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Database: PDB
Entry: 2FIP
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Original site: 2FIP 
HEADER    TRANSCRIPTION                           30-DEC-05   2FIP              
TITLE     PHAGE PHI29 TRANSCRIPTION REGULATOR P4                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LATE GENES ACTIVATOR;                                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 SYNONYM: EARLY PROTEIN GP4;                                          
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS PHAGE PHI29;                           
SOURCE   3 ORGANISM_TAXID: 10756;                                               
SOURCE   4 GENE: 4;                                                             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PROTEIN-DNA COMPLEX; N-HOOK DNA-BINDING MOTIF; TRANSCRIPTION          
KEYWDS   2 REGULATION, TRANSCRIPTION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BADIA,A.CAMACHO,L.PEREZ-LAGO,C.ESCANDON,M.SALAS,M.COLL              
REVDAT   4   18-OCT-17 2FIP    1       REMARK                                   
REVDAT   3   24-FEB-09 2FIP    1       VERSN                                    
REVDAT   2   03-OCT-06 2FIP    1       JRNL                                     
REVDAT   1   26-SEP-06 2FIP    0                                                
JRNL        AUTH   D.BADIA,A.CAMACHO,L.PEREZ-LAGO,C.ESCANDON,M.SALAS,M.COLL     
JRNL        TITL   THE STRUCTURE OF PHAGE PHI29 TRANSCRIPTION REGULATOR P4-DNA  
JRNL        TITL 2 COMPLEX REVEALS AN N-HOOK MOTIF FOR DNA                      
JRNL        REF    MOL.CELL                      V.  22    73 2006              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   16600871                                                     
JRNL        DOI    10.1016/J.MOLCEL.2006.02.019                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 81377                          
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) : 0.227                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8164                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5837                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 562                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.24100                                              
REMARK   3    B22 (A**2) : -6.65000                                             
REMARK   3    B33 (A**2) : 2.40900                                              
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.240                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 51.61                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2FIP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000035924.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
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 : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 81606                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 0.9                                
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.9                                
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   (%): 67.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NACL, 10% PEG 6000, PH 7.5, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       33.17450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.20450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       68.11600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.20450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.17450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       68.11600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 1680 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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     ARG D   116                                                      
REMARK 465     GLN F   113                                                      
REMARK 465     LYS F   114                                                      
REMARK 465     PRO F   115                                                      
REMARK 465     ARG F   116                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   43   OE1  OE2                                            
REMARK 480     LYS A   50   CD   CE   NZ                                        
REMARK 480     LYS A   84   CE   NZ                                             
REMARK 480     ASP A   86   CG   OD1  OD2                                       
REMARK 480     ASN A  105   CG   OD1  ND2                                       
REMARK 480     THR A  106   CG2                                                 
REMARK 480     LYS B   46   NZ                                                  
REMARK 480     LYS B   50   CD   CE   NZ                                        
REMARK 480     LYS B  114   CE   NZ                                             
REMARK 480     ARG B  116   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU C   43   CG   CD   OE1  OE2                                  
REMARK 480     LYS C   46   CE   NZ                                             
REMARK 480     LYS C   47   CG   CD   CE   NZ                                   
REMARK 480     LYS C   50   CE   NZ                                             
REMARK 480     GLU C   73   CD   OE1  OE2                                       
REMARK 480     ARG C  116   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN D    5   CG   CD   OE1  NE2                                  
REMARK 480     LYS D   13   CD   CE   NZ                                        
REMARK 480     LYS D  114   CD   CE   NZ                                        
REMARK 480     LYS E   13   CD   CE   NZ                                        
REMARK 480     LYS E   36   CD   CE   NZ                                        
REMARK 480     LYS E   47   NZ                                                  
REMARK 480     LYS E   50   CD   CE   NZ                                        
REMARK 480     GLN F    5   CG   CD   OE1  NE2                                  
REMARK 480     ASN F   11   ND2                                                 
REMARK 480     LYS F   51   NZ                                                  
REMARK 480     LYS F   84   CG   CD   CE   NZ                                   
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  22      -20.67     86.93                                   
REMARK 500    THR B  22      -12.20     87.79                                   
REMARK 500    THR C  22      -15.33     85.11                                   
REMARK 500    MET C  62       32.22    -93.23                                   
REMARK 500    THR D  22      -19.64     89.70                                   
REMARK 500    LYS D 114       62.23     37.96                                   
REMARK 500    THR E  22      -15.18     84.55                                   
REMARK 500    LYS F  13       -9.48    -59.84                                   
REMARK 500    THR F  22      -18.63     80.62                                   
REMARK 500    LEU F  83       73.84   -100.63                                   
REMARK 500    LYS F  84       93.20     66.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FIO   RELATED DB: PDB                                   
REMARK 900 PHAGE PHI29 TRANSCRIPTION REGULATOR P4-DNA COMPLEX                   
DBREF  2FIP A    2   116  UNP    P03682   VG4_BPPH2        2    116             
DBREF  2FIP B    2   116  UNP    P03682   VG4_BPPH2        2    116             
DBREF  2FIP C    2   116  UNP    P03682   VG4_BPPH2        2    116             
DBREF  2FIP D    2   116  UNP    P03682   VG4_BPPH2        2    116             
DBREF  2FIP E    2   116  UNP    P03682   VG4_BPPH2        2    116             
DBREF  2FIP F    2   116  UNP    P03682   VG4_BPPH2        2    116             
SEQRES   1 A  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 A  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 A  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 A  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 A  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 A  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 A  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 A  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 A  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
SEQRES   1 B  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 B  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 B  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 B  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 B  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 B  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 B  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 B  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 B  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
SEQRES   1 C  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 C  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 C  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 C  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 C  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 C  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 C  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 C  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 C  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
SEQRES   1 D  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 D  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 D  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 D  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 D  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 D  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 D  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 D  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 D  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
SEQRES   1 E  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 E  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 E  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 E  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 E  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 E  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 E  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 E  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 E  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
SEQRES   1 F  115  PRO LYS THR GLN ARG GLY ILE TYR HIS ASN LEU LYS GLU          
SEQRES   2 F  115  SER GLU TYR VAL ALA SER ASN THR ASP VAL THR PHE PHE          
SEQRES   3 F  115  PHE SER SER GLU LEU TYR LEU ASN LYS PHE LEU ASP GLY          
SEQRES   4 F  115  TYR GLN GLU TYR ARG LYS LYS PHE ASN LYS LYS ILE GLU          
SEQRES   5 F  115  ARG VAL ALA VAL THR PRO TRP ASN MET ASP MET LEU ALA          
SEQRES   6 F  115  ASP ILE THR PHE TYR SER GLU VAL GLU LYS ARG GLY PHE          
SEQRES   7 F  115  HIS ALA TRP LEU LYS GLY ASP ASN ALA THR TRP ARG GLU          
SEQRES   8 F  115  VAL HIS VAL TYR ALA LEU ARG ILE MET THR LYS PRO ASN          
SEQRES   9 F  115  THR LEU ASP TRP SER ARG ILE GLN LYS PRO ARG                  
FORMUL   7  HOH   *562(H2 O)                                                    
HELIX    1   1 ASN A   11  SER A   15  5                                   5    
HELIX    2   2 SER A   30  ARG A   54  1                                  25    
HELIX    3   3 MET A   62  GLU A   75  1                                  14    
HELIX    4   4 THR A   89  MET A  101  1                                  13    
HELIX    5   5 ASN B   11  SER B   15  5                                   5    
HELIX    6   6 SER B   30  ARG B   54  1                                  25    
HELIX    7   7 MET B   62  GLU B   75  1                                  14    
HELIX    8   8 THR B   89  MET B  101  1                                  13    
HELIX    9   9 ASN C   11  SER C   15  5                                   5    
HELIX   10  10 SER C   30  ALA C   56  1                                  27    
HELIX   11  11 MET C   62  GLU C   75  1                                  14    
HELIX   12  12 THR C   89  MET C  101  1                                  13    
HELIX   13  13 ASN D   11  SER D   15  5                                   5    
HELIX   14  14 SER D   30  ARG D   54  1                                  25    
HELIX   15  15 MET D   62  GLU D   75  1                                  14    
HELIX   16  16 THR D   89  ILE D  100  1                                  12    
HELIX   17  17 MET D  101  LYS D  103  5                                   3    
HELIX   18  18 ASN E   11  SER E   15  5                                   5    
HELIX   19  19 SER E   30  ALA E   56  1                                  27    
HELIX   20  20 MET E   62  GLU E   75  1                                  14    
HELIX   21  21 THR E   89  MET E  101  1                                  13    
HELIX   22  22 ASN F   11  SER F   15  5                                   5    
HELIX   23  23 SER F   30  ARG F   54  1                                  25    
HELIX   24  24 MET F   62  GLU F   75  1                                  14    
HELIX   25  25 THR F   89  ILE F  100  1                                  12    
HELIX   26  26 MET F  101  LYS F  103  5                                   3    
SHEET    1   A 5 ASP A  86  ALA A  88  0                                        
SHEET    2   A 5 ALA A  81  LEU A  83 -1  N  LEU A  83   O  ASP A  86           
SHEET    3   A 5 VAL A  24  PHE A  27 -1  N  THR A  25   O  TRP A  82           
SHEET    4   A 5 VAL A  18  SER A  20 -1  N  ALA A  19   O  PHE A  26           
SHEET    5   A 5 SER A 110  ILE A 112 -1  O  SER A 110   N  SER A  20           
SHEET    1   B 5 ASP B  86  ALA B  88  0                                        
SHEET    2   B 5 ALA B  81  LEU B  83 -1  N  LEU B  83   O  ASP B  86           
SHEET    3   B 5 VAL B  24  PHE B  28 -1  N  THR B  25   O  TRP B  82           
SHEET    4   B 5 TYR B  17  SER B  20 -1  N  TYR B  17   O  PHE B  28           
SHEET    5   B 5 SER B 110  ILE B 112 -1  O  SER B 110   N  SER B  20           
SHEET    1   C 5 ASP C  86  ALA C  88  0                                        
SHEET    2   C 5 ALA C  81  LEU C  83 -1  N  LEU C  83   O  ASP C  86           
SHEET    3   C 5 VAL C  24  PHE C  28 -1  N  THR C  25   O  TRP C  82           
SHEET    4   C 5 TYR C  17  SER C  20 -1  N  TYR C  17   O  PHE C  28           
SHEET    5   C 5 SER C 110  ILE C 112 -1  O  SER C 110   N  SER C  20           
SHEET    1   D 5 ASP D  86  ALA D  88  0                                        
SHEET    2   D 5 ALA D  81  LEU D  83 -1  N  LEU D  83   O  ASP D  86           
SHEET    3   D 5 VAL D  24  PHE D  27 -1  N  THR D  25   O  TRP D  82           
SHEET    4   D 5 VAL D  18  SER D  20 -1  N  ALA D  19   O  PHE D  26           
SHEET    5   D 5 SER D 110  ARG D 111 -1  O  SER D 110   N  SER D  20           
SHEET    1   E 5 ASP E  86  ALA E  88  0                                        
SHEET    2   E 5 ALA E  81  LEU E  83 -1  N  LEU E  83   O  ASP E  86           
SHEET    3   E 5 VAL E  24  PHE E  28 -1  N  THR E  25   O  TRP E  82           
SHEET    4   E 5 TYR E  17  SER E  20 -1  N  TYR E  17   O  PHE E  28           
SHEET    5   E 5 SER E 110  ILE E 112 -1  O  SER E 110   N  SER E  20           
SHEET    1   F 5 ASP F  86  ALA F  88  0                                        
SHEET    2   F 5 ALA F  81  LEU F  83 -1  N  ALA F  81   O  ALA F  88           
SHEET    3   F 5 THR F  25  PHE F  28 -1  N  THR F  25   O  TRP F  82           
SHEET    4   F 5 TYR F  17  SER F  20 -1  N  TYR F  17   O  PHE F  28           
SHEET    5   F 5 SER F 110  ARG F 111 -1  O  SER F 110   N  SER F  20           
CRYST1   66.349  136.232  140.409  90.00  90.00  90.00 P 21 21 21   24          
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      0.015072  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007340  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007122        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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