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Database: PDB
Entry: 3ULA
LinkDB: 3ULA
Original site: 3ULA 
HEADER    IMMUNE SYSTEM                           10-NOV-11   3ULA              
TITLE     CRYSTAL STRUCTURE OF THE TV3 MUTANT F63W-MD-2-ERITORAN COMPLEX        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLL-LIKE RECEPTOR 4, VARIABLE LYMPHOCYTE RECEPTOR B;      
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 27-228, UNP RESIDUES 126-199;                 
COMPND   5 SYNONYM: HTOLL;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: THE FUSION PROTEIN OF TLR4 (UNP RESIDUES 27-228) AND  
COMPND   9 VLRB (UNP RESIDUES 126-199);                                         
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND  12 CHAIN: B, D;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 19-158;                                       
COMPND  14 SYNONYM: LY-96, ESOP-1, PROTEIN MD-2;                                
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, EPTATRETUS BURGERI;               
SOURCE   3 ORGANISM_COMMON: HUMAN, INSHORE HAGFISH;                             
SOURCE   4 ORGANISM_TAXID: 9606, 7764;                                          
SOURCE   5 GENE: TLR4, VLRB;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: LY96, ESOP1, MD2;                                              
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    LRR, LPS BINDING, MD-2, EXTRACELLULAR MATRIX, IMMUNE SYSTEM           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.KIM,H.K.CHEONG,Y.H.JEON                                           
REVDAT   4   29-JUL-20 3ULA    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       HETSYN LINK   SITE   ATOM                
REVDAT   3   23-AUG-17 3ULA    1       SOURCE REMARK                            
REVDAT   2   09-OCT-13 3ULA    1       REMARK                                   
REVDAT   1   04-APR-12 3ULA    0                                                
JRNL        AUTH   J.HAN,H.J.KIM,S.C.LEE,S.HONG,K.PARK,Y.H.JEON,D.KIM,          
JRNL        AUTH 2 H.K.CHEONG,H.S.KIM                                           
JRNL        TITL   STRUCTURE-BASED RATIONAL DESIGN OF A TOLL-LIKE RECEPTOR 4    
JRNL        TITL 2 (TLR4) DECOY RECEPTOR WITH HIGH BINDING AFFINITY FOR A       
JRNL        TITL 3 TARGET PROTEIN.                                              
JRNL        REF    PLOS ONE                      V.   7 30929 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22363519                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0030929                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 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 : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 15790                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.306                           
REMARK   3   FREE R VALUE                     : 0.341                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 769                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.79                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6650                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 312                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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 3ULA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000068896.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2Z65                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE (PH4.5), 22% W/V     
REMARK 280  PEG 8000, 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE 296K   
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       40.10500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.75300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       63.46750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.75300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.10500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       63.46750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     THR A   303                                                      
REMARK 465     GLY B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     SER C    26                                                      
REMARK 465     THR C   303                                                      
REMARK 465     GLY D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 145   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO A 202   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    PRO B 142   C   -  N   -  CA  ANGL. DEV. = -13.2 DEGREES          
REMARK 500    PRO B 142   C   -  N   -  CD  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PRO C 145   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO C 202   C   -  N   -  CA  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    PRO D 142   C   -  N   -  CA  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    PRO D 142   C   -  N   -  CD  ANGL. DEV. =  14.0 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       16.27     56.50                                   
REMARK 500    ILE A  36      -56.34   -131.70                                   
REMARK 500    CYS A  40       44.37    -85.71                                   
REMARK 500    LEU A  43       30.41    -87.05                                   
REMARK 500    ASN A  44       27.96     43.86                                   
REMARK 500    PRO A  49     -170.99    -57.78                                   
REMARK 500    ASP A  50        2.39   -177.18                                   
REMARK 500    PRO A  53      162.20    -38.49                                   
REMARK 500    THR A  56      136.74    -37.26                                   
REMARK 500    PRO A  65       53.38    -50.17                                   
REMARK 500    ARG A  67      -44.17     39.50                                   
REMARK 500    SER A  71      136.48    -34.56                                   
REMARK 500    SER A  73      -12.41    -44.55                                   
REMARK 500    PHE A  75       -7.87    -47.31                                   
REMARK 500    PRO A  78       -2.98    -56.24                                   
REMARK 500    GLN A  81      -53.34   -122.22                                   
REMARK 500    LEU A  85       39.67   -140.01                                   
REMARK 500    ARG A  87       67.43     31.00                                   
REMARK 500    GLU A  89       16.63     41.10                                   
REMARK 500    ASP A  95      148.78    -34.95                                   
REMARK 500    GLN A  99      -43.51    -18.87                                   
REMARK 500    LEU A 101       58.31    -94.03                                   
REMARK 500    PRO A 113       49.06    -50.37                                   
REMARK 500    GLN A 115      -26.55   -144.84                                   
REMARK 500    LEU A 119       35.62    -73.36                                   
REMARK 500    ALA A 121      -68.83    -28.51                                   
REMARK 500    LEU A 125       48.21    -80.78                                   
REMARK 500    GLN A 129      -57.52   -135.32                                   
REMARK 500    ALA A 133       37.06   -155.88                                   
REMARK 500    PRO A 145       43.69    -52.89                                   
REMARK 500    ASN A 160     -155.91   -124.75                                   
REMARK 500    LEU A 167      123.95    -28.91                                   
REMARK 500    TYR A 170      -17.35    -48.35                                   
REMARK 500    ASN A 173       -6.55    -59.30                                   
REMARK 500    LEU A 174       43.55    -86.80                                   
REMARK 500    THR A 175       22.42    -58.54                                   
REMARK 500    ASN A 176       -5.53   -154.10                                   
REMARK 500    LEU A 182       34.02   -146.44                                   
REMARK 500    ASN A 185     -161.66   -115.88                                   
REMARK 500    CYS A 192      -80.57    -56.60                                   
REMARK 500    THR A 193      -44.66    -25.98                                   
REMARK 500    ASP A 194      -29.35    -35.67                                   
REMARK 500    ARG A 196      -71.90    -30.92                                   
REMARK 500    VAL A 197      -34.50    -34.11                                   
REMARK 500    ASN A 205       50.01    -97.44                                   
REMARK 500    PRO A 214       39.50    -83.89                                   
REMARK 500    ASN A 216       16.27   -146.20                                   
REMARK 500    ARG A 227       78.31   -109.01                                   
REMARK 500    ASN A 236     -141.64   -107.87                                   
REMARK 500    GLN A 237       45.08   -143.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     167 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A 1205                                                       
REMARK 610     NAG C  406                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3UL7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UL8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3UL9   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 FOR THE CHAIN B/D, THE PROTEIN OF MD2 (UNP RESIDUES 19-158), GLY56   
REMARK 999 IS NATURAL VARIANT. FOR THE CHAIN A/C, THE FUSION PROTEIN OF TLR4    
REMARK 999 (UNP RESIDUES 27-228) AND VLRB.61 (UNP RESIDUES 126-199).            
DBREF  3ULA A   27   228  UNP    O00206   TLR4_HUMAN      27    228             
DBREF  3ULA A  229   302  UNP    Q4G1L2   Q4G1L2_EPTBU   126    199             
DBREF  3ULA B   19   158  UNP    Q9Y6Y9   LY96_HUMAN      19    158             
DBREF  3ULA C   27   228  UNP    O00206   TLR4_HUMAN      27    228             
DBREF  3ULA C  229   302  UNP    Q4G1L2   Q4G1L2_EPTBU   126    199             
DBREF  3ULA D   19   158  UNP    Q9Y6Y9   LY96_HUMAN      19    158             
SEQADV 3ULA GLY A   25  UNP  O00206              EXPRESSION TAG                 
SEQADV 3ULA SER A   26  UNP  O00206              EXPRESSION TAG                 
SEQADV 3ULA TRP A   63  UNP  O00206    PHE    63 ENGINEERED MUTATION            
SEQADV 3ULA THR A  303  UNP  Q4G1L2              EXPRESSION TAG                 
SEQADV 3ULA GLY B   17  UNP  Q9Y6Y9              EXPRESSION TAG                 
SEQADV 3ULA SER B   18  UNP  Q9Y6Y9              EXPRESSION TAG                 
SEQADV 3ULA GLY B   56  UNP  Q9Y6Y9    ARG    56 SEE REMARK 999                 
SEQADV 3ULA GLY C   25  UNP  O00206              EXPRESSION TAG                 
SEQADV 3ULA SER C   26  UNP  O00206              EXPRESSION TAG                 
SEQADV 3ULA TRP C   63  UNP  O00206    PHE    63 ENGINEERED MUTATION            
SEQADV 3ULA THR C  303  UNP  Q4G1L2              EXPRESSION TAG                 
SEQADV 3ULA GLY D   17  UNP  Q9Y6Y9              EXPRESSION TAG                 
SEQADV 3ULA SER D   18  UNP  Q9Y6Y9              EXPRESSION TAG                 
SEQADV 3ULA GLY D   56  UNP  Q9Y6Y9    ARG    56 SEE REMARK 999                 
SEQRES   1 A  279  GLY SER GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR          
SEQRES   2 A  279  TYR GLN CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP          
SEQRES   3 A  279  ASN LEU PRO PHE SER THR LYS ASN LEU ASP LEU SER TRP          
SEQRES   4 A  279  ASN PRO LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER          
SEQRES   5 A  279  PHE PRO GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU          
SEQRES   6 A  279  ILE GLN THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER          
SEQRES   7 A  279  HIS LEU SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN          
SEQRES   8 A  279  SER LEU ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU          
SEQRES   9 A  279  GLN LYS LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU          
SEQRES  10 A  279  GLU ASN PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU          
SEQRES  11 A  279  LEU ASN VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU          
SEQRES  12 A  279  PRO GLU TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU          
SEQRES  13 A  279  ASP LEU SER SER ASN LYS ILE GLN SER ILE TYR CYS THR          
SEQRES  14 A  279  ASP LEU ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU          
SEQRES  15 A  279  SER LEU ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN          
SEQRES  16 A  279  PRO GLY ALA PHE LYS GLU ILE ARG LEU LYS GLU LEU ALA          
SEQRES  17 A  279  LEU ASP THR ASN GLN LEU LYS SER VAL PRO ASP GLY ILE          
SEQRES  18 A  279  PHE ASP ARG LEU THR SER LEU GLN LYS ILE TRP LEU HIS          
SEQRES  19 A  279  THR ASN PRO TRP ASP CYS SER CYS PRO ARG ILE ASP TYR          
SEQRES  20 A  279  LEU SER ARG TRP LEU ASN LYS ASN SER GLN LYS GLU GLN          
SEQRES  21 A  279  GLY SER ALA LYS CYS SER GLY SER GLY LYS PRO VAL ARG          
SEQRES  22 A  279  SER ILE ILE CYS PRO THR                                      
SEQRES   1 B  142  GLY SER GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP          
SEQRES   2 B  142  ALA SER ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR          
SEQRES   3 B  142  PRO ILE SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS          
SEQRES   4 B  142  GLY SER LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG          
SEQRES   5 B  142  ARG ASP LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR          
SEQRES   6 B  142  VAL ASN THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE          
SEQRES   7 B  142  CYS ARG GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 B  142  LEU LYS GLY GLU THR VAL ASN THR THR ILE SER PHE SER          
SEQRES   9 B  142  PHE LYS GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS          
SEQRES  10 B  142  VAL VAL GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU          
SEQRES  11 B  142  PHE CYS LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN              
SEQRES   1 C  279  GLY SER GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR          
SEQRES   2 C  279  TYR GLN CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP          
SEQRES   3 C  279  ASN LEU PRO PHE SER THR LYS ASN LEU ASP LEU SER TRP          
SEQRES   4 C  279  ASN PRO LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER          
SEQRES   5 C  279  PHE PRO GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU          
SEQRES   6 C  279  ILE GLN THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER          
SEQRES   7 C  279  HIS LEU SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN          
SEQRES   8 C  279  SER LEU ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU          
SEQRES   9 C  279  GLN LYS LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU          
SEQRES  10 C  279  GLU ASN PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU          
SEQRES  11 C  279  LEU ASN VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU          
SEQRES  12 C  279  PRO GLU TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU          
SEQRES  13 C  279  ASP LEU SER SER ASN LYS ILE GLN SER ILE TYR CYS THR          
SEQRES  14 C  279  ASP LEU ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU          
SEQRES  15 C  279  SER LEU ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN          
SEQRES  16 C  279  PRO GLY ALA PHE LYS GLU ILE ARG LEU LYS GLU LEU ALA          
SEQRES  17 C  279  LEU ASP THR ASN GLN LEU LYS SER VAL PRO ASP GLY ILE          
SEQRES  18 C  279  PHE ASP ARG LEU THR SER LEU GLN LYS ILE TRP LEU HIS          
SEQRES  19 C  279  THR ASN PRO TRP ASP CYS SER CYS PRO ARG ILE ASP TYR          
SEQRES  20 C  279  LEU SER ARG TRP LEU ASN LYS ASN SER GLN LYS GLU GLN          
SEQRES  21 C  279  GLY SER ALA LYS CYS SER GLY SER GLY LYS PRO VAL ARG          
SEQRES  22 C  279  SER ILE ILE CYS PRO THR                                      
SEQRES   1 D  142  GLY SER GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP          
SEQRES   2 D  142  ALA SER ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR          
SEQRES   3 D  142  PRO ILE SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS          
SEQRES   4 D  142  GLY SER LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG          
SEQRES   5 D  142  ARG ASP LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR          
SEQRES   6 D  142  VAL ASN THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE          
SEQRES   7 D  142  CYS ARG GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 D  142  LEU LYS GLY GLU THR VAL ASN THR THR ILE SER PHE SER          
SEQRES   9 D  142  PHE LYS GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS          
SEQRES  10 D  142  VAL VAL GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU          
SEQRES  11 D  142  PHE CYS LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN              
MODRES 3ULA ASN A  205  ASN  GLYCOSYLATION SITE                                 
MODRES 3ULA ASN C  205  ASN  GLYCOSYLATION SITE                                 
MODRES 3ULA ASN A   35  ASN  GLYCOSYLATION SITE                                 
MODRES 3ULA ASN C   35  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    NAG  A1201      14                                                       
HET    NAG  A1205      14                                                       
HET    E55  A1206      89                                                       
HET    E55  C 401      89                                                       
HET    NAG  C 402      14                                                       
HET    NAG  C 406      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     E55 3-O-DECYL-2-DEOXY-6-O-{2-DEOXY-3-O-[(3R)-3-                      
HETNAM   2 E55  METHOXYDECYL]-6-O-METHYL-2-[(11Z)-OCTADEC-11-                   
HETNAM   3 E55  ENOYLAMINO]-4-O-PHOSPHONO-BETA-D-GLUCOPYRANOSYL}-2-             
HETNAM   4 E55  [(3-OXOTETRADECANOYL)AMINO]-1-O-PHOSPHONO-ALPHA-D-              
HETNAM   5 E55  GLUCOPYRANOSE                                                   
HETSYN     E55 E5564; ERITORAN                                                  
FORMUL   5  NAG    8(C8 H15 N O6)                                               
FORMUL   5  BMA    2(C6 H12 O6)                                                 
FORMUL   9  E55    2(C66 H126 N2 O19 P2)                                        
HELIX    1   1 SER A  140  PHE A  144  5                                   5    
HELIX    2   2 PRO A  168  LEU A  174  5                                   7    
HELIX    3   3 CYS A  192  MET A  201  5                                  10    
HELIX    4   4 ILE A  269  ASN A  279  1                                  11    
HELIX    5   5 PRO A  295  ILE A  299  5                                   5    
HELIX    6   6 TYR B  102  ALA B  107  5                                   6    
HELIX    7   7 SER C  140  PHE C  144  5                                   5    
HELIX    8   8 PRO C  168  LEU C  174  5                                   7    
HELIX    9   9 CYS C  192  MET C  201  5                                  10    
HELIX   10  10 ILE C  269  ASN C  279  1                                  11    
HELIX   11  11 PRO C  295  ILE C  299  5                                   5    
HELIX   12  12 TYR D  102  ALA D  107  5                                   6    
SHEET    1   A 5 GLU A  31  VAL A  33  0                                        
SHEET    2   A 5 THR A  37  GLN A  39 -1  O  THR A  37   N  VAL A  32           
SHEET    3   A 5 ASN A  58  ASP A  60  1  O  ASP A  60   N  TYR A  38           
SHEET    4   A 5 VAL A  82  ASP A  84  1  O  VAL A  82   N  LEU A  59           
SHEET    5   A 5 THR A 106  ILE A 108  1  O  ILE A 108   N  LEU A  83           
SHEET    1   B 2 HIS A  68  LEU A  69  0                                        
SHEET    2   B 2 THR A  92  ILE A  93  1  O  THR A  92   N  LEU A  69           
SHEET    1   C 7 LYS A 130  VAL A 132  0                                        
SHEET    2   C 7 GLU A 154  ASN A 156  1  O  GLU A 154   N  LEU A 131           
SHEET    3   C 7 HIS A 179  ASP A 181  1  O  HIS A 179   N  LEU A 155           
SHEET    4   C 7 SER A 207  ASP A 209  1  O  SER A 207   N  LEU A 180           
SHEET    5   C 7 GLU A 230  ALA A 232  1  O  GLU A 230   N  LEU A 208           
SHEET    6   C 7 LYS A 254  TRP A 256  1  O  LYS A 254   N  LEU A 231           
SHEET    7   C 7 GLU A 283  GLN A 284  1  O  GLN A 284   N  ILE A 255           
SHEET    1   D 2 SER A 189  ILE A 190  0                                        
SHEET    2   D 2 PHE A 217  ILE A 218  1  O  PHE A 217   N  ILE A 190           
SHEET    1   E 6 TYR B  22  SER B  27  0                                        
SHEET    2   E 6 ALA B  30  THR B  35 -1  O  ILE B  32   N  CYS B  25           
SHEET    3   E 6 GLU B 150  LEU B 154 -1  O  VAL B 152   N  SER B  33           
SHEET    4   E 6 TYR B 131  SER B 139 -1  N  CYS B 133   O  PHE B 151           
SHEET    5   E 6 TYR B  75  THR B  81 -1  N  TYR B  75   O  ILE B 138           
SHEET    6   E 6 ARG B  90  VAL B  93 -1  O  ARG B  90   N  LEU B  78           
SHEET    1   F 5 TYR B  22  SER B  27  0                                        
SHEET    2   F 5 ALA B  30  THR B  35 -1  O  ILE B  32   N  CYS B  25           
SHEET    3   F 5 GLU B 150  LEU B 154 -1  O  VAL B 152   N  SER B  33           
SHEET    4   F 5 TYR B 131  SER B 139 -1  N  CYS B 133   O  PHE B 151           
SHEET    5   F 5 GLU B 144  PHE B 147 -1  O  LEU B 146   N  ALA B 137           
SHEET    1   G 3 SER B  45  ASN B  49  0                                        
SHEET    2   G 3 SER B  57  TYR B  65 -1  O  LEU B  60   N  ASN B  49           
SHEET    3   G 3 VAL B 113  PHE B 121 -1  O  PHE B 119   N  GLY B  59           
SHEET    1   H 5 GLU C  31  VAL C  33  0                                        
SHEET    2   H 5 THR C  37  GLN C  39 -1  O  THR C  37   N  VAL C  32           
SHEET    3   H 5 ASN C  58  ASP C  60  1  O  ASP C  60   N  TYR C  38           
SHEET    4   H 5 VAL C  82  ASP C  84  1  O  VAL C  82   N  LEU C  59           
SHEET    5   H 5 THR C 106  ILE C 108  1  O  ILE C 108   N  LEU C  83           
SHEET    1   I 2 HIS C  68  LEU C  69  0                                        
SHEET    2   I 2 THR C  92  ILE C  93  1  O  THR C  92   N  LEU C  69           
SHEET    1   J 7 LYS C 130  VAL C 132  0                                        
SHEET    2   J 7 GLU C 154  ASN C 156  1  O  GLU C 154   N  LEU C 131           
SHEET    3   J 7 HIS C 179  ASP C 181  1  O  HIS C 179   N  LEU C 155           
SHEET    4   J 7 SER C 207  ASP C 209  1  O  SER C 207   N  LEU C 180           
SHEET    5   J 7 GLU C 230  ALA C 232  1  O  GLU C 230   N  LEU C 208           
SHEET    6   J 7 LYS C 254  TRP C 256  1  O  LYS C 254   N  LEU C 231           
SHEET    7   J 7 GLU C 283  GLN C 284  1  O  GLN C 284   N  ILE C 255           
SHEET    1   K 2 SER C 189  ILE C 190  0                                        
SHEET    2   K 2 PHE C 217  ILE C 218  1  O  PHE C 217   N  ILE C 190           
SHEET    1   L 6 TYR D  22  SER D  27  0                                        
SHEET    2   L 6 ALA D  30  THR D  35 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   L 6 GLU D 150  LEU D 154 -1  O  VAL D 152   N  SER D  33           
SHEET    4   L 6 TYR D 131  SER D 139 -1  N  CYS D 133   O  PHE D 151           
SHEET    5   L 6 TYR D  75  THR D  81 -1  N  TYR D  75   O  ILE D 138           
SHEET    6   L 6 ARG D  90  VAL D  93 -1  O  ARG D  90   N  LEU D  78           
SHEET    1   M 5 TYR D  22  SER D  27  0                                        
SHEET    2   M 5 ALA D  30  THR D  35 -1  O  ILE D  32   N  CYS D  25           
SHEET    3   M 5 GLU D 150  LEU D 154 -1  O  VAL D 152   N  SER D  33           
SHEET    4   M 5 TYR D 131  SER D 139 -1  N  CYS D 133   O  PHE D 151           
SHEET    5   M 5 GLU D 144  PHE D 147 -1  O  LEU D 146   N  ALA D 137           
SHEET    1   N 3 SER D  45  ASN D  49  0                                        
SHEET    2   N 3 SER D  57  TYR D  65 -1  O  LEU D  60   N  ASN D  49           
SHEET    3   N 3 VAL D 113  PHE D 121 -1  O  PHE D 119   N  GLY D  59           
SSBOND   1 CYS A   29    CYS A   40                          1555   1555  2.05  
SSBOND   2 CYS A  264    CYS A  289                          1555   1555  2.03  
SSBOND   3 CYS A  266    CYS A  301                          1555   1555  2.04  
SSBOND   4 CYS B   25    CYS B   51                          1555   1555  2.06  
SSBOND   5 CYS B   37    CYS B  148                          1555   1555  2.06  
SSBOND   6 CYS B   95    CYS B  105                          1555   1555  2.03  
SSBOND   7 CYS C   29    CYS C   40                          1555   1555  2.06  
SSBOND   8 CYS C  264    CYS C  289                          1555   1555  2.04  
SSBOND   9 CYS C  266    CYS C  301                          1555   1555  2.05  
SSBOND  10 CYS D   25    CYS D   51                          1555   1555  2.06  
SSBOND  11 CYS D   37    CYS D  148                          1555   1555  2.05  
SSBOND  12 CYS D   95    CYS D  105                          1555   1555  2.02  
LINK         ND2 ASN A  35                 C1  NAG A1201     1555   1555  1.46  
LINK         ND2 ASN A 205                 C1  NAG E   1     1555   1555  1.45  
LINK         ND2 ASN C  35                 C1  NAG C 402     1555   1555  1.47  
LINK         ND2 ASN C 205                 C1  NAG F   1     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.40  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.40  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.40  
LINK         O4  NAG F   2                 C1  BMA F   3     1555   1555  1.40  
CISPEP   1 CYS A  266    PRO A  267          0         0.19                     
CISPEP   2 ASN B   49    PRO B   50          0        -0.15                     
CISPEP   3 CYS C  266    PRO C  267          0         0.18                     
CISPEP   4 ASN D   49    PRO D   50          0        -0.09                     
CRYST1   80.210  126.935  129.506  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      0.012467  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007878  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007722        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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