GenomeNet

Database: PDB
Entry: 3C5J
LinkDB: 3C5J
Original site: 3C5J 
HEADER    MEMBRANE PROTEIN                        31-JAN-08   3C5J              
TITLE     CRYSTAL STRUCTURE OF HLA DR52C                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-206;                                       
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MHC CLASS II ANTIGEN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 30-219;                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: ELONGATION FACTOR 1-ALPHA 2;                               
COMPND  14 CHAIN: C;                                                            
COMPND  15 FRAGMENT: UNP RESIDUES 343-355;                                      
COMPND  16 SYNONYM: EF-1-ALPHA-2, ELONGATION FACTOR 1 A-2, EEF1A-2, STATIN S1;  
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DRA, HLA-DRA1;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HLA-DRB3;                                                      
SOURCE  16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: EEF1A2, EEF1AL, STN;                                           
SOURCE  26 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  27 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  30 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    HLA, MHC CLASS II, GLYCOPROTEIN, IMMUNE RESPONSE, MEMBRANE, MHC II,   
KEYWDS   2 TRANSMEMBRANE, ELONGATION FACTOR, GTP-BINDING, METHYLATION,          
KEYWDS   3 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS,   
KEYWDS   4 MEMBRANE PROTEIN                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DAI,J.W.KAPPLER                                                     
REVDAT   7   29-JUL-20 3C5J    1       COMPND REMARK HETNAM LINK                
REVDAT   7 2                   1       SITE                                     
REVDAT   6   25-OCT-17 3C5J    1       REMARK                                   
REVDAT   5   13-JUL-11 3C5J    1       VERSN                                    
REVDAT   4   09-JUN-09 3C5J    1       REVDAT                                   
REVDAT   3   24-FEB-09 3C5J    1       VERSN                                    
REVDAT   2   02-DEC-08 3C5J    1       JRNL                                     
REVDAT   1   05-AUG-08 3C5J    0                                                
JRNL        AUTH   S.DAI,F.CRAWFORD,P.MARRACK,J.W.KAPPLER                       
JRNL        TITL   THE STRUCTURE OF HLA-DR52C: COMPARISON TO OTHER HLA-DRB3     
JRNL        TITL 2 ALLELES.                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105 11893 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18697946                                                     
JRNL        DOI    10.1073/PNAS.0805810105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.69                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2282868.250                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42672                          
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) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2141                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6084                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 351                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3066                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 454                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.37000                                              
REMARK   3    B22 (A**2) : 1.37000                                              
REMARK   3    B33 (A**2) : -2.74000                                             
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) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.21                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.750                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 66.17                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5                         
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : &_1_TOPOLOGY_INFILE_1                          
REMARK   3  TOPOLOGY FILE  2   : &_1_TOPOLOGY_INFILE_2                          
REMARK   3  TOPOLOGY FILE  3   : &_1_TOPOLOGY_INFILE_3                          
REMARK   3  TOPOLOGY FILE  4   : &_1_TOPOLOGY_INFILE_4                          
REMARK   3  TOPOLOGY FILE  5   : &_1_TOPOLOGY_INFILE_5                          
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3C5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046367.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42787                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, PH 7.5, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.45500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       99.68250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       33.22750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       66.45500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       33.22750            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       99.68250            
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: 7400 ANGSTROM**2                          
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17090 ANGSTROM**2                         
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   BIOMT1   2  0.000000 -1.000000  0.000000       83.38000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       83.38000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       99.68250            
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     ASP A   181                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     THR B   106                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
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    GLU A   4      -41.75   -131.58                                   
REMARK 500    TYR A  79       29.50     47.96                                   
REMARK 500    THR A 113      146.50   -171.68                                   
REMARK 500    GLN B  34       -5.86     76.98                                   
REMARK 500    THR B  90      -71.61   -130.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CHAIN C AND CHAIN B ARE FUSED TOGETHER                               
REMARK 999 THROUGH A LINKER ( GGGGSLVPRGSGGGGS ). HOWEVER THIS LINKER IS        
REMARK 999 DISORDERED                                                           
DBREF  3C5J A    1   181  UNP    P01903   2DRA_HUMAN      26    206             
DBREF  3C5J B    1   190  UNP    Q6YJU6   Q6YJU6_HUMAN    30    219             
DBREF  3C5J C    1    13  UNP    Q05639   EF1A2_HUMAN    343    355             
SEQRES   1 A  181  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  181  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  181  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  181  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  181  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 A  181  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  181  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  181  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  181  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  181  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  181  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  181  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  181  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  181  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP              
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU GLU LEU LEU LYS SER          
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE          
SEQRES   3 B  190  LEU GLU ARG TYR PHE HIS ASN GLN GLU GLU PHE VAL 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 VAL ALA GLU SER TRP ASN SER GLN LYS          
SEQRES   6 B  190  ASP LEU LEU GLU GLN LYS ARG GLY GLN VAL ASP ASN TYR          
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL VAL GLU SER PHE THR VAL          
SEQRES   8 B  190  GLN ARG ARG VAL HIS PRO GLN VAL THR VAL TYR PRO ALA          
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS THR GLY VAL VAL          
SEQRES  12 B  190  SER THR GLY LEU ILE HIS 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   13  GLN VAL ILE ILE LEU ASN HIS PRO GLY GLN ILE SER ALA          
MODRES 3C5J ASN A  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3C5J ASN B   19  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 182      14                                                       
HET    NAG  B 191      14                                                       
HET    SO4  B 192       5                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *454(H2 O)                                                    
HELIX    1   1 LEU A   45  PHE A   51  5                                   7    
HELIX    2   2 GLU A   55  SER A   77  1                                  23    
HELIX    3   3 THR B   51  LEU B   53  5                                   3    
HELIX    4   4 GLY B   54  SER B   63  1                                  10    
HELIX    5   5 GLN B   64  ARG B   72  1                                   9    
HELIX    6   6 GLY B   73  TYR B   78  1                                   6    
HELIX    7   7 TYR B   78  GLU B   87  1                                  10    
HELIX    8   8 SER B   88  THR B   90  5                                   3    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42           
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ILE A   8   O  ASP A  25           
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B  17   N  HIS A   5           
SHEET    6   A 8 ARG B  23  HIS B  32 -1  O  LEU B  27   N  GLU B  14           
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  PHE B  40   N  GLU B  28           
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1   B 4 GLU A  88  THR A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109           
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   C 4 GLU A  88  THR A  93  0                                        
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92           
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LYS A 147   N  ILE A 109           
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   D 4 LYS A 126  VAL A 128  0                                        
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  TRP A 121   O  VAL A 128           
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ARG A 164   N  THR A 120           
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  LEU A 174   N  VAL A 165           
SHEET    1   E 4 GLN B  98  ALA B 104  0                                        
SHEET    2   E 4 LEU B 114  PHE B 122 -1  O  SER B 118   N  THR B 100           
SHEET    3   E 4 PHE B 155  LEU B 161 -1  O  VAL B 159   N  CYS B 117           
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1   F 4 GLN B  98  ALA B 104  0                                        
SHEET    2   F 4 LEU B 114  PHE B 122 -1  O  SER B 118   N  THR B 100           
SHEET    3   F 4 PHE B 155  LEU B 161 -1  O  VAL B 159   N  CYS B 117           
SHEET    4   F 4 ILE B 148  HIS B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1   G 4 GLN B 136  GLU B 137  0                                        
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130           
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  TRP B 188   N  TYR B 171           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.67  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.02  
LINK         ND2 ASN A 118                 C1  NAG A 182     1555   1555  1.45  
LINK         ND2 ASN B  19                 C1  NAG B 191     1555   1555  1.45  
CISPEP   1 ASN A   15    PRO A   16          0        -0.17                     
CISPEP   2 THR A  113    PRO A  114          0         0.04                     
CISPEP   3 TYR B  123    PRO B  124          0         0.29                     
CRYST1   83.380   83.380  132.910  90.00  90.00  90.00 P 43 2 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011993  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011993  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007524        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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