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Database: PDB
Entry: 1HQR
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Original site: 1HQR 
HEADER    IMMUNE SYSTEM                           19-DEC-00   1HQR              
TITLE     CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE HIGH-                
TITLE    2 AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA-DR ALPHA CHAIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DRA*0101;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HLA-DR BETA CHAIN;                                         
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: DRB5*0101;                                                  
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: MYELIN BASIC PROTEIN;                                      
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: MBP;                                                        
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: STREPTOCOCCAL PYROGENIC EXOTOXIN C;                        
COMPND  18 CHAIN: D;                                                            
COMPND  19 SYNONYM: SPE-C;                                                      
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 MOL_ID: 4;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;                         
SOURCE  22 ORGANISM_TAXID: 1314;                                                
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    SUPERANTIGEN-MHC CLASS II COMPLEX, IMMUNE SYSTEM                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.LI,H.LI,N.DIMASI,P.SCHLIEVERT,R.MARIUZZA                            
REVDAT   4   24-FEB-09 1HQR    1       VERSN                                    
REVDAT   3   01-APR-03 1HQR    1       JRNL                                     
REVDAT   2   04-APR-01 1HQR    1       JRNL                                     
REVDAT   1   03-JAN-01 1HQR    0                                                
JRNL        AUTH   Y.LI,H.LI,N.DIMASI,J.K.MCCORMICK,R.MARTIN,P.SCHUCK,          
JRNL        AUTH 2 P.M.SCHLIEVERT,R.A.MARIUZZA                                  
JRNL        TITL   CRYSTAL STRUCTURE OF A SUPERANTIGEN BOUND TO THE             
JRNL        TITL 2 HIGH-AFFINITY, ZINC-DEPENDENT SITE ON MHC CLASS II.          
JRNL        REF    IMMUNITY                      V.  14    93 2001              
JRNL        REFN                   ISSN 1074-7613                               
JRNL        PMID   11163233                                                     
JRNL        DOI    10.1016/S1074-7613(01)00092-9                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.4                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1943820.410                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11585                          
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) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.288                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.200                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1187                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
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) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.40                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1715                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2730                       
REMARK   3   BIN FREE R VALUE                    : 0.3230                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 12.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 234                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4538                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.45000                                             
REMARK   3    B22 (A**2) : -14.05000                                            
REMARK   3    B33 (A**2) : 1.59000                                              
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) : 0.35                            
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) : 0.47                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
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) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.87                            
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) : 10.110; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 15.290; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.900; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 15.390; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 69.48                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1HQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB012528.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.100                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG 400, SODIUM        
REMARK 280  CACODYLATE, ZNCL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 298.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-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   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+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 -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        0.00000            
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       30.91350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       55.97500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      108.30850            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       30.91350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       55.97500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      108.30850            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       30.91350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       55.97500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      108.30850            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       30.91350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       55.97500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      108.30850            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ILE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     THR A   130                                                      
REMARK 465     GLY B   201                                                      
REMARK 465     ARG B   305                                                      
REMARK 465     THR B   306                                                      
REMARK 465     GLN B   307                                                      
REMARK 465     THR B   308                                                      
REMARK 465     LEU B   309                                                      
REMARK 465     GLN B   310                                                      
REMARK 465     HIS B   311                                                      
REMARK 465     SER B   367                                                      
REMARK 465     GLY B   368                                                      
REMARK 465     ARG C   416                                                      
REMARK 465     THR C   417                                                      
REMARK 465     PRO C   418                                                      
REMARK 465     ASP D   501                                                      
REMARK 465     SER D   502                                                      
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     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  39    CD   CE   NZ                                        
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  67    CD   CE   NZ                                        
REMARK 470     LYS A  75    CE   NZ                                             
REMARK 470     LEU A  92    CG   CD1  CD2                                       
REMARK 470     GLU A  98    CD   OE1  OE2                                       
REMARK 470     THR A 120    OG1  CG2                                            
REMARK 470     ARG A 123    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     THR A 129    O                                                   
REMARK 470     VAL A 132    CG1  CG2                                            
REMARK 470     SER A 133    OG                                                  
REMARK 470     ARG A 164    CZ   NH1  NH2                                       
REMARK 470     GLU A 172    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 176    CD   CE   NZ                                        
REMARK 470     ASP A 181    O    CG   OD1  OD2                                  
REMARK 470     THR B 203    OG1  CG2                                            
REMARK 470     ASN B 219    OD1  ND2                                            
REMARK 470     GLU B 259    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 264    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 269    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 296    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 298    CD   CE   NZ                                        
REMARK 470     HIS B 312    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASN B 313    CG   OD1  ND2                                       
REMARK 470     LEU B 315    CG   CD1  CD2                                       
REMARK 470     VAL B 316    CG1  CG2                                            
REMARK 470     SER B 326    OG                                                  
REMARK 470     GLU B 328    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 335    OG                                                  
REMARK 470     GLN B 336    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 337    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 339    CG   CD   CE   NZ                                   
REMARK 470     GLN B 349    CD   OE1  NE2                                       
REMARK 470     GLU B 362    CG   CD   OE1  OE2                                  
REMARK 470     PRO B 365    CG   CD                                             
REMARK 470     ARG B 366    O    CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLN B 374    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 376    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 380    CG1  CG2                                            
REMARK 470     VAL B 386    CG1  CG2                                            
REMARK 470     GLU B 387    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 389    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 503    N    CA   CB   CG   CD   CE   NZ                    
REMARK 470     LYS D 510    CG   CD   CE   NZ                                   
REMARK 470     SER D 532    OG                                                  
REMARK 470     HIS D 535    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP D 540    CG   OD1  OD2                                       
REMARK 470     LYS D 547    CD   CE   NZ                                        
REMARK 470     SER D 552    OG                                                  
REMARK 470     SER D 560    OG                                                  
REMARK 470     GLN D 561    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 562    CE   NZ                                             
REMARK 470     ASP D 566    CG   OD1  OD2                                       
REMARK 470     LYS D 597    CD   CE   NZ                                        
REMARK 470     SER D 609    OG                                                  
REMARK 470     LYS D 619    CG   CD   CE   NZ                                   
REMARK 470     LYS D 666    CG   CD   CE   NZ                                   
REMARK 470     GLN D 669    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 678    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 689    CG   CD   CE   NZ                                   
REMARK 470     LYS D 708    CG   CD   CE   NZ                                   
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   NH2  ARG A    44     O    GLY B   351              2.15            
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    ASP A  27       15.33     38.32                                   
REMARK 500    GLU A  46      -30.45    -37.64                                   
REMARK 500    GLU A  55       96.27    -59.58                                   
REMARK 500    ARG A  76      -31.56    -38.65                                   
REMARK 500    TYR A  79       68.08     31.16                                   
REMARK 500    PRO A  81     -167.15    -59.09                                   
REMARK 500    THR A  90      137.28    168.86                                   
REMARK 500    LEU A  99      126.04    -20.92                                   
REMARK 500    ARG A 100      -36.40     66.60                                   
REMARK 500    PRO A 102      141.86    -31.42                                   
REMARK 500    PRO A 115       64.92    -61.09                                   
REMARK 500    ASN A 124      -36.64     67.27                                   
REMARK 500    VAL A 132     -176.78    -66.76                                   
REMARK 500    SER A 133      107.45    149.59                                   
REMARK 500    PHE A 137      106.80    -53.44                                   
REMARK 500    GLU A 141      -14.94    -44.46                                   
REMARK 500    LEU A 151      111.32   -160.69                                   
REMARK 500    PRO A 155      150.41    -38.03                                   
REMARK 500    SER A 156     -142.97   -154.80                                   
REMARK 500    THR A 157      -20.38   -152.05                                   
REMARK 500    TRP A 168       47.18    -74.94                                   
REMARK 500    PRO A 173      153.31    -49.47                                   
REMARK 500    TRP A 178      138.13   -174.43                                   
REMARK 500    ASN B 219       71.46     51.30                                   
REMARK 500    ASN B 233      -61.35     67.15                                   
REMARK 500    GLN B 234      -17.51   -166.93                                   
REMARK 500    PHE B 240      123.80   -171.57                                   
REMARK 500    ASP B 243      -16.89    -41.98                                   
REMARK 500    TYR B 260      -70.28    -62.01                                   
REMARK 500    GLN B 264       72.14   -109.09                                   
REMARK 500    LYS B 265      -46.13    -26.80                                   
REMARK 500    ASP B 266      -89.43    -43.11                                   
REMARK 500    PHE B 267      -22.80    -36.72                                   
REMARK 500    ASP B 276      -70.64   -102.14                                   
REMARK 500    TYR B 278      -60.21   -123.29                                   
REMARK 500    GLU B 287      -62.66    -19.06                                   
REMARK 500    THR B 290      -71.65   -129.10                                   
REMARK 500    PRO B 297     -134.22    -63.22                                   
REMARK 500    LYS B 298      107.96    165.40                                   
REMARK 500    TYR B 323      138.01   -171.22                                   
REMARK 500    PRO B 324     -175.84    -69.82                                   
REMARK 500    ASN B 334      -45.65     59.62                                   
REMARK 500    SER B 335       25.57   -169.04                                   
REMARK 500    GLU B 338       91.72    -62.15                                   
REMARK 500    ALA B 340      135.26   -174.94                                   
REMARK 500    VAL B 370      102.84   -161.11                                   
REMARK 500    PRO B 378        0.05    -47.23                                   
REMARK 500    VAL B 380      106.71   -160.67                                   
REMARK 500    LYS D 504       65.96     60.16                                   
REMARK 500    ASP D 505      125.58    -36.64                                   
REMARK 500    ASP D 526       79.37     60.78                                   
REMARK 500    THR D 533     -141.78   -120.94                                   
REMARK 500    THR D 534      -84.33   -103.88                                   
REMARK 500    THR D 536     -166.36   -101.15                                   
REMARK 500    LEU D 537      108.20    175.02                                   
REMARK 500    THR D 541       36.54    -74.44                                   
REMARK 500    TYR D 544      -65.21   -124.83                                   
REMARK 500    ASP D 548        9.03     83.19                                   
REMARK 500    TYR D 550     -170.87   -175.07                                   
REMARK 500    SER D 560       -8.06    -58.14                                   
REMARK 500    ARG D 565      154.36    -25.99                                   
REMARK 500    ASP D 566      -11.14     67.33                                   
REMARK 500    PHE D 572       85.13   -160.23                                   
REMARK 500    ASN D 579       39.84     36.39                                   
REMARK 500    SER D 580       55.41   -104.93                                   
REMARK 500    HIS D 581     -115.62     71.49                                   
REMARK 500    SER D 609       98.19    -52.57                                   
REMARK 500    LEU D 616       47.59   -104.33                                   
REMARK 500    ASN D 618       42.29     35.53                                   
REMARK 500    ILE D 646       -9.94    -56.05                                   
REMARK 500    TYR D 653      120.42    -20.18                                   
REMARK 500    ASP D 671      129.29    -37.12                                   
REMARK 500    ASN D 677     -148.72     57.38                                   
REMARK 500    ASP D 690       -4.50    -51.51                                   
REMARK 500    ASN D 691       24.00     41.79                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 709  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 281   ND1                                                    
REMARK 620 2 HIS D 667   NE2 114.8                                              
REMARK 620 3 ASP D 703   OD2 114.2 102.4                                        
REMARK 620 4 HIS D 701   NE2  98.3 132.1  93.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 709                  
DBREF  1HQR A    1   181  UNP    P01903   2DRA_HUMAN      26    206             
DBREF  1HQR B  201   390  UNP    Q29703   Q29703_HUMAN    30    219             
DBREF  1HQR C  406   418  UNP    P02686   MBP_HUMAN      114    126             
DBREF  1HQR D  501   708  UNP    P13380   SPEC_STRPY      28    235             
SEQRES   1 A  181  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  181  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  181  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  181  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  181  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL          
SEQRES   6 A  181  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  181  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  181  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  181  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  181  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  181  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  181  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  181  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  181  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP              
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU GLN GLN ASP LYS TYR          
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG PHE          
SEQRES   3 B  190  LEU HIS ARG ASP ILE TYR ASN GLN GLU GLU ASP LEU ARG          
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU          
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS          
SEQRES   6 B  190  ASP PHE LEU GLU ASP ARG ARG ALA ALA VAL ASP THR TYR          
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL          
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO ALA          
SEQRES   9 B  190  ARG THR GLN THR LEU GLN HIS HIS ASN LEU LEU VAL CYS          
SEQRES  10 B  190  SER VAL ASN GLY PHE TYR PRO GLY SER ILE GLU VAL ARG          
SEQRES  11 B  190  TRP PHE ARG ASN SER GLN GLU GLU LYS ALA GLY VAL VAL          
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN          
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU          
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER          
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA                              
SEQRES   1 C   13  VAL HIS PHE PHE LYS ASN ILE VAL THR PRO ARG THR PRO          
SEQRES   1 D  208  ASP SER LYS LYS ASP ILE SER ASN VAL LYS SER ASP LEU          
SEQRES   2 D  208  LEU TYR ALA TYR THR ILE THR PRO TYR ASP TYR LYS ASP          
SEQRES   3 D  208  CYS ARG VAL ASN PHE SER THR THR HIS THR LEU ASN ILE          
SEQRES   4 D  208  ASP THR GLN LYS TYR ARG GLY LYS ASP TYR TYR ILE SER          
SEQRES   5 D  208  SER GLU MET SER TYR GLU ALA SER GLN LYS PHE LYS ARG          
SEQRES   6 D  208  ASP ASP HIS VAL ASP VAL PHE GLY LEU PHE TYR ILE LEU          
SEQRES   7 D  208  ASN SER HIS THR GLY GLU TYR ILE TYR GLY GLY ILE THR          
SEQRES   8 D  208  PRO ALA GLN ASN ASN LYS VAL ASN HIS LYS LEU LEU GLY          
SEQRES   9 D  208  ASN LEU PHE ILE SER GLY GLU SER GLN GLN ASN LEU ASN          
SEQRES  10 D  208  ASN LYS ILE ILE LEU GLU LYS ASP ILE VAL THR PHE GLN          
SEQRES  11 D  208  GLU ILE ASP PHE LYS ILE ARG LYS TYR LEU MET ASP ASN          
SEQRES  12 D  208  TYR LYS ILE TYR ASP ALA THR SER PRO TYR VAL SER GLY          
SEQRES  13 D  208  ARG ILE GLU ILE GLY THR LYS ASP GLY LYS HIS GLU GLN          
SEQRES  14 D  208  ILE ASP LEU PHE ASP SER PRO ASN GLU GLY THR ARG SER          
SEQRES  15 D  208  ASP ILE PHE ALA LYS TYR LYS ASP ASN ARG ILE ILE ASN          
SEQRES  16 D  208  MET LYS ASN PHE SER HIS PHE ASP ILE TYR LEU GLU LYS          
HET     ZN  D 709       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    ZN 2+                                                        
HELIX    1   1 GLU A   47  PHE A   51  5                                   5    
HELIX    2   2 GLU A   55  SER A   77  1                                  23    
HELIX    3   3 THR B  251  LEU B  253  5                                   3    
HELIX    4   4 GLY B  254  ASN B  262  1                                   9    
HELIX    5   5 GLN B  264  ALA B  273  1                                  10    
HELIX    6   6 ALA B  273  TYR B  278  1                                   6    
HELIX    7   7 TYR B  278  GLU B  287  1                                  10    
HELIX    8   8 SER B  288  THR B  290  5                                   3    
HELIX    9   9 ASP D  505  THR D  518  1                                  14    
HELIX   10  10 SER D  556  GLN D  561  1                                   6    
HELIX   11  11 PHE D  629  LYS D  645  1                                  17    
HELIX   12  12 THR D  680  PHE D  685  1                                   6    
HELIX   13  13 ALA D  686  ASN D  691  5                                   6    
SHEET    1   A 8 GLU A  40  TRP A  43  0                                        
SHEET    2   A 8 ASP A  29  ASP A  35 -1  O  HIS A  33   N  VAL A  42           
SHEET    3   A 8 SER A  19  PHE A  26 -1  O  PHE A  22   N  VAL A  34           
SHEET    4   A 8 HIS A   5  ASN A  15 -1  O  ILE A   8   N  ASP A  25           
SHEET    5   A 8 PHE B 207  PHE B 218 -1  N  PHE B 207   O  ASN A  15           
SHEET    6   A 8 ARG B 223  TYR B 232 -1  N  ARG B 223   O  PHE B 218           
SHEET    7   A 8 GLU B 235  ASP B 241 -1  N  GLU B 235   O  TYR B 232           
SHEET    8   A 8 TYR B 247  ALA B 249 -1  O  ARG B 248   N  ARG B 239           
SHEET    1   B 4 VAL A  91  THR A  93  0                                        
SHEET    2   B 4 ASN A 103  PHE A 112 -1  N  ILE A 106   O  LEU A  92           
SHEET    3   B 4 PHE A 145  PHE A 153 -1  N  PHE A 145   O  PHE A 112           
SHEET    4   B 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   C 4 LYS A 126  VAL A 128  0                                        
SHEET    2   C 4 ASN A 118  ARG A 123 -1  O  TRP A 121   N  VAL A 128           
SHEET    3   C 4 TYR A 161  GLU A 166 -1  O  ASP A 162   N  LEU A 122           
SHEET    4   C 4 HIS A 177  TRP A 178 -1  O  TRP A 178   N  TYR A 161           
SHEET    1   D 4 VAL B 299  TYR B 302  0                                        
SHEET    2   D 4 ASN B 313  PHE B 322 -1  N  VAL B 316   O  TYR B 302           
SHEET    3   D 4 PHE B 355  THR B 363 -1  N  PHE B 355   O  PHE B 322           
SHEET    4   D 4 VAL B 342  SER B 344 -1  O  VAL B 343   N  MET B 360           
SHEET    1   E 4 VAL B 299  TYR B 302  0                                        
SHEET    2   E 4 ASN B 313  PHE B 322 -1  N  VAL B 316   O  TYR B 302           
SHEET    3   E 4 PHE B 355  THR B 363 -1  N  PHE B 355   O  PHE B 322           
SHEET    4   E 4 ILE B 348  GLN B 349 -1  N  ILE B 348   O  GLN B 356           
SHEET    1   F 4 GLN B 336  GLU B 337  0                                        
SHEET    2   F 4 GLU B 328  ARG B 333 -1  N  ARG B 333   O  GLN B 336           
SHEET    3   F 4 VAL B 370  HIS B 377 -1  O  THR B 372   N  PHE B 332           
SHEET    4   F 4 VAL B 380  ARG B 389 -1  N  VAL B 380   O  HIS B 377           
SHEET    1   G 6 TYR D 585  TYR D 587  0                                        
SHEET    2   G 6 ILE D 551  GLU D 554  1  O  SER D 552   N  ILE D 586           
SHEET    3   G 6 ASN D 538  ASP D 540 -1  N  ILE D 539   O  ILE D 551           
SHEET    4   G 6 CYS D 527  VAL D 529 -1  O  ARG D 528   N  ASP D 540           
SHEET    5   G 6 HIS D 568  VAL D 571 -1  O  VAL D 569   N  CYS D 527           
SHEET    6   G 6 ILE D 590  PRO D 592 -1  O  THR D 591   N  ASP D 570           
SHEET    1   H 2 HIS D 600  LYS D 601  0                                        
SHEET    2   H 2 ILE D 621  LEU D 622 -1  O  LEU D 622   N  HIS D 600           
SHEET    1   I 3 GLY D 604  SER D 609  0                                        
SHEET    2   I 3 PHE D 699  GLU D 707  1  O  PHE D 702   N  ASN D 605           
SHEET    3   I 3 SER D 655  THR D 662 -1  O  SER D 655   N  GLU D 707           
SHEET    1   J 2 ILE D 626  THR D 628  0                                        
SHEET    2   J 2 ILE D 693  ASN D 695 -1  O  ILE D 694   N  VAL D 627           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03  
SSBOND   2 CYS B  215    CYS B  279                          1555   1555  2.03  
SSBOND   3 CYS B  317    CYS B  373                          1555   1555  2.03  
LINK        ZN    ZN D 709                 ND1 HIS B 281     1555   1555  1.93  
LINK        ZN    ZN D 709                 NE2 HIS D 667     1555   1555  2.12  
LINK        ZN    ZN D 709                 OD2 ASP D 703     1555   1555  1.92  
LINK        ZN    ZN D 709                 NE2 HIS D 701     1555   1555  2.14  
CISPEP   1 ASN A   15    PRO A   16          0        -0.10                     
CISPEP   2 TYR B  323    PRO B  324          0         0.56                     
SITE     1 AC1  4 HIS B 281  HIS D 667  HIS D 701  ASP D 703                    
CRYST1   61.827  111.950  216.617  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016174  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008933  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004616        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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