GenomeNet

Database: PDB
Entry: 3GFT
LinkDB: 3GFT
Original site: 3GFT 
HEADER    SIGNALING PROTEIN                       27-FEB-09   3GFT              
TITLE     HUMAN K-RAS (Q61H) IN COMPLEX WITH A GTP ANALOGUE                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE KRAS;                                               
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: ISOFORM 2, RESIDUES 1-169;                                 
COMPND   5 SYNONYM: K-RAS 2, KI-RAS, C-K-RAS, C-KI-RAS;                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KRAS, KRAS2, RASK2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL                                
KEYWDS    CANCER, SMALL GTPASE, MUTATIONS, GTP ANALOGUE, STRUCTURAL GENOMICS    
KEYWDS   2 CONSORTIUM, SGC, CARDIOMYOPATHY, CELL MEMBRANE, DEAFNESS, DISEASE    
KEYWDS   3 MUTATION, GTP-BINDING, LIPOPROTEIN, MEMBRANE, METHYLATION,           
KEYWDS   4 NUCLEOTIDE-BINDING, PALMITATE, PRENYLATION, PROTO-ONCOGENE,          
KEYWDS   5 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TONG,W.TEMPEL,L.SHEN,C.H.ARROWSMITH,A.M.EDWARDS,M.SUNDSTROM,        
AUTHOR   2 J.WEIGELT,A.BOCHKAREV,H.PARK,STRUCTURAL GENOMICS CONSORTIUM (SGC)    
REVDAT   4   01-NOV-17 3GFT    1       REMARK                                   
REVDAT   3   28-JAN-15 3GFT    1       TITLE                                    
REVDAT   2   05-SEP-12 3GFT    1       REMARK VERSN                             
REVDAT   1   10-MAR-09 3GFT    0                                                
SPRSDE     10-MAR-09 3GFT      2PMX                                             
JRNL        AUTH   Y.TONG,W.TEMPEL,L.SHEN,C.H.ARROWSMITH,A.M.EDWARDS,           
JRNL        AUTH 2 M.SUNDSTROM,J.WEIGELT,A.BOCHKAREV,H.PARK                     
JRNL        TITL   HUMAN K-RAS IN COMPLEX WITH A GTP ANALOGUE                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 55104                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN RESOLUTION SHELLS          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.213                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.698                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2589                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3902                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : 0.3290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7566                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 212                                     
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.92800                                             
REMARK   3    B22 (A**2) : 1.45900                                              
REMARK   3    B33 (A**2) : -0.53100                                             
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.311         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.242         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.172         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.798         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8079 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5336 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10989 ; 1.423 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13064 ; 1.823 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1001 ; 5.373 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   377 ;39.228 ;24.536       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1405 ;15.173 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;17.393 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1244 ; 0.064 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8893 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1573 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4873 ; 1.993 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2007 ; 0.483 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  7907 ; 3.197 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3206 ; 2.219 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3065 ; 3.392 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK BULK SOLVENT                                    
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. PROGRAMS COOT, MOLPROBITY HAVE ALSO BEEN USED IN         
REMARK   3  REFINEMENT.                                                         
REMARK   4                                                                      
REMARK   4 3GFT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051805.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-APR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E DW                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69383                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.15100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AGP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2M LITHIUM CITRATE, PH   
REMARK 280  4.5, VAPOR DIFFUSION, TEMPERATURE 291K                              
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       31.76750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       78.41800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.13750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       78.41800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.76750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.13750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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 300 REMARK: AUTHORS STATE THAT THE BIOLOGICAL UNIT OF THIS PROTEIN IS    
REMARK 300 UNKNOWN.                                                             
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     MET B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     HIS B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     TYR B    64                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     LYS B   169                                                      
REMARK 465     MET C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     ARG C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     ASN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     ILE C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     HIS C    61                                                      
REMARK 465     GLU C    62                                                      
REMARK 465     GLU C    63                                                      
REMARK 465     TYR C    64                                                      
REMARK 465     GLU C   168                                                      
REMARK 465     LYS C   169                                                      
REMARK 465     MET D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     ARG D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     ASN D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     TYR D    -3                                                      
REMARK 465     PHE D    -2                                                      
REMARK 465     GLN D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     TYR D    32                                                      
REMARK 465     ASP D    33                                                      
REMARK 465     PRO D    34                                                      
REMARK 465     THR D    35                                                      
REMARK 465     ILE D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     HIS D    61                                                      
REMARK 465     GLU D    62                                                      
REMARK 465     GLU D    63                                                      
REMARK 465     TYR D    64                                                      
REMARK 465     SER D    65                                                      
REMARK 465     ALA D    66                                                      
REMARK 465     MET D    67                                                      
REMARK 465     ARG D    68                                                      
REMARK 465     ASP D    69                                                      
REMARK 465     GLN D    70                                                      
REMARK 465     TYR D    71                                                      
REMARK 465     GLU D   168                                                      
REMARK 465     LYS D   169                                                      
REMARK 465     MET E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     ARG E    -7                                                      
REMARK 465     GLU E    -6                                                      
REMARK 465     ASN E    -5                                                      
REMARK 465     LEU E    -4                                                      
REMARK 465     TYR E    -3                                                      
REMARK 465     HIS E    61                                                      
REMARK 465     GLU E    62                                                      
REMARK 465     GLU E    63                                                      
REMARK 465     TYR E    64                                                      
REMARK 465     SER E    65                                                      
REMARK 465     ALA E    66                                                      
REMARK 465     MET E    67                                                      
REMARK 465     GLU E   168                                                      
REMARK 465     LYS E   169                                                      
REMARK 465     MET F   -17                                                      
REMARK 465     HIS F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     GLY F    -8                                                      
REMARK 465     ARG F    -7                                                      
REMARK 465     GLU F    -6                                                      
REMARK 465     ASN F    -5                                                      
REMARK 465     LEU F    -4                                                      
REMARK 465     TYR F    -3                                                      
REMARK 465     TYR F    32                                                      
REMARK 465     ASP F    33                                                      
REMARK 465     PRO F    34                                                      
REMARK 465     THR F    35                                                      
REMARK 465     ILE F    36                                                      
REMARK 465     GLU F    37                                                      
REMARK 465     GLY F    60                                                      
REMARK 465     HIS F    61                                                      
REMARK 465     GLU F    62                                                      
REMARK 465     GLU F    63                                                      
REMARK 465     TYR F    64                                                      
REMARK 465     SER F    65                                                      
REMARK 465     ALA F    66                                                      
REMARK 465     MET F    67                                                      
REMARK 465     ARG F    68                                                      
REMARK 465     GLU F   168                                                      
REMARK 465     LYS F   169                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A  61    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B  37    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  41    NE   CZ   NH1  NH2                                  
REMARK 470     MET B  67    CG   SD   CE                                        
REMARK 470     ARG B  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  70    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  88    CE   NZ                                             
REMARK 470     ARG B 135    NE   CZ   NH1  NH2                                  
REMARK 470     TYR C  32    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU C  49    CG   CD   OE1  OE2                                  
REMARK 470     MET C  67    CG   SD   CE                                        
REMARK 470     ARG C  68    NE   CZ   NH1  NH2                                  
REMARK 470     GLN C  99    CD   OE1  NE2                                       
REMARK 470     LYS C 101    CD   CE   NZ                                        
REMARK 470     ARG C 102    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU D  49    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  31    CG   CD   OE1  OE2                                  
REMARK 470     GLU E  37    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN E  70    CG   CD   OE1  NE2                                  
REMARK 470     ARG E  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E 101    CG   CD   CE   NZ                                   
REMARK 470     GLU E 107    CG   CD   OE1  OE2                                  
REMARK 470     GLN F  70    CG   CD   OE1  NE2                                  
REMARK 470     ARG F 102    NE   CZ   NH1  NH2                                  
REMARK 470     ARG F 135    NE   CZ   NH1  NH2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   97   CA   CB   CG   CD   NE   CZ   NH1                   
REMARK 480     ARG A   97   NH2                                                 
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    ARG A  97   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 161   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG F 161   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    ILE A  36      -64.21   -102.40                                   
REMARK 500    GLU A  37      115.58   -163.51                                   
REMARK 500    HIS A  61       79.86   -106.02                                   
REMARK 500    GLU A  63     -166.58    -76.33                                   
REMARK 500    LYS A 117       30.46     71.43                                   
REMARK 500    ARG A 149        1.64     85.22                                   
REMARK 500    ILE B  36      -72.42    -79.30                                   
REMARK 500    LYS B 117       30.47     76.57                                   
REMARK 500    ARG B 149       -3.48     80.54                                   
REMARK 500    LYS C 117       32.24     70.47                                   
REMARK 500    CYS C 118        1.32    -69.14                                   
REMARK 500    HIS C 166      -72.51    -58.11                                   
REMARK 500    ASP D 108       57.75   -115.56                                   
REMARK 500    ASP D 108       55.57   -110.99                                   
REMARK 500    ARG D 149       -0.83     77.67                                   
REMARK 500    GLU E  37      125.42   -178.25                                   
REMARK 500    LYS E 117       40.88     72.10                                   
REMARK 500    SER E 122       45.91    -95.45                                   
REMARK 500    MET F   1      162.52    -45.63                                   
REMARK 500    SER F 122       43.07   -106.48                                   
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 A 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 THR A  35   OG1  89.0                                              
REMARK 620 3 GNP A 201   O1B  98.0 173.0                                        
REMARK 620 4 GNP A 201   O2G 171.1  84.3  88.9                                  
REMARK 620 5 HOH A 401   O    82.3  91.1  90.6  92.0                            
REMARK 620 6 HOH A 402   O    97.1  89.5  88.9  88.7 179.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER B  17   OG                                                     
REMARK 620 2 THR B  35   OG1  80.3                                              
REMARK 620 3 GNP B 201   O2G 173.5  94.5                                        
REMARK 620 4 GNP B 201   O1B  95.2 175.2  90.1                                  
REMARK 620 5 HOH B 403   O    87.6  94.0  88.8  87.7                            
REMARK 620 6 HOH B 404   O    89.6  90.0  94.4  88.1 174.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER C  17   OG                                                     
REMARK 620 2 THR C  35   OG1  82.7                                              
REMARK 620 3 GNP C 201   O1B  90.5 170.9                                        
REMARK 620 4 GNP C 201   O2G 164.5  94.4  90.4                                  
REMARK 620 5 HOH C 405   O    83.5  91.1  82.0  81.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER E  17   OG                                                     
REMARK 620 2 THR E  35   OG1  76.1                                              
REMARK 620 3 GNP E 201   O2G 148.1  90.9                                        
REMARK 620 4 GNP E 201   O1B  92.0 158.7  90.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F  17   OG                                                     
REMARK 620 2 GNP F 201   O1B  85.7                                              
REMARK 620 3 GNP F 201   O2G 152.6  77.0                                        
REMARK 620 4 HOH F 407   O    92.1  84.3 107.0                                  
REMARK 620 5 HOH F 406   O    83.0  77.7  72.8 161.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP D 201   O1B                                                    
REMARK 620 2 GNP D 201   O2G  71.7                                              
REMARK 620 3 SER D  17   OG   74.3 111.0                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 170                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT F 301                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE OF THIS PROTEIN IS THE 2B ISOFORM                       
REMARK 999 OF UNIPROT ENTRY P01116, RESIDUES 1-169.                             
REMARK 999 AUTHORS CONFIRMED THE SEQUENCE AT POSITION 61 BY                     
REMARK 999 DNA SEQUENCING AND MASS SPECTROSCOPY.                                
DBREF  3GFT A    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  3GFT B    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  3GFT C    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  3GFT D    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  3GFT E    1   169  UNP    P01116   RASK_HUMAN       1    169             
DBREF  3GFT F    1   169  UNP    P01116   RASK_HUMAN       1    169             
SEQADV 3GFT MET A  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER A  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER A   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY A   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG A   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU A   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN A   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU A   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR A   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE A   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN A   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY A    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS A   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQADV 3GFT MET B  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER B  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER B   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY B   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG B   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU B   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN B   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU B   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR B   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE B   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN B   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY B    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS B   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQADV 3GFT MET C  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER C  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER C   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY C   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG C   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU C   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN C   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU C   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR C   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE C   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN C   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY C    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS C   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQADV 3GFT MET D  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER D  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER D   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY D   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG D   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU D   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN D   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU D   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR D   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE D   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN D   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY D    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS D   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQADV 3GFT MET E  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER E  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER E   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY E   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG E   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU E   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN E   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU E   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR E   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE E   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN E   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY E    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS E   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQADV 3GFT MET F  -17  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -16  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -15  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -14  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -13  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -12  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F  -11  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER F  -10  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT SER F   -9  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY F   -8  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ARG F   -7  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLU F   -6  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT ASN F   -5  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT LEU F   -4  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT TYR F   -3  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT PHE F   -2  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLN F   -1  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT GLY F    0  UNP  P01116              EXPRESSION TAG                 
SEQADV 3GFT HIS F   61  UNP  P01116    GLN    61 SEE REMARK 999                 
SEQRES   1 A  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 A  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 A  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 A  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 A  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 A  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 A  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 A  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 A  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 A  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 A  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 A  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 A  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 A  187  LYS HIS LYS GLU LYS                                          
SEQRES   1 B  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 B  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 B  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 B  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 B  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 B  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 B  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 B  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 B  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 B  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 B  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 B  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 B  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 B  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 B  187  LYS HIS LYS GLU LYS                                          
SEQRES   1 C  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 C  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 C  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 C  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 C  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 C  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 C  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 C  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 C  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 C  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 C  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 C  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 C  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 C  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 C  187  LYS HIS LYS GLU LYS                                          
SEQRES   1 D  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 D  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 D  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 D  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 D  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 D  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 D  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 D  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 D  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 D  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 D  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 D  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 D  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 D  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 D  187  LYS HIS LYS GLU LYS                                          
SEQRES   1 E  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 E  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 E  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 E  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 E  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 E  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 E  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 E  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 E  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 E  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 E  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 E  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 E  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 E  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 E  187  LYS HIS LYS GLU LYS                                          
SEQRES   1 F  187  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 F  187  LEU TYR PHE GLN GLY MET THR GLU TYR LYS LEU VAL VAL          
SEQRES   3 F  187  VAL GLY ALA GLY GLY VAL GLY LYS SER ALA LEU THR ILE          
SEQRES   4 F  187  GLN LEU ILE GLN ASN HIS PHE VAL ASP GLU TYR ASP PRO          
SEQRES   5 F  187  THR ILE GLU ASP SER TYR ARG LYS GLN VAL VAL ILE ASP          
SEQRES   6 F  187  GLY GLU THR CYS LEU LEU ASP ILE LEU ASP THR ALA GLY          
SEQRES   7 F  187  HIS GLU GLU TYR SER ALA MET ARG ASP GLN TYR MET ARG          
SEQRES   8 F  187  THR GLY GLU GLY PHE LEU CYS VAL PHE ALA ILE ASN ASN          
SEQRES   9 F  187  THR LYS SER PHE GLU ASP ILE HIS HIS TYR ARG GLU GLN          
SEQRES  10 F  187  ILE LYS ARG VAL LYS ASP SER GLU ASP VAL PRO MET VAL          
SEQRES  11 F  187  LEU VAL GLY ASN LYS CYS ASP LEU PRO SER ARG THR VAL          
SEQRES  12 F  187  ASP THR LYS GLN ALA GLN ASP LEU ALA ARG SER TYR GLY          
SEQRES  13 F  187  ILE PRO PHE ILE GLU THR SER ALA LYS THR ARG GLN GLY          
SEQRES  14 F  187  VAL ASP ASP ALA PHE TYR THR LEU VAL ARG GLU ILE ARG          
SEQRES  15 F  187  LYS HIS LYS GLU LYS                                          
HET     MG  A 202       1                                                       
HET    GNP  A 201      32                                                       
HET    UNX  A 170       1                                                       
HET     MG  B 202       1                                                       
HET    GNP  B 201      32                                                       
HET     MG  C 202       1                                                       
HET    GNP  C 201      32                                                       
HET     MG  D 202       1                                                       
HET    GNP  D 201      32                                                       
HET     MG  E 202       1                                                       
HET    GNP  E 201      32                                                       
HET     MG  F 202       1                                                       
HET    GNP  F 201      32                                                       
HET    CIT  F 301      13                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     CIT CITRIC ACID                                                      
FORMUL   7   MG    6(MG 2+)                                                     
FORMUL   8  GNP    6(C10 H17 N6 O13 P3)                                         
FORMUL   9  UNX    X                                                            
FORMUL  20  CIT    C6 H8 O7                                                     
FORMUL  21  HOH   *142(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 SER A   65  ARG A   73  1                                   9    
HELIX    3   3 ASN A   86  ASP A   92  1                                   7    
HELIX    4   4 ASP A   92  ASP A  105  1                                  14    
HELIX    5   5 ASP A  126  GLY A  138  1                                  13    
HELIX    6   6 GLY A  151  LYS A  167  1                                  17    
HELIX    7   7 GLY B   15  ASN B   26  1                                  12    
HELIX    8   8 SER B   65  GLY B   75  1                                  11    
HELIX    9   9 ASN B   86  ASP B  105  1                                  20    
HELIX   10  10 ASP B  126  GLY B  138  1                                  13    
HELIX   11  11 GLY B  151  LYS B  167  1                                  17    
HELIX   12  12 GLY C   15  ASN C   26  1                                  12    
HELIX   13  13 SER C   65  GLY C   75  1                                  11    
HELIX   14  14 ASN C   86  ASP C  105  1                                  20    
HELIX   15  15 ASP C  126  GLY C  138  1                                  13    
HELIX   16  16 GLY C  151  LYS C  167  1                                  17    
HELIX   17  17 GLY D   15  ASN D   26  1                                  12    
HELIX   18  18 ASN D   86  ASP D   92  1                                   7    
HELIX   19  19 ASP D   92  ASP D  105  1                                  14    
HELIX   20  20 ASP D  126  TYR D  137  1                                  12    
HELIX   21  21 GLY D  151  LYS D  167  1                                  17    
HELIX   22  22 GLY E   15  ASN E   26  1                                  12    
HELIX   23  23 ASP E   69  GLY E   75  1                                   7    
HELIX   24  24 ASN E   86  ASP E   92  1                                   7    
HELIX   25  25 ASP E   92  LYS E  104  1                                  13    
HELIX   26  26 ASP E  126  GLY E  138  1                                  13    
HELIX   27  27 GLY E  151  LYS E  167  1                                  17    
HELIX   28  28 GLY F   15  ASN F   26  1                                  12    
HELIX   29  29 ASP F   69  GLY F   75  1                                   7    
HELIX   30  30 ASN F   86  ASP F   92  1                                   7    
HELIX   31  31 ASP F   92  ASP F  105  1                                  14    
HELIX   32  32 ASP F  126  TYR F  137  1                                  12    
HELIX   33  33 GLY F  151  LYS F  167  1                                  17    
SHEET    1   A 6 GLU A  37  ILE A  46  0                                        
SHEET    2   A 6 GLU A  49  THR A  58 -1  O  LEU A  53   N  LYS A  42           
SHEET    3   A 6 THR A   2  GLY A  10  1  N  VAL A   8   O  LEU A  56           
SHEET    4   A 6 GLY A  77  ALA A  83  1  O  LEU A  79   N  VAL A   7           
SHEET    5   A 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6   A 6 PHE A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
SHEET    1   B 6 GLU B  37  ILE B  46  0                                        
SHEET    2   B 6 GLU B  49  THR B  58 -1  O  CYS B  51   N  VAL B  44           
SHEET    3   B 6 THR B   2  GLY B  10  1  N  LEU B   6   O  LEU B  56           
SHEET    4   B 6 GLY B  77  ALA B  83  1  O  VAL B  81   N  VAL B   9           
SHEET    5   B 6 MET B 111  ASN B 116  1  O  ASN B 116   N  PHE B  82           
SHEET    6   B 6 PHE B 141  THR B 144  1  O  ILE B 142   N  LEU B 113           
SHEET    1   C 6 SER C  39  ILE C  46  0                                        
SHEET    2   C 6 GLU C  49  ASP C  57 -1  O  LEU C  53   N  LYS C  42           
SHEET    3   C 6 THR C   2  VAL C   9  1  N  LEU C   6   O  LEU C  56           
SHEET    4   C 6 GLY C  77  ALA C  83  1  O  VAL C  81   N  VAL C   9           
SHEET    5   C 6 MET C 111  ASN C 116  1  O  VAL C 114   N  CYS C  80           
SHEET    6   C 6 PHE C 141  GLU C 143  1  O  ILE C 142   N  LEU C 113           
SHEET    1   D 6 SER D  39  ILE D  46  0                                        
SHEET    2   D 6 GLU D  49  ASP D  57 -1  O  LEU D  53   N  LYS D  42           
SHEET    3   D 6 THR D   2  VAL D   9  1  N  THR D   2   O  LEU D  52           
SHEET    4   D 6 GLY D  77  ALA D  83  1  O  VAL D  81   N  VAL D   9           
SHEET    5   D 6 MET D 111  ASN D 116  1  O  VAL D 112   N  CYS D  80           
SHEET    6   D 6 PHE D 141  GLU D 143  1  O  ILE D 142   N  GLY D 115           
SHEET    1   E 6 GLU E  37  ILE E  46  0                                        
SHEET    2   E 6 GLU E  49  THR E  58 -1  O  ILE E  55   N  TYR E  40           
SHEET    3   E 6 THR E   2  VAL E   9  1  N  LEU E   6   O  ASP E  54           
SHEET    4   E 6 GLY E  77  ALA E  83  1  O  LEU E  79   N  VAL E   9           
SHEET    5   E 6 MET E 111  ASN E 116  1  O  ASN E 116   N  PHE E  82           
SHEET    6   E 6 PHE E 141  GLU E 143  1  O  ILE E 142   N  GLY E 115           
SHEET    1   F 6 SER F  39  ILE F  46  0                                        
SHEET    2   F 6 GLU F  49  ASP F  57 -1  O  CYS F  51   N  VAL F  44           
SHEET    3   F 6 THR F   2  GLY F  10  1  N  THR F   2   O  LEU F  52           
SHEET    4   F 6 GLY F  77  ALA F  83  1  O  LEU F  79   N  VAL F   7           
SHEET    5   F 6 MET F 111  ASN F 116  1  O  ASN F 116   N  PHE F  82           
SHEET    6   F 6 PHE F 141  GLU F 143  1  O  ILE F 142   N  GLY F 115           
LINK         OG  SER A  17                MG    MG A 202     1555   1555  2.04  
LINK         OG1 THR A  35                MG    MG A 202     1555   1555  2.12  
LINK         OG  SER B  17                MG    MG B 202     1555   1555  2.18  
LINK         OG1 THR B  35                MG    MG B 202     1555   1555  2.19  
LINK         OG  SER C  17                MG    MG C 202     1555   1555  2.28  
LINK         OG1 THR C  35                MG    MG C 202     1555   1555  2.24  
LINK         OG  SER E  17                MG    MG E 202     1555   1555  2.15  
LINK         OG1 THR E  35                MG    MG E 202     1555   1555  2.47  
LINK         OG  SER F  17                MG    MG F 202     1555   1555  2.25  
LINK        MG    MG A 202                 O1B GNP A 201     1555   1555  2.02  
LINK        MG    MG A 202                 O2G GNP A 201     1555   1555  2.11  
LINK        MG    MG B 202                 O2G GNP B 201     1555   1555  1.87  
LINK        MG    MG B 202                 O1B GNP B 201     1555   1555  1.99  
LINK        MG    MG C 202                 O1B GNP C 201     1555   1555  2.02  
LINK        MG    MG C 202                 O2G GNP C 201     1555   1555  2.01  
LINK        MG    MG D 202                 O1B GNP D 201     1555   1555  2.23  
LINK        MG    MG D 202                 O2G GNP D 201     1555   1555  2.20  
LINK        MG    MG E 202                 O2G GNP E 201     1555   1555  1.77  
LINK        MG    MG E 202                 O1B GNP E 201     1555   1555  2.10  
LINK        MG    MG F 202                 O1B GNP F 201     1555   1555  2.23  
LINK        MG    MG F 202                 O2G GNP F 201     1555   1555  1.91  
LINK        MG    MG A 202                 O   HOH A 401     1555   1555  2.12  
LINK        MG    MG A 202                 O   HOH A 402     1555   1555  2.19  
LINK        MG    MG B 202                 O   HOH B 403     1555   1555  2.36  
LINK        MG    MG B 202                 O   HOH B 404     1555   1555  2.16  
LINK        MG    MG C 202                 O   HOH C 405     1555   1555  2.06  
LINK        MG    MG F 202                 O   HOH F 407     1555   1555  1.95  
LINK        MG    MG F 202                 O   HOH F 406     1555   1555  2.47  
LINK         OG  SER D  17                MG    MG D 202     1555   1555  2.76  
SITE     1 AC1  5 SER A  17  THR A  35  GNP A 201  HOH A 401                    
SITE     2 AC1  5 HOH A 402                                                     
SITE     1 AC2 27 GLY A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC2 27 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC2 27 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC2 27 PRO A  34  THR A  35  GLY A  60  ASN A 116                    
SITE     5 AC2 27 LYS A 117  ASP A 119  LEU A 120  SER A 145                    
SITE     6 AC2 27 ALA A 146  LYS A 147   MG A 202  HOH A 401                    
SITE     7 AC2 27 HOH A 402  HOH A 463  HOH A 483                               
SITE     1 AC3  5 ILE A  36  ALA A  59  GLU A  62  TYR A  71                    
SITE     2 AC3  5 HIS B  95                                                     
SITE     1 AC4  5 SER B  17  THR B  35  GNP B 201  HOH B 403                    
SITE     2 AC4  5 HOH B 404                                                     
SITE     1 AC5 24 GLY B  12  GLY B  13  VAL B  14  GLY B  15                    
SITE     2 AC5 24 LYS B  16  SER B  17  ALA B  18  PHE B  28                    
SITE     3 AC5 24 VAL B  29  ASP B  30  GLU B  31  TYR B  32                    
SITE     4 AC5 24 PRO B  34  THR B  35  GLY B  60  ASN B 116                    
SITE     5 AC5 24 LYS B 117  ASP B 119  LEU B 120  SER B 145                    
SITE     6 AC5 24 ALA B 146   MG B 202  HOH B 403  HOH B 404                    
SITE     1 AC6  4 SER C  17  THR C  35  GNP C 201  HOH C 405                    
SITE     1 AC7 20 GLY C  12  GLY C  13  VAL C  14  GLY C  15                    
SITE     2 AC7 20 LYS C  16  SER C  17  ALA C  18  PHE C  28                    
SITE     3 AC7 20 VAL C  29  ASP C  30  THR C  35  GLY C  60                    
SITE     4 AC7 20 ASN C 116  LYS C 117  ASP C 119  LEU C 120                    
SITE     5 AC7 20 SER C 145  ALA C 146   MG C 202  HOH C 405                    
SITE     1 AC8  4 SER D  17  ASP D  57  THR D  58  GNP D 201                    
SITE     1 AC9 19 GLY D  12  GLY D  13  VAL D  14  GLY D  15                    
SITE     2 AC9 19 LYS D  16  SER D  17  ALA D  18  PHE D  28                    
SITE     3 AC9 19 VAL D  29  ASP D  30  GLU D  31  GLY D  60                    
SITE     4 AC9 19 ASN D 116  LYS D 117  ASP D 119  LEU D 120                    
SITE     5 AC9 19 SER D 145  ALA D 146   MG D 202                               
SITE     1 BC1  3 SER E  17  THR E  35  GNP E 201                               
SITE     1 BC2 19 GLY E  13  VAL E  14  GLY E  15  LYS E  16                    
SITE     2 BC2 19 SER E  17  ALA E  18  PHE E  28  VAL E  29                    
SITE     3 BC2 19 ASP E  30  TYR E  32  THR E  35  GLY E  60                    
SITE     4 BC2 19 ASN E 116  LYS E 117  ASP E 119  LEU E 120                    
SITE     5 BC2 19 SER E 145  ALA E 146   MG E 202                               
SITE     1 BC3  4 SER F  17  GNP F 201  HOH F 406  HOH F 407                    
SITE     1 BC4 20 GLY F  12  GLY F  13  VAL F  14  GLY F  15                    
SITE     2 BC4 20 LYS F  16  SER F  17  ALA F  18  PHE F  28                    
SITE     3 BC4 20 VAL F  29  ASP F  30  ALA F  59  ASN F 116                    
SITE     4 BC4 20 LYS F 117  ASP F 119  LEU F 120  SER F 145                    
SITE     5 BC4 20 ALA F 146   MG F 202  HOH F 406  HOH F 407                    
SITE     1 BC5  8 ARG A 123  ASP A 126  THR A 127  LYS F  88                    
SITE     2 BC5  8 GLU F  91  ASP F  92  HIS F  94  HIS F  95                    
CRYST1   63.535  118.275  156.836  90.00  90.00  90.00 P 21 21 21   24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015739  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006376        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system