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Database: PDB
Entry: 2FNP
LinkDB: 2FNP
Original site: 2FNP 
HEADER    TRANSCRIPTION                           11-JAN-06   2FNP              
TITLE     CRYSTAL STRUCTURE OF SARA                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STAPHYLOCOCCAL ACCESSORY REGULATOR A;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: STRAIN MW2;                                                  
SOURCE   5 GENE: SARA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL-21;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET30-B                                    
KEYWDS    WING-HELIX, DNA BINDING, TRANSCRIPTION                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LIU,A.C.MANNA,C.H.PAN,A.L.CHEUNG,G.ZHANG                            
REVDAT   4   14-FEB-24 2FNP    1       SEQADV                                   
REVDAT   3   24-FEB-09 2FNP    1       VERSN                                    
REVDAT   2   14-MAR-06 2FNP    1       JRNL                                     
REVDAT   1   31-JAN-06 2FNP    0                                                
JRNL        AUTH   Y.LIU,A.C.MANNA,C.H.PAN,I.A.KRIKSUNOV,D.J.THIEL,A.L.CHEUNG,  
JRNL        AUTH 2 G.ZHANG                                                      
JRNL        TITL   STRUCTURAL AND FUNCTION ANALYSES OF THE GLOBAL REGULATORY    
JRNL        TITL 2 PROTEIN SARA FROM STAPHYLOCOCCUS AUREUS.                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103  2392 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   16455801                                                     
JRNL        DOI    10.1073/PNAS.0510439103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.17                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 732953.630                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 9426                           
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) : 0.285                           
REMARK   3   FREE R VALUE                     : 0.308                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 506                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.014                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 77.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1236                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5170                       
REMARK   3   BIN FREE R VALUE                    : 0.4460                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 72                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.053                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2052                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 11                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 70.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.18000                                            
REMARK   3    B22 (A**2) : -30.62000                                            
REMARK   3    B33 (A**2) : 40.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 23.24000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.52                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.93                            
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) : 0.86                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.910                           
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        : 0.33                                                 
REMARK   3   BSOL        : 50.59                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FNP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000036093.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 52.074                             
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, TRUNCATE                   
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9772                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06800                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 8000, 0.2M CALCIUM CHLORIDE,     
REMARK 280  0.1M CACODYLATE, PH 6.5, VAPOR DIFFUSION, TEMPERATURE 277K          
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       32.37900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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     MET A   101                                                      
REMARK 465     ALA A   102                                                      
REMARK 465     MET B   101                                                      
REMARK 465     ALA B   102                                                      
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   OD1  ASN A   197     OE1  GLN A   200              2.11            
REMARK 500   O    ASN B   146     OH   TYR B   151              2.14            
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   O    GLU B   129     ND2  ASN B   185     2455     2.17            
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    ASN A 185   N   -  CA  -  C   ANGL. DEV. =  19.1 DEGREES          
REMARK 500    ASP A 188   N   -  CA  -  C   ANGL. DEV. = -16.8 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    THR A 104       84.78     82.62                                   
REMARK 500    ASP A 120      -34.08    -39.55                                   
REMARK 500    LYS A 127        7.23    -68.28                                   
REMARK 500    HIS A 159      -28.40    -27.76                                   
REMARK 500    LEU A 160      -84.06    -85.56                                   
REMARK 500    ASN A 161        8.06    146.31                                   
REMARK 500    LYS A 163       58.07   -106.94                                   
REMARK 500    GLN A 164      -83.82     40.72                                   
REMARK 500    VAL A 167      -82.22    -59.60                                   
REMARK 500    VAL A 168      -56.18    -18.68                                   
REMARK 500    ASP A 178       87.49     72.74                                   
REMARK 500    GLU A 186      -71.34   -103.71                                   
REMARK 500    ASP A 188       12.15     84.17                                   
REMARK 500    ARG A 190       72.87     -7.48                                   
REMARK 500    THR A 191       50.59   -175.27                                   
REMARK 500    ALA A 198      -31.31    -33.20                                   
REMARK 500    ASP B 108     -160.77   -170.32                                   
REMARK 500    ASN B 146       72.20   -119.39                                   
REMARK 500    LYS B 147      106.50    -55.63                                   
REMARK 500    ASN B 161       45.59     99.71                                   
REMARK 500    TYR B 162     -155.08   -112.50                                   
REMARK 500    GLN B 164      -67.93     -4.05                                   
REMARK 500    VAL B 167      -86.13    -74.94                                   
REMARK 500    VAL B 168      -61.05    -11.20                                   
REMARK 500    GLU B 186     -101.72     95.36                                   
REMARK 500    HIS B 187       77.68    -44.06                                   
REMARK 500    GLU B 189      -13.18     64.84                                   
REMARK 500    ARG B 190      -82.76    -71.45                                   
REMARK 500    THR B 191      133.55    -29.57                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2FNP A  102   224  UNP    Q7A1N5   SARA_STAAW       1    123             
DBREF  2FNP B  102   224  UNP    Q7A1N5   SARA_STAAW       1    123             
SEQADV 2FNP MET A  101  UNP  Q7A1N5              INITIATING METHIONINE          
SEQADV 2FNP MET B  101  UNP  Q7A1N5              INITIATING METHIONINE          
SEQRES   1 A  124  MET ALA ILE THR LYS ILE ASN ASP CYS PHE GLU LEU LEU          
SEQRES   2 A  124  SER MET VAL THR TYR ALA ASP LYS LEU LYS SER LEU ILE          
SEQRES   3 A  124  LYS LYS GLU PHE SER ILE SER PHE GLU GLU PHE ALA VAL          
SEQRES   4 A  124  LEU THR TYR ILE SER GLU ASN LYS GLU LYS GLU TYR TYR          
SEQRES   5 A  124  PHE LYS ASP ILE ILE ASN HIS LEU ASN TYR LYS GLN PRO          
SEQRES   6 A  124  GLN VAL VAL LYS ALA VAL LYS ILE LEU SER GLN GLU ASP          
SEQRES   7 A  124  TYR PHE ASP LYS LYS ARG ASN GLU HIS ASP GLU ARG THR          
SEQRES   8 A  124  VAL LEU ILE LEU VAL ASN ALA GLN GLN ARG LYS LYS ILE          
SEQRES   9 A  124  GLU SER LEU LEU SER ARG VAL ASN LYS ARG ILE THR GLU          
SEQRES  10 A  124  ALA ASN ASN GLU ILE GLU LEU                                  
SEQRES   1 B  124  MET ALA ILE THR LYS ILE ASN ASP CYS PHE GLU LEU LEU          
SEQRES   2 B  124  SER MET VAL THR TYR ALA ASP LYS LEU LYS SER LEU ILE          
SEQRES   3 B  124  LYS LYS GLU PHE SER ILE SER PHE GLU GLU PHE ALA VAL          
SEQRES   4 B  124  LEU THR TYR ILE SER GLU ASN LYS GLU LYS GLU TYR TYR          
SEQRES   5 B  124  PHE LYS ASP ILE ILE ASN HIS LEU ASN TYR LYS GLN PRO          
SEQRES   6 B  124  GLN VAL VAL LYS ALA VAL LYS ILE LEU SER GLN GLU ASP          
SEQRES   7 B  124  TYR PHE ASP LYS LYS ARG ASN GLU HIS ASP GLU ARG THR          
SEQRES   8 B  124  VAL LEU ILE LEU VAL ASN ALA GLN GLN ARG LYS LYS ILE          
SEQRES   9 B  124  GLU SER LEU LEU SER ARG VAL ASN LYS ARG ILE THR GLU          
SEQRES  10 B  124  ALA ASN ASN GLU ILE GLU LEU                                  
FORMUL   3  HOH   *11(H2 O)                                                     
HELIX    1   1 ASP A  108  PHE A  130  1                                  23    
HELIX    2   2 SER A  133  ASN A  146  1                                  14    
HELIX    3   3 PHE A  153  ASN A  161  1                                   9    
HELIX    4   4 GLN A  164  ASP A  178  1                                  15    
HELIX    5   5 GLN A  199  ASN A  219  1                                  21    
HELIX    6   6 ASP B  108  SER B  131  1                                  24    
HELIX    7   7 SER B  133  ASN B  146  1                                  14    
HELIX    8   8 PHE B  153  ASN B  161  1                                   9    
HELIX    9   9 LYS B  163  GLN B  176  1                                  14    
HELIX   10  10 GLU B  186  ARG B  190  5                                   5    
HELIX   11  11 GLN B  199  ASN B  219  1                                  21    
SHEET    1   A 3 GLU A 150  TYR A 152  0                                        
SHEET    2   A 3 VAL A 192  LEU A 195 -1  O  ILE A 194   N  TYR A 151           
SHEET    3   A 3 ASP A 181  ARG A 184 -1  N  LYS A 183   O  LEU A 193           
SHEET    1   B 3 GLU B 150  TYR B 152  0                                        
SHEET    2   B 3 LEU B 193  LEU B 195 -1  O  ILE B 194   N  TYR B 151           
SHEET    3   B 3 ASP B 181  LYS B 183 -1  N  LYS B 183   O  LEU B 193           
CRYST1   52.074   64.758   55.564  90.00 117.73  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      0.019203  0.000000  0.010095        0.00000                         
SCALE2      0.000000  0.015442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020332        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system