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Database: PDB
Entry: 4ILS
LinkDB: 4ILS
Original site: 4ILS 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   31-DEC-12   4ILS              
TITLE     CRYSTAL STRUCTURE OF ENGINEERED PROTEIN. NORTHEAST STRUCTURAL GENOMICS
TITLE    2 CONSORTIUM TARGET OR117                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENGINEERED PROTEIN;                                        
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   3 ORGANISM_TAXID: 32630;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)GOLD;                          
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET29B+                                   
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, NORTHEAST STRUCTURAL GENOMICS       
KEYWDS   2 CONSORTIUM, NESG, MBH ENZYME DESIGN, UNKNOWN FUNCTION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SEETHARAMAN,S.LEW,L.NIVON,D.BAKER,S.BJELIC,C.CICCOSANTI,S.SAHDEV,   
AUTHOR   2 R.XIAO,J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,L.TONG,J.F.HUNT,         
AUTHOR   3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)                      
REVDAT   1   20-MAR-13 4ILS    0                                                
JRNL        AUTH   J.SEETHARAMAN,S.LEW,L.NIVON,D.BAKER,S.BJELIC,C.CICCOSANTI,   
JRNL        AUTH 2 S.SAHDEV,R.XIAO,J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,L.TONG, 
JRNL        AUTH 3 J.F.HUNT                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF ENGINEERED PROTEIN. NORTHEAST           
JRNL        TITL 2 STRUCTURAL GENOMICS CONSORTIUM TARGET OR117                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 49981                          
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 + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2674                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3554                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.61                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 199                          
REMARK   3   BIN FREE R VALUE                    : 0.3350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8233                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 271                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.77000                                             
REMARK   3    B22 (A**2) : -1.77000                                             
REMARK   3    B33 (A**2) : 3.54000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.406         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.278         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.200         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.851         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8439 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11443 ; 1.373 ; 1.949       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1021 ; 6.455 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   387 ;35.765 ;22.558       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1394 ;18.848 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    74 ;20.896 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1271 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6388 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1      A     2   381       B     2    381      361  0.13  0.05    
REMARK   3    2      A     2   381       C     2    381      357  0.14  0.05    
REMARK   3    3      B     2   381       C     2    381      358  0.10  0.05    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4ILS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB076912.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
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) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52922                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.900                              
REMARK 200  R MERGE                    (I) : 0.08200                            
REMARK 200  R SYM                      (I) : 0.06100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3UW6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.88M POTASSIUM ACETATE (KC2H3O2), 0.1   
REMARK 280  M MES PH 6, MICROBATCH UNDER OIL METHOD, TEMPERATURE 277K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      116.09300            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       56.42600            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       56.42600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.04650            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       56.42600            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       56.42600            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      174.13950            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       56.42600            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       56.42600            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.04650            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       56.42600            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       56.42600            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      174.13950            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      116.09300            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      232.18600            
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: 5330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 79110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000     -112.85200            
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   BIOMT1   2  0.000000  1.000000  0.000000     -112.85200            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      232.18600            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000     -112.85200            
REMARK 350   BIOMT2   4  1.000000  0.000000  0.000000      112.85200            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      232.18600            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 476  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     GLY A   135                                                      
REMARK 465     SER A   136                                                      
REMARK 465     LEU A   137                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     THR A   169                                                      
REMARK 465     ALA A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     GLU A   172                                                      
REMARK 465     VAL A   173                                                      
REMARK 465     ASN A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     TYR A   177                                                      
REMARK 465     PHE A   178                                                      
REMARK 465     SER A   179                                                      
REMARK 465     ALA A   205                                                      
REMARK 465     ALA A   206                                                      
REMARK 465     SER A   207                                                      
REMARK 465     PHE A   210                                                      
REMARK 465     PRO A   211                                                      
REMARK 465     ASP A   212                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     SER A   230                                                      
REMARK 465     PRO A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     ILE A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     PRO A   235                                                      
REMARK 465     LEU A   236                                                      
REMARK 465     LEU A   237                                                      
REMARK 465     PRO A   238                                                      
REMARK 465     ARG A   383                                                      
REMARK 465     GLY A   384                                                      
REMARK 465     GLU A   385                                                      
REMARK 465     SER A   386                                                      
REMARK 465     SER A   387                                                      
REMARK 465     ALA A   388                                                      
REMARK 465     GLY A   389                                                      
REMARK 465     SER A   390                                                      
REMARK 465     PHE B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     THR B   169                                                      
REMARK 465     ALA B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     VAL B   173                                                      
REMARK 465     ASN B   174                                                      
REMARK 465     THR B   175                                                      
REMARK 465     ASP B   176                                                      
REMARK 465     TYR B   177                                                      
REMARK 465     PHE B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     ALA B   205                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     SER B   207                                                      
REMARK 465     LEU B   208                                                      
REMARK 465     ARG B   209                                                      
REMARK 465     PHE B   210                                                      
REMARK 465     PRO B   211                                                      
REMARK 465     ASP B   212                                                      
REMARK 465     ARG B   213                                                      
REMARK 465     PRO B   229                                                      
REMARK 465     SER B   230                                                      
REMARK 465     PRO B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     ILE B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     PRO B   235                                                      
REMARK 465     LEU B   236                                                      
REMARK 465     LEU B   237                                                      
REMARK 465     PRO B   238                                                      
REMARK 465     TYR B   239                                                      
REMARK 465     SER B   264                                                      
REMARK 465     TYR B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ARG B   383                                                      
REMARK 465     GLY B   384                                                      
REMARK 465     GLU B   385                                                      
REMARK 465     SER B   386                                                      
REMARK 465     SER B   387                                                      
REMARK 465     ALA B   388                                                      
REMARK 465     GLY B   389                                                      
REMARK 465     SER B   390                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C   169                                                      
REMARK 465     ALA C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     GLU C   172                                                      
REMARK 465     VAL C   173                                                      
REMARK 465     ASN C   174                                                      
REMARK 465     THR C   175                                                      
REMARK 465     ASP C   176                                                      
REMARK 465     TYR C   177                                                      
REMARK 465     PHE C   178                                                      
REMARK 465     SER C   179                                                      
REMARK 465     TYR C   180                                                      
REMARK 465     ASN C   203                                                      
REMARK 465     SER C   204                                                      
REMARK 465     ALA C   205                                                      
REMARK 465     ALA C   206                                                      
REMARK 465     SER C   207                                                      
REMARK 465     LEU C   208                                                      
REMARK 465     ARG C   209                                                      
REMARK 465     PHE C   210                                                      
REMARK 465     PRO C   211                                                      
REMARK 465     ASP C   212                                                      
REMARK 465     ARG C   213                                                      
REMARK 465     ALA C   228                                                      
REMARK 465     PRO C   229                                                      
REMARK 465     SER C   230                                                      
REMARK 465     PRO C   231                                                      
REMARK 465     GLY C   232                                                      
REMARK 465     ILE C   233                                                      
REMARK 465     LYS C   234                                                      
REMARK 465     PRO C   235                                                      
REMARK 465     LEU C   236                                                      
REMARK 465     LEU C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     TYR C   239                                                      
REMARK 465     PRO C   240                                                      
REMARK 465     TYR C   265                                                      
REMARK 465     GLY C   266                                                      
REMARK 465     ALA C   267                                                      
REMARK 465     GLY C   382                                                      
REMARK 465     ARG C   383                                                      
REMARK 465     GLY C   384                                                      
REMARK 465     GLU C   385                                                      
REMARK 465     SER C   386                                                      
REMARK 465     SER C   387                                                      
REMARK 465     ALA C   388                                                      
REMARK 465     GLY C   389                                                      
REMARK 465     SER C   390                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 204    OG                                                  
REMARK 470     LEU A 208    CG   CD1  CD2                                       
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 213    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 264    OG                                                  
REMARK 470     TYR B 180    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 183    CB   OG1  CG2                                       
REMARK 470     ARG B 184    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR B 214    OG1  CG2                                            
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    GLN A 293   N   -  CA  -  C   ANGL. DEV. = -16.5 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    PHE A 215       95.42     76.31                                   
REMARK 500    THR A 268      108.48     97.63                                   
REMARK 500    HIS A 294      -46.27     94.55                                   
REMARK 500    PHE A 295      162.18    -46.25                                   
REMARK 500    LYS A 372       -2.60     56.38                                   
REMARK 500    ILE A 381       43.45   -107.55                                   
REMARK 500    ASN B   2       78.10   -114.83                                   
REMARK 500    THR B 132       38.94    -85.46                                   
REMARK 500    ALA B 202       35.51     77.68                                   
REMARK 500    PRO B 322       95.50    -65.60                                   
REMARK 500    LYS B 372       -3.48     65.23                                   
REMARK 500    MET B 375      -61.90    -91.02                                   
REMARK 500    ASP C   3      127.86    176.76                                   
REMARK 500    ASP C  47      -96.02      0.04                                   
REMARK 500    MET C 134       45.68    -83.96                                   
REMARK 500    VAL C 263     -140.81    -96.75                                   
REMARK 500    ARG C 291        9.54    -66.05                                   
REMARK 500    GLN C 293       12.83    -63.93                                   
REMARK 500    HIS C 294       13.67   -141.54                                   
REMARK 500    ASP C 300      -56.52     64.27                                   
REMARK 500    LYS C 372      -32.91     66.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    PHE A 215        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 495        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH B 488        DISTANCE =  5.09 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NESG-OR117   RELATED DB: TARGETTRACK                     
DBREF  4ILS A    1   390  PDB    4ILS     4ILS             1    390             
DBREF  4ILS B    1   390  PDB    4ILS     4ILS             1    390             
DBREF  4ILS C    1   390  PDB    4ILS     4ILS             1    390             
SEQRES   1 A  390  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 A  390  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 A  390  LEU LEU PRO ASP ASP THR HIS ILE MET ALA SER VAL CYS          
SEQRES   4 A  390  GLY ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 A  390  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 A  390  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 A  390  GLU ALA PRO ILE LEU VAL THR GLY ALA SER ARG PRO ALA          
SEQRES   8 A  390  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 A  390  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 A  390  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU TYR MET          
SEQRES  11 A  390  ASP THR GLY MET GLY SER LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 A  390  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 A  390  HIS PHE VAL LEU GLU GLY LEU TRP THR TRP PHE ALA THR          
SEQRES  14 A  390  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 A  390  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 A  390  PRO PRO LEU VAL PHE CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 A  390  ARG PHE PRO ASP ARG THR PHE ASN MET VAL GLN PHE GLY          
SEQRES  18 A  390  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 A  390  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 A  390  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 A  390  GLU LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 A  390  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR LYS ASP          
SEQRES  23 A  390  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 A  390  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE LEU MET          
SEQRES  25 A  390  ASP MET CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 A  390  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP LYS          
SEQRES  27 A  390  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 A  390  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 A  390  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 A  390  ARG ASN ALA ILE GLY ARG GLY GLU SER SER ALA GLY SER          
SEQRES   1 B  390  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 B  390  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 B  390  LEU LEU PRO ASP ASP THR HIS ILE MET ALA SER VAL CYS          
SEQRES   4 B  390  GLY ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 B  390  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 B  390  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 B  390  GLU ALA PRO ILE LEU VAL THR GLY ALA SER ARG PRO ALA          
SEQRES   8 B  390  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 B  390  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 B  390  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU TYR MET          
SEQRES  11 B  390  ASP THR GLY MET GLY SER LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 B  390  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 B  390  HIS PHE VAL LEU GLU GLY LEU TRP THR TRP PHE ALA THR          
SEQRES  14 B  390  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 B  390  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 B  390  PRO PRO LEU VAL PHE CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 B  390  ARG PHE PRO ASP ARG THR PHE ASN MET VAL GLN PHE GLY          
SEQRES  18 B  390  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 B  390  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 B  390  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 B  390  GLU LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 B  390  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR LYS ASP          
SEQRES  23 B  390  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 B  390  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE LEU MET          
SEQRES  25 B  390  ASP MET CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 B  390  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP LYS          
SEQRES  27 B  390  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 B  390  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 B  390  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 B  390  ARG ASN ALA ILE GLY ARG GLY GLU SER SER ALA GLY SER          
SEQRES   1 C  390  MET ASN ASP PHE HIS ARG ASP THR TRP ALA GLU VAL ASP          
SEQRES   2 C  390  LEU ASP ALA ILE TYR ASP ASN VAL GLU ASN LEU ARG ARG          
SEQRES   3 C  390  LEU LEU PRO ASP ASP THR HIS ILE MET ALA SER VAL CYS          
SEQRES   4 C  390  GLY ASN ALA TYR GLY HIS GLY ASP VAL GLN VAL ALA ARG          
SEQRES   5 C  390  THR ALA LEU GLU ALA GLY ALA SER ARG LEU ALA VAL ALA          
SEQRES   6 C  390  PHE LEU ASP GLU ALA LEU ALA LEU ARG GLU LYS GLY ILE          
SEQRES   7 C  390  GLU ALA PRO ILE LEU VAL THR GLY ALA SER ARG PRO ALA          
SEQRES   8 C  390  ASP ALA ALA LEU ALA ALA GLN GLN ARG ILE ALA LEU THR          
SEQRES   9 C  390  VAL PHE ARG SER ASP TRP LEU GLU GLU ALA SER ALA LEU          
SEQRES  10 C  390  TYR SER GLY PRO PHE PRO ILE HIS PHE HIS LEU TYR MET          
SEQRES  11 C  390  ASP THR GLY MET GLY SER LEU GLY VAL LYS ASP GLU GLU          
SEQRES  12 C  390  GLU THR LYS ARG ILE VAL ALA LEU ILE GLU ARG HIS PRO          
SEQRES  13 C  390  HIS PHE VAL LEU GLU GLY LEU TRP THR TRP PHE ALA THR          
SEQRES  14 C  390  ALA ASP GLU VAL ASN THR ASP TYR PHE SER TYR GLN TYR          
SEQRES  15 C  390  THR ARG PHE LEU HIS MET LEU GLU TRP LEU PRO SER ARG          
SEQRES  16 C  390  PRO PRO LEU VAL PHE CYS ALA ASN SER ALA ALA SER LEU          
SEQRES  17 C  390  ARG PHE PRO ASP ARG THR PHE ASN MET VAL GLN PHE GLY          
SEQRES  18 C  390  ILE ALA MET TYR GLY LEU ALA PRO SER PRO GLY ILE LYS          
SEQRES  19 C  390  PRO LEU LEU PRO TYR PRO LEU LYS GLU ALA PHE SER LEU          
SEQRES  20 C  390  HIS SER ARG LEU VAL HIS VAL LYS LYS LEU GLN PRO GLY          
SEQRES  21 C  390  GLU LYS VAL SER TYR GLY ALA THR TYR THR ALA GLN THR          
SEQRES  22 C  390  GLU GLU TRP ILE GLY THR ILE PRO ILE GLY TYR LYS ASP          
SEQRES  23 C  390  GLY TRP LEU ARG ARG LEU GLN HIS PHE HIS VAL LEU VAL          
SEQRES  24 C  390  ASP GLY GLN LYS ALA PRO ILE VAL GLY ARG ILE LEU MET          
SEQRES  25 C  390  ASP MET CYS MET ILE ARG LEU PRO GLY PRO LEU PRO VAL          
SEQRES  26 C  390  GLY THR LYS VAL THR LEU ILE GLY ARG GLN GLY ASP LYS          
SEQRES  27 C  390  VAL ILE SER ILE ASP ASP VAL ALA ARG HIS LEU GLU THR          
SEQRES  28 C  390  ILE ASN TYR GLU VAL PRO CYS THR ILE SER TYR ARG VAL          
SEQRES  29 C  390  PRO ARG ILE PHE PHE ARG HIS LYS ARG ILE MET GLU VAL          
SEQRES  30 C  390  ARG ASN ALA ILE GLY ARG GLY GLU SER SER ALA GLY SER          
FORMUL   4  HOH   *271(H2 O)                                                    
HELIX    1   1 LEU A   14  LEU A   28  1                                  15    
HELIX    2   2 VAL A   38  GLY A   44  1                                   7    
HELIX    3   3 GLY A   46  ALA A   57  1                                  12    
HELIX    4   4 PHE A   66  LYS A   76  1                                  11    
HELIX    5   5 ARG A   89  ALA A   91  5                                   3    
HELIX    6   6 ASP A   92  GLN A   99  1                                   8    
HELIX    7   7 ARG A  107  TYR A  118  1                                  12    
HELIX    8   8 ASP A  141  HIS A  155  1                                  15    
HELIX    9   9 GLN A  181  TRP A  191  1                                  11    
HELIX   10  10 GLY A  221  GLY A  226  5                                   6    
HELIX   11  11 GLY A  283  GLY A  287  5                                   5    
HELIX   12  12 LEU A  289  GLN A  293  5                                   5    
HELIX   13  13 SER A  341  GLU A  350  1                                  10    
HELIX   14  14 TYR A  354  ILE A  360  1                                   7    
HELIX   15  15 LEU B   14  LEU B   28  1                                  15    
HELIX   16  16 VAL B   38  HIS B   45  1                                   8    
HELIX   17  17 GLY B   46  GLY B   58  1                                  13    
HELIX   18  18 PHE B   66  LYS B   76  1                                  11    
HELIX   19  19 ARG B   89  ALA B   91  5                                   3    
HELIX   20  20 ASP B   92  GLN B   99  1                                   8    
HELIX   21  21 ARG B  107  TYR B  118  1                                  12    
HELIX   22  22 ASP B  141  HIS B  155  1                                  15    
HELIX   23  23 GLN B  181  TRP B  191  1                                  11    
HELIX   24  24 GLY B  221  GLY B  226  5                                   6    
HELIX   25  25 GLY B  283  GLY B  287  5                                   5    
HELIX   26  26 LEU B  289  GLN B  293  5                                   5    
HELIX   27  27 SER B  341  GLU B  350  1                                  10    
HELIX   28  28 TYR B  354  ILE B  360  1                                   7    
HELIX   29  29 LEU C   14  LEU C   28  1                                  15    
HELIX   30  30 VAL C   38  GLY C   44  1                                   7    
HELIX   31  31 GLY C   46  ALA C   57  1                                  12    
HELIX   32  32 PHE C   66  LYS C   76  1                                  11    
HELIX   33  33 ARG C   89  ALA C   91  5                                   3    
HELIX   34  34 ASP C   92  GLN C   99  1                                   8    
HELIX   35  35 ARG C  107  TYR C  118  1                                  12    
HELIX   36  36 ASP C  141  HIS C  155  1                                  15    
HELIX   37  37 TYR C  182  TRP C  191  1                                  10    
HELIX   38  38 GLY C  221  GLY C  226  5                                   6    
HELIX   39  39 GLY C  283  GLY C  287  5                                   5    
HELIX   40  40 LEU C  289  GLN C  293  5                                   5    
HELIX   41  41 SER C  341  GLU C  350  1                                  10    
HELIX   42  42 TYR C  354  ILE C  360  1                                   7    
SHEET    1   A 7 HIS A 253  LEU A 257  0                                        
SHEET    2   A 7 GLU A 275  ILE A 280 -1  O  GLU A 275   N  LEU A 257           
SHEET    3   A 7 CYS A 315  LEU A 319 -1  O  LEU A 319   N  TRP A 276           
SHEET    4   A 7 GLN A 302  VAL A 307 -1  N  VAL A 307   O  MET A 316           
SHEET    5   A 7 HIS A 296  VAL A 299 -1  N  VAL A 297   O  ALA A 304           
SHEET    6   A 7 LYS A 328  GLN A 335 -1  O  THR A 330   N  LEU A 298           
SHEET    7   A 7 LYS A 338  ILE A 340 -1  O  ILE A 340   N  GLY A 333           
SHEET    1   B10 HIS A 253  LEU A 257  0                                        
SHEET    2   B10 GLU A 275  ILE A 280 -1  O  GLU A 275   N  LEU A 257           
SHEET    3   B10 CYS A 315  LEU A 319 -1  O  LEU A 319   N  TRP A 276           
SHEET    4   B10 GLN A 302  VAL A 307 -1  N  VAL A 307   O  MET A 316           
SHEET    5   B10 HIS A 296  VAL A 299 -1  N  VAL A 297   O  ALA A 304           
SHEET    6   B10 LYS A 328  GLN A 335 -1  O  THR A 330   N  LEU A 298           
SHEET    7   B10 PHE A 245  ARG A 250 -1  N  SER A 249   O  VAL A 329           
SHEET    8   B10 THR A   8  ASP A  13 -1  N  GLU A  11   O  SER A 246           
SHEET    9   B10 ARG A 366  ARG A 370  1  O  ILE A 367   N  VAL A  12           
SHEET   10   B10 ARG A 373  ARG A 378 -1  O  GLU A 376   N  PHE A 368           
SHEET    1   C 8 LEU A 198  CYS A 201  0                                        
SHEET    2   C 8 PHE A 158  THR A 165  1  N  GLU A 161   O  LEU A 198           
SHEET    3   C 8 ILE A 124  TYR A 129  1  N  PHE A 126   O  VAL A 159           
SHEET    4   C 8 ILE A 101  VAL A 105  1  N  VAL A 105   O  HIS A 127           
SHEET    5   C 8 ILE A  82  VAL A  84  1  N  VAL A  84   O  ALA A 102           
SHEET    6   C 8 ARG A  61  VAL A  64  1  N  LEU A  62   O  LEU A  83           
SHEET    7   C 8 HIS A  33  SER A  37  1  N  ALA A  36   O  ARG A  61           
SHEET    8   C 8 MET A 217  PHE A 220  1  O  VAL A 218   N  MET A  35           
SHEET    1   D 2 LYS A 262  VAL A 263  0                                        
SHEET    2   D 2 TYR A 269  THR A 270 -1  O  TYR A 269   N  VAL A 263           
SHEET    1   E 7 HIS B 253  LEU B 257  0                                        
SHEET    2   E 7 GLU B 275  ILE B 280 -1  O  GLU B 275   N  LEU B 257           
SHEET    3   E 7 CYS B 315  ARG B 318 -1  O  ILE B 317   N  GLY B 278           
SHEET    4   E 7 GLN B 302  VAL B 307 -1  N  VAL B 307   O  MET B 316           
SHEET    5   E 7 HIS B 296  VAL B 299 -1  N  VAL B 297   O  ALA B 304           
SHEET    6   E 7 LYS B 328  GLN B 335 -1  O  THR B 330   N  LEU B 298           
SHEET    7   E 7 LYS B 338  ILE B 340 -1  O  ILE B 340   N  GLY B 333           
SHEET    1   F10 HIS B 253  LEU B 257  0                                        
SHEET    2   F10 GLU B 275  ILE B 280 -1  O  GLU B 275   N  LEU B 257           
SHEET    3   F10 CYS B 315  ARG B 318 -1  O  ILE B 317   N  GLY B 278           
SHEET    4   F10 GLN B 302  VAL B 307 -1  N  VAL B 307   O  MET B 316           
SHEET    5   F10 HIS B 296  VAL B 299 -1  N  VAL B 297   O  ALA B 304           
SHEET    6   F10 LYS B 328  GLN B 335 -1  O  THR B 330   N  LEU B 298           
SHEET    7   F10 PHE B 245  ARG B 250 -1  N  SER B 249   O  VAL B 329           
SHEET    8   F10 THR B   8  ASP B  13 -1  N  TRP B   9   O  HIS B 248           
SHEET    9   F10 ARG B 366  ARG B 370  1  O  ILE B 367   N  VAL B  12           
SHEET   10   F10 ARG B 373  ARG B 378 -1  O  MET B 375   N  PHE B 368           
SHEET    1   G 8 LEU B 198  PHE B 200  0                                        
SHEET    2   G 8 PHE B 158  TRP B 164  1  N  LEU B 163   O  PHE B 200           
SHEET    3   G 8 ILE B 124  TYR B 129  1  N  PHE B 126   O  VAL B 159           
SHEET    4   G 8 ILE B 101  VAL B 105  1  N  VAL B 105   O  HIS B 127           
SHEET    5   G 8 ILE B  82  VAL B  84  1  N  ILE B  82   O  ALA B 102           
SHEET    6   G 8 ARG B  61  VAL B  64  1  N  LEU B  62   O  LEU B  83           
SHEET    7   G 8 HIS B  33  SER B  37  1  N  ALA B  36   O  ARG B  61           
SHEET    8   G 8 MET B 217  PHE B 220  1  O  PHE B 220   N  MET B  35           
SHEET    1   H 7 HIS C 253  LEU C 257  0                                        
SHEET    2   H 7 GLU C 275  ILE C 280 -1  O  GLU C 275   N  LEU C 257           
SHEET    3   H 7 CYS C 315  ARG C 318 -1  O  ILE C 317   N  GLY C 278           
SHEET    4   H 7 GLN C 302  VAL C 307 -1  N  VAL C 307   O  MET C 316           
SHEET    5   H 7 HIS C 296  VAL C 299 -1  O  VAL C 299   N  GLN C 302           
SHEET    6   H 7 LYS C 328  GLN C 335 -1  O  THR C 330   N  LEU C 298           
SHEET    7   H 7 LYS C 338  ILE C 340 -1  O  ILE C 340   N  GLY C 333           
SHEET    1   I10 HIS C 253  LEU C 257  0                                        
SHEET    2   I10 GLU C 275  ILE C 280 -1  O  GLU C 275   N  LEU C 257           
SHEET    3   I10 CYS C 315  ARG C 318 -1  O  ILE C 317   N  GLY C 278           
SHEET    4   I10 GLN C 302  VAL C 307 -1  N  VAL C 307   O  MET C 316           
SHEET    5   I10 HIS C 296  VAL C 299 -1  O  VAL C 299   N  GLN C 302           
SHEET    6   I10 LYS C 328  GLN C 335 -1  O  THR C 330   N  LEU C 298           
SHEET    7   I10 PHE C 245  ARG C 250 -1  N  SER C 249   O  VAL C 329           
SHEET    8   I10 THR C   8  ASP C  13 -1  N  GLU C  11   O  SER C 246           
SHEET    9   I10 ARG C 366  ARG C 370  1  O  ILE C 367   N  VAL C  12           
SHEET   10   I10 ARG C 373  ARG C 378 -1  O  GLU C 376   N  PHE C 368           
SHEET    1   J 8 LEU C 198  CYS C 201  0                                        
SHEET    2   J 8 PHE C 158  THR C 165  1  N  LEU C 163   O  PHE C 200           
SHEET    3   J 8 ILE C 124  TYR C 129  1  N  PHE C 126   O  VAL C 159           
SHEET    4   J 8 ILE C 101  VAL C 105  1  N  VAL C 105   O  HIS C 127           
SHEET    5   J 8 ILE C  82  VAL C  84  1  N  VAL C  84   O  ALA C 102           
SHEET    6   J 8 ARG C  61  VAL C  64  1  N  LEU C  62   O  LEU C  83           
SHEET    7   J 8 HIS C  33  SER C  37  1  N  ALA C  36   O  ALA C  63           
SHEET    8   J 8 MET C 217  PHE C 220  1  O  VAL C 218   N  MET C  35           
CISPEP   1 GLY A  120    PRO A  121          0         7.10                     
CISPEP   2 THR A  214    PHE A  215          0       -19.09                     
CISPEP   3 TYR A  239    PRO A  240          0       -10.68                     
CISPEP   4 GLY B  120    PRO B  121          0         3.80                     
CISPEP   5 GLY C  120    PRO C  121          0         3.80                     
CRYST1  112.852  112.852  232.186  90.00  90.00  90.00 P 41 21 2    24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008861  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004307        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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