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Database: PDB
Entry: 2Z65
LinkDB: 2Z65
Original site: 2Z65 
HEADER    IMMUNE SYSTEM                           22-JUL-07   2Z65              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN TLR4 TV3 HYBRID-MD-2-ERITORAN COMPLEX  
CAVEAT     2Z65    NAG A 1201 HAS WRONG CHIRALITY AT ATOM C1 NAG B 1301 HAS     
CAVEAT   2 2Z65    WRONG CHIRALITY AT ATOM C1 NAG B 1201 HAS WRONG CHIRALITY    
CAVEAT   3 2Z65    AT ATOM C1                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TOLL-LIKE RECEPTOR 4, VARIABLE LYMPHOCYTE RECEPTOR B;      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: TV3, UNP RESIDUES 27-228(HUMAN), E5564, UNP RESIDUES 19-   
COMPND   5 158(INSHORE HAGFISH);                                                
COMPND   6 SYNONYM: HTOLL, CD284 ANTIGEN(HUMAN);                                
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 SYNONYM: MD-2 PROTEIN, ESOP-1;                                       
COMPND  12 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.61;                                                 
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: HI-5;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PVL1393;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: MD-2;                                                          
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: HI-5;                                      
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PVL1393                                   
KEYWDS    TLR4, TOLL-LIKE RECEPTOR, MD-2, LPS, E5564, ERITORAN, GLYCOPROTEIN,   
KEYWDS   2 IMMUNE RESPONSE, INFLAMMATORY RESPONSE, INNATE IMMUNITY, LEUCINE-    
KEYWDS   3 RICH REPEAT, MEMBRANE, TRANSMEMBRANE, SECRETED, IMMUNE SYSTEM        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-O.LEE,H.M.KIM,B.S.PARK                                             
REVDAT   6   29-JUL-20 2Z65    1       CAVEAT COMPND REMARK HET                 
REVDAT   6 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   6 3                   1       SITE   ATOM                              
REVDAT   5   09-AUG-17 2Z65    1       SOURCE REMARK                            
REVDAT   4   13-JUL-11 2Z65    1       VERSN                                    
REVDAT   3   21-JUL-10 2Z65    1       REMARK                                   
REVDAT   2   24-FEB-09 2Z65    1       VERSN                                    
REVDAT   1   18-SEP-07 2Z65    0                                                
JRNL        AUTH   H.M.KIM,B.S.PARK,J.-I.KIM,S.E.KIM,J.LEE,S.C.OH,P.ENKHBAYAR,  
JRNL        AUTH 2 N.MATSUSHIMA,H.LEE,O.J.YOO,J.-O.LEE                          
JRNL        TITL   CRYSTAL STRUCTURE OF THE TLR4-MD-2 COMPLEX WITH BOUND        
JRNL        TITL 2 ENDOTOXIN ANTAGONIST ERITORAN                                
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 130   906 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   17803912                                                     
JRNL        DOI    10.1016/J.CELL.2007.08.002                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27898                          
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) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1462                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1582                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.04                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6646                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 287                                     
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.91000                                              
REMARK   3    B22 (A**2) : -2.26000                                             
REMARK   3    B33 (A**2) : -0.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.93000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.414         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.350         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.680        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.864                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7101 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9614 ; 1.393 ; 2.023       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   828 ; 6.584 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   298 ;40.442 ;24.899       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1222 ;18.508 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;17.737 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1100 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5132 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3101 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4715 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   242 ; 0.172 ; 0.200       
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):   110 ; 0.260 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.160 ; 0.200       
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):  4282 ; 2.658 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6788 ; 4.228 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3129 ; 6.769 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2826 ; 9.905 ; 4.500       
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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     27       A     302      1                      
REMARK   3           1     B     27       B     302      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2189 ;  0.05 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2189 ;  0.83 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C     19       C     123      1                      
REMARK   3           1     D     19       D     123      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    C    (A):    855 ;  0.03 ;  0.05           
REMARK   3   TIGHT THERMAL      2    C (A**2):    855 ;  0.75 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    128       C     158      1                      
REMARK   3           1     D    128       D     158      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    C    (A):    245 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      3    C (A**2):    245 ;  0.75 ;  0.50           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C      1       C       1      1                      
REMARK   3           1     D      1       D       1      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   4    A    (A):     89 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      4    A (A**2):     89 ;  1.36 ;  0.50           
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 : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    27        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6332   5.1410  32.1018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0993 T22:  -0.1295                                     
REMARK   3      T33:  -0.1048 T12:   0.0551                                     
REMARK   3      T13:   0.0214 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6490 L22:   1.2047                                     
REMARK   3      L33:   6.0521 L12:  -0.0828                                     
REMARK   3      L13:  -0.2961 L23:  -1.3079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0597 S12:  -0.1020 S13:  -0.1646                       
REMARK   3      S21:   0.1847 S22:   0.0687 S23:   0.0139                       
REMARK   3      S31:   0.3559 S32:  -0.2484 S33:  -0.1284                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    19        C   158                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6273  23.9018  39.4335              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0834 T22:   0.0066                                     
REMARK   3      T33:  -0.1015 T12:   0.0835                                     
REMARK   3      T13:  -0.0858 T23:  -0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5234 L22:   6.6885                                     
REMARK   3      L33:   3.4797 L12:   0.9792                                     
REMARK   3      L13:   0.6025 L23:   0.1096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1359 S12:  -0.0660 S13:  -0.1106                       
REMARK   3      S21:   0.3325 S22:  -0.0328 S23:  -0.8884                       
REMARK   3      S31:  -0.0641 S32:   0.4320 S33:  -0.1031                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    27        B   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0299 -32.1918  18.2252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1887 T22:  -0.1685                                     
REMARK   3      T33:  -0.1064 T12:   0.0374                                     
REMARK   3      T13:   0.1019 T23:   0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0762 L22:   1.6285                                     
REMARK   3      L33:   2.4088 L12:  -1.3256                                     
REMARK   3      L13:   2.5333 L23:  -0.7381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1300 S12:  -0.2385 S13:   0.2997                       
REMARK   3      S21:   0.2273 S22:   0.0292 S23:   0.2098                       
REMARK   3      S31:  -0.2603 S32:  -0.1278 S33:   0.1008                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    19        D   158                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0682 -50.6230  -6.4620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2172 T22:  -0.1726                                     
REMARK   3      T33:  -0.0496 T12:  -0.0282                                     
REMARK   3      T13:   0.0236 T23:   0.0367                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9685 L22:   6.7394                                     
REMARK   3      L33:   6.4958 L12:   0.1268                                     
REMARK   3      L13:  -0.6007 L23:   1.2500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1025 S12:   0.1087 S13:  -0.1935                       
REMARK   3      S21:  -0.7951 S22:   0.1712 S23:  -0.2592                       
REMARK   3      S31:  -0.0325 S32:   0.2250 S33:  -0.0687                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z65 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000027569.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-APR-07                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27898                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08900                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2Z62, 2Z64                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M SODIUM       
REMARK 280  ACETATE, 20% PEG 4000, 5% ETHANOL, PH 4.5, VAPOR DIFFUSION,         
REMARK 280  TEMPERATURE 296K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       40.49350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: AUTHOR DETERMINED BIOLOGICAL UNIT: UNKNOWN                   
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    LEU A 155   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU B 155   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    CYS A  29     -179.00    -66.97                                   
REMARK 500    ASN A  35        4.67     59.65                                   
REMARK 500    CYS A  40       44.04   -108.18                                   
REMARK 500    LEU A  43       30.22    -94.58                                   
REMARK 500    ASP A  50      -14.05   -156.99                                   
REMARK 500    ASN A  51       40.77    -79.44                                   
REMARK 500    THR A  56      131.42    -36.72                                   
REMARK 500    PHE A  63       39.95     76.21                                   
REMARK 500    PRO A  65       41.77    -53.28                                   
REMARK 500    ARG A  67      -52.35     67.28                                   
REMARK 500    PHE A  77       55.96   -146.79                                   
REMARK 500    LEU A 101       64.25   -112.11                                   
REMARK 500    PRO A 113       46.91    -67.95                                   
REMARK 500    GLN A 115      -72.61   -109.46                                   
REMARK 500    LEU A 125       58.41    -95.29                                   
REMARK 500    ALA A 133       45.04   -106.74                                   
REMARK 500    ASN A 143       35.98    -95.05                                   
REMARK 500    ASN A 160     -152.75   -105.03                                   
REMARK 500    LEU A 174       52.95    -68.76                                   
REMARK 500    ASN A 185     -158.16    -91.07                                   
REMARK 500    MET A 201       76.69   -119.21                                   
REMARK 500    ASN A 236     -146.60    -90.39                                   
REMARK 500    ARG A 248       72.93   -103.86                                   
REMARK 500    PRO A 261       62.44    -69.04                                   
REMARK 500    CYS A 264       39.08    -98.72                                   
REMARK 500    CYS B  29     -176.25    -65.31                                   
REMARK 500    ASN B  35        9.11     57.98                                   
REMARK 500    ILE B  36      -45.01   -130.22                                   
REMARK 500    CYS B  40       42.32   -108.09                                   
REMARK 500    LEU B  43       32.00    -93.52                                   
REMARK 500    ASP B  50      -12.60   -154.40                                   
REMARK 500    ASN B  51       43.91    -81.36                                   
REMARK 500    THR B  56      129.71    -30.55                                   
REMARK 500    PHE B  63       40.33     78.61                                   
REMARK 500    PRO B  65       43.14    -53.38                                   
REMARK 500    ARG B  67      -51.14     66.67                                   
REMARK 500    PHE B  77       54.41   -148.83                                   
REMARK 500    LEU B 101       67.56   -114.85                                   
REMARK 500    PRO B 113       48.87    -68.30                                   
REMARK 500    LEU B 119       15.19    -67.68                                   
REMARK 500    LEU B 125       56.29    -92.68                                   
REMARK 500    ALA B 133       49.44   -105.15                                   
REMARK 500    ASN B 143       37.84    -95.74                                   
REMARK 500    ASN B 160     -154.99   -102.71                                   
REMARK 500    THR B 175        4.95    -68.46                                   
REMARK 500    ASN B 185     -158.55    -95.63                                   
REMARK 500    THR B 193      -38.58    -36.80                                   
REMARK 500    ASN B 236     -142.90    -91.96                                   
REMARK 500    ARG B 248       73.89   -106.23                                   
REMARK 500    CYS B 264       34.76    -95.96                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 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 SER C  141     PRO C  142                  149.86                    
REMARK 500 SER D  141     PRO D  142                  149.66                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 POLYSACCHARIDES WERE ORIGINALLY ASSIGNED TO CHAINS M1401, M(1301-    
REMARK 600 1304), M1201, N1401, N1301, AND N1201, RESPECTIVELY.                 
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 1401                                                       
REMARK 610     NAG B 1401                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Z62   RELATED DB: PDB                                   
REMARK 900 THE TV3 HYBRID OF HUMAN TLR4 AND HAGFISH VLRB.61                     
REMARK 900 RELATED ID: 2Z63   RELATED DB: PDB                                   
REMARK 900 THE TV8 HYBRID OF HUMAN TLR4 AND HAGFISH VLRB.61                     
REMARK 900 RELATED ID: 2Z64   RELATED DB: PDB                                   
REMARK 900 THE MOUSE TLR4 AND MOUSE MD-2 COMPLEX                                
REMARK 900 RELATED ID: 2Z66   RELATED DB: PDB                                   
REMARK 900 THE VT3 HYBRID OF HUMAN TLR4 AND HAGFISH VLRB.61                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT INCLUDES A LINKER THAT CONSIST OF 229TH LYS AND       
REMARK 999 230TH GLU.                                                           
DBREF  2Z65 A   27   228  UNP    O00206   TLR4_HUMAN      27    228             
DBREF  2Z65 A  231   302  UNP    Q4G1L2   Q4G1L2_EPTBU   128    199             
DBREF  2Z65 B   27   228  UNP    O00206   TLR4_HUMAN      27    228             
DBREF  2Z65 B  231   302  UNP    Q4G1L2   Q4G1L2_EPTBU   128    199             
DBREF  2Z65 C   19   158  UNP    Q9Y6Y9   LY96_HUMAN      19    158             
DBREF  2Z65 D   19   158  UNP    Q9Y6Y9   LY96_HUMAN      19    158             
SEQADV 2Z65 LYS A  229  UNP  O00206              SEE REMARK 999                 
SEQADV 2Z65 GLU A  230  UNP  O00206              SEE REMARK 999                 
SEQADV 2Z65 LYS B  229  UNP  O00206              SEE REMARK 999                 
SEQADV 2Z65 GLU B  230  UNP  O00206              SEE REMARK 999                 
SEQRES   1 A  276  GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN          
SEQRES   2 A  276  CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU          
SEQRES   3 A  276  PRO PHE SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO          
SEQRES   4 A  276  LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO          
SEQRES   5 A  276  GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN          
SEQRES   6 A  276  THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU          
SEQRES   7 A  276  SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU          
SEQRES   8 A  276  ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS          
SEQRES   9 A  276  LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN          
SEQRES  10 A  276  PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN          
SEQRES  11 A  276  VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU          
SEQRES  12 A  276  TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU          
SEQRES  13 A  276  SER SER ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU          
SEQRES  14 A  276  ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU          
SEQRES  15 A  276  ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY          
SEQRES  16 A  276  ALA PHE LYS GLU ILE ARG LEU LYS GLU LEU ALA LEU ASP          
SEQRES  17 A  276  THR ASN GLN LEU LYS SER VAL PRO ASP GLY ILE PHE ASP          
SEQRES  18 A  276  ARG LEU THR SER LEU GLN LYS ILE TRP LEU HIS THR ASN          
SEQRES  19 A  276  PRO TRP ASP CYS SER CYS PRO ARG ILE ASP TYR LEU SER          
SEQRES  20 A  276  ARG TRP LEU ASN LYS ASN SER GLN LYS GLU GLN GLY SER          
SEQRES  21 A  276  ALA LYS CYS SER GLY SER GLY LYS PRO VAL ARG SER ILE          
SEQRES  22 A  276  ILE CYS PRO                                                  
SEQRES   1 B  276  GLU PRO CYS VAL GLU VAL VAL PRO ASN ILE THR TYR GLN          
SEQRES   2 B  276  CYS MET GLU LEU ASN PHE TYR LYS ILE PRO ASP ASN LEU          
SEQRES   3 B  276  PRO PHE SER THR LYS ASN LEU ASP LEU SER PHE ASN PRO          
SEQRES   4 B  276  LEU ARG HIS LEU GLY SER TYR SER PHE PHE SER PHE PRO          
SEQRES   5 B  276  GLU LEU GLN VAL LEU ASP LEU SER ARG CYS GLU ILE GLN          
SEQRES   6 B  276  THR ILE GLU ASP GLY ALA TYR GLN SER LEU SER HIS LEU          
SEQRES   7 B  276  SER THR LEU ILE LEU THR GLY ASN PRO ILE GLN SER LEU          
SEQRES   8 B  276  ALA LEU GLY ALA PHE SER GLY LEU SER SER LEU GLN LYS          
SEQRES   9 B  276  LEU VAL ALA VAL GLU THR ASN LEU ALA SER LEU GLU ASN          
SEQRES  10 B  276  PHE PRO ILE GLY HIS LEU LYS THR LEU LYS GLU LEU ASN          
SEQRES  11 B  276  VAL ALA HIS ASN LEU ILE GLN SER PHE LYS LEU PRO GLU          
SEQRES  12 B  276  TYR PHE SER ASN LEU THR ASN LEU GLU HIS LEU ASP LEU          
SEQRES  13 B  276  SER SER ASN LYS ILE GLN SER ILE TYR CYS THR ASP LEU          
SEQRES  14 B  276  ARG VAL LEU HIS GLN MET PRO LEU LEU ASN LEU SER LEU          
SEQRES  15 B  276  ASP LEU SER LEU ASN PRO MET ASN PHE ILE GLN PRO GLY          
SEQRES  16 B  276  ALA PHE LYS GLU ILE ARG LEU LYS GLU LEU ALA LEU ASP          
SEQRES  17 B  276  THR ASN GLN LEU LYS SER VAL PRO ASP GLY ILE PHE ASP          
SEQRES  18 B  276  ARG LEU THR SER LEU GLN LYS ILE TRP LEU HIS THR ASN          
SEQRES  19 B  276  PRO TRP ASP CYS SER CYS PRO ARG ILE ASP TYR LEU SER          
SEQRES  20 B  276  ARG TRP LEU ASN LYS ASN SER GLN LYS GLU GLN GLY SER          
SEQRES  21 B  276  ALA LYS CYS SER GLY SER GLY LYS PRO VAL ARG SER ILE          
SEQRES  22 B  276  ILE CYS PRO                                                  
SEQRES   1 C  140  GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP ALA SER          
SEQRES   2 C  140  ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR PRO ILE          
SEQRES   3 C  140  SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS GLY SER          
SEQRES   4 C  140  LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG ARG ASP          
SEQRES   5 C  140  LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR VAL ASN          
SEQRES   6 C  140  THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE CYS ARG          
SEQRES   7 C  140  GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA LEU LYS          
SEQRES   8 C  140  GLY GLU THR VAL ASN THR THR ILE SER PHE SER PHE LYS          
SEQRES   9 C  140  GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS VAL VAL          
SEQRES  10 C  140  GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU PHE CYS          
SEQRES  11 C  140  LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN                      
SEQRES   1 D  140  GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP ALA SER          
SEQRES   2 D  140  ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR PRO ILE          
SEQRES   3 D  140  SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS GLY SER          
SEQRES   4 D  140  LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG ARG ASP          
SEQRES   5 D  140  LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR VAL ASN          
SEQRES   6 D  140  THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE CYS ARG          
SEQRES   7 D  140  GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA LEU LYS          
SEQRES   8 D  140  GLY GLU THR VAL ASN THR THR ILE SER PHE SER PHE LYS          
SEQRES   9 D  140  GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS VAL VAL          
SEQRES  10 D  140  GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU PHE CYS          
SEQRES  11 D  140  LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN                      
MODRES 2Z65 ASN A   35  ASN  GLYCOSYLATION SITE                                 
MODRES 2Z65 ASN A  205  ASN  GLYCOSYLATION SITE                                 
MODRES 2Z65 ASN B   35  ASN  GLYCOSYLATION SITE                                 
MODRES 2Z65 ASN B  205  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    NAG  A1401      14                                                       
HET    NAG  A1201      14                                                       
HET    NAG  B1401      14                                                       
HET    NAG  B1301      14                                                       
HET    NAG  B1201      14                                                       
HET    E55  C   1      89                                                       
HET    E55  D   1      89                                                       
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    7(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL  11  E55    2(C66 H126 N2 O19 P2)                                        
FORMUL  13  HOH   *163(H2 O)                                                    
HELIX    1   1 PRO A  168  ASN A  173  5                                   6    
HELIX    2   2 CYS A  192  MET A  201  5                                  10    
HELIX    3   3 ILE A  269  ASN A  279  1                                  11    
HELIX    4   4 PRO A  295  ILE A  299  5                                   5    
HELIX    5   5 SER B  140  PHE B  144  5                                   5    
HELIX    6   6 PRO B  168  ASN B  173  5                                   6    
HELIX    7   7 CYS B  192  MET B  201  5                                  10    
HELIX    8   8 ILE B  269  ASN B  279  1                                  11    
HELIX    9   9 PRO B  295  ILE B  299  5                                   5    
HELIX   10  10 TYR C  102  ALA C  107  5                                   6    
HELIX   11  11 TYR D  102  ALA D  107  5                                   6    
SHEET    1   A11 VAL A  30  VAL A  33  0                                        
SHEET    2   A11 THR A  37  GLN A  39 -1  O  THR A  37   N  VAL A  33           
SHEET    3   A11 ASN A  58  ASP A  60  1  O  ASP A  60   N  TYR A  38           
SHEET    4   A11 VAL A  82  ASP A  84  1  O  ASP A  84   N  LEU A  59           
SHEET    5   A11 THR A 106  ILE A 108  1  O  THR A 106   N  LEU A  83           
SHEET    6   A11 LYS A 130  VAL A 132  1  O  VAL A 132   N  LEU A 107           
SHEET    7   A11 GLU A 154  ASN A 156  1  O  GLU A 154   N  LEU A 131           
SHEET    8   A11 HIS A 179  ASP A 181  1  O  ASP A 181   N  LEU A 155           
SHEET    9   A11 LEU A 206  ASP A 209  1  O  SER A 207   N  LEU A 180           
SHEET   10   A11 ILE A 226  ALA A 232  1  O  ALA A 232   N  LEU A 208           
SHEET   11   A11 LEU A 249  THR A 250  1  O  THR A 250   N  ILE A 226           
SHEET    1   B12 VAL A  30  VAL A  33  0                                        
SHEET    2   B12 THR A  37  GLN A  39 -1  O  THR A  37   N  VAL A  33           
SHEET    3   B12 ASN A  58  ASP A  60  1  O  ASP A  60   N  TYR A  38           
SHEET    4   B12 VAL A  82  ASP A  84  1  O  ASP A  84   N  LEU A  59           
SHEET    5   B12 THR A 106  ILE A 108  1  O  THR A 106   N  LEU A  83           
SHEET    6   B12 LYS A 130  VAL A 132  1  O  VAL A 132   N  LEU A 107           
SHEET    7   B12 GLU A 154  ASN A 156  1  O  GLU A 154   N  LEU A 131           
SHEET    8   B12 HIS A 179  ASP A 181  1  O  ASP A 181   N  LEU A 155           
SHEET    9   B12 LEU A 206  ASP A 209  1  O  SER A 207   N  LEU A 180           
SHEET   10   B12 ILE A 226  ALA A 232  1  O  ALA A 232   N  LEU A 208           
SHEET   11   B12 LYS A 254  TRP A 256  1  O  LYS A 254   N  LEU A 231           
SHEET   12   B12 GLU A 283  GLN A 284  1  O  GLN A 284   N  ILE A 255           
SHEET    1   C 2 HIS A  68  LEU A  69  0                                        
SHEET    2   C 2 THR A  92  ILE A  93  1  O  THR A  92   N  LEU A  69           
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   E11 VAL B  30  VAL B  33  0                                        
SHEET    2   E11 THR B  37  GLN B  39 -1  O  THR B  37   N  VAL B  33           
SHEET    3   E11 ASN B  58  ASP B  60  1  O  ASN B  58   N  TYR B  38           
SHEET    4   E11 VAL B  82  ASP B  84  1  O  ASP B  84   N  LEU B  59           
SHEET    5   E11 THR B 106  ILE B 108  1  O  THR B 106   N  LEU B  83           
SHEET    6   E11 LYS B 130  VAL B 132  1  O  VAL B 132   N  LEU B 107           
SHEET    7   E11 GLU B 154  ASN B 156  1  O  GLU B 154   N  LEU B 131           
SHEET    8   E11 HIS B 179  ASP B 181  1  O  ASP B 181   N  LEU B 155           
SHEET    9   E11 LEU B 206  ASP B 209  1  O  ASP B 209   N  LEU B 180           
SHEET   10   E11 ILE B 226  ALA B 232  1  O  GLU B 230   N  LEU B 208           
SHEET   11   E11 LEU B 249  THR B 250  1  O  THR B 250   N  ILE B 226           
SHEET    1   F12 VAL B  30  VAL B  33  0                                        
SHEET    2   F12 THR B  37  GLN B  39 -1  O  THR B  37   N  VAL B  33           
SHEET    3   F12 ASN B  58  ASP B  60  1  O  ASN B  58   N  TYR B  38           
SHEET    4   F12 VAL B  82  ASP B  84  1  O  ASP B  84   N  LEU B  59           
SHEET    5   F12 THR B 106  ILE B 108  1  O  THR B 106   N  LEU B  83           
SHEET    6   F12 LYS B 130  VAL B 132  1  O  VAL B 132   N  LEU B 107           
SHEET    7   F12 GLU B 154  ASN B 156  1  O  GLU B 154   N  LEU B 131           
SHEET    8   F12 HIS B 179  ASP B 181  1  O  ASP B 181   N  LEU B 155           
SHEET    9   F12 LEU B 206  ASP B 209  1  O  ASP B 209   N  LEU B 180           
SHEET   10   F12 ILE B 226  ALA B 232  1  O  GLU B 230   N  LEU B 208           
SHEET   11   F12 LYS B 254  TRP B 256  1  O  LYS B 254   N  LEU B 231           
SHEET   12   F12 GLU B 283  GLN B 284  1  O  GLN B 284   N  ILE B 255           
SHEET    1   G 2 HIS B  68  LEU B  69  0                                        
SHEET    2   G 2 THR B  92  ILE B  93  1  O  THR B  92   N  LEU B  69           
SHEET    1   H 2 SER B 189  ILE B 190  0                                        
SHEET    2   H 2 PHE B 217  ILE B 218  1  O  PHE B 217   N  ILE B 190           
SHEET    1   I 6 TYR C  22  ASN C  26  0                                        
SHEET    2   I 6 SER C  31  TYR C  36 -1  O  TYR C  34   N  TYR C  22           
SHEET    3   I 6 GLU C 144  LEU C 154 -1  O  GLU C 150   N  THR C  35           
SHEET    4   I 6 TYR C 131  SER C 139 -1  N  ALA C 137   O  LEU C 146           
SHEET    5   I 6 TYR C  75  VAL C  82 -1  N  TYR C  79   O  VAL C 134           
SHEET    6   I 6 MET C  85  ASN C  86 -1  O  MET C  85   N  VAL C  82           
SHEET    1   J 6 TYR C  22  ASN C  26  0                                        
SHEET    2   J 6 SER C  31  TYR C  36 -1  O  TYR C  34   N  TYR C  22           
SHEET    3   J 6 GLU C 144  LEU C 154 -1  O  GLU C 150   N  THR C  35           
SHEET    4   J 6 TYR C 131  SER C 139 -1  N  ALA C 137   O  LEU C 146           
SHEET    5   J 6 TYR C  75  VAL C  82 -1  N  TYR C  79   O  VAL C 134           
SHEET    6   J 6 ARG C  90  VAL C  93 -1  O  GLU C  92   N  PHE C  76           
SHEET    1   K 3 SER C  45  ASN C  49  0                                        
SHEET    2   K 3 GLY C  56  TYR C  65 -1  O  HIS C  62   N  ASN C  47           
SHEET    3   K 3 VAL C 113  LYS C 122 -1  O  ILE C 117   N  LEU C  61           
SHEET    1   L 6 TYR D  22  ASN D  26  0                                        
SHEET    2   L 6 SER D  31  TYR D  36 -1  O  TYR D  34   N  TYR D  22           
SHEET    3   L 6 GLU D 144  LEU D 154 -1  O  GLU D 150   N  THR D  35           
SHEET    4   L 6 TYR D 131  SER D 139 -1  N  ALA D 137   O  LEU D 146           
SHEET    5   L 6 TYR D  75  VAL D  82 -1  N  TYR D  79   O  VAL D 134           
SHEET    6   L 6 MET D  85  ASN D  86 -1  O  MET D  85   N  VAL D  82           
SHEET    1   M 6 TYR D  22  ASN D  26  0                                        
SHEET    2   M 6 SER D  31  TYR D  36 -1  O  TYR D  34   N  TYR D  22           
SHEET    3   M 6 GLU D 144  LEU D 154 -1  O  GLU D 150   N  THR D  35           
SHEET    4   M 6 TYR D 131  SER D 139 -1  N  ALA D 137   O  LEU D 146           
SHEET    5   M 6 TYR D  75  VAL D  82 -1  N  TYR D  79   O  VAL D 134           
SHEET    6   M 6 ARG D  90  VAL D  93 -1  O  GLU D  92   N  PHE D  76           
SHEET    1   N 3 SER D  45  ASN D  49  0                                        
SHEET    2   N 3 GLY D  56  TYR D  65 -1  O  HIS D  62   N  ASN D  47           
SHEET    3   N 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  2.05  
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   29    CYS B   40                          1555   1555  2.06  
SSBOND   5 CYS B  264    CYS B  289                          1555   1555  2.03  
SSBOND   6 CYS B  266    CYS B  301                          1555   1555  2.04  
SSBOND   7 CYS C   25    CYS C   51                          1555   1555  2.76  
SSBOND   8 CYS C   37    CYS C  148                          1555   1555  2.06  
SSBOND   9 CYS C   95    CYS C  105                          1555   1555  2.02  
SSBOND  10 CYS D   25    CYS D   51                          1555   1555  2.75  
SSBOND  11 CYS D   37    CYS D  148                          1555   1555  2.07  
SSBOND  12 CYS D   95    CYS D  105                          1555   1555  2.03  
LINK         ND2 ASN A  35                 C1  NAG A1201     1555   1555  1.45  
LINK         ND2 ASN A 205                 C1  NAG E   1     1555   1555  1.46  
LINK         ND2 ASN B  35                 C1  NAG B1201     1555   1555  1.45  
LINK         ND2 ASN B 205                 C1  NAG B1301     1555   1555  1.44  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.46  
CISPEP   1 CYS A  266    PRO A  267          0         1.58                     
CISPEP   2 CYS B  266    PRO B  267          0         0.42                     
CISPEP   3 ASN C   49    PRO C   50          0         0.31                     
CISPEP   4 ASN D   49    PRO D   50          0        -2.67                     
CRYST1   67.192   80.987  107.762  90.00  93.01  90.00 P 1 21 1      4          
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      0.014883  0.000000  0.000783        0.00000                         
SCALE2      0.000000  0.012348  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009293        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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