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Database: PDB
Entry: 2E59
LinkDB: 2E59
Original site: 2E59 
HEADER    LIPID BINDING PROTEIN                   19-DEC-06   2E59              
TITLE     CRYSTAL STRUCTURE OF HUMAN MD-2 IN COMPLEX WITH LIPID IVA             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYMPHOCYTE ANTIGEN 96;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MD-2 PROTEIN, ESOP-1;                                       
COMPND   5 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: LY96, ESOP1, MD2;                                              
SOURCE   6 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPIC9, PPICZA, PPIC6A                     
KEYWDS    INNATE IMMUNITY, LIPID-BINDING, LIPID BINDING PROTEIN                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    U.OHTO,Y.SATOW                                                        
REVDAT   5   29-JUL-20 2E59    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   13-JUL-11 2E59    1       VERSN                                    
REVDAT   3   14-APR-09 2E59    1       CONECT                                   
REVDAT   2   24-FEB-09 2E59    1       VERSN                                    
REVDAT   1   26-JUN-07 2E59    0                                                
JRNL        AUTH   U.OHTO,K.FUKASE,K.MIYAKE,Y.SATOW                             
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN MD-2 AND ITS COMPLEX WITH        
JRNL        TITL 2 ANTIENDOTOXIC LIPID IVA                                      
JRNL        REF    SCIENCE                       V. 316  1632 2007              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   17569869                                                     
JRNL        DOI    10.1126/SCIENCE.1139111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.21 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) : 2.21                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.500                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 6291                           
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 297                             
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) : 2.21                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 184                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 31.95                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 8                            
REMARK   3   BIN FREE R VALUE                    : 0.2990                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1162                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 123                                     
REMARK   3   SOLVENT ATOMS            : 89                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.08000                                              
REMARK   3    B22 (A**2) : 1.08000                                              
REMARK   3    B33 (A**2) : -2.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.674         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.300         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
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):  1326 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1782 ; 1.495 ; 2.059       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   145 ; 6.597 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;33.862 ;24.340       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   220 ;16.278 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ; 8.002 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   197 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   921 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   554 ; 0.259 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   899 ; 0.344 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   134 ; 0.233 ; 0.500       
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):    46 ; 0.255 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.218 ; 0.500       
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):   725 ; 4.014 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1181 ; 6.072 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   601 ; 4.389 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   601 ; 6.181 ; 3.000       
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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2E59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-DEC-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000026241.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
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          : RIGAKU JUPITER 210                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7629                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.7                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
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: PDB ENTRY 2E56                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 40MM NA-CITRATE, PH 5.4,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.0K                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       55.44450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.39750            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.39750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       27.72225            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.39750            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.39750            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       83.16675            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.39750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.39750            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       27.72225            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.39750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.39750            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       83.16675            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       55.44450            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: 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   O6   LP5 A   501     O5   LP4 A   601              1.96            
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    SER A  27     -164.70   -105.44                                   
REMARK 500    ASP A  38     -147.36     43.61                                   
REMARK 500    GLN A  41     -162.33   -113.28                                   
REMARK 500    LYS A  55        4.02    -69.42                                   
REMARK 500    THR A  84      -13.52     68.59                                   
REMARK 500    LYS A  89      150.89    -46.42                                   
REMARK 500    ARG A  96     -128.45   -102.32                                   
REMARK 500    SER A  98     -139.10     44.35                                   
REMARK 500    LYS A 109      113.00    -33.38                                   
REMARK 500    THR A 112      124.54    -38.55                                   
REMARK 500    SER A 141      111.83    -19.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2E56   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN                                                     
DBREF  2E59 A   17   160  UNP    Q9Y6Y9   LY96_HUMAN      17    160             
SEQRES   1 A  144  GLU ALA GLN LYS GLN TYR TRP VAL CYS ASN SER SER ASP          
SEQRES   2 A  144  ALA SER ILE SER TYR THR TYR CYS ASP LYS MET GLN TYR          
SEQRES   3 A  144  PRO ILE SER ILE ASN VAL ASN PRO CYS ILE GLU LEU LYS          
SEQRES   4 A  144  GLY SER LYS GLY LEU LEU HIS ILE PHE TYR ILE PRO ARG          
SEQRES   5 A  144  ARG ASP LEU LYS GLN LEU TYR PHE ASN LEU TYR ILE THR          
SEQRES   6 A  144  VAL ASN THR MET ASN LEU PRO LYS ARG LYS GLU VAL ILE          
SEQRES   7 A  144  CYS ARG GLY SER ASP ASP ASP TYR SER PHE CYS ARG ALA          
SEQRES   8 A  144  LEU LYS GLY GLU THR VAL ASN THR THR ILE SER PHE SER          
SEQRES   9 A  144  PHE LYS GLY ILE LYS PHE SER LYS GLY LYS TYR LYS CYS          
SEQRES  10 A  144  VAL VAL GLU ALA ILE SER GLY SER PRO GLU GLU MET LEU          
SEQRES  11 A  144  PHE CYS LEU GLU PHE VAL ILE LEU HIS GLN PRO ASN SER          
SEQRES  12 A  144  ASN                                                          
MODRES 2E59 ASN A   26  ASN  GLYCOSYLATION SITE                                 
MODRES 2E59 ASN A  114  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 801      14                                                       
HET    NAG  A 901      14                                                       
HET    LP5  A 501      48                                                       
HET    LP4  A 601      47                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-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     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                                                   
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   4  LP5    C34 H66 N O12 P                                              
FORMUL   5  LP4    C34 H66 N O12 P                                              
FORMUL   6  HOH   *89(H2 O)                                                     
HELIX    1   1 TYR A  102  ALA A  107  5                                   6    
SHEET    1   A 6 TYR A  22  ASN A  26  0                                        
SHEET    2   A 6 ALA A  30  TYR A  36 -1  O  ILE A  32   N  CYS A  25           
SHEET    3   A 6 GLU A 144  HIS A 155 -1  O  LEU A 154   N  SER A  31           
SHEET    4   A 6 LYS A 130  SER A 139 -1  N  ALA A 137   O  LEU A 146           
SHEET    5   A 6 TYR A  75  VAL A  82 -1  N  TYR A  75   O  ILE A 138           
SHEET    6   A 6 MET A  85  ASN A  86 -1  O  MET A  85   N  VAL A  82           
SHEET    1   B 6 TYR A  22  ASN A  26  0                                        
SHEET    2   B 6 ALA A  30  TYR A  36 -1  O  ILE A  32   N  CYS A  25           
SHEET    3   B 6 GLU A 144  HIS A 155 -1  O  LEU A 154   N  SER A  31           
SHEET    4   B 6 LYS A 130  SER A 139 -1  N  ALA A 137   O  LEU A 146           
SHEET    5   B 6 TYR A  75  VAL A  82 -1  N  TYR A  75   O  ILE A 138           
SHEET    6   B 6 ARG A  90  VAL A  93 -1  O  ARG A  90   N  LEU A  78           
SHEET    1   C 3 ILE A  44  ASN A  49  0                                        
SHEET    2   C 3 SER A  57  TYR A  65 -1  O  LEU A  60   N  ASN A  49           
SHEET    3   C 3 VAL A 113  PHE A 121 -1  O  VAL A 113   N  TYR A  65           
SSBOND   1 CYS A   25    CYS A   51                          1555   1555  2.02  
SSBOND   2 CYS A   37    CYS A  148                          1555   1555  2.04  
SSBOND   3 CYS A   95    CYS A  105                          1555   1555  2.04  
LINK         ND2 ASN A  26                 C1  NAG A 801     1555   1555  1.45  
LINK         ND2 ASN A 114                 C1  NAG A 901     1555   1555  1.43  
LINK         O6  LP5 A 501                 C1  LP4 A 601     1555   1555  1.33  
CISPEP   1 ASN A   49    PRO A   50          0        -9.37                     
CISPEP   2 SER A  141    PRO A  142          0        13.63                     
CRYST1   52.795   52.795  110.889  90.00  90.00  90.00 P 41 21 2     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      0.018941  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018941  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009018        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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