LYS A  130  ILE A  135  5                                   6    
HELIX    7   7 ILE A  149  MSE A  158  1                                  10    
HELIX    8   8 THR A  161  GLY A  188  1                                  28    
HELIX    9   9 GLY A  212  LYS A  218  1                                   7    
HELIX   10  10 THR A  225  ILE A  233  1                                   9    
HELIX   11  11 LEU A  278  ASN A  283  1                                   6    
HELIX   12  12 ASP A  290  TYR A  295  1                                   6    
HELIX   13  13 ASP A  298  SER A  312  1                                  15    
SHEET    1   A 4 VAL A  79  GLY A  81  0                                        
SHEET    2   A 4 VAL A  61  VAL A  63  1  N  VAL A  61   O  VAL A  80           
SHEET    3   A 4 LEU A 118  TRP A 122  1  O  LEU A 118   N  VAL A  62           
SHEET    4   A 4 THR A 138  VAL A 141  1  O  VAL A 141   N  VAL A 121           
SHEET    1   B 3 ASP A 201  PHE A 205  0                                        
SHEET    2   B 3 ILE A 192  ASN A 198 -1  N  ASN A 198   O  ASP A 201           
SHEET    3   B 3 TYR A 254  PHE A 256  1  O  PHE A 256   N  SER A 193           
LINK         C   VAL A  63                 N   MSE A  64     1555   1555  1.32  
LINK         C   MSE A  64                 N   ALA A  65     1555   1555  1.33  
LINK         C   LYS A 157                 N   MSE A 158     1555   1555  1.33  
LINK         C   MSE A 158                 N   THR A 159     1555   1555  1.33  
LINK         C   ILE A 194                 N   MSE A 195     1555   1555  1.33  
LINK         C   MSE A 195                 N   GLN A 196     1555   1555  1.33  
LINK         C   LYS A 288                 N   MSE A 289     1555   1555  1.32  
LINK         C   MSE A 289                 N   ASP A 290     1555   1555  1.33  
CRYST1   71.453  126.955   38.610  90.00  90.00  90.00 P 21 21 2     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      0.013995  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007877  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.025900        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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