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Database: PDB
Entry: 1A6A
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HEADER    COMPLEX (TRANSMEMBRANE/GLYCOPROTEIN)    22-FEB-98   1A6A              
TITLE     THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION: CLIP     
TITLE    2 BOUND TO HLA-DR3                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN;  
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, GAMMA CHAIN;      
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: CLIP FRAGMENT 87 - 101 OF INVARIANT CHAIN                  
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: 9.5.3;                                                    
SOURCE   6 CELL: B-LYMPHOCYTE;                                                  
SOURCE   7 CELLULAR_LOCATION: PLASMA MEMBRANE;                                  
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 CELL_LINE: 9.5.3;                                                    
SOURCE  13 CELL: B-LYMPHOCYTE;                                                  
SOURCE  14 CELLULAR_LOCATION: PLASMA MEMBRANE;                                  
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 CELL_LINE: 9.5.3;                                                    
SOURCE  20 CELL: B-LYMPHOCYTE;                                                  
SOURCE  21 CELLULAR_LOCATION: PLASMA MEMBRANE                                   
KEYWDS    MHC GLYCOPROTEIN, COMPLEX (TRANSMEMBRANE-GLYCOPROTEIN), COMPLEX       
KEYWDS   2 (TRANSMEMBRANE-GLYCOPROTEIN) COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.GHOSH,M.AMAYA,E.MELLINS,D.C.WILEY                                   
REVDAT   4   29-JUL-20 1A6A    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   13-JUL-11 1A6A    1       VERSN                                    
REVDAT   2   24-FEB-09 1A6A    1       VERSN                                    
REVDAT   1   27-MAY-98 1A6A    0                                                
JRNL        AUTH   P.GHOSH,M.AMAYA,E.MELLINS,D.C.WILEY                          
JRNL        TITL   THE STRUCTURE OF AN INTERMEDIATE IN CLASS II MHC MATURATION: 
JRNL        TITL 2 CLIP BOUND TO HLA-DR3.                                       
JRNL        REF    NATURE                        V. 378   457 1995              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   7477400                                                      
JRNL        DOI    10.1038/378457A0                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13095                          
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) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.325                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1323                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.009                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.86                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1442                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3730                       
REMARK   3   BIN FREE R VALUE                    : 0.4440                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.10                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 162                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.036                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3108                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 22                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -10.00000                                            
REMARK   3    B22 (A**2) : -10.00000                                            
REMARK   3    B33 (A**2) : 10.00000                                             
REMARK   3    B12 (A**2) : -10.00000                                            
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) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
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) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.72                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.015                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.310                           
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) : 3.530 ; 3.000                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 5.980 ; 4.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.520 ; 4.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 9.350 ; 6.000                
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  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : PARAM3_MOD.CHO                                 
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH3.CHO                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  RESIDUES 5 - 180 OF THE ALPHA SUBUNIT AND RESIDUES 5 - 191          
REMARK   3  OF THE BETA SUBUNIT ARE CLEARLY VISIBLE IN 2FO-FC ELECTRON          
REMARK   3  DENSITY MAPS.  THREE SMALL BREAKS IN MAIN-CHAIN DENSITY             
REMARK   3  OCCUR IN LOOP REGIONS OF THE BETA 2 DOMAIN (AT BETA 109,            
REMARK   3  172, AND 189).                                                      
REMARK   4                                                                      
REMARK   4 1A6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170445.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JUL-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, ROTAVATA/AGROVATA           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, ROTAVATA           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14428                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1DLH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4K, 100 MM MGCL2, 100 MM         
REMARK 280  ACETATE BUFFER, PH 4.5                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -Y,-X,-Z+1/3                                            
REMARK 290       5555   -X+Y,Y,-Z+2/3                                           
REMARK 290       6555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      106.06667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       53.03333            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       53.03333            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      106.06667            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 33650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  123   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ASN B   19   CG   OD1  ND2                                       
REMARK 480     GLU B   22   CG   CD   OE1  OE2                                  
REMARK 480     ARG B   23   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  105   CG   CD   CE   NZ                                   
REMARK 480     GLN B  107   CG   CD   OE1  NE2                                  
REMARK 480     LEU B  109   CG   CD1  CD2                                       
REMARK 480     GLN B  110   CG   CD   OE1  NE2                                  
REMARK 480     HIS B  111   CG   ND1  CD2  CE1  NE2                             
REMARK 480     GLN B  136   CG   CD   OE1  NE2                                  
REMARK 480     GLU B  138   CG   CD   OE1  OE2                                  
REMARK 480     ARG B  166   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     SER B  167   OG                                                  
REMARK 480     ARG B  189   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG B  191   CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE B  31   C     HIS B  32   N      -0.159                       
REMARK 500    GLU B  87   CD    GLU B  87   OE2     0.083                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE B  31   O   -  C   -  N   ANGL. DEV. = -10.0 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    PHE A  32     -176.31   -171.75                                   
REMARK 500    THR A  90      116.89   -163.29                                   
REMARK 500    LYS A 111       73.71     46.38                                   
REMARK 500    THR A 130       76.22    -66.28                                   
REMARK 500    HIS A 143       43.33     39.60                                   
REMARK 500    LEU A 144     -166.23   -109.78                                   
REMARK 500    LYS A 147      133.60    177.85                                   
REMARK 500    SER A 156     -164.53   -125.40                                   
REMARK 500    THR A 157       -2.32   -140.14                                   
REMARK 500    LEU A 170      102.73   -175.38                                   
REMARK 500    ASP A 171      -73.12    -35.99                                   
REMARK 500    PRO A 173       99.39    -60.90                                   
REMARK 500    GLU A 179      144.41   -170.93                                   
REMARK 500    ASN B  19       70.53     58.37                                   
REMARK 500    GLU B  22      -71.62    -52.47                                   
REMARK 500    GLN B  34       -7.37     71.60                                   
REMARK 500    SER B  88      -71.83    -52.62                                   
REMARK 500    THR B  90      -74.71   -120.03                                   
REMARK 500    HIS B 112       92.20    -61.30                                   
REMARK 500    TYR B 123      130.30   -175.42                                   
REMARK 500    PRO B 124     -172.28    -64.34                                   
REMARK 500    ASN B 134       21.48     49.43                                   
REMARK 500    GLU B 138       89.09    -60.77                                   
REMARK 500    ASP B 152       36.13    -99.97                                   
REMARK 500    SER B 167       67.98    -63.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 150         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1A6A A    5   180  UNP    P01903   2DRA_HUMAN      30    205             
DBREF  1A6A B    5   191  UNP    P01912   HB2B_HUMAN      34    220             
DBREF  1A6A C   87   101  UNP    P04233   HG2A_HUMAN     103    117             
SEQRES   1 A  176  HIS VAL ILE ILE GLN ALA GLU PHE TYR LEU ASN PRO ASP          
SEQRES   2 A  176  GLN SER GLY GLU PHE MET PHE ASP PHE ASP GLY ASP GLU          
SEQRES   3 A  176  ILE PHE HIS VAL ASP MET ALA LYS LYS GLU THR VAL TRP          
SEQRES   4 A  176  ARG LEU GLU GLU PHE GLY ARG PHE ALA SER PHE GLU ALA          
SEQRES   5 A  176  GLN GLY ALA LEU ALA ASN ILE ALA VAL ASP LYS ALA ASN          
SEQRES   6 A  176  LEU GLU ILE MET THR LYS ARG SER ASN TYR THR PRO ILE          
SEQRES   7 A  176  THR ASN VAL PRO PRO GLU VAL THR VAL LEU THR ASN SER          
SEQRES   8 A  176  PRO VAL GLU LEU ARG GLU PRO ASN VAL LEU ILE CYS PHE          
SEQRES   9 A  176  ILE ASP LYS PHE THR PRO PRO VAL VAL ASN VAL THR TRP          
SEQRES  10 A  176  LEU ARG ASN GLY LYS PRO VAL THR THR GLY VAL SER GLU          
SEQRES  11 A  176  THR VAL PHE LEU PRO ARG GLU ASP HIS LEU PHE ARG LYS          
SEQRES  12 A  176  PHE HIS TYR LEU PRO PHE LEU PRO SER THR GLU ASP VAL          
SEQRES  13 A  176  TYR ASP CYS ARG VAL GLU HIS TRP GLY LEU ASP GLU PRO          
SEQRES  14 A  176  LEU LEU LYS HIS TRP GLU PHE                                  
SEQRES   1 B  187  PRO ARG PHE LEU GLU TYR SER THR SER GLU CYS HIS PHE          
SEQRES   2 B  187  PHE ASN GLY THR GLU ARG VAL ARG TYR LEU ASP ARG TYR          
SEQRES   3 B  187  PHE HIS ASN GLN GLU GLU ASN VAL ARG PHE ASP SER ASP          
SEQRES   4 B  187  VAL GLY GLU PHE ARG ALA VAL THR GLU LEU GLY ARG PRO          
SEQRES   5 B  187  ASP ALA GLU TYR TRP ASN SER GLN LYS ASP LEU LEU GLU          
SEQRES   6 B  187  GLN LYS ARG GLY ARG VAL ASP ASN TYR CYS ARG HIS ASN          
SEQRES   7 B  187  TYR GLY VAL VAL GLU SER PHE THR VAL GLN ARG ARG VAL          
SEQRES   8 B  187  HIS PRO LYS VAL THR VAL TYR PRO SER LYS THR GLN PRO          
SEQRES   9 B  187  LEU GLN HIS HIS ASN LEU LEU VAL CYS SER VAL SER GLY          
SEQRES  10 B  187  PHE TYR PRO GLY SER ILE GLU VAL ARG TRP PHE ARG ASN          
SEQRES  11 B  187  GLY GLN GLU GLU LYS THR GLY VAL VAL SER THR GLY LEU          
SEQRES  12 B  187  ILE HIS ASN GLY ASP TRP THR PHE GLN THR LEU VAL MET          
SEQRES  13 B  187  LEU GLU THR VAL PRO ARG SER GLY GLU VAL TYR THR CYS          
SEQRES  14 B  187  GLN VAL GLU HIS PRO SER VAL THR SER PRO LEU THR VAL          
SEQRES  15 B  187  GLU TRP ARG ALA ARG                                          
SEQRES   1 C   15  PRO VAL SER LYS MET ARG MET ALA THR PRO LEU LEU MET          
SEQRES   2 C   15  GLN ALA                                                      
MODRES 1A6A ASN A   78  ASN  GLYCOSYLATION SITE                                 
MODRES 1A6A ASN A  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 181      14                                                       
HET    NAG  A 200      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   6  HOH   *22(H2 O)                                                     
HELIX    1   1 GLU A   46  PHE A   51  1                                   6    
HELIX    2   2 ALA A   56  ARG A   76  1                                  21    
HELIX    3   3 GLU B   52  SER B   63  5                                  12    
HELIX    4   4 LYS B   65  ASN B   77  1                                  13    
HELIX    5   5 CYS B   79  VAL B   86  1                                   8    
SHEET    1   A 4 ILE A   7  LEU A  14  0                                        
SHEET    2   A 4 SER A  19  PHE A  26 -1  N  ASP A  25   O  ILE A   8           
SHEET    3   A 4 ASP A  29  ASP A  35 -1  N  PHE A  32   O  PHE A  24           
SHEET    4   A 4 GLU A  40  TRP A  43 -1  N  VAL A  42   O  HIS A  33           
SHEET    1   B 4 THR A  90  THR A  93  0                                        
SHEET    2   B 4 ASN A 103  ILE A 109 -1  N  PHE A 108   O  THR A  90           
SHEET    3   B 4 LYS A 147  PHE A 153 -1  N  PHE A 153   O  ASN A 103           
SHEET    4   B 4 VAL A 132  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   C 3 ASN A 118  ARG A 123  0                                        
SHEET    2   C 3 VAL A 160  GLU A 166 -1  N  GLU A 166   O  ASN A 118           
SHEET    3   C 3 LEU A 174  GLU A 179 -1  N  TRP A 178   O  TYR A 161           
SHEET    1   D 4 GLU B   9  PHE B  18  0                                        
SHEET    2   D 4 ARG B  23  HIS B  32 -1  N  PHE B  31   O  TYR B  10           
SHEET    3   D 4 GLU B  35  ASP B  41 -1  N  PHE B  40   O  ASP B  28           
SHEET    4   D 4 PHE B  47  ALA B  49 -1  N  ARG B  48   O  ARG B  39           
SHEET    1   E 3 LYS B  98  PRO B 103  0                                        
SHEET    2   E 3 LEU B 115  SER B 120 -1  N  SER B 120   O  LYS B  98           
SHEET    3   E 3 GLN B 156  LEU B 158 -1  N  THR B 157   O  VAL B 119           
SHEET    1   F 3 ILE B 127  ARG B 133  0                                        
SHEET    2   F 3 VAL B 170  HIS B 177 -1  N  GLU B 176   O  GLU B 128           
SHEET    3   F 3 LEU B 184  ARG B 189 -1  N  TRP B 188   O  TYR B 171           
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03  
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.03  
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.05  
LINK         ND2 ASN A  78                 C1  NAG A 181     1555   1555  1.45  
LINK         ND2 ASN A 118                 C1  NAG A 200     1555   1555  1.44  
CISPEP   1 THR A  113    PRO A  114          0        -0.11                     
CISPEP   2 TYR B  123    PRO B  124          0        -0.51                     
CRYST1   78.450   78.450  159.100  90.00  90.00 120.00 P 32 1 2      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012747  0.007359  0.000000        0.00000                         
SCALE2      0.000000  0.014719  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006285        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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