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Database: PDB
Entry: 5TSW
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HEADER    LYMPHOKINE                              22-APR-99   5TSW              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF A HUMAN TNF-ALPHA                
TITLE    2 MUTANT                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (TUMOR NECROSIS FACTOR-ALPHA);                     
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)                                 
KEYWDS    LYMPHOKINE, LOW SYSTEMIC TOXICITY, MUTANT                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.-S.CHA,J.-S.KIM,H.-S.CHO,B.-H.OH                                    
REVDAT   3   24-FEB-09 5TSW    1       VERSN                                    
REVDAT   2   23-SEP-03 5TSW    1       DBREF  SEQADV                            
REVDAT   1   07-MAY-99 5TSW    0                                                
SPRSDE     30-APR-99 5TSW      4TSW                                             
JRNL        AUTH   S.S.CHA,J.S.KIM,H.S.CHO,N.K.SHIN,W.JEONG,H.C.SHIN,           
JRNL        AUTH 2 Y.J.KIM,J.H.HAHN,B.H.OH                                      
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURE OF A HUMAN TUMOR           
JRNL        TITL 2 NECROSIS FACTOR-ALPHA MUTANT WITH LOW SYSTEMIC               
JRNL        TITL 3 TOXICITY.                                                    
JRNL        REF    J.BIOL.CHEM.                  V. 273  2153 1998              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9442056                                                      
JRNL        DOI    10.1074/JBC.273.4.2153                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.J.ECK,S.R.SPRANG                                           
REMARK   1  TITL   THE STRUCTURE OF TUMOR NECROSIS FACTOR-ALPHA AT              
REMARK   1  TITL 2 2.6 A RESOLUTION. IMPLICATIONS FOR RECEPTOR BINDING          
REMARK   1  REF    J.BIOL.CHEM.                  V. 264 17595 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.01                                          
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 41282                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8190                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 1068                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.99                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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 5TSW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB000954.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-DEC-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : MACSCIENCE M18XHF                  
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MACSCIENCE                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41282                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENEGLYCOL 4000, 0.1 M       
REMARK 280  SODIUM CITRATE PH 5.6, PH 6.8                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.08500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.94500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.28000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.94500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.08500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.28000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A     8                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     PRO E     8                                                      
REMARK 465     PRO F     8                                                      
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   9    OG                                                  
REMARK 470     ASP A  10    CG   OD1  OD2                                       
REMARK 470     GLU A  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR A  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 157    O                                                   
REMARK 470     SER B   9    OG                                                  
REMARK 470     ASP B  10    CG   OD1  OD2                                       
REMARK 470     GLU B  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR B  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 157    O                                                   
REMARK 470     SER C   9    OG                                                  
REMARK 470     ASP C  10    CG   OD1  OD2                                       
REMARK 470     GLU C  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR C  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN C  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 110    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 157    O                                                   
REMARK 470     SER D   9    OG                                                  
REMARK 470     ASP D  10    CG   OD1  OD2                                       
REMARK 470     GLU D  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN D  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR D  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN D  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG D 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 157    O                                                   
REMARK 470     SER E   9    OG                                                  
REMARK 470     ASP E  10    CG   OD1  OD2                                       
REMARK 470     GLU E  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN E  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR E  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN E  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG E 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU E 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU E 157    O                                                   
REMARK 470     SER F   9    OG                                                  
REMARK 470     ASP F  10    CG   OD1  OD2                                       
REMARK 470     GLU F  23    CG   CD   OE1  OE2                                  
REMARK 470     GLN F  25    CG   CD   OE1  NE2                                  
REMARK 470     TYR F  87    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN F  88    CG   CD   OE1  NE2                                  
REMARK 470     ARG F 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F 104    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 107    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 110    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 146    CG   CD   OE1  OE2                                  
REMARK 470     LEU F 157    O                                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA E    84     N    SER E    86              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLU B    53     NH2  ARG E    31     4455     2.05            
REMARK 500   O    HOH A   177     O    HOH F   192     4555     2.08            
REMARK 500   O    HOH A   180     O    HOH F  1578     4555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A  88   C     THR A  89   N      -0.229                       
REMARK 500    GLU B 110   C     ALA B 111   N      -0.156                       
REMARK 500    GLN C  88   C     THR C  89   N      -0.148                       
REMARK 500    PRO D  70   C     SER D  71   N      -0.207                       
REMARK 500    PRO E  70   C     SER E  71   N      -0.181                       
REMARK 500    ALA E  84   C     VAL E  85   N      -0.283                       
REMARK 500    GLU E 104   C     THR E 105   N       0.138                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU B 104   O   -  C   -  N   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    PRO C  70   O   -  C   -  N   ANGL. DEV. = -11.1 DEGREES          
REMARK 500    ALA D  84   O   -  C   -  N   ANGL. DEV. = -10.7 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    HIS A  15       87.88   -159.72                                   
REMARK 500    ALA A  22      112.49    -27.15                                   
REMARK 500    GLU A  23       86.79    -64.07                                   
REMARK 500    ARG A  31       40.77   -100.59                                   
REMARK 500    LEU A  37       89.57   -176.87                                   
REMARK 500    ASP A  45       33.92     71.16                                   
REMARK 500    PRO A  70       59.82    -54.52                                   
REMARK 500    SER A  71     -159.66     56.49                                   
REMARK 500    THR A  72      163.86     56.85                                   
REMARK 500    ALA A  84     -158.87    -73.04                                   
REMARK 500    VAL A  85     -115.60     32.72                                   
REMARK 500    TYR A  87      101.19     64.75                                   
REMARK 500    GLN A  88     -101.68   -112.01                                   
REMARK 500    GLU A 104      108.89    158.30                                   
REMARK 500    THR A 105      -49.56   -157.27                                   
REMARK 500    ALA A 109     -173.79    164.50                                   
REMARK 500    ALA A 111      134.00     76.11                                   
REMARK 500    LYS A 112       84.78    168.92                                   
REMARK 500    ASP A 143       76.62   -106.92                                   
REMARK 500    SER A 147     -160.67     41.80                                   
REMARK 500    HIS B  15       93.98   -162.79                                   
REMARK 500    ARG B  31       57.15    -96.25                                   
REMARK 500    SER B  60      146.63   -178.97                                   
REMARK 500    CYS B  69       56.95   -158.26                                   
REMARK 500    PRO B  70       83.46    -38.78                                   
REMARK 500    SER B  71      161.42     71.88                                   
REMARK 500    THR B  72      147.40     62.86                                   
REMARK 500    VAL B  85      -79.51     51.91                                   
REMARK 500    SER B  86      100.83    174.75                                   
REMARK 500    GLU B 104      109.48   -173.65                                   
REMARK 500    GLU B 107      156.77     84.22                                   
REMARK 500    ALA B 111       74.93    -19.28                                   
REMARK 500    PRO C  20        1.01    -64.84                                   
REMARK 500    LEU C  37       83.06   -174.18                                   
REMARK 500    SER C  60      151.52    174.83                                   
REMARK 500    GLN C  67      127.88   -171.73                                   
REMARK 500    PRO C  70       72.54    -60.10                                   
REMARK 500    SER C  71      173.05     54.58                                   
REMARK 500    THR C  72       92.02     54.23                                   
REMARK 500    VAL C  85      -91.55     57.43                                   
REMARK 500    SER C  86       64.40   -161.79                                   
REMARK 500    TYR C  87       69.77     77.48                                   
REMARK 500    GLN C  88     -134.73    -99.24                                   
REMARK 500    GLU C 104      -14.32    165.95                                   
REMARK 500    THR C 105      136.43    -14.59                                   
REMARK 500    GLU C 107      129.17     64.07                                   
REMARK 500    ALA C 109     -156.04    -78.91                                   
REMARK 500    GLU C 110      156.65    173.96                                   
REMARK 500    PRO D  20        8.45    -64.86                                   
REMARK 500    LEU D  37       97.20   -175.37                                   
REMARK 500    ARG D  44     -104.61    -87.62                                   
REMARK 500    PRO D  70       62.58    -46.60                                   
REMARK 500    SER D  71     -149.50     58.70                                   
REMARK 500    THR D  72      156.72     41.44                                   
REMARK 500    VAL D  85      -77.34     59.51                                   
REMARK 500    SER D  86       85.91    164.25                                   
REMARK 500    TYR D  87       94.12     71.70                                   
REMARK 500    GLN D  88      -80.51   -132.26                                   
REMARK 500    GLU D 104       97.44   -171.58                                   
REMARK 500    GLU D 107     -163.45     62.21                                   
REMARK 500    ALA D 109     -150.64     82.97                                   
REMARK 500    GLU D 110     -166.19    173.11                                   
REMARK 500    ALA D 111      112.97     83.63                                   
REMARK 500    LYS D 112      108.03   -163.69                                   
REMARK 500    ASP D 143       79.79   -116.61                                   
REMARK 500    HIS E  15       84.87   -159.14                                   
REMARK 500    ASN E  34       46.87     75.60                                   
REMARK 500    LEU E  37       76.64   -175.74                                   
REMARK 500    ARG E  44     -108.10    -89.23                                   
REMARK 500    PRO E  70       72.66    -46.71                                   
REMARK 500    SER E  71     -147.38     43.65                                   
REMARK 500    THR E  72     -156.19     28.40                                   
REMARK 500    ALA E  84       86.23    -27.58                                   
REMARK 500    VAL E  85      -74.58     47.12                                   
REMARK 500    TYR E  87        9.02     50.69                                   
REMARK 500    THR E  89      113.96    -29.18                                   
REMARK 500    GLU E 104       62.62    179.61                                   
REMARK 500    THR E 105      -98.44   -120.87                                   
REMARK 500    GLU E 107     -159.00    -84.16                                   
REMARK 500    LEU F  37       84.46    158.06                                   
REMARK 500    ASN F  46        8.96     59.44                                   
REMARK 500    CYS F  69       63.46   -157.33                                   
REMARK 500    PRO F  70       88.04    -62.07                                   
REMARK 500    SER F  71      154.25     76.21                                   
REMARK 500    THR F  72      131.50     61.53                                   
REMARK 500    ALA F  84     -175.06    -65.65                                   
REMARK 500    VAL F  85      -81.46     32.45                                   
REMARK 500    SER F  86      109.64   -161.17                                   
REMARK 500    GLU F 104      104.45   -167.31                                   
REMARK 500    PRO F 106       79.83    -60.55                                   
REMARK 500    GLU F 107      -93.48     64.01                                   
REMARK 500    ALA F 111       77.18     81.46                                   
REMARK 500    SER F 147     -141.05     35.90                                   
REMARK 500    PHE F 152      125.64   -171.27                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR D 119         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ALA A  84        -12.63                                           
REMARK 500    PRO B  70         14.26                                           
REMARK 500    GLU B 104         21.18                                           
REMARK 500    PRO C  70        -18.96                                           
REMARK 500    ALA C  84        -21.49                                           
REMARK 500    ALA D  84        -17.14                                           
REMARK 500    GLU D 104         11.19                                           
REMARK 500    PRO F  70         10.93                                           
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 D 167        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH E 216        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH D 191        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A 197        DISTANCE = 10.71 ANGSTROMS                       
REMARK 525    HOH C 201        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH F 304        DISTANCE =  6.29 ANGSTROMS                       
REMARK 525    HOH A 204        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH A 205        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH F1532        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH E1537        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH A 208        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH F1534        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH B 218        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH B 219        DISTANCE =  8.62 ANGSTROMS                       
DBREF  5TSW A    8   157  UNP    P01375   TNFA_HUMAN      84    233             
DBREF  5TSW B    8   157  UNP    P01375   TNFA_HUMAN      84    233             
DBREF  5TSW C    8   157  UNP    P01375   TNFA_HUMAN      84    233             
DBREF  5TSW D    8   157  UNP    P01375   TNFA_HUMAN      84    233             
DBREF  5TSW E    8   157  UNP    P01375   TNFA_HUMAN      84    233             
DBREF  5TSW F    8   157  UNP    P01375   TNFA_HUMAN      84    233             
SEQADV 5TSW SER A   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE A   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE A   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQADV 5TSW SER B   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE B   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE B   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQADV 5TSW SER C   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE C   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE C   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQADV 5TSW SER D   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE D   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE D   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQADV 5TSW SER E   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE E   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE E   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQADV 5TSW SER F   29  UNP  P01375    LEU   105 ENGINEERED                     
SEQADV 5TSW ILE F   52  UNP  P01375    SER   128 ENGINEERED                     
SEQADV 5TSW PHE F   56  UNP  P01375    TYR   132 ENGINEERED                     
SEQRES   1 A  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 A  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 A  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 A  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 A  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 A  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 A  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 A  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 A  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 A  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 A  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 A  150  TYR PHE GLY ILE ILE ALA LEU                                  
SEQRES   1 B  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 B  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 B  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 B  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 B  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 B  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 B  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 B  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 B  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 B  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 B  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 B  150  TYR PHE GLY ILE ILE ALA LEU                                  
SEQRES   1 C  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 C  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 C  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 C  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 C  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 C  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 C  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 C  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 C  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 C  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 C  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 C  150  TYR PHE GLY ILE ILE ALA LEU                                  
SEQRES   1 D  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 D  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 D  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 D  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 D  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 D  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 D  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 D  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 D  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 D  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 D  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 D  150  TYR PHE GLY ILE ILE ALA LEU                                  
SEQRES   1 E  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 E  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 E  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 E  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 E  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 E  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 E  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 E  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 E  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 E  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 E  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 E  150  TYR PHE GLY ILE ILE ALA LEU                                  
SEQRES   1 F  150  PRO SER ASP LYS PRO VAL ALA HIS VAL VAL ALA ASN PRO          
SEQRES   2 F  150  GLN ALA GLU GLY GLN LEU GLN TRP SER ASN ARG ARG ALA          
SEQRES   3 F  150  ASN ALA LEU LEU ALA ASN GLY VAL GLU LEU ARG ASP ASN          
SEQRES   4 F  150  GLN LEU VAL VAL PRO ILE GLU GLY LEU PHE LEU ILE TYR          
SEQRES   5 F  150  SER GLN VAL LEU PHE LYS GLY GLN GLY CYS PRO SER THR          
SEQRES   6 F  150  HIS VAL LEU LEU THR HIS THR ILE SER ARG ILE ALA VAL          
SEQRES   7 F  150  SER TYR GLN THR LYS VAL ASN LEU LEU SER ALA ILE LYS          
SEQRES   8 F  150  SER PRO CYS GLN ARG GLU THR PRO GLU GLY ALA GLU ALA          
SEQRES   9 F  150  LYS PRO TRP TYR GLU PRO ILE TYR LEU GLY GLY VAL PHE          
SEQRES  10 F  150  GLN LEU GLU LYS GLY ASP ARG LEU SER ALA GLU ILE ASN          
SEQRES  11 F  150  ARG PRO ASP TYR LEU ASP PHE ALA GLU SER GLY GLN VAL          
SEQRES  12 F  150  TYR PHE GLY ILE ILE ALA LEU                                  
FORMUL   7  HOH   *356(H2 O)                                                    
HELIX    1   1 PRO B  139  TYR B  141  5                                   3    
HELIX    2   2 PRO C  139  TYR C  141  5                                   3    
HELIX    3   3 PRO E   20  ALA E   22  5                                   3    
HELIX    4   4 PRO E  139  TYR E  141  5                                   3    
HELIX    5   5 PRO F  139  TYR F  141  5                                   3    
SHEET    1   A 5 LEU A  36  ALA A  38  0                                        
SHEET    2   A 5 VAL A  13  VAL A  17 -1  N  HIS A  15   O  LEU A  36           
SHEET    3   A 5 TYR A 151  ALA A 156 -1  N  ILE A 154   O  ALA A  14           
SHEET    4   A 5 GLY A  54  GLN A  67 -1  N  GLN A  61   O  TYR A 151           
SHEET    5   A 5 PRO A 113  LEU A 126 -1  N  LEU A 126   O  GLY A  54           
SHEET    1   B 3 ARG A 131  ILE A 136  0                                        
SHEET    2   B 3 LEU A  76  ILE A  83 -1  N  ILE A  83   O  ARG A 131           
SHEET    3   B 3 VAL A  91  LYS A  98 -1  N  LYS A  98   O  LEU A  76           
SHEET    1   C 5 LEU B  36  ALA B  38  0                                        
SHEET    2   C 5 VAL B  13  VAL B  17 -1  N  HIS B  15   O  LEU B  36           
SHEET    3   C 5 TYR B 151  ALA B 156 -1  N  ILE B 154   O  ALA B  14           
SHEET    4   C 5 GLY B  54  GLN B  67 -1  N  GLN B  61   O  TYR B 151           
SHEET    5   C 5 PRO B 113  LEU B 126 -1  N  LEU B 126   O  GLY B  54           
SHEET    1   D 2 GLU B  42  ARG B  44  0                                        
SHEET    2   D 2 GLN B  47  VAL B  49 -1  N  VAL B  49   O  GLU B  42           
SHEET    1   E 3 ARG B 131  ILE B 136  0                                        
SHEET    2   E 3 LEU B  76  ILE B  83 -1  N  ILE B  83   O  ARG B 131           
SHEET    3   E 3 LYS B  90  LYS B  98 -1  N  LYS B  98   O  LEU B  76           
SHEET    1   F 5 LEU C  36  ALA C  38  0                                        
SHEET    2   F 5 VAL C  13  VAL C  17 -1  N  HIS C  15   O  LEU C  36           
SHEET    3   F 5 TYR C 151  ALA C 156 -1  N  ILE C 154   O  ALA C  14           
SHEET    4   F 5 GLY C  54  GLN C  67 -1  N  GLN C  61   O  TYR C 151           
SHEET    5   F 5 PRO C 113  LEU C 126 -1  N  LEU C 126   O  GLY C  54           
SHEET    1   G 2 GLU C  42  ARG C  44  0                                        
SHEET    2   G 2 GLN C  47  VAL C  49 -1  N  VAL C  49   O  GLU C  42           
SHEET    1   H 3 ARG C 131  ILE C 136  0                                        
SHEET    2   H 3 LEU C  75  ILE C  83 -1  N  ILE C  83   O  ARG C 131           
SHEET    3   H 3 LYS C  90  SER C  99 -1  N  LYS C  98   O  LEU C  76           
SHEET    1   I 5 LEU D  36  ALA D  38  0                                        
SHEET    2   I 5 VAL D  13  VAL D  17 -1  N  HIS D  15   O  LEU D  36           
SHEET    3   I 5 TYR D 151  ALA D 156 -1  N  ILE D 154   O  ALA D  14           
SHEET    4   I 5 GLY D  54  GLN D  67 -1  N  GLN D  61   O  TYR D 151           
SHEET    5   I 5 PRO D 113  LEU D 126 -1  N  LEU D 126   O  GLY D  54           
SHEET    1   J 3 ARG D 131  ILE D 136  0                                        
SHEET    2   J 3 LEU D  76  ILE D  83 -1  N  ILE D  83   O  ARG D 131           
SHEET    3   J 3 LYS D  90  LYS D  98 -1  N  LYS D  98   O  LEU D  76           
SHEET    1   K 5 LEU E  36  ALA E  38  0                                        
SHEET    2   K 5 VAL E  13  VAL E  17 -1  N  HIS E  15   O  LEU E  36           
SHEET    3   K 5 TYR E 151  ALA E 156 -1  N  ILE E 154   O  ALA E  14           
SHEET    4   K 5 GLY E  54  GLN E  67 -1  N  GLN E  61   O  TYR E 151           
SHEET    5   K 5 PRO E 113  LEU E 126 -1  N  LEU E 126   O  GLY E  54           
SHEET    1   L 3 ARG E 131  ILE E 136  0                                        
SHEET    2   L 3 LEU E  75  ILE E  83 -1  N  ILE E  83   O  ARG E 131           
SHEET    3   L 3 LYS E  90  SER E  99 -1  N  LYS E  98   O  LEU E  76           
SHEET    1   M 5 LEU F  36  ALA F  38  0                                        
SHEET    2   M 5 VAL F  13  VAL F  17 -1  N  HIS F  15   O  LEU F  36           
SHEET    3   M 5 TYR F 151  ALA F 156 -1  N  ILE F 154   O  ALA F  14           
SHEET    4   M 5 GLY F  54  GLN F  67 -1  N  GLN F  61   O  TYR F 151           
SHEET    5   M 5 PRO F 113  LEU F 126 -1  N  LEU F 126   O  GLY F  54           
SHEET    1   N 2 GLU F  42  ARG F  44  0                                        
SHEET    2   N 2 GLN F  47  VAL F  49 -1  N  VAL F  49   O  GLU F  42           
SHEET    1   O 3 ARG F 131  ILE F 136  0                                        
SHEET    2   O 3 LEU F  76  ILE F  83 -1  N  ILE F  83   O  ARG F 131           
SHEET    3   O 3 LYS F  90  LYS F  98 -1  N  LYS F  98   O  LEU F  76           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  2.47  
SSBOND   2 CYS E   69    CYS E  101                          1555   1555  2.24  
SSBOND   3 CYS F   69    CYS F  101                          1555   1555  2.45  
CRYST1   94.170   94.560   95.890  90.00  90.00  90.00 P 21 21 21   24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010619  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010575  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010429        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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