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Database: PDB
Entry: 2PHZ
LinkDB: 2PHZ
Original site: 2PHZ 
HEADER    TRANSPORT PROTEIN                       12-APR-07   2PHZ              
TITLE     CRYSTAL STRUCTURE OF IRON-UPTAKE SYSTEM-BINDING PROTEIN FEUA FROM     
TITLE    2 BACILLUS SUBTILIS. NORTHEAST STRUCTURAL GENOMICS TARGET SR580.       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON-UPTAKE SYSTEM-BINDING PROTEIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: FEUA, BSU01630;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    SR580, IRON UPTAKE, NESG, STRUCTURAL GENOMICS, PSI-2, PROTEIN         
KEYWDS   2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,      
KEYWDS   3 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.BENACH,H.NEELY,J.SEETHARAMAN,C.X.CHEN,K.CUNNINGHAM,L.-C.MA,         
AUTHOR   2 H.JANJUA,R.XIAO,M.BARAN,T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,    
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)                      
REVDAT   5   24-JAN-18 2PHZ    1       AUTHOR JRNL                              
REVDAT   4   25-OCT-17 2PHZ    1       REMARK                                   
REVDAT   3   18-OCT-17 2PHZ    1       REMARK                                   
REVDAT   2   24-FEB-09 2PHZ    1       VERSN                                    
REVDAT   1   24-APR-07 2PHZ    0                                                
JRNL        AUTH   J.BENACH,H.NEELY,J.SEETHARAMAN,C.X.CHEN,K.CUNNINGHAM,        
JRNL        AUTH 2 L.-C.MA,H.JANJUA,R.XIAO,M.BARAN,T.B.ACTON,G.T.MONTELIONE,    
JRNL        AUTH 3 L.TONG,J.F.HUNT,                                             
JRNL        AUTH 4 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)              
JRNL        TITL   CRYSTAL STRUCTURE OF IRON-UPTAKE SYSTEM-BINDING PROTEIN FEUA 
JRNL        TITL 2 FROM BACILLUS SUBTILIS.                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26990                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2569                            
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           : 50                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 444                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2250                       
REMARK   3   BIN FREE R VALUE                    : 0.2210                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 51                           
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            : 2184                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 146                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.54800                                             
REMARK   3    B22 (A**2) : 2.22500                                              
REMARK   3    B33 (A**2) : -0.67700                                             
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) : 0.004                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.087                           
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) : 2.517 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.881 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.817 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.727 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 51.07                                                
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.PAR                                
REMARK   3  PARAMETER FILE  2  : 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: THE FRIEDEL PAIRS WERE USED FOR PHASING   
REMARK   4                                                                      
REMARK   4 2PHZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042394.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950, 0.97900, 0.95000          
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35899                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.100                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.8000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: RESOLVE 2.08, SNB                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: THE STRUCTURE FACTOR FILE CONTAINS FRIEDEL PAIRS             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITER PROTEIN SOLUTION PLUS 1     
REMARK 280  MICROLITER RESERVOIR SOLUTION, 50MM MGNO3, 50MM MES PH 6.5, 27.5%   
REMARK 280  PEG400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.77550            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       27.73050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       27.73050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.38775            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       27.73050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       27.73050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      133.16325            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       27.73050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       27.73050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       44.38775            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       27.73050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       27.73050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      133.16325            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       88.77550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). AUTHORS STATE THAT STATIC              
REMARK 300 LIGHT SCATTERING SHOWS THAT THE PROTEIN IS A MONOMER IN              
REMARK 300 SOLUTION. SEE REMARK 350 FOR INFORMATION ON GENERATING               
REMARK 300 THE BIOLOGICAL MOLECULE(S).                                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MSE A    -4                                                      
REMARK 465     ALA A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     SER A     7                                                      
REMARK 465     THR A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     LYS A    19                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     ASN A   298                                                      
REMARK 465     LEU A   299                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     HIS A   301                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     HIS A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
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   CG   MSE A   134     O    HOH A  3164              1.92            
REMARK 500   OE2  GLU A   189     O    HOH A  3141              1.99            
REMARK 500   NE2  GLN A   112     O    HOH A  3167              2.01            
REMARK 500   CE   MSE A   134     O    HOH A  3164              2.09            
REMARK 500   O    ILE A   165     O    HOH A  3134              2.12            
REMARK 500   O    HOH A  3057     O    HOH A  3139              2.13            
REMARK 500   O    HOH A  3137     O    HOH A  3138              2.16            
REMARK 500   CE   MSE A    47     O    HOH A  3145              2.17            
REMARK 500   N    GLY A   279     O    HOH A  3131              2.19            
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    HOH A  3148     O    HOH A  3149     6465     1.68            
REMARK 500   OD2  ASP A   237     O    HOH A  3133     7556     1.81            
REMARK 500   NZ   LYS A   248     O    HOH A  3162     7556     1.81            
REMARK 500   O    HOH A  3141     O    HOH A  3142     6455     1.84            
REMARK 500   O    HOH A  3135     O    HOH A  3136     7556     1.86            
REMARK 500   OD1  ASP A    54     O    HOH A  3136     7556     1.90            
REMARK 500   CG2  ILE A    74     O    HOH A  3150     7556     1.92            
REMARK 500   CB   GLU A   221     O    HOH A  3132     6465     1.93            
REMARK 500   O    HOH A  3019     O    HOH A  3155     6565     1.98            
REMARK 500   O    HOH A  3133     O    HOH A  3160     7556     1.99            
REMARK 500   O    HOH A  3107     O    HOH A  3146     7556     2.03            
REMARK 500   CE   LYS A   248     O    HOH A  3162     7556     2.07            
REMARK 500   NZ   LYS A   168     O    HOH A  3149     6465     2.12            
REMARK 500   O    HOH A  3101     O    HOH A  3135     7556     2.16            
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    ALA A 102     -158.08    -96.39                                   
REMARK 500    TYR A 192     -143.76     55.28                                   
REMARK 500    ASP A 242       40.70    -94.76                                   
REMARK 500    LYS A 243       45.52    176.85                                   
REMARK 500    ASP A 273      127.72    -38.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: SR580   RELATED DB: TARGETDB                             
DBREF  2PHZ A    2   298  UNP    P40409   FEUA_BACSU      21    317             
SEQADV 2PHZ MSE A   -4  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ ALA A   -3  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ GLY A   -2  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ ASP A   -1  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ PRO A    0  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ MSE A    1  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ MSE A   47  UNP  P40409    MET    66 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A   70  UNP  P40409    MET    89 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A   85  UNP  P40409    MET   104 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A   95  UNP  P40409    MET   114 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A  134  UNP  P40409    MET   153 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A  135  UNP  P40409    MET   154 MODIFIED RESIDUE               
SEQADV 2PHZ MSE A  226  UNP  P40409    MET   245 MODIFIED RESIDUE               
SEQADV 2PHZ LEU A  299  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ GLU A  300  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  301  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  302  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  303  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  304  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  305  UNP  P40409              CLONING ARTIFACT               
SEQADV 2PHZ HIS A  306  UNP  P40409              CLONING ARTIFACT               
SEQRES   1 A  311  MSE ALA GLY ASP PRO MSE GLY SER LYS ASN GLU SER THR          
SEQRES   2 A  311  ALA SER LYS ALA SER GLY THR ALA SER GLU LYS LYS LYS          
SEQRES   3 A  311  ILE GLU TYR LEU ASP LYS THR TYR GLU VAL THR VAL PRO          
SEQRES   4 A  311  THR ASP LYS ILE ALA ILE THR GLY SER VAL GLU SER MSE          
SEQRES   5 A  311  GLU ASP ALA LYS LEU LEU ASP VAL HIS PRO GLN GLY ALA          
SEQRES   6 A  311  ILE SER PHE SER GLY LYS PHE PRO ASP MSE PHE LYS ASP          
SEQRES   7 A  311  ILE THR ASP LYS ALA GLU PRO THR GLY GLU LYS MSE GLU          
SEQRES   8 A  311  PRO ASN ILE GLU LYS ILE LEU GLU MSE LYS PRO ASP VAL          
SEQRES   9 A  311  ILE LEU ALA SER THR LYS PHE PRO GLU LYS THR LEU GLN          
SEQRES  10 A  311  LYS ILE SER THR ALA GLY THR THR ILE PRO VAL SER HIS          
SEQRES  11 A  311  ILE SER SER ASN TRP LYS GLU ASN MSE MSE LEU LEU ALA          
SEQRES  12 A  311  GLN LEU THR GLY LYS GLU LYS LYS ALA LYS LYS ILE ILE          
SEQRES  13 A  311  ALA ASP TYR GLU GLN ASP LEU LYS GLU ILE LYS THR LYS          
SEQRES  14 A  311  ILE ASN ASP LYS ALA LYS ASP SER LYS ALA LEU VAL ILE          
SEQRES  15 A  311  ARG ILE ARG GLN GLY ASN ILE TYR ILE TYR PRO GLU GLN          
SEQRES  16 A  311  VAL TYR PHE ASN SER THR LEU TYR GLY ASP LEU GLY LEU          
SEQRES  17 A  311  LYS ALA PRO ASN GLU VAL LYS ALA ALA LYS ALA GLN GLU          
SEQRES  18 A  311  LEU SER SER LEU GLU LYS LEU SER GLU MSE ASN PRO ASP          
SEQRES  19 A  311  HIS ILE PHE VAL GLN PHE SER ASP ASP GLU ASN ALA ASP          
SEQRES  20 A  311  LYS PRO ASP ALA LEU LYS ASP LEU GLU LYS ASN PRO ILE          
SEQRES  21 A  311  TRP LYS SER LEU LYS ALA VAL LYS GLU ASP HIS VAL TYR          
SEQRES  22 A  311  VAL ASN SER VAL ASP PRO LEU ALA GLN GLY GLY THR ALA          
SEQRES  23 A  311  TRP SER LYS VAL ARG PHE LEU LYS ALA ALA ALA GLU LYS          
SEQRES  24 A  311  LEU THR GLN ASN LEU GLU HIS HIS HIS HIS HIS HIS              
MODRES 2PHZ MSE A   47  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A   70  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A   85  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A   95  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A  134  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A  135  MET  SELENOMETHIONINE                                   
MODRES 2PHZ MSE A  226  MET  SELENOMETHIONINE                                   
HET    MSE  A  47       8                                                       
HET    MSE  A  70       8                                                       
HET    MSE  A  85       8                                                       
HET    MSE  A  95       8                                                       
HET    MSE  A 134       8                                                       
HET    MSE  A 135       8                                                       
HET    MSE  A 226       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    7(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *146(H2 O)                                                    
HELIX    1   1 SER A   43  ASP A   54  1                                  12    
HELIX    2   2 PRO A   68  LYS A   72  5                                   5    
HELIX    3   3 ASN A   88  LYS A   96  1                                   9    
HELIX    4   4 PRO A  107  THR A  116  1                                  10    
HELIX    5   5 ILE A  126  SER A  128  5                                   3    
HELIX    6   6 ASN A  129  GLY A  142  1                                  14    
HELIX    7   7 LYS A  143  ILE A  165  1                                  23    
HELIX    8   8 ASN A  166  ASP A  171  1                                   6    
HELIX    9   9 PHE A  193  TYR A  198  1                                   6    
HELIX   10  10 PRO A  206  ALA A  212  1                                   7    
HELIX   11  11 SER A  219  ASN A  227  1                                   9    
HELIX   12  12 ASP A  237  ASN A  240  5                                   4    
HELIX   13  13 ASP A  245  ASN A  253  1                                   9    
HELIX   14  14 ASN A  253  LEU A  259  1                                   7    
HELIX   15  15 LEU A  259  GLU A  264  1                                   6    
HELIX   16  16 THR A  280  THR A  296  1                                  17    
SHEET    1   A 2 LYS A  21  TYR A  24  0                                        
SHEET    2   A 2 LYS A  27  GLU A  30 -1  O  TYR A  29   N  ILE A  22           
SHEET    1   B 3 ILE A  38  ILE A  40  0                                        
SHEET    2   B 3 VAL A  99  SER A 103  1  O  LEU A 101   N  ALA A  39           
SHEET    3   B 3 THR A 120  VAL A 123  1  O  ILE A 121   N  ILE A 100           
SHEET    1   C 3 GLY A  59  SER A  62  0                                        
SHEET    2   C 3 GLU A  79  GLU A  83  1  O  GLU A  79   N  ALA A  60           
SHEET    3   C 3 GLU A  86  PRO A  87 -1  O  GLU A  86   N  GLU A  83           
SHEET    1   D 5 GLU A 216  LEU A 217  0                                        
SHEET    2   D 5 ASN A 183  ILE A 186 -1  N  ILE A 186   O  GLU A 216           
SHEET    3   D 5 ALA A 174  ARG A 180 -1  N  ARG A 180   O  ASN A 183           
SHEET    4   D 5 HIS A 230  PHE A 235  1  O  PHE A 232   N  LEU A 175           
SHEET    5   D 5 VAL A 267  VAL A 269  1  O  TYR A 268   N  VAL A 233           
LINK         C   SER A  46                 N   MSE A  47     1555   1555  1.33  
LINK         C   MSE A  47                 N   GLU A  48     1555   1555  1.33  
LINK         C   ASP A  69                 N   MSE A  70     1555   1555  1.33  
LINK         C   MSE A  70                 N   PHE A  71     1555   1555  1.33  
LINK         C   LYS A  84                 N   MSE A  85     1555   1555  1.33  
LINK         C   MSE A  85                 N   GLU A  86     1555   1555  1.33  
LINK         C   GLU A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   LYS A  96     1555   1555  1.33  
LINK         C   ASN A 133                 N   MSE A 134     1555   1555  1.33  
LINK         C   MSE A 134                 N   MSE A 135     1555   1555  1.33  
LINK         C   MSE A 135                 N   LEU A 136     1555   1555  1.33  
LINK         C   GLU A 225                 N   MSE A 226     1555   1555  1.33  
LINK         C   MSE A 226                 N   ASN A 227     1555   1555  1.33  
CISPEP   1 VAL A   33    PRO A   34          0        -0.13                     
CRYST1   55.461   55.461  177.551  90.00  90.00  90.00 P 41 21 2     8          
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      0.018031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005632        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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