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Database: PDB
Entry: 1ED3
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Original site: 1ED3 
HEADER    IMMUNE SYSTEM                           26-JAN-00   1ED3              
TITLE     CRYSTAL STRUCTURE OF RAT MINOR HISTOCOMPATIBILITY ANTIGEN COMPLEX RT1-
TITLE    2 AA/MTF-E.                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CLASS I MAJOR HISTOCOMPATIBILITY ANTIGEN RT1-AA;           
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAINS;                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND   8 CHAIN: B, E;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: PEPTIDE MTF-E (13N3E);                                     
COMPND  12 CHAIN: C, F;                                                         
COMPND  13 FRAGMENT: RESIDUES 29-41 OF RAT ATPASE 6;                            
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET-22B;                                  
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  10 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  11 ORGANISM_TAXID: 10116;                                               
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PET-22B;                                  
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN RATS                
KEYWDS    MAJOR HISTOCOMPATIBILITY COMPLEX, RAT MINOR HISTOCOMPATIBILITY        
KEYWDS   2 COMPLEX, MHC, IMMUNOLOGY, PEPTIDE ANTIGEN PRESENTATION, CELLULAR     
KEYWDS   3 IMMUNITY, CELL SURFACE RECEPTOR, T CELL RECEPTOR LIGAND, IMMUNE      
KEYWDS   4 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.SPEIR,J.STEVENS,E.JOLY,G.W.BUTCHER,I.A.WILSON                     
REVDAT   4   24-JAN-18 1ED3    1       JRNL                                     
REVDAT   3   24-FEB-09 1ED3    1       VERSN                                    
REVDAT   2   01-APR-03 1ED3    1       JRNL                                     
REVDAT   1   28-FEB-01 1ED3    0                                                
JRNL        AUTH   J.A.SPEIR,J.STEVENS,E.JOLY,G.W.BUTCHER,I.A.WILSON            
JRNL        TITL   TWO DIFFERENT, HIGHLY EXPOSED, BULGED STRUCTURES FOR AN      
JRNL        TITL 2 UNUSUALLY LONG PEPTIDE BOUND TO RAT MHC CLASS I RT1-AA.      
JRNL        REF    IMMUNITY                      V.  14    81 2001              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   11163232                                                     
JRNL        DOI    10.1016/S1074-7613(01)00091-7                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.K.BHUYAN,L.L.YOUNG,K.F.LINDAHL,G.W.BUTCHER                 
REMARK   1  TITL   IDENTIFICATION OF THE RAT MATERNALLY TRANSMITTED MINOR       
REMARK   1  TITL 2 HISTOCOMPATIBILITY ANTIGEN                                   
REMARK   1  REF    J.IMMUNOL.                    V. 158  3753 1997              
REMARK   1  REFN                   ISSN 0022-1767                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.STEVENS,K.-H.WIESMULLER,P.J.BARKER,P.WALDEN,G.W.BUCHER,    
REMARK   1  AUTH 2 E.JOLY                                                       
REMARK   1  TITL   EFFICIENT GENERATION OF MAJOR HISTOCOMPATIBILITY COMPLEX     
REMARK   1  TITL 2 CLASS I-PEPTIDE COMPLEXES USING SYNTHETIC PEPTIDE LIBRARIES  
REMARK   1  REF    J.BIOL.CHEM.                  V. 273  2874 1998              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  DOI    10.1074/JBC.273.5.2874                                       
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.STEVENS,K.-H.WIESMULLER,P.WALDEN,E.JOLY                    
REMARK   1  TITL   PEPTIDE LENGTH PREFERENCES FOR RAT AND MOUSE MHC CLASS I     
REMARK   1  TITL 2 MOLECULES USING RANDOM PEPTIDE LIBRARIES                     
REMARK   1  REF    EUR.J.BIOCHEM.                V.  28  1272 1998              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  DOI    10.1002/(SICI)1521-4141(199804)28:04<1272::AID-IMMU1272>3.0. 
REMARK   1  DOI  2 CO;2-E                                                       
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   S.J.POWIS,L.L.YOUNG,E.JOLY,P.J.BARKER,L.RICHARDSON,          
REMARK   1  AUTH 2 R.P.BRANDT,C.J.MELIEF,J.C.HOWARD,G.W.BUTCHER                 
REMARK   1  TITL   THE RAT CIM EFFECT: TAP ALLELE-DEPENDENT CHANGES IN A CLASS  
REMARK   1  TITL 2 I MHC ANCHOR MOTIF AND EVIDENCE AGAINST C-TERMINAL TRIMMING  
REMARK   1  TITL 3 OF PEPTIDES IN THE ER                                        
REMARK   1  REF    IMMUNITY                      V.   4   159 1996              
REMARK   1  REFN                   ISSN 1074-7613                               
REMARK   1  DOI    10.1016/S1074-7613(00)80680-9                                
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   C.J.THORPE,D.S.MOSS,S.J.POWIS,J.C.HOWARD,G.W.BUTCHER,        
REMARK   1  AUTH 2 P.J.TRAVERS                                                  
REMARK   1  TITL   AN ANALYSIS OF THE ANTIGEN BINDING SITE OF RT1-AA SUGGESTS   
REMARK   1  TITL 2 AN ALLELE-SPECIFIC MOTIF                                     
REMARK   1  REF    IMMUNOGENETICS                V.  41   329 1995              
REMARK   1  REFN                   ISSN 0093-7711                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER AS IMPLEMENTED IN X-PLOR AND CNS   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28978                          
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) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2177                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 86.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2414                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 197                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.026                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6380                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.20000                                              
REMARK   3    B22 (A**2) : -6.74000                                             
REMARK   3    B33 (A**2) : 3.54000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.39                            
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) : 0.42                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.47                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.460 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.290 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.430 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.460 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 33.81                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINED, RESTRAINED, RESTRAINED                      
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.040 ; 300                  
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.044 ; 300                  
REMARK   3   GROUP  2  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3   GROUP  3  POSITIONAL            (A) : 0.039 ; 300                  
REMARK   3   GROUP  3  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ED3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000010462.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28978                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
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: 2CLR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MORPHOLINE ETHANSULFONIC ACID       
REMARK 280  (MES), 0.2M AMMONIUM SULFATE, 15-20% MPEG 5000, 0.025M BETA-        
REMARK 280  OCTYL-GLUCOSIDE, 0.5% GLYCEROL, PH 6.5, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 290K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       43.47500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.70500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.36000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.70500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.47500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.36000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THERE ARE TWO HETEROTRIMERIC BIOLOGICAL ASSEMBLIES IN THE    
REMARK 300 ASYMMETRIC UNIT CONSTRUCTED FROM CHAINS A, B, AND C, OR CHAINS D, E, 
REMARK 300 AND F.                                                               
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: 4640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 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: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OG1  THR A   163     OE2  GLU E    69     3655     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A  43   C   -  N   -  CA  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    PRO C   4   C   -  N   -  CA  ANGL. DEV. = -10.2 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    ASP A  29     -128.58     60.31                                   
REMARK 500    ASN A  42      112.13    178.11                                   
REMARK 500    PRO A  43      115.10    -34.48                                   
REMARK 500    GLU A  55      -31.81   -139.54                                   
REMARK 500    ARG A 111      146.74   -176.69                                   
REMARK 500    TYR A 123      -84.40   -124.09                                   
REMARK 500    PRO A 210     -177.79    -63.48                                   
REMARK 500    LEU A 224       36.19    -78.34                                   
REMARK 500    ASP A 227       69.95   -116.58                                   
REMARK 500    HIS B  31      135.79    179.71                                   
REMARK 500    ASN B  48       86.72     41.76                                   
REMARK 500    TRP B  60       -9.12     77.00                                   
REMARK 500    PHE C   3      -72.67    -47.80                                   
REMARK 500    ASP D  29     -130.76     62.48                                   
REMARK 500    ARG D  44      142.53   -176.05                                   
REMARK 500    GLU D  89      179.84    -57.83                                   
REMARK 500    ASP D 106       30.52    -99.08                                   
REMARK 500    LEU D 109      101.63    -53.76                                   
REMARK 500    ARG D 111      145.67   -177.33                                   
REMARK 500    TYR D 123      -83.38   -123.20                                   
REMARK 500    SER D 182      119.33   -160.36                                   
REMARK 500    PRO D 195       -7.52    -53.81                                   
REMARK 500    PRO D 210     -176.56    -65.94                                   
REMARK 500    ASN D 220       42.95     70.16                                   
REMARK 500    HIS E  31      134.29   -176.37                                   
REMARK 500    PRO E  47      -72.68    -61.59                                   
REMARK 500    LEU E  54      151.54    -47.44                                   
REMARK 500    TRP E  60      -13.06     80.74                                   
REMARK 500    SER F   6      177.46    -57.49                                   
REMARK 500    ARG F   8       61.53     32.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1ED3 A    1   275  UNP    P16391   HA12_RAT        25    299             
DBREF  1ED3 B    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  1ED3 C    1    13  UNP    P05504   ATP6_RAT        29     41             
DBREF  1ED3 D    1   275  UNP    P16391   HA12_RAT        25    299             
DBREF  1ED3 E    1    99  UNP    P07151   B2MG_RAT        29    119             
DBREF  1ED3 F    1    13  UNP    P05504   ATP6_RAT        29     41             
SEQRES   1 A  275  GLY SER HIS SER LEU ARG TYR PHE TYR THR ALA VAL SER          
SEQRES   2 A  275  ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  275  TYR VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  275  ALA GLU ASN PRO ARG MET GLU PRO ARG ALA ARG TRP MET          
SEQRES   5 A  275  GLU ARG GLU GLY PRO GLU TYR TRP GLU GLN GLN THR ARG          
SEQRES   6 A  275  ILE ALA LYS GLU TRP GLU GLN ILE TYR ARG VAL ASP LEU          
SEQRES   7 A  275  ARG THR LEU ARG GLY TYR TYR ASN GLN SER GLU GLY GLY          
SEQRES   8 A  275  SER HIS THR ILE GLN GLU MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  275  SER ASP GLY SER LEU LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 A  275  TYR ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  275  LYS THR TRP THR ALA ALA ASP PHE ALA ALA GLN ILE THR          
SEQRES  12 A  275  ARG ASN LYS TRP GLU ARG ALA ARG TYR ALA GLU ARG LEU          
SEQRES  13 A  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU SER          
SEQRES  14 A  275  ARG TYR LEU GLU LEU GLY LYS GLU THR LEU LEU ARG SER          
SEQRES  15 A  275  ASP PRO PRO GLU ALA HIS VAL THR LEU HIS PRO ARG PRO          
SEQRES  16 A  275  GLU GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  275  TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY          
SEQRES  18 A  275  GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG          
SEQRES  19 A  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL          
SEQRES  20 A  275  VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG          
SEQRES  21 A  275  VAL GLU HIS GLU GLY LEU PRO LYS PRO LEU SER GLN ARG          
SEQRES  22 A  275  TRP GLU                                                      
SEQRES   1 B   99  ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 B   99  PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS TYR          
SEQRES   3 B   99  VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU LEU          
SEQRES   4 B   99  LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET SER          
SEQRES   5 B   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU          
SEQRES   6 B   99  ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL TYR          
SEQRES   7 B   99  ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO LYS          
SEQRES   8 B   99  THR VAL THR TRP ASP ARG ASP MET                              
SEQRES   1 C   13  ILE LEU PHE PRO SER SER GLU ARG LEU ILE SER ASN ARG          
SEQRES   1 D  275  GLY SER HIS SER LEU ARG TYR PHE TYR THR ALA VAL SER          
SEQRES   2 D  275  ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 D  275  TYR VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 D  275  ALA GLU ASN PRO ARG MET GLU PRO ARG ALA ARG TRP MET          
SEQRES   5 D  275  GLU ARG GLU GLY PRO GLU TYR TRP GLU GLN GLN THR ARG          
SEQRES   6 D  275  ILE ALA LYS GLU TRP GLU GLN ILE TYR ARG VAL ASP LEU          
SEQRES   7 D  275  ARG THR LEU ARG GLY TYR TYR ASN GLN SER GLU GLY GLY          
SEQRES   8 D  275  SER HIS THR ILE GLN GLU MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 D  275  SER ASP GLY SER LEU LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 D  275  TYR ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 D  275  LYS THR TRP THR ALA ALA ASP PHE ALA ALA GLN ILE THR          
SEQRES  12 D  275  ARG ASN LYS TRP GLU ARG ALA ARG TYR ALA GLU ARG LEU          
SEQRES  13 D  275  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU SER          
SEQRES  14 D  275  ARG TYR LEU GLU LEU GLY LYS GLU THR LEU LEU ARG SER          
SEQRES  15 D  275  ASP PRO PRO GLU ALA HIS VAL THR LEU HIS PRO ARG PRO          
SEQRES  16 D  275  GLU GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 D  275  TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY          
SEQRES  18 D  275  GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG          
SEQRES  19 D  275  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL          
SEQRES  20 D  275  VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG          
SEQRES  21 D  275  VAL GLU HIS GLU GLY LEU PRO LYS PRO LEU SER GLN ARG          
SEQRES  22 D  275  TRP GLU                                                      
SEQRES   1 E   99  ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG HIS          
SEQRES   2 E   99  PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS TYR          
SEQRES   3 E   99  VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU LEU          
SEQRES   4 E   99  LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET SER          
SEQRES   5 E   99  ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE LEU          
SEQRES   6 E   99  ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL TYR          
SEQRES   7 E   99  ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO LYS          
SEQRES   8 E   99  THR VAL THR TRP ASP ARG ASP MET                              
SEQRES   1 F   13  ILE LEU PHE PRO SER SER GLU ARG LEU ILE SER ASN ARG          
FORMUL   7  HOH   *139(H2 O)                                                    
HELIX    1   1 ALA A   49  GLU A   53  5                                   5    
HELIX    2   2 GLY A   56  TYR A   85  1                                  30    
HELIX    3   3 ASP A  137  ALA A  150  1                                  14    
HELIX    4   4 ARG A  151  GLY A  162  1                                  12    
HELIX    5   5 GLY A  162  GLY A  175  1                                  14    
HELIX    6   6 GLY A  175  LEU A  180  1                                   6    
HELIX    7   7 LYS A  253  GLN A  255  5                                   3    
HELIX    8   8 ALA D   49  GLU D   53  5                                   5    
HELIX    9   9 GLY D   56  TYR D   85  1                                  30    
HELIX   10  10 ASP D  137  ALA D  150  1                                  14    
HELIX   11  11 ARG D  151  GLY D  162  1                                  12    
HELIX   12  12 GLY D  162  GLY D  175  1                                  14    
HELIX   13  13 GLY D  175  LEU D  180  1                                   6    
HELIX   14  14 LEU D  224  GLN D  226  5                                   3    
HELIX   15  15 LYS D  253  GLN D  255  5                                   3    
SHEET    1   A 8 GLU A  46  PRO A  47  0                                        
SHEET    2   A 8 THR A  31  ASP A  37 -1  O  ARG A  35   N  GLU A  46           
SHEET    3   A 8 ARG A  21  VAL A  28 -1  N  ALA A  24   O  PHE A  36           
SHEET    4   A 8 SER A   2  VAL A  12 -1  O  ARG A   6   N  TYR A  27           
SHEET    5   A 8 THR A  94  GLY A 104 -1  O  ILE A  95   N  ALA A  11           
SHEET    6   A 8 LEU A 109  TYR A 118 -1  N  LEU A 110   O  ASP A 102           
SHEET    7   A 8 ARG A 121  LEU A 126 -1  O  ARG A 121   N  TYR A 118           
SHEET    8   A 8 TRP A 133  ALA A 135 -1  N  THR A 134   O  ALA A 125           
SHEET    1   B 4 GLU A 186  PRO A 193  0                                        
SHEET    2   B 4 VAL A 199  PHE A 208 -1  N  THR A 200   O  HIS A 192           
SHEET    3   B 4 PHE A 241  VAL A 249 -1  N  PHE A 241   O  PHE A 208           
SHEET    4   B 4 GLU A 229  LEU A 230 -1  N  GLU A 229   O  SER A 246           
SHEET    1   C 4 GLU A 186  PRO A 193  0                                        
SHEET    2   C 4 VAL A 199  PHE A 208 -1  N  THR A 200   O  HIS A 192           
SHEET    3   C 4 PHE A 241  VAL A 249 -1  N  PHE A 241   O  PHE A 208           
SHEET    4   C 4 ARG A 234  PRO A 235 -1  N  ARG A 234   O  GLN A 242           
SHEET    1   D 4 GLU A 222  ASP A 223  0                                        
SHEET    2   D 4 ILE A 213  LEU A 219 -1  N  LEU A 219   O  GLU A 222           
SHEET    3   D 4 TYR A 257  HIS A 263 -1  N  THR A 258   O  GLN A 218           
SHEET    4   D 4 LEU A 270  GLN A 272 -1  N  LEU A 270   O  VAL A 261           
SHEET    1   E 4 GLN B   6  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  N  ASN B  24   O  TYR B  10           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  N  PHE B  62   O  PHE B  30           
SHEET    4   E 4 GLU B  50  MET B  51 -1  N  GLU B  50   O  HIS B  67           
SHEET    1   F 4 GLN B   6  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  N  ASN B  24   O  TYR B  10           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  N  PHE B  62   O  PHE B  30           
SHEET    4   F 4 SER B  55  PHE B  56 -1  O  SER B  55   N  TYR B  63           
SHEET    1   G 4 LYS B  44  LYS B  45  0                                        
SHEET    2   G 4 ILE B  35  LYS B  41 -1  N  LYS B  41   O  LYS B  44           
SHEET    3   G 4 TYR B  78  HIS B  84 -1  O  ALA B  79   N  LEU B  40           
SHEET    4   G 4 LYS B  91  THR B  94 -1  N  LYS B  91   O  VAL B  82           
SHEET    1   H 8 GLU D  46  PRO D  47  0                                        
SHEET    2   H 8 THR D  31  ASP D  37 -1  O  ARG D  35   N  GLU D  46           
SHEET    3   H 8 ARG D  21  VAL D  28 -1  N  ALA D  24   O  PHE D  36           
SHEET    4   H 8 HIS D   3  VAL D  12 -1  O  ARG D   6   N  TYR D  27           
SHEET    5   H 8 THR D  94  VAL D 103 -1  O  ILE D  95   N  ALA D  11           
SHEET    6   H 8 LEU D 109  TYR D 118 -1  N  LEU D 110   O  ASP D 102           
SHEET    7   H 8 ARG D 121  LEU D 126 -1  O  ARG D 121   N  TYR D 118           
SHEET    8   H 8 TRP D 133  ALA D 135 -1  N  THR D 134   O  ALA D 125           
SHEET    1   I 4 GLU D 186  PRO D 193  0                                        
SHEET    2   I 4 VAL D 199  PHE D 208 -1  N  THR D 200   O  HIS D 192           
SHEET    3   I 4 PHE D 241  VAL D 249 -1  N  PHE D 241   O  PHE D 208           
SHEET    4   I 4 MET D 228  LEU D 230 -1  O  GLU D 229   N  SER D 246           
SHEET    1   J 4 GLU D 186  PRO D 193  0                                        
SHEET    2   J 4 VAL D 199  PHE D 208 -1  N  THR D 200   O  HIS D 192           
SHEET    3   J 4 PHE D 241  VAL D 249 -1  N  PHE D 241   O  PHE D 208           
SHEET    4   J 4 ARG D 234  PRO D 235 -1  N  ARG D 234   O  GLN D 242           
SHEET    1   K 3 THR D 214  LEU D 219  0                                        
SHEET    2   K 3 TYR D 257  GLU D 262 -1  N  THR D 258   O  GLN D 218           
SHEET    3   K 3 LEU D 270  GLN D 272 -1  N  LEU D 270   O  VAL D 261           
SHEET    1   L 4 GLN E   6  SER E  11  0                                        
SHEET    2   L 4 ASN E  21  PHE E  30 -1  N  ASN E  24   O  TYR E  10           
SHEET    3   L 4 PHE E  62  PHE E  70 -1  N  PHE E  62   O  PHE E  30           
SHEET    4   L 4 GLU E  50  MET E  51 -1  N  GLU E  50   O  HIS E  67           
SHEET    1   M 4 LYS E  44  LYS E  45  0                                        
SHEET    2   M 4 GLU E  36  LYS E  41 -1  N  LYS E  41   O  LYS E  44           
SHEET    3   M 4 TYR E  78  LYS E  83 -1  O  ALA E  79   N  LEU E  40           
SHEET    4   M 4 LYS E  91  THR E  94 -1  N  LYS E  91   O  VAL E  82           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.04  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.04  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.04  
SSBOND   4 CYS D  101    CYS D  164                          1555   1555  2.04  
SSBOND   5 CYS D  203    CYS D  259                          1555   1555  2.02  
SSBOND   6 CYS E   25    CYS E   80                          1555   1555  2.03  
CISPEP   1 TYR A  209    PRO A  210          0         0.00                     
CISPEP   2 HIS B   31    PRO B   32          0        -0.37                     
CISPEP   3 TYR D  209    PRO D  210          0        -0.11                     
CISPEP   4 HIS E   31    PRO E   32          0         0.00                     
CRYST1   86.950   90.720  117.410  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011501  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011023  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008517        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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