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Database: PDB
Entry: 4TWT
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Original site: 4TWT 
HEADER    CYTOKINE/INHIBITOR                      01-JUL-14   4TWT              
TITLE     HUMAN TNFA DIMER IN COMPLEX WITH THE SEMI-SYNTHETIC BICYCLIC PEPTIDE  
TITLE    2 M21                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 77-233;                                       
COMPND   5 SYNONYM: CACHECTIN,TNF-ALPHA,TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY
COMPND   6 MEMBER 2,TNF-A;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: ALA-CYS-PRO-PRO-CYS-LEU-TRP-GLN-VAL-LEU-CYS-GLY;           
COMPND  10 CHAIN: E, F;                                                         
COMPND  11 SYNONYM: PEPTIDE M21;                                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNF, TNFA, TNFSF2;                                             
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    TUMOR NECROSIS FACTOR-ALPHA, BICYCLO COMPOUNDS, PEPTIDES, CYTOKINE-   
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LUZI,Y.KONDO,E.BERNARD,L.STADLER,G.WINTER,P.HOLLIGER                
REVDAT   1   04-FEB-15 4TWT    0                                                
JRNL        AUTH   S.LUZI,Y.KONDO,E.BERNARD,L.K.STADLER,M.VAYSBURD,G.WINTER,    
JRNL        AUTH 2 P.HOLLIGER                                                   
JRNL        TITL   SUBUNIT DISASSEMBLY AND INHIBITION OF TNF ALPHA BY A         
JRNL        TITL 2 SEMI-SYNTHETIC BICYCLIC PEPTIDE.                             
JRNL        REF    PROTEIN ENG.DES.SEL.          V.  28    45 2015              
JRNL        REFN                   ESSN 1741-0134                               
JRNL        PMID   25614525                                                     
JRNL        DOI    10.1093/PROTEIN/GZU055                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.79                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 18737                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.286                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1005                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1360                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3710                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.4420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4533                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 60                                      
REMARK   3   SOLVENT ATOMS            : 36                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : 0.31000                                              
REMARK   3    B33 (A**2) : -1.00000                                             
REMARK   3    B12 (A**2) : 0.15000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 3.012         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.414         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.355         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.940        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4696 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4509 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6383 ; 1.692 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10315 ; 2.596 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   574 ; 6.892 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   200 ;39.507 ;24.550       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   726 ;17.151 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.942 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   725 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5283 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1057 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2331 ; 5.801 ; 8.172       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2331 ; 5.801 ; 8.172       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2892 ; 9.173 ;12.219       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2893 ; 9.171 ;12.220       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2365 ; 5.701 ; 8.442       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2365 ; 5.693 ; 8.443       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3492 ; 8.722 ;12.521       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 18211 ;14.881 ;76.393       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 18210 ;14.881 ;76.394       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 7                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A    10    157       B    10    157    7253  0.16  0.05     
REMARK   3    2     A     9    157       C     9    157    7540  0.16  0.05     
REMARK   3    3     A     9    157       D     9    157    6567  0.18  0.05     
REMARK   3    4     B    10    157       C    10    157    7042  0.17  0.05     
REMARK   3    5     B    10    157       D    10    157    6791  0.16  0.05     
REMARK   3    6     E     1     12       F     1     12     476  0.12  0.05     
REMARK   3    7     C     9    157       D     9    157    6621  0.18  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4TWT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202347.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAY-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19797                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.14400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.24700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1TNF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: HEXAGONAL                                                    
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.5% PEG 8000, 0.085 M NA CACODYLATE    
REMARK 280  PH 6.5, 0.17M AMMONIUM SULFATE, 15% GLYCEROL., VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      153.58333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       76.79167            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       76.79167            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      153.58333            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, 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     VAL A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     ARG B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     ASN B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     PRO C   106                                                      
REMARK 465     GLU C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     ALA C   109                                                      
REMARK 465     GLU C   110                                                      
REMARK 465     ALA C   111                                                      
REMARK 465     VAL D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ARG D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ARG D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     ASN D    34                                                      
REMARK 465     ALA D    35                                                      
REMARK 465     LEU D    36                                                      
REMARK 465     LEU D    37                                                      
REMARK 465     ALA D    38                                                      
REMARK 465     PRO D    70                                                      
REMARK 465     GLU D   104                                                      
REMARK 465     THR D   105                                                      
REMARK 465     PRO D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     GLY D   108                                                      
REMARK 465     ALA D   109                                                      
REMARK 465     GLU D   110                                                      
REMARK 465     ALA D   111                                                      
REMARK 465     LYS D   112                                                      
REMARK 465     ASP D   143                                                      
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     GLN A  21    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  23    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  32    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     LEU A 157    O                                                   
REMARK 470     ARG B 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 104    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 112    CG   CD   CE   NZ                                   
REMARK 470     LEU B 157    O                                                   
REMARK 470     GLU C  23    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 103    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 104    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 112    CG   CD   CE   NZ                                   
REMARK 470     LEU C 157    O                                                   
REMARK 470     GLU D  23    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS D  73    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU D 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 C    38     O    HOH C   308              1.92            
REMARK 500   O    GLU A   107     O    ALA A   109              2.09            
REMARK 500   O    VAL C    13     O    LEU C    37              2.13            
REMARK 500   OXT  GLY E    12     O2   GOL E   102              2.14            
REMARK 500   O    CYS C    69     O    GLU C   104              2.19            
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    ASN B  39       35.39     73.62                                   
REMARK 500    ALA C  38       31.23     71.37                                   
REMARK 500    ASN C  39      -61.96     73.51                                   
REMARK 500    HIS C  73       52.88    -90.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A   31     ARG A   32                  143.50                    
REMARK 500 SER D   86     TYR D   87                 -125.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for peptide chain E                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for peptide chain F                   
DBREF  4TWT A    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  4TWT B    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  4TWT E    1    12  PDB    4TWT     4TWT             1     12             
DBREF  4TWT F    1    12  PDB    4TWT     4TWT             1     12             
DBREF  4TWT C    1   157  UNP    P01375   TNFA_HUMAN      77    233             
DBREF  4TWT D    1   157  UNP    P01375   TNFA_HUMAN      77    233             
SEQRES   1 A  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 A  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 A  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 A  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 A  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 A  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 A  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 A  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 A  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 A  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 A  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 A  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 A  157  LEU                                                          
SEQRES   1 B  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 B  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 B  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 B  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 B  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 B  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 B  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 B  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 B  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 B  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 B  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 B  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 B  157  LEU                                                          
SEQRES   1 E   12  ALA CYS PRO PRO CYS LEU TRP GLN VAL LEU CYS GLY              
SEQRES   1 F   12  ALA CYS PRO PRO CYS LEU TRP GLN VAL LEU CYS GLY              
SEQRES   1 C  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 C  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 C  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 C  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 C  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 C  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 C  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 C  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 C  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 C  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 C  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 C  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 C  157  LEU                                                          
SEQRES   1 D  157  VAL ARG SER SER SER ARG THR PRO SER ASP LYS PRO VAL          
SEQRES   2 D  157  ALA HIS VAL VAL ALA ASN PRO GLN ALA GLU GLY GLN LEU          
SEQRES   3 D  157  GLN TRP LEU ASN ARG ARG ALA ASN ALA LEU LEU ALA ASN          
SEQRES   4 D  157  GLY VAL GLU LEU ARG ASP ASN GLN LEU VAL VAL PRO SER          
SEQRES   5 D  157  GLU GLY LEU TYR LEU ILE TYR SER GLN VAL LEU PHE LYS          
SEQRES   6 D  157  GLY GLN GLY CYS PRO SER THR HIS VAL LEU LEU THR HIS          
SEQRES   7 D  157  THR ILE SER ARG ILE ALA VAL SER TYR GLN THR LYS VAL          
SEQRES   8 D  157  ASN LEU LEU SER ALA ILE LYS SER PRO CYS GLN ARG GLU          
SEQRES   9 D  157  THR PRO GLU GLY ALA GLU ALA LYS PRO TRP TYR GLU PRO          
SEQRES  10 D  157  ILE TYR LEU GLY GLY VAL PHE GLN LEU GLU LYS GLY ASP          
SEQRES  11 D  157  ARG LEU SER ALA GLU ILE ASN ARG PRO ASP TYR LEU ASP          
SEQRES  12 D  157  PHE ALA GLU SER GLY GLN VAL TYR PHE GLY ILE ILE ALA          
SEQRES  13 D  157  LEU                                                          
HET    GOL  B 201       6                                                       
HET    GOL  B 202       6                                                       
HET    GOL  E 101       6                                                       
HET    GOL  E 102       6                                                       
HET    38A  E 103      12                                                       
HET    38A  F 101      12                                                       
HET    GOL  C 201       6                                                       
HET    GOL  D 201       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     38A (2,4,6-TRIMETHYLBENZENE-1,3,5-TRIYL)TRIMETHANOL                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GOL    6(C3 H8 O3)                                                  
FORMUL  11  38A    2(C12 H18 O3)                                                
FORMUL  15  HOH   *36(H2 O)                                                     
HELIX    1 AA1 ARG A  138  LEU A  142  5                                   5    
HELIX    2 AA2 ARG B  138  LEU B  142  5                                   5    
HELIX    3 AA3 TRP E    7  GLY E   12  5                                   6    
HELIX    4 AA4 CYS F    5  CYS F   11  5                                   7    
HELIX    5 AA5 ARG C  138  LEU C  142  5                                   5    
HELIX    6 AA6 ARG D  138  LEU D  142  5                                   5    
SHEET    1 AA1 3 TRP A  28  LEU A  29  0                                        
SHEET    2 AA1 3 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA1 3 LEU A  36  ALA A  38 -1  O  LEU A  36   N  HIS A  15           
SHEET    1 AA2 5 TRP A  28  LEU A  29  0                                        
SHEET    2 AA2 5 VAL A  13  ALA A  18 -1  N  VAL A  17   O  LEU A  29           
SHEET    3 AA2 5 TYR A 151  ALA A 156 -1  O  PHE A 152   N  VAL A  16           
SHEET    4 AA2 5 GLY A  54  GLN A  67 -1  N  TYR A  59   O  GLY A 153           
SHEET    5 AA2 5 PRO A 113  LEU A 126 -1  O  TRP A 114   N  GLY A  66           
SHEET    1 AA310 GLU A  42  ARG A  44  0                                        
SHEET    2 AA310 GLN A  47  VAL A  49 -1  O  VAL A  49   N  GLU A  42           
SHEET    3 AA310 ARG A 131  ILE A 136 -1  O  LEU A 132   N  LEU A  48           
SHEET    4 AA310 LEU A  76  ILE A  83 -1  N  THR A  79   O  GLU A 135           
SHEET    5 AA310 LYS A  90  LYS A  98 -1  O  LYS A  98   N  LEU A  76           
SHEET    6 AA310 LYS C  90  LYS C  98 -1  O  LYS C  90   N  SER A  95           
SHEET    7 AA310 LEU C  76  ILE C  83 -1  N  LEU C  76   O  LYS C  98           
SHEET    8 AA310 ARG C 131  ILE C 136 -1  O  GLU C 135   N  THR C  79           
SHEET    9 AA310 GLN C  47  VAL C  49 -1  N  LEU C  48   O  LEU C 132           
SHEET   10 AA310 GLU C  42  ARG C  44 -1  N  GLU C  42   O  VAL C  49           
SHEET    1 AA4 4 VAL B  13  VAL B  17  0                                        
SHEET    2 AA4 4 TYR B 151  ALA B 156 -1  O  PHE B 152   N  VAL B  16           
SHEET    3 AA4 4 GLY B  54  GLN B  67 -1  N  TYR B  59   O  GLY B 153           
SHEET    4 AA4 4 PRO B 113  LEU B 126 -1  O  TRP B 114   N  GLY B  66           
SHEET    1 AA5 5 GLU B  42  ARG B  44  0                                        
SHEET    2 AA5 5 GLN B  47  VAL B  49 -1  O  VAL B  49   N  GLU B  42           
SHEET    3 AA5 5 ARG B 131  ILE B 136 -1  O  LEU B 132   N  LEU B  48           
SHEET    4 AA5 5 LEU B  76  ILE B  83 -1  N  THR B  79   O  GLU B 135           
SHEET    5 AA5 5 LYS B  90  LYS B  98 -1  O  LYS B  98   N  LEU B  76           
SHEET    1 AA6 5 TRP C  28  LEU C  29  0                                        
SHEET    2 AA6 5 VAL C  13  ALA C  18 -1  N  VAL C  17   O  LEU C  29           
SHEET    3 AA6 5 TYR C 151  ALA C 156 -1  O  PHE C 152   N  VAL C  16           
SHEET    4 AA6 5 GLY C  54  GLN C  67 -1  N  TYR C  59   O  GLY C 153           
SHEET    5 AA6 5 PRO C 113  LEU C 126 -1  O  TRP C 114   N  GLY C  66           
SHEET    1 AA7 5 TRP D  28  LEU D  29  0                                        
SHEET    2 AA7 5 VAL D  13  ALA D  18 -1  N  VAL D  17   O  LEU D  29           
SHEET    3 AA7 5 TYR D 151  ALA D 156 -1  O  PHE D 152   N  VAL D  16           
SHEET    4 AA7 5 GLY D  54  GLY D  66 -1  N  TYR D  59   O  GLY D 153           
SHEET    5 AA7 5 TRP D 114  LEU D 126 -1  O  TRP D 114   N  GLY D  66           
SHEET    1 AA8 5 GLU D  42  ARG D  44  0                                        
SHEET    2 AA8 5 GLN D  47  VAL D  49 -1  O  VAL D  49   N  GLU D  42           
SHEET    3 AA8 5 ARG D 131  ILE D 136 -1  O  LEU D 132   N  LEU D  48           
SHEET    4 AA8 5 LEU D  76  ILE D  83 -1  N  THR D  79   O  GLU D 135           
SHEET    5 AA8 5 LYS D  90  LYS D  98 -1  O  LYS D  98   N  LEU D  76           
SSBOND   1 CYS A   69    CYS A  101                          1555   1555  1.95  
SSBOND   2 CYS B   69    CYS B  101                          1555   1555  1.99  
SSBOND   3 CYS C   69    CYS C  101                          1555   1555  2.01  
SSBOND   4 CYS D   69    CYS D  101                          1555   1555  2.02  
LINK         SG  CYS E   2                 CAK 38A E 103     1555   1555  1.66  
LINK         SG  CYS E   5                 CAJ 38A E 103     1555   1555  1.68  
LINK         SG  CYS E  11                 CAL 38A E 103     1555   1555  1.66  
LINK         SG  CYS F   2                 CAK 38A F 101     1555   1555  1.60  
LINK         SG  CYS F   5                 CAJ 38A F 101     1555   1555  1.65  
LINK         SG  CYS F  11                 CAL 38A F 101     1555   1555  1.63  
SITE     1 AC1  4 TYR A 119  PRO B 117  ILE B 118  TYR B 119                    
SITE     1 AC2  5 LEU B  26  ALA B 134  GLU B 135  ILE B 136                    
SITE     2 AC2  5 PRO B 139                                                     
SITE     1 AC3  4 ARG A 138  TYR A 141  ALA E   1  CYS E   2                    
SITE     1 AC4  1 GLY E  12                                                     
SITE     1 AC5  1 PRO C  51                                                     
SITE     1 AC6  4 PRO C 117  ILE C 118  TYR C 119  TYR D 119                    
SITE     1 AC7 13 LEU A  57  TYR A 119  ARG A 138  TYR A 141                    
SITE     2 AC7 13 LEU A 157  HIS B  15  LEU B  57  TYR B  59                    
SITE     3 AC7 13 LEU B 120  GLY B 148  GLN B 149  TYR B 151                    
SITE     4 AC7 13 TYR C  87                                                     
SITE     1 AC8  9 TYR C 119  LEU C 157  HIS D  15  LEU D  57                    
SITE     2 AC8  9 TYR D  59  SER D 147  GLY D 148  GLN D 149                    
SITE     3 AC8  9 TYR D 151                                                     
CRYST1   78.444   78.444  230.375  90.00  90.00 120.00 P 32 2 1     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      0.012748  0.007360  0.000000        0.00000                         
SCALE2      0.000000  0.014720  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004341        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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