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Database: PDB
Entry: 3UFX
LinkDB: 3UFX
Original site: 3UFX 
HEADER    LIGASE                                  01-NOV-11   3UFX              
TITLE     THERMUS AQUATICUS SUCCINYL-COA SYNTHETASE IN COMPLEX WITH GDP-MN2+    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINYL-COA SYNTHETASE ALPHA SUBUNIT;                     
COMPND   3 CHAIN: A, D, F, H;                                                   
COMPND   4 SYNONYM: SUCCINYL-COA LIGASE ALPHA SUBUNIT;                          
COMPND   5 EC: 6.2.1.-;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SUCCINYL-COA SYNTHETASE BETA SUBUNIT;                      
COMPND   9 CHAIN: B, E, G, I;                                                   
COMPND  10 SYNONYM: SUCCINYL-COA LIGASE BETA SUBUNIT;                           
COMPND  11 EC: 6.2.1.-;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS AQUATICUS;                              
SOURCE   3 ORGANISM_TAXID: 271;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: THERMUS AQUATICUS;                              
SOURCE   8 ORGANISM_TAXID: 271;                                                 
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ATP-GRASP FOLD, LIGASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.FRASER                                                            
REVDAT   3   08-NOV-17 3UFX    1       REMARK                                   
REVDAT   2   23-JAN-13 3UFX    1       JRNL                                     
REVDAT   1   27-JUN-12 3UFX    0                                                
JRNL        AUTH   M.A.JOYCE,K.HAYAKAWA,W.T.WOLODKO,M.E.FRASER                  
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF THE           
JRNL        TITL 2 GTP-PREFERRING SUCCINYL-COA SYNTHETASE FROM THERMUS          
JRNL        TITL 3 AQUATICUS.                                                   
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   751 2012              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   22751660                                                     
JRNL        DOI    10.1107/S0907444912010852                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.4_486                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 120075                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6048                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 51.0060 -  7.2945    0.91     4061   247  0.2042 0.2109        
REMARK   3     2  7.2945 -  5.7925    0.93     4146   201  0.2221 0.2478        
REMARK   3     3  5.7925 -  5.0610    0.94     4129   229  0.1769 0.2111        
REMARK   3     4  5.0610 -  4.5986    0.95     4203   220  0.1402 0.1684        
REMARK   3     5  4.5986 -  4.2692    0.95     4170   218  0.1305 0.1891        
REMARK   3     6  4.2692 -  4.0176    0.95     4220   207  0.1551 0.1836        
REMARK   3     7  4.0176 -  3.8165    0.95     4185   212  0.1678 0.2019        
REMARK   3     8  3.8165 -  3.6504    0.96     4218   213  0.1868 0.2206        
REMARK   3     9  3.6504 -  3.5099    0.95     4163   231  0.2047 0.2240        
REMARK   3    10  3.5099 -  3.3888    0.95     4142   238  0.2120 0.2754        
REMARK   3    11  3.3888 -  3.2829    0.94     4123   226  0.2344 0.2513        
REMARK   3    12  3.2829 -  3.1890    0.94     4129   212  0.2273 0.2783        
REMARK   3    13  3.1890 -  3.1051    0.94     4088   216  0.2309 0.2800        
REMARK   3    14  3.1051 -  3.0293    0.94     4114   234  0.2189 0.2704        
REMARK   3    15  3.0293 -  2.9605    0.93     4094   215  0.2281 0.2858        
REMARK   3    16  2.9605 -  2.8975    0.94     4111   210  0.2291 0.3181        
REMARK   3    17  2.8975 -  2.8395    0.93     4062   203  0.2349 0.3041        
REMARK   3    18  2.8395 -  2.7860    0.93     4057   242  0.2329 0.2884        
REMARK   3    19  2.7860 -  2.7362    0.92     4009   212  0.2421 0.2765        
REMARK   3    20  2.7362 -  2.6898    0.91     3908   228  0.2315 0.2705        
REMARK   3    21  2.6898 -  2.6464    0.89     3915   191  0.2269 0.2639        
REMARK   3    22  2.6464 -  2.6057    0.88     3872   207  0.2325 0.3214        
REMARK   3    23  2.6057 -  2.5674    0.86     3714   204  0.2478 0.3291        
REMARK   3    24  2.5674 -  2.5312    0.83     3631   182  0.2771 0.3419        
REMARK   3    25  2.5312 -  2.4970    0.78     3424   181  0.2889 0.3469        
REMARK   3    26  2.4970 -  2.4646    0.73     3153   171  0.2864 0.3408        
REMARK   3    27  2.4646 -  2.4338    0.67     2903   149  0.2990 0.3456        
REMARK   3    28  2.4338 -  2.4045    0.60     2607   142  0.2976 0.3295        
REMARK   3    29  2.4045 -  2.3765    0.55     2448   114  0.3228 0.3486        
REMARK   3    30  2.3765 -  2.3500    0.47     2028    93  0.3197 0.3355        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 28.30                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 10.46110                                             
REMARK   3    B22 (A**2) : -10.77430                                            
REMARK   3    B33 (A**2) : 0.31330                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 7.15640                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008          20131                                  
REMARK   3   ANGLE     :  1.041          27265                                  
REMARK   3   CHIRALITY :  0.064           3178                                  
REMARK   3   PLANARITY :  0.004           3509                                  
REMARK   3   DIHEDRAL  : 13.799           7469                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3UFX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068704.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-OCT-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1159                             
REMARK 200  MONOCHROMATOR                  : KOHZU DOUBLE FLAT CRYSTAL          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 120106                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 200.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 49.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRIES 1JKJ AND 1OI7                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG3350, 100 MM MES, 200 MM          
REMARK 280  POTASSIUM CHLORIDE, PH 6.4, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      130.85000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      130.85000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       63.40000            
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 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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, I                            
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: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G                                  
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: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, I                                  
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     TRP A   289                                                      
REMARK 465     ASN A   290                                                      
REMARK 465     SER A   291                                                      
REMARK 465     ARG A   292                                                      
REMARK 465     PRO A   293                                                      
REMARK 465     GLY A   294                                                      
REMARK 465     ILE A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     TRP B   379                                                      
REMARK 465     LEU B   380                                                      
REMARK 465     GLU B   381                                                      
REMARK 465     PHE B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     PRO B   384                                                      
REMARK 465     GLY B   385                                                      
REMARK 465     ASP B   386                                                      
REMARK 465     LEU B   387                                                      
REMARK 465     PRO B   388                                                      
REMARK 465     MET B   389                                                      
REMARK 465     VAL B   390                                                      
REMARK 465     HIS B   391                                                      
REMARK 465     SER B   392                                                      
REMARK 465     GLN B   393                                                      
REMARK 465     TYR B   394                                                      
REMARK 465     ASN B   395                                                      
REMARK 465     LEU B   396                                                      
REMARK 465     LEU B   397                                                      
REMARK 465     TRP D   289                                                      
REMARK 465     ASN D   290                                                      
REMARK 465     SER D   291                                                      
REMARK 465     ARG D   292                                                      
REMARK 465     PRO D   293                                                      
REMARK 465     GLY D   294                                                      
REMARK 465     ILE D   295                                                      
REMARK 465     LEU D   296                                                      
REMARK 465     LYS E   374                                                      
REMARK 465     GLY E   375                                                      
REMARK 465     GLY E   376                                                      
REMARK 465     ALA E   377                                                      
REMARK 465     ALA E   378                                                      
REMARK 465     TRP E   379                                                      
REMARK 465     LEU E   380                                                      
REMARK 465     GLU E   381                                                      
REMARK 465     PHE E   382                                                      
REMARK 465     ALA E   383                                                      
REMARK 465     PRO E   384                                                      
REMARK 465     GLY E   385                                                      
REMARK 465     ASP E   386                                                      
REMARK 465     LEU E   387                                                      
REMARK 465     PRO E   388                                                      
REMARK 465     MET E   389                                                      
REMARK 465     VAL E   390                                                      
REMARK 465     HIS E   391                                                      
REMARK 465     SER E   392                                                      
REMARK 465     GLN E   393                                                      
REMARK 465     TYR E   394                                                      
REMARK 465     ASN E   395                                                      
REMARK 465     LEU E   396                                                      
REMARK 465     LEU E   397                                                      
REMARK 465     TRP F   289                                                      
REMARK 465     ASN F   290                                                      
REMARK 465     SER F   291                                                      
REMARK 465     ARG F   292                                                      
REMARK 465     PRO F   293                                                      
REMARK 465     GLY F   294                                                      
REMARK 465     ILE F   295                                                      
REMARK 465     LEU F   296                                                      
REMARK 465     GLU G   353                                                      
REMARK 465     GLY G   354                                                      
REMARK 465     ALA G   372                                                      
REMARK 465     MET G   373                                                      
REMARK 465     LYS G   374                                                      
REMARK 465     GLY G   375                                                      
REMARK 465     GLY G   376                                                      
REMARK 465     ALA G   377                                                      
REMARK 465     ALA G   378                                                      
REMARK 465     TRP G   379                                                      
REMARK 465     LEU G   380                                                      
REMARK 465     GLU G   381                                                      
REMARK 465     PHE G   382                                                      
REMARK 465     ALA G   383                                                      
REMARK 465     PRO G   384                                                      
REMARK 465     GLY G   385                                                      
REMARK 465     ASP G   386                                                      
REMARK 465     LEU G   387                                                      
REMARK 465     PRO G   388                                                      
REMARK 465     MET G   389                                                      
REMARK 465     VAL G   390                                                      
REMARK 465     HIS G   391                                                      
REMARK 465     SER G   392                                                      
REMARK 465     GLN G   393                                                      
REMARK 465     TYR G   394                                                      
REMARK 465     ASN G   395                                                      
REMARK 465     LEU G   396                                                      
REMARK 465     LEU G   397                                                      
REMARK 465     TRP H   289                                                      
REMARK 465     ASN H   290                                                      
REMARK 465     SER H   291                                                      
REMARK 465     ARG H   292                                                      
REMARK 465     PRO H   293                                                      
REMARK 465     GLY H   294                                                      
REMARK 465     ILE H   295                                                      
REMARK 465     LEU H   296                                                      
REMARK 465     ALA I   372                                                      
REMARK 465     MET I   373                                                      
REMARK 465     LYS I   374                                                      
REMARK 465     GLY I   375                                                      
REMARK 465     GLY I   376                                                      
REMARK 465     ALA I   377                                                      
REMARK 465     ALA I   378                                                      
REMARK 465     TRP I   379                                                      
REMARK 465     LEU I   380                                                      
REMARK 465     GLU I   381                                                      
REMARK 465     PHE I   382                                                      
REMARK 465     ALA I   383                                                      
REMARK 465     PRO I   384                                                      
REMARK 465     GLY I   385                                                      
REMARK 465     ASP I   386                                                      
REMARK 465     LEU I   387                                                      
REMARK 465     PRO I   388                                                      
REMARK 465     MET I   389                                                      
REMARK 465     VAL I   390                                                      
REMARK 465     HIS I   391                                                      
REMARK 465     SER I   392                                                      
REMARK 465     GLN I   393                                                      
REMARK 465     TYR I   394                                                      
REMARK 465     ASN I   395                                                      
REMARK 465     LEU I   396                                                      
REMARK 465     LEU I   397                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR B   358     OH   TYR B   358     2657     2.14            
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    LEU A   3      -51.01     73.17                                   
REMARK 500    MET A  45     -178.23    -69.86                                   
REMARK 500    GLU A 131      -55.90   -124.36                                   
REMARK 500    PHE A 142       77.20   -110.14                                   
REMARK 500    THR A 172      -96.01   -101.02                                   
REMARK 500    SER A 212       33.65   -142.95                                   
REMARK 500    LYS B  81       57.99     35.48                                   
REMARK 500    ASP B 124      106.33    -51.19                                   
REMARK 500    GLU B 131      -76.39    -60.09                                   
REMARK 500    ASP B 219      -55.19    -25.86                                   
REMARK 500    PRO B 356       47.75    -66.47                                   
REMARK 500    LEU D   3      -50.93     70.30                                   
REMARK 500    GLU D 131      -56.68   -123.40                                   
REMARK 500    PHE D 142       79.30   -110.57                                   
REMARK 500    THR D 172      -95.82   -101.86                                   
REMARK 500    SER D 212       33.68   -140.91                                   
REMARK 500    LYS E  81       57.99     35.64                                   
REMARK 500    ASP E 124      115.58    -38.99                                   
REMARK 500    ARG E 132       81.52   -161.56                                   
REMARK 500    PRO E 356       47.03    -75.50                                   
REMARK 500    LEU F   3      -51.81     72.47                                   
REMARK 500    GLU F 131      -54.75   -126.75                                   
REMARK 500    PHE F 142       77.34   -111.15                                   
REMARK 500    THR F 172      -96.81   -103.68                                   
REMARK 500    SER F 212       35.44   -141.92                                   
REMARK 500    MET F 252       74.72   -103.00                                   
REMARK 500    LYS G  81       56.09     37.25                                   
REMARK 500    ASP G 124      105.69    -58.62                                   
REMARK 500    LYS G 350       35.80    -79.10                                   
REMARK 500    PRO G 356       47.21    -63.92                                   
REMARK 500    LEU H   3      -50.26     70.32                                   
REMARK 500    GLU H 131      -55.65   -124.12                                   
REMARK 500    PHE H 142       79.27   -111.23                                   
REMARK 500    THR H 172      -96.06   -102.59                                   
REMARK 500    SER H 212       32.62   -141.73                                   
REMARK 500    LYS I  81       57.82     35.26                                   
REMARK 500    ASP I 124      118.30    -36.67                                   
REMARK 500    ARG I 132       66.10   -156.61                                   
REMARK 500    PRO I 356       46.23    -72.37                                   
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                              MN B 399  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP B 398   O2A                                                    
REMARK 620 2 ASN B 190   O    99.9                                              
REMARK 620 3 GDP B 398   O3B  73.3 168.8                                        
REMARK 620 4 ASP B 204   OD2  81.3  84.5 102.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E 399  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP E 398   O3B                                                    
REMARK 620 2 ASN E 190   O   169.5                                              
REMARK 620 3 GDP E 398   O2A  79.1  93.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G 399  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP G 398   O3B                                                    
REMARK 620 2 ASN G 190   O   158.3                                              
REMARK 620 3 GDP G 398   O2A  65.1  94.4                                        
REMARK 620 4 ASP G 204   OD2  77.4  88.5  68.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN I 399  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP I 398   O3B                                                    
REMARK 620 2 ASN I 190   O   156.7                                              
REMARK 620 3 GDP I 398   O2A  80.5  96.3                                        
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 GDP B 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 399                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP E 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 399                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP G 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 399                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP I 398                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN I 399                  
DBREF  3UFX A    1   296  PDB    3UFX     3UFX             1    296             
DBREF  3UFX D    1   296  PDB    3UFX     3UFX             1    296             
DBREF  3UFX F    1   296  PDB    3UFX     3UFX             1    296             
DBREF  3UFX H    1   296  PDB    3UFX     3UFX             1    296             
DBREF  3UFX B    1   397  PDB    3UFX     3UFX             1    397             
DBREF  3UFX E    1   397  PDB    3UFX     3UFX             1    397             
DBREF  3UFX G    1   397  PDB    3UFX     3UFX             1    397             
DBREF  3UFX I    1   397  PDB    3UFX     3UFX             1    397             
SEQRES   1 A  296  MET ILE LEU VAL ASN LYS GLU THR ARG VAL LEU VAL GLN          
SEQRES   2 A  296  GLY ILE THR GLY ARG GLU GLY GLN PHE HIS THR LYS GLN          
SEQRES   3 A  296  MET LEU SER TYR GLY THR LYS ILE VAL ALA GLY VAL THR          
SEQRES   4 A  296  PRO GLY LYS GLY GLY MET GLU VAL LEU GLY VAL PRO VAL          
SEQRES   5 A  296  TYR ASP THR VAL LYS GLU ALA VAL ALA HIS HIS GLU VAL          
SEQRES   6 A  296  ASP ALA SER ILE ILE PHE VAL PRO ALA PRO ALA ALA ALA          
SEQRES   7 A  296  ASP ALA ALA LEU GLU ALA ALA HIS ALA GLY ILE PRO LEU          
SEQRES   8 A  296  ILE VAL LEU ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 A  296  VAL ARG ALA VAL GLU GLU ILE LYS ALA LEU GLY SER ARG          
SEQRES  10 A  296  LEU ILE GLY GLY ASN CYS PRO GLY ILE ILE SER ALA GLU          
SEQRES  11 A  296  GLU THR LYS ILE GLY ILE MET PRO GLY HIS VAL PHE LYS          
SEQRES  12 A  296  ARG GLY ARG VAL GLY ILE ILE SER ARG SER GLY THR LEU          
SEQRES  13 A  296  THR TYR GLU ALA ALA ALA ALA LEU SER GLN ALA GLY LEU          
SEQRES  14 A  296  GLY THR THR THR THR VAL GLY ILE GLY GLY ASP PRO VAL          
SEQRES  15 A  296  ILE GLY THR THR PHE LYS ASP LEU LEU PRO LEU PHE ASN          
SEQRES  16 A  296  GLU ASP PRO GLU THR GLU ALA VAL VAL LEU ILE GLY GLU          
SEQRES  17 A  296  ILE GLY GLY SER ASP GLU GLU GLU ALA ALA ALA TRP VAL          
SEQRES  18 A  296  LYS ASP HIS MET LYS LYS PRO VAL VAL GLY PHE ILE GLY          
SEQRES  19 A  296  GLY ARG SER ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 A  296  GLY ALA ILE ILE MET GLY ASN VAL GLY THR PRO GLU SER          
SEQRES  21 A  296  LYS LEU ARG ALA PHE ALA GLU ALA GLY ILE PRO VAL ALA          
SEQRES  22 A  296  ASP THR ILE ASP GLU ILE VAL GLU LEU VAL LYS LYS ALA          
SEQRES  23 A  296  LEU GLY TRP ASN SER ARG PRO GLY ILE LEU                      
SEQRES   1 B  397  MET ASN LEU HIS GLU TYR GLN ALA LYS GLU ILE LEU ALA          
SEQRES   2 B  397  ARG TYR GLY VAL PRO VAL PRO PRO GLY LYS VAL ALA TYR          
SEQRES   3 B  397  THR PRO GLU GLU ALA LYS ARG ILE ALA GLU GLU PHE GLY          
SEQRES   4 B  397  LYS ARG VAL VAL ILE LYS ALA GLN VAL HIS VAL GLY GLY          
SEQRES   5 B  397  ARG GLY LYS ALA GLY GLY VAL LYS LEU ALA ASP THR PRO          
SEQRES   6 B  397  GLN GLU ALA TYR GLU LYS ALA GLN ALA ILE LEU GLY MET          
SEQRES   7 B  397  ASN ILE LYS GLY LEU THR VAL LYS LYS VAL LEU VAL ALA          
SEQRES   8 B  397  GLU ALA VAL ASP ILE ALA LYS GLU TYR TYR ALA GLY LEU          
SEQRES   9 B  397  ILE LEU ASP ARG ALA LYS LYS ARG VAL VAL LEU MET LEU          
SEQRES  10 B  397  SER LYS GLU GLY GLY VAL ASP ILE GLU GLU VAL ALA ALA          
SEQRES  11 B  397  GLU ARG PRO GLU ALA ILE HIS LYS PHE TRP ILE ASP PRO          
SEQRES  12 B  397  HIS LYS GLY PHE ARG PRO PHE GLU ALA ARG GLU MET VAL          
SEQRES  13 B  397  LYS ARG ALA GLY LEU GLU GLY ASN LEU ASN LYS LEU ALA          
SEQRES  14 B  397  GLN VAL LEU VAL ALA LEU TYR ARG ALA TYR GLU GLY VAL          
SEQRES  15 B  397  ASP ALA SER ILE ALA GLU ILE ASN PRO LEU VAL VAL THR          
SEQRES  16 B  397  THR ASP GLY GLY ILE VAL ALA ALA ASP ALA LYS ILE VAL          
SEQRES  17 B  397  LEU ASP ASP ASN ALA LEU PHE ARG HIS PRO ASP LEU ALA          
SEQRES  18 B  397  GLU LEU ARG GLU VAL GLU ALA GLU HIS PRO LEU GLU VAL          
SEQRES  19 B  397  GLU ALA SER ASN TYR GLY PHE ALA TYR VAL LYS LEU ASP          
SEQRES  20 B  397  GLY ASN ILE GLY ILE ILE GLY ASN GLY ALA GLY LEU VAL          
SEQRES  21 B  397  MET TYR THR LEU ASP LEU VAL ASN ARG VAL GLY GLY LYS          
SEQRES  22 B  397  PRO ALA ASN PHE LEU ASP ILE GLY GLY GLY ALA LYS ALA          
SEQRES  23 B  397  ASP VAL VAL TYR ASN ALA LEU LYS VAL VAL LEU LYS ASP          
SEQRES  24 B  397  PRO ASP VAL LYS GLY VAL PHE ILE ASN ILE PHE GLY GLY          
SEQRES  25 B  397  ILE THR ARG ALA ASP GLU VAL ALA LYS GLY VAL ILE ARG          
SEQRES  26 B  397  ALA LEU GLU GLU GLY LEU LEU THR LYS PRO VAL VAL MET          
SEQRES  27 B  397  ARG VAL ALA GLY THR ALA GLU GLU GLU ALA LYS LYS LEU          
SEQRES  28 B  397  LEU GLU GLY LYS PRO VAL TYR MET TYR PRO THR SER ILE          
SEQRES  29 B  397  GLU ALA ALA LYS VAL THR VAL ALA MET LYS GLY GLY ALA          
SEQRES  30 B  397  ALA TRP LEU GLU PHE ALA PRO GLY ASP LEU PRO MET VAL          
SEQRES  31 B  397  HIS SER GLN TYR ASN LEU LEU                                  
SEQRES   1 D  296  MET ILE LEU VAL ASN LYS GLU THR ARG VAL LEU VAL GLN          
SEQRES   2 D  296  GLY ILE THR GLY ARG GLU GLY GLN PHE HIS THR LYS GLN          
SEQRES   3 D  296  MET LEU SER TYR GLY THR LYS ILE VAL ALA GLY VAL THR          
SEQRES   4 D  296  PRO GLY LYS GLY GLY MET GLU VAL LEU GLY VAL PRO VAL          
SEQRES   5 D  296  TYR ASP THR VAL LYS GLU ALA VAL ALA HIS HIS GLU VAL          
SEQRES   6 D  296  ASP ALA SER ILE ILE PHE VAL PRO ALA PRO ALA ALA ALA          
SEQRES   7 D  296  ASP ALA ALA LEU GLU ALA ALA HIS ALA GLY ILE PRO LEU          
SEQRES   8 D  296  ILE VAL LEU ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 D  296  VAL ARG ALA VAL GLU GLU ILE LYS ALA LEU GLY SER ARG          
SEQRES  10 D  296  LEU ILE GLY GLY ASN CYS PRO GLY ILE ILE SER ALA GLU          
SEQRES  11 D  296  GLU THR LYS ILE GLY ILE MET PRO GLY HIS VAL PHE LYS          
SEQRES  12 D  296  ARG GLY ARG VAL GLY ILE ILE SER ARG SER GLY THR LEU          
SEQRES  13 D  296  THR TYR GLU ALA ALA ALA ALA LEU SER GLN ALA GLY LEU          
SEQRES  14 D  296  GLY THR THR THR THR VAL GLY ILE GLY GLY ASP PRO VAL          
SEQRES  15 D  296  ILE GLY THR THR PHE LYS ASP LEU LEU PRO LEU PHE ASN          
SEQRES  16 D  296  GLU ASP PRO GLU THR GLU ALA VAL VAL LEU ILE GLY GLU          
SEQRES  17 D  296  ILE GLY GLY SER ASP GLU GLU GLU ALA ALA ALA TRP VAL          
SEQRES  18 D  296  LYS ASP HIS MET LYS LYS PRO VAL VAL GLY PHE ILE GLY          
SEQRES  19 D  296  GLY ARG SER ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 D  296  GLY ALA ILE ILE MET GLY ASN VAL GLY THR PRO GLU SER          
SEQRES  21 D  296  LYS LEU ARG ALA PHE ALA GLU ALA GLY ILE PRO VAL ALA          
SEQRES  22 D  296  ASP THR ILE ASP GLU ILE VAL GLU LEU VAL LYS LYS ALA          
SEQRES  23 D  296  LEU GLY TRP ASN SER ARG PRO GLY ILE LEU                      
SEQRES   1 E  397  MET ASN LEU HIS GLU TYR GLN ALA LYS GLU ILE LEU ALA          
SEQRES   2 E  397  ARG TYR GLY VAL PRO VAL PRO PRO GLY LYS VAL ALA TYR          
SEQRES   3 E  397  THR PRO GLU GLU ALA LYS ARG ILE ALA GLU GLU PHE GLY          
SEQRES   4 E  397  LYS ARG VAL VAL ILE LYS ALA GLN VAL HIS VAL GLY GLY          
SEQRES   5 E  397  ARG GLY LYS ALA GLY GLY VAL LYS LEU ALA ASP THR PRO          
SEQRES   6 E  397  GLN GLU ALA TYR GLU LYS ALA GLN ALA ILE LEU GLY MET          
SEQRES   7 E  397  ASN ILE LYS GLY LEU THR VAL LYS LYS VAL LEU VAL ALA          
SEQRES   8 E  397  GLU ALA VAL ASP ILE ALA LYS GLU TYR TYR ALA GLY LEU          
SEQRES   9 E  397  ILE LEU ASP ARG ALA LYS LYS ARG VAL VAL LEU MET LEU          
SEQRES  10 E  397  SER LYS GLU GLY GLY VAL ASP ILE GLU GLU VAL ALA ALA          
SEQRES  11 E  397  GLU ARG PRO GLU ALA ILE HIS LYS PHE TRP ILE ASP PRO          
SEQRES  12 E  397  HIS LYS GLY PHE ARG PRO PHE GLU ALA ARG GLU MET VAL          
SEQRES  13 E  397  LYS ARG ALA GLY LEU GLU GLY ASN LEU ASN LYS LEU ALA          
SEQRES  14 E  397  GLN VAL LEU VAL ALA LEU TYR ARG ALA TYR GLU GLY VAL          
SEQRES  15 E  397  ASP ALA SER ILE ALA GLU ILE ASN PRO LEU VAL VAL THR          
SEQRES  16 E  397  THR ASP GLY GLY ILE VAL ALA ALA ASP ALA LYS ILE VAL          
SEQRES  17 E  397  LEU ASP ASP ASN ALA LEU PHE ARG HIS PRO ASP LEU ALA          
SEQRES  18 E  397  GLU LEU ARG GLU VAL GLU ALA GLU HIS PRO LEU GLU VAL          
SEQRES  19 E  397  GLU ALA SER ASN TYR GLY PHE ALA TYR VAL LYS LEU ASP          
SEQRES  20 E  397  GLY ASN ILE GLY ILE ILE GLY ASN GLY ALA GLY LEU VAL          
SEQRES  21 E  397  MET TYR THR LEU ASP LEU VAL ASN ARG VAL GLY GLY LYS          
SEQRES  22 E  397  PRO ALA ASN PHE LEU ASP ILE GLY GLY GLY ALA LYS ALA          
SEQRES  23 E  397  ASP VAL VAL TYR ASN ALA LEU LYS VAL VAL LEU LYS ASP          
SEQRES  24 E  397  PRO ASP VAL LYS GLY VAL PHE ILE ASN ILE PHE GLY GLY          
SEQRES  25 E  397  ILE THR ARG ALA ASP GLU VAL ALA LYS GLY VAL ILE ARG          
SEQRES  26 E  397  ALA LEU GLU GLU GLY LEU LEU THR LYS PRO VAL VAL MET          
SEQRES  27 E  397  ARG VAL ALA GLY THR ALA GLU GLU GLU ALA LYS LYS LEU          
SEQRES  28 E  397  LEU GLU GLY LYS PRO VAL TYR MET TYR PRO THR SER ILE          
SEQRES  29 E  397  GLU ALA ALA LYS VAL THR VAL ALA MET LYS GLY GLY ALA          
SEQRES  30 E  397  ALA TRP LEU GLU PHE ALA PRO GLY ASP LEU PRO MET VAL          
SEQRES  31 E  397  HIS SER GLN TYR ASN LEU LEU                                  
SEQRES   1 F  296  MET ILE LEU VAL ASN LYS GLU THR ARG VAL LEU VAL GLN          
SEQRES   2 F  296  GLY ILE THR GLY ARG GLU GLY GLN PHE HIS THR LYS GLN          
SEQRES   3 F  296  MET LEU SER TYR GLY THR LYS ILE VAL ALA GLY VAL THR          
SEQRES   4 F  296  PRO GLY LYS GLY GLY MET GLU VAL LEU GLY VAL PRO VAL          
SEQRES   5 F  296  TYR ASP THR VAL LYS GLU ALA VAL ALA HIS HIS GLU VAL          
SEQRES   6 F  296  ASP ALA SER ILE ILE PHE VAL PRO ALA PRO ALA ALA ALA          
SEQRES   7 F  296  ASP ALA ALA LEU GLU ALA ALA HIS ALA GLY ILE PRO LEU          
SEQRES   8 F  296  ILE VAL LEU ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 F  296  VAL ARG ALA VAL GLU GLU ILE LYS ALA LEU GLY SER ARG          
SEQRES  10 F  296  LEU ILE GLY GLY ASN CYS PRO GLY ILE ILE SER ALA GLU          
SEQRES  11 F  296  GLU THR LYS ILE GLY ILE MET PRO GLY HIS VAL PHE LYS          
SEQRES  12 F  296  ARG GLY ARG VAL GLY ILE ILE SER ARG SER GLY THR LEU          
SEQRES  13 F  296  THR TYR GLU ALA ALA ALA ALA LEU SER GLN ALA GLY LEU          
SEQRES  14 F  296  GLY THR THR THR THR VAL GLY ILE GLY GLY ASP PRO VAL          
SEQRES  15 F  296  ILE GLY THR THR PHE LYS ASP LEU LEU PRO LEU PHE ASN          
SEQRES  16 F  296  GLU ASP PRO GLU THR GLU ALA VAL VAL LEU ILE GLY GLU          
SEQRES  17 F  296  ILE GLY GLY SER ASP GLU GLU GLU ALA ALA ALA TRP VAL          
SEQRES  18 F  296  LYS ASP HIS MET LYS LYS PRO VAL VAL GLY PHE ILE GLY          
SEQRES  19 F  296  GLY ARG SER ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 F  296  GLY ALA ILE ILE MET GLY ASN VAL GLY THR PRO GLU SER          
SEQRES  21 F  296  LYS LEU ARG ALA PHE ALA GLU ALA GLY ILE PRO VAL ALA          
SEQRES  22 F  296  ASP THR ILE ASP GLU ILE VAL GLU LEU VAL LYS LYS ALA          
SEQRES  23 F  296  LEU GLY TRP ASN SER ARG PRO GLY ILE LEU                      
SEQRES   1 G  397  MET ASN LEU HIS GLU TYR GLN ALA LYS GLU ILE LEU ALA          
SEQRES   2 G  397  ARG TYR GLY VAL PRO VAL PRO PRO GLY LYS VAL ALA TYR          
SEQRES   3 G  397  THR PRO GLU GLU ALA LYS ARG ILE ALA GLU GLU PHE GLY          
SEQRES   4 G  397  LYS ARG VAL VAL ILE LYS ALA GLN VAL HIS VAL GLY GLY          
SEQRES   5 G  397  ARG GLY LYS ALA GLY GLY VAL LYS LEU ALA ASP THR PRO          
SEQRES   6 G  397  GLN GLU ALA TYR GLU LYS ALA GLN ALA ILE LEU GLY MET          
SEQRES   7 G  397  ASN ILE LYS GLY LEU THR VAL LYS LYS VAL LEU VAL ALA          
SEQRES   8 G  397  GLU ALA VAL ASP ILE ALA LYS GLU TYR TYR ALA GLY LEU          
SEQRES   9 G  397  ILE LEU ASP ARG ALA LYS LYS ARG VAL VAL LEU MET LEU          
SEQRES  10 G  397  SER LYS GLU GLY GLY VAL ASP ILE GLU GLU VAL ALA ALA          
SEQRES  11 G  397  GLU ARG PRO GLU ALA ILE HIS LYS PHE TRP ILE ASP PRO          
SEQRES  12 G  397  HIS LYS GLY PHE ARG PRO PHE GLU ALA ARG GLU MET VAL          
SEQRES  13 G  397  LYS ARG ALA GLY LEU GLU GLY ASN LEU ASN LYS LEU ALA          
SEQRES  14 G  397  GLN VAL LEU VAL ALA LEU TYR ARG ALA TYR GLU GLY VAL          
SEQRES  15 G  397  ASP ALA SER ILE ALA GLU ILE ASN PRO LEU VAL VAL THR          
SEQRES  16 G  397  THR ASP GLY GLY ILE VAL ALA ALA ASP ALA LYS ILE VAL          
SEQRES  17 G  397  LEU ASP ASP ASN ALA LEU PHE ARG HIS PRO ASP LEU ALA          
SEQRES  18 G  397  GLU LEU ARG GLU VAL GLU ALA GLU HIS PRO LEU GLU VAL          
SEQRES  19 G  397  GLU ALA SER ASN TYR GLY PHE ALA TYR VAL LYS LEU ASP          
SEQRES  20 G  397  GLY ASN ILE GLY ILE ILE GLY ASN GLY ALA GLY LEU VAL          
SEQRES  21 G  397  MET TYR THR LEU ASP LEU VAL ASN ARG VAL GLY GLY LYS          
SEQRES  22 G  397  PRO ALA ASN PHE LEU ASP ILE GLY GLY GLY ALA LYS ALA          
SEQRES  23 G  397  ASP VAL VAL TYR ASN ALA LEU LYS VAL VAL LEU LYS ASP          
SEQRES  24 G  397  PRO ASP VAL LYS GLY VAL PHE ILE ASN ILE PHE GLY GLY          
SEQRES  25 G  397  ILE THR ARG ALA ASP GLU VAL ALA LYS GLY VAL ILE ARG          
SEQRES  26 G  397  ALA LEU GLU GLU GLY LEU LEU THR LYS PRO VAL VAL MET          
SEQRES  27 G  397  ARG VAL ALA GLY THR ALA GLU GLU GLU ALA LYS LYS LEU          
SEQRES  28 G  397  LEU GLU GLY LYS PRO VAL TYR MET TYR PRO THR SER ILE          
SEQRES  29 G  397  GLU ALA ALA LYS VAL THR VAL ALA MET LYS GLY GLY ALA          
SEQRES  30 G  397  ALA TRP LEU GLU PHE ALA PRO GLY ASP LEU PRO MET VAL          
SEQRES  31 G  397  HIS SER GLN TYR ASN LEU LEU                                  
SEQRES   1 H  296  MET ILE LEU VAL ASN LYS GLU THR ARG VAL LEU VAL GLN          
SEQRES   2 H  296  GLY ILE THR GLY ARG GLU GLY GLN PHE HIS THR LYS GLN          
SEQRES   3 H  296  MET LEU SER TYR GLY THR LYS ILE VAL ALA GLY VAL THR          
SEQRES   4 H  296  PRO GLY LYS GLY GLY MET GLU VAL LEU GLY VAL PRO VAL          
SEQRES   5 H  296  TYR ASP THR VAL LYS GLU ALA VAL ALA HIS HIS GLU VAL          
SEQRES   6 H  296  ASP ALA SER ILE ILE PHE VAL PRO ALA PRO ALA ALA ALA          
SEQRES   7 H  296  ASP ALA ALA LEU GLU ALA ALA HIS ALA GLY ILE PRO LEU          
SEQRES   8 H  296  ILE VAL LEU ILE THR GLU GLY ILE PRO THR LEU ASP MET          
SEQRES   9 H  296  VAL ARG ALA VAL GLU GLU ILE LYS ALA LEU GLY SER ARG          
SEQRES  10 H  296  LEU ILE GLY GLY ASN CYS PRO GLY ILE ILE SER ALA GLU          
SEQRES  11 H  296  GLU THR LYS ILE GLY ILE MET PRO GLY HIS VAL PHE LYS          
SEQRES  12 H  296  ARG GLY ARG VAL GLY ILE ILE SER ARG SER GLY THR LEU          
SEQRES  13 H  296  THR TYR GLU ALA ALA ALA ALA LEU SER GLN ALA GLY LEU          
SEQRES  14 H  296  GLY THR THR THR THR VAL GLY ILE GLY GLY ASP PRO VAL          
SEQRES  15 H  296  ILE GLY THR THR PHE LYS ASP LEU LEU PRO LEU PHE ASN          
SEQRES  16 H  296  GLU ASP PRO GLU THR GLU ALA VAL VAL LEU ILE GLY GLU          
SEQRES  17 H  296  ILE GLY GLY SER ASP GLU GLU GLU ALA ALA ALA TRP VAL          
SEQRES  18 H  296  LYS ASP HIS MET LYS LYS PRO VAL VAL GLY PHE ILE GLY          
SEQRES  19 H  296  GLY ARG SER ALA PRO LYS GLY LYS ARG MET GLY HIS ALA          
SEQRES  20 H  296  GLY ALA ILE ILE MET GLY ASN VAL GLY THR PRO GLU SER          
SEQRES  21 H  296  LYS LEU ARG ALA PHE ALA GLU ALA GLY ILE PRO VAL ALA          
SEQRES  22 H  296  ASP THR ILE ASP GLU ILE VAL GLU LEU VAL LYS LYS ALA          
SEQRES  23 H  296  LEU GLY TRP ASN SER ARG PRO GLY ILE LEU                      
SEQRES   1 I  397  MET ASN LEU HIS GLU TYR GLN ALA LYS GLU ILE LEU ALA          
SEQRES   2 I  397  ARG TYR GLY VAL PRO VAL PRO PRO GLY LYS VAL ALA TYR          
SEQRES   3 I  397  THR PRO GLU GLU ALA LYS ARG ILE ALA GLU GLU PHE GLY          
SEQRES   4 I  397  LYS ARG VAL VAL ILE LYS ALA GLN VAL HIS VAL GLY GLY          
SEQRES   5 I  397  ARG GLY LYS ALA GLY GLY VAL LYS LEU ALA ASP THR PRO          
SEQRES   6 I  397  GLN GLU ALA TYR GLU LYS ALA GLN ALA ILE LEU GLY MET          
SEQRES   7 I  397  ASN ILE LYS GLY LEU THR VAL LYS LYS VAL LEU VAL ALA          
SEQRES   8 I  397  GLU ALA VAL ASP ILE ALA LYS GLU TYR TYR ALA GLY LEU          
SEQRES   9 I  397  ILE LEU ASP ARG ALA LYS LYS ARG VAL VAL LEU MET LEU          
SEQRES  10 I  397  SER LYS GLU GLY GLY VAL ASP ILE GLU GLU VAL ALA ALA          
SEQRES  11 I  397  GLU ARG PRO GLU ALA ILE HIS LYS PHE TRP ILE ASP PRO          
SEQRES  12 I  397  HIS LYS GLY PHE ARG PRO PHE GLU ALA ARG GLU MET VAL          
SEQRES  13 I  397  LYS ARG ALA GLY LEU GLU GLY ASN LEU ASN LYS LEU ALA          
SEQRES  14 I  397  GLN VAL LEU VAL ALA LEU TYR ARG ALA TYR GLU GLY VAL          
SEQRES  15 I  397  ASP ALA SER ILE ALA GLU ILE ASN PRO LEU VAL VAL THR          
SEQRES  16 I  397  THR ASP GLY GLY ILE VAL ALA ALA ASP ALA LYS ILE VAL          
SEQRES  17 I  397  LEU ASP ASP ASN ALA LEU PHE ARG HIS PRO ASP LEU ALA          
SEQRES  18 I  397  GLU LEU ARG GLU VAL GLU ALA GLU HIS PRO LEU GLU VAL          
SEQRES  19 I  397  GLU ALA SER ASN TYR GLY PHE ALA TYR VAL LYS LEU ASP          
SEQRES  20 I  397  GLY ASN ILE GLY ILE ILE GLY ASN GLY ALA GLY LEU VAL          
SEQRES  21 I  397  MET TYR THR LEU ASP LEU VAL ASN ARG VAL GLY GLY LYS          
SEQRES  22 I  397  PRO ALA ASN PHE LEU ASP ILE GLY GLY GLY ALA LYS ALA          
SEQRES  23 I  397  ASP VAL VAL TYR ASN ALA LEU LYS VAL VAL LEU LYS ASP          
SEQRES  24 I  397  PRO ASP VAL LYS GLY VAL PHE ILE ASN ILE PHE GLY GLY          
SEQRES  25 I  397  ILE THR ARG ALA ASP GLU VAL ALA LYS GLY VAL ILE ARG          
SEQRES  26 I  397  ALA LEU GLU GLU GLY LEU LEU THR LYS PRO VAL VAL MET          
SEQRES  27 I  397  ARG VAL ALA GLY THR ALA GLU GLU GLU ALA LYS LYS LEU          
SEQRES  28 I  397  LEU GLU GLY LYS PRO VAL TYR MET TYR PRO THR SER ILE          
SEQRES  29 I  397  GLU ALA ALA LYS VAL THR VAL ALA MET LYS GLY GLY ALA          
SEQRES  30 I  397  ALA TRP LEU GLU PHE ALA PRO GLY ASP LEU PRO MET VAL          
SEQRES  31 I  397  HIS SER GLN TYR ASN LEU LEU                                  
HET    GDP  B 398      28                                                       
HET     MN  B 399       1                                                       
HET    GDP  E 398      28                                                       
HET     MN  E 399       1                                                       
HET    GDP  G 398      28                                                       
HET     MN  G 399       1                                                       
HET    GDP  I 398      28                                                       
HET     MN  I 399       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   9  GDP    4(C10 H15 N5 O11 P2)                                         
FORMUL  10   MN    4(MN 2+)                                                     
FORMUL  17  HOH   *735(H2 O)                                                    
HELIX    1   1 GLY A   17  GLY A   31  1                                  15    
HELIX    2   2 THR A   55  HIS A   63  1                                   9    
HELIX    3   3 PRO A   73  ALA A   87  1                                  15    
HELIX    4   4 PRO A  100  GLY A  115  1                                  16    
HELIX    5   5 PRO A  138  PHE A  142  5                                   5    
HELIX    6   6 GLY A  154  ALA A  167  1                                  14    
HELIX    7   7 THR A  186  GLU A  196  1                                  11    
HELIX    8   8 SER A  212  MET A  225  1                                  14    
HELIX    9   9 THR A  257  ALA A  268  1                                  12    
HELIX   10  10 THR A  275  LEU A  287  1                                  13    
HELIX   11  11 HIS B    4  TYR B   15  1                                  12    
HELIX   12  12 THR B   27  GLY B   39  1                                  13    
HELIX   13  13 THR B   64  LEU B   76  1                                  13    
HELIX   14  14 ASP B  124  ARG B  132  1                                   9    
HELIX   15  15 PRO B  133  ILE B  136  5                                   4    
HELIX   16  16 ARG B  148  GLY B  160  1                                  13    
HELIX   17  17 ASN B  164  VAL B  182  1                                  19    
HELIX   18  18 ASP B  211  ARG B  216  5                                   6    
HELIX   19  19 HIS B  217  GLU B  222  1                                   6    
HELIX   20  20 LEU B  223  ALA B  228  1                                   6    
HELIX   21  21 HIS B  230  TYR B  239  1                                  10    
HELIX   22  22 GLY B  256  VAL B  270  1                                  15    
HELIX   23  23 LYS B  285  LYS B  298  1                                  14    
HELIX   24  24 ALA B  316  GLU B  328  1                                  13    
HELIX   25  25 ALA B  344  LEU B  352  1                                   9    
HELIX   26  26 THR B  362  MET B  373  1                                  12    
HELIX   27  27 GLY D   17  GLY D   31  1                                  15    
HELIX   28  28 THR D   55  HIS D   63  1                                   9    
HELIX   29  29 PRO D   73  ALA D   87  1                                  15    
HELIX   30  30 PRO D  100  LEU D  114  1                                  15    
HELIX   31  31 PRO D  138  PHE D  142  5                                   5    
HELIX   32  32 GLY D  154  ALA D  167  1                                  14    
HELIX   33  33 THR D  186  GLU D  196  1                                  11    
HELIX   34  34 SER D  212  MET D  225  1                                  14    
HELIX   35  35 THR D  257  ALA D  268  1                                  12    
HELIX   36  36 THR D  275  LEU D  287  1                                  13    
HELIX   37  37 HIS E    4  TYR E   15  1                                  12    
HELIX   38  38 THR E   27  GLY E   39  1                                  13    
HELIX   39  39 THR E   64  LEU E   76  1                                  13    
HELIX   40  40 ASP E  124  ARG E  132  1                                   9    
HELIX   41  41 PRO E  133  ILE E  136  5                                   4    
HELIX   42  42 ARG E  148  GLY E  160  1                                  13    
HELIX   43  43 ASN E  164  VAL E  182  1                                  19    
HELIX   44  44 ASP E  211  ARG E  216  5                                   6    
HELIX   45  45 HIS E  217  GLU E  222  1                                   6    
HELIX   46  46 LEU E  223  ALA E  228  1                                   6    
HELIX   47  47 HIS E  230  TYR E  239  1                                  10    
HELIX   48  48 GLY E  256  VAL E  270  1                                  15    
HELIX   49  49 LYS E  285  LYS E  298  1                                  14    
HELIX   50  50 ALA E  316  GLU E  328  1                                  13    
HELIX   51  51 ALA E  344  LYS E  350  1                                   7    
HELIX   52  52 THR E  362  ALA E  372  1                                  11    
HELIX   53  53 GLY F   17  GLY F   31  1                                  15    
HELIX   54  54 THR F   55  HIS F   63  1                                   9    
HELIX   55  55 PRO F   73  ALA F   87  1                                  15    
HELIX   56  56 PRO F  100  LEU F  114  1                                  15    
HELIX   57  57 PRO F  138  PHE F  142  5                                   5    
HELIX   58  58 GLY F  154  ALA F  167  1                                  14    
HELIX   59  59 THR F  186  GLU F  196  1                                  11    
HELIX   60  60 SER F  212  MET F  225  1                                  14    
HELIX   61  61 THR F  257  ALA F  268  1                                  12    
HELIX   62  62 THR F  275  LEU F  287  1                                  13    
HELIX   63  63 HIS G    4  TYR G   15  1                                  12    
HELIX   64  64 THR G   27  GLY G   39  1                                  13    
HELIX   65  65 THR G   64  LEU G   76  1                                  13    
HELIX   66  66 ASP G  124  ARG G  132  1                                   9    
HELIX   67  67 PRO G  133  ILE G  136  5                                   4    
HELIX   68  68 ARG G  148  GLY G  160  1                                  13    
HELIX   69  69 ASN G  164  VAL G  182  1                                  19    
HELIX   70  70 ASP G  211  ARG G  216  5                                   6    
HELIX   71  71 HIS G  217  GLU G  222  1                                   6    
HELIX   72  72 LEU G  223  ALA G  228  1                                   6    
HELIX   73  73 HIS G  230  TYR G  239  1                                  10    
HELIX   74  74 GLY G  256  VAL G  270  1                                  15    
HELIX   75  75 LYS G  285  LYS G  298  1                                  14    
HELIX   76  76 ALA G  316  GLU G  329  1                                  14    
HELIX   77  77 GLU G  345  LYS G  350  1                                   6    
HELIX   78  78 THR G  362  THR G  370  1                                   9    
HELIX   79  79 GLY H   17  GLY H   31  1                                  15    
HELIX   80  80 THR H   55  HIS H   63  1                                   9    
HELIX   81  81 PRO H   73  ALA H   87  1                                  15    
HELIX   82  82 PRO H  100  LEU H  114  1                                  15    
HELIX   83  83 PRO H  138  PHE H  142  5                                   5    
HELIX   84  84 GLY H  154  ALA H  167  1                                  14    
HELIX   85  85 THR H  186  GLU H  196  1                                  11    
HELIX   86  86 SER H  212  MET H  225  1                                  14    
HELIX   87  87 THR H  257  ALA H  268  1                                  12    
HELIX   88  88 THR H  275  LEU H  287  1                                  13    
HELIX   89  89 HIS I    4  TYR I   15  1                                  12    
HELIX   90  90 THR I   27  GLY I   39  1                                  13    
HELIX   91  91 THR I   64  LEU I   76  1                                  13    
HELIX   92  92 ASP I  124  ARG I  132  1                                   9    
HELIX   93  93 PRO I  133  ILE I  136  5                                   4    
HELIX   94  94 ARG I  148  GLY I  160  1                                  13    
HELIX   95  95 ASN I  164  VAL I  182  1                                  19    
HELIX   96  96 ASP I  211  ARG I  216  5                                   6    
HELIX   97  97 HIS I  217  GLU I  222  1                                   6    
HELIX   98  98 LEU I  223  ALA I  228  1                                   6    
HELIX   99  99 HIS I  230  TYR I  239  1                                  10    
HELIX  100 100 GLY I  256  VAL I  270  1                                  15    
HELIX  101 101 LYS I  285  LYS I  298  1                                  14    
HELIX  102 102 ALA I  316  GLU I  329  1                                  14    
HELIX  103 103 ALA I  344  LEU I  352  1                                   9    
HELIX  104 104 THR I  362  VAL I  371  1                                  10    
SHEET    1   A 7 GLU A  46  VAL A  47  0                                        
SHEET    2   A 7 VAL A  50  TYR A  53 -1  O  VAL A  50   N  VAL A  47           
SHEET    3   A 7 LYS A  33  VAL A  38  1  N  GLY A  37   O  TYR A  53           
SHEET    4   A 7 ARG A   9  GLN A  13  1  N  VAL A  10   O  LYS A  33           
SHEET    5   A 7 ALA A  67  ILE A  70  1  O  ALA A  67   N  LEU A  11           
SHEET    6   A 7 LEU A  91  LEU A  94  1  O  VAL A  93   N  SER A  68           
SHEET    7   A 7 ARG A 117  GLY A 120  1  O  ILE A 119   N  LEU A  94           
SHEET    1   B 6 THR A 132  GLY A 135  0                                        
SHEET    2   B 6 GLY A 125  SER A 128 -1  N  ILE A 126   O  ILE A 134           
SHEET    3   B 6 THR A 171  GLY A 176 -1  O  GLY A 176   N  GLY A 125           
SHEET    4   B 6 VAL A 147  SER A 151  1  N  ILE A 149   O  VAL A 175           
SHEET    5   B 6 ALA A 202  GLU A 208  1  O  ALA A 202   N  GLY A 148           
SHEET    6   B 6 VAL A 229  GLY A 234  1  O  PHE A 232   N  GLY A 207           
SHEET    1   C 4 GLY B  22  ALA B  25  0                                        
SHEET    2   C 4 VAL B  88  GLU B  92 -1  O  VAL B  88   N  ALA B  25           
SHEET    3   C 4 VAL B  42  ALA B  46 -1  N  LYS B  45   O  LEU B  89           
SHEET    4   C 4 VAL B  59  ALA B  62 -1  O  LYS B  60   N  ILE B  44           
SHEET    1   D 2 ASN B  79  ILE B  80  0                                        
SHEET    2   D 2 LEU B  83  THR B  84 -1  O  LEU B  83   N  ILE B  80           
SHEET    1   E 5 HIS B 137  TRP B 140  0                                        
SHEET    2   E 5 ARG B 112  SER B 118 -1  N  LEU B 117   O  HIS B 137           
SHEET    3   E 5 ILE B  96  ASP B 107 -1  N  ILE B 105   O  VAL B 114           
SHEET    4   E 5 ALA B 184  THR B 195 -1  O  LEU B 192   N  TYR B 100           
SHEET    5   E 5 ILE B 200  ALA B 202 -1  O  VAL B 201   N  VAL B 193           
SHEET    1   F 5 HIS B 137  TRP B 140  0                                        
SHEET    2   F 5 ARG B 112  SER B 118 -1  N  LEU B 117   O  HIS B 137           
SHEET    3   F 5 ILE B  96  ASP B 107 -1  N  ILE B 105   O  VAL B 114           
SHEET    4   F 5 ALA B 184  THR B 195 -1  O  LEU B 192   N  TYR B 100           
SHEET    5   F 5 LYS B 206  LEU B 209 -1  O  VAL B 208   N  SER B 185           
SHEET    1   G 2 ALA B 242  LYS B 245  0                                        
SHEET    2   G 2 ASN B 276  ASP B 279 -1  O  PHE B 277   N  VAL B 244           
SHEET    1   H 4 ILE B 250  GLY B 254  0                                        
SHEET    2   H 4 GLY B 304  ARG B 315  1  O  PHE B 306   N  GLY B 251           
SHEET    3   H 4 VAL B 336  THR B 343  1  O  ALA B 341   N  GLY B 311           
SHEET    4   H 4 VAL B 357  MET B 359  1  O  TYR B 358   N  MET B 338           
SHEET    1   I 7 GLU D  46  VAL D  47  0                                        
SHEET    2   I 7 VAL D  50  TYR D  53 -1  O  VAL D  50   N  VAL D  47           
SHEET    3   I 7 LYS D  33  VAL D  38  1  N  GLY D  37   O  TYR D  53           
SHEET    4   I 7 ARG D   9  GLN D  13  1  N  VAL D  10   O  LYS D  33           
SHEET    5   I 7 ALA D  67  ILE D  70  1  O  ALA D  67   N  LEU D  11           
SHEET    6   I 7 LEU D  91  LEU D  94  1  O  VAL D  93   N  SER D  68           
SHEET    7   I 7 ARG D 117  GLY D 120  1  O  ILE D 119   N  LEU D  94           
SHEET    1   J 6 THR D 132  GLY D 135  0                                        
SHEET    2   J 6 GLY D 125  SER D 128 -1  N  ILE D 126   O  ILE D 134           
SHEET    3   J 6 THR D 171  GLY D 176 -1  O  GLY D 176   N  GLY D 125           
SHEET    4   J 6 VAL D 147  SER D 151  1  N  ILE D 149   O  VAL D 175           
SHEET    5   J 6 ALA D 202  GLU D 208  1  O  ALA D 202   N  GLY D 148           
SHEET    6   J 6 VAL D 229  GLY D 234  1  O  PHE D 232   N  GLY D 207           
SHEET    1   K 4 GLY E  22  ALA E  25  0                                        
SHEET    2   K 4 VAL E  88  GLU E  92 -1  O  VAL E  88   N  ALA E  25           
SHEET    3   K 4 VAL E  42  ALA E  46 -1  N  LYS E  45   O  LEU E  89           
SHEET    4   K 4 VAL E  59  ALA E  62 -1  O  LYS E  60   N  ILE E  44           
SHEET    1   L 2 ASN E  79  ILE E  80  0                                        
SHEET    2   L 2 LEU E  83  THR E  84 -1  O  LEU E  83   N  ILE E  80           
SHEET    1   M 5 HIS E 137  TRP E 140  0                                        
SHEET    2   M 5 ARG E 112  SER E 118 -1  N  LEU E 117   O  HIS E 137           
SHEET    3   M 5 ILE E  96  ASP E 107 -1  N  ILE E 105   O  VAL E 114           
SHEET    4   M 5 ALA E 184  THR E 195 -1  O  LEU E 192   N  TYR E 100           
SHEET    5   M 5 ILE E 200  ALA E 202 -1  O  VAL E 201   N  VAL E 193           
SHEET    1   N 5 HIS E 137  TRP E 140  0                                        
SHEET    2   N 5 ARG E 112  SER E 118 -1  N  LEU E 117   O  HIS E 137           
SHEET    3   N 5 ILE E  96  ASP E 107 -1  N  ILE E 105   O  VAL E 114           
SHEET    4   N 5 ALA E 184  THR E 195 -1  O  LEU E 192   N  TYR E 100           
SHEET    5   N 5 LYS E 206  LEU E 209 -1  O  VAL E 208   N  SER E 185           
SHEET    1   O 2 ALA E 242  LYS E 245  0                                        
SHEET    2   O 2 ASN E 276  ASP E 279 -1  O  PHE E 277   N  VAL E 244           
SHEET    1   P 4 ILE E 250  GLY E 254  0                                        
SHEET    2   P 4 GLY E 304  ARG E 315  1  O  PHE E 306   N  GLY E 251           
SHEET    3   P 4 VAL E 336  THR E 343  1  O  ALA E 341   N  GLY E 311           
SHEET    4   P 4 VAL E 357  MET E 359  1  O  TYR E 358   N  MET E 338           
SHEET    1   Q 7 GLU F  46  VAL F  47  0                                        
SHEET    2   Q 7 VAL F  50  TYR F  53 -1  O  VAL F  50   N  VAL F  47           
SHEET    3   Q 7 LYS F  33  VAL F  38  1  N  GLY F  37   O  TYR F  53           
SHEET    4   Q 7 ARG F   9  GLN F  13  1  N  VAL F  10   O  LYS F  33           
SHEET    5   Q 7 ALA F  67  ILE F  70  1  O  ALA F  67   N  LEU F  11           
SHEET    6   Q 7 LEU F  91  LEU F  94  1  O  VAL F  93   N  SER F  68           
SHEET    7   Q 7 ARG F 117  GLY F 120  1  O  ILE F 119   N  LEU F  94           
SHEET    1   R 6 THR F 132  GLY F 135  0                                        
SHEET    2   R 6 GLY F 125  SER F 128 -1  N  ILE F 126   O  ILE F 134           
SHEET    3   R 6 THR F 171  GLY F 176 -1  O  GLY F 176   N  GLY F 125           
SHEET    4   R 6 VAL F 147  SER F 151  1  N  ILE F 149   O  VAL F 175           
SHEET    5   R 6 ALA F 202  GLU F 208  1  O  ALA F 202   N  GLY F 148           
SHEET    6   R 6 VAL F 229  GLY F 234  1  O  PHE F 232   N  GLY F 207           
SHEET    1   S 4 GLY G  22  ALA G  25  0                                        
SHEET    2   S 4 VAL G  88  GLU G  92 -1  O  VAL G  88   N  ALA G  25           
SHEET    3   S 4 VAL G  42  ALA G  46 -1  N  LYS G  45   O  LEU G  89           
SHEET    4   S 4 VAL G  59  ALA G  62 -1  O  LYS G  60   N  ILE G  44           
SHEET    1   T 2 ASN G  79  ILE G  80  0                                        
SHEET    2   T 2 LEU G  83  THR G  84 -1  O  LEU G  83   N  ILE G  80           
SHEET    1   U 5 HIS G 137  TRP G 140  0                                        
SHEET    2   U 5 ARG G 112  SER G 118 -1  N  LEU G 117   O  HIS G 137           
SHEET    3   U 5 ILE G  96  ASP G 107 -1  N  ILE G 105   O  VAL G 114           
SHEET    4   U 5 ALA G 184  THR G 195 -1  O  LEU G 192   N  TYR G 100           
SHEET    5   U 5 ILE G 200  ALA G 202 -1  O  VAL G 201   N  VAL G 193           
SHEET    1   V 5 HIS G 137  TRP G 140  0                                        
SHEET    2   V 5 ARG G 112  SER G 118 -1  N  LEU G 117   O  HIS G 137           
SHEET    3   V 5 ILE G  96  ASP G 107 -1  N  ILE G 105   O  VAL G 114           
SHEET    4   V 5 ALA G 184  THR G 195 -1  O  LEU G 192   N  TYR G 100           
SHEET    5   V 5 LYS G 206  LEU G 209 -1  O  VAL G 208   N  SER G 185           
SHEET    1   W 2 ALA G 242  LYS G 245  0                                        
SHEET    2   W 2 ASN G 276  ASP G 279 -1  O  PHE G 277   N  VAL G 244           
SHEET    1   X 4 ILE G 250  GLY G 254  0                                        
SHEET    2   X 4 GLY G 304  ARG G 315  1  O  PHE G 306   N  GLY G 251           
SHEET    3   X 4 VAL G 336  THR G 343  1  O  ALA G 341   N  GLY G 311           
SHEET    4   X 4 VAL G 357  MET G 359  1  O  TYR G 358   N  MET G 338           
SHEET    1   Y 7 GLU H  46  VAL H  47  0                                        
SHEET    2   Y 7 VAL H  50  TYR H  53 -1  O  VAL H  50   N  VAL H  47           
SHEET    3   Y 7 LYS H  33  VAL H  38  1  N  GLY H  37   O  TYR H  53           
SHEET    4   Y 7 ARG H   9  GLN H  13  1  N  VAL H  10   O  LYS H  33           
SHEET    5   Y 7 ALA H  67  ILE H  70  1  O  ALA H  67   N  LEU H  11           
SHEET    6   Y 7 LEU H  91  LEU H  94  1  O  VAL H  93   N  SER H  68           
SHEET    7   Y 7 ARG H 117  GLY H 120  1  O  ILE H 119   N  LEU H  94           
SHEET    1   Z 6 THR H 132  GLY H 135  0                                        
SHEET    2   Z 6 GLY H 125  SER H 128 -1  N  ILE H 126   O  ILE H 134           
SHEET    3   Z 6 THR H 171  GLY H 176 -1  O  THR H 174   N  ILE H 127           
SHEET    4   Z 6 VAL H 147  SER H 151  1  N  ILE H 149   O  VAL H 175           
SHEET    5   Z 6 ALA H 202  GLU H 208  1  O  ALA H 202   N  GLY H 148           
SHEET    6   Z 6 VAL H 229  GLY H 234  1  O  PHE H 232   N  GLY H 207           
SHEET    1  AA 4 GLY I  22  ALA I  25  0                                        
SHEET    2  AA 4 VAL I  88  GLU I  92 -1  O  VAL I  88   N  ALA I  25           
SHEET    3  AA 4 VAL I  42  ALA I  46 -1  N  LYS I  45   O  LEU I  89           
SHEET    4  AA 4 VAL I  59  ALA I  62 -1  O  LYS I  60   N  ILE I  44           
SHEET    1  AB 2 ASN I  79  ILE I  80  0                                        
SHEET    2  AB 2 LEU I  83  THR I  84 -1  O  LEU I  83   N  ILE I  80           
SHEET    1  AC 5 HIS I 137  TRP I 140  0                                        
SHEET    2  AC 5 ARG I 112  SER I 118 -1  N  LEU I 117   O  HIS I 137           
SHEET    3  AC 5 ILE I  96  ASP I 107 -1  N  ILE I 105   O  VAL I 114           
SHEET    4  AC 5 ALA I 184  THR I 195 -1  O  LEU I 192   N  TYR I 100           
SHEET    5  AC 5 ILE I 200  ALA I 202 -1  O  VAL I 201   N  VAL I 193           
SHEET    1  AD 5 HIS I 137  TRP I 140  0                                        
SHEET    2  AD 5 ARG I 112  SER I 118 -1  N  LEU I 117   O  HIS I 137           
SHEET    3  AD 5 ILE I  96  ASP I 107 -1  N  ILE I 105   O  VAL I 114           
SHEET    4  AD 5 ALA I 184  THR I 195 -1  O  LEU I 192   N  TYR I 100           
SHEET    5  AD 5 LYS I 206  LEU I 209 -1  O  VAL I 208   N  SER I 185           
SHEET    1  AE 2 ALA I 242  LYS I 245  0                                        
SHEET    2  AE 2 ASN I 276  ASP I 279 -1  O  PHE I 277   N  VAL I 244           
SHEET    1  AF 4 ILE I 250  GLY I 254  0                                        
SHEET    2  AF 4 GLY I 304  ARG I 315  1  O  PHE I 306   N  GLY I 251           
SHEET    3  AF 4 VAL I 336  THR I 343  1  O  ALA I 341   N  GLY I 311           
SHEET    4  AF 4 VAL I 357  MET I 359  1  O  TYR I 358   N  MET I 338           
LINK         O2A GDP B 398                MN    MN B 399     1555   1555  2.21  
LINK         O3B GDP E 398                MN    MN E 399     1555   1555  2.24  
LINK         O3B GDP G 398                MN    MN G 399     1555   1555  2.24  
LINK         O3B GDP I 398                MN    MN I 399     1555   1555  2.26  
LINK         O   ASN E 190                MN    MN E 399     1555   1555  2.30  
LINK         O   ASN G 190                MN    MN G 399     1555   1555  2.34  
LINK         O   ASN I 190                MN    MN I 399     1555   1555  2.36  
LINK         O2A GDP I 398                MN    MN I 399     1555   1555  2.39  
LINK         O2A GDP E 398                MN    MN E 399     1555   1555  2.43  
LINK         O2A GDP G 398                MN    MN G 399     1555   1555  2.45  
LINK         O   ASN B 190                MN    MN B 399     1555   1555  2.51  
LINK         O3B GDP B 398                MN    MN B 399     1555   1555  2.56  
LINK         OD2 ASP G 204                MN    MN G 399     1555   1555  2.58  
LINK         OD2 ASP B 204                MN    MN B 399     1555   1555  2.60  
CISPEP   1 GLY A  120    GLY A  121          0         3.28                     
CISPEP   2 ASN B  190    PRO B  191          0         7.39                     
CISPEP   3 GLY D  120    GLY D  121          0         2.68                     
CISPEP   4 ASN E  190    PRO E  191          0         6.84                     
CISPEP   5 GLY F  120    GLY F  121          0         5.38                     
CISPEP   6 ASN G  190    PRO G  191          0         6.78                     
CISPEP   7 GLY H  120    GLY H  121          0         4.24                     
CISPEP   8 ASN I  190    PRO I  191          0         6.88                     
SITE     1 AC1 16 VAL B  43  LYS B  45  GLY B  52  ARG B  53                    
SITE     2 AC1 16 GLY B  54  ALA B  93  VAL B  94  ILE B  96                    
SITE     3 AC1 16 GLU B  99  GLY B 122  ASN B 190  ASP B 204                    
SITE     4 AC1 16  MN B 399  HOH B 414  HOH B 422  HOH B 449                    
SITE     1 AC2  3 ASN B 190  ASP B 204  GDP B 398                               
SITE     1 AC3 14 VAL E  43  LYS E  45  GLY E  52  ARG E  53                    
SITE     2 AC3 14 GLY E  54  ALA E  93  VAL E  94  ILE E  96                    
SITE     3 AC3 14 GLU E  99  ASN E 190  ASP E 204   MN E 399                    
SITE     4 AC3 14 HOH E 685  HOH E 732                                          
SITE     1 AC4  3 ASN E 190  ASP E 204  GDP E 398                               
SITE     1 AC5 15 VAL G  43  LYS G  45  GLY G  52  ARG G  53                    
SITE     2 AC5 15 GLY G  54  ALA G  93  VAL G  94  ILE G  96                    
SITE     3 AC5 15 GLU G  99  ASN G 190  ASP G 204   MN G 399                    
SITE     4 AC5 15 HOH G 402  HOH G 733  HOH G 736                               
SITE     1 AC6  3 ASN G 190  ASP G 204  GDP G 398                               
SITE     1 AC7 14 VAL I  43  LYS I  45  GLY I  52  ARG I  53                    
SITE     2 AC7 14 GLY I  54  ALA I  93  VAL I  94  ILE I  96                    
SITE     3 AC7 14 GLU I  99  ASN I 190  ASP I 204   MN I 399                    
SITE     4 AC7 14 HOH I 734  HOH I 735                                          
SITE     1 AC8  3 ASN I 190  ASP I 204  GDP I 398                               
CRYST1  261.700  126.800  110.600  90.00 112.76  90.00 C 1 2 1      16          
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      0.003821  0.000000  0.001603        0.00000                         
SCALE2      0.000000  0.007886  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009805        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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