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Database: PDB
Entry: 1K8I
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Original site: 1K8I 
HEADER    IMMUNE SYSTEM                           24-OCT-01   1K8I              
TITLE     CRYSTAL STRUCTURE OF MOUSE H2-DM                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MHC CLASS II H2-M ALPHA CHAIN;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MHC CLASS II H2-M BETA 2 CHAIN;                            
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: H2-DM;                                                         
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: H2-DM;                                                         
SOURCE  16 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  17 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE  19 EXPRESSION_SYSTEM_CELL_LINE: HIGH-FIVE;                              
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    MHC, IMMUNE SYSTEM                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.H.FREMONT,F.CRAWFORD,P.MARRACK,W.HENDRICKSON,J.KAPPLER              
REVDAT   5   29-JUL-20 1K8I    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   13-JUL-11 1K8I    1       VERSN                                    
REVDAT   3   24-FEB-09 1K8I    1       VERSN                                    
REVDAT   2   01-APR-03 1K8I    1       JRNL                                     
REVDAT   1   05-DEC-01 1K8I    0                                                
JRNL        AUTH   D.H.FREMONT,F.CRAWFORD,P.MARRACK,W.A.HENDRICKSON,J.KAPPLER   
JRNL        TITL   CRYSTAL STRUCTURE OF MOUSE H2-M.                             
JRNL        REF    IMMUNITY                      V.   9   385 1998              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   9768758                                                      
JRNL        DOI    10.1016/S1074-7613(00)80621-4                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0100                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 13711                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 690                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.21                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.60                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1225                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3340                       
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 6.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 78                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.038                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2934                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 74.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.46000                                             
REMARK   3    B22 (A**2) : -1.46000                                             
REMARK   3    B33 (A**2) : 2.92000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.37                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.67                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.79                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.260                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM3_MOD.CHO                                 
REMARK   3  PARAMETER FILE  3  : PARAMCSDX.MISC                                 
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1K8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-NOV-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000014692.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5                                
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13711                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.560                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.710                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR,MIR                       
REMARK 200 SOFTWARE USED: AMORE, X-PLOR                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LITHIUM SULFATE, 0.1M MES, PH      
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       71.35000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       71.35000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       38.45000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       71.35000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       71.35000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       38.45000            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       71.35000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       71.35000            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       38.45000            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       71.35000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       71.35000            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       38.45000            
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: 5700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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     ALA A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     PHE A     6                                                      
REMARK 465     TRP A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     GLY B   191                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 167   C   -  N   -  CA  ANGL. DEV. =   9.7 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    ILE A  25     -107.71     36.02                                   
REMARK 500    GLU A  36      -19.53     75.95                                   
REMARK 500    ALA A  57      -68.71     11.01                                   
REMARK 500    GLN A  63      -32.91     69.67                                   
REMARK 500    PRO A 126       77.14    -69.48                                   
REMARK 500    SER A 136      -21.12     70.64                                   
REMARK 500    PRO A 167      -30.98    -34.52                                   
REMARK 500    LEU A 170       89.70   -162.51                                   
REMARK 500    GLU A 178       59.34     38.04                                   
REMARK 500    ILE A 179      -72.58     65.87                                   
REMARK 500    TYR A 182      115.66     89.97                                   
REMARK 500    PRO A 190       99.89    -66.63                                   
REMARK 500    ALA B  15      -62.35     76.45                                   
REMARK 500    ASN B  28     -156.75     57.36                                   
REMARK 500    LEU B  32      -76.20    -96.67                                   
REMARK 500    CYS B  45     -139.73   -133.95                                   
REMARK 500    GLU B  46       84.01    -11.26                                   
REMARK 500    GLU B  63       45.15    -77.99                                   
REMARK 500    GLN B  83      -64.25    -29.80                                   
REMARK 500    PHE B 106     -115.76    -82.20                                   
REMARK 500    THR B 108      160.31     99.25                                   
REMARK 500    PRO B 123     -169.59    -72.75                                   
REMARK 500    HIS B 140      100.26   -163.44                                   
REMARK 500    GLU B 144     -104.61   -104.41                                   
REMARK 500    LYS B 145     -151.49    173.80                                   
REMARK 500    ALA B 147      100.35      9.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1K8I A    1   191  UNP    P28078   2DMA_MOUSE      30    220             
DBREF  1K8I B    1   191  UNP    Q31099   Q31099_MOUSE    20    210             
SEQRES   1 A  191  ALA SER THR PRO VAL PHE TRP ASP ASP PRO GLN ASN HIS          
SEQRES   2 A  191  THR PHE ARG HIS THR LEU PHE CYS GLN ASP GLY ILE PRO          
SEQRES   3 A  191  ASN ILE GLY LEU SER GLU THR TYR ASP GLU ASP GLU LEU          
SEQRES   4 A  191  PHE SER PHE ASP PHE SER GLN ASN THR ARG VAL PRO ARG          
SEQRES   5 A  191  LEU PRO ASP PHE ALA GLU TRP ALA GLN GLY GLN GLY ASP          
SEQRES   6 A  191  ALA SER ALA ILE ALA PHE ASP LYS SER PHE CYS GLU MET          
SEQRES   7 A  191  LEU MET ARG GLU VAL SER PRO LYS LEU GLU GLY GLN ILE          
SEQRES   8 A  191  PRO VAL SER ARG GLY LEU PRO VAL ALA GLU VAL PHE THR          
SEQRES   9 A  191  LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN THR LEU VAL          
SEQRES  10 A  191  CYS PHE ILE SER ASN LEU PHE PRO PRO THR LEU THR VAL          
SEQRES  11 A  191  ASN TRP GLN LEU HIS SER ALA PRO VAL GLU GLY ALA SER          
SEQRES  12 A  191  PRO THR SER ILE SER ALA VAL ASP GLY LEU THR PHE GLN          
SEQRES  13 A  191  ALA PHE SER TYR LEU ASN PHE THR PRO GLU PRO PHE ASP          
SEQRES  14 A  191  LEU TYR SER CYS THR VAL THR HIS GLU ILE ASP ARG TYR          
SEQRES  15 A  191  THR ALA ILE ALA TYR TRP VAL PRO GLN                          
SEQRES   1 B  191  GLY PHE VAL ALA HIS VAL GLU SER THR CYS VAL LEU ASN          
SEQRES   2 B  191  ASP ALA GLY THR PRO GLN ASP PHE THR TYR CYS VAL SER          
SEQRES   3 B  191  PHE ASN LYS ASP LEU LEU ALA CYS TRP ASP PRO ASP VAL          
SEQRES   4 B  191  GLY LYS ILE VAL PRO CYS GLU PHE GLY VAL LEU SER ARG          
SEQRES   5 B  191  LEU ALA GLU ILE ILE SER ASN ILE LEU ASN GLU GLN GLU          
SEQRES   6 B  191  SER LEU ILE HIS ARG LEU GLN ASN GLY LEU GLN ASP CYS          
SEQRES   7 B  191  ALA THR HIS THR GLN PRO PHE TRP ASP VAL LEU THR HIS          
SEQRES   8 B  191  ARG THR ARG ALA PRO SER VAL ARG VAL ALA GLN THR THR          
SEQRES   9 B  191  PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS TYR          
SEQRES  10 B  191  VAL TRP GLY PHE TYR PRO ALA ASP VAL THR ILE THR TRP          
SEQRES  11 B  191  MET LYS ASN GLY GLN LEU VAL PRO SER HIS SER ASN LYS          
SEQRES  12 B  191  GLU LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR GLN          
SEQRES  13 B  191  THR VAL SER TYR LEU ALA LEU THR PRO SER TYR GLY ASP          
SEQRES  14 B  191  VAL TYR THR CYS VAL VAL GLN HIS SER GLY THR SER GLU          
SEQRES  15 B  191  PRO ILE ARG GLY ASP TRP THR PRO GLY                          
MODRES 1K8I ASN A   12  ASN  GLYCOSYLATION SITE                                 
MODRES 1K8I ASN A  162  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 192      14                                                       
HET    NAG  A 193      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   3  NAG    2(C8 H15 N O6)                                               
HELIX    1   1 ALA A   57  GLY A   62  1                                   6    
HELIX    2   2 ASP A   65  GLU A   82  1                                  18    
HELIX    3   3 GLU A   82  GLU A   88  1                                   7    
HELIX    4   4 LEU B   50  GLU B   63  1                                  14    
HELIX    5   5 GLN B   64  GLY B   74  1                                  11    
HELIX    6   6 GLY B   74  HIS B   91  1                                  18    
SHEET    1   A 6 THR A  48  PRO A  51  0                                        
SHEET    2   A 6 ASP A  37  ASP A  43 -1  N  ASP A  43   O  THR A  48           
SHEET    3   A 6 ILE A  28  TYR A  34 -1  N  GLU A  32   O  LEU A  39           
SHEET    4   A 6 ASN A  12  GLN A  22 -1  N  PHE A  20   O  GLY A  29           
SHEET    5   A 6 VAL B   3  ASN B  13 -1  O  CYS B  10   N  PHE A  15           
SHEET    6   A 6 PRO B  18  PHE B  21 -1  O  GLN B  19   N  VAL B  11           
SHEET    1   B 8 THR A  48  PRO A  51  0                                        
SHEET    2   B 8 ASP A  37  ASP A  43 -1  N  ASP A  43   O  THR A  48           
SHEET    3   B 8 ILE A  28  TYR A  34 -1  N  GLU A  32   O  LEU A  39           
SHEET    4   B 8 ASN A  12  GLN A  22 -1  N  PHE A  20   O  GLY A  29           
SHEET    5   B 8 VAL B   3  ASN B  13 -1  O  CYS B  10   N  PHE A  15           
SHEET    6   B 8 CYS B  24  PHE B  27 -1  O  CYS B  24   N  GLU B   7           
SHEET    7   B 8 ALA B  33  ASP B  36 -1  O  ALA B  33   N  VAL B  25           
SHEET    8   B 8 LYS B  41  PRO B  44 -1  O  VAL B  43   N  CYS B  34           
SHEET    1   C 4 VAL A  99  THR A 104  0                                        
SHEET    2   C 4 ASN A 114  LEU A 123 -1  O  SER A 121   N  VAL A  99           
SHEET    3   C 4 THR A 154  PHE A 163 -1  O  LEU A 161   N  LEU A 116           
SHEET    4   C 4 SER A 146  VAL A 150 -1  N  VAL A 150   O  THR A 154           
SHEET    1   D 4 ALA A 137  VAL A 139  0                                        
SHEET    2   D 4 LEU A 128  LEU A 134 -1  N  LEU A 134   O  ALA A 137           
SHEET    3   D 4 TYR A 171  HIS A 177 -1  O  THR A 174   N  ASN A 131           
SHEET    4   D 4 THR A 183  TRP A 188 -1  O  ALA A 184   N  VAL A 175           
SHEET    1   E 4 SER B  97  THR B 103  0                                        
SHEET    2   E 4 VAL B 112  PHE B 121 -1  O  ALA B 115   N  ALA B 101           
SHEET    3   E 4 TYR B 155  LEU B 163 -1  O  LEU B 161   N  LEU B 114           
SHEET    4   E 4 GLN B 148  PRO B 149 -1  N  GLN B 148   O  GLN B 156           
SHEET    1   F 4 GLN B 135  LEU B 136  0                                        
SHEET    2   F 4 VAL B 126  LYS B 132 -1  N  LYS B 132   O  GLN B 135           
SHEET    3   F 4 TYR B 171  HIS B 177 -1  O  VAL B 174   N  THR B 129           
SHEET    4   F 4 THR B 180  TRP B 188 -1  O  TRP B 188   N  TYR B 171           
SSBOND   1 CYS A   21    CYS A   76                          1555   1555  2.03  
SSBOND   2 CYS A  118    CYS A  173                          1555   1555  2.01  
SSBOND   3 CYS B   10    CYS B   78                          1555   1555  2.03  
SSBOND   4 CYS B   24    CYS B   34                          1555   1555  2.04  
SSBOND   5 CYS B  116    CYS B  173                          1555   1555  2.03  
LINK         ND2 ASN A  12                 C1  NAG A 192     1555   1555  1.46  
LINK         ND2 ASN A 162                 C1  NAG A 193     1555   1555  1.46  
CISPEP   1 PHE A  124    PRO A  125          0         0.10                     
CISPEP   2 TYR B  122    PRO B  123          0        -0.07                     
CRYST1  142.700  142.700   76.900  90.00  90.00  90.00 I 4           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007008  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007008  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013004        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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