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Database: PDB
Entry: 3LQZ
LinkDB: 3LQZ
Original site: 3LQZ 
HEADER    IMMUNE SYSTEM                           10-FEB-10   3LQZ              
TITLE     CRYSTAL STRUCTURE OF HLA-DP2                                          
CAVEAT     3LQZ    NAG B 190 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DP ALPHA 1 CHAIN; 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HLA-SB ALPHA CHAIN, MHC CLASS II DP3-ALPHA, DP(W3), DP(W4); 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HLA-DP2 BETA CHAIN LINKED WITH DRA PEPTIDE;                
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: MAJOR HISTOCOMPATIBILITY COMPLEX, CLASS II, DP BETA 1;      
COMPND  10 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-DP1A, HLA-DPA1, HLA-DPA1*0103, HLASB;                      
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BTI-TN-5B1-4;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: DAMA-245O6.7-001, HLA-DPB1, HLA-DPB1*0201;                     
SOURCE  14 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 10469;                                      
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BTI-TN-5B1-4                               
KEYWDS    HLA, MHC, IMMUNE, DISULFIDE BOND, GLYCOPROTEIN, IMMUNE RESPONSE,      
KEYWDS   2 MEMBRANE, MHC II, TRANSMEMBRANE, IMMUNE SYSTEM                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DAI                                                                 
REVDAT   5   29-JUL-20 3LQZ    1       CAVEAT COMPND REMARK HET                 
REVDAT   5 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   5 3                   1       ATOM                                     
REVDAT   4   04-SEP-19 3LQZ    1       LINK   CRYST1                            
REVDAT   3   13-JUL-11 3LQZ    1       VERSN                                    
REVDAT   2   05-MAY-10 3LQZ    1       JRNL                                     
REVDAT   1   14-APR-10 3LQZ    0                                                
JRNL        AUTH   S.DAI,G.A.MURPHY,F.CRAWFORD,D.G.MACK,M.T.FALTA,P.MARRACK,    
JRNL        AUTH 2 J.W.KAPPLER,A.P.FONTENOT                                     
JRNL        TITL   CRYSTAL STRUCTURE OF HLA-DP2 AND IMPLICATIONS FOR CHRONIC    
JRNL        TITL 2 BERYLLIUM DISEASE.                                           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107  7425 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20356827                                                     
JRNL        DOI    10.1073/PNAS.1001772107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0040                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11332                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 645                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 902                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 58                           
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3114                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 93.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.94000                                              
REMARK   3    B22 (A**2) : 5.94000                                              
REMARK   3    B33 (A**2) : -8.91000                                             
REMARK   3    B12 (A**2) : 2.97000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.439         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.355         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.178        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3252 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4426 ; 1.490 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   375 ; 6.719 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   179 ;41.920 ;24.246       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   506 ;21.430 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.275 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   467 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2564 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1383 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2177 ; 0.319 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    89 ; 0.182 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    26 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.079 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1930 ; 0.364 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3076 ; 0.672 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1488 ; 0.957 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1350 ; 1.661 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.0400 -37.2810   5.3790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3006 T22:  -0.2296                                     
REMARK   3      T33:  -0.2938 T12:  -0.0666                                     
REMARK   3      T13:  -0.1266 T23:  -0.0450                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8359 L22:   2.3171                                     
REMARK   3      L33:   4.3693 L12:   0.4828                                     
REMARK   3      L13:  -1.6206 L23:  -0.2668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0777 S12:  -0.1584 S13:   0.2297                       
REMARK   3      S21:  -0.0476 S22:  -0.0119 S23:   0.2631                       
REMARK   3      S31:  -0.8404 S32:  -0.5076 S33:  -0.0659                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   189                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.8590 -53.4290   2.2190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4210 T22:  -0.3195                                     
REMARK   3      T33:  -0.2652 T12:  -0.2041                                     
REMARK   3      T13:  -0.1996 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5036 L22:   1.9270                                     
REMARK   3      L33:   4.2617 L12:   0.6654                                     
REMARK   3      L13:  -1.3225 L23:  -0.8028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0501 S12:  -0.1263 S13:  -0.2653                       
REMARK   3      S21:  -0.0530 S22:  -0.0407 S23:  -0.0557                       
REMARK   3      S31:   0.1003 S32:  -0.3247 S33:   0.0908                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   -22        B    -8                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2640 -41.6900 -11.0350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2836 T22:  -0.4628                                     
REMARK   3      T33:  -0.0249 T12:  -0.1997                                     
REMARK   3      T13:   0.0796 T23:   0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6055 L22:  11.0906                                     
REMARK   3      L33:   3.0329 L12:  -3.7948                                     
REMARK   3      L13:   0.2394 L23:  -3.0525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5502 S12:   0.7031 S13:   0.7665                       
REMARK   3      S21:  -1.4606 S22:  -0.9247 S23:  -0.6661                       
REMARK   3      S31:   1.5095 S32:   1.0758 S33:   0.3745                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3LQZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000057620.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : 170; NULL                          
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : ALS; APS                           
REMARK 200  BEAMLINE                       : 8.2.2; 19-ID                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0; 1.0                           
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315; NULL             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12053                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 136.080                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG4000, 300MM SODIUM CHLORIDE,      
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       20.60160            
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       41.20320            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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       41.20320            
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       20.60160            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     LEU B    -7                                                      
REMARK 465     VAL B    -6                                                      
REMARK 465     PRO B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     PRO B   106                                                      
REMARK 465     LEU B   107                                                      
REMARK 465     GLN B   108                                                      
REMARK 465     HIS B   109                                                      
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    ARG A  17      -77.18      0.31                                   
REMARK 500    GLU A  28      -15.12     71.90                                   
REMARK 500    MET A  31      -62.71    -90.07                                   
REMARK 500    GLN A  75      -80.21    -74.57                                   
REMARK 500    ARG A  76       54.29    -62.33                                   
REMARK 500    SER A  77       19.77   -175.50                                   
REMARK 500    ASN A  78       36.52     39.27                                   
REMARK 500    LEU A  99      114.22    -26.68                                   
REMARK 500    PRO A 102      125.30    -36.21                                   
REMARK 500    THR A 129      -68.25   -109.52                                   
REMARK 500    GLU A 134      149.50   -170.74                                   
REMARK 500    PHE A 137       91.90    -59.50                                   
REMARK 500    PRO A 155       94.17    -47.88                                   
REMARK 500    ASP A 159      120.65    179.40                                   
REMARK 500    LEU A 170     -160.00   -103.29                                   
REMARK 500    ASP A 171      -24.69   -169.97                                   
REMARK 500    PHE B  18     -124.30   -112.67                                   
REMARK 500    ARG B  32      -19.32     82.16                                   
REMARK 500    ARG B  37      144.45   -179.71                                   
REMARK 500    PRO B  73      -25.20    -38.55                                   
REMARK 500    ARG B  75      -95.41    -78.75                                   
REMARK 500    THR B  88      -64.12   -104.05                                   
REMARK 500    PRO B 101     -153.82    -64.34                                   
REMARK 500    SER B 102       82.46    135.52                                   
REMARK 500    LYS B 103      -87.07   -126.65                                   
REMARK 500    LYS B 104     -176.38    -59.52                                   
REMARK 500    ASN B 111      121.36   -170.05                                   
REMARK 500    ASP B 119       60.16     70.94                                   
REMARK 500    ASP B 150       31.45   -153.94                                   
REMARK 500    THR B 162       77.04   -152.48                                   
REMARK 500    GLN B 164      -85.49    -91.49                                   
REMARK 500    GLN B 165      -67.31   -152.24                                   
REMARK 500    SER B 177      -73.54    -70.44                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DRA PEPTIDE + LINKER + HLA-DP2 BETA CHAIN                            
DBREF  3LQZ A    1   181  UNP    P20036   DPA1_HUMAN      32    212             
DBREF  3LQZ B    4   189  UNP    Q5EP54   Q5EP54_HUMAN    33    218             
SEQADV 3LQZ ARG B  -22  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ LYS B  -21  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ PHE B  -20  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ HIS B  -19  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ TYR B  -18  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ LEU B  -17  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ PRO B  -16  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ PHE B  -15  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ LEU B  -14  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ PRO B  -13  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ SER B  -12  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ THR B  -11  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B  -10  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B   -9  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ SER B   -8  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ LEU B   -7  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ VAL B   -6  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ PRO B   -5  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ ARG B   -4  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B   -3  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ SER B   -2  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B   -1  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B    0  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B    1  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ GLY B    2  UNP  Q5EP54              SEE REMARK 999                 
SEQADV 3LQZ SER B    3  UNP  Q5EP54              SEE REMARK 999                 
SEQRES   1 A  181  ILE LYS ALA ASP HIS VAL SER THR TYR ALA ALA PHE VAL          
SEQRES   2 A  181  GLN THR HIS ARG PRO THR GLY GLU PHE MET PHE GLU PHE          
SEQRES   3 A  181  ASP GLU ASP GLU MET PHE TYR VAL ASP LEU ASP LYS LYS          
SEQRES   4 A  181  GLU THR VAL TRP HIS LEU GLU GLU PHE GLY GLN ALA PHE          
SEQRES   5 A  181  SER PHE GLU ALA GLN GLY GLY LEU ALA ASN ILE ALA ILE          
SEQRES   6 A  181  LEU ASN ASN ASN LEU ASN THR LEU ILE GLN ARG SER ASN          
SEQRES   7 A  181  HIS THR GLN ALA THR ASN ASP PRO PRO GLU VAL THR VAL          
SEQRES   8 A  181  PHE PRO LYS GLU PRO VAL GLU LEU GLY GLN PRO ASN THR          
SEQRES   9 A  181  LEU ILE CYS HIS ILE ASP LYS PHE PHE PRO PRO VAL LEU          
SEQRES  10 A  181  ASN VAL THR TRP LEU CYS ASN GLY GLU LEU VAL THR GLU          
SEQRES  11 A  181  GLY VAL ALA GLU SER LEU PHE LEU PRO ARG THR ASP TYR          
SEQRES  12 A  181  SER PHE HIS LYS PHE HIS TYR LEU THR PHE VAL PRO SER          
SEQRES  13 A  181  ALA GLU ASP PHE TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  181  LEU ASP GLN PRO LEU LEU LYS HIS TRP GLU ALA GLN              
SEQRES   1 B  212  ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLY          
SEQRES   2 B  212  GLY SER LEU VAL PRO ARG GLY SER GLY GLY GLY GLY SER          
SEQRES   3 B  212  PRO GLU ASN TYR LEU PHE GLN GLY ARG GLN GLU CYS TYR          
SEQRES   4 B  212  ALA PHE ASN GLY THR GLN ARG PHE LEU GLU ARG TYR ILE          
SEQRES   5 B  212  TYR ASN ARG GLU GLU PHE VAL ARG PHE ASP SER ASP VAL          
SEQRES   6 B  212  GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO ASP          
SEQRES   7 B  212  GLU GLU TYR TRP ASN SER GLN LYS ASP ILE LEU GLU GLU          
SEQRES   8 B  212  GLU ARG ALA VAL PRO ASP ARG MET CYS ARG HIS ASN TYR          
SEQRES   9 B  212  GLU LEU GLY GLY PRO MET THR LEU GLN ARG ARG VAL GLN          
SEQRES  10 B  212  PRO ARG VAL ASN VAL SER PRO SER LYS LYS GLY PRO LEU          
SEQRES  11 B  212  GLN HIS HIS ASN LEU LEU VAL CYS HIS VAL THR ASP PHE          
SEQRES  12 B  212  TYR PRO GLY SER ILE GLN VAL ARG TRP PHE LEU ASN GLY          
SEQRES  13 B  212  GLN GLU GLU THR ALA GLY VAL VAL SER THR ASN LEU ILE          
SEQRES  14 B  212  ARG ASN GLY ASP TRP THR PHE GLN ILE LEU VAL MET LEU          
SEQRES  15 B  212  GLU MET THR PRO GLN GLN GLY ASP VAL TYR THR CYS GLN          
SEQRES  16 B  212  VAL GLU HIS THR SER LEU ASP SER PRO VAL THR VAL GLU          
SEQRES  17 B  212  TRP LYS ALA GLN                                              
MODRES 3LQZ ASN B   19  ASN  GLYCOSYLATION SITE                                 
MODRES 3LQZ ASN A  118  ASN  GLYCOSYLATION SITE                                 
MODRES 3LQZ ASN A   78  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 182      14                                                       
HET    NAG  A 183      14                                                       
HET    NAG  B 190      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    3(C8 H15 N O6)                                               
HELIX    1   1 LEU A   45  GLN A   50  1                                   6    
HELIX    2   2 GLU A   55  ARG A   76  1                                  22    
HELIX    3   3 THR B   49  LEU B   51  5                                   3    
HELIX    4   4 GLY B   52  SER B   61  1                                  10    
HELIX    5   5 GLN B   62  VAL B   72  1                                  11    
HELIX    6   6 ARG B   75  LEU B   89  1                                  15    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  TYR A  33   O  VAL A  42           
SHEET    3   A 8 GLY A  20  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    4   A 8 HIS A   5  GLN A  14 -1  N  ALA A  10   O  MET A  23           
SHEET    5   A 8 LEU B   8  ALA B  17 -1  O  CYS B  15   N  SER A   7           
SHEET    6   A 8 GLN B  22  TYR B  30 -1  O  ILE B  29   N  GLN B  10           
SHEET    7   A 8 GLU B  33  ASP B  39 -1  O  GLU B  33   N  TYR B  30           
SHEET    8   A 8 PHE B  45  ALA B  47 -1  O  ARG B  46   N  ARG B  37           
SHEET    1   B 4 GLU A  88  PRO A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  PHE A  92           
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  ALA A 133   O  TYR A 150           
SHEET    1   C 4 GLU A  88  PRO A  93  0                                        
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  PHE A  92           
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  LEU A 151   N  LEU A 105           
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  HIS A 146           
SHEET    1   D 4 GLU A 126  LEU A 127  0                                        
SHEET    2   D 4 ASN A 118  CYS A 123 -1  N  CYS A 123   O  GLU A 126           
SHEET    3   D 4 TYR A 161  GLU A 166 -1  O  GLU A 166   N  ASN A 118           
SHEET    4   D 4 LEU A 174  TRP A 178 -1  O  LYS A 176   N  CYS A 163           
SHEET    1   E 4 VAL B  99  SER B 100  0                                        
SHEET    2   E 4 LEU B 112  PHE B 120 -1  O  VAL B 114   N  SER B 100           
SHEET    3   E 4 PHE B 153  GLU B 160 -1  O  ILE B 155   N  VAL B 117           
SHEET    4   E 4 VAL B 141  SER B 142 -1  N  VAL B 141   O  MET B 158           
SHEET    1   F 4 VAL B  99  SER B 100  0                                        
SHEET    2   F 4 LEU B 112  PHE B 120 -1  O  VAL B 114   N  SER B 100           
SHEET    3   F 4 PHE B 153  GLU B 160 -1  O  ILE B 155   N  VAL B 117           
SHEET    4   F 4 ILE B 146  ARG B 147 -1  N  ILE B 146   O  GLN B 154           
SHEET    1   G 4 GLN B 134  GLU B 135  0                                        
SHEET    2   G 4 ILE B 125  LEU B 131 -1  N  LEU B 131   O  GLN B 134           
SHEET    3   G 4 TYR B 169  HIS B 175 -1  O  GLN B 172   N  ARG B 128           
SHEET    4   G 4 THR B 183  TRP B 186 -1  O  VAL B 184   N  CYS B 171           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.06  
SSBOND   2 CYS B   15    CYS B   77                          1555   1555  2.06  
SSBOND   3 CYS B  115    CYS B  171                          1555   1555  2.05  
LINK         ND2 ASN A  78                 C1  NAG A 183     1555   1555  1.46  
LINK         ND2 ASN A 118                 C1  NAG A 182     1555   1555  1.46  
LINK         ND2 ASN B  19                 C1  NAG B 190     1555   1555  1.45  
CISPEP   1 PHE A  113    PRO A  114          0        -0.90                     
CISPEP   2 TYR B  121    PRO B  122          0        -1.30                     
CRYST1  157.282  157.282   61.805  90.00  90.00 120.00 P 31 2 1      6          
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      0.006362  0.003673  0.000000        0.00000                         
SCALE2      0.000000  0.007347  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016172        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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