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Database: PDB
Entry: 2EP5
LinkDB: 2EP5
Original site: 2EP5 
HEADER    OXIDOREDUCTASE                          29-MAR-07   2EP5              
TITLE     STRUCTURAL STUDY OF PROJECT ID ST1242 FROM SULFOLOBUS TOKODAII STRAIN7
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 350AA LONG HYPOTHETICAL ASPARTATE-SEMIALDEHYDE             
COMPND   3 DEHYDROGENASE;                                                       
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 EC: 1.2.1.11;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;                            
SOURCE   3 ORGANISM_TAXID: 111955;                                              
SOURCE   4 STRAIN: STRAIN7;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL-21 CODONPLUS(DE3)-RIL;                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
KEYWDS    OXIDOREDUCTASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON      
KEYWDS   2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL         
KEYWDS   3 GENOMICS/PROTEOMICS INITIATIVE, RSGI                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ASADA,N.KUNISHIMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE   
AUTHOR   2 (RSGI)                                                               
REVDAT   4   13-MAR-24 2EP5    1       REMARK                                   
REVDAT   3   13-JUL-11 2EP5    1       VERSN                                    
REVDAT   2   24-FEB-09 2EP5    1       VERSN                                    
REVDAT   1   02-OCT-07 2EP5    0                                                
JRNL        AUTH   Y.ASADA,N.KUNISHIMA                                          
JRNL        TITL   STRUCTURAL STUDY OF PROJECT ID ST1242 FROM SULFOLOBUS        
JRNL        TITL 2 TOKODAII STRAIN7                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.27                          
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)   (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 58141                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RAMDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2901                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.51                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 348                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10823                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 677                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.17                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.40000                                             
REMARK   3    B22 (A**2) : 7.19000                                              
REMARK   3    B33 (A**2) : -3.79000                                             
REMARK   3    B12 (A**2) : 4.73000                                              
REMARK   3    B13 (A**2) : -2.31000                                             
REMARK   3    B23 (A**2) : -2.25000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.31                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.870                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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: NULL                                      
REMARK   4                                                                      
REMARK   4 2EP5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-JUN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000026934.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL26B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58141                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8W/V(%) PEG 4K, 0.1M ACET, PH 4.6,       
REMARK 280  MICROBATCH, TEMPERATURE 291K                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 50790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
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    PRO B 122   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 111      -11.16     77.75                                   
REMARK 500    PRO A 122      -72.96    -18.82                                   
REMARK 500    ASN A 125       50.71   -145.05                                   
REMARK 500    LYS A 169       62.48   -104.59                                   
REMARK 500    PRO A 199       24.53    -69.60                                   
REMARK 500    LYS A 202      123.36    -37.28                                   
REMARK 500    GLU A 316     -168.77   -113.48                                   
REMARK 500    VAL A 330      -77.33    -99.29                                   
REMARK 500    ALA A 333      -86.96   -159.52                                   
REMARK 500    PHE B 111       -3.64     73.92                                   
REMARK 500    PRO B 122      -74.35     -9.08                                   
REMARK 500    ASN B 125       42.00   -147.90                                   
REMARK 500    PRO B 162        0.67    -66.47                                   
REMARK 500    LYS B 169       58.02   -105.06                                   
REMARK 500    PRO B 199       36.86    -65.90                                   
REMARK 500    LYS B 202      119.74    -34.55                                   
REMARK 500    ALA B 302      120.03    -39.32                                   
REMARK 500    VAL B 330      -79.97    -98.80                                   
REMARK 500    ALA B 333      -79.21   -161.04                                   
REMARK 500    PHE C 111       -2.35     72.38                                   
REMARK 500    PRO C 122      -67.52    -16.78                                   
REMARK 500    ASN C 125       41.24   -152.37                                   
REMARK 500    LYS C 169       46.26   -105.87                                   
REMARK 500    PRO C 199       40.37    -73.23                                   
REMARK 500    LYS C 202      115.44    -35.11                                   
REMARK 500    ALA C 302      120.43    -34.36                                   
REMARK 500    ASN C 317      -69.37   -171.65                                   
REMARK 500    VAL C 330      -69.63   -102.44                                   
REMARK 500    ALA C 333      -79.24   -158.39                                   
REMARK 500    PRO D 122      -76.92     -9.09                                   
REMARK 500    ASN D 125       54.94   -157.77                                   
REMARK 500    PRO D 199       39.55    -70.80                                   
REMARK 500    LYS D 202      115.77    -28.79                                   
REMARK 500    VAL D 330      -69.28   -105.50                                   
REMARK 500    ALA D 333      -78.07   -162.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: STO001001242.1   RELATED DB: TARGETDB                    
DBREF  2EP5 A    1   350  UNP    Q971Y6   Q971Y6_SULTO     1    350             
DBREF  2EP5 B    1   350  UNP    Q971Y6   Q971Y6_SULTO     1    350             
DBREF  2EP5 C    1   350  UNP    Q971Y6   Q971Y6_SULTO     1    350             
DBREF  2EP5 D    1   350  UNP    Q971Y6   Q971Y6_SULTO     1    350             
SEQRES   1 A  350  MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR          
SEQRES   2 A  350  GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS          
SEQRES   3 A  350  HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO          
SEQRES   4 A  350  SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP          
SEQRES   5 A  350  ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU          
SEQRES   6 A  350  PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL          
SEQRES   7 A  350  ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU          
SEQRES   8 A  350  SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL          
SEQRES   9 A  350  VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL          
SEQRES  10 A  350  PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU          
SEQRES  11 A  350  LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY          
SEQRES  12 A  350  ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET          
SEQRES  13 A  350  SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS          
SEQRES  14 A  350  SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY          
SEQRES  15 A  350  ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY          
SEQRES  16 A  350  ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE          
SEQRES  17 A  350  ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN          
SEQRES  18 A  350  ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR          
SEQRES  19 A  350  SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL          
SEQRES  20 A  350  ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU          
SEQRES  21 A  350  ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN          
SEQRES  22 A  350  GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE          
SEQRES  23 A  350  VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP          
SEQRES  24 A  350  VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG          
SEQRES  25 A  350  ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU          
SEQRES  26 A  350  GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE          
SEQRES  27 A  350  LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE              
SEQRES   1 B  350  MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR          
SEQRES   2 B  350  GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS          
SEQRES   3 B  350  HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO          
SEQRES   4 B  350  SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP          
SEQRES   5 B  350  ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU          
SEQRES   6 B  350  PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL          
SEQRES   7 B  350  ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU          
SEQRES   8 B  350  SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL          
SEQRES   9 B  350  VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL          
SEQRES  10 B  350  PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU          
SEQRES  11 B  350  LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY          
SEQRES  12 B  350  ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET          
SEQRES  13 B  350  SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS          
SEQRES  14 B  350  SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY          
SEQRES  15 B  350  ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY          
SEQRES  16 B  350  ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE          
SEQRES  17 B  350  ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN          
SEQRES  18 B  350  ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR          
SEQRES  19 B  350  SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL          
SEQRES  20 B  350  ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU          
SEQRES  21 B  350  ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN          
SEQRES  22 B  350  GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE          
SEQRES  23 B  350  VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP          
SEQRES  24 B  350  VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG          
SEQRES  25 B  350  ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU          
SEQRES  26 B  350  GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE          
SEQRES  27 B  350  LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE              
SEQRES   1 C  350  MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR          
SEQRES   2 C  350  GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS          
SEQRES   3 C  350  HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO          
SEQRES   4 C  350  SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP          
SEQRES   5 C  350  ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU          
SEQRES   6 C  350  PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL          
SEQRES   7 C  350  ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU          
SEQRES   8 C  350  SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL          
SEQRES   9 C  350  VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL          
SEQRES  10 C  350  PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU          
SEQRES  11 C  350  LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY          
SEQRES  12 C  350  ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET          
SEQRES  13 C  350  SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS          
SEQRES  14 C  350  SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY          
SEQRES  15 C  350  ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY          
SEQRES  16 C  350  ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE          
SEQRES  17 C  350  ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN          
SEQRES  18 C  350  ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR          
SEQRES  19 C  350  SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL          
SEQRES  20 C  350  ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU          
SEQRES  21 C  350  ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN          
SEQRES  22 C  350  GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE          
SEQRES  23 C  350  VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP          
SEQRES  24 C  350  VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG          
SEQRES  25 C  350  ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU          
SEQRES  26 C  350  GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE          
SEQRES  27 C  350  LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE              
SEQRES   1 D  350  MET ALA ASP LYS ILE LYS VAL SER LEU LEU GLY SER THR          
SEQRES   2 D  350  GLY MET VAL GLY GLN LYS MET VAL LYS MET LEU ALA LYS          
SEQRES   3 D  350  HIS PRO TYR LEU GLU LEU VAL LYS VAL SER ALA SER PRO          
SEQRES   4 D  350  SER LYS ILE GLY LYS LYS TYR LYS ASP ALA VAL LYS TRP          
SEQRES   5 D  350  ILE GLU GLN GLY ASP ILE PRO GLU GLU VAL GLN ASP LEU          
SEQRES   6 D  350  PRO ILE VAL SER THR ASN TYR GLU ASP HIS LYS ASP VAL          
SEQRES   7 D  350  ASP VAL VAL LEU SER ALA LEU PRO ASN GLU LEU ALA GLU          
SEQRES   8 D  350  SER ILE GLU LEU GLU LEU VAL LYS ASN GLY LYS ILE VAL          
SEQRES   9 D  350  VAL SER ASN ALA SER PRO PHE ARG MET ASP PRO ASP VAL          
SEQRES  10 D  350  PRO LEU ILE ASN PRO GLU ILE ASN TRP GLU HIS LEU GLU          
SEQRES  11 D  350  LEU LEU LYS PHE GLN LYS GLU ARG LYS GLY TRP LYS GLY          
SEQRES  12 D  350  ILE LEU VAL LYS ASN PRO ASN CYS THR ALA ALA ILE MET          
SEQRES  13 D  350  SER MET PRO ILE LYS PRO LEU ILE GLU ILE ALA THR LYS          
SEQRES  14 D  350  SER LYS ILE ILE ILE THR THR LEU GLN ALA VAL SER GLY          
SEQRES  15 D  350  ALA GLY TYR ASN GLY ILE SER PHE MET ALA ILE GLU GLY          
SEQRES  16 D  350  ASN ILE ILE PRO TYR ILE LYS GLY GLU GLU ASP LYS ILE          
SEQRES  17 D  350  ALA LYS GLU LEU THR LYS LEU ASN GLY LYS LEU GLU ASN          
SEQRES  18 D  350  ASN GLN ILE ILE PRO ALA ASN LEU ASP SER THR VAL THR          
SEQRES  19 D  350  SER ILE ARG VAL PRO THR ARG VAL GLY HIS MET GLY VAL          
SEQRES  20 D  350  ILE ASN ILE VAL THR ASN GLU ARG ILE ASN ILE GLU GLU          
SEQRES  21 D  350  ILE LYS LYS THR LEU LYS ASN PHE LYS SER LEU PRO GLN          
SEQRES  22 D  350  GLN LYS ASN LEU PRO THR ALA PRO LYS GLN PRO ILE ILE          
SEQRES  23 D  350  VAL ARG ASP GLU GLU ASP ARG PRO GLN PRO ILE ILE ASP          
SEQRES  24 D  350  VAL ASN ALA GLU SER GLY MET ALA VAL THR VAL GLY ARG          
SEQRES  25 D  350  ILE ARG HIS GLU ASN ASN VAL LEU ARG LEU VAL VAL LEU          
SEQRES  26 D  350  GLY ASP ASN LEU VAL ARG GLY ALA ALA GLY ILE THR ILE          
SEQRES  27 D  350  LEU THR VAL GLU VAL MET LYS GLU LEU GLY TYR ILE              
FORMUL   5  HOH   *677(H2 O)                                                    
HELIX    1   1 GLY A   14  ALA A   25  1                                  12    
HELIX    2   2 SER A   38  ILE A   42  5                                   5    
HELIX    3   3 LYS A   45  VAL A   50  1                                   6    
HELIX    4   4 PRO A   59  ASP A   64  1                                   6    
HELIX    5   5 ASN A   71  LYS A   76  5                                   6    
HELIX    6   6 PRO A   86  ASN A  100  1                                  15    
HELIX    7   7 ASN A  121  TRP A  126  1                                   6    
HELIX    8   8 GLU A  127  GLU A  130  5                                   4    
HELIX    9   9 LEU A  131  GLY A  140  1                                  10    
HELIX   10  10 ASN A  150  LYS A  161  1                                  12    
HELIX   11  11 LEU A  163  LYS A  169  1                                   7    
HELIX   12  12 VAL A  180  GLY A  184  5                                   5    
HELIX   13  13 SER A  189  GLU A  194  1                                   6    
HELIX   14  14 GLY A  203  ASN A  216  1                                  14    
HELIX   15  15 ASN A  257  ASN A  267  1                                  11    
HELIX   16  16 SER A  270  LYS A  275  1                                   6    
HELIX   17  17 GLN A  295  VAL A  300  1                                   6    
HELIX   18  18 ASN A  301  MET A  306  5                                   6    
HELIX   19  19 ALA A  333  LEU A  347  1                                  15    
HELIX   20  20 GLY B   14  ALA B   25  1                                  12    
HELIX   21  21 SER B   38  ILE B   42  5                                   5    
HELIX   22  22 LYS B   45  ALA B   49  5                                   5    
HELIX   23  23 ASN B   71  HIS B   75  5                                   5    
HELIX   24  24 PRO B   86  ASN B  100  1                                  15    
HELIX   25  25 ASN B  121  TRP B  126  1                                   6    
HELIX   26  26 GLU B  127  LYS B  133  5                                   7    
HELIX   27  27 PHE B  134  GLY B  140  1                                   7    
HELIX   28  28 ASN B  150  LYS B  161  1                                  12    
HELIX   29  29 LEU B  163  LYS B  169  1                                   7    
HELIX   30  30 ALA B  179  GLY B  184  5                                   6    
HELIX   31  31 SER B  189  GLU B  194  1                                   6    
HELIX   32  32 GLY B  203  ASN B  216  1                                  14    
HELIX   33  33 ASN B  257  ASN B  267  1                                  11    
HELIX   34  34 SER B  270  LYS B  275  1                                   6    
HELIX   35  35 GLN B  295  VAL B  300  1                                   6    
HELIX   36  36 ASN B  301  MET B  306  5                                   6    
HELIX   37  37 ALA B  333  LEU B  347  1                                  15    
HELIX   38  38 GLY C   14  LYS C   26  1                                  13    
HELIX   39  39 SER C   38  ILE C   42  5                                   5    
HELIX   40  40 LYS C   45  VAL C   50  1                                   6    
HELIX   41  41 ASN C   71  HIS C   75  5                                   5    
HELIX   42  42 PRO C   86  ASN C  100  1                                  15    
HELIX   43  43 ASN C  121  TRP C  126  1                                   6    
HELIX   44  44 GLU C  127  GLU C  130  5                                   4    
HELIX   45  45 LEU C  131  GLY C  140  1                                  10    
HELIX   46  46 ASN C  150  LYS C  161  1                                  12    
HELIX   47  47 LEU C  163  THR C  168  1                                   6    
HELIX   48  48 ALA C  179  GLY C  184  5                                   6    
HELIX   49  49 SER C  189  GLU C  194  1                                   6    
HELIX   50  50 GLY C  203  ASN C  216  1                                  14    
HELIX   51  51 ASN C  257  ASN C  267  1                                  11    
HELIX   52  52 SER C  270  LYS C  275  1                                   6    
HELIX   53  53 GLN C  295  VAL C  300  1                                   6    
HELIX   54  54 ALA C  333  LEU C  347  1                                  15    
HELIX   55  55 GLY D   14  ALA D   25  1                                  12    
HELIX   56  56 SER D   38  ILE D   42  5                                   5    
HELIX   57  57 LYS D   45  VAL D   50  1                                   6    
HELIX   58  58 ASN D   71  HIS D   75  5                                   5    
HELIX   59  59 PRO D   86  LYS D   99  1                                  14    
HELIX   60  60 ASN D  121  TRP D  126  1                                   6    
HELIX   61  61 GLU D  127  GLU D  130  5                                   4    
HELIX   62  62 LEU D  131  GLY D  140  1                                  10    
HELIX   63  63 ASN D  150  LYS D  161  1                                  12    
HELIX   64  64 LEU D  163  LYS D  169  1                                   7    
HELIX   65  65 ALA D  179  GLY D  184  5                                   6    
HELIX   66  66 SER D  189  GLU D  194  1                                   6    
HELIX   67  67 GLY D  203  ASN D  216  1                                  14    
HELIX   68  68 ASN D  257  ASN D  267  1                                  11    
HELIX   69  69 SER D  270  LYS D  275  1                                   6    
HELIX   70  70 GLN D  295  VAL D  300  1                                   6    
HELIX   71  71 ASN D  301  MET D  306  5                                   6    
HELIX   72  72 ALA D  333  LEU D  347  1                                  15    
SHEET    1   A 6 ILE A  67  VAL A  68  0                                        
SHEET    2   A 6 LEU A  30  SER A  36  1  N  VAL A  35   O  VAL A  68           
SHEET    3   A 6 ILE A   5  LEU A  10  1  N  LEU A   9   O  SER A  36           
SHEET    4   A 6 VAL A  80  SER A  83  1  O  LEU A  82   N  LEU A  10           
SHEET    5   A 6 ILE A 103  SER A 106  1  O  ILE A 103   N  VAL A  81           
SHEET    6   A 6 ILE A 144  LYS A 147  1  O  ILE A 144   N  VAL A 104           
SHEET    1   B 6 ASP A 230  ARG A 237  0                                        
SHEET    2   B 6 LYS A 171  GLN A 178  1  N  THR A 176   O  ILE A 236           
SHEET    3   B 6 HIS A 244  VAL A 251 -1  O  VAL A 247   N  THR A 175           
SHEET    4   B 6 VAL A 319  GLY A 326 -1  O  LEU A 320   N  ILE A 250           
SHEET    5   B 6 VAL A 308  GLU A 316 -1  N  ARG A 314   O  ARG A 321           
SHEET    6   B 6 ILE A 285  VAL A 287  1  N  ILE A 286   O  VAL A 310           
SHEET    1   C 2 LYS A 218  LEU A 219  0                                        
SHEET    2   C 2 ILE A 224  ILE A 225 -1  O  ILE A 225   N  LYS A 218           
SHEET    1   D 6 ILE B  67  VAL B  68  0                                        
SHEET    2   D 6 LEU B  30  SER B  36  1  N  VAL B  35   O  VAL B  68           
SHEET    3   D 6 ILE B   5  LEU B  10  1  N  ILE B   5   O  GLU B  31           
SHEET    4   D 6 VAL B  80  SER B  83  1  O  LEU B  82   N  SER B   8           
SHEET    5   D 6 ILE B 103  SER B 106  1  O  ILE B 103   N  VAL B  81           
SHEET    6   D 6 ILE B 144  LYS B 147  1  O  ILE B 144   N  VAL B 104           
SHEET    1   E 6 ASP B 230  ARG B 237  0                                        
SHEET    2   E 6 LYS B 171  GLN B 178  1  N  THR B 176   O  THR B 234           
SHEET    3   E 6 HIS B 244  VAL B 251 -1  O  MET B 245   N  LEU B 177           
SHEET    4   E 6 VAL B 319  GLY B 326 -1  O  VAL B 324   N  GLY B 246           
SHEET    5   E 6 VAL B 308  GLU B 316 -1  N  THR B 309   O  LEU B 325           
SHEET    6   E 6 ILE B 285  ARG B 288  1  N  ILE B 286   O  VAL B 310           
SHEET    1   F 2 LYS B 218  LEU B 219  0                                        
SHEET    2   F 2 ILE B 224  ILE B 225 -1  O  ILE B 225   N  LYS B 218           
SHEET    1   G 6 ILE C  67  VAL C  68  0                                        
SHEET    2   G 6 LEU C  30  SER C  36  1  N  VAL C  35   O  VAL C  68           
SHEET    3   G 6 ILE C   5  LEU C  10  1  N  ILE C   5   O  GLU C  31           
SHEET    4   G 6 VAL C  80  SER C  83  1  O  LEU C  82   N  SER C   8           
SHEET    5   G 6 ILE C 103  SER C 106  1  O  ILE C 103   N  VAL C  81           
SHEET    6   G 6 ILE C 144  LYS C 147  1  O  ILE C 144   N  VAL C 104           
SHEET    1   H 6 ASP C 230  ARG C 237  0                                        
SHEET    2   H 6 LYS C 171  GLN C 178  1  N  THR C 176   O  ILE C 236           
SHEET    3   H 6 HIS C 244  VAL C 251 -1  O  VAL C 247   N  THR C 175           
SHEET    4   H 6 VAL C 319  GLY C 326 -1  O  LEU C 320   N  ILE C 250           
SHEET    5   H 6 VAL C 308  HIS C 315 -1  N  ARG C 314   O  ARG C 321           
SHEET    6   H 6 ILE C 285  VAL C 287  1  N  ILE C 286   O  VAL C 310           
SHEET    1   I 2 LYS C 218  LEU C 219  0                                        
SHEET    2   I 2 ILE C 224  ILE C 225 -1  O  ILE C 225   N  LYS C 218           
SHEET    1   J 6 ILE D  67  VAL D  68  0                                        
SHEET    2   J 6 LEU D  30  SER D  36  1  N  VAL D  35   O  VAL D  68           
SHEET    3   J 6 ILE D   5  LEU D  10  1  N  ILE D   5   O  GLU D  31           
SHEET    4   J 6 VAL D  80  SER D  83  1  O  LEU D  82   N  LEU D  10           
SHEET    5   J 6 ILE D 103  SER D 106  1  O  ILE D 103   N  VAL D  81           
SHEET    6   J 6 ILE D 144  LYS D 147  1  O  VAL D 146   N  VAL D 104           
SHEET    1   K 6 ASP D 230  ARG D 237  0                                        
SHEET    2   K 6 LYS D 171  GLN D 178  1  N  GLN D 178   O  ILE D 236           
SHEET    3   K 6 HIS D 244  VAL D 251 -1  O  MET D 245   N  LEU D 177           
SHEET    4   K 6 VAL D 319  GLY D 326 -1  O  LEU D 320   N  ILE D 250           
SHEET    5   K 6 VAL D 308  HIS D 315 -1  N  ARG D 314   O  ARG D 321           
SHEET    6   K 6 ILE D 285  ARG D 288  1  N  ILE D 286   O  VAL D 310           
SHEET    1   L 2 LYS D 218  LEU D 219  0                                        
SHEET    2   L 2 ILE D 224  ILE D 225 -1  O  ILE D 225   N  LYS D 218           
CISPEP   1 ARG A  293    PRO A  294          0         0.24                     
CISPEP   2 ARG B  293    PRO B  294          0         0.40                     
CISPEP   3 ARG C  293    PRO C  294          0         0.12                     
CISPEP   4 ARG D  293    PRO D  294          0         0.06                     
CRYST1   70.157   73.986   91.552  68.10  68.39  86.04 P 1           4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014254 -0.000988 -0.005690        0.00000                         
SCALE2      0.000000  0.013548 -0.005475        0.00000                         
SCALE3      0.000000  0.000000  0.012671        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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