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Database: PDB
Entry: 3EAA
LinkDB: 3EAA
Original site: 3EAA 
HEADER    UNKNOWN FUNCTION                        25-AUG-08   3EAA              
TITLE     STRUCTURE OF A TYPE SIX SECRETION SYSTEM PROTEIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EVPC;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EDWARDSIELLA TARDA;                             
SOURCE   3 ORGANISM_TAXID: 636;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PETM                                      
KEYWDS    EVPC, T6SS, UNKNOWN FUNCTION                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.JOBICHEN,J.SIVARAMAN                                                
REVDAT   2   27-OCT-10 3EAA    1       JRNL                                     
REVDAT   1   25-AUG-09 3EAA    0                                                
JRNL        AUTH   C.JOBICHEN,S.CHAKRABORTY,M.LI,J.ZHENG,L.JOSEPH,Y.K.MOK,      
JRNL        AUTH 2 K.Y.LEUNG,J.SIVARAMAN                                        
JRNL        TITL   STRUCTURAL BASIS FOR THE SECRETION OF EVPC: A KEY TYPE VI    
JRNL        TITL 2 SECRETION SYSTEM PROTEIN FROM EDWARDSIELLA TARDA             
JRNL        REF    PLOS ONE                      V.   5 E1291 2010              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   20886112                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0012910                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.96                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.200                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 9073                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.780                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 434                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.9650 -  4.0270    0.99     3083   150  0.2100 0.2480        
REMARK   3     2  4.0270 -  3.1980    0.91     2775   157  0.2470 0.2880        
REMARK   3     3  3.1980 -  2.7940    0.91     2781   127  0.2520 0.3260        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.23                                          
REMARK   3   B_SOL              : 17.43                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.37100                                             
REMARK   3    B22 (A**2) : -4.37100                                             
REMARK   3    B33 (A**2) : 8.74100                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2400                                  
REMARK   3   ANGLE     :  1.032           3252                                  
REMARK   3   CHIRALITY :  0.063            348                                  
REMARK   3   PLANARITY :  0.003            422                                  
REMARK   3   DIHEDRAL  : 18.624            800                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 2:163 )                 
REMARK   3     SELECTION          : chain B and (resseq 2:163 )                 
REMARK   3     ATOM PAIRS NUMBER  : 1174                                        
REMARK   3     RMSD               : 0.015                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3EAA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB049072.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : CN1707                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 9073                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.794                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB CODE 1Y12                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULPHATE, 0.1M BIS-        
REMARK 280  TRIS(PH 6.5), 25% PEG 3350, PH 7.5, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 295K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17300 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  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     1                                                      
REMARK 465     MSE B     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE A   3    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  20    CG   CD   CE   NZ                                   
REMARK 470     MSE A  40    CG  SE    CE                                        
REMARK 470     GLU A  41    CB   CG   CD   OE1  OE2                             
REMARK 470     SER A  42    OG                                                  
REMARK 470     THR A  44    OG1  CG2                                            
REMARK 470     ASN A  48    CG   OD1  ND2                                       
REMARK 470     GLN A  90    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA A  91    CB                                                  
REMARK 470     ASP A  93    CB   CG   OD1  OD2                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     ALA A 115    CB                                                  
REMARK 470     THR A 116    CB   OG1  CG2                                       
REMARK 470     ARG A 121    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP A 141    CG   OD1  OD2                                       
REMARK 470     GLN A 142    CB   CG   CD   OE1  NE2                             
REMARK 470     ASN A 143    CB   CG   OD1  ND2                                  
REMARK 470     LYS A 145    CB   CG   CD   CE   NZ                              
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     LYS A 163    CG   CD   CE   NZ                                   
REMARK 470     PHE B   3    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B  20    CG   CD   CE   NZ                                   
REMARK 470     MSE B  40    CG  SE    CE                                        
REMARK 470     GLU B  41    CB   CG   CD   OE1  OE2                             
REMARK 470     SER B  42    OG                                                  
REMARK 470     THR B  44    OG1  CG2                                            
REMARK 470     ASN B  48    CG   OD1  ND2                                       
REMARK 470     GLN B  90    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA B  91    CB                                                  
REMARK 470     ASP B  93    CB   CG   OD1  OD2                                  
REMARK 470     LYS B  94    CG   CD   CE   NZ                                   
REMARK 470     ALA B 115    CB                                                  
REMARK 470     THR B 116    CB   OG1  CG2                                       
REMARK 470     ARG B 121    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP B 141    CG   OD1  OD2                                       
REMARK 470     GLN B 142    CB   CG   CD   OE1  NE2                             
REMARK 470     ASN B 143    CB   CG   OD1  ND2                                  
REMARK 470     LYS B 145    CB   CG   CD   CE   NZ                              
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     LYS B 163    CG   CD   CE   NZ                                   
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   O    PHE B    30     O    ARG B    58              2.17            
REMARK 500   O    PHE A    30     O    ARG A    58              2.18            
REMARK 500   O    ILE A    99     O    TRP A   135              2.18            
REMARK 500   O    ILE B    99     O    TRP B   135              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MSE A  53   CG    MSE A  53  SE       0.343                       
REMARK 500    MSE A  54   CG    MSE A  54  SE       0.321                       
REMARK 500    MSE B  53   CG    MSE B  53  SE       0.343                       
REMARK 500    MSE B  54   CG    MSE B  54  SE       0.332                       
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    MSE A  53   CG  - SE   -  CE  ANGL. DEV. = -38.9 DEGREES          
REMARK 500    MSE A  54   CG  - SE   -  CE  ANGL. DEV. = -38.5 DEGREES          
REMARK 500    MSE B  54   CG  - SE   -  CE  ANGL. DEV. = -38.8 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    VAL A  12       76.66   -150.20                                   
REMARK 500    ALA A  31      121.28     52.73                                   
REMARK 500    GLU A  37       59.13    -99.78                                   
REMARK 500    GLU A  41      -80.62     33.86                                   
REMARK 500    ASN A  48       72.53     81.27                                   
REMARK 500    ASP A  64     -150.56   -143.74                                   
REMARK 500    ALA A  74      -73.68    -43.37                                   
REMARK 500    ALA A  91     -157.07    -94.02                                   
REMARK 500    LYS A  94       27.91     47.60                                   
REMARK 500    HIS A 104       58.99     72.14                                   
REMARK 500    SER A 113      147.74   -171.38                                   
REMARK 500    THR A 116      -57.79    113.66                                   
REMARK 500    ARG A 121      120.22     68.52                                   
REMARK 500    TRP A 135      -74.98    -82.22                                   
REMARK 500    GLU A 136      116.71     59.23                                   
REMARK 500    PRO A 152      108.85    -52.76                                   
REMARK 500    ALA B  31      120.24     53.74                                   
REMARK 500    GLU B  37       59.41   -100.47                                   
REMARK 500    GLU B  41      -80.41     33.94                                   
REMARK 500    ASN B  48       72.00     81.38                                   
REMARK 500    ASP B  64     -150.86   -144.22                                   
REMARK 500    ALA B  74      -72.07    -43.80                                   
REMARK 500    ALA B  91     -157.37    -93.91                                   
REMARK 500    LYS B  94       27.86     46.69                                   
REMARK 500    HIS B 104       59.16     71.46                                   
REMARK 500    SER B 113      146.77   -170.90                                   
REMARK 500    THR B 116      -56.91    114.04                                   
REMARK 500    ARG B 121      119.52     68.66                                   
REMARK 500    TRP B 135      -73.98    -82.43                                   
REMARK 500    GLU B 136      116.56     58.26                                   
REMARK 500    PRO B 152      108.51    -53.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    MSE A  53        19.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3EAA A    1   163  UNP    Q6EE19   Q6EE19_EDWTA     1    163             
DBREF  3EAA B    1   163  UNP    Q6EE19   Q6EE19_EDWTA     1    163             
SEQRES   1 A  163  MSE ALA PHE ASP THR TYR ILE LYS LEU ASP LYS VAL ASP          
SEQRES   2 A  163  GLY GLU SER THR ASP ASP LYS HIS LYS LYS TRP ILE GLU          
SEQRES   3 A  163  VAL LEU GLY PHE ALA TRP GLY ALA GLY ASN GLU CYS THR          
SEQRES   4 A  163  MSE GLU SER GLY THR GLN GLY LEU ASN THR GLY LYS ALA          
SEQRES   5 A  163  MSE MSE SER VAL LEU ARG VAL THR LYS TRP MSE ASP CYS          
SEQRES   6 A  163  ALA SER VAL LYS LEU ALA SER ALA ALA VAL GLN GLY GLN          
SEQRES   7 A  163  ASN PHE PRO THR LEU GLU LEU GLU ILE CYS THR GLN ALA          
SEQRES   8 A  163  GLY ASP LYS PHE ALA PHE CYS ILE TYR LYS PHE THR HIS          
SEQRES   9 A  163  VAL ALA VAL SER SER TYR GLN CYS SER GLY ALA THR GLY          
SEQRES  10 A  163  GLY SER ASP ARG PRO GLN GLU THR ILE ASP PHE ALA TYR          
SEQRES  11 A  163  LYS GLU VAL THR TRP GLU TYR VAL PRO GLN ASP GLN ASN          
SEQRES  12 A  163  GLY LYS ALA GLY GLY LYS ILE GLY PRO GLU GLY TRP SER          
SEQRES  13 A  163  LEU ILE THR ASN LYS LYS LYS                                  
SEQRES   1 B  163  MSE ALA PHE ASP THR TYR ILE LYS LEU ASP LYS VAL ASP          
SEQRES   2 B  163  GLY GLU SER THR ASP ASP LYS HIS LYS LYS TRP ILE GLU          
SEQRES   3 B  163  VAL LEU GLY PHE ALA TRP GLY ALA GLY ASN GLU CYS THR          
SEQRES   4 B  163  MSE GLU SER GLY THR GLN GLY LEU ASN THR GLY LYS ALA          
SEQRES   5 B  163  MSE MSE SER VAL LEU ARG VAL THR LYS TRP MSE ASP CYS          
SEQRES   6 B  163  ALA SER VAL LYS LEU ALA SER ALA ALA VAL GLN GLY GLN          
SEQRES   7 B  163  ASN PHE PRO THR LEU GLU LEU GLU ILE CYS THR GLN ALA          
SEQRES   8 B  163  GLY ASP LYS PHE ALA PHE CYS ILE TYR LYS PHE THR HIS          
SEQRES   9 B  163  VAL ALA VAL SER SER TYR GLN CYS SER GLY ALA THR GLY          
SEQRES  10 B  163  GLY SER ASP ARG PRO GLN GLU THR ILE ASP PHE ALA TYR          
SEQRES  11 B  163  LYS GLU VAL THR TRP GLU TYR VAL PRO GLN ASP GLN ASN          
SEQRES  12 B  163  GLY LYS ALA GLY GLY LYS ILE GLY PRO GLU GLY TRP SER          
SEQRES  13 B  163  LEU ILE THR ASN LYS LYS LYS                                  
MODRES 3EAA MSE A   40  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE A   53  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE A   54  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE A   63  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE B   40  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE B   53  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE B   54  MET  SELENOMETHIONINE                                   
MODRES 3EAA MSE B   63  MET  SELENOMETHIONINE                                   
HET    MSE  A  40       5                                                       
HET    MSE  A  53       8                                                       
HET    MSE  A  54       8                                                       
HET    MSE  A  63       8                                                       
HET    MSE  B  40       5                                                       
HET    MSE  B  53       8                                                       
HET    MSE  B  54       8                                                       
HET    MSE  B  63       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *38(H2 O)                                                     
HELIX    1   1 ASP A   18  LYS A   22  5                                   5    
HELIX    2   2 ALA A   66  GLY A   77  1                                  12    
HELIX    3   3 ASP B   18  LYS B   22  5                                   5    
HELIX    4   4 ALA B   66  GLY B   77  1                                  12    
SHEET    1   A 6 ILE A  25  VAL A  27  0                                        
SHEET    2   A 6 ASP A   4  LEU A   9 -1  N  THR A   5   O  VAL A  27           
SHEET    3   A 6 PHE A  80  CYS A  88 -1  O  GLU A  86   N  TYR A   6           
SHEET    4   A 6 ALA A  96  SER A 113 -1  O  PHE A 102   N  LEU A  83           
SHEET    5   A 6 GLN A 123  ALA A 129 -1  O  ALA A 129   N  ALA A 106           
SHEET    6   A 6 LEU A  57  TRP A  62 -1  N  VAL A  59   O  ILE A 126           
SHEET    1   B 7 ILE A  25  VAL A  27  0                                        
SHEET    2   B 7 ASP A   4  LEU A   9 -1  N  THR A   5   O  VAL A  27           
SHEET    3   B 7 PHE A  80  CYS A  88 -1  O  GLU A  86   N  TYR A   6           
SHEET    4   B 7 ALA A  96  SER A 113 -1  O  PHE A 102   N  LEU A  83           
SHEET    5   B 7 GLU A 132  THR A 134 -1  O  GLU A 132   N  THR A 103           
SHEET    6   B 7 GLY A 154  SER A 156 -1  O  TRP A 155   N  VAL A 133           
SHEET    7   B 7 LYS A 161  LYS A 162 -1  O  LYS A 161   N  SER A 156           
SHEET    1   C 2 ALA A  34  ASN A  36  0                                        
SHEET    2   C 2 ALA A  52  MSE A  54 -1  O  MSE A  53   N  GLY A  35           
SHEET    1   D 6 ILE B  25  VAL B  27  0                                        
SHEET    2   D 6 ASP B   4  LEU B   9 -1  N  THR B   5   O  VAL B  27           
SHEET    3   D 6 PHE B  80  CYS B  88 -1  O  GLU B  86   N  TYR B   6           
SHEET    4   D 6 ALA B  96  SER B 113 -1  O  PHE B 102   N  LEU B  83           
SHEET    5   D 6 GLN B 123  ALA B 129 -1  O  ALA B 129   N  ALA B 106           
SHEET    6   D 6 LEU B  57  TRP B  62 -1  N  VAL B  59   O  ILE B 126           
SHEET    1   E 7 ILE B  25  VAL B  27  0                                        
SHEET    2   E 7 ASP B   4  LEU B   9 -1  N  THR B   5   O  VAL B  27           
SHEET    3   E 7 PHE B  80  CYS B  88 -1  O  GLU B  86   N  TYR B   6           
SHEET    4   E 7 ALA B  96  SER B 113 -1  O  PHE B 102   N  LEU B  83           
SHEET    5   E 7 GLU B 132  THR B 134 -1  O  GLU B 132   N  THR B 103           
SHEET    6   E 7 GLY B 154  SER B 156 -1  O  TRP B 155   N  VAL B 133           
SHEET    7   E 7 LYS B 161  LYS B 162 -1  O  LYS B 161   N  SER B 156           
SHEET    1   F 2 ALA B  34  ASN B  36  0                                        
SHEET    2   F 2 ALA B  52  MSE B  54 -1  O  MSE B  53   N  GLY B  35           
LINK         C   THR A  39                 N   MSE A  40     1555   1555  1.33  
LINK         C   MSE A  40                 N   GLU A  41     1555   1555  1.34  
LINK         C   ALA A  52                 N   MSE A  53     1555   1555  1.30  
LINK         C   MSE A  53                 N   MSE A  54     1555   1555  1.32  
LINK         C   MSE A  54                 N   SER A  55     1555   1555  1.31  
LINK         C   TRP A  62                 N   MSE A  63     1555   1555  1.32  
LINK         C   MSE A  63                 N   ASP A  64     1555   1555  1.32  
LINK         C   THR B  39                 N   MSE B  40     1555   1555  1.33  
LINK         C   MSE B  40                 N   GLU B  41     1555   1555  1.34  
LINK         C   ALA B  52                 N   MSE B  53     1555   1555  1.30  
LINK         C   MSE B  53                 N   MSE B  54     1555   1555  1.32  
LINK         C   MSE B  54                 N   SER B  55     1555   1555  1.33  
LINK         C   TRP B  62                 N   MSE B  63     1555   1555  1.32  
LINK         C   MSE B  63                 N   ASP B  64     1555   1555  1.32  
CRYST1   85.459   85.459   93.066  90.00  90.00 120.00 P 6          12          
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      0.011702  0.006756  0.000000        0.00000                         
SCALE2      0.000000  0.013512  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010745        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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