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Database: PDB
Entry: 1KJM
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HEADER    IMMUNE SYSTEM                           04-DEC-01   1KJM              
TITLE     TAP-A-ASSOCIATED RAT MHC CLASS I MOLECULE                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RT1 CLASS I HISTOCOMPATIBILITY ANTIGEN, AA ALPHA CHAIN,    
COMPND   3 HEAVY CHAIN;                                                         
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAIN, RESIDUES 25-300, NUMBERED 1-276, PLUS
COMPND   6 C-TERMINAL HIS TAG;                                                  
COMPND   7 SYNONYM: MHC CLASS I RT1-AA HEAVY CHAIN;                             
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: BETA-2-MICROGLOBULIN;                                      
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: RESIDUES 21-119, NUMBERED 1-99;                            
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: B6 PEPTIDE;                                                
COMPND  16 CHAIN: P;                                                            
COMPND  17 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 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   9 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  10 ORGANISM_TAXID: 10116;                                               
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE  
SOURCE  16 OF THE PEPTIDE WAS DERIVED FROM BIOCHEMICAL BINDING DATA.            
KEYWDS    PEPTIDE-MHC COMPLEX, HETERODIMER, EXTRACELLULAR DOMAIN, IMMUNE SYSTEM 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.G.RUDOLPH,J.STEVENS,J.A.SPEIR,J.TROWSDALE,G.W.BUTCHER,E.JOLY,       
AUTHOR   2 I.A.WILSON                                                           
REVDAT   4   13-JUL-11 1KJM    1       VERSN                                    
REVDAT   3   24-FEB-09 1KJM    1       VERSN                                    
REVDAT   2   13-JAN-04 1KJM    1       JRNL                                     
REVDAT   1   18-DEC-02 1KJM    0                                                
JRNL        AUTH   M.G.RUDOLPH,J.STEVENS,J.A.SPEIR,J.TROWSDALE,G.W.BUTCHER,     
JRNL        AUTH 2 E.JOLY,I.A.WILSON                                            
JRNL        TITL   CRYSTAL STRUCTURES OF TWO RAT MHC CLASS IA (RT1-A) MOLECULES 
JRNL        TITL 2 THAT ARE ASSOCIATED DIFFERENTIALLY WITH PEPTIDE TRANSPORTER  
JRNL        TITL 3 ALLELES TAP-A AND TAP-B.                                     
JRNL        REF    J.MOL.BIOL.                   V. 324   975 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12470953                                                     
JRNL        DOI    10.1016/S0022-2836(02)01095-1                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.A.SPEIR,J.S.STEVENS,E.JOLY,G.W.BUTCHER,I.A.WILSON          
REMARK   1  TITL   TWO DIFFERENT, HIGHLY EXPOSED, BULGED STRUCTURES FOR AN      
REMARK   1  TITL 2 UNUSUALLY LONG PEPTIDE BOUND TO RAT MHC CLASS I RT1-AA       
REMARK   1  REF    IMMUNITY                      V.  14    81 2001              
REMARK   1  REFN                   ISSN 1074-7613                               
REMARK   1  DOI    10.1016/S1074-7613(01)00091-7                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5                                             
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 21660                          
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) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2156                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.41                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1280                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 135                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3149                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 144                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 32.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.12000                                             
REMARK   3    B22 (A**2) : 5.96000                                              
REMARK   3    B33 (A**2) : -4.85000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.440         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.271         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.307         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.910        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.910                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3244 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2813 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4409 ; 1.463 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6547 ; 0.783 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   382 ; 3.077 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   583 ;18.483 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   453 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3628 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   697 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   759 ; 0.249 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3091 ; 0.252 ; 0.300       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   260 ; 0.176 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     7 ; 0.217 ; 0.500       
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):     8 ; 0.192 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):    53 ; 0.249 ; 0.300       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.751 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1925 ; 0.319 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3108 ; 0.614 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1319 ; 1.126 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1301 ; 1.978 ; 4.500       
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  : 4                                          
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   180                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6160   5.1390  14.5530              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2293 T22:   0.0435                                     
REMARK   3      T33:   0.2770 T12:   0.0490                                     
REMARK   3      T13:  -0.0056 T23:  -0.0133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0406 L22:   1.6267                                     
REMARK   3      L33:   3.0459 L12:  -0.2830                                     
REMARK   3      L13:   0.6330 L23:   0.2399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1070 S12:   0.0330 S13:  -0.1069                       
REMARK   3      S21:  -0.0178 S22:  -0.0900 S23:   0.1852                       
REMARK   3      S31:   0.0213 S32:  -0.3833 S33:  -0.0169                       
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 :   P     1        P     9                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3830   1.6990  14.0960              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2586 T22:   0.0773                                     
REMARK   3      T33:   0.2182 T12:   0.0624                                     
REMARK   3      T13:  -0.0228 T23:  -0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3180 L22:   1.0391                                     
REMARK   3      L33:   1.9241 L12:   2.9577                                     
REMARK   3      L13:   0.1175 L23:   0.8108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2763 S12:   0.1025 S13:  -0.0623                       
REMARK   3      S21:   0.0142 S22:  -0.1753 S23:   0.1163                       
REMARK   3      S31:   0.2604 S32:  -0.1397 S33:  -0.1010                       
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 :   A   181        A   277                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6120  30.8030  10.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3931 T22:   0.2550                                     
REMARK   3      T33:   0.5303 T12:   0.0227                                     
REMARK   3      T13:   0.0086 T23:  -0.0806                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4569 L22:   8.9264                                     
REMARK   3      L33:   3.1667 L12:  -1.5530                                     
REMARK   3      L13:  -0.8358 L23:   2.9840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1872 S12:   0.2815 S13:  -0.1878                       
REMARK   3      S21:  -0.3005 S22:   0.0288 S23:  -0.5335                       
REMARK   3      S31:   0.1991 S32:   0.2590 S33:  -0.2160                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    99                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3460  16.5690  27.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4982 T22:   0.4537                                     
REMARK   3      T33:   0.7382 T12:   0.0219                                     
REMARK   3      T13:   0.0630 T23:  -0.1715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.8844 L22:   2.5497                                     
REMARK   3      L33:   5.3520 L12:  -2.8088                                     
REMARK   3      L13:  -2.4991 L23:  -0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2084 S12:  -0.3097 S13:   0.0118                       
REMARK   3      S21:   0.2942 S22:  -0.2557 S23:   0.8340                       
REMARK   3      S31:   0.0537 S32:  -0.7229 S33:   0.0474                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1KJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB015019.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : CYCLINDRICALLY BENT TRIANGULAR     
REMARK 200                                   SI(111) ASYMMETRIC CUT,            
REMARK 200                                   HORIZONTAL MONOCHROMATOR           
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   : 22313                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 2.760                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.38                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.860                              
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: PDB ENTRY 1ED3 MOLECULE 1                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 1% GLYCEROL, 0.1 M TRIS/   
REMARK 280  HCL, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       55.02450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.78300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       55.02450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.78300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 361  LIES ON A SPECIAL POSITION.                          
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 A   278                                                      
REMARK 465     GLU A   279                                                      
REMARK 465     HIS A   280                                                      
REMARK 465     HIS A   281                                                      
REMARK 465     HIS A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     HIS A   285                                                      
REMARK 465     MET B     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 260    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLU B    89     N    LYS B    91              2.18            
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    ASP A 116   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A 129   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    PRO B  90   C   -  N   -  CA  ANGL. DEV. =   9.2 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    PRO A  15      125.50    -35.20                                   
REMARK 500    ASP A  29     -125.81     66.33                                   
REMARK 500    SER A  38        5.95    -69.37                                   
REMARK 500    TRP A  51        1.08    -64.22                                   
REMARK 500    GLU A  53       27.11    -76.91                                   
REMARK 500    ASP A 122      152.85    -45.77                                   
REMARK 500    TYR A 123      -78.57   -134.08                                   
REMARK 500    ASP A 137     -159.82   -138.25                                   
REMARK 500    ASP A 198     -169.80   -100.33                                   
REMARK 500    PRO A 210      -94.38    -56.27                                   
REMARK 500    ALA A 211      -19.58   -161.60                                   
REMARK 500    ASP A 223      159.02    -43.62                                   
REMARK 500    LEU A 224       73.33   -156.80                                   
REMARK 500    ASP A 227       49.79   -142.27                                   
REMARK 500    GLU B  16       96.12   -164.82                                   
REMARK 500    ASN B  17       85.60    -48.38                                   
REMARK 500    LYS B  19       90.44    -37.72                                   
REMARK 500    ASN B  21     -142.22   -144.63                                   
REMARK 500    HIS B  31      132.64   -178.29                                   
REMARK 500    ASN B  42       10.32     50.99                                   
REMARK 500    SER B  52     -175.16    -63.34                                   
REMARK 500    LEU B  54      156.83    -39.48                                   
REMARK 500    PRO B  90       35.96    -38.25                                   
REMARK 500    LYS B  91      104.42    -21.27                                   
REMARK 500    ASP B  98      -16.31   -150.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 398        DISTANCE =  5.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 286                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ED3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1KJV   RELATED DB: PDB                                   
DBREF  1KJM A    1   276  UNP    P16391   HA12_RAT        25    300             
DBREF  1KJM B    1    99  UNP    P07151   B2MG_RAT        21    119             
DBREF  1KJM P    1     9  PDB    1KJM     1KJM             1      9             
SEQADV 1KJM LEU A  277  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM GLU A  262  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  263  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  280  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  281  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  282  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  283  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM HIS A  284  UNP  P16391              EXPRESSION TAG                 
SEQADV 1KJM MET B    0  UNP  P07151              INITIATING MET                 
SEQRES   1 A  285  GLY SER HIS SER LEU ARG TYR PHE TYR THR ALA VAL SER          
SEQRES   2 A  285  ARG PRO GLY LEU GLY GLU PRO ARG PHE ILE ALA VAL GLY          
SEQRES   3 A  285  TYR VAL ASP ASP THR GLU PHE VAL ARG PHE ASP SER ASP          
SEQRES   4 A  285  ALA GLU ASN PRO ARG MET GLU PRO ARG ALA ARG TRP MET          
SEQRES   5 A  285  GLU ARG GLU GLY PRO GLU TYR TRP GLU GLN GLN THR ARG          
SEQRES   6 A  285  ILE ALA LYS GLU TRP GLU GLN ILE TYR ARG VAL ASP LEU          
SEQRES   7 A  285  ARG THR LEU ARG GLY TYR TYR ASN GLN SER GLU GLY GLY          
SEQRES   8 A  285  SER HIS THR ILE GLN GLU MET TYR GLY CYS ASP VAL GLY          
SEQRES   9 A  285  SER ASP GLY SER LEU LEU ARG GLY TYR ARG GLN ASP ALA          
SEQRES  10 A  285  TYR ASP GLY ARG ASP TYR ILE ALA LEU ASN GLU ASP LEU          
SEQRES  11 A  285  LYS THR TRP THR ALA ALA ASP PHE ALA ALA GLN ILE THR          
SEQRES  12 A  285  ARG ASN LYS TRP GLU ARG ALA ARG TYR ALA GLU ARG LEU          
SEQRES  13 A  285  ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU SER          
SEQRES  14 A  285  ARG TYR LEU GLU LEU GLY LYS GLU THR LEU LEU ARG SER          
SEQRES  15 A  285  ASP PRO PRO GLU ALA HIS VAL THR LEU HIS PRO ARG PRO          
SEQRES  16 A  285  GLU GLY ASP VAL THR LEU ARG CYS TRP ALA LEU GLY PHE          
SEQRES  17 A  285  TYR PRO ALA ASP ILE THR LEU THR TRP GLN LEU ASN GLY          
SEQRES  18 A  285  GLU ASP LEU THR GLN ASP MET GLU LEU VAL GLU THR ARG          
SEQRES  19 A  285  PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA SER VAL          
SEQRES  20 A  285  VAL VAL PRO LEU GLY LYS GLU GLN ASN TYR THR CYS ARG          
SEQRES  21 A  285  VAL GLU HIS GLU GLY LEU PRO LYS PRO LEU SER GLN ARG          
SEQRES  22 A  285  TRP GLU PRO LEU LEU GLU HIS HIS HIS HIS HIS HIS              
SEQRES   1 B  100  MET ILE GLN LYS THR PRO GLN ILE GLN VAL TYR SER ARG          
SEQRES   2 B  100  HIS PRO PRO GLU ASN GLY LYS PRO ASN PHE LEU ASN CYS          
SEQRES   3 B  100  TYR VAL SER GLN PHE HIS PRO PRO GLN ILE GLU ILE GLU          
SEQRES   4 B  100  LEU LEU LYS ASN GLY LYS LYS ILE PRO ASN ILE GLU MET          
SEQRES   5 B  100  SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR ILE          
SEQRES   6 B  100  LEU ALA HIS THR GLU PHE THR PRO THR GLU THR ASP VAL          
SEQRES   7 B  100  TYR ALA CYS ARG VAL LYS HIS VAL THR LEU LYS GLU PRO          
SEQRES   8 B  100  LYS THR VAL THR TRP ASP ARG ASP MET                          
SEQRES   1 P    9  ALA GLN PHE SER ALA SER ALA SER ARG                          
HET    SO4  A 286       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  HOH   *144(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 PHE A  138  ALA A  150  1                                  13    
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    
SHEET    1   A 8 GLU A  46  PRO A  47  0                                        
SHEET    2   A 8 THR A  31  ASP A  37 -1  N  ARG A  35   O  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  N  ARG A   6   O  TYR A  27           
SHEET    5   A 8 THR A  94  GLY A 104 -1  O  VAL A 103   N  HIS A   3           
SHEET    6   A 8 LEU A 109  TYR A 118 -1  O  LEU A 110   N  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  O  THR A 134   N  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  O  LEU A 206   N  GLU A 186           
SHEET    3   B 4 PHE A 241  VAL A 249 -1  O  VAL A 249   N  VAL A 199           
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  O  LEU A 206   N  GLU A 186           
SHEET    3   C 4 PHE A 241  VAL A 249 -1  O  VAL A 249   N  VAL A 199           
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 THR A 214  LEU A 219 -1  N  LEU A 219   O  GLU A 222           
SHEET    3   D 4 TYR A 257  GLU A 262 -1  O  THR A 258   N  GLN A 218           
SHEET    4   D 4 LEU A 270  GLN A 272 -1  O  LEU A 270   N  VAL A 261           
SHEET    1   E 4 VAL B   9  SER B  11  0                                        
SHEET    2   E 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   E 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   E 4 GLU B  50  MET B  51 -1  N  GLU B  50   O  HIS B  67           
SHEET    1   F 4 VAL B   9  SER B  11  0                                        
SHEET    2   F 4 ASN B  21  PHE B  30 -1  O  ASN B  24   N  TYR B  10           
SHEET    3   F 4 PHE B  62  PHE B  70 -1  O  THR B  68   N  LEU B  23           
SHEET    4   F 4 SER B  55  PHE B  56 -1  N  SER B  55   O  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  ARG B  81   N  GLU B  38           
SHEET    4   G 4 THR B  92  THR B  94 -1  O  VAL B  93   N  CYS B  80           
SSBOND   1 CYS A  101    CYS A  164                          1555   1555  2.04  
SSBOND   2 CYS A  203    CYS A  259                          1555   1555  2.02  
SSBOND   3 CYS B   25    CYS B   80                          1555   1555  2.04  
CISPEP   1 TYR A  209    PRO A  210          0         2.37                     
CISPEP   2 HIS B   31    PRO B   32          0         1.11                     
SITE     1 AC1  5 ASN A  86  LYS A 131  ARG A 157  HOH A 329                    
SITE     2 AC1  5 HOH A 362                                                     
CRYST1  110.049  109.566   45.300  90.00  90.00  90.00 P 21 21 2     4          
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      0.009087  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009127  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022075        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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