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Database: PDB
Entry: 4G8A
LinkDB: 4G8A
Original site: 4G8A 
HEADER    IMMUNE SYSTEM                           23-JUL-12   4G8A              
TITLE     CRYSTAL STRUCTURE OF HUMAN TLR4 POLYMORPHIC VARIANT D299G AND T399I IN
TITLE    2 COMPLEX WITH MD-2 AND LPS                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLL-LIKE RECEPTOR 4;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 23-629;                                       
COMPND   5 SYNONYM: HTOLL, PROTEIN TLR4;                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 SYNONYM: LY-96, ESOP-1, PROTEIN MD-2;                                
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TLR4;                                                          
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: S2;                                     
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: LY96, ESOP1, MD2;                                              
SOURCE  16 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FRUIT FLIES;                               
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: S2;                                     
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    LEUCINE RICH REPEAT MD-2 RELATED LIPID RECOGNITION, RECEPTOR, INNATE  
KEYWDS   2 IMMUNITY, LIPID BINDING, GLYCOSYLATION, IMMUNE SYSTEM                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.OHTO,T.SHIMIZU                                                      
REVDAT   3   29-JUL-20 4G8A    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   04-SEP-13 4G8A    1       JRNL   HETATM FORMUL                     
REVDAT   1   17-OCT-12 4G8A    0                                                
JRNL        AUTH   U.OHTO,N.YAMAKAWA,S.AKASHI-TAKAMURA,K.MIYAKE,T.SHIMIZU       
JRNL        TITL   STRUCTURAL ANALYSES OF HUMAN TOLL-LIKE RECEPTOR 4            
JRNL        TITL 2 POLYMORPHISMS D299G AND T399I                                
JRNL        REF    J.BIOL.CHEM.                  V. 287 40611 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   23055527                                                     
JRNL        DOI    10.1074/JBC.M112.404608                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 70730                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3753                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4831                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 239                          
REMARK   3   BIN FREE R VALUE                    : 0.3020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11902                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 440                                     
REMARK   3   SOLVENT ATOMS            : 39                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 0.03000                                              
REMARK   3    B33 (A**2) : -0.10000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.15000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.375         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.255         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.183         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.685        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12685 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17134 ; 1.462 ; 2.004       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1482 ; 6.772 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   572 ;37.089 ;25.052       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2170 ;19.194 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;17.738 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1972 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9276 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   627                          
REMARK   3    RESIDUE RANGE :   A   701        A   705                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4211  -0.9770 -57.8301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0338 T22:   0.0231                                     
REMARK   3      T33:   0.0337 T12:   0.0131                                     
REMARK   3      T13:   0.0192 T23:  -0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1837 L22:   0.1383                                     
REMARK   3      L33:   0.3900 L12:  -0.0379                                     
REMARK   3      L13:   0.2573 L23:   0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0162 S12:  -0.0043 S13:   0.0059                       
REMARK   3      S21:  -0.0153 S22:  -0.0140 S23:  -0.0241                       
REMARK   3      S31:   0.0194 S32:  -0.0099 S33:  -0.0022                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    23        B   627                          
REMARK   3    RESIDUE RANGE :   B   701        B   704                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.5380   1.6622  -7.4762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0169 T22:   0.0696                                     
REMARK   3      T33:   0.0286 T12:   0.0239                                     
REMARK   3      T13:  -0.0011 T23:  -0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1827 L22:   0.3695                                     
REMARK   3      L33:   0.3111 L12:   0.0659                                     
REMARK   3      L13:  -0.0942 L23:  -0.2625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0289 S12:  -0.0701 S13:   0.0099                       
REMARK   3      S21:  -0.0140 S22:   0.0340 S23:  -0.0310                       
REMARK   3      S31:  -0.0049 S32:   0.0085 S33:  -0.0051                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    19        C   158                          
REMARK   3    RESIDUE RANGE :   C   201        C   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7959  18.6607 -57.2015              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0933 T22:   0.0294                                     
REMARK   3      T33:   0.0318 T12:  -0.0065                                     
REMARK   3      T13:   0.0034 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1173 L22:   0.4785                                     
REMARK   3      L33:   1.8944 L12:   0.0264                                     
REMARK   3      L13:  -0.1607 L23:   0.5851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0392 S12:   0.0486 S13:  -0.0486                       
REMARK   3      S21:  -0.0075 S22:   0.0078 S23:  -0.0215                       
REMARK   3      S31:  -0.3041 S32:   0.0234 S33:  -0.0469                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    19        D   158                          
REMARK   3    RESIDUE RANGE :   D   201        D   201                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1475 -16.8907  -7.9134              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0221 T22:   0.0494                                     
REMARK   3      T33:   0.0217 T12:   0.0115                                     
REMARK   3      T13:  -0.0164 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1448 L22:   0.0972                                     
REMARK   3      L33:   1.0072 L12:  -0.1438                                     
REMARK   3      L13:  -0.7987 L23:  -0.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0085 S12:  -0.1310 S13:  -0.0144                       
REMARK   3      S21:  -0.0124 S22:   0.0096 S23:   0.0260                       
REMARK   3      S31:  -0.0049 S32:   0.1178 S33:  -0.0011                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4G8A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073863.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70730                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.12900                            
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3FXI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30% (W/V) PEG1000, 0.1M TRIS-HCL      
REMARK 280  (PH 8.0), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       79.01900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.34000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       79.01900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       62.34000            
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: 21420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 61.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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     ARG A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     TRP A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     TYR A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     LYS A    14                                                      
REMARK 465     LEU A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     ILE A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     TRP A    26                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     MET A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     GLY A   631                                                      
REMARK 465     HIS A   632                                                      
REMARK 465     HIS A   633                                                      
REMARK 465     HIS A   634                                                      
REMARK 465     HIS A   635                                                      
REMARK 465     HIS A   636                                                      
REMARK 465     HIS A   637                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     TRP B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     TYR B     8                                                      
REMARK 465     LYS B     9                                                      
REMARK 465     ASP B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     ASP B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     LEU B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     SER B    21                                                      
REMARK 465     ILE B    22                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     MET B   629                                                      
REMARK 465     THR B   630                                                      
REMARK 465     GLY B   631                                                      
REMARK 465     HIS B   632                                                      
REMARK 465     HIS B   633                                                      
REMARK 465     HIS B   634                                                      
REMARK 465     HIS B   635                                                      
REMARK 465     HIS B   636                                                      
REMARK 465     HIS B   637                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     ALA C    18                                                      
REMARK 465     SER C   159                                                      
REMARK 465     ASN C   160                                                      
REMARK 465     GLU D    17                                                      
REMARK 465     ALA D    18                                                      
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   O44  LP4 D   202     O2   DAO D   204              2.00            
REMARK 500   O44  LP4 C   202     C2   DAO C   204              2.00            
REMARK 500   O6   LP4 C   202     O6   KDO C   206              2.00            
REMARK 500   OD1  ASP A    60     OG   SER A    62              2.03            
REMARK 500   O44  LP4 D   202     C2   DAO D   204              2.03            
REMARK 500   O43  LP4 D   202     C2   MYR D   205              2.08            
REMARK 500   O43  LP4 C   202     C2   MYR C   205              2.11            
REMARK 500   O6   LP4 C   202     C1   KDO C   206              2.14            
REMARK 500   OG1  THR A   537     O    GLU A   563              2.16            
REMARK 500   O    PRO C    67     O    LYS C   109              2.16            
REMARK 500   O6   LP4 D   202     C1   KDO D   206              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS B 529   CG    HIS B 529   CD2     0.057                       
REMARK 500    HIS C  62   CG    HIS C  62   CD2     0.055                       
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    PRO A 612   C   -  N   -  CA  ANGL. DEV. =  -9.5 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       -2.76     64.50                                   
REMARK 500    ILE A  36      -63.58   -122.25                                   
REMARK 500    ARG A  67      -33.28     66.29                                   
REMARK 500    ASN A 143       48.25    -98.28                                   
REMARK 500    ASN A 160     -153.96   -130.25                                   
REMARK 500    ASN A 185     -156.51   -107.81                                   
REMARK 500    MET A 201       65.71   -119.31                                   
REMARK 500    PHE A 272       90.76   -167.33                                   
REMARK 500    TYR A 292      124.85     65.78                                   
REMARK 500    ASP A 302      -21.67     81.66                                   
REMARK 500    ASN A 365       24.99   -157.23                                   
REMARK 500    GLN A 430      122.51    -29.55                                   
REMARK 500    PHE A 440     -177.08   -177.22                                   
REMARK 500    ALA A 462       16.95   -142.74                                   
REMARK 500    MET A 478       23.49   -142.65                                   
REMARK 500    ASN A 481     -158.63   -105.03                                   
REMARK 500    LEU A 495       56.02    -98.08                                   
REMARK 500    ASN A 530     -162.90   -107.73                                   
REMARK 500    LEU A 553       30.02     73.04                                   
REMARK 500    ASN A 554     -155.31   -103.07                                   
REMARK 500    GLN A 562       42.66    -66.24                                   
REMARK 500    LEU A 564      -15.06    -39.48                                   
REMARK 500    HIS A 566       38.25    -92.75                                   
REMARK 500    ASP A 580       54.94   -106.59                                   
REMARK 500    ILE A 625       50.81    -95.17                                   
REMARK 500    ASN B  35      -22.46     73.68                                   
REMARK 500    ARG B  67      -33.07     59.08                                   
REMARK 500    ALA B  97      -35.23    -36.49                                   
REMARK 500    THR B 110      135.26    -39.32                                   
REMARK 500    ASN B 160     -163.41   -128.93                                   
REMARK 500    LYS B 166      108.86    -58.70                                   
REMARK 500    LEU B 177      109.92    -59.74                                   
REMARK 500    ASN B 185     -155.23   -117.32                                   
REMARK 500    PRO B 202     -103.00    -69.59                                   
REMARK 500    LEU B 203       98.67    -52.41                                   
REMARK 500    GLU B 225       13.75     56.44                                   
REMARK 500    PHE B 272       94.20   -162.23                                   
REMARK 500    TYR B 292      128.83     63.24                                   
REMARK 500    ASP B 302       -9.31     74.04                                   
REMARK 500    ASN B 365       10.47   -163.41                                   
REMARK 500    ASN B 409     -166.71   -121.15                                   
REMARK 500    ASN B 417       56.10    -92.19                                   
REMARK 500    GLN B 430      126.16    -35.06                                   
REMARK 500    LEU B 470       53.53    -92.91                                   
REMARK 500    MET B 478       37.60   -145.06                                   
REMARK 500    ASN B 481     -160.58   -107.50                                   
REMARK 500    PRO B 513       -8.85    -57.39                                   
REMARK 500    ASN B 530     -168.45   -117.37                                   
REMARK 500    ASN B 554     -157.33   -102.17                                   
REMARK 500    ASP B 580       52.82    -98.53                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      61 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  610     THR A  611                 -148.31                    
REMARK 500 LYS C  122     GLY C  123                  149.20                    
REMARK 500 SER C  141     PRO C  142                 -136.84                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THE RESIDUES 202-206 (LP4 LP5 DAO MYR KDO) ARE LIPOPOLYSACCHARIDES   
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     LP4 C  202                                                       
REMARK 610     LP4 D  202                                                       
DBREF  4G8A A   23   629  UNP    O00206   TLR4_HUMAN      23    629             
DBREF  4G8A B   23   629  UNP    O00206   TLR4_HUMAN      23    629             
DBREF  4G8A C   17   160  UNP    Q9Y6Y9   LY96_HUMAN      17    160             
DBREF  4G8A D   17   160  UNP    Q9Y6Y9   LY96_HUMAN      17    160             
SEQADV 4G8A ARG A    3  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER A    4  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A PRO A    5  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A TRP A    6  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP A    7  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A TYR A    8  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LYS A    9  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP A   10  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP A   11  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP A   12  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP A   13  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LYS A   14  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LEU A   15  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA A   16  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA A   17  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA A   18  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASN A   19  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER A   20  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER A   21  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ILE A   22  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A GLY A  299  UNP  O00206    ASP   299 ENGINEERED MUTATION            
SEQADV 4G8A ILE A  399  UNP  O00206    THR   399 ENGINEERED MUTATION            
SEQADV 4G8A THR A  630  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A GLY A  631  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  632  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  633  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  634  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  635  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  636  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS A  637  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ARG B    3  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER B    4  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A PRO B    5  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A TRP B    6  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP B    7  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A TYR B    8  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LYS B    9  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP B   10  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP B   11  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP B   12  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASP B   13  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LYS B   14  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A LEU B   15  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA B   16  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA B   17  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ALA B   18  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ASN B   19  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER B   20  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A SER B   21  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A ILE B   22  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A GLY B  299  UNP  O00206    ASP   299 ENGINEERED MUTATION            
SEQADV 4G8A ILE B  399  UNP  O00206    THR   399 ENGINEERED MUTATION            
SEQADV 4G8A THR B  630  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A GLY B  631  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  632  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  633  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  634  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  635  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  636  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A HIS B  637  UNP  O00206              EXPRESSION TAG                 
SEQADV 4G8A GLY C   56  UNP  Q9Y6Y9    ARG    56 ENGINEERED MUTATION            
SEQADV 4G8A GLY D   56  UNP  Q9Y6Y9    ARG    56 ENGINEERED MUTATION            
SEQRES   1 A  635  ARG SER PRO TRP ASP TYR LYS ASP ASP ASP ASP LYS LEU          
SEQRES   2 A  635  ALA ALA ALA ASN SER SER ILE PRO GLU SER TRP GLU PRO          
SEQRES   3 A  635  CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN CYS MET          
SEQRES   4 A  635  GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU PRO PHE          
SEQRES   5 A  635  SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO LEU ARG          
SEQRES   6 A  635  HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO GLU LEU          
SEQRES   7 A  635  GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN THR ILE          
SEQRES   8 A  635  GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU SER THR          
SEQRES   9 A  635  LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU ALA LEU          
SEQRES  10 A  635  GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS LEU VAL          
SEQRES  11 A  635  ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN PHE PRO          
SEQRES  12 A  635  ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN VAL ALA          
SEQRES  13 A  635  HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU TYR PHE          
SEQRES  14 A  635  SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU SER SER          
SEQRES  15 A  635  ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU ARG VAL          
SEQRES  16 A  635  LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU ASP LEU          
SEQRES  17 A  635  SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY ALA PHE          
SEQRES  18 A  635  LYS GLU ILE ARG LEU HIS LYS LEU THR LEU ARG ASN ASN          
SEQRES  19 A  635  PHE ASP SER LEU ASN VAL MET LYS THR CYS ILE GLN GLY          
SEQRES  20 A  635  LEU ALA GLY LEU GLU VAL HIS ARG LEU VAL LEU GLY GLU          
SEQRES  21 A  635  PHE ARG ASN GLU GLY ASN LEU GLU LYS PHE ASP LYS SER          
SEQRES  22 A  635  ALA LEU GLU GLY LEU CYS ASN LEU THR ILE GLU GLU PHE          
SEQRES  23 A  635  ARG LEU ALA TYR LEU ASP TYR TYR LEU ASP GLY ILE ILE          
SEQRES  24 A  635  ASP LEU PHE ASN CYS LEU THR ASN VAL SER SER PHE SER          
SEQRES  25 A  635  LEU VAL SER VAL THR ILE GLU ARG VAL LYS ASP PHE SER          
SEQRES  26 A  635  TYR ASN PHE GLY TRP GLN HIS LEU GLU LEU VAL ASN CYS          
SEQRES  27 A  635  LYS PHE GLY GLN PHE PRO THR LEU LYS LEU LYS SER LEU          
SEQRES  28 A  635  LYS ARG LEU THR PHE THR SER ASN LYS GLY GLY ASN ALA          
SEQRES  29 A  635  PHE SER GLU VAL ASP LEU PRO SER LEU GLU PHE LEU ASP          
SEQRES  30 A  635  LEU SER ARG ASN GLY LEU SER PHE LYS GLY CYS CYS SER          
SEQRES  31 A  635  GLN SER ASP PHE GLY THR ILE SER LEU LYS TYR LEU ASP          
SEQRES  32 A  635  LEU SER PHE ASN GLY VAL ILE THR MET SER SER ASN PHE          
SEQRES  33 A  635  LEU GLY LEU GLU GLN LEU GLU HIS LEU ASP PHE GLN HIS          
SEQRES  34 A  635  SER ASN LEU LYS GLN MET SER GLU PHE SER VAL PHE LEU          
SEQRES  35 A  635  SER LEU ARG ASN LEU ILE TYR LEU ASP ILE SER HIS THR          
SEQRES  36 A  635  HIS THR ARG VAL ALA PHE ASN GLY ILE PHE ASN GLY LEU          
SEQRES  37 A  635  SER SER LEU GLU VAL LEU LYS MET ALA GLY ASN SER PHE          
SEQRES  38 A  635  GLN GLU ASN PHE LEU PRO ASP ILE PHE THR GLU LEU ARG          
SEQRES  39 A  635  ASN LEU THR PHE LEU ASP LEU SER GLN CYS GLN LEU GLU          
SEQRES  40 A  635  GLN LEU SER PRO THR ALA PHE ASN SER LEU SER SER LEU          
SEQRES  41 A  635  GLN VAL LEU ASN MET SER HIS ASN ASN PHE PHE SER LEU          
SEQRES  42 A  635  ASP THR PHE PRO TYR LYS CYS LEU ASN SER LEU GLN VAL          
SEQRES  43 A  635  LEU ASP TYR SER LEU ASN HIS ILE MET THR SER LYS LYS          
SEQRES  44 A  635  GLN GLU LEU GLN HIS PHE PRO SER SER LEU ALA PHE LEU          
SEQRES  45 A  635  ASN LEU THR GLN ASN ASP PHE ALA CYS THR CYS GLU HIS          
SEQRES  46 A  635  GLN SER PHE LEU GLN TRP ILE LYS ASP GLN ARG GLN LEU          
SEQRES  47 A  635  LEU VAL GLU VAL GLU ARG MET GLU CYS ALA THR PRO SER          
SEQRES  48 A  635  ASP LYS GLN GLY MET PRO VAL LEU SER LEU ASN ILE THR          
SEQRES  49 A  635  CYS GLN MET THR GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  635  ARG SER PRO TRP ASP TYR LYS ASP ASP ASP ASP LYS LEU          
SEQRES   2 B  635  ALA ALA ALA ASN SER SER ILE PRO GLU SER TRP GLU PRO          
SEQRES   3 B  635  CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN CYS MET          
SEQRES   4 B  635  GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU PRO PHE          
SEQRES   5 B  635  SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO LEU ARG          
SEQRES   6 B  635  HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO GLU LEU          
SEQRES   7 B  635  GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN THR ILE          
SEQRES   8 B  635  GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU SER THR          
SEQRES   9 B  635  LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU ALA LEU          
SEQRES  10 B  635  GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS LEU VAL          
SEQRES  11 B  635  ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN PHE PRO          
SEQRES  12 B  635  ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN VAL ALA          
SEQRES  13 B  635  HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU TYR PHE          
SEQRES  14 B  635  SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU SER SER          
SEQRES  15 B  635  ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU ARG VAL          
SEQRES  16 B  635  LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU ASP LEU          
SEQRES  17 B  635  SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY ALA PHE          
SEQRES  18 B  635  LYS GLU ILE ARG LEU HIS LYS LEU THR LEU ARG ASN ASN          
SEQRES  19 B  635  PHE ASP SER LEU ASN VAL MET LYS THR CYS ILE GLN GLY          
SEQRES  20 B  635  LEU ALA GLY LEU GLU VAL HIS ARG LEU VAL LEU GLY GLU          
SEQRES  21 B  635  PHE ARG ASN GLU GLY ASN LEU GLU LYS PHE ASP LYS SER          
SEQRES  22 B  635  ALA LEU GLU GLY LEU CYS ASN LEU THR ILE GLU GLU PHE          
SEQRES  23 B  635  ARG LEU ALA TYR LEU ASP TYR TYR LEU ASP GLY ILE ILE          
SEQRES  24 B  635  ASP LEU PHE ASN CYS LEU THR ASN VAL SER SER PHE SER          
SEQRES  25 B  635  LEU VAL SER VAL THR ILE GLU ARG VAL LYS ASP PHE SER          
SEQRES  26 B  635  TYR ASN PHE GLY TRP GLN HIS LEU GLU LEU VAL ASN CYS          
SEQRES  27 B  635  LYS PHE GLY GLN PHE PRO THR LEU LYS LEU LYS SER LEU          
SEQRES  28 B  635  LYS ARG LEU THR PHE THR SER ASN LYS GLY GLY ASN ALA          
SEQRES  29 B  635  PHE SER GLU VAL ASP LEU PRO SER LEU GLU PHE LEU ASP          
SEQRES  30 B  635  LEU SER ARG ASN GLY LEU SER PHE LYS GLY CYS CYS SER          
SEQRES  31 B  635  GLN SER ASP PHE GLY THR ILE SER LEU LYS TYR LEU ASP          
SEQRES  32 B  635  LEU SER PHE ASN GLY VAL ILE THR MET SER SER ASN PHE          
SEQRES  33 B  635  LEU GLY LEU GLU GLN LEU GLU HIS LEU ASP PHE GLN HIS          
SEQRES  34 B  635  SER ASN LEU LYS GLN MET SER GLU PHE SER VAL PHE LEU          
SEQRES  35 B  635  SER LEU ARG ASN LEU ILE TYR LEU ASP ILE SER HIS THR          
SEQRES  36 B  635  HIS THR ARG VAL ALA PHE ASN GLY ILE PHE ASN GLY LEU          
SEQRES  37 B  635  SER SER LEU GLU VAL LEU LYS MET ALA GLY ASN SER PHE          
SEQRES  38 B  635  GLN GLU ASN PHE LEU PRO ASP ILE PHE THR GLU LEU ARG          
SEQRES  39 B  635  ASN LEU THR PHE LEU ASP LEU SER GLN CYS GLN LEU GLU          
SEQRES  40 B  635  GLN LEU SER PRO THR ALA PHE ASN SER LEU SER SER LEU          
SEQRES  41 B  635  GLN VAL LEU ASN MET SER HIS ASN ASN PHE PHE SER LEU          
SEQRES  42 B  635  ASP THR PHE PRO TYR LYS CYS LEU ASN SER LEU GLN VAL          
SEQRES  43 B  635  LEU ASP TYR SER LEU ASN HIS ILE MET THR SER LYS LYS          
SEQRES  44 B  635  GLN GLU LEU GLN HIS PHE PRO SER SER LEU ALA PHE LEU          
SEQRES  45 B  635  ASN LEU THR GLN ASN ASP PHE ALA CYS THR CYS GLU HIS          
SEQRES  46 B  635  GLN SER PHE LEU GLN TRP ILE LYS ASP GLN ARG GLN LEU          
SEQRES  47 B  635  LEU VAL GLU VAL GLU ARG MET GLU CYS ALA THR PRO SER          
SEQRES  48 B  635  ASP LYS GLN GLY MET PRO VAL LEU SER LEU ASN ILE THR          
SEQRES  49 B  635  CYS GLN MET THR GLY HIS HIS HIS HIS HIS HIS                  
SEQRES   1 C  144  GLU ALA GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP          
SEQRES   2 C  144  ALA SER ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR          
SEQRES   3 C  144  PRO ILE SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS          
SEQRES   4 C  144  GLY SER LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG          
SEQRES   5 C  144  ARG ASP LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR          
SEQRES   6 C  144  VAL ASN THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE          
SEQRES   7 C  144  CYS ARG GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 C  144  LEU LYS GLY GLU THR VAL ASN THR THR ILE SER PHE SER          
SEQRES   9 C  144  PHE LYS GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS          
SEQRES  10 C  144  VAL VAL GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU          
SEQRES  11 C  144  PHE CYS LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN SER          
SEQRES  12 C  144  ASN                                                          
SEQRES   1 D  144  GLU ALA GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP          
SEQRES   2 D  144  ALA SER ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR          
SEQRES   3 D  144  PRO ILE SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS          
SEQRES   4 D  144  GLY SER LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG          
SEQRES   5 D  144  ARG ASP LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR          
SEQRES   6 D  144  VAL ASN THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE          
SEQRES   7 D  144  CYS ARG GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 D  144  LEU LYS GLY GLU THR VAL ASN THR THR ILE SER PHE SER          
SEQRES   9 D  144  PHE LYS GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS          
SEQRES  10 D  144  VAL VAL GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU          
SEQRES  11 D  144  PHE CYS LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN SER          
SEQRES  12 D  144  ASN                                                          
MODRES 4G8A ASN B  526  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN B  173  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN C  114  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN D  114  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN B  575  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN A  526  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN A  575  ASN  GLYCOSYLATION SITE                                 
MODRES 4G8A ASN A  173  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  A 701      14                                                       
HET    NAG  B 701      14                                                       
HET    NAG  C 201      14                                                       
HET    LP4  C 202      45                                                       
HET    LP5  C 203      48                                                       
HET    DAO  C 204      13                                                       
HET    MYR  C 205      15                                                       
HET    KDO  C 206      15                                                       
HET    NAG  D 201      14                                                       
HET    LP4  D 202      45                                                       
HET    LP5  D 203      48                                                       
HET    DAO  D 204      13                                                       
HET    MYR  D 205      15                                                       
HET    KDO  D 206      15                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     LP4 2-DEOXY-3-O-[(3R)-3-HYDROXYTETRADECANOYL]-2-{[(3R)-3-            
HETNAM   2 LP4  HYDROXYTETRADECANOYL]AMINO}-4-O-PHOSPHONO-BETA-D-               
HETNAM   3 LP4  GLUCOPYRANOSE                                                   
HETNAM     LP5 (R)-((2R,3S,4R,5R,6R)-3-HYDROXY-2-(HYDROXYMETHYL)-5-             
HETNAM   2 LP5  ((R)-3-HYDROXYTETRADECANAMIDO)-6-(PHOSPHONOOXY)                 
HETNAM   3 LP5  TETRAHYDRO-2H-PYRAN-4-YL) 3-HYDROXYTETRADECANOATE               
HETNAM     DAO LAURIC ACID                                                      
HETNAM     MYR MYRISTIC ACID                                                    
HETNAM     KDO 3-DEOXY-ALPHA-D-MANNO-OCT-2-ULOPYRANOSONIC ACID                  
FORMUL   5  NAG    12(C8 H15 N O6)                                              
FORMUL  12  LP4    2(C34 H66 N O12 P)                                           
FORMUL  13  LP5    2(C34 H66 N O12 P)                                           
FORMUL  14  DAO    2(C12 H24 O2)                                                
FORMUL  15  MYR    2(C14 H28 O2)                                                
FORMUL  16  KDO    2(C8 H14 O8)                                                 
FORMUL  23  HOH   *39(H2 O)                                                     
HELIX    1   1 LEU A  119  SER A  123  5                                   5    
HELIX    2   2 PRO A  168  LEU A  174  5                                   7    
HELIX    3   3 TYR A  191  ASP A  194  5                                   4    
HELIX    4   4 LEU A  195  GLN A  200  1                                   6    
HELIX    5   5 SER A  239  GLY A  249  1                                  11    
HELIX    6   6 LEU A  277  LEU A  283  5                                   7    
HELIX    7   7 PHE A  304  THR A  308  5                                   5    
HELIX    8   8 VAL A  323  TYR A  328  5                                   6    
HELIX    9   9 SER A  392  GLY A  397  1                                   6    
HELIX   10  10 THR A  537  LYS A  541  5                                   5    
HELIX   11  11 THR A  584  GLU A  586  5                                   3    
HELIX   12  12 HIS A  587  GLN A  597  1                                  11    
HELIX   13  13 GLU A  603  MET A  607  5                                   5    
HELIX   14  14 PRO A  619  LEU A  623  5                                   5    
HELIX   15  15 PRO B  168  ASN B  173  5                                   6    
HELIX   16  16 TYR B  191  MET B  201  5                                  11    
HELIX   17  17 SER B  239  GLY B  249  1                                  11    
HELIX   18  18 LEU B  277  LEU B  283  5                                   7    
HELIX   19  19 PHE B  304  THR B  308  5                                   5    
HELIX   20  20 VAL B  323  TYR B  328  5                                   6    
HELIX   21  21 SER B  392  GLY B  397  1                                   6    
HELIX   22  22 THR B  537  LYS B  541  5                                   5    
HELIX   23  23 LYS B  561  GLN B  565  5                                   5    
HELIX   24  24 THR B  584  GLU B  586  5                                   3    
HELIX   25  25 HIS B  587  GLN B  597  1                                  11    
HELIX   26  26 GLU B  603  MET B  607  5                                   5    
HELIX   27  27 TYR C  102  ALA C  107  5                                   6    
HELIX   28  28 TYR D  102  ALA D  107  5                                   6    
SHEET    1   A24 VAL A  30  VAL A  33  0                                        
SHEET    2   A24 THR A  37  GLN A  39 -1  O  GLN A  39   N  VAL A  30           
SHEET    3   A24 ASN A  58  ASP A  60  1  O  ASN A  58   N  TYR A  38           
SHEET    4   A24 VAL A  82  ASP A  84  1  O  VAL A  82   N  LEU A  59           
SHEET    5   A24 THR A 106  ILE A 108  1  O  ILE A 108   N  LEU A  83           
SHEET    6   A24 LYS A 130  VAL A 132  1  O  VAL A 132   N  LEU A 107           
SHEET    7   A24 GLU A 154  ASN A 156  1  O  GLU A 154   N  LEU A 131           
SHEET    8   A24 HIS A 179  ASP A 181  1  O  HIS A 179   N  LEU A 155           
SHEET    9   A24 SER A 207  ASP A 209  1  O  SER A 207   N  LEU A 180           
SHEET   10   A24 ARG A 227  ARG A 234  1  O  LYS A 230   N  LEU A 208           
SHEET   11   A24 GLU A 254  GLY A 261  1  O  GLU A 254   N  LEU A 228           
SHEET   12   A24 THR A 284  ALA A 291  1  O  GLU A 287   N  LEU A 258           
SHEET   13   A24 SER A 312  VAL A 316  1  O  VAL A 316   N  LEU A 290           
SHEET   14   A24 HIS A 334  VAL A 338  1  O  HIS A 334   N  PHE A 313           
SHEET   15   A24 ARG A 355  THR A 359  1  O  THR A 357   N  LEU A 337           
SHEET   16   A24 PHE A 377  ASP A 379  1  O  ASP A 379   N  PHE A 358           
SHEET   17   A24 TYR A 403  ASP A 405  1  O  ASP A 405   N  LEU A 378           
SHEET   18   A24 HIS A 426  ASP A 428  1  O  ASP A 428   N  LEU A 404           
SHEET   19   A24 TYR A 451  ASP A 453  1  O  ASP A 453   N  LEU A 427           
SHEET   20   A24 VAL A 475  LYS A 477  1  O  LYS A 477   N  LEU A 452           
SHEET   21   A24 PHE A 500  ASP A 502  1  O  PHE A 500   N  LEU A 476           
SHEET   22   A24 VAL A 524  ASN A 526  1  O  ASN A 526   N  LEU A 501           
SHEET   23   A24 VAL A 548  ASP A 550  1  O  VAL A 548   N  LEU A 525           
SHEET   24   A24 PHE A 573  ASN A 575  1  O  PHE A 573   N  LEU A 549           
SHEET    1   B 3 HIS A  68  LEU A  69  0                                        
SHEET    2   B 3 THR A  92  ILE A  93  1  O  THR A  92   N  LEU A  69           
SHEET    3   B 3 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 LEU A 297  GLY A 299  0                                        
SHEET    2   D 3 THR A 319  ARG A 322  1  O  ARG A 322   N  ASP A 298           
SHEET    3   D 3 LYS A 341  PHE A 342  1  O  LYS A 341   N  ILE A 320           
SHEET    1   E 3 PHE A 387  CYS A 390  0                                        
SHEET    2   E 3 VAL A 411  MET A 414  1  O  THR A 413   N  CYS A 390           
SHEET    3   E 3 ASN A 433  LYS A 435  1  O  ASN A 433   N  ILE A 412           
SHEET    1   F 2 ARG A 460  VAL A 461  0                                        
SHEET    2   F 2 SER A 482  PHE A 483  1  O  SER A 482   N  VAL A 461           
SHEET    1   G 2 PHE A 487  LEU A 488  0                                        
SHEET    2   G 2 GLN A 510  LEU A 511  1  O  GLN A 510   N  LEU A 488           
SHEET    1   H24 VAL B  30  VAL B  33  0                                        
SHEET    2   H24 THR B  37  GLN B  39 -1  O  GLN B  39   N  VAL B  30           
SHEET    3   H24 ASN B  58  ASP B  60  1  O  ASP B  60   N  TYR B  38           
SHEET    4   H24 VAL B  82  ASP B  84  1  O  ASP B  84   N  LEU B  59           
SHEET    5   H24 THR B 106  ILE B 108  1  O  ILE B 108   N  LEU B  83           
SHEET    6   H24 LYS B 130  VAL B 132  1  O  VAL B 132   N  LEU B 107           
SHEET    7   H24 GLU B 154  ASN B 156  1  O  GLU B 154   N  LEU B 131           
SHEET    8   H24 HIS B 179  ASP B 181  1  O  HIS B 179   N  LEU B 155           
SHEET    9   H24 SER B 207  ASP B 209  1  O  SER B 207   N  LEU B 180           
SHEET   10   H24 ARG B 227  ARG B 234  1  O  LYS B 230   N  LEU B 208           
SHEET   11   H24 GLU B 254  GLY B 261  1  O  GLU B 254   N  LEU B 228           
SHEET   12   H24 THR B 284  ALA B 291  1  O  THR B 284   N  VAL B 255           
SHEET   13   H24 SER B 312  VAL B 316  1  O  SER B 312   N  PHE B 288           
SHEET   14   H24 HIS B 334  VAL B 338  1  O  HIS B 334   N  PHE B 313           
SHEET   15   H24 ARG B 355  THR B 359  1  O  THR B 357   N  LEU B 337           
SHEET   16   H24 PHE B 377  ASP B 379  1  O  ASP B 379   N  PHE B 358           
SHEET   17   H24 TYR B 403  ASP B 405  1  O  ASP B 405   N  LEU B 378           
SHEET   18   H24 HIS B 426  ASP B 428  1  O  HIS B 426   N  LEU B 404           
SHEET   19   H24 TYR B 451  ASP B 453  1  O  TYR B 451   N  LEU B 427           
SHEET   20   H24 VAL B 475  LYS B 477  1  O  LYS B 477   N  LEU B 452           
SHEET   21   H24 PHE B 500  ASP B 502  1  O  PHE B 500   N  LEU B 476           
SHEET   22   H24 VAL B 524  ASN B 526  1  O  ASN B 526   N  LEU B 501           
SHEET   23   H24 VAL B 548  ASP B 550  1  O  VAL B 548   N  LEU B 525           
SHEET   24   H24 PHE B 573  ASN B 575  1  O  PHE B 573   N  LEU B 549           
SHEET    1   I 3 HIS B  68  LEU B  69  0                                        
SHEET    2   I 3 THR B  92  ILE B  93  1  O  THR B  92   N  LEU B  69           
SHEET    3   I 3 SER B 116  LEU B 117  1  O  SER B 116   N  ILE B  93           
SHEET    1   J 2 SER B 189  ILE B 190  0                                        
SHEET    2   J 2 PHE B 217  ILE B 218  1  O  PHE B 217   N  ILE B 190           
SHEET    1   K 4 LEU B 297  GLY B 299  0                                        
SHEET    2   K 4 THR B 319  ARG B 322  1  O  ARG B 322   N  ASP B 298           
SHEET    3   K 4 LYS B 341  PHE B 342  1  O  LYS B 341   N  ILE B 320           
SHEET    4   K 4 LYS B 362  GLY B 363  1  O  LYS B 362   N  PHE B 342           
SHEET    1   L 3 PHE B 387  CYS B 390  0                                        
SHEET    2   L 3 VAL B 411  MET B 414  1  O  THR B 413   N  CYS B 390           
SHEET    3   L 3 ASN B 433  LYS B 435  1  O  ASN B 433   N  ILE B 412           
SHEET    1   M 2 ARG B 460  VAL B 461  0                                        
SHEET    2   M 2 SER B 482  PHE B 483  1  O  SER B 482   N  VAL B 461           
SHEET    1   N 2 PHE B 487  LEU B 488  0                                        
SHEET    2   N 2 GLN B 510  LEU B 511  1  O  GLN B 510   N  LEU B 488           
SHEET    1   O 2 PHE B 581  ALA B 582  0                                        
SHEET    2   O 2 CYS B 609  THR B 611  1  O  ALA B 610   N  PHE B 581           
SHEET    1   P 6 TYR C  22  ASN C  26  0                                        
SHEET    2   P 6 ALA C  30  TYR C  36 -1  O  TYR C  34   N  TYR C  22           
SHEET    3   P 6 GLU C 144  HIS C 155 -1  O  VAL C 152   N  SER C  33           
SHEET    4   P 6 GLY C 129  SER C 139 -1  N  TYR C 131   O  ILE C 153           
SHEET    5   P 6 TYR C  75  VAL C  82 -1  N  THR C  81   O  LYS C 132           
SHEET    6   P 6 MET C  85  ASN C  86 -1  O  MET C  85   N  VAL C  82           
SHEET    1   Q 6 TYR C  22  ASN C  26  0                                        
SHEET    2   Q 6 ALA C  30  TYR C  36 -1  O  TYR C  34   N  TYR C  22           
SHEET    3   Q 6 GLU C 144  HIS C 155 -1  O  VAL C 152   N  SER C  33           
SHEET    4   Q 6 GLY C 129  SER C 139 -1  N  TYR C 131   O  ILE C 153           
SHEET    5   Q 6 TYR C  75  VAL C  82 -1  N  THR C  81   O  LYS C 132           
SHEET    6   Q 6 ARG C  90  VAL C  93 -1  O  ARG C  90   N  LEU C  78           
SHEET    1   R 3 SER C  45  ASN C  49  0                                        
SHEET    2   R 3 GLY C  56  TYR C  65 -1  O  HIS C  62   N  ASN C  47           
SHEET    3   R 3 VAL C 113  LYS C 122 -1  O  ILE C 117   N  LEU C  61           
SHEET    1   S 6 TYR D  22  ASN D  26  0                                        
SHEET    2   S 6 ALA D  30  TYR D  36 -1  O  TYR D  34   N  TYR D  22           
SHEET    3   S 6 GLU D 144  HIS D 155 -1  O  GLU D 150   N  THR D  35           
SHEET    4   S 6 GLY D 129  SER D 139 -1  N  VAL D 135   O  LEU D 149           
SHEET    5   S 6 TYR D  75  VAL D  82 -1  N  ASN D  77   O  GLU D 136           
SHEET    6   S 6 MET D  85  ASN D  86 -1  O  MET D  85   N  VAL D  82           
SHEET    1   T 6 TYR D  22  ASN D  26  0                                        
SHEET    2   T 6 ALA D  30  TYR D  36 -1  O  TYR D  34   N  TYR D  22           
SHEET    3   T 6 GLU D 144  HIS D 155 -1  O  GLU D 150   N  THR D  35           
SHEET    4   T 6 GLY D 129  SER D 139 -1  N  VAL D 135   O  LEU D 149           
SHEET    5   T 6 TYR D  75  VAL D  82 -1  N  ASN D  77   O  GLU D 136           
SHEET    6   T 6 ARG D  90  VAL D  93 -1  O  GLU D  92   N  PHE D  76           
SHEET    1   U 3 SER D  45  ASN D  49  0                                        
SHEET    2   U 3 GLY D  56  TYR D  65 -1  O  HIS D  62   N  ASN D  47           
SHEET    3   U 3 VAL D 113  LYS D 122 -1  O  ILE D 117   N  LEU D  61           
SSBOND   1 CYS A   29    CYS A   40                          1555   1555  2.08  
SSBOND   2 CYS A  281    CYS A  306                          1555   1555  2.05  
SSBOND   3 CYS A  390    CYS A  391                          1555   1555  1.99  
SSBOND   4 CYS A  583    CYS A  609                          1555   1555  2.03  
SSBOND   5 CYS A  585    CYS A  627                          1555   1555  2.03  
SSBOND   6 CYS B   29    CYS B   40                          1555   1555  2.06  
SSBOND   7 CYS B  281    CYS B  306                          1555   1555  2.05  
SSBOND   8 CYS B  390    CYS B  391                          1555   1555  1.99  
SSBOND   9 CYS B  583    CYS B  609                          1555   1555  2.03  
SSBOND  10 CYS B  585    CYS B  627                          1555   1555  2.05  
SSBOND  11 CYS C   25    CYS C   51                          1555   1555  2.04  
SSBOND  12 CYS C   37    CYS C  148                          1555   1555  2.06  
SSBOND  13 CYS C   95    CYS C  105                          1555   1555  2.02  
SSBOND  14 CYS D   25    CYS D   51                          1555   1555  2.05  
SSBOND  15 CYS D   37    CYS D  148                          1555   1555  2.06  
SSBOND  16 CYS D   95    CYS D  105                          1555   1555  2.02  
LINK         ND2 ASN A 173                 C1  NAG A 701     1555   1555  1.45  
LINK         ND2 ASN A 526                 C1  NAG E   1     1555   1555  1.44  
LINK         ND2 ASN A 575                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN B 173                 C1  NAG B 701     1555   1555  1.43  
LINK         ND2 ASN B 526                 C1  NAG G   1     1555   1555  1.43  
LINK         ND2 ASN B 575                 C1  NAG H   1     1555   1555  1.44  
LINK         ND2 ASN C 114                 C1  NAG C 201     1555   1555  1.43  
LINK         C1  LP4 C 202                 O6  LP5 C 203     1555   1555  1.44  
LINK         O44 LP4 C 202                 C1  DAO C 204     1555   1555  1.45  
LINK         O43 LP4 C 202                 C1  MYR C 205     1555   1555  1.44  
LINK         O6  LP4 C 202                 C2  KDO C 206     1555   1555  1.42  
LINK         ND2 ASN D 114                 C1  NAG D 201     1555   1555  1.44  
LINK         C1  LP4 D 202                 O6  LP5 D 203     1555   1555  1.44  
LINK         O44 LP4 D 202                 C1  DAO D 204     1555   1555  1.45  
LINK         O43 LP4 D 202                 C1  MYR D 205     1555   1555  1.45  
LINK         O6  LP4 D 202                 C2  KDO D 206     1555   1555  1.42  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.43  
CISPEP   1 CYS A  390    CYS A  391          0       -11.91                     
CISPEP   2 GLU B   27    PRO B   28          0         7.51                     
CISPEP   3 CYS B  390    CYS B  391          0       -18.50                     
CISPEP   4 THR B  611    PRO B  612          0       -11.44                     
CISPEP   5 ASN C   49    PRO C   50          0        -9.90                     
CISPEP   6 ASN D   49    PRO D   50          0        -8.47                     
CRYST1  158.038  124.680  109.140  90.00 115.72  90.00 C 1 2 1       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      0.006328  0.000000  0.003048        0.00000                         
SCALE2      0.000000  0.008021  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010170        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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