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Database: PDB
Entry: 1HDM
LinkDB: 1HDM
Original site: 1HDM 
HEADER    IMMUNE SYSTEM                           09-SEP-98   1HDM              
TITLE     HISTOCOMPATIBILITY ANTIGEN HLA-DM                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (CLASS II HISTOCOMPATIBILITY ANTIGEN, M            
COMPND   3 ALPHA CHAIN);                                                        
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: EXTRACELLULAR DOMAINS;                                     
COMPND   6 SYNONYM: RING6, HLA-DMA;                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTEIN (CLASS II HISTOCOMPATIBILITY ANTIGEN, M            
COMPND  10 BETA CHAIN);                                                         
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: EXTRACELLULAR DOMAINS;                                     
COMPND  13 SYNONYM: RING7, HLA-DMB;                                             
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL: B-LYMPHOCYTE;                                                  
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA HYDEI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7224;                                       
SOURCE   8 OTHER_DETAILS: DROSOPHILA S2 INSECT CELLS;                           
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 CELL: B-LYMPHOCYTE;                                                  
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA HYDEI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7224;                                       
SOURCE  16 OTHER_DETAILS: DROSOPHILA S2 INSECT CELLS                            
KEYWDS    HISTOCOMPATIBILITY PROTEIN, IMMUNE SYSTEM                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.WILEY,L.MOSYAK                                                    
REVDAT   2   24-FEB-09 1HDM    1       VERSN                                    
REVDAT   1   10-SEP-99 1HDM    0                                                
JRNL        AUTH   L.MOSYAK,D.M.ZALLER,D.C.WILEY                                
JRNL        TITL   THE STRUCTURE OF HLA-DM, THE PEPTIDE EXCHANGE                
JRNL        TITL 2 CATALYST THAT LOADS ANTIGEN ONTO CLASS II MHC                
JRNL        TITL 3 MOLECULES DURING ANTIGEN PRESENTATION.                       
JRNL        REF    IMMUNITY                      V.   9   377 1998              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   9768757                                                      
JRNL        DOI    10.1016/S1074-7613(00)80620-2                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 18727                          
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) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1842                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.66                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2795                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3100                       
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 299                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2927                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
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) : 0.37                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.40                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 28.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.69                            
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : PARAM3.CHO                                     
REMARK   3  PARAMETER FILE  3  : NULL                                           
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   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL WAS USED               
REMARK   4                                                                      
REMARK   4 1HDM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007321.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
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   : 18729                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.55000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.21000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.900                              
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: 1DLH                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.4                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       52.56000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.56000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       47.69500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.96500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.96500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       52.56000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       54.96500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       52.56000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.69500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       54.96500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 5300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       95.39000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       52.56000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      109.93000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      105.12000            
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     VAL A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     MET A     8                                                      
REMARK 465     TRP A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     ASP A   197                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     LEU A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     ASN A   201                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LEU B   186                                                      
REMARK 465     SER B   187                                                      
REMARK 465     PRO B   188                                                      
REMARK 465     MET B   189                                                      
REMARK 465     GLN B   190                                                      
REMARK 465     THR B   191                                                      
REMARK 465     LEU B   192                                                      
REMARK 465     LYS B   193                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  38     -122.47     61.98                                   
REMARK 500    GLU A 109      103.33   -164.57                                   
REMARK 500    ASN A 122       16.95     58.97                                   
REMARK 500    PHE A 124      118.44   -169.94                                   
REMARK 500    THR B  99      108.83    -58.01                                   
REMARK 500    PRO B 118     -177.94    -63.27                                   
REMARK 500    TRP B 147       40.14     71.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1HDM A    1   201  UNP    P28067   2DMA_HUMAN      27    227             
DBREF  1HDM B    1   193  UNP    P28068   2DMB_HUMAN      19    211             
SEQADV 1HDM     A       UNP  P28067    ALA    95 SEE REMARK 999                 
SEQADV 1HDM     A       UNP  P28067    PRO    96 SEE REMARK 999                 
SEQADV 1HDM     A       UNP  P28067    GLY   113 SEE REMARK 999                 
SEQADV 1HDM PRO A  179  UNP  P28067    ILE   208 CONFLICT                       
SEQADV 1HDM     B       UNP  P28068    GLU    65 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    PHE    66 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    GLY    67 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    VAL    68 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    LEU    69 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    ARG    91 SEE REMARK 999                 
SEQADV 1HDM     B       UNP  P28068    PRO   158 SEE REMARK 999                 
SEQRES   1 A  201  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU          
SEQRES   2 A  201  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP          
SEQRES   3 A  201  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU          
SEQRES   4 A  201  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG          
SEQRES   5 A  201  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU          
SEQRES   6 A  201  GLN GLY ASP ALA ILE LEU PHE ASP LYS GLU PHE CYS GLU          
SEQRES   7 A  201  TRP MET ILE GLN GLN ILE PRO LYS LEU ASP GLY LYS ILE          
SEQRES   8 A  201  PRO VAL SER ARG GLY PHE PRO ILE ALA GLU VAL PHE THR          
SEQRES   9 A  201  LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN THR LEU VAL          
SEQRES  10 A  201  CYS PHE VAL SER ASN LEU PHE PRO PRO MET LEU THR VAL          
SEQRES  11 A  201  ASN TRP HIS ASP HIS SER VAL PRO VAL GLU GLY PHE GLY          
SEQRES  12 A  201  PRO THR PHE VAL SER ALA VAL ASP GLY LEU SER PHE GLN          
SEQRES  13 A  201  ALA PHE SER TYR LEU ASN PHE THR PRO GLU PRO SER ASP          
SEQRES  14 A  201  ILE PHE SER CYS ILE VAL THR HIS GLU PRO ASP ARG TYR          
SEQRES  15 A  201  THR ALA ILE ALA TYR TRP VAL PRO ARG ASN ALA LEU PRO          
SEQRES  16 A  201  SER ASP LEU LEU GLU ASN                                      
SEQRES   1 B  193  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU          
SEQRES   2 B  193  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE          
SEQRES   3 B  193  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU          
SEQRES   4 B  193  GLU ASN LYS MET ALA PRO CYS ASN SER LEU ALA ASN VAL          
SEQRES   5 B  193  LEU SER GLN HIS LEU ASN GLN LYS ASP THR LEU MET GLN          
SEQRES   6 B  193  ARG LEU ASN GLY LEU GLN ASN CYS ALA THR HIS THR GLN          
SEQRES   7 B  193  PRO PHE TRP GLY SER LEU THR ASN ARG THR ARG PRO PRO          
SEQRES   8 B  193  SER VAL GLN VAL ALA LYS THR THR PRO PHE ASN THR ARG          
SEQRES   9 B  193  GLU PRO VAL MET LEU ALA CYS TYR VAL TRP GLY PHE TYR          
SEQRES  10 B  193  PRO ALA GLU VAL THR ILE THR TRP ARG LYS ASN GLY LYS          
SEQRES  11 B  193  LEU VAL MET HIS SER SER ALA HIS LYS THR ALA GLN PRO          
SEQRES  12 B  193  ASN GLY ASP TRP THR TYR GLN THR LEU SER HIS LEU ALA          
SEQRES  13 B  193  LEU THR PRO SER TYR GLY ASP THR TYR THR CYS VAL VAL          
SEQRES  14 B  193  GLU HIS ILE GLY ALA PRO GLU PRO ILE LEU ARG ASP TRP          
SEQRES  15 B  193  THR PRO GLY LEU SER PRO MET GLN THR LEU LYS                  
HELIX    1   1 PRO A   57  TRP A   62  5                                   6    
HELIX    2   2 ILE A   70  ILE A   84  1                                  15    
HELIX    3   3 SER B   48  ASN B   58  1                                  11    
HELIX    4   4 ASP B   61  ARG B   66  1                                   6    
HELIX    5   5 GLY B   69  GLN B   78  1                                  10    
HELIX    6   6 TRP B   81  THR B   85  1                                   5    
SHEET    1   A 4 PHE A  18  CYS A  24  0                                        
SHEET    2   A 4 VAL A  31  TYR A  37 -1  N  ALA A  36   O  LEU A  19           
SHEET    3   A 4 ASP A  40  ASP A  46 -1  N  PHE A  43   O  GLU A  35           
SHEET    4   A 4 THR A  51  PRO A  54 -1  N  VAL A  53   O  PHE A  44           
SHEET    1   B 4 ILE A  99  THR A 104  0                                        
SHEET    2   B 4 PRO A 113  SER A 121 -1  N  SER A 121   O  ILE A  99           
SHEET    3   B 4 SER A 154  THR A 164 -1  N  PHE A 163   O  ASN A 114           
SHEET    4   B 4 THR A 145  VAL A 150 -1  N  VAL A 150   O  SER A 154           
SHEET    1   C 3 LEU A 128  ASP A 134  0                                        
SHEET    2   C 3 PHE A 171  HIS A 177 -1  N  THR A 176   O  THR A 129           
SHEET    3   C 3 TYR A 182  TRP A 188 -1  N  TRP A 188   O  PHE A 171           
SHEET    1   D 4 LYS B  42  PRO B  45  0                                        
SHEET    2   D 4 ASP B  31  ASP B  37 -1  N  ASP B  37   O  LYS B  42           
SHEET    3   D 4 PRO B  19  PHE B  28 -1  N  PHE B  28   O  ASP B  31           
SHEET    4   D 4 ALA B   5  LEU B  13 -1  N  LEU B  12   O  LYS B  20           
SHEET    1   E 3 SER B  92  LYS B  97  0                                        
SHEET    2   E 3 VAL B 107  PHE B 116 -1  N  TRP B 114   O  SER B  92           
SHEET    3   E 3 TYR B 149  LEU B 157 -1  N  LEU B 157   O  VAL B 107           
SHEET    1   F 3 THR B 122  LYS B 127  0                                        
SHEET    2   F 3 TYR B 165  GLU B 170 -1  N  GLU B 170   O  THR B 122           
SHEET    3   F 3 ILE B 178  TRP B 182 -1  N  TRP B 182   O  TYR B 165           
SSBOND   1 CYS A   24    CYS A   77                          1555   1555  2.04  
SSBOND   2 CYS A  118    CYS A  173                          1555   1555  2.03  
SSBOND   3 CYS B   11    CYS B   73                          1555   1555  2.04  
SSBOND   4 CYS B   25    CYS B   35                          1555   1555  2.03  
SSBOND   5 CYS B  111    CYS B  167                          1555   1555  2.03  
CISPEP   1 SER A   28    PRO A   29          0        -0.15                     
CISPEP   2 PHE A  124    PRO A  125          0         0.26                     
CISPEP   3 GLU A  178    PRO A  179          0        -0.87                     
CISPEP   4 TYR B  117    PRO B  118          0         0.29                     
CRYST1   95.390  109.930  105.120  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010483  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009097  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009513        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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