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Database: PDB
Entry: 1H15
LinkDB: 1H15
Original site: 1H15 
HEADER    IMMUNE SYSTEM/TRANSFERASE               02-JUL-02   1H15              
TITLE     X-RAY CRYSTAL STRUCTURE OF HLA-DRA1*0101/DRB5*0101 COMPLEXED WITH A   
TITLE    2 PEPTIDE FROM EPSTEIN BARR VIRUS DNA POLYMERASE                       
CAVEAT     1H15    NAG G 2 HAS WRONG CHIRALITY AT ATOM C1 NAG D 1184 HAS WRONG  
CAVEAT   2 1H15    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: ALPHA CHAIN, RESIDUES 26-207;                              
COMPND   5 SYNONYM: HLA-DRA, MAJOR HISTOCOMPATIBILITY COMPLEX A CHAIN;          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR BETA 1 CHAIN;  
COMPND   9 CHAIN: B, E;                                                         
COMPND  10 FRAGMENT: BETA CHAIN, RESIDUES 30-219;                               
COMPND  11 SYNONYM: HLA-DRB1, MAJOR HISTOCOMPATIBILITY COMPLEX B CHAIN;         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: DNA POLYMERASE;                                            
COMPND  15 CHAIN: C, F;                                                         
COMPND  16 FRAGMENT: RESIDUES 628-641;                                          
COMPND  17 SYNONYM: EPSTEIN BARR VIUS (EBV) DNA POLYMERASE;                     
COMPND  18 EC: 2.7.7.7;                                                         
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: S2;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: S2;                                     
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;                            
SOURCE  18 ORGANISM_COMMON: EPSTEIN BARR VIRUS;                                 
SOURCE  19 ORGANISM_TAXID: 10376;                                               
SOURCE  20 OTHER_DETAILS: THE PROTEIN OCCURS NATURALLY IN EBV BUT THE PEPTIDE   
SOURCE  21 WAS SYNTHESISED CHEMICALLY                                           
KEYWDS    IMMUNE SYSTEM/TRANSFERASE, COMPLEX (MHC-ANTIGEN), IMMUNE SYSTEM, MHC, 
KEYWDS   2 HLA, CLASS II, DR2, DRB5, EBV, DNA POLYMERASE, DNA-DIRECTED DNA      
KEYWDS   3 POLYMERASE, IMMUNE SYSTEM-TRANSFERASE COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.LANG,H.JACOBSEN,S.IKEMIZU,C.ANDERSSON,K.HARLOS,L.MADSEN,P.HJORTH,   
AUTHOR   2 L.SONDERGAARD,A.SVEJGAARD,K.WUCHERPFENNIG,D.I.STUART,J.I.BELL,       
AUTHOR   3 E.Y.JONES,L.FUGGER                                                   
REVDAT   5   29-JUL-20 1H15    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE   ATOM                       
REVDAT   4   27-JUN-12 1H15    1       JRNL                                     
REVDAT   3   28-SEP-11 1H15    1       CAVEAT REMARK HET    FORMUL              
REVDAT   3 2                   1       HETNAM HETSYN LINK   SITE                
REVDAT   3 3                   1       HETATM CONECT VERSN                      
REVDAT   2   24-FEB-09 1H15    1       VERSN                                    
REVDAT   1   03-OCT-02 1H15    0                                                
JRNL        AUTH   H.LANG,H.JACOBSEN,S.IKEMIZU,C.ANDERSSON,K.HARLOS,L.MADSEN,   
JRNL        AUTH 2 P.HJORTH,L.SONDERGAARD,A.SVEJGAARD,K.WUCHERPFENNIG,          
JRNL        AUTH 3 D.I.STUART,J.I.BELL,E.Y.JONES,L.FUGGER                       
JRNL        TITL   A FUNCTIONAL AND STRUCTURAL BASIS FOR TCR CROSS-REACTIVITY   
JRNL        TITL 2 IN MULTIPLE SCLEROSIS                                        
JRNL        REF    NAT.IMMUNOL.                  V.   3   940 2002              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   12244309                                                     
JRNL        DOI    10.1038/NI835                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 64350.380                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28750                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.256                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1415                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 71.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3455                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4560                       
REMARK   3   BIN FREE R VALUE                    : 0.4790                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 197                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.034                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6320                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 30                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.37000                                              
REMARK   3    B22 (A**2) : 2.37000                                              
REMARK   3    B33 (A**2) : -4.74000                                             
REMARK   3    B12 (A**2) : 12.75000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.49                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.87                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.62                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 1.07                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.920                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.520 ; 2.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.350 ; 3.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.540 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.900 ; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 80.00                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290009971.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 3.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : SI111 / SI311 CRYSTALS, LN2        
REMARK 200                                   COOLED                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28750                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.41400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.77400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: SINGLE COPY OF 1FV1 (A AND B CHAINS) MINUS PEPTIDE   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 3550, 100MM GLYCINE AND 10MM     
REMARK 280  TRIS AT PH 3.5-4.0., PH 3.50                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.92267            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.96133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       46.44200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.48067            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       77.40333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ILE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ILE D     1                                                      
REMARK 465     LYS D     2                                                      
REMARK 465     GLY E     1                                                      
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    GLU A  88   N   -  CA  -  C   ANGL. DEV. = -16.6 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    ALA A  37      -71.60    -49.88                                   
REMARK 500    ARG A  50       -9.64    -57.28                                   
REMARK 500    ARG A  76      -15.12    -46.95                                   
REMARK 500    TYR A  79       58.00     31.91                                   
REMARK 500    PRO A  87     -161.65    -58.72                                   
REMARK 500    GLU A  88      102.73   -168.09                                   
REMARK 500    LEU A  99      140.86    -37.89                                   
REMARK 500    ARG A 100       23.86     47.12                                   
REMARK 500    PRO A 102      145.75    -34.45                                   
REMARK 500    THR A 113      147.24    165.92                                   
REMARK 500    PRO A 115       67.96    -66.21                                   
REMARK 500    ASN A 124       74.53     59.83                                   
REMARK 500    LEU A 144     -161.44   -104.73                                   
REMARK 500    PRO A 155      104.54    -44.23                                   
REMARK 500    ASP A 181       71.87     83.18                                   
REMARK 500    ASN B  33      -81.08     52.64                                   
REMARK 500    GLN B  34       13.22   -145.88                                   
REMARK 500    GLU B  52      -16.51    -49.87                                   
REMARK 500    ARG B  55      -64.26    -26.07                                   
REMARK 500    VAL B  75      -14.19    -46.64                                   
REMARK 500    ASP B  76      -57.89   -122.17                                   
REMARK 500    TYR B  78      -60.94   -107.05                                   
REMARK 500    CYS B  79      -81.49    -60.54                                   
REMARK 500    THR B  90      -69.81   -146.33                                   
REMARK 500    ARG B 105      109.63     47.88                                   
REMARK 500    GLN B 107      -36.63    -36.79                                   
REMARK 500    TYR B 123      -86.36    -92.88                                   
REMARK 500    PRO B 124      114.99    -32.17                                   
REMARK 500    SER B 135       70.83     35.03                                   
REMARK 500    GLN B 136      111.16   -170.62                                   
REMARK 500    GLU B 138       50.43    -93.83                                   
REMARK 500    LYS B 139      -15.32    -29.79                                   
REMARK 500    PRO B 178       46.78    -55.37                                   
REMARK 500    GLU D   4      -36.21   -131.36                                   
REMARK 500    ALA D  37      -75.65    -47.85                                   
REMARK 500    ARG D  76        9.73    -58.19                                   
REMARK 500    ASN D  84      109.63    -58.73                                   
REMARK 500    PRO D  96      168.49    -45.78                                   
REMARK 500    LEU D  99      132.12    -33.35                                   
REMARK 500    ARG D 100       -7.16     73.13                                   
REMARK 500    PRO D 102      109.10    -49.10                                   
REMARK 500    ASN D 103     -167.17   -116.25                                   
REMARK 500    THR D 113      152.28    175.80                                   
REMARK 500    PRO D 115       70.46    -66.05                                   
REMARK 500    ASN D 124      -20.56     64.05                                   
REMARK 500    THR D 130       95.99    -65.77                                   
REMARK 500    VAL D 136     -125.47    -85.88                                   
REMARK 500    HIS D 143       33.49     80.52                                   
REMARK 500    LEU D 144     -164.48   -105.27                                   
REMARK 500    PRO D 155       98.92    -32.85                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1A6A   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION: CLIP    
REMARK 900 BOUND TO HLA-DR3                                                     
REMARK 900 RELATED ID: 1AQD   RELATED DB: PDB                                   
REMARK 900 HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II HISTOCOMPATIBILITYPROTEIN    
REMARK 900 (EXTRACELLULAR DOMAIN) COMPLEXED WITH ENDOGENOUSPEPTIDE              
REMARK 900 RELATED ID: 1D5M   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH PEPTIDE            
REMARK 900 RELATED ID: 1D5X   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH DIPEPTIDE MIMETIC  
REMARK 900 RELATED ID: 1D5Z   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH PEPTIDOMIMETIC     
REMARK 900 RELATED ID: 1D6E   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HLA-DR4 COMPLEX WITH PEPTIDOMIMETIC AND SEB     
REMARK 900 RELATED ID: 1DLH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FV1   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL BASIS FOR THE BINDING OF AN IMMUNODOMINANTPEPTIDE FROM    
REMARK 900 MYELIN BASIC PROTEIN IN DIFFERENT REGISTERS BY TWO HLA-DR2 ALLELES   
REMARK 900 RELATED ID: 1HQR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-AFFINITY,      
REMARK 900 ZINC-DEPENDENT SITE ON MHC CLASS II                                  
REMARK 900 RELATED ID: 1HXY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN H INCOMPLEX WITH     
REMARK 900 HUMAN MHC CLASS II                                                   
REMARK 900 RELATED ID: 1J8H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELLRECEPTOR, 
REMARK 900 INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS IIMOLECULE, HLA-DR4      
REMARK 900 RELATED ID: 1KG0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE EPSTEIN-BARR VIRUS GP42 PROTEIN BOUND TOTHE MHC     
REMARK 900 CLASS II RECEPTOR HLA-DR1                                            
REMARK 900 RELATED ID: 1SEB   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-DR1 ANDTHE        
REMARK 900 BACTERIAL SUPERANTIGEN SEB                                           
REMARK 900 RELATED ID: 2SEB   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HLA-DR4 COMPLEXED WITH A PEPTIDE FROM     
REMARK 900 HUMAN COLLAGEN II                                                    
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUES 26-207 OF DATABASE SEQUENCE                                 
REMARK 999  RESIDUES 30-219 OF DATABASE SEQUENCE                                
DBREF  1H15 A    1   182  UNP    P01903   HA2R_HUMAN      26    207             
DBREF  1H15 B    1   190  UNP    Q30126   Q30126          30    219             
DBREF  1H15 C  628   641  UNP    P03198   DPOL_EBV       628    641             
DBREF  1H15 D    1   182  UNP    P01903   HA2R_HUMAN      26    207             
DBREF  1H15 E    1   190  UNP    Q30126   Q30126          30    219             
DBREF  1H15 F  628   641  UNP    P03198   DPOL_EBV       628    641             
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR          
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE          
SEQRES   3 B  190  LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG          
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU          
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS          
SEQRES   6 B  190  ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR          
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL          
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA          
SEQRES   9 B  190  ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 B  190  SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 B  190  TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL          
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN          
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU          
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER          
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA                              
SEQRES   1 C   14  GLY GLY VAL TYR HIS PHE VAL LYS LYS HIS VAL HIS GLU          
SEQRES   2 C   14  SER                                                          
SEQRES   1 D  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 D  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 D  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 D  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 D  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 D  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 D  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 D  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 D  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 D  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 D  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 D  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 D  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 D  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES   1 E  190  GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR          
SEQRES   2 E  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE          
SEQRES   3 E  190  LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG          
SEQRES   4 E  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU          
SEQRES   5 E  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS          
SEQRES   6 E  190  ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR          
SEQRES   7 E  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL          
SEQRES   8 E  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA          
SEQRES   9 E  190  ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 E  190  SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 E  190  TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL          
SEQRES  12 E  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN          
SEQRES  13 E  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU          
SEQRES  14 E  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER          
SEQRES  15 E  190  PRO LEU THR VAL GLU TRP ARG ALA                              
SEQRES   1 F   14  GLY GLY VAL TYR HIS PHE VAL LYS LYS HIS VAL HIS GLU          
SEQRES   2 F   14  SER                                                          
MODRES 1H15 ASN A   78  ASN  GLYCOSYLATION SITE                                 
MODRES 1H15 ASN A  118  ASN  GLYCOSYLATION SITE                                 
MODRES 1H15 ASN D   78  ASN  GLYCOSYLATION SITE                                 
MODRES 1H15 ASN D  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    NAG  A1185      14                                                       
HET    NAG  D1183      14                                                       
HET    NAG  D1184      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   7  NAG    5(C8 H15 N O6)                                               
FORMUL  11  HOH   *30(H2 O)                                                     
HELIX    1   1 LEU A   45  PHE A   51  1                                   7    
HELIX    2   2 GLU A   55  ARG A   76  1                                  22    
HELIX    3   3 GLN B   64  ALA B   73  1                                  10    
HELIX    4   4 ALA B   73  TYR B   78  1                                   6    
HELIX    5   5 TYR B   78  VAL B   85  5                                   8    
HELIX    6   6 LEU D   45  PHE D   51  1                                   7    
HELIX    7   7 GLU D   55  ARG D   76  1                                  22    
HELIX    8   8 GLN E   64  ALA E   73  1                                  10    
HELIX    9   9 ALA E   73  TYR E   78  1                                   6    
HELIX   10  10 TYR E   78  VAL E   85  5                                   8    
SHEET    1  AA 8 GLU A  40  TRP A  43  0                                        
SHEET    2  AA 8 ASP A  29  ASP A  35 -1  O  HIS A  33   N  VAL A  42           
SHEET    3  AA 8 SER A  19  PHE A  26 -1  O  PHE A  22   N  VAL A  34           
SHEET    4  AA 8 HIS A   5  ASN A  15 -1  O  ILE A   8   N  ASP A  25           
SHEET    5  AA 8 PHE B   7  PHE B  18 -1  O  PHE B   7   N  ASN A  15           
SHEET    6  AA 8 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18           
SHEET    7  AA 8 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32           
SHEET    8  AA 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1  AB 2 ALA A  52  SER A  53  0                                        
SHEET    2  AB 2 GLY C 629  VAL C 630  1  O  GLY C 629   N  SER A  53           
SHEET    1  AC 4 VAL A  89  THR A  93  0                                        
SHEET    2  AC 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3  AC 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  PHE A 112           
SHEET    4  AC 4 SER A 133  GLU A 134 -1  O  SER A 133   N  TYR A 150           
SHEET    1  AD 4 VAL A  89  THR A  93  0                                        
SHEET    2  AD 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3  AD 4 PHE A 145  PHE A 153 -1  O  PHE A 145   N  PHE A 112           
SHEET    4  AD 4 LEU A 138  PRO A 139 -1  O  LEU A 138   N  ARG A 146           
SHEET    1  AE 4 LYS A 126  VAL A 128  0                                        
SHEET    2  AE 4 VAL A 117  ARG A 123 -1  O  TRP A 121   N  VAL A 128           
SHEET    3  AE 4 VAL A 160  HIS A 167 -1  O  ASP A 162   N  LEU A 122           
SHEET    4  AE 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165           
SHEET    1  BA 4 VAL B 101  ALA B 104  0                                        
SHEET    2  BA 4 ASN B 113  PHE B 122 -1  O  LEU B 114   N  ALA B 104           
SHEET    3  BA 4 PHE B 155  THR B 163 -1  O  PHE B 155   N  GLY B 121           
SHEET    4  BA 4 VAL B 142  SER B 144 -1  O  VAL B 143   N  MET B 160           
SHEET    1  BB 4 VAL B 101  ALA B 104  0                                        
SHEET    2  BB 4 ASN B 113  PHE B 122 -1  O  LEU B 114   N  ALA B 104           
SHEET    3  BB 4 PHE B 155  THR B 163 -1  O  PHE B 155   N  GLY B 121           
SHEET    4  BB 4 ILE B 148  GLN B 149 -1  O  ILE B 148   N  GLN B 156           
SHEET    1  BC 3 GLU B 128  ARG B 133  0                                        
SHEET    2  BC 3 VAL B 170  GLU B 176 -1  O  THR B 172   N  PHE B 132           
SHEET    3  BC 3 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175           
SHEET    1  DA 8 GLU D  40  TRP D  43  0                                        
SHEET    2  DA 8 ASP D  29  ASP D  35 -1  O  HIS D  33   N  VAL D  42           
SHEET    3  DA 8 SER D  19  PHE D  26 -1  O  PHE D  22   N  VAL D  34           
SHEET    4  DA 8 HIS D   5  LEU D  14 -1  O  ILE D   8   N  ASP D  25           
SHEET    5  DA 8 LEU E   8  PHE E  18 -1  O  GLN E   9   N  TYR D  13           
SHEET    6  DA 8 ARG E  23  TYR E  32 -1  O  ARG E  23   N  PHE E  18           
SHEET    7  DA 8 GLU E  35  ASP E  41 -1  O  GLU E  35   N  TYR E  32           
SHEET    8  DA 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39           
SHEET    1  DB 2 ALA D  52  SER D  53  0                                        
SHEET    2  DB 2 GLY F 629  VAL F 630  1  O  GLY F 629   N  SER D  53           
SHEET    1  DC 4 GLU D  88  THR D  93  0                                        
SHEET    2  DC 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92           
SHEET    3  DC 4 PHE D 145  PHE D 153 -1  O  PHE D 145   N  PHE D 112           
SHEET    4  DC 4 LEU D 138  PRO D 139 -1  O  LEU D 138   N  ARG D 146           
SHEET    1  DD 4 LYS D 126  PRO D 127  0                                        
SHEET    2  DD 4 THR D 120  ARG D 123 -1  O  ARG D 123   N  LYS D 126           
SHEET    3  DD 4 TYR D 161  VAL D 165 -1  O  ASP D 162   N  LEU D 122           
SHEET    4  DD 4 LEU D 174  TRP D 178 -1  O  LEU D 174   N  VAL D 165           
SHEET    1  EA 4 LYS E  98  PRO E 103  0                                        
SHEET    2  EA 4 LEU E 115  ASN E 120 -1  O  VAL E 116   N  TYR E 102           
SHEET    3  EA 4 GLN E 156  LEU E 161 -1  O  THR E 157   N  VAL E 119           
SHEET    4  EA 4 VAL E 142  SER E 144 -1  O  VAL E 143   N  MET E 160           
SHEET    1  EB 4 GLN E 136  GLU E 138  0                                        
SHEET    2  EB 4 GLU E 128  ARG E 133 -1  O  TRP E 131   N  GLU E 138           
SHEET    3  EB 4 VAL E 170  GLU E 176 -1  O  THR E 172   N  PHE E 132           
SHEET    4  EB 4 LEU E 184  ARG E 189 -1  O  LEU E 184   N  VAL E 175           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.02  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.03  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.02  
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.03  
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.04  
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.03  
LINK         ND2 ASN A  78                 C1  NAG A1185     1555   1555  1.46  
LINK         ND2 ASN A 118                 C1  NAG G   1     1555   1555  1.45  
LINK         ND2 ASN D  78                 C1  NAG D1184     1555   1555  1.46  
LINK         ND2 ASN D 118                 C1  NAG D1183     1555   1555  1.45  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.39  
CISPEP   1 ASN A   15    PRO A   16          0         0.42                     
CISPEP   2 THR A  113    PRO A  114          0         0.33                     
CISPEP   3 THR D  113    PRO D  114          0        -0.21                     
CRYST1  179.244  179.244   92.884  90.00  90.00 120.00 P 65         12          
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      0.005579  0.003221  0.000000        0.00000                         
SCALE2      0.000000  0.006442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010766        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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