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Database: PDB
Entry: 1FOE
LinkDB: 1FOE
Original site: 1FOE 
HEADER    SIGNALING PROTEIN, IMMUNE SYSTEM/SIGNALI27-AUG-00   1FOE              
TITLE     CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH THE GUANINE                 
TITLE    2 NUCLEOTIDE EXCHANGE REGION OF TIAM1                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: T-LYMPHOMA INVASION AND METASTASIS INDUCING                
COMPND   3 PROTEIN 1;                                                           
COMPND   4 CHAIN: A, C, E, G;                                                   
COMPND   5 FRAGMENT: RESIDUES 1033 TO 1406 FROM MURINE T-LYMPHOMA               
COMPND   6 INVASION AND METASTASIS FACTOR 1, PLECKSTRIN HOMOLOGY                
COMPND   7 DOMAIN;                                                              
COMPND   8 SYNONYM: TIAM1 PROTEIN, T-CELL LYMPHOMA INVASION AND                 
COMPND   9 METASTASIS 1;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 OTHER_DETAILS: ALA-MET-GLY CLONING ARTIFACT ADDED TO N-              
COMPND  13 TERMINUS;                                                            
COMPND  14 MOL_ID: 2;                                                           
COMPND  15 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE;                  
COMPND  16 CHAIN: B, D, F, H;                                                   
COMPND  17 FRAGMENT: RESIDUES 1 TO 177 FROM HUMAN RAC1;                         
COMPND  18 SYNONYM: P21-RAC1, RAS-LIKE PROTEIN TC25, RAC1 P21(SMALL)            
COMPND  19 GTP-BINDING PROTEIN;                                                 
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPROEXHTA;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET-15B                                   
KEYWDS    DBL HOMOLOGY DOMAIN, PLECKSTRIN HOMOLOGY DOMAIN, GTPASE,              
KEYWDS   2 GUANINE NUCLEOTIDE EXCHANGE FACTOR, SIGNALING PROTEIN,               
KEYWDS   3 IMMUNE SYSTEM/SIGNALING PROTEIN COMPLEX                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.K.WORTHYLAKE,K.L.ROSSMAN,J.SONDEK                                   
REVDAT   2   24-FEB-09 1FOE    1       VERSN                                    
REVDAT   1   17-JAN-01 1FOE    0                                                
JRNL        AUTH   D.K.WORTHYLAKE,K.L.ROSSMAN,J.SONDEK                          
JRNL        TITL   CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH THE                
JRNL        TITL 2 GUANINE NUCLEOTIDE EXCHANGE REGION OF TIAM1.                 
JRNL        REF    NATURE                        V. 408   682 2000              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   11130063                                                     
JRNL        DOI    10.1038/35047014                                             
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 80511                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.262                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4051                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 17461                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 63.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED MAXIMUM LIKELIHOOD TARGET            
REMARK   3  FUNCTION IN CNS                                                     
REMARK   4                                                                      
REMARK   4 1FOE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011769.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-AUG-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9729,0.9787,0.9724               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 80441                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.8                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LI2SO4, MES, GLYCEROL, PH      
REMARK 280  6.0, VAPOR DIFFUSION, TEMPERATURE 277.0K                            
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       93.47500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.63500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       93.47500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       74.63500            
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, 7                                     
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: THE BIOLOGICAL ASSEMBLY IS A HETERODIMER COMPOSED OF A       
REMARK 300 TIAM1 DBL/PLECKSTRIN ELEMENT (CHAINS A,C,E,G) IN COMPLEX WITH A      
REMARK 300 RAC1 MOLECULE (CHAINS B,D,F,H). THERE ARE 4 HETERODIMERS IN THE      
REMARK 300 CRYSTAL ASYMMETRIC UNIT                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 21680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 99880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -175.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H, C, D, E, 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 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 52470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, H                            
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: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 52340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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     ALA A  1030                                                      
REMARK 465     MSE A  1031                                                      
REMARK 465     GLY A  1032                                                      
REMARK 465     ARG A  1033                                                      
REMARK 465     LEU A  1402                                                      
REMARK 465     LEU A  1403                                                      
REMARK 465     LYS A  1404                                                      
REMARK 465     THR A  1405                                                      
REMARK 465     GLU A  1406                                                      
REMARK 465     ALA C  1030                                                      
REMARK 465     MSE C  1031                                                      
REMARK 465     GLY C  1032                                                      
REMARK 465     ARG C  1033                                                      
REMARK 465     GLN C  1034                                                      
REMARK 465     LEU C  1035                                                      
REMARK 465     LEU C  1402                                                      
REMARK 465     LEU C  1403                                                      
REMARK 465     LYS C  1404                                                      
REMARK 465     THR C  1405                                                      
REMARK 465     GLU C  1406                                                      
REMARK 465     ALA E  1030                                                      
REMARK 465     MSE E  1031                                                      
REMARK 465     GLY E  1032                                                      
REMARK 465     ARG E  1033                                                      
REMARK 465     GLN E  1034                                                      
REMARK 465     LEU E  1402                                                      
REMARK 465     LEU E  1403                                                      
REMARK 465     LYS E  1404                                                      
REMARK 465     THR E  1405                                                      
REMARK 465     GLU E  1406                                                      
REMARK 465     ALA G  1030                                                      
REMARK 465     MSE G  1031                                                      
REMARK 465     GLY G  1032                                                      
REMARK 465     ARG G  1033                                                      
REMARK 465     GLN G  1034                                                      
REMARK 465     LEU G  1402                                                      
REMARK 465     LEU G  1403                                                      
REMARK 465     LYS G  1404                                                      
REMARK 465     THR G  1405                                                      
REMARK 465     GLU G  1406                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     THR A 1253                                                       
REMARK 475     GLY A 1254                                                       
REMARK 475     GLU A 1255                                                       
REMARK 475     LYS A 1256                                                       
REMARK 475     LYS A 1257                                                       
REMARK 475     GLU A 1258                                                       
REMARK 475     ASP A 1306                                                       
REMARK 475     GLY A 1307                                                       
REMARK 475     SER A 1308                                                       
REMARK 475     LYS A 1309                                                       
REMARK 475     GLN A 1310                                                       
REMARK 475     LYS A 1311                                                       
REMARK 475     LYS A 1312                                                       
REMARK 475     LYS A 1313                                                       
REMARK 475     LEU A 1314                                                       
REMARK 475     VAL A 1315                                                       
REMARK 475     GLY A 1316                                                       
REMARK 475     SER A 1317                                                       
REMARK 475     HIS A 1318                                                       
REMARK 475     ARG A 1319                                                       
REMARK 475     LEU A 1320                                                       
REMARK 475     SER A 1321                                                       
REMARK 475     ILE A 1322                                                       
REMARK 475     TYR A 1323                                                       
REMARK 475     GLU A 1324                                                       
REMARK 475     GLU A 1325                                                       
REMARK 475     TRP A 1326                                                       
REMARK 475     ASP A 1327                                                       
REMARK 475     PRO A 1328                                                       
REMARK 475     PHE A 1329                                                       
REMARK 475     ARG A 1330                                                       
REMARK 475     THR C 1253                                                       
REMARK 475     GLY C 1254                                                       
REMARK 475     GLU C 1255                                                       
REMARK 475     LYS C 1256                                                       
REMARK 475     LYS C 1257                                                       
REMARK 475     GLU C 1258                                                       
REMARK 475     SER C 1308                                                       
REMARK 475     LYS C 1309                                                       
REMARK 475     GLN C 1310                                                       
REMARK 475     LYS C 1311                                                       
REMARK 475     LYS C 1312                                                       
REMARK 475     LYS C 1313                                                       
REMARK 475     LEU C 1314                                                       
REMARK 475     VAL C 1315                                                       
REMARK 475     GLY C 1316                                                       
REMARK 475     SER C 1317                                                       
REMARK 475     HIS C 1318                                                       
REMARK 475     ARG C 1319                                                       
REMARK 475     LEU C 1320                                                       
REMARK 475     SER C 1321                                                       
REMARK 475     ILE C 1322                                                       
REMARK 475     TYR C 1323                                                       
REMARK 475     GLU C 1324                                                       
REMARK 475     GLU C 1325                                                       
REMARK 475     TRP C 1326                                                       
REMARK 475     THR E 1253                                                       
REMARK 475     GLY E 1254                                                       
REMARK 475     GLU E 1255                                                       
REMARK 475     LYS E 1256                                                       
REMARK 475     LYS E 1257                                                       
REMARK 475     GLU E 1258                                                       
REMARK 475     ASP E 1306                                                       
REMARK 475     GLY E 1307                                                       
REMARK 475     SER E 1308                                                       
REMARK 475     LYS E 1309                                                       
REMARK 475     GLN E 1310                                                       
REMARK 475     LYS E 1311                                                       
REMARK 475     LYS E 1312                                                       
REMARK 475     LYS E 1313                                                       
REMARK 475     LEU E 1314                                                       
REMARK 475     VAL E 1315                                                       
REMARK 475     GLY E 1316                                                       
REMARK 475     SER E 1317                                                       
REMARK 475     HIS E 1318                                                       
REMARK 475     ARG E 1319                                                       
REMARK 475     LEU E 1320                                                       
REMARK 475     SER E 1321                                                       
REMARK 475     ILE E 1322                                                       
REMARK 475     TYR E 1323                                                       
REMARK 475     GLU E 1324                                                       
REMARK 475     GLU E 1325                                                       
REMARK 475     TRP E 1326                                                       
REMARK 475     ASP E 1327                                                       
REMARK 475     PRO E 1328                                                       
REMARK 475     PHE E 1329                                                       
REMARK 475     ARG E 1330                                                       
REMARK 475     THR G 1253                                                       
REMARK 475     GLY G 1254                                                       
REMARK 475     GLU G 1255                                                       
REMARK 475     LYS G 1256                                                       
REMARK 475     LYS G 1257                                                       
REMARK 475     GLU G 1258                                                       
REMARK 475     LYS G 1309                                                       
REMARK 475     GLN G 1310                                                       
REMARK 475     LYS G 1311                                                       
REMARK 475     LYS G 1312                                                       
REMARK 475     LYS G 1313                                                       
REMARK 475     LEU G 1314                                                       
REMARK 475     VAL G 1315                                                       
REMARK 475     GLY G 1316                                                       
REMARK 475     SER G 1317                                                       
REMARK 475     HIS G 1318                                                       
REMARK 475     ARG G 1319                                                       
REMARK 475     LEU G 1320                                                       
REMARK 475     SER G 1321                                                       
REMARK 475     ILE G 1322                                                       
REMARK 475     TYR G 1323                                                       
REMARK 475     GLU G 1324                                                       
REMARK 475     GLU G 1325                                                       
REMARK 475     TRP G 1326                                                       
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     LYS A 1057   CG    CD    CE    NZ                                
REMARK 480     LYS A 1072   CG    CD    CE    NZ                                
REMARK 480     THR A 1074   OG1   CG2                                           
REMARK 480     GLU A 1113   CG    CD    OE1   OE2                               
REMARK 480     LYS A 1114   CG    CD    CE    NZ                                
REMARK 480     LYS A 1158   CG    CD    CE    NZ                                
REMARK 480     THR A 1161   OG1   CG2                                           
REMARK 480     ASP A 1162   CG    OD1   OD2                                     
REMARK 480     THR A 1163   OG1   CG2                                           
REMARK 480     ARG A 1175   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS A 1226   CE    NZ                                            
REMARK 480     GLN A 1247   CG    CD    OE1   NE2                               
REMARK 480     LEU A 1282   CG    CD1   CD2                                     
REMARK 480     LYS A 1284   CG    CD    CE    NZ                                
REMARK 480     LYS A 1305   CG    CD    CE    NZ                                
REMARK 480     GLU A 1338   CG    CD    OE1   OE2                               
REMARK 480     SER A 1347   OG                                                  
REMARK 480     ASP A 1349   CG    OD1   OD2                                     
REMARK 480     GLU A 1351   CG    CD    OE1   OE2                               
REMARK 480     ASN A 1353   CG    OD1   ND2                                     
REMARK 480     LYS A 1362   CG    CD    CE    NZ                                
REMARK 480     GLU A 1364   CG    CD    OE1   OE2                               
REMARK 480     ARG A 1383   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG A 1395   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS A 1397   CG    CD    CE    NZ                                
REMARK 480     HIS A 1398   CG    ND1   CD2   CE1   NE2                         
REMARK 480     ARG A 1399   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG A 1400   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     GLN A 1401   CG    CD    OE1   NE2                               
REMARK 480     MET B   45   CG    SD    CE                                      
REMARK 480     ASP B  124   CG    OD1   OD2                                     
REMARK 480     GLU B  127   CG    CD    OE1   OE2                               
REMARK 480     GLU B  131   CG    CD    OE1   OE2                               
REMARK 480     LYS C 1057   CG    CD    CE    NZ                                
REMARK 480     LYS C 1072   CG    CD    CE    NZ                                
REMARK 480     THR C 1074   OG1   CG2                                           
REMARK 480     GLU C 1113   CG    CD    OE1   OE2                               
REMARK 480     LYS C 1114   CG    CD    CE    NZ                                
REMARK 480     LYS C 1158   CG    CD    CE    NZ                                
REMARK 480     THR C 1161   OG1   CG2                                           
REMARK 480     ASP C 1162   CG    OD1   OD2                                     
REMARK 480     THR C 1163   OG1   CG2                                           
REMARK 480     ARG C 1175   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS C 1226   CE    NZ                                            
REMARK 480     LYS C 1284   CG    CD    CE    NZ                                
REMARK 480     GLU C 1338   CG    CD    OE1   OE2                               
REMARK 480     SER C 1347   OG                                                  
REMARK 480     ASP C 1349   CG    OD1   OD2                                     
REMARK 480     GLU C 1351   CG    CD    OE1   OE2                               
REMARK 480     ASN C 1353   CG    OD1   ND2                                     
REMARK 480     LYS C 1362   CG    CD    CE    NZ                                
REMARK 480     GLU C 1364   CG    CD    OE1   OE2                               
REMARK 480     ARG C 1383   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG C 1395   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS C 1397   CG    CD    CE    NZ                                
REMARK 480     HIS C 1398   CG    ND1   CD2   CE1   NE2                         
REMARK 480     ARG C 1399   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG C 1400   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     GLN C 1401   CG    CD    OE1   NE2                               
REMARK 480     MET D   45   CG    SD    CE                                      
REMARK 480     ASP D  124   CG    OD1   OD2                                     
REMARK 480     GLU D  127   CG    CD    OE1   OE2                               
REMARK 480     GLU D  131   CG    CD    OE1   OE2                               
REMARK 480     LYS E 1057   CG    CD    CE    NZ                                
REMARK 480     LYS E 1072   CG    CD    CE    NZ                                
REMARK 480     THR E 1074   OG1   CG2                                           
REMARK 480     GLU E 1113   CG    CD    OE1   OE2                               
REMARK 480     LYS E 1114   CG    CD    CE    NZ                                
REMARK 480     LYS E 1158   CG    CD    CE    NZ                                
REMARK 480     THR E 1161   OG1   CG2                                           
REMARK 480     ASP E 1162   CG    OD1   OD2                                     
REMARK 480     THR E 1163   OG1   CG2                                           
REMARK 480     ARG E 1175   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS E 1226   CE    NZ                                            
REMARK 480     GLN E 1247   CG    CD    OE1   NE2                               
REMARK 480     LEU E 1282   CG    CD1   CD2                                     
REMARK 480     LYS E 1284   CG    CD    CE    NZ                                
REMARK 480     LYS E 1305   CG    CD    CE    NZ                                
REMARK 480     GLU E 1338   CG    CD    OE1   OE2                               
REMARK 480     SER E 1347   OG                                                  
REMARK 480     ASP E 1349   CG    OD1   OD2                                     
REMARK 480     GLU E 1351   CG    CD    OE1   OE2                               
REMARK 480     ASN E 1353   CG    OD1   ND2                                     
REMARK 480     LYS E 1362   CG    CD    CE    NZ                                
REMARK 480     GLU E 1364   CG    CD    OE1   OE2                               
REMARK 480     ARG E 1383   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG E 1395   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS E 1397   CG    CD    CE    NZ                                
REMARK 480     HIS E 1398   CG    ND1   CD2   CE1   NE2                         
REMARK 480     ARG E 1399   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG E 1400   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     GLN E 1401   CG    CD    OE1   NE2                               
REMARK 480     MET F   45   CG    SD    CE                                      
REMARK 480     ASP F  124   CG    OD1   OD2                                     
REMARK 480     GLU F  127   CG    CD    OE1   OE2                               
REMARK 480     GLU F  131   CG    CD    OE1   OE2                               
REMARK 480     LYS G 1057   CG    CD    CE    NZ                                
REMARK 480     LYS G 1072   CG    CD    CE    NZ                                
REMARK 480     THR G 1074   OG1   CG2                                           
REMARK 480     GLU G 1113   CG    CD    OE1   OE2                               
REMARK 480     LYS G 1114   CG    CD    CE    NZ                                
REMARK 480     LYS G 1158   CG    CD    CE    NZ                                
REMARK 480     THR G 1161   OG1   CG2                                           
REMARK 480     ASP G 1162   CG    OD1   OD2                                     
REMARK 480     THR G 1163   OG1   CG2                                           
REMARK 480     ARG G 1175   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS G 1226   CE    NZ                                            
REMARK 480     GLN G 1247   CG    CD    OE1   NE2                               
REMARK 480     LYS G 1284   CG    CD    CE    NZ                                
REMARK 480     GLU G 1338   CG    CD    OE1   OE2                               
REMARK 480     SER G 1347   OG                                                  
REMARK 480     ASP G 1349   CG    OD1   OD2                                     
REMARK 480     GLU G 1351   CG    CD    OE1   OE2                               
REMARK 480     ASN G 1353   CG    OD1   ND2                                     
REMARK 480     LYS G 1362   CG    CD    CE    NZ                                
REMARK 480     GLU G 1364   CG    CD    OE1   OE2                               
REMARK 480     ARG G 1383   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG G 1395   CD    NE    CZ    NH1   NH2                         
REMARK 480     LYS G 1397   CG    CD    CE    NZ                                
REMARK 480     HIS G 1398   CG    ND1   CD2   CE1   NE2                         
REMARK 480     ARG G 1399   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ARG G 1400   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     GLN G 1401   CG    CD    OE1   NE2                               
REMARK 480     MET H   45   CG    SD    CE                                      
REMARK 480     ASP H  124   CG    OD1   OD2                                     
REMARK 480     GLU H  127   CG    CD    OE1   OE2                               
REMARK 480     GLU H  131   CG    CD    OE1   OE2                               
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 F   139     OD1  ASN H   107     2657     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ILE B   4   CB  -  CA  -  C   ANGL. DEV. = -15.9 DEGREES          
REMARK 500    ILE B   4   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    LYS B   5   N   -  CA  -  CB  ANGL. DEV. = -24.9 DEGREES          
REMARK 500    ILE D   4   CB  -  CA  -  C   ANGL. DEV. = -16.0 DEGREES          
REMARK 500    ILE D   4   N   -  CA  -  C   ANGL. DEV. = -17.6 DEGREES          
REMARK 500    LYS D   5   N   -  CA  -  CB  ANGL. DEV. = -24.0 DEGREES          
REMARK 500    ILE F   4   CB  -  CA  -  C   ANGL. DEV. = -15.6 DEGREES          
REMARK 500    ILE F   4   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    LYS F   5   N   -  CA  -  CB  ANGL. DEV. = -23.8 DEGREES          
REMARK 500    ILE H   4   CB  -  CA  -  C   ANGL. DEV. = -15.7 DEGREES          
REMARK 500    ILE H   4   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LYS H   5   N   -  CA  -  CB  ANGL. DEV. = -24.0 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    LYS A1072       46.19    -77.33                                   
REMARK 500    PHE A1085      -81.51    -59.77                                   
REMARK 500    ASN A1087       22.09     32.23                                   
REMARK 500    LEU A1108        0.14    -63.94                                   
REMARK 500    THR A1161      -67.46    -99.79                                   
REMARK 500    ASN A1173       73.49   -116.83                                   
REMARK 500    ARG A1175       -7.02    -54.25                                   
REMARK 500    SER A1179       -3.53    -59.59                                   
REMARK 500    LEU A1186       -1.73    -59.69                                   
REMARK 500    GLU A1251        3.41     58.45                                   
REMARK 500    GLN A1252       87.08    -58.58                                   
REMARK 500    THR A1253       83.38     -8.41                                   
REMARK 500    LYS A1256       53.43    -98.49                                   
REMARK 500    LYS A1257       80.61     64.66                                   
REMARK 500    VAL A1259      -63.67   -105.53                                   
REMARK 500    ASP A1261       99.31    153.30                                   
REMARK 500    ASN A1277       58.68   -116.72                                   
REMARK 500    ALA A1299      169.43    177.83                                   
REMARK 500    LYS A1305      -96.52    -98.56                                   
REMARK 500    ASP A1306       88.44     58.00                                   
REMARK 500    SER A1308       18.81   -150.31                                   
REMARK 500    LYS A1312       99.59     59.08                                   
REMARK 500    VAL A1315      142.23   -170.14                                   
REMARK 500    SER A1317      -91.44   -108.01                                   
REMARK 500    HIS A1318      -94.92     58.02                                   
REMARK 500    ARG A1319      -24.62   -148.33                                   
REMARK 500    ILE A1322      -84.94     60.92                                   
REMARK 500    TYR A1323     -176.55    -67.35                                   
REMARK 500    GLU A1324      156.25     64.08                                   
REMARK 500    GLU A1325       77.38     59.76                                   
REMARK 500    PRO A1328      -71.29    -54.82                                   
REMARK 500    ARG A1330      -97.84   -123.78                                   
REMARK 500    ASP A1349       55.33    -98.02                                   
REMARK 500    ALA A1350      171.98    -53.14                                   
REMARK 500    GLU A1351       -2.23     73.30                                   
REMARK 500    VAL A1361      151.75    -45.49                                   
REMARK 500    GLU A1366      -27.40     69.13                                   
REMARK 500    ARG A1399      -71.41    -51.05                                   
REMARK 500    ASP B  11      149.11    -32.40                                   
REMARK 500    TYR B  23      -72.29    -59.74                                   
REMARK 500    PRO B  34      152.48    -49.78                                   
REMARK 500    ASP B  65      -14.28    -47.84                                   
REMARK 500    PHE B  82      143.12   -172.74                                   
REMARK 500    LYS B  96      -72.49   -121.54                                   
REMARK 500    LYS C1072       45.62    -76.63                                   
REMARK 500    PHE C1085      -81.74    -60.02                                   
REMARK 500    ASN C1087       22.75     33.18                                   
REMARK 500    LEU C1108        0.81    -64.30                                   
REMARK 500    ALA C1136      -39.47    -39.20                                   
REMARK 500    THR C1161      -67.13    -99.69                                   
REMARK 500    ASN C1173       73.46   -117.43                                   
REMARK 500    ARG C1175       -6.53    -55.11                                   
REMARK 500    LEU C1186       -0.81    -58.75                                   
REMARK 500    GLU C1251        2.61     57.89                                   
REMARK 500    GLN C1252       87.07    -56.93                                   
REMARK 500    THR C1253       83.28     -8.33                                   
REMARK 500    LYS C1256       53.50    -98.50                                   
REMARK 500    LYS C1257       80.51     64.59                                   
REMARK 500    VAL C1259      -67.09   -105.18                                   
REMARK 500    ASP C1261       98.27    153.90                                   
REMARK 500    ASN C1277       60.19   -115.84                                   
REMARK 500    ALA C1299      170.20    179.05                                   
REMARK 500    SER C1308      -68.09   -156.01                                   
REMARK 500    LYS C1311       97.00     61.65                                   
REMARK 500    LYS C1312     -101.31     49.35                                   
REMARK 500    LYS C1313     -175.48   -170.06                                   
REMARK 500    ARG C1319      -75.39   -101.26                                   
REMARK 500    GLU C1325       37.62     37.69                                   
REMARK 500    ASP C1327      114.63   -169.94                                   
REMARK 500    ASP C1349       55.02    -98.78                                   
REMARK 500    ALA C1350      171.68    -53.41                                   
REMARK 500    GLU C1351       -2.75     73.40                                   
REMARK 500    VAL C1361      150.97    -43.84                                   
REMARK 500    GLU C1366      -28.00     69.18                                   
REMARK 500    LYS C1397       49.18    -79.66                                   
REMARK 500    ARG C1400      -61.30   -125.10                                   
REMARK 500    ASP D  11      150.76    -33.19                                   
REMARK 500    TYR D  23      -73.31    -58.19                                   
REMARK 500    ASP D  65      -13.85    -47.57                                   
REMARK 500    PHE D  82      142.53   -174.62                                   
REMARK 500    LYS D  96      -75.21   -122.53                                   
REMARK 500    LYS E1072       45.30    -76.24                                   
REMARK 500    PHE E1085      -81.29    -59.13                                   
REMARK 500    ASN E1087       21.51     33.16                                   
REMARK 500    LEU E1108        0.35    -64.56                                   
REMARK 500    THR E1161      -67.72    -99.21                                   
REMARK 500    ASN E1173       73.16   -116.71                                   
REMARK 500    ARG E1175       -6.48    -54.90                                   
REMARK 500    SER E1179       -3.07    -59.76                                   
REMARK 500    LEU E1186       -1.40    -59.59                                   
REMARK 500    GLU E1251        6.02     58.53                                   
REMARK 500    GLN E1252       88.03    -60.92                                   
REMARK 500    THR E1253       83.31     -8.96                                   
REMARK 500    LYS E1256       53.55    -98.70                                   
REMARK 500    LYS E1257       80.51     64.63                                   
REMARK 500    VAL E1259      -63.58   -105.47                                   
REMARK 500    ASP E1261       99.90    156.16                                   
REMARK 500    ASN E1277       60.04   -116.55                                   
REMARK 500    ALA E1299      169.77    178.12                                   
REMARK 500    LYS E1305      -83.97    -51.21                                   
REMARK 500    ASP E1306      123.65     60.59                                   
REMARK 500    LYS E1312       35.70    -78.08                                   
REMARK 500    HIS E1318      -96.84     56.92                                   
REMARK 500    SER E1321       99.67   -172.45                                   
REMARK 500    GLU E1325       89.15     54.27                                   
REMARK 500    ASP E1327      141.01     65.03                                   
REMARK 500    ARG E1330      -99.41   -111.74                                   
REMARK 500    ASP E1349       54.82    -97.69                                   
REMARK 500    ALA E1350      172.08    -52.38                                   
REMARK 500    GLU E1351       -2.45     73.11                                   
REMARK 500    VAL E1361      150.99    -45.64                                   
REMARK 500    GLU E1366      -27.57     69.30                                   
REMARK 500    ARG E1400        4.29    -65.92                                   
REMARK 500    ASP F  11      149.89    -34.00                                   
REMARK 500    ALA F  13       36.28     71.17                                   
REMARK 500    TYR F  23      -72.40    -58.57                                   
REMARK 500    PRO F  34      151.30    -49.62                                   
REMARK 500    ASP F  65      -14.82    -49.00                                   
REMARK 500    PHE F  82      142.40   -177.61                                   
REMARK 500    LYS F  96      -74.11   -122.40                                   
REMARK 500    LYS G1072       44.86    -78.05                                   
REMARK 500    PHE G1085      -81.92    -58.47                                   
REMARK 500    ASN G1087       20.75     32.54                                   
REMARK 500    LEU G1108        1.97    -64.74                                   
REMARK 500    VAL G1157       20.19    -75.37                                   
REMARK 500    THR G1161      -67.65    -98.93                                   
REMARK 500    ASN G1173       72.77   -116.26                                   
REMARK 500    ARG G1175       -5.87    -55.97                                   
REMARK 500    GLU G1251        2.92     57.52                                   
REMARK 500    GLN G1252       88.16    -58.14                                   
REMARK 500    THR G1253       83.13     -8.88                                   
REMARK 500    LYS G1256       53.47    -98.53                                   
REMARK 500    LYS G1257       80.75     64.66                                   
REMARK 500    VAL G1259      -65.93   -105.93                                   
REMARK 500    ALA G1260       72.52     43.22                                   
REMARK 500    ASP G1261       98.99    154.30                                   
REMARK 500    ASN G1277       60.19   -116.25                                   
REMARK 500    ALA G1299      168.67    177.87                                   
REMARK 500    SER G1308     -165.41   -110.35                                   
REMARK 500    LYS G1309      -89.41   -112.69                                   
REMARK 500    LYS G1311       89.53     57.54                                   
REMARK 500    HIS G1318     -159.66     56.65                                   
REMARK 500    LEU G1320     -159.86     56.53                                   
REMARK 500    TYR G1323      -16.06   -159.44                                   
REMARK 500    GLU G1324      -95.86     51.22                                   
REMARK 500    GLU G1325      -85.50   -169.28                                   
REMARK 500    TRP G1326      -15.59     65.14                                   
REMARK 500    ASP G1349       55.71    -98.17                                   
REMARK 500    ALA G1350      172.15    -53.80                                   
REMARK 500    GLU G1351       -2.83     73.19                                   
REMARK 500    VAL G1361      151.35    -44.69                                   
REMARK 500    GLU G1366      -27.39     70.37                                   
REMARK 500    ARG G1399        5.16    -59.62                                   
REMARK 500    ARG G1400      -40.39   -131.20                                   
REMARK 500    ASP H  11      148.54    -34.13                                   
REMARK 500    TYR H  23      -72.90    -57.42                                   
REMARK 500    ASP H  65      -16.55    -48.87                                   
REMARK 500    PHE H  82      142.22   -173.66                                   
REMARK 500    LYS H  96      -74.74   -124.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4001                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4002                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 4003                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 4004                
DBREF  1FOE A 1030  1406  UNP    Q60610   TIAM1_MOUSE   1030   1406             
DBREF  1FOE C 1030  1406  UNP    Q60610   TIAM1_MOUSE   1030   1406             
DBREF  1FOE E 1030  1406  UNP    Q60610   TIAM1_MOUSE   1030   1406             
DBREF  1FOE G 1030  1406  UNP    Q60610   TIAM1_MOUSE   1030   1406             
DBREF  1FOE B    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  1FOE D    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  1FOE F    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  1FOE H    1   177  UNP    P63000   RAC1_HUMAN       1    177             
SEQADV 1FOE MSE A 1031  UNP  Q60610    THR  1031 MODIFIED RESIDUE               
SEQADV 1FOE GLY A 1032  UNP  Q60610    THR  1032 CLONING ARTIFACT               
SEQADV 1FOE MSE A 1063  UNP  Q60610    MET  1063 MODIFIED RESIDUE               
SEQADV 1FOE MSE A 1091  UNP  Q60610    MET  1091 MODIFIED RESIDUE               
SEQADV 1FOE MSE A 1224  UNP  Q60610    MET  1224 MODIFIED RESIDUE               
SEQADV 1FOE MSE A 1234  UNP  Q60610    MET  1234 MODIFIED RESIDUE               
SEQADV 1FOE MSE A 1264  UNP  Q60610    MET  1264 MODIFIED RESIDUE               
SEQADV 1FOE MSE A 1334  UNP  Q60610    MET  1334 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1031  UNP  Q60610    THR  1031 MODIFIED RESIDUE               
SEQADV 1FOE GLY C 1032  UNP  Q60610    THR  1032 CLONING ARTIFACT               
SEQADV 1FOE MSE C 1063  UNP  Q60610    MET  1063 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1091  UNP  Q60610    MET  1091 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1224  UNP  Q60610    MET  1224 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1234  UNP  Q60610    MET  1234 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1264  UNP  Q60610    MET  1264 MODIFIED RESIDUE               
SEQADV 1FOE MSE C 1334  UNP  Q60610    MET  1334 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1031  UNP  Q60610    THR  1031 MODIFIED RESIDUE               
SEQADV 1FOE GLY E 1032  UNP  Q60610    THR  1032 CLONING ARTIFACT               
SEQADV 1FOE MSE E 1063  UNP  Q60610    MET  1063 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1091  UNP  Q60610    MET  1091 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1224  UNP  Q60610    MET  1224 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1234  UNP  Q60610    MET  1234 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1264  UNP  Q60610    MET  1264 MODIFIED RESIDUE               
SEQADV 1FOE MSE E 1334  UNP  Q60610    MET  1334 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1031  UNP  Q60610    THR  1031 MODIFIED RESIDUE               
SEQADV 1FOE GLY G 1032  UNP  Q60610    THR  1032 CLONING ARTIFACT               
SEQADV 1FOE MSE G 1063  UNP  Q60610    MET  1063 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1091  UNP  Q60610    MET  1091 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1224  UNP  Q60610    MET  1224 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1234  UNP  Q60610    MET  1234 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1264  UNP  Q60610    MET  1264 MODIFIED RESIDUE               
SEQADV 1FOE MSE G 1334  UNP  Q60610    MET  1334 MODIFIED RESIDUE               
SEQRES   1 A  377  ALA MSE GLY ARG GLN LEU SER ASP ALA ASP LYS LEU ARG          
SEQRES   2 A  377  LYS VAL ILE CYS GLU LEU LEU GLU THR GLU ARG THR TYR          
SEQRES   3 A  377  VAL LYS ASP LEU ASN CYS LEU MSE GLU ARG TYR LEU LYS          
SEQRES   4 A  377  PRO LEU GLN LYS GLU THR PHE LEU THR GLN ASP GLU LEU          
SEQRES   5 A  377  ASP VAL LEU PHE GLY ASN LEU THR GLU MSE VAL GLU PHE          
SEQRES   6 A  377  GLN VAL GLU PHE LEU LYS THR LEU GLU ASP GLY VAL ARG          
SEQRES   7 A  377  LEU VAL PRO ASP LEU GLU LYS LEU GLU LYS VAL ASP GLN          
SEQRES   8 A  377  PHE LYS LYS VAL LEU PHE SER LEU GLY GLY SER PHE LEU          
SEQRES   9 A  377  TYR TYR ALA ASP ARG PHE LYS LEU TYR SER ALA PHE CYS          
SEQRES  10 A  377  ALA SER HIS THR LYS VAL PRO LYS VAL LEU VAL LYS ALA          
SEQRES  11 A  377  LYS THR ASP THR ALA PHE LYS ALA PHE LEU ASP ALA GLN          
SEQRES  12 A  377  ASN PRO ARG GLN GLN HIS SER SER THR LEU GLU SER TYR          
SEQRES  13 A  377  LEU ILE LYS PRO ILE GLN ARG VAL LEU LYS TYR PRO LEU          
SEQRES  14 A  377  LEU LEU ARG GLU LEU PHE ALA LEU THR ASP ALA GLU SER          
SEQRES  15 A  377  GLU GLU HIS TYR HIS LEU ASP VAL ALA ILE LYS THR MSE          
SEQRES  16 A  377  ASN LYS VAL ALA SER HIS ILE ASN GLU MSE GLN LYS ILE          
SEQRES  17 A  377  HIS GLU GLU PHE GLY ALA VAL PHE ASP GLN LEU ILE ALA          
SEQRES  18 A  377  GLU GLN THR GLY GLU LYS LYS GLU VAL ALA ASP LEU SER          
SEQRES  19 A  377  MSE GLY ASP LEU LEU LEU HIS THR SER VAL ILE TRP LEU          
SEQRES  20 A  377  ASN PRO PRO ALA SER LEU GLY LYS TRP LYS LYS GLU PRO          
SEQRES  21 A  377  GLU LEU ALA ALA PHE VAL PHE LYS THR ALA VAL VAL LEU          
SEQRES  22 A  377  VAL TYR LYS ASP GLY SER LYS GLN LYS LYS LYS LEU VAL          
SEQRES  23 A  377  GLY SER HIS ARG LEU SER ILE TYR GLU GLU TRP ASP PRO          
SEQRES  24 A  377  PHE ARG PHE ARG HIS MSE ILE PRO THR GLU ALA LEU GLN          
SEQRES  25 A  377  VAL ARG ALA LEU PRO SER ALA ASP ALA GLU ALA ASN ALA          
SEQRES  26 A  377  VAL CYS GLU ILE VAL HIS VAL LYS SER GLU SER GLU GLY          
SEQRES  27 A  377  ARG PRO GLU ARG VAL PHE HIS LEU CYS CYS SER SER PRO          
SEQRES  28 A  377  GLU SER ARG LYS ASP PHE LEU LYS SER VAL HIS SER ILE          
SEQRES  29 A  377  LEU ARG ASP LYS HIS ARG ARG GLN LEU LEU LYS THR GLU          
SEQRES   1 B  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 B  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 B  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 B  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 B  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 B  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 B  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 B  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 B  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 B  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 B  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 B  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 B  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 B  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
SEQRES   1 C  377  ALA MSE GLY ARG GLN LEU SER ASP ALA ASP LYS LEU ARG          
SEQRES   2 C  377  LYS VAL ILE CYS GLU LEU LEU GLU THR GLU ARG THR TYR          
SEQRES   3 C  377  VAL LYS ASP LEU ASN CYS LEU MSE GLU ARG TYR LEU LYS          
SEQRES   4 C  377  PRO LEU GLN LYS GLU THR PHE LEU THR GLN ASP GLU LEU          
SEQRES   5 C  377  ASP VAL LEU PHE GLY ASN LEU THR GLU MSE VAL GLU PHE          
SEQRES   6 C  377  GLN VAL GLU PHE LEU LYS THR LEU GLU ASP GLY VAL ARG          
SEQRES   7 C  377  LEU VAL PRO ASP LEU GLU LYS LEU GLU LYS VAL ASP GLN          
SEQRES   8 C  377  PHE LYS LYS VAL LEU PHE SER LEU GLY GLY SER PHE LEU          
SEQRES   9 C  377  TYR TYR ALA ASP ARG PHE LYS LEU TYR SER ALA PHE CYS          
SEQRES  10 C  377  ALA SER HIS THR LYS VAL PRO LYS VAL LEU VAL LYS ALA          
SEQRES  11 C  377  LYS THR ASP THR ALA PHE LYS ALA PHE LEU ASP ALA GLN          
SEQRES  12 C  377  ASN PRO ARG GLN GLN HIS SER SER THR LEU GLU SER TYR          
SEQRES  13 C  377  LEU ILE LYS PRO ILE GLN ARG VAL LEU LYS TYR PRO LEU          
SEQRES  14 C  377  LEU LEU ARG GLU LEU PHE ALA LEU THR ASP ALA GLU SER          
SEQRES  15 C  377  GLU GLU HIS TYR HIS LEU ASP VAL ALA ILE LYS THR MSE          
SEQRES  16 C  377  ASN LYS VAL ALA SER HIS ILE ASN GLU MSE GLN LYS ILE          
SEQRES  17 C  377  HIS GLU GLU PHE GLY ALA VAL PHE ASP GLN LEU ILE ALA          
SEQRES  18 C  377  GLU GLN THR GLY GLU LYS LYS GLU VAL ALA ASP LEU SER          
SEQRES  19 C  377  MSE GLY ASP LEU LEU LEU HIS THR SER VAL ILE TRP LEU          
SEQRES  20 C  377  ASN PRO PRO ALA SER LEU GLY LYS TRP LYS LYS GLU PRO          
SEQRES  21 C  377  GLU LEU ALA ALA PHE VAL PHE LYS THR ALA VAL VAL LEU          
SEQRES  22 C  377  VAL TYR LYS ASP GLY SER LYS GLN LYS LYS LYS LEU VAL          
SEQRES  23 C  377  GLY SER HIS ARG LEU SER ILE TYR GLU GLU TRP ASP PRO          
SEQRES  24 C  377  PHE ARG PHE ARG HIS MSE ILE PRO THR GLU ALA LEU GLN          
SEQRES  25 C  377  VAL ARG ALA LEU PRO SER ALA ASP ALA GLU ALA ASN ALA          
SEQRES  26 C  377  VAL CYS GLU ILE VAL HIS VAL LYS SER GLU SER GLU GLY          
SEQRES  27 C  377  ARG PRO GLU ARG VAL PHE HIS LEU CYS CYS SER SER PRO          
SEQRES  28 C  377  GLU SER ARG LYS ASP PHE LEU LYS SER VAL HIS SER ILE          
SEQRES  29 C  377  LEU ARG ASP LYS HIS ARG ARG GLN LEU LEU LYS THR GLU          
SEQRES   1 D  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 D  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 D  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 D  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 D  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 D  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 D  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 D  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 D  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 D  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 D  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 D  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 D  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 D  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
SEQRES   1 E  377  ALA MSE GLY ARG GLN LEU SER ASP ALA ASP LYS LEU ARG          
SEQRES   2 E  377  LYS VAL ILE CYS GLU LEU LEU GLU THR GLU ARG THR TYR          
SEQRES   3 E  377  VAL LYS ASP LEU ASN CYS LEU MSE GLU ARG TYR LEU LYS          
SEQRES   4 E  377  PRO LEU GLN LYS GLU THR PHE LEU THR GLN ASP GLU LEU          
SEQRES   5 E  377  ASP VAL LEU PHE GLY ASN LEU THR GLU MSE VAL GLU PHE          
SEQRES   6 E  377  GLN VAL GLU PHE LEU LYS THR LEU GLU ASP GLY VAL ARG          
SEQRES   7 E  377  LEU VAL PRO ASP LEU GLU LYS LEU GLU LYS VAL ASP GLN          
SEQRES   8 E  377  PHE LYS LYS VAL LEU PHE SER LEU GLY GLY SER PHE LEU          
SEQRES   9 E  377  TYR TYR ALA ASP ARG PHE LYS LEU TYR SER ALA PHE CYS          
SEQRES  10 E  377  ALA SER HIS THR LYS VAL PRO LYS VAL LEU VAL LYS ALA          
SEQRES  11 E  377  LYS THR ASP THR ALA PHE LYS ALA PHE LEU ASP ALA GLN          
SEQRES  12 E  377  ASN PRO ARG GLN GLN HIS SER SER THR LEU GLU SER TYR          
SEQRES  13 E  377  LEU ILE LYS PRO ILE GLN ARG VAL LEU LYS TYR PRO LEU          
SEQRES  14 E  377  LEU LEU ARG GLU LEU PHE ALA LEU THR ASP ALA GLU SER          
SEQRES  15 E  377  GLU GLU HIS TYR HIS LEU ASP VAL ALA ILE LYS THR MSE          
SEQRES  16 E  377  ASN LYS VAL ALA SER HIS ILE ASN GLU MSE GLN LYS ILE          
SEQRES  17 E  377  HIS GLU GLU PHE GLY ALA VAL PHE ASP GLN LEU ILE ALA          
SEQRES  18 E  377  GLU GLN THR GLY GLU LYS LYS GLU VAL ALA ASP LEU SER          
SEQRES  19 E  377  MSE GLY ASP LEU LEU LEU HIS THR SER VAL ILE TRP LEU          
SEQRES  20 E  377  ASN PRO PRO ALA SER LEU GLY LYS TRP LYS LYS GLU PRO          
SEQRES  21 E  377  GLU LEU ALA ALA PHE VAL PHE LYS THR ALA VAL VAL LEU          
SEQRES  22 E  377  VAL TYR LYS ASP GLY SER LYS GLN LYS LYS LYS LEU VAL          
SEQRES  23 E  377  GLY SER HIS ARG LEU SER ILE TYR GLU GLU TRP ASP PRO          
SEQRES  24 E  377  PHE ARG PHE ARG HIS MSE ILE PRO THR GLU ALA LEU GLN          
SEQRES  25 E  377  VAL ARG ALA LEU PRO SER ALA ASP ALA GLU ALA ASN ALA          
SEQRES  26 E  377  VAL CYS GLU ILE VAL HIS VAL LYS SER GLU SER GLU GLY          
SEQRES  27 E  377  ARG PRO GLU ARG VAL PHE HIS LEU CYS CYS SER SER PRO          
SEQRES  28 E  377  GLU SER ARG LYS ASP PHE LEU LYS SER VAL HIS SER ILE          
SEQRES  29 E  377  LEU ARG ASP LYS HIS ARG ARG GLN LEU LEU LYS THR GLU          
SEQRES   1 F  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 F  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 F  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 F  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 F  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 F  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 F  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 F  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 F  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 F  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 F  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 F  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 F  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 F  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
SEQRES   1 G  377  ALA MSE GLY ARG GLN LEU SER ASP ALA ASP LYS LEU ARG          
SEQRES   2 G  377  LYS VAL ILE CYS GLU LEU LEU GLU THR GLU ARG THR TYR          
SEQRES   3 G  377  VAL LYS ASP LEU ASN CYS LEU MSE GLU ARG TYR LEU LYS          
SEQRES   4 G  377  PRO LEU GLN LYS GLU THR PHE LEU THR GLN ASP GLU LEU          
SEQRES   5 G  377  ASP VAL LEU PHE GLY ASN LEU THR GLU MSE VAL GLU PHE          
SEQRES   6 G  377  GLN VAL GLU PHE LEU LYS THR LEU GLU ASP GLY VAL ARG          
SEQRES   7 G  377  LEU VAL PRO ASP LEU GLU LYS LEU GLU LYS VAL ASP GLN          
SEQRES   8 G  377  PHE LYS LYS VAL LEU PHE SER LEU GLY GLY SER PHE LEU          
SEQRES   9 G  377  TYR TYR ALA ASP ARG PHE LYS LEU TYR SER ALA PHE CYS          
SEQRES  10 G  377  ALA SER HIS THR LYS VAL PRO LYS VAL LEU VAL LYS ALA          
SEQRES  11 G  377  LYS THR ASP THR ALA PHE LYS ALA PHE LEU ASP ALA GLN          
SEQRES  12 G  377  ASN PRO ARG GLN GLN HIS SER SER THR LEU GLU SER TYR          
SEQRES  13 G  377  LEU ILE LYS PRO ILE GLN ARG VAL LEU LYS TYR PRO LEU          
SEQRES  14 G  377  LEU LEU ARG GLU LEU PHE ALA LEU THR ASP ALA GLU SER          
SEQRES  15 G  377  GLU GLU HIS TYR HIS LEU ASP VAL ALA ILE LYS THR MSE          
SEQRES  16 G  377  ASN LYS VAL ALA SER HIS ILE ASN GLU MSE GLN LYS ILE          
SEQRES  17 G  377  HIS GLU GLU PHE GLY ALA VAL PHE ASP GLN LEU ILE ALA          
SEQRES  18 G  377  GLU GLN THR GLY GLU LYS LYS GLU VAL ALA ASP LEU SER          
SEQRES  19 G  377  MSE GLY ASP LEU LEU LEU HIS THR SER VAL ILE TRP LEU          
SEQRES  20 G  377  ASN PRO PRO ALA SER LEU GLY LYS TRP LYS LYS GLU PRO          
SEQRES  21 G  377  GLU LEU ALA ALA PHE VAL PHE LYS THR ALA VAL VAL LEU          
SEQRES  22 G  377  VAL TYR LYS ASP GLY SER LYS GLN LYS LYS LYS LEU VAL          
SEQRES  23 G  377  GLY SER HIS ARG LEU SER ILE TYR GLU GLU TRP ASP PRO          
SEQRES  24 G  377  PHE ARG PHE ARG HIS MSE ILE PRO THR GLU ALA LEU GLN          
SEQRES  25 G  377  VAL ARG ALA LEU PRO SER ALA ASP ALA GLU ALA ASN ALA          
SEQRES  26 G  377  VAL CYS GLU ILE VAL HIS VAL LYS SER GLU SER GLU GLY          
SEQRES  27 G  377  ARG PRO GLU ARG VAL PHE HIS LEU CYS CYS SER SER PRO          
SEQRES  28 G  377  GLU SER ARG LYS ASP PHE LEU LYS SER VAL HIS SER ILE          
SEQRES  29 G  377  LEU ARG ASP LYS HIS ARG ARG GLN LEU LEU LYS THR GLU          
SEQRES   1 H  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 H  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 H  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 H  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 H  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 H  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 H  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 H  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 H  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 H  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 H  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 H  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 H  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 H  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
MODRES 1FOE MSE A 1063  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE A 1091  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE A 1224  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE A 1234  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE A 1264  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE A 1334  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1063  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1091  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1224  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1234  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1264  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE C 1334  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1063  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1091  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1224  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1234  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1264  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE E 1334  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1063  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1091  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1224  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1234  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1264  MET  SELENOMETHIONINE                                   
MODRES 1FOE MSE G 1334  MET  SELENOMETHIONINE                                   
HET    MSE  A1063       8                                                       
HET    MSE  A1091       8                                                       
HET    MSE  A1224       8                                                       
HET    MSE  A1234       8                                                       
HET    MSE  A1264       8                                                       
HET    MSE  A1334       8                                                       
HET    MSE  C1063       8                                                       
HET    MSE  C1091       8                                                       
HET    MSE  C1224       8                                                       
HET    MSE  C1234       8                                                       
HET    MSE  C1264       8                                                       
HET    MSE  C1334       8                                                       
HET    MSE  E1063       8                                                       
HET    MSE  E1091       8                                                       
HET    MSE  E1224       8                                                       
HET    MSE  E1234       8                                                       
HET    MSE  E1264       8                                                       
HET    MSE  E1334       8                                                       
HET    MSE  G1063       8                                                       
HET    MSE  G1091       8                                                       
HET    MSE  G1224       8                                                       
HET    MSE  G1234       8                                                       
HET    MSE  G1264       8                                                       
HET    MSE  G1334       8                                                       
HET    SO4  B4001       5                                                       
HET    SO4  D4002       5                                                       
HET    SO4  F4003       5                                                       
HET    SO4  H4004       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    24(C5 H11 N O2 SE)                                           
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  13  HOH   *93(H2 O)                                                     
HELIX    1   1 SER A 1036  TYR A 1066  1                                  31    
HELIX    2   2 TYR A 1066  LYS A 1072  1                                   7    
HELIX    3   3 THR A 1077  GLY A 1086  1                                  10    
HELIX    4   4 ASN A 1087  ARG A 1107  1                                  21    
HELIX    5   5 ASP A 1111  LEU A 1115  5                                   5    
HELIX    6   6 LYS A 1117  GLN A 1120  5                                   4    
HELIX    7   7 PHE A 1121  ALA A 1136  1                                  16    
HELIX    8   8 ASP A 1137  LYS A 1140  5                                   4    
HELIX    9   9 LEU A 1141  HIS A 1149  1                                   9    
HELIX   10  10 LYS A 1151  VAL A 1157  1                                   7    
HELIX   11  11 ASP A 1162  ASN A 1173  1                                  12    
HELIX   12  12 GLN A 1177  SER A 1180  5                                   4    
HELIX   13  13 THR A 1181  LEU A 1186  1                                   6    
HELIX   14  14 ILE A 1187  LEU A 1194  1                                   8    
HELIX   15  15 LYS A 1195  LEU A 1206  1                                  12    
HELIX   16  16 SER A 1211  GLY A 1242  1                                  32    
HELIX   17  17 PHE A 1241  ALA A 1250  1                                  10    
HELIX   18  18 SER A 1263  GLY A 1265  5                                   3    
HELIX   19  19 PRO A 1279  LYS A 1284  1                                   6    
HELIX   20  20 GLU A 1364  GLY A 1367  5                                   4    
HELIX   21  21 SER A 1379  GLN A 1401  1                                  23    
HELIX   22  22 GLY B   15  ASN B   26  1                                  12    
HELIX   23  23 LEU B   67  SER B   71  5                                   5    
HELIX   24  24 SER B   86  LYS B   96  1                                  11    
HELIX   25  25 LYS B   96  CYS B  105  1                                  10    
HELIX   26  26 LYS B  116  ARG B  120  5                                   5    
HELIX   27  27 ASP B  122  LYS B  132  1                                  11    
HELIX   28  28 THR B  138  ILE B  149  1                                  12    
HELIX   29  29 GLY B  164  LEU B  177  1                                  14    
HELIX   30  30 SER C 1036  TYR C 1066  1                                  31    
HELIX   31  31 TYR C 1066  LYS C 1072  1                                   7    
HELIX   32  32 THR C 1077  GLY C 1086  1                                  10    
HELIX   33  33 ASN C 1087  ARG C 1107  1                                  21    
HELIX   34  34 ASP C 1111  LEU C 1115  5                                   5    
HELIX   35  35 LYS C 1117  GLN C 1120  5                                   4    
HELIX   36  36 PHE C 1121  ALA C 1136  1                                  16    
HELIX   37  37 ASP C 1137  LYS C 1140  5                                   4    
HELIX   38  38 LEU C 1141  HIS C 1149  1                                   9    
HELIX   39  39 LYS C 1151  VAL C 1157  1                                   7    
HELIX   40  40 ASP C 1162  ASN C 1173  1                                  12    
HELIX   41  41 GLN C 1177  SER C 1180  5                                   4    
HELIX   42  42 THR C 1181  LEU C 1186  1                                   6    
HELIX   43  43 ILE C 1187  LEU C 1194  1                                   8    
HELIX   44  44 LYS C 1195  LEU C 1206  1                                  12    
HELIX   45  45 SER C 1211  GLY C 1242  1                                  32    
HELIX   46  46 PHE C 1241  ALA C 1250  1                                  10    
HELIX   47  47 PRO C 1279  LYS C 1284  1                                   6    
HELIX   48  48 GLU C 1364  GLY C 1367  5                                   4    
HELIX   49  49 SER C 1379  LYS C 1397  1                                  19    
HELIX   50  50 GLY D   15  ASN D   26  1                                  12    
HELIX   51  51 LEU D   67  SER D   71  5                                   5    
HELIX   52  52 SER D   86  LYS D   96  1                                  11    
HELIX   53  53 LYS D   96  CYS D  105  1                                  10    
HELIX   54  54 LYS D  116  ARG D  120  5                                   5    
HELIX   55  55 ASP D  122  GLU D  131  1                                  10    
HELIX   56  56 THR D  138  ILE D  149  1                                  12    
HELIX   57  57 GLY D  164  LEU D  177  1                                  14    
HELIX   58  58 SER E 1036  TYR E 1066  1                                  31    
HELIX   59  59 TYR E 1066  LYS E 1072  1                                   7    
HELIX   60  60 THR E 1077  GLY E 1086  1                                  10    
HELIX   61  61 ASN E 1087  ARG E 1107  1                                  21    
HELIX   62  62 ASP E 1111  LEU E 1115  5                                   5    
HELIX   63  63 LYS E 1117  GLN E 1120  5                                   4    
HELIX   64  64 PHE E 1121  ALA E 1136  1                                  16    
HELIX   65  65 ASP E 1137  LYS E 1140  5                                   4    
HELIX   66  66 LEU E 1141  HIS E 1149  1                                   9    
HELIX   67  67 LYS E 1151  VAL E 1157  1                                   7    
HELIX   68  68 ASP E 1162  ASN E 1173  1                                  12    
HELIX   69  69 GLN E 1177  SER E 1180  5                                   4    
HELIX   70  70 THR E 1181  LEU E 1186  1                                   6    
HELIX   71  71 ILE E 1187  LEU E 1206  1                                  20    
HELIX   72  72 SER E 1211  GLY E 1242  1                                  32    
HELIX   73  73 PHE E 1241  ALA E 1250  1                                  10    
HELIX   74  74 SER E 1263  GLY E 1265  5                                   3    
HELIX   75  75 PRO E 1279  LYS E 1284  1                                   6    
HELIX   76  76 GLU E 1364  GLY E 1367  5                                   4    
HELIX   77  77 SER E 1379  GLN E 1401  1                                  23    
HELIX   78  78 GLY F   15  ASN F   26  1                                  12    
HELIX   79  79 LEU F   67  SER F   71  5                                   5    
HELIX   80  80 SER F   86  LYS F   96  1                                  11    
HELIX   81  81 LYS F   96  CYS F  105  1                                  10    
HELIX   82  82 LYS F  116  ARG F  120  5                                   5    
HELIX   83  83 ASP F  122  LYS F  132  1                                  11    
HELIX   84  84 THR F  138  ILE F  149  1                                  12    
HELIX   85  85 GLY F  164  LEU F  177  1                                  14    
HELIX   86  86 SER G 1036  TYR G 1066  1                                  31    
HELIX   87  87 TYR G 1066  LYS G 1072  1                                   7    
HELIX   88  88 THR G 1077  GLY G 1086  1                                  10    
HELIX   89  89 ASN G 1087  ARG G 1107  1                                  21    
HELIX   90  90 ASP G 1111  LEU G 1115  5                                   5    
HELIX   91  91 LYS G 1117  GLN G 1120  5                                   4    
HELIX   92  92 PHE G 1121  ALA G 1136  1                                  16    
HELIX   93  93 ASP G 1137  LYS G 1140  5                                   4    
HELIX   94  94 LEU G 1141  HIS G 1149  1                                   9    
HELIX   95  95 LYS G 1151  VAL G 1157  1                                   7    
HELIX   96  96 ASP G 1162  ASN G 1173  1                                  12    
HELIX   97  97 GLN G 1177  SER G 1180  5                                   4    
HELIX   98  98 THR G 1181  LEU G 1186  1                                   6    
HELIX   99  99 ILE G 1187  LEU G 1194  1                                   8    
HELIX  100 100 LYS G 1195  LEU G 1206  1                                  12    
HELIX  101 101 SER G 1211  GLY G 1242  1                                  32    
HELIX  102 102 PHE G 1241  ALA G 1250  1                                  10    
HELIX  103 103 PRO G 1279  LYS G 1284  1                                   6    
HELIX  104 104 GLU G 1364  GLY G 1367  5                                   4    
HELIX  105 105 SER G 1379  ARG G 1399  1                                  21    
HELIX  106 106 GLY H   15  ASN H   26  1                                  12    
HELIX  107 107 LEU H   67  SER H   71  5                                   5    
HELIX  108 108 SER H   86  LYS H   96  1                                  11    
HELIX  109 109 LYS H   96  CYS H  105  1                                  10    
HELIX  110 110 LYS H  116  ARG H  120  5                                   5    
HELIX  111 111 ASP H  122  LYS H  132  1                                  11    
HELIX  112 112 THR H  138  ILE H  149  1                                  12    
HELIX  113 113 GLY H  164  LEU H  177  1                                  14    
SHEET    1   A 7 ARG A1332  PRO A1336  0                                        
SHEET    2   A 7 ALA A1299  TYR A1304 -1  O  VAL A1300   N  ILE A1335           
SHEET    3   A 7 GLU A1290  PHE A1296 -1  N  ALA A1292   O  VAL A1303           
SHEET    4   A 7 LEU A1267  TRP A1275 -1  N  LEU A1268   O  VAL A1295           
SHEET    5   A 7 ARG A1371  CYS A1377 -1  N  CYS A1376   O  ILE A1274           
SHEET    6   A 7 VAL A1355  HIS A1360 -1  O  CYS A1356   N  LEU A1375           
SHEET    7   A 7 LEU A1340  ARG A1343 -1  O  GLN A1341   N  VAL A1359           
SHEET    1   B 6 TYR B  40  VAL B  46  0                                        
SHEET    2   B 6 LYS B  49  TRP B  56 -1  O  LYS B  49   N  VAL B  46           
SHEET    3   B 6 ALA B   3  VAL B   9  1  O  ILE B   4   N  GLY B  54           
SHEET    4   B 6 VAL B  77  SER B  83  1  O  VAL B  77   N  VAL B   7           
SHEET    5   B 6 ILE B 110  THR B 115  1  N  ILE B 111   O  PHE B  78           
SHEET    6   B 6 LYS B 153  GLU B 156  1  O  LYS B 153   N  LEU B 112           
SHEET    1   C 7 PHE C1329  PRO C1336  0                                        
SHEET    2   C 7 ALA C1299  LYS C1305 -1  O  VAL C1300   N  ILE C1335           
SHEET    3   C 7 GLU C1290  PHE C1296 -1  N  ALA C1292   O  VAL C1303           
SHEET    4   C 7 LEU C1267  TRP C1275 -1  N  LEU C1268   O  VAL C1295           
SHEET    5   C 7 ARG C1371  CYS C1377 -1  N  CYS C1376   O  ILE C1274           
SHEET    6   C 7 VAL C1355  HIS C1360 -1  O  CYS C1356   N  LEU C1375           
SHEET    7   C 7 LEU C1340  ARG C1343 -1  O  GLN C1341   N  VAL C1359           
SHEET    1   D 6 TYR D  40  VAL D  46  0                                        
SHEET    2   D 6 LYS D  49  TRP D  56 -1  O  LYS D  49   N  VAL D  46           
SHEET    3   D 6 ALA D   3  VAL D   9  1  O  ILE D   4   N  GLY D  54           
SHEET    4   D 6 VAL D  77  SER D  83  1  O  VAL D  77   N  VAL D   7           
SHEET    5   D 6 ILE D 110  THR D 115  1  N  ILE D 111   O  PHE D  78           
SHEET    6   D 6 LYS D 153  GLU D 156  1  O  LYS D 153   N  LEU D 112           
SHEET    1   E 7 ARG E1332  PRO E1336  0                                        
SHEET    2   E 7 ALA E1299  TYR E1304 -1  O  VAL E1300   N  ILE E1335           
SHEET    3   E 7 GLU E1290  PHE E1296 -1  N  ALA E1292   O  VAL E1303           
SHEET    4   E 7 LEU E1267  TRP E1275 -1  N  LEU E1268   O  VAL E1295           
SHEET    5   E 7 ARG E1371  CYS E1377 -1  N  CYS E1376   O  ILE E1274           
SHEET    6   E 7 VAL E1355  HIS E1360 -1  O  CYS E1356   N  LEU E1375           
SHEET    7   E 7 LEU E1340  ARG E1343 -1  O  GLN E1341   N  VAL E1359           
SHEET    1   F 6 TYR F  40  VAL F  46  0                                        
SHEET    2   F 6 LYS F  49  TRP F  56 -1  O  LYS F  49   N  VAL F  46           
SHEET    3   F 6 ALA F   3  VAL F   9  1  O  ILE F   4   N  GLY F  54           
SHEET    4   F 6 VAL F  77  SER F  83  1  O  VAL F  77   N  VAL F   7           
SHEET    5   F 6 ILE F 110  THR F 115  1  N  ILE F 111   O  PHE F  78           
SHEET    6   F 6 LYS F 153  GLU F 156  1  O  LYS F 153   N  LEU F 112           
SHEET    1   G 7 PHE G1331  PRO G1336  0                                        
SHEET    2   G 7 ALA G1299  TYR G1304 -1  O  VAL G1300   N  ILE G1335           
SHEET    3   G 7 GLU G1290  PHE G1296 -1  N  ALA G1292   O  VAL G1303           
SHEET    4   G 7 LEU G1267  TRP G1275 -1  N  LEU G1268   O  VAL G1295           
SHEET    5   G 7 ARG G1371  CYS G1376 -1  N  CYS G1376   O  ILE G1274           
SHEET    6   G 7 VAL G1355  HIS G1360 -1  O  CYS G1356   N  LEU G1375           
SHEET    7   G 7 LEU G1340  ARG G1343 -1  O  GLN G1341   N  VAL G1359           
SHEET    1   H 6 TYR H  40  VAL H  46  0                                        
SHEET    2   H 6 LYS H  49  TRP H  56 -1  O  LYS H  49   N  VAL H  46           
SHEET    3   H 6 ALA H   3  VAL H   9  1  O  ILE H   4   N  GLY H  54           
SHEET    4   H 6 VAL H  77  SER H  83  1  O  VAL H  77   N  VAL H   7           
SHEET    5   H 6 ILE H 110  THR H 115  1  N  ILE H 111   O  PHE H  78           
SHEET    6   H 6 LYS H 153  GLU H 156  1  O  LYS H 153   N  LEU H 112           
LINK         C   LEU A1062                 N   MSE A1063     1555   1555  1.33  
LINK         C   MSE A1063                 N   GLU A1064     1555   1555  1.33  
LINK         C   GLU A1090                 N   MSE A1091     1555   1555  1.33  
LINK         C   MSE A1091                 N   VAL A1092     1555   1555  1.33  
LINK         C   THR A1223                 N   MSE A1224     1555   1555  1.34  
LINK         C   MSE A1224                 N   ASN A1225     1555   1555  1.33  
LINK         C   GLU A1233                 N   MSE A1234     1555   1555  1.33  
LINK         C   MSE A1234                 N   GLN A1235     1555   1555  1.33  
LINK         C   SER A1263                 N   MSE A1264     1555   1555  1.33  
LINK         C   MSE A1264                 N   GLY A1265     1555   1555  1.33  
LINK         C   HIS A1333                 N   MSE A1334     1555   1555  1.33  
LINK         C   MSE A1334                 N   ILE A1335     1555   1555  1.33  
LINK         C   LEU C1062                 N   MSE C1063     1555   1555  1.33  
LINK         C   MSE C1063                 N   GLU C1064     1555   1555  1.33  
LINK         C   GLU C1090                 N   MSE C1091     1555   1555  1.33  
LINK         C   MSE C1091                 N   VAL C1092     1555   1555  1.33  
LINK         C   THR C1223                 N   MSE C1224     1555   1555  1.33  
LINK         C   MSE C1224                 N   ASN C1225     1555   1555  1.33  
LINK         C   GLU C1233                 N   MSE C1234     1555   1555  1.33  
LINK         C   MSE C1234                 N   GLN C1235     1555   1555  1.33  
LINK         C   SER C1263                 N   MSE C1264     1555   1555  1.33  
LINK         C   MSE C1264                 N   GLY C1265     1555   1555  1.33  
LINK         C   HIS C1333                 N   MSE C1334     1555   1555  1.33  
LINK         C   MSE C1334                 N   ILE C1335     1555   1555  1.33  
LINK         C   LEU E1062                 N   MSE E1063     1555   1555  1.33  
LINK         C   MSE E1063                 N   GLU E1064     1555   1555  1.33  
LINK         C   GLU E1090                 N   MSE E1091     1555   1555  1.33  
LINK         C   MSE E1091                 N   VAL E1092     1555   1555  1.33  
LINK         C   THR E1223                 N   MSE E1224     1555   1555  1.34  
LINK         C   MSE E1224                 N   ASN E1225     1555   1555  1.33  
LINK         C   GLU E1233                 N   MSE E1234     1555   1555  1.33  
LINK         C   MSE E1234                 N   GLN E1235     1555   1555  1.33  
LINK         C   SER E1263                 N   MSE E1264     1555   1555  1.32  
LINK         C   MSE E1264                 N   GLY E1265     1555   1555  1.33  
LINK         C   HIS E1333                 N   MSE E1334     1555   1555  1.33  
LINK         C   MSE E1334                 N   ILE E1335     1555   1555  1.32  
LINK         C   LEU G1062                 N   MSE G1063     1555   1555  1.33  
LINK         C   MSE G1063                 N   GLU G1064     1555   1555  1.33  
LINK         C   GLU G1090                 N   MSE G1091     1555   1555  1.33  
LINK         C   MSE G1091                 N   VAL G1092     1555   1555  1.33  
LINK         C   THR G1223                 N   MSE G1224     1555   1555  1.33  
LINK         C   MSE G1224                 N   ASN G1225     1555   1555  1.33  
LINK         C   GLU G1233                 N   MSE G1234     1555   1555  1.33  
LINK         C   MSE G1234                 N   GLN G1235     1555   1555  1.33  
LINK         C   SER G1263                 N   MSE G1264     1555   1555  1.33  
LINK         C   MSE G1264                 N   GLY G1265     1555   1555  1.33  
LINK         C   HIS G1333                 N   MSE G1334     1555   1555  1.33  
LINK         C   MSE G1334                 N   ILE G1335     1555   1555  1.33  
SITE     1 AC1  7 ASP B  11  GLY B  12  ALA B  13  VAL B  14                    
SITE     2 AC1  7 GLY B  15  LYS B  16  THR B  17                               
SITE     1 AC2  7 ASP D  11  GLY D  12  ALA D  13  VAL D  14                    
SITE     2 AC2  7 GLY D  15  LYS D  16  THR D  17                               
SITE     1 AC3  7 ASP F  11  GLY F  12  ALA F  13  VAL F  14                    
SITE     2 AC3  7 GLY F  15  LYS F  16  THR F  17                               
SITE     1 AC4  7 ASP H  11  GLY H  12  ALA H  13  VAL H  14                    
SITE     2 AC4  7 GLY H  15  LYS H  16  THR H  17                               
CRYST1  186.950  149.270  149.210  90.00 121.00  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      0.005349  0.000000  0.003214        0.00000                         
SCALE2      0.000000  0.006699  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007819        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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