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Database: PDB
Entry: 3FXI
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Original site: 3FXI 
HEADER    IMMUNE SYSTEM                           21-JAN-09   3FXI              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN TLR4-HUMAN MD-2-E.COLI LPS RA COMPLEX  
CAVEAT     3FXI    PA1 E 2 HAS WRONG CHIRALITY AT ATOM C1                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLL-LIKE RECEPTOR 4;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 27-631;                     
COMPND   5 SYNONYM: TLR4, HTOLL;                                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 SYNONYM: MD-2, PROTEIN MD-2, ESOP-1;                                 
COMPND  11 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: TLR4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL: HIGH FIVE CELLS;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PACGP67A;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ESOP1, LY96, MD-2, MD2;                                        
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL: HIGH FIVE CELLS;                             
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PACGP67A                                  
KEYWDS    LEUCINE RICH REPEAT, GLYCOPROTEIN, IMMUNE RESPONSE, INFLAMMATORY      
KEYWDS   2 RESPONSE, INNATE IMMUNITY, MEMBRANE, RECEPTOR, TRANSMEMBRANE,        
KEYWDS   3 SECRETED, IMMUNE SYSTEM                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.S.PARK,D.H.SONG,H.M.KIM,J.-O.LEE                                    
REVDAT   6   29-JUL-20 3FXI    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   6 2                   1       LINK   SITE   ATOM                       
REVDAT   5   01-JUL-20 3FXI    1       CAVEAT REMARK LINK                       
REVDAT   4   20-JUN-12 3FXI    1       HETNAM                                   
REVDAT   3   13-JUL-11 3FXI    1       VERSN                                    
REVDAT   2   12-MAY-09 3FXI    1       JRNL                                     
REVDAT   1   03-MAR-09 3FXI    0                                                
JRNL        AUTH   B.S.PARK,D.H.SONG,H.M.KIM,B.-S.CHOI,H.LEE,J.-O.LEE           
JRNL        TITL   THE STRUCTURAL BASIS OF LIPOPOLYSACCHARIDE RECOGNITION BY    
JRNL        TITL 2 THE TLR4-MD-2 COMPLEX                                        
JRNL        REF    NATURE                        V. 458  1191 2009              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   19252480                                                     
JRNL        DOI    10.1038/NATURE07830                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2098397.300                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 41542                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2068                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5872                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3610                       
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 289                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11872                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 626                                     
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 91.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.72000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 13.24000                                             
REMARK   3    B13 (A**2) : -22.96000                                            
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.67                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.80                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.790                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051162.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 41586                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.10100                            
REMARK 200  R SYM                      (I) : 0.10100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.880                              
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: PDB ENTRY 2Z65, 2Z66                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MGCL2, 0.1M NA-HEPES PH 7.5, 30%    
REMARK 280  PEG MME 550, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 278K        
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       45.58000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      125.90500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      125.90500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.58000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 27360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 142.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J          
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     GLN A   628                                                      
REMARK 465     MET A   629                                                      
REMARK 465     ASN A   630                                                      
REMARK 465     LYS A   631                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     MET B   629                                                      
REMARK 465     ASN B   630                                                      
REMARK 465     LYS B   631                                                      
REMARK 465     SER C   159                                                      
REMARK 465     ASN C   160                                                      
REMARK 465     SER D   159                                                      
REMARK 465     ASN D   160                                                      
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   N2   GCS H     2     C1   FTT B  1005              1.34            
REMARK 500   N2   PA1 H     1     C1   FTT B  1003              1.35            
REMARK 500   N2   PA1 E     1     C1   FTT A  1003              1.35            
REMARK 500   N2   PA1 E     2     C1   FTT A  1005              1.35            
REMARK 500   O3   PA1 E     2     C1   FTT A  1006              1.41            
REMARK 500   O3   GCS H     2     C1   FTT B  1006              1.41            
REMARK 500   O3   PA1 H     1     C1   FTT B  1004              1.42            
REMARK 500   O3   PA1 E     1     C1   FTT A  1004              1.42            
REMARK 500   O4   PA1 E     2     P    PO4 A  1010              1.47            
REMARK 500   O4   GCS H     2     P    PO4 B  1010              1.48            
REMARK 500   O1   PA1 H     1     P    PO4 B  1011              1.50            
REMARK 500   O1   PA1 E     1     P    PO4 A  1011              1.50            
REMARK 500   O6   GCS H     2     O6   KDO H     3              2.14            
REMARK 500   O6   PA1 E     2     O6   KDO E     3              2.14            
REMARK 500   O4   KDO H     3     C3   KDO H     7              2.15            
REMARK 500   O4   KDO E     3     C3   KDO E     7              2.15            
REMARK 500   ND2  ASN B   497     O5   NAG B   841              2.19            
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    ARG A  67   CB  -  CA  -  C   ANGL. DEV. = -13.8 DEGREES          
REMARK 500    HIS A  68   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ARG B  67   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    HIS B  68   N   -  CA  -  CB  ANGL. DEV. =  11.2 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    ASN A  35        4.33     57.61                                   
REMARK 500    ILE A  36      -53.10   -130.25                                   
REMARK 500    CYS A  40       58.16    -98.71                                   
REMARK 500    ASP A  50      -18.88   -141.11                                   
REMARK 500    ASN A  51       24.33    -74.48                                   
REMARK 500    PRO A  53      159.39    -47.10                                   
REMARK 500    ARG A  67       -7.37     64.42                                   
REMARK 500    PHE A  75      -25.33   -146.66                                   
REMARK 500    GLU A  89       17.24     52.29                                   
REMARK 500    LEU A 101       69.77   -112.58                                   
REMARK 500    ASN A 137       10.82     59.33                                   
REMARK 500    LYS A 166      103.15    -59.90                                   
REMARK 500    TYR A 170       -9.15    -59.52                                   
REMARK 500    ASN A 185     -156.45   -126.33                                   
REMARK 500    PRO A 202      -77.13    -49.01                                   
REMARK 500    LEU A 204       81.24   -177.66                                   
REMARK 500    PRO A 214       64.29    -69.43                                   
REMARK 500    ASN A 216        4.52   -157.87                                   
REMARK 500    PHE A 272       71.40   -150.51                                   
REMARK 500    LYS A 274       -0.31    -52.08                                   
REMARK 500    TYR A 292      116.49     76.91                                   
REMARK 500    ASP A 298      -65.56    -99.69                                   
REMARK 500    ARG A 322       14.11    -64.46                                   
REMARK 500    ASN A 365       20.25   -147.01                                   
REMARK 500    LEU A 372       76.97   -115.47                                   
REMARK 500    GLN A 430      129.44    -38.85                                   
REMARK 500    SER A 438       53.65   -100.36                                   
REMARK 500    PHE A 440     -177.51    172.88                                   
REMARK 500    ALA A 462       34.95   -154.62                                   
REMARK 500    ASN A 464       13.08    -69.78                                   
REMARK 500    ASN A 481     -134.59    -93.38                                   
REMARK 500    ASN A 497        2.07    -61.63                                   
REMARK 500    LEU A 498      109.98    -49.97                                   
REMARK 500    LEU A 501       97.81   -163.72                                   
REMARK 500    LEU A 503       28.54   -148.19                                   
REMARK 500    GLN A 505       18.97     46.10                                   
REMARK 500    GLN A 507       24.26     48.11                                   
REMARK 500    GLU A 509      -62.29   -123.56                                   
REMARK 500    ALA A 515      -87.93    -40.75                                   
REMARK 500    ASN A 517       -9.32    -45.62                                   
REMARK 500    LEU A 525       95.54   -164.07                                   
REMARK 500    MET A 527       23.60   -143.78                                   
REMARK 500    HIS A 529       48.42     19.96                                   
REMARK 500    ASN A 530     -155.28   -102.15                                   
REMARK 500    THR A 537       -5.77   -153.74                                   
REMARK 500    LEU A 549       84.97   -158.09                                   
REMARK 500    TYR A 551       14.96   -148.99                                   
REMARK 500    SER A 552     -179.11    -63.72                                   
REMARK 500    LEU A 553       28.72     38.50                                   
REMARK 500    ASN A 554     -153.67    -95.44                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     169 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 RESIDUES FROM 1001 TO 1018 IN THE CHAINS A AND B ARE E.COLI          
REMARK 600 LIPOPOLYSACCHARIDES                                                  
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A   1   O                                                      
REMARK 620 2 ASP A 294   OD2  61.5                                              
REMARK 620 N                    1                                               
DBREF  3FXI A   27   631  UNP    O00206   TLR4_HUMAN      27    631             
DBREF  3FXI B   27   631  UNP    O00206   TLR4_HUMAN      27    631             
DBREF  3FXI C   19   160  UNP    Q9Y6Y9   LY96_HUMAN      19    160             
DBREF  3FXI D   19   160  UNP    Q9Y6Y9   LY96_HUMAN      19    160             
SEQRES   1 A  605  GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN          
SEQRES   2 A  605  CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU          
SEQRES   3 A  605  PRO PHE SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO          
SEQRES   4 A  605  LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO          
SEQRES   5 A  605  GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN          
SEQRES   6 A  605  THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU          
SEQRES   7 A  605  SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU          
SEQRES   8 A  605  ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS          
SEQRES   9 A  605  LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN          
SEQRES  10 A  605  PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN          
SEQRES  11 A  605  VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU          
SEQRES  12 A  605  TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU          
SEQRES  13 A  605  SER SER ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU          
SEQRES  14 A  605  ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU          
SEQRES  15 A  605  ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY          
SEQRES  16 A  605  ALA PHE LYS GLU ILE ARG LEU HIS LYS LEU THR LEU ARG          
SEQRES  17 A  605  ASN ASN PHE ASP SER LEU ASN VAL MET LYS THR CYS ILE          
SEQRES  18 A  605  GLN GLY LEU ALA GLY LEU GLU VAL HIS ARG LEU VAL LEU          
SEQRES  19 A  605  GLY GLU PHE ARG ASN GLU GLY ASN LEU GLU LYS PHE ASP          
SEQRES  20 A  605  LYS SER ALA LEU GLU GLY LEU CYS ASN LEU THR ILE GLU          
SEQRES  21 A  605  GLU PHE ARG LEU ALA TYR LEU ASP TYR TYR LEU ASP ASP          
SEQRES  22 A  605  ILE ILE ASP LEU PHE ASN CYS LEU THR ASN VAL SER SER          
SEQRES  23 A  605  PHE SER LEU VAL SER VAL THR ILE GLU ARG VAL LYS ASP          
SEQRES  24 A  605  PHE SER TYR ASN PHE GLY TRP GLN HIS LEU GLU LEU VAL          
SEQRES  25 A  605  ASN CYS LYS PHE GLY GLN PHE PRO THR LEU LYS LEU LYS          
SEQRES  26 A  605  SER LEU LYS ARG LEU THR PHE THR SER ASN LYS GLY GLY          
SEQRES  27 A  605  ASN ALA PHE SER GLU VAL ASP LEU PRO SER LEU GLU PHE          
SEQRES  28 A  605  LEU ASP LEU SER ARG ASN GLY LEU SER PHE LYS GLY CYS          
SEQRES  29 A  605  CYS SER GLN SER ASP PHE GLY THR THR SER LEU LYS TYR          
SEQRES  30 A  605  LEU ASP LEU SER PHE ASN GLY VAL ILE THR MET SER SER          
SEQRES  31 A  605  ASN PHE LEU GLY LEU GLU GLN LEU GLU HIS LEU ASP PHE          
SEQRES  32 A  605  GLN HIS SER ASN LEU LYS GLN MET SER GLU PHE SER VAL          
SEQRES  33 A  605  PHE LEU SER LEU ARG ASN LEU ILE TYR LEU ASP ILE SER          
SEQRES  34 A  605  HIS THR HIS THR ARG VAL ALA PHE ASN GLY ILE PHE ASN          
SEQRES  35 A  605  GLY LEU SER SER LEU GLU VAL LEU LYS MET ALA GLY ASN          
SEQRES  36 A  605  SER PHE GLN GLU ASN PHE LEU PRO ASP ILE PHE THR GLU          
SEQRES  37 A  605  LEU ARG ASN LEU THR PHE LEU ASP LEU SER GLN CYS GLN          
SEQRES  38 A  605  LEU GLU GLN LEU SER PRO THR ALA PHE ASN SER LEU SER          
SEQRES  39 A  605  SER LEU GLN VAL LEU ASN MET SER HIS ASN ASN PHE PHE          
SEQRES  40 A  605  SER LEU ASP THR PHE PRO TYR LYS CYS LEU ASN SER LEU          
SEQRES  41 A  605  GLN VAL LEU ASP TYR SER LEU ASN HIS ILE MET THR SER          
SEQRES  42 A  605  LYS LYS GLN GLU LEU GLN HIS PHE PRO SER SER LEU ALA          
SEQRES  43 A  605  PHE LEU ASN LEU THR GLN ASN ASP PHE ALA CYS THR CYS          
SEQRES  44 A  605  GLU HIS GLN SER PHE LEU GLN TRP ILE LYS ASP GLN ARG          
SEQRES  45 A  605  GLN LEU LEU VAL GLU VAL GLU ARG MET GLU CYS ALA THR          
SEQRES  46 A  605  PRO SER ASP LYS GLN GLY MET PRO VAL LEU SER LEU ASN          
SEQRES  47 A  605  ILE THR CYS GLN MET ASN LYS                                  
SEQRES   1 B  605  GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN          
SEQRES   2 B  605  CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU          
SEQRES   3 B  605  PRO PHE SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO          
SEQRES   4 B  605  LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO          
SEQRES   5 B  605  GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN          
SEQRES   6 B  605  THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU          
SEQRES   7 B  605  SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU          
SEQRES   8 B  605  ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS          
SEQRES   9 B  605  LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN          
SEQRES  10 B  605  PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN          
SEQRES  11 B  605  VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU          
SEQRES  12 B  605  TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU          
SEQRES  13 B  605  SER SER ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU          
SEQRES  14 B  605  ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU          
SEQRES  15 B  605  ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY          
SEQRES  16 B  605  ALA PHE LYS GLU ILE ARG LEU HIS LYS LEU THR LEU ARG          
SEQRES  17 B  605  ASN ASN PHE ASP SER LEU ASN VAL MET LYS THR CYS ILE          
SEQRES  18 B  605  GLN GLY LEU ALA GLY LEU GLU VAL HIS ARG LEU VAL LEU          
SEQRES  19 B  605  GLY GLU PHE ARG ASN GLU GLY ASN LEU GLU LYS PHE ASP          
SEQRES  20 B  605  LYS SER ALA LEU GLU GLY LEU CYS ASN LEU THR ILE GLU          
SEQRES  21 B  605  GLU PHE ARG LEU ALA TYR LEU ASP TYR TYR LEU ASP ASP          
SEQRES  22 B  605  ILE ILE ASP LEU PHE ASN CYS LEU THR ASN VAL SER SER          
SEQRES  23 B  605  PHE SER LEU VAL SER VAL THR ILE GLU ARG VAL LYS ASP          
SEQRES  24 B  605  PHE SER TYR ASN PHE GLY TRP GLN HIS LEU GLU LEU VAL          
SEQRES  25 B  605  ASN CYS LYS PHE GLY GLN PHE PRO THR LEU LYS LEU LYS          
SEQRES  26 B  605  SER LEU LYS ARG LEU THR PHE THR SER ASN LYS GLY GLY          
SEQRES  27 B  605  ASN ALA PHE SER GLU VAL ASP LEU PRO SER LEU GLU PHE          
SEQRES  28 B  605  LEU ASP LEU SER ARG ASN GLY LEU SER PHE LYS GLY CYS          
SEQRES  29 B  605  CYS SER GLN SER ASP PHE GLY THR THR SER LEU LYS TYR          
SEQRES  30 B  605  LEU ASP LEU SER PHE ASN GLY VAL ILE THR MET SER SER          
SEQRES  31 B  605  ASN PHE LEU GLY LEU GLU GLN LEU GLU HIS LEU ASP PHE          
SEQRES  32 B  605  GLN HIS SER ASN LEU LYS GLN MET SER GLU PHE SER VAL          
SEQRES  33 B  605  PHE LEU SER LEU ARG ASN LEU ILE TYR LEU ASP ILE SER          
SEQRES  34 B  605  HIS THR HIS THR ARG VAL ALA PHE ASN GLY ILE PHE ASN          
SEQRES  35 B  605  GLY LEU SER SER LEU GLU VAL LEU LYS MET ALA GLY ASN          
SEQRES  36 B  605  SER PHE GLN GLU ASN PHE LEU PRO ASP ILE PHE THR GLU          
SEQRES  37 B  605  LEU ARG ASN LEU THR PHE LEU ASP LEU SER GLN CYS GLN          
SEQRES  38 B  605  LEU GLU GLN LEU SER PRO THR ALA PHE ASN SER LEU SER          
SEQRES  39 B  605  SER LEU GLN VAL LEU ASN MET SER HIS ASN ASN PHE PHE          
SEQRES  40 B  605  SER LEU ASP THR PHE PRO TYR LYS CYS LEU ASN SER LEU          
SEQRES  41 B  605  GLN VAL LEU ASP TYR SER LEU ASN HIS ILE MET THR SER          
SEQRES  42 B  605  LYS LYS GLN GLU LEU GLN HIS PHE PRO SER SER LEU ALA          
SEQRES  43 B  605  PHE LEU ASN LEU THR GLN ASN ASP PHE ALA CYS THR CYS          
SEQRES  44 B  605  GLU HIS GLN SER PHE LEU GLN TRP ILE LYS ASP GLN ARG          
SEQRES  45 B  605  GLN LEU LEU VAL GLU VAL GLU ARG MET GLU CYS ALA THR          
SEQRES  46 B  605  PRO SER ASP LYS GLN GLY MET PRO VAL LEU SER LEU ASN          
SEQRES  47 B  605  ILE THR CYS GLN MET ASN LYS                                  
SEQRES   1 C  142  GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP ALA SER          
SEQRES   2 C  142  ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR PRO ILE          
SEQRES   3 C  142  SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS GLY SER          
SEQRES   4 C  142  LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG ARG ASP          
SEQRES   5 C  142  LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR VAL ASN          
SEQRES   6 C  142  THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE CYS ARG          
SEQRES   7 C  142  GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA LEU LYS          
SEQRES   8 C  142  GLY GLU THR VAL ASN THR THR ILE SER PHE SER PHE LYS          
SEQRES   9 C  142  GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS VAL VAL          
SEQRES  10 C  142  GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU PHE CYS          
SEQRES  11 C  142  LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN SER ASN              
SEQRES   1 D  142  GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP ALA SER          
SEQRES   2 D  142  ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR PRO ILE          
SEQRES   3 D  142  SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS GLY SER          
SEQRES   4 D  142  LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG ARG ASP          
SEQRES   5 D  142  LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR VAL ASN          
SEQRES   6 D  142  THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE CYS ARG          
SEQRES   7 D  142  GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA LEU LYS          
SEQRES   8 D  142  GLY GLU THR VAL ASN THR THR ILE SER PHE SER PHE LYS          
SEQRES   9 D  142  GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS VAL VAL          
SEQRES  10 D  142  GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU PHE CYS          
SEQRES  11 D  142  LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN SER ASN              
MODRES 3FXI ASN A  173  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN A  205  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN A  497  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN A  526  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN A  575  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN B  173  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN B  205  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN B  497  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN B  526  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN B  575  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN C  114  ASN  GLYCOSYLATION SITE                                 
MODRES 3FXI ASN D  114  ASN  GLYCOSYLATION SITE                                 
HET    PA1  E   1      12                                                       
HET    PA1  E   2      11                                                       
HET    KDO  E   3      15                                                       
HET    GMH  E   4      13                                                       
HET    GMH  E   5      13                                                       
HET    GMH  E   6      13                                                       
HET    KDO  E   7      15                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    PA1  H   1      12                                                       
HET    GCS  H   2      11                                                       
HET    KDO  H   3      15                                                       
HET    GMH  H   4      13                                                       
HET    GMH  H   5      13                                                       
HET    GMH  H   6      13                                                       
HET    KDO  H   7      15                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    FTT  A1003      16                                                       
HET    FTT  A1004      16                                                       
HET    FTT  A1005      16                                                       
HET    FTT  A1006      16                                                       
HET    DAO  A1007      13                                                       
HET    MYR  A1008      15                                                       
HET    PO4  A1010       4                                                       
HET    PO4  A1011       4                                                       
HET    PO4  A1017       4                                                       
HET    PO4  A1018       4                                                       
HET    NAG  A 711      14                                                       
HET    NAG  A 721      14                                                       
HET    NAG  A 741      14                                                       
HET     MG  A2001       1                                                       
HET    FTT  B1003      16                                                       
HET    FTT  B1004      16                                                       
HET    FTT  B1005      16                                                       
HET    FTT  B1006      16                                                       
HET    DAO  B1007      13                                                       
HET    MYR  B1008      15                                                       
HET    PO4  B1010       4                                                       
HET    PO4  B1011       4                                                       
HET    PO4  B1017       4                                                       
HET    PO4  B1018       4                                                       
HET    NAG  B 811      14                                                       
HET    NAG  B 821      14                                                       
HET    NAG  B 841      14                                                       
HET     MG  B2001       1                                                       
HET    NAG  C 751      14                                                       
HET    NAG  D 851      14                                                       
HETNAM     PA1 2-AMINO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                            
HETNAM     KDO 3-DEOXY-ALPHA-D-MANNO-OCT-2-ULOPYRANOSONIC ACID                  
HETNAM     GMH L-GLYCERO-ALPHA-D-MANNO-HEPTOPYRANOSE                            
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GCS 2-AMINO-2-DEOXY-BETA-D-GLUCOPYRANOSE                             
HETNAM     FTT 3-HYDROXY-TETRADECANOIC ACID                                     
HETNAM     DAO LAURIC ACID                                                      
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GCS 2-AMINO-2-DEOXY-D-GLUCOSE                                        
HETSYN     FTT 3-HYDROXY-MYRISTIC ACID                                          
FORMUL   5  PA1    3(C6 H13 N O5)                                               
FORMUL   5  KDO    4(C8 H14 O8)                                                 
FORMUL   5  GMH    6(C7 H14 O7)                                                 
FORMUL   6  NAG    16(C8 H15 N O6)                                              
FORMUL   8  GCS    C6 H13 N O5                                                  
FORMUL  11  FTT    8(C14 H28 O3)                                                
FORMUL  15  DAO    2(C12 H24 O2)                                                
FORMUL  16  MYR    2(C14 H28 O2)                                                
FORMUL  17  PO4    8(O4 P 3-)                                                   
FORMUL  24   MG    2(MG 2+)                                                     
FORMUL  41  HOH   *2(H2 O)                                                      
HELIX    1   1 PRO A  168  SER A  172  5                                   5    
HELIX    2   2 TYR A  191  ARG A  196  5                                   6    
HELIX    3   3 VAL A  197  MET A  201  5                                   5    
HELIX    4   4 SER A  239  LEU A  250  1                                  12    
HELIX    5   5 LEU A  277  LEU A  283  5                                   7    
HELIX    6   6 PHE A  304  THR A  308  5                                   5    
HELIX    7   7 GLN A  393  GLY A  397  1                                   5    
HELIX    8   8 GLN A  436  PHE A  440  5                                   5    
HELIX    9   9 PHE A  483  PHE A  487  5                                   5    
HELIX   10  10 ALA A  515  LEU A  519  5                                   5    
HELIX   11  11 PHE A  538  LEU A  543  5                                   6    
HELIX   12  12 THR A  584  GLU A  586  5                                   3    
HELIX   13  13 HIS A  587  GLN A  597  1                                  11    
HELIX   14  14 GLU A  603  MET A  607  5                                   5    
HELIX   15  15 PRO B  168  ASN B  173  5                                   6    
HELIX   16  16 TYR B  191  ARG B  196  5                                   6    
HELIX   17  17 VAL B  197  MET B  201  5                                   5    
HELIX   18  18 SER B  239  LEU B  250  1                                  12    
HELIX   19  19 LEU B  277  LEU B  283  5                                   7    
HELIX   20  20 PHE B  304  THR B  308  5                                   5    
HELIX   21  21 GLN B  436  PHE B  440  5                                   5    
HELIX   22  22 PHE B  483  PHE B  487  5                                   5    
HELIX   23  23 ALA B  515  LEU B  519  5                                   5    
HELIX   24  24 PHE B  538  LEU B  543  5                                   6    
HELIX   25  25 THR B  584  GLU B  586  5                                   3    
HELIX   26  26 HIS B  587  GLN B  597  1                                  11    
HELIX   27  27 GLU B  603  MET B  607  5                                   5    
HELIX   28  28 TYR C  102  ALA C  107  5                                   6    
HELIX   29  29 TYR D  102  ALA D  107  5                                   6    
SHEET    1   A19 VAL A  30  VAL A  33  0                                        
SHEET    2   A19 THR A  37  GLN A  39 -1  O  THR A  37   N  VAL A  33           
SHEET    3   A19 ASN A  58  ASP A  60  1  O  ASN A  58   N  TYR A  38           
SHEET    4   A19 VAL A  82  ASP A  84  1  O  VAL A  82   N  LEU A  59           
SHEET    5   A19 THR A 106  ILE A 108  1  O  THR A 106   N  LEU A  83           
SHEET    6   A19 LYS A 130  VAL A 132  1  O  VAL A 132   N  LEU A 107           
SHEET    7   A19 GLU A 154  ASN A 156  1  O  ASN A 156   N  LEU A 131           
SHEET    8   A19 HIS A 179  ASP A 181  1  O  HIS A 179   N  LEU A 155           
SHEET    9   A19 SER A 207  ASP A 209  1  O  SER A 207   N  LEU A 180           
SHEET   10   A19 ARG A 227  ARG A 234  1  O  LYS A 230   N  LEU A 208           
SHEET   11   A19 GLU A 254  GLY A 261  1  O  VAL A 259   N  LEU A 231           
SHEET   12   A19 THR A 284  LEU A 293  1  O  ALA A 291   N  LEU A 260           
SHEET   13   A19 SER A 312  VAL A 318  1  O  SER A 312   N  PHE A 288           
SHEET   14   A19 HIS A 334  VAL A 338  1  O  HIS A 334   N  PHE A 313           
SHEET   15   A19 ARG A 355  THR A 359  1  O  THR A 357   N  LEU A 335           
SHEET   16   A19 PHE A 377  ASP A 379  1  O  ASP A 379   N  PHE A 358           
SHEET   17   A19 TYR A 403  ASP A 405  1  O  ASP A 405   N  LEU A 378           
SHEET   18   A19 HIS A 426  ASP A 428  1  O  ASP A 428   N  LEU A 404           
SHEET   19   A19 TYR A 451  ASP A 453  1  O  ASP A 453   N  LEU A 427           
SHEET    1   B 2 THR A  92  ILE A  93  0                                        
SHEET    2   B 2 SER A 116  LEU A 117  1  O  SER A 116   N  ILE A  93           
SHEET    1   C 2 SER A 189  ILE A 190  0                                        
SHEET    2   C 2 PHE A 217  ILE A 218  1  O  PHE A 217   N  ILE A 190           
SHEET    1   D 3 PHE A 387  SER A 392  0                                        
SHEET    2   D 3 VAL A 411  LEU A 419  1  O  SER A 415   N  CYS A 390           
SHEET    3   D 3 ASN A 433  LYS A 435  1  O  ASN A 433   N  ILE A 412           
SHEET    1   E19 VAL B  30  VAL B  33  0                                        
SHEET    2   E19 THR B  37  GLN B  39 -1  O  THR B  37   N  VAL B  33           
SHEET    3   E19 ASN B  58  ASP B  60  1  O  ASN B  58   N  TYR B  38           
SHEET    4   E19 VAL B  82  ASP B  84  1  O  VAL B  82   N  LEU B  59           
SHEET    5   E19 THR B 106  ILE B 108  1  O  THR B 106   N  LEU B  83           
SHEET    6   E19 LYS B 130  VAL B 132  1  O  VAL B 132   N  LEU B 107           
SHEET    7   E19 GLU B 154  ASN B 156  1  O  ASN B 156   N  LEU B 131           
SHEET    8   E19 HIS B 179  ASP B 181  1  O  HIS B 179   N  LEU B 155           
SHEET    9   E19 SER B 207  ASP B 209  1  O  SER B 207   N  LEU B 180           
SHEET   10   E19 ARG B 227  ARG B 234  1  O  LYS B 230   N  LEU B 208           
SHEET   11   E19 GLU B 254  GLY B 261  1  O  VAL B 259   N  LEU B 231           
SHEET   12   E19 THR B 284  LEU B 293  1  O  ALA B 291   N  LEU B 260           
SHEET   13   E19 SER B 312  VAL B 318  1  O  SER B 312   N  PHE B 288           
SHEET   14   E19 HIS B 334  VAL B 338  1  O  HIS B 334   N  PHE B 313           
SHEET   15   E19 ARG B 355  THR B 359  1  O  THR B 357   N  LEU B 337           
SHEET   16   E19 PHE B 377  ASP B 379  1  O  ASP B 379   N  PHE B 358           
SHEET   17   E19 TYR B 403  ASP B 405  1  O  ASP B 405   N  LEU B 378           
SHEET   18   E19 HIS B 426  ASP B 428  1  O  ASP B 428   N  LEU B 404           
SHEET   19   E19 TYR B 451  ASP B 453  1  O  ASP B 453   N  LEU B 427           
SHEET    1   F 2 THR B  92  ILE B  93  0                                        
SHEET    2   F 2 SER B 116  LEU B 117  1  O  SER B 116   N  ILE B  93           
SHEET    1   G 2 SER B 189  ILE B 190  0                                        
SHEET    2   G 2 PHE B 217  ILE B 218  1  O  PHE B 217   N  ILE B 190           
SHEET    1   H 3 PHE B 387  SER B 392  0                                        
SHEET    2   H 3 VAL B 411  LEU B 419  1  O  SER B 415   N  CYS B 390           
SHEET    3   H 3 ASN B 433  LYS B 435  1  O  LYS B 435   N  MET B 414           
SHEET    1   I 6 TYR C  22  ASN C  26  0                                        
SHEET    2   I 6 ALA C  30  TYR C  36 -1  O  ILE C  32   N  CYS C  25           
SHEET    3   I 6 GLU C 144  HIS C 155 -1  O  VAL C 152   N  SER C  33           
SHEET    4   I 6 GLY C 129  SER C 139 -1  N  TYR C 131   O  ILE C 153           
SHEET    5   I 6 TYR C  75  VAL C  82 -1  N  TYR C  79   O  VAL C 134           
SHEET    6   I 6 MET C  85  ASN C  86 -1  O  MET C  85   N  VAL C  82           
SHEET    1   J 6 TYR C  22  ASN C  26  0                                        
SHEET    2   J 6 ALA C  30  TYR C  36 -1  O  ILE C  32   N  CYS C  25           
SHEET    3   J 6 GLU C 144  HIS C 155 -1  O  VAL C 152   N  SER C  33           
SHEET    4   J 6 GLY C 129  SER C 139 -1  N  TYR C 131   O  ILE C 153           
SHEET    5   J 6 TYR C  75  VAL C  82 -1  N  TYR C  79   O  VAL C 134           
SHEET    6   J 6 ARG C  90  VAL C  93 -1  O  ARG C  90   N  LEU C  78           
SHEET    1   K 3 SER C  45  ASN C  49  0                                        
SHEET    2   K 3 LEU C  60  TYR C  65 -1  O  LEU C  60   N  ASN C  49           
SHEET    3   K 3 VAL C 113  SER C 118 -1  O  ILE C 117   N  LEU C  61           
SHEET    1   L 6 TYR D  22  ASN D  26  0                                        
SHEET    2   L 6 ALA D  30  TYR D  36 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   L 6 GLU D 144  HIS D 155 -1  O  VAL D 152   N  SER D  33           
SHEET    4   L 6 GLY D 129  SER D 139 -1  N  ALA D 137   O  PHE D 147           
SHEET    5   L 6 TYR D  75  VAL D  82 -1  N  TYR D  79   O  VAL D 134           
SHEET    6   L 6 MET D  85  ASN D  86 -1  O  MET D  85   N  VAL D  82           
SHEET    1   M 6 TYR D  22  ASN D  26  0                                        
SHEET    2   M 6 ALA D  30  TYR D  36 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   M 6 GLU D 144  HIS D 155 -1  O  VAL D 152   N  SER D  33           
SHEET    4   M 6 GLY D 129  SER D 139 -1  N  ALA D 137   O  PHE D 147           
SHEET    5   M 6 TYR D  75  VAL D  82 -1  N  TYR D  79   O  VAL D 134           
SHEET    6   M 6 ARG D  90  VAL D  93 -1  O  ARG D  90   N  LEU D  78           
SHEET    1   N 3 SER D  45  ASN D  49  0                                        
SHEET    2   N 3 LEU D  60  TYR D  65 -1  O  LEU D  60   N  ASN D  49           
SHEET    3   N 3 VAL D 113  SER D 118 -1  O  ILE D 117   N  LEU D  61           
SSBOND   1 CYS A   29    CYS A   40                          1555   1555  2.05  
SSBOND   2 CYS A  281    CYS A  306                          1555   1555  2.04  
SSBOND   3 CYS A  390    CYS A  391                          1555   1555  2.03  
SSBOND   4 CYS A  583    CYS A  609                          1555   1555  2.03  
SSBOND   5 CYS A  585    CYS A  627                          1555   1555  2.04  
SSBOND   6 CYS B   29    CYS B   40                          1555   1555  2.04  
SSBOND   7 CYS B  281    CYS B  306                          1555   1555  2.05  
SSBOND   8 CYS B  390    CYS B  391                          1555   1555  2.03  
SSBOND   9 CYS B  583    CYS B  609                          1555   1555  2.04  
SSBOND  10 CYS B  585    CYS B  627                          1555   1555  2.04  
SSBOND  11 CYS C   25    CYS C   51                          1555   1555  2.04  
SSBOND  12 CYS C   37    CYS C  148                          1555   1555  2.05  
SSBOND  13 CYS C   95    CYS C  105                          1555   1555  2.02  
SSBOND  14 CYS D   25    CYS D   51                          1555   1555  2.04  
SSBOND  15 CYS D   37    CYS D  148                          1555   1555  2.06  
SSBOND  16 CYS D   95    CYS D  105                          1555   1555  2.03  
LINK         ND2 ASN A 173                 C1  NAG A 711     1555   1555  1.46  
LINK         ND2 ASN A 205                 C1  NAG A 721     1555   1555  1.46  
LINK         ND2 ASN A 497                 C1  NAG A 741     1555   1555  1.46  
LINK         ND2 ASN A 526                 C1  NAG F   1     1555   1555  1.46  
LINK         ND2 ASN A 575                 C1  NAG G   1     1555   1555  1.46  
LINK         O3  FTT A1005                 C1  DAO A1007     1555   1555  1.42  
LINK         O3  FTT A1006                 C1  MYR A1008     1555   1555  1.39  
LINK         P   PO4 A1017                 O4  GMH E   5     1555   1555  1.49  
LINK         P   PO4 A1018                 O4  GMH E   4     1555   1555  1.49  
LINK         ND2 ASN B 173                 C1  NAG B 811     1555   1555  1.46  
LINK         ND2 ASN B 205                 C1  NAG B 821     1555   1555  1.46  
LINK         ND2 ASN B 497                 C1  NAG B 841     1555   1555  1.48  
LINK         ND2 ASN B 526                 C1  NAG I   1     1555   1555  1.45  
LINK         ND2 ASN B 575                 C1  NAG J   1     1555   1555  1.46  
LINK         O3  FTT B1005                 C1  DAO B1007     1555   1555  1.41  
LINK         O3  FTT B1006                 C1  MYR B1008     1555   1555  1.39  
LINK         P   PO4 B1017                 O4  GMH H   5     1555   1555  1.49  
LINK         P   PO4 B1018                 O4  GMH H   4     1555   1555  1.49  
LINK         ND2 ASN C 114                 C1  NAG C 751     1555   1555  1.46  
LINK         ND2 ASN D 114                 C1  NAG D 851     1555   1555  1.45  
LINK         O6  PA1 E   1                 C1  PA1 E   2     1555   1555  1.43  
LINK         O6  PA1 E   2                 C2  KDO E   3     1555   1555  1.42  
LINK         O5  KDO E   3                 C1  GMH E   4     1555   1555  1.42  
LINK         O4  KDO E   3                 C2  KDO E   7     1555   1555  1.48  
LINK         O3  GMH E   4                 C1  GMH E   5     1555   1555  1.43  
LINK         O7  GMH E   5                 C1  GMH E   6     1555   1555  1.42  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.41  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.40  
LINK         O6  PA1 H   1                 C1  GCS H   2     1555   1555  1.43  
LINK         O6  GCS H   2                 C2  KDO H   3     1555   1555  1.42  
LINK         O5  KDO H   3                 C1  GMH H   4     1555   1555  1.42  
LINK         O4  KDO H   3                 C2  KDO H   7     1555   1555  1.49  
LINK         O3  GMH H   4                 C1  GMH H   5     1555   1555  1.43  
LINK         O7  GMH H   5                 C1  GMH H   6     1555   1555  1.42  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.39  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.40  
LINK         O   HOH A   1                MG    MG A2001     1555   1555  2.90  
LINK         OD2 ASP A 294                MG    MG A2001     1555   1555  2.96  
CISPEP   1 CYS A  390    CYS A  391          0        -4.06                     
CISPEP   2 CYS B  390    CYS B  391          0        -4.06                     
CISPEP   3 ASN C   49    PRO C   50          0         0.10                     
CISPEP   4 ASN D   49    PRO D   50          0        -0.25                     
CRYST1   91.160  103.500  251.810  90.00  90.00  90.00 P 21 21 21    8          
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      0.010970  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009662  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003971        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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