GenomeNet

Database: PDB
Entry: 2F2A
LinkDB: 2F2A
Original site: 2F2A 
HEADER    LIGASE                                  15-NOV-05   2F2A              
TITLE     STRUCTURE OF TRNA-DEPENDENT AMIDOTRANSFERASE GATCAB                   
TITLE    2 COMPLEXED WITH GLN                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GLU/ASP-TRNA(GLN/ASN) AMIDOTRANSFERASE A SUBUNIT,           
COMPND   5 GLU-ADT SUBUNIT A;                                                   
COMPND   6 EC: 6.3.5.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ASPARTYL/GLUTAMYL-TRNA(ASN/GLN) AMIDOTRANSFERASE           
COMPND  10 SUBUNIT B;                                                           
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: GLU/ASP-TRNA(GLN/ASN) AMIDOTRANSFERASE B SUBUNIT,           
COMPND  13 ASP/GLU-ADT SUBUNIT B;                                               
COMPND  14 EC: 6.3.5.-;                                                         
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: ASPARTYL/GLUTAMYL-TRNA(ASN/GLN) AMIDOTRANSFERASE           
COMPND  18 SUBUNIT C;                                                           
COMPND  19 CHAIN: C;                                                            
COMPND  20 SYNONYM: GLU/ASP-TRNA(GLN/ASN) AMIDOTRANSFERASE C SUBUNIT,           
COMPND  21 ASP/GLU-ADT SUBUNIT C;                                               
COMPND  22 EC: 6.3.5.-;                                                         
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 STRAIN: MU50;                                                        
SOURCE   5 GENE: SAV1900;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  13 ORGANISM_TAXID: 1280;                                                
SOURCE  14 STRAIN: MU50;                                                        
SOURCE  15 GENE: SAV1899;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28B;                                   
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  23 ORGANISM_TAXID: 1280;                                                
SOURCE  24 STRAIN: MU50;                                                        
SOURCE  25 GENE: SAV1901;                                                       
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    TRNA, AMIDOTRANSFERASE, LIGASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.NAKAMURA,M.YAO,I.TANAKA                                             
REVDAT   2   24-FEB-09 2F2A    1       VERSN                                    
REVDAT   1   18-JUL-06 2F2A    0                                                
JRNL        AUTH   A.NAKAMURA,M.YAO,S.CHIMNARONK,N.SAKAI,I.TANAKA               
JRNL        TITL   AMMONIA CHANNEL COUPLES GLUTAMINASE WITH                     
JRNL        TITL 2 TRANSAMIDASE REACTIONS IN GATCAB                             
JRNL        REF    SCIENCE                       V. 312  1954 2006              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   16809541                                                     
JRNL        DOI    10.1126/SCIENCE.1127156                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2715052.780                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 56332                          
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) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5525                            
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8353                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2510                       
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 897                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7697                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 393                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.32000                                              
REMARK   3    B22 (A**2) : 6.20000                                              
REMARK   3    B33 (A**2) : -11.52000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.28                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.89                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.310 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.150 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.940 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.820 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.32                                                 
REMARK   3   BSOL        : 40.28                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2F2A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035363.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56446                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : 0.06700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.028                              
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: 2G5H                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG MME 550, 0.005M MAGNESIUM        
REMARK 280  CHLORIDE, 0.05M HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
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       38.59350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       91.70050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.11100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       91.70050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.59350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.11100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     PHE B     3                                                      
REMARK 465     ILE B   412                                                      
REMARK 465     SER B   413                                                      
REMARK 465     ASP B   414                                                      
REMARK 465     GLU B   415                                                      
REMARK 465     ALA B   416                                                      
REMARK 465     THR B   417                                                      
REMARK 465     LEU B   418                                                      
REMARK 465     LEU B   419                                                      
REMARK 465     LYS B   420                                                      
REMARK 465     PHE B   421                                                      
REMARK 465     VAL B   422                                                      
REMARK 465     ASN B   423                                                      
REMARK 465     GLU B   424                                                      
REMARK 465     ALA B   425                                                      
REMARK 465     LEU B   426                                                      
REMARK 465     ASP B   427                                                      
REMARK 465     ASN B   428                                                      
REMARK 465     ASN B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     GLN B   431                                                      
REMARK 465     SER B   432                                                      
REMARK 465     VAL B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     ASP B   435                                                      
REMARK 465     TYR B   436                                                      
REMARK 465     LYS B   437                                                      
REMARK 465     ASN B   438                                                      
REMARK 465     GLY B   439                                                      
REMARK 465     LYS B   440                                                      
REMARK 465     GLY B   441                                                      
REMARK 465     LYS B   442                                                      
REMARK 465     ALA B   443                                                      
REMARK 465     MET B   444                                                      
REMARK 465     GLY B   445                                                      
REMARK 465     PHE B   446                                                      
REMARK 465     LEU B   447                                                      
REMARK 465     VAL B   448                                                      
REMARK 465     GLY B   449                                                      
REMARK 465     GLN B   450                                                      
REMARK 465     ILE B   451                                                      
REMARK 465     MET B   452                                                      
REMARK 465     LYS B   453                                                      
REMARK 465     ALA B   454                                                      
REMARK 465     SER B   455                                                      
REMARK 465     LYS B   456                                                      
REMARK 465     GLY B   457                                                      
REMARK 465     GLN B   458                                                      
REMARK 465     ALA B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     PRO B   461                                                      
REMARK 465     GLN B   462                                                      
REMARK 465     LEU B   463                                                      
REMARK 465     VAL B   464                                                      
REMARK 465     ASN B   465                                                      
REMARK 465     GLN B   466                                                      
REMARK 465     LEU B   467                                                      
REMARK 465     LEU B   468                                                      
REMARK 465     LYS B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     LEU B   472                                                      
REMARK 465     ASP B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     ARG B   475                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     GLU B   477                                                      
REMARK 465     HIS B   478                                                      
REMARK 465     HIS B   479                                                      
REMARK 465     HIS B   480                                                      
REMARK 465     HIS B   481                                                      
REMARK 465     HIS B   482                                                      
REMARK 465     HIS B   483                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     MET C    95                                                      
REMARK 465     ASN C    96                                                      
REMARK 465     GLU C    97                                                      
REMARK 465     GLU C    98                                                      
REMARK 465     ASP C    99                                                      
REMARK 465     ALA C   100                                                      
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    LEU A 169   CA  -  CB  -  CG  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    VAL B 410   N   -  CA  -  C   ANGL. DEV. =  16.6 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    PRO A  22      -39.63    -39.14                                   
REMARK 500    LEU A  44     -116.53   -110.39                                   
REMARK 500    ASP A  80       28.16    -68.22                                   
REMARK 500    GLU A  88      123.07    -39.81                                   
REMARK 500    SER A 132       -4.20   -149.68                                   
REMARK 500    THR A 133       -4.92     71.19                                   
REMARK 500    ASP A 146      103.20   -168.95                                   
REMARK 500    HIS A 147       -7.89    -56.11                                   
REMARK 500    SER A 155       45.52    -87.34                                   
REMARK 500    SER A 178        1.27    -68.43                                   
REMARK 500    PHE A 206      -81.72   -108.14                                   
REMARK 500    GLU A 335       27.07    -68.13                                   
REMARK 500    TYR A 374      -73.13   -107.49                                   
REMARK 500    THR B   5       81.11     68.79                                   
REMARK 500    LYS B  16       38.61    -77.33                                   
REMARK 500    TYR B  81      136.59   -177.34                                   
REMARK 500    TYR B  83      135.36    179.75                                   
REMARK 500    SER B  93     -155.99   -143.30                                   
REMARK 500    PHE B  95      -79.22   -104.86                                   
REMARK 500    HIS B 132       98.94    -62.14                                   
REMARK 500    VAL B 182       52.35     39.79                                   
REMARK 500    SER B 188        5.06    -66.50                                   
REMARK 500    ARG B 198      135.36    173.37                                   
REMARK 500    THR B 207     -147.87     54.48                                   
REMARK 500    ALA B 209       50.08   -152.24                                   
REMARK 500    GLU B 210       94.52    -46.97                                   
REMARK 500    PHE B 217      -88.68    -41.26                                   
REMARK 500    TYR B 219     -152.15    -67.13                                   
REMARK 500    VAL B 220      -73.83    -31.54                                   
REMARK 500    ASN B 237       45.66    -88.49                                   
REMARK 500    GLU B 240      163.03    -31.68                                   
REMARK 500    ILE B 241       22.83    -66.62                                   
REMARK 500    GLN B 243      175.80     68.70                                   
REMARK 500    GLU B 244      -60.46   -147.71                                   
REMARK 500    GLU B 250      -89.52    -59.72                                   
REMARK 500    LYS B 254      159.05    176.41                                   
REMARK 500    LEU B 257       65.45    -59.51                                   
REMARK 500    MET B 258      -59.56    -27.31                                   
REMARK 500    LYS B 261      143.15    -27.81                                   
REMARK 500    SER B 264      106.23    170.45                                   
REMARK 500    ASN B 355      -12.78   -177.94                                   
REMARK 500    THR B 362     -166.93    -66.82                                   
REMARK 500    GLU B 377        6.54    -67.95                                   
REMARK 500    THR B 380        3.88    -62.32                                   
REMARK 500    GLN B 402      -15.05   -157.89                                   
REMARK 500    MET B 404        6.90    -68.27                                   
REMARK 500    LEU B 409       66.50   -113.14                                   
REMARK 500    VAL C   4       94.16     69.71                                   
REMARK 500    PRO C  22       52.64    -64.79                                   
REMARK 500    GLU C  23      -42.40   -165.81                                   
REMARK 500    LYS C  40        5.98    -62.62                                   
REMARK 500    ASN C  61       73.19     34.82                                   
REMARK 500    ASP C  66       68.33    -69.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLN A 501         0.17    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 637   O                                                      
REMARK 620 2 HOH B 638   O    94.3                                              
REMARK 620 3 HOH B 636   O    85.1  98.5                                        
REMARK 620 4 HIS B  12   NE2  97.9  90.6 170.1                                  
REMARK 620 5 GLU B 124   OE2 172.1  88.1  87.0  89.6                            
REMARK 620 6 GLU B 150   OE1  83.8 177.9  82.3  88.6  93.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLN A 501                 
DBREF  2F2A A    1   485  UNP    P63488   GATA_STAAM       1    485             
DBREF  2F2A B    1   475  UNP    P64201   GATB_STAAM       1    475             
DBREF  2F2A C    1   100  UNP    P68807   GATC_STAAM       1    100             
SEQADV 2F2A LEU B  476  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A GLU B  477  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  478  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  479  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  480  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  481  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  482  UNP  P64201              EXPRESSION TAG                 
SEQADV 2F2A HIS B  483  UNP  P64201              EXPRESSION TAG                 
SEQRES   1 A  485  MET SER ILE ARG TYR GLU SER VAL GLU ASN LEU LEU THR          
SEQRES   2 A  485  LEU ILE LYS ASP LYS LYS ILE LYS PRO SER ASP VAL VAL          
SEQRES   3 A  485  LYS ASP ILE TYR ASP ALA ILE GLU GLU THR ASP PRO THR          
SEQRES   4 A  485  ILE LYS SER PHE LEU ALA LEU ASP LYS GLU ASN ALA ILE          
SEQRES   5 A  485  LYS LYS ALA GLN GLU LEU ASP GLU LEU GLN ALA LYS ASP          
SEQRES   6 A  485  GLN MET ASP GLY LYS LEU PHE GLY ILE PRO MET GLY ILE          
SEQRES   7 A  485  LYS ASP ASN ILE ILE THR ASN GLY LEU GLU THR THR CYS          
SEQRES   8 A  485  ALA SER LYS MET LEU GLU GLY PHE VAL PRO ILE TYR GLU          
SEQRES   9 A  485  SER THR VAL MET GLU LYS LEU HIS LYS GLU ASN ALA VAL          
SEQRES  10 A  485  LEU ILE GLY LYS LEU ASN MET ASP GLU PHE ALA MET GLY          
SEQRES  11 A  485  GLY SER THR GLU THR SER TYR PHE LYS LYS THR VAL ASN          
SEQRES  12 A  485  PRO PHE ASP HIS LYS ALA VAL PRO GLY GLY SER SER GLY          
SEQRES  13 A  485  GLY SER ALA ALA ALA VAL ALA ALA GLY LEU VAL PRO LEU          
SEQRES  14 A  485  SER LEU GLY SER ASP THR GLY GLY SER ILE ARG GLN PRO          
SEQRES  15 A  485  ALA ALA TYR CYS GLY VAL VAL GLY MET LYS PRO THR TYR          
SEQRES  16 A  485  GLY ARG VAL SER ARG PHE GLY LEU VAL ALA PHE ALA SER          
SEQRES  17 A  485  SER LEU ASP GLN ILE GLY PRO LEU THR ARG ASN VAL LYS          
SEQRES  18 A  485  ASP ASN ALA ILE VAL LEU GLU ALA ILE SER GLY ALA ASP          
SEQRES  19 A  485  VAL ASN ASP SER THR SER ALA PRO VAL ASP ASP VAL ASP          
SEQRES  20 A  485  PHE THR SER GLU ILE GLY LYS ASP ILE LYS GLY LEU LYS          
SEQRES  21 A  485  VAL ALA LEU PRO LYS GLU TYR LEU GLY GLU GLY VAL ALA          
SEQRES  22 A  485  ASP ASP VAL LYS GLU ALA VAL GLN ASN ALA VAL GLU THR          
SEQRES  23 A  485  LEU LYS SER LEU GLY ALA VAL VAL GLU GLU VAL SER LEU          
SEQRES  24 A  485  PRO ASN THR LYS PHE GLY ILE PRO SER TYR TYR VAL ILE          
SEQRES  25 A  485  ALA SER SER GLU ALA SER SER ASN LEU SER ARG PHE ASP          
SEQRES  26 A  485  GLY ILE ARG TYR GLY TYR HIS SER LYS GLU ALA HIS SER          
SEQRES  27 A  485  LEU GLU GLU LEU TYR LYS MET SER ARG SER GLU GLY PHE          
SEQRES  28 A  485  GLY LYS GLU VAL LYS ARG ARG ILE PHE LEU GLY THR PHE          
SEQRES  29 A  485  ALA LEU SER SER GLY TYR TYR ASP ALA TYR TYR LYS LYS          
SEQRES  30 A  485  SER GLN LYS VAL ARG THR LEU ILE LYS ASN ASP PHE ASP          
SEQRES  31 A  485  LYS VAL PHE GLU ASN TYR ASP VAL VAL VAL GLY PRO THR          
SEQRES  32 A  485  ALA PRO THR THR ALA PHE ASN LEU GLY GLU GLU ILE ASP          
SEQRES  33 A  485  ASP PRO LEU THR MET TYR ALA ASN ASP LEU LEU THR THR          
SEQRES  34 A  485  PRO VAL ASN LEU ALA GLY LEU PRO GLY ILE SER VAL PRO          
SEQRES  35 A  485  CYS GLY GLN SER ASN GLY ARG PRO ILE GLY LEU GLN PHE          
SEQRES  36 A  485  ILE GLY LYS PRO PHE ASP GLU LYS THR LEU TYR ARG VAL          
SEQRES  37 A  485  ALA TYR GLN TYR GLU THR GLN TYR ASN LEU HIS ASP VAL          
SEQRES  38 A  485  TYR GLU LYS LEU                                              
SEQRES   1 B  483  MET HIS PHE GLU THR VAL ILE GLY LEU GLU VAL HIS VAL          
SEQRES   2 B  483  GLU LEU LYS THR ASP SER LYS MET PHE SER PRO SER PRO          
SEQRES   3 B  483  ALA HIS PHE GLY ALA GLU PRO ASN SER ASN THR ASN VAL          
SEQRES   4 B  483  ILE ASP LEU ALA TYR PRO GLY VAL LEU PRO VAL VAL ASN          
SEQRES   5 B  483  LYS ARG ALA VAL ASP TRP ALA MET ARG ALA ALA MET ALA          
SEQRES   6 B  483  LEU ASN MET GLU ILE ALA THR GLU SER LYS PHE ASP ARG          
SEQRES   7 B  483  LYS ASN TYR PHE TYR PRO ASP ASN PRO LYS ALA TYR GLN          
SEQRES   8 B  483  ILE SER GLN PHE ASP GLN PRO ILE GLY GLU ASN GLY TYR          
SEQRES   9 B  483  ILE ASP ILE GLU VAL ASP GLY GLU THR LYS ARG ILE GLY          
SEQRES  10 B  483  ILE THR ARG LEU HIS MET GLU GLU ASP ALA GLY LYS SER          
SEQRES  11 B  483  THR HIS LYS GLY GLU TYR SER LEU VAL ASP LEU ASN ARG          
SEQRES  12 B  483  GLN GLY THR PRO LEU ILE GLU ILE VAL SER GLU PRO ASP          
SEQRES  13 B  483  ILE ARG SER PRO LYS GLU ALA TYR ALA TYR LEU GLU LYS          
SEQRES  14 B  483  LEU ARG SER ILE ILE GLN TYR THR GLY VAL SER ASP VAL          
SEQRES  15 B  483  LYS MET GLU GLU GLY SER LEU ARG CYS ASP ALA ASN ILE          
SEQRES  16 B  483  SER LEU ARG PRO TYR GLY GLN GLU LYS PHE GLY THR LYS          
SEQRES  17 B  483  ALA GLU LEU LYS ASN LEU ASN SER PHE ASN TYR VAL ARG          
SEQRES  18 B  483  LYS GLY LEU GLU TYR GLU GLU LYS ARG GLN GLU GLU GLU          
SEQRES  19 B  483  LEU LEU ASN GLY GLY GLU ILE GLY GLN GLU THR ARG ARG          
SEQRES  20 B  483  PHE ASP GLU SER THR GLY LYS THR ILE LEU MET ARG VAL          
SEQRES  21 B  483  LYS GLU GLY SER ASP ASP TYR ARG TYR PHE PRO GLU PRO          
SEQRES  22 B  483  ASP ILE VAL PRO LEU TYR ILE ASP ASP ALA TRP LYS GLU          
SEQRES  23 B  483  ARG VAL ARG GLN THR ILE PRO GLU LEU PRO ASP GLU ARG          
SEQRES  24 B  483  LYS ALA LYS TYR VAL ASN GLU LEU GLY LEU PRO ALA TYR          
SEQRES  25 B  483  ASP ALA HIS VAL LEU THR LEU THR LYS GLU MET SER ASP          
SEQRES  26 B  483  PHE PHE GLU SER THR ILE GLU HIS GLY ALA ASP VAL LYS          
SEQRES  27 B  483  LEU THR SER ASN TRP LEU MET GLY GLY VAL ASN GLU TYR          
SEQRES  28 B  483  LEU ASN LYS ASN GLN VAL GLU LEU LEU ASP THR LYS LEU          
SEQRES  29 B  483  THR PRO GLU ASN LEU ALA GLY MET ILE LYS LEU ILE GLU          
SEQRES  30 B  483  ASP GLY THR MET SER SER LYS ILE ALA LYS LYS VAL PHE          
SEQRES  31 B  483  PRO GLU LEU ALA ALA LYS GLY GLY ASN ALA LYS GLN ILE          
SEQRES  32 B  483  MET GLU ASP ASN GLY LEU VAL GLN ILE SER ASP GLU ALA          
SEQRES  33 B  483  THR LEU LEU LYS PHE VAL ASN GLU ALA LEU ASP ASN ASN          
SEQRES  34 B  483  GLU GLN SER VAL GLU ASP TYR LYS ASN GLY LYS GLY LYS          
SEQRES  35 B  483  ALA MET GLY PHE LEU VAL GLY GLN ILE MET LYS ALA SER          
SEQRES  36 B  483  LYS GLY GLN ALA ASN PRO GLN LEU VAL ASN GLN LEU LEU          
SEQRES  37 B  483  LYS GLN GLU LEU ASP LYS ARG LEU GLU HIS HIS HIS HIS          
SEQRES  38 B  483  HIS HIS                                                      
SEQRES   1 C  100  MET THR LYS VAL THR ARG GLU GLU VAL GLU HIS ILE ALA          
SEQRES   2 C  100  ASN LEU ALA ARG LEU GLN ILE SER PRO GLU GLU THR GLU          
SEQRES   3 C  100  GLU MET ALA ASN THR LEU GLU SER ILE LEU ASP PHE ALA          
SEQRES   4 C  100  LYS GLN ASN ASP SER ALA ASP THR GLU GLY VAL GLU PRO          
SEQRES   5 C  100  THR TYR HIS VAL LEU ASP LEU GLN ASN VAL LEU ARG GLU          
SEQRES   6 C  100  ASP LYS ALA ILE LYS GLY ILE PRO GLN GLU LEU ALA LEU          
SEQRES   7 C  100  LYS ASN ALA LYS GLU THR GLU ASP GLY GLN PHE LYS VAL          
SEQRES   8 C  100  PRO THR ILE MET ASN GLU GLU ASP ALA                          
HET     MG  B 601       1                                                       
HET    GLN  A 501      10                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GLN GLUTAMINE                                                        
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GLN    C5 H10 N2 O3                                                 
FORMUL   6  HOH   *393(H2 O)                                                    
HELIX    1   1 SER A    7  ASP A   17  1                                  11    
HELIX    2   2 LYS A   21  LYS A   41  1                                  21    
HELIX    3   3 ASP A   47  LYS A   64  1                                  18    
HELIX    4   4 SER A   93  GLU A   97  5                                   5    
HELIX    5   5 SER A  105  GLU A  114  1                                  10    
HELIX    6   6 ASP A  125  MET A  129  5                                   5    
HELIX    7   7 SER A  155  ALA A  164  1                                  10    
HELIX    8   8 ILE A  179  CYS A  186  1                                   8    
HELIX    9   9 ASN A  219  SER A  231  1                                  13    
HELIX   10  10 GLU A  266  GLY A  269  5                                   4    
HELIX   11  11 ALA A  273  LEU A  290  1                                  18    
HELIX   12  12 ASN A  301  LYS A  303  5                                   3    
HELIX   13  13 PHE A  304  LEU A  321  1                                  18    
HELIX   14  14 SER A  338  PHE A  351  1                                  14    
HELIX   15  15 GLY A  352  SER A  367  1                                  16    
HELIX   16  16 TYR A  374  PHE A  393  1                                  20    
HELIX   17  17 ASP A  417  ALA A  423  1                                   7    
HELIX   18  18 ASN A  424  LEU A  426  5                                   3    
HELIX   19  19 THR A  428  GLY A  435  1                                   8    
HELIX   20  20 ASP A  461  TYR A  476  1                                  16    
HELIX   21  21 VAL A  481  LEU A  485  5                                   5    
HELIX   22  22 ASN B   52  LEU B   66  1                                  15    
HELIX   23  23 SER B  159  GLY B  178  1                                  20    
HELIX   24  24 LYS B  183  GLY B  187  5                                   5    
HELIX   25  25 VAL B  220  LEU B  235  1                                  16    
HELIX   26  26 ASP B  281  GLN B  290  1                                  10    
HELIX   27  27 LEU B  295  GLU B  306  1                                  12    
HELIX   28  28 PRO B  310  THR B  318  1                                   9    
HELIX   29  29 THR B  320  GLU B  332  1                                  13    
HELIX   30  30 ASP B  336  GLY B  346  1                                  11    
HELIX   31  31 GLY B  346  LYS B  354  1                                   9    
HELIX   32  32 THR B  365  GLU B  377  1                                  13    
HELIX   33  33 SER B  382  LYS B  396  1                                  15    
HELIX   34  34 GLN B  402  ASN B  407  1                                   6    
HELIX   35  35 THR C    5  ALA C   16  1                                  12    
HELIX   36  36 GLU C   23  LYS C   40  1                                  18    
HELIX   37  37 GLN C   41  ALA C   45  5                                   5    
HELIX   38  38 PRO C   73  LYS C   79  1                                   7    
SHEET    1   A11 PHE A  43  LEU A  46  0                                        
SHEET    2   A11 VAL A 117  LEU A 122 -1  O  LYS A 121   N  LEU A  44           
SHEET    3   A11 PRO A  75  LYS A  79  1  N  ILE A  78   O  LEU A 122           
SHEET    4   A11 SER A 170  SER A 173  1  O  LEU A 171   N  GLY A  77           
SHEET    5   A11 ILE A 213  THR A 217 -1  O  GLY A 214   N  GLY A 172           
SHEET    6   A11 VAL A 189  LYS A 192 -1  N  VAL A 189   O  THR A 217           
SHEET    7   A11 GLY A 438  SER A 446 -1  O  GLY A 438   N  LYS A 192           
SHEET    8   A11 ARG A 449  ILE A 456 -1  O  LEU A 453   N  VAL A 441           
SHEET    9   A11 VAL A 398  PRO A 402 -1  N  GLY A 401   O  GLN A 454           
SHEET   10   A11 LYS A 260  PRO A 264  1  N  ALA A 262   O  VAL A 398           
SHEET   11   A11 VAL A 293  VAL A 297  1  O  GLU A 295   N  LEU A 263           
SHEET    1   B 6 GLU B  69  ILE B  70  0                                        
SHEET    2   B 6 GLY B 100  VAL B 109 -1  O  GLU B 101   N  GLU B  69           
SHEET    3   B 6 GLU B 112  GLU B 125 -1  O  GLU B 112   N  VAL B 109           
SHEET    4   B 6 PRO B 147  SER B 153 -1  O  LEU B 148   N  GLU B 124           
SHEET    5   B 6 VAL B   6  GLU B  14 -1  N  VAL B  11   O  ILE B 151           
SHEET    6   B 6 LEU B 189  SER B 196 -1  O  ASP B 192   N  GLU B  10           
SHEET    1   C 2 GLU B  73  SER B  74  0                                        
SHEET    2   C 2 LEU B 278  TYR B 279 -1  O  LEU B 278   N  SER B  74           
SHEET    1   D 3 TYR B  90  SER B  93  0                                        
SHEET    2   D 3 ASP B  77  ASN B  80 -1  N  ASP B  77   O  SER B  93           
SHEET    3   D 3 PHE B 270  PRO B 271 -1  O  PHE B 270   N  ARG B  78           
SHEET    1   E 4 LYS B 129  HIS B 132  0                                        
SHEET    2   E 4 TYR B 136  ASP B 140 -1  O  ASP B 140   N  LYS B 129           
SHEET    3   E 4 GLN C  88  PRO C  92 -1  O  VAL C  91   N  SER B 137           
SHEET    4   E 4 THR C  84  GLU C  85 -1  N  GLU C  85   O  GLN C  88           
SHEET    1   F 3 GLU B 210  LYS B 212  0                                        
SHEET    2   F 3 THR B 245  ASP B 249  1  O  ARG B 246   N  LYS B 212           
SHEET    3   F 3 LYS B 254  ARG B 259 -1  O  LYS B 254   N  ASP B 249           
LINK         CD  GLN A 501                 OG  SER A 178     1555   1555  1.44  
LINK         CG  GLN A 501                 OG  SER A 178     1555   1555  2.17  
LINK        MG    MG B 601                 O   HOH B 637     1555   1555  2.28  
LINK        MG    MG B 601                 O   HOH B 638     1555   1555  2.38  
LINK        MG    MG B 601                 O   HOH B 636     1555   1555  2.31  
LINK        MG    MG B 601                 NE2 HIS B  12     1555   1555  2.14  
LINK        MG    MG B 601                 OE2 GLU B 124     1555   1555  2.01  
LINK        MG    MG B 601                 OE1 GLU B 150     1555   1555  2.13  
CISPEP   1 GLY A  153    SER A  154          0         1.22                     
SITE     1 AC1  6 HIS B  12  GLU B 124  GLU B 150  HOH B 636                    
SITE     2 AC1  6 HOH B 637  HOH B 638                                          
SITE     1 AC2 17 ALA A 128  MET A 129  GLY A 130  SER A 154                    
SITE     2 AC2 17 ASP A 174  THR A 175  GLY A 176  GLY A 177                    
SITE     3 AC2 17 SER A 178  PHE A 206  TYR A 309  TYR A 310                    
SITE     4 AC2 17 ARG A 358  ASP A 425  HOH A 508  HOH A 529                    
SITE     5 AC2 17 HOH A 701                                                     
CRYST1   77.187   88.222  183.401  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012956  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005453        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system