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Database: PDB
Entry: 2BC4
LinkDB: 2BC4
Original site: 2BC4 
HEADER    IMMUNE SYSTEM                           18-OCT-05   2BC4              
TITLE     CRYSTAL STRUCTURE OF HLA-DM                                           
CAVEAT     2BC4    NAG E 1 HAS WRONG CHIRALITY AT ATOM C1 NAG F 1 HAS WRONG     
CAVEAT   2 2BC4    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;   
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: MHC CLASS II ANTIGEN DMA;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;    
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 SYNONYM: MHC CLASS II ANTIGEN DMB;                                   
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HLA-DMA, DMA, RING6;                                           
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRMHA-3;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: HLA-DMB, DMB, RING7;                                           
SOURCE  16 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  17 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;          
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRMHA-3                                   
KEYWDS    MHC CLASS II, IMMUNE SYSTEM                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.J.NICHOLSON,B.MORADI,N.P.SETH,X.XING,G.D.CUNY,R.L.STEIN,            
AUTHOR   2 K.W.WUCHERPFENNIG                                                    
REVDAT   4   29-JUL-20 2BC4    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   18-OCT-17 2BC4    1       REMARK                                   
REVDAT   2   24-FEB-09 2BC4    1       VERSN                                    
REVDAT   1   23-MAY-06 2BC4    0                                                
JRNL        AUTH   M.J.NICHOLSON,B.MORADI,N.P.SETH,X.XING,G.D.CUNY,R.L.STEIN,   
JRNL        AUTH 2 K.W.WUCHERPFENNIG                                            
JRNL        TITL   SMALL MOLECULES THAT ENHANCE THE CATALYTIC EFFICIENCY OF     
JRNL        TITL 2 HLA-DM.                                                      
JRNL        REF    J.IMMUNOL.                    V. 176  4208 2006              
JRNL        REFN                   ISSN 0022-1767                               
JRNL        PMID   16547258                                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 54814                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1477                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6143                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 104                                     
REMARK   3   SOLVENT ATOMS            : 420                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.13700                                             
REMARK   3    B22 (A**2) : 4.40400                                              
REMARK   3    B33 (A**2) : -2.26700                                             
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) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.413                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 41.12                                                
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  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : CNS_TOPPAR:ION.PARAM                           
REMARK   3  PARAMETER FILE  5  : CNS_TOPPAR:CARBOHYDRATE.PARAM                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : CNS_TOPPAR:PROTEIN.TOP                         
REMARK   3  TOPOLOGY FILE  2   : CNS_TOPPAR:DNA-RNA.TOP                         
REMARK   3  TOPOLOGY FILE  3   : CNS_TOPPAR:WATER.TOP                           
REMARK   3  TOPOLOGY FILE  4   : CNS_TOPPAR:ION.TOP                             
REMARK   3  TOPOLOGY FILE  5   : CNS_TOPPAR:CARBOHYDRATE.TOP                    
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2BC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034923.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9195                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59797                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.31000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.020                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HDM (ALANINE SUBSTITUTION)                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULFATE, 0.3M AMMONIUM      
REMARK 280  SULFATE, 0.1M SODIUM CITRATE BUFFER, PH 5.4, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       49.03400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.10350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.10350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.03400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.21000            
REMARK 290   SMTRY3   4  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 300 REMARK: THE BIOLOGICAL UNIT IS A HETERODIMER. THERE ARE 2            
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A & B AND CHAINS C & 
REMARK 300 D).                                                                  
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: 6510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
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 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       98.06800            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -54.21000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       55.10350            
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     LEU A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     ASP A   204                                                      
REMARK 465     TYR A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     ASP A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     ASP A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B   194                                                      
REMARK 465     PRO B   195                                                      
REMARK 465     MET B   196                                                      
REMARK 465     GLN B   197                                                      
REMARK 465     THR B   198                                                      
REMARK 465     LEU B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     PRO B   202                                                      
REMARK 465     PRO B   203                                                      
REMARK 465     THR B   204                                                      
REMARK 465     PRO B   205                                                      
REMARK 465     PRO B   206                                                      
REMARK 465     PRO B   207                                                      
REMARK 465     GLU B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     GLU B   210                                                      
REMARK 465     THR B   211                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     MET C     8                                                      
REMARK 465     TRP C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     ASP C   207                                                      
REMARK 465     ASP C   208                                                      
REMARK 465     ASP C   209                                                      
REMARK 465     ASP C   210                                                      
REMARK 465     LYS C   211                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     LYS D   200                                                      
REMARK 465     LYS D   201                                                      
REMARK 465     PRO D   202                                                      
REMARK 465     PRO D   203                                                      
REMARK 465     THR D   204                                                      
REMARK 465     PRO D   205                                                      
REMARK 465     PRO D   206                                                      
REMARK 465     PRO D   207                                                      
REMARK 465     GLU D   208                                                      
REMARK 465     PRO D   209                                                      
REMARK 465     GLU D   210                                                      
REMARK 465     THR D   211                                                      
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    ARG A  98   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A  98   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.3 DEGREES          
REMARK 500    ARG A  98   NE  -  CZ  -  NH2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG C  98   CD  -  NE  -  CZ  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG C  98   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG C  98   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  38     -123.78     53.07                                   
REMARK 500    ASP A  91      107.44    -58.28                                   
REMARK 500    GLU A 181      128.71    -25.58                                   
REMARK 500    ILE A 182       47.02     80.08                                   
REMARK 500    GLU B  39       31.91    -76.98                                   
REMARK 500    GLU B  40      -18.93   -160.54                                   
REMARK 500    PRO B 124     -173.02    -66.18                                   
REMARK 500    SER B 167       18.58   -143.14                                   
REMARK 500    TYR B 168      -26.81     61.12                                   
REMARK 500    LEU C  13      109.83     64.99                                   
REMARK 500    ASP C  38     -124.31     54.84                                   
REMARK 500    GLU C  65      128.17    -32.56                                   
REMARK 500    ALA C  69      -62.61    -23.62                                   
REMARK 500    GLU C 181      128.69    -24.78                                   
REMARK 500    ILE C 182       47.15     79.89                                   
REMARK 500    GLU D  39       21.67    -72.83                                   
REMARK 500    GLU D  40      -13.67   -145.10                                   
REMARK 500    PRO D 124     -174.50    -66.08                                   
REMARK 500    HIS D 141       35.18    -83.30                                   
REMARK 500    SER D 167       31.89   -143.37                                   
REMARK 500    TYR D 168      -14.20     45.44                                   
REMARK 500    ILE D 179       -9.57    -58.20                                   
REMARK 500    PRO D 184      154.77    -47.08                                   
REMARK 500    SER D 194      -45.19    -29.09                                   
REMARK 500    THR D 198     -157.38   -146.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2BC4 A    1   203  GB     18765715 NP_006111       27    229             
DBREF  2BC4 C    1   203  GB     18765715 NP_006111       27    229             
DBREF  2BC4 B    1   200  GB     4504399  NP_002109       19    218             
DBREF  2BC4 D    1   200  GB     4504399  NP_002109       19    218             
SEQADV 2BC4 ASP A  204  GB   18765715            FLAG TAG                       
SEQADV 2BC4 TYR A  205  GB   18765715            FLAG TAG                       
SEQADV 2BC4 LYS A  206  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP A  207  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP A  208  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP A  209  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP A  210  GB   18765715            FLAG TAG                       
SEQADV 2BC4 LYS A  211  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP C  204  GB   18765715            FLAG TAG                       
SEQADV 2BC4 TYR C  205  GB   18765715            FLAG TAG                       
SEQADV 2BC4 LYS C  206  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP C  207  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP C  208  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP C  209  GB   18765715            FLAG TAG                       
SEQADV 2BC4 ASP C  210  GB   18765715            FLAG TAG                       
SEQADV 2BC4 LYS C  211  GB   18765715            FLAG TAG                       
SEQADV 2BC4 LYS B  201  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  202  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  203  GB   4504399             KT3 TAG                        
SEQADV 2BC4 THR B  204  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  205  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  206  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  207  GB   4504399             KT3 TAG                        
SEQADV 2BC4 GLU B  208  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO B  209  GB   4504399             KT3 TAG                        
SEQADV 2BC4 GLU B  210  GB   4504399             KT3 TAG                        
SEQADV 2BC4 THR B  211  GB   4504399             KT3 TAG                        
SEQADV 2BC4 LYS D  201  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  202  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  203  GB   4504399             KT3 TAG                        
SEQADV 2BC4 THR D  204  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  205  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  206  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  207  GB   4504399             KT3 TAG                        
SEQADV 2BC4 GLU D  208  GB   4504399             KT3 TAG                        
SEQADV 2BC4 PRO D  209  GB   4504399             KT3 TAG                        
SEQADV 2BC4 GLU D  210  GB   4504399             KT3 TAG                        
SEQADV 2BC4 THR D  211  GB   4504399             KT3 TAG                        
SEQRES   1 A  211  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU          
SEQRES   2 A  211  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP          
SEQRES   3 A  211  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU          
SEQRES   4 A  211  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG          
SEQRES   5 A  211  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU          
SEQRES   6 A  211  GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE          
SEQRES   7 A  211  CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP          
SEQRES   8 A  211  GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU          
SEQRES   9 A  211  VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN          
SEQRES  10 A  211  THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET          
SEQRES  11 A  211  LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU          
SEQRES  12 A  211  GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU          
SEQRES  13 A  211  SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO GLU          
SEQRES  14 A  211  PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE          
SEQRES  15 A  211  ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN          
SEQRES  16 A  211  ALA LEU PRO SER ASP LEU LEU GLU ASP TYR LYS ASP ASP          
SEQRES  17 A  211  ASP ASP LYS                                                  
SEQRES   1 B  211  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU          
SEQRES   2 B  211  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE          
SEQRES   3 B  211  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU          
SEQRES   4 B  211  GLU ASN LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN          
SEQRES   5 B  211  SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS          
SEQRES   6 B  211  ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN          
SEQRES   7 B  211  CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR          
SEQRES   8 B  211  ASN ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR          
SEQRES   9 B  211  THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS          
SEQRES  10 B  211  TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR          
SEQRES  11 B  211  TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER          
SEQRES  12 B  211  ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR          
SEQRES  13 B  211  GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY          
SEQRES  14 B  211  ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO          
SEQRES  15 B  211  GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU SER PRO          
SEQRES  16 B  211  MET GLN THR LEU LYS LYS PRO PRO THR PRO PRO PRO GLU          
SEQRES  17 B  211  PRO GLU THR                                                  
SEQRES   1 C  211  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU          
SEQRES   2 C  211  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP          
SEQRES   3 C  211  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU          
SEQRES   4 C  211  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG          
SEQRES   5 C  211  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU          
SEQRES   6 C  211  GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE          
SEQRES   7 C  211  CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP          
SEQRES   8 C  211  GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU          
SEQRES   9 C  211  VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN          
SEQRES  10 C  211  THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET          
SEQRES  11 C  211  LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU          
SEQRES  12 C  211  GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU          
SEQRES  13 C  211  SER PHE GLN ALA PHE SER TYR LEU ASN PHE THR PRO GLU          
SEQRES  14 C  211  PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE          
SEQRES  15 C  211  ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN          
SEQRES  16 C  211  ALA LEU PRO SER ASP LEU LEU GLU ASP TYR LYS ASP ASP          
SEQRES  17 C  211  ASP ASP LYS                                                  
SEQRES   1 D  211  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU          
SEQRES   2 D  211  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE          
SEQRES   3 D  211  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU          
SEQRES   4 D  211  GLU ASN LYS MET ALA PRO CYS GLU PHE GLY VAL LEU ASN          
SEQRES   5 D  211  SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS          
SEQRES   6 D  211  ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN          
SEQRES   7 D  211  CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR          
SEQRES   8 D  211  ASN ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR          
SEQRES   9 D  211  THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS          
SEQRES  10 D  211  TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR          
SEQRES  11 D  211  TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER          
SEQRES  12 D  211  ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR          
SEQRES  13 D  211  GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY          
SEQRES  14 D  211  ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO          
SEQRES  15 D  211  GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU SER PRO          
SEQRES  16 D  211  MET GLN THR LEU LYS LYS PRO PRO THR PRO PRO PRO GLU          
SEQRES  17 D  211  PRO GLU THR                                                  
MODRES 2BC4 ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 2BC4 ASN C   15  ASN  GLYCOSYLATION SITE                                 
HET    NAG  E   1      14                                                       
HET    NDG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    BMA  E   4      11                                                       
HET    NAG  F   1      14                                                       
HET    NDG  F   2      14                                                       
HET    BMA  F   3      11                                                       
HET    BMA  F   4      11                                                       
HET     CL  A 503       1                                                       
HET     CL  B 501       1                                                       
HET     CL  C 504       1                                                       
HET     CL  D 502       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM      CL CHLORIDE ION                                                     
FORMUL   5  NAG    2(C8 H15 N O6)                                               
FORMUL   5  NDG    2(C8 H15 N O6)                                               
FORMUL   5  BMA    4(C6 H12 O6)                                                 
FORMUL   7   CL    4(CL 1-)                                                     
FORMUL  11  HOH   *420(H2 O)                                                    
HELIX    1   1 LEU A   56  GLN A   64  5                                   9    
HELIX    2   2 ASP A   68  GLN A   85  1                                  18    
HELIX    3   3 LEU B   51  GLN B   64  1                                  14    
HELIX    4   4 LYS B   65  ASN B   74  1                                  10    
HELIX    5   5 ASN B   74  ASN B   92  1                                  19    
HELIX    6   6 LEU C   56  GLU C   58  5                                   3    
HELIX    7   7 PHE C   59  GLN C   64  1                                   6    
HELIX    8   8 ASP C   68  ILE C   86  1                                  19    
HELIX    9   9 LEU C  202  LYS C  206  5                                   5    
HELIX   10  10 PRO D   38  ASN D   41  5                                   4    
HELIX   11  11 LEU D   51  GLN D   64  1                                  14    
HELIX   12  12 LYS D   65  ASN D   74  1                                  10    
HELIX   13  13 ASN D   74  ASN D   92  1                                  19    
HELIX   14  14 LEU D  193  PRO D  195  5                                   3    
SHEET    1   A 8 THR A  51  PRO A  54  0                                        
SHEET    2   A 8 ASP A  40  ASP A  46 -1  N  ASP A  46   O  THR A  51           
SHEET    3   A 8 VAL A  31  TYR A  37 -1  N  GLU A  35   O  LEU A  42           
SHEET    4   A 8 ASN A  15  GLN A  25 -1  N  THR A  21   O  SER A  34           
SHEET    5   A 8 VAL B   4  ASP B  14 -1  O  SER B   9   N  HIS A  20           
SHEET    6   A 8 PRO B  19  PHE B  28 -1  O  LYS B  20   N  LEU B  12           
SHEET    7   A 8 ASP B  31  ASP B  37 -1  O  THR B  34   N  ILE B  26           
SHEET    8   A 8 LYS B  42  PRO B  45 -1  O  ALA B  44   N  CYS B  35           
SHEET    1   B 4 ILE A 102  THR A 107  0                                        
SHEET    2   B 4 ASN A 117  LEU A 126 -1  O  VAL A 120   N  PHE A 106           
SHEET    3   B 4 SER A 157  PHE A 166 -1  O  LEU A 164   N  LEU A 119           
SHEET    4   B 4 PHE A 149  VAL A 153 -1  N  PHE A 149   O  PHE A 161           
SHEET    1   C 4 VAL A 140  VAL A 142  0                                        
SHEET    2   C 4 LEU A 131  HIS A 137 -1  N  HIS A 137   O  VAL A 140           
SHEET    3   C 4 PHE A 174  HIS A 180 -1  O  ILE A 177   N  ASN A 134           
SHEET    4   C 4 TYR A 185  TRP A 191 -1  O  ALA A 187   N  VAL A 178           
SHEET    1   D 4 SER B  98  LYS B 103  0                                        
SHEET    2   D 4 VAL B 113  PHE B 122 -1  O  TYR B 118   N  GLN B 100           
SHEET    3   D 4 TYR B 156  LEU B 164 -1  O  LEU B 164   N  VAL B 113           
SHEET    4   D 4 GLN B 149  PRO B 150 -1  N  GLN B 149   O  GLN B 157           
SHEET    1   E 4 LYS B 136  VAL B 138  0                                        
SHEET    2   E 4 THR B 128  LYS B 133 -1  N  LYS B 133   O  LYS B 136           
SHEET    3   E 4 TYR B 172  GLU B 177 -1  O  THR B 173   N  ARG B 132           
SHEET    4   E 4 ILE B 185  TRP B 189 -1  O  ILE B 185   N  VAL B 176           
SHEET    1   F 8 THR C  51  PRO C  54  0                                        
SHEET    2   F 8 ASP C  40  ASP C  46 -1  N  ASP C  46   O  THR C  51           
SHEET    3   F 8 VAL C  31  TYR C  37 -1  N  GLU C  35   O  LEU C  42           
SHEET    4   F 8 ASN C  15  GLN C  25 -1  N  THR C  21   O  SER C  34           
SHEET    5   F 8 VAL D   4  ASP D  14 -1  O  SER D   9   N  HIS C  20           
SHEET    6   F 8 PRO D  19  PHE D  28 -1  O  LYS D  20   N  LEU D  12           
SHEET    7   F 8 ASP D  31  TRP D  36 -1  O  THR D  34   N  ILE D  26           
SHEET    8   F 8 MET D  43  PRO D  45 -1  O  ALA D  44   N  CYS D  35           
SHEET    1   G 4 ILE C 102  THR C 107  0                                        
SHEET    2   G 4 ASN C 117  LEU C 126 -1  O  VAL C 120   N  PHE C 106           
SHEET    3   G 4 SER C 157  PHE C 166 -1  O  LEU C 164   N  LEU C 119           
SHEET    4   G 4 PHE C 145  VAL C 153 -1  N  PHE C 145   O  TYR C 163           
SHEET    1   H 4 VAL C 140  VAL C 142  0                                        
SHEET    2   H 4 LEU C 131  HIS C 137 -1  N  HIS C 137   O  VAL C 140           
SHEET    3   H 4 PHE C 174  HIS C 180 -1  O  ILE C 177   N  ASN C 134           
SHEET    4   H 4 TYR C 185  TRP C 191 -1  O  ALA C 187   N  VAL C 178           
SHEET    1   I 2 SER C 199  ASP C 200  0                                        
SHEET    2   I 2 GLN D 197  THR D 198 -1  O  THR D 198   N  SER C 199           
SHEET    1   J 4 SER D  98  LYS D 103  0                                        
SHEET    2   J 4 VAL D 113  PHE D 122 -1  O  TYR D 118   N  GLN D 100           
SHEET    3   J 4 TYR D 156  LEU D 164 -1  O  SER D 160   N  CYS D 117           
SHEET    4   J 4 GLN D 149  PRO D 150 -1  N  GLN D 149   O  GLN D 157           
SHEET    1   K 4 LEU D 137  VAL D 138  0                                        
SHEET    2   K 4 THR D 128  LYS D 133 -1  N  TRP D 131   O  VAL D 138           
SHEET    3   K 4 TYR D 172  GLU D 177 -1  O  VAL D 175   N  THR D 130           
SHEET    4   K 4 ILE D 185  TRP D 189 -1  O  ARG D 187   N  CYS D 174           
SSBOND   1 CYS A   24    CYS A   79                          1555   1555  2.04  
SSBOND   2 CYS A  121    CYS A  176                          1555   1555  2.03  
SSBOND   3 CYS B   11    CYS B   79                          1555   1555  2.04  
SSBOND   4 CYS B   25    CYS B   35                          1555   1555  2.04  
SSBOND   5 CYS B  117    CYS B  174                          1555   1555  2.03  
SSBOND   6 CYS C   24    CYS C   79                          1555   1555  2.03  
SSBOND   7 CYS C  121    CYS C  176                          1555   1555  2.03  
SSBOND   8 CYS D   11    CYS D   79                          1555   1555  2.04  
SSBOND   9 CYS D   25    CYS D   35                          1555   1555  2.04  
SSBOND  10 CYS D  117    CYS D  174                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG E   1     1555   1555  1.46  
LINK         ND2 ASN C  15                 C1  NAG F   1     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NDG E   2     1555   1555  1.40  
LINK         O4  NDG E   2                 C1  BMA E   3     1555   1555  1.39  
LINK         O3  BMA E   3                 C1  BMA E   4     1555   1555  1.40  
LINK         O4  NAG F   1                 C1  NDG F   2     1555   1555  1.40  
LINK         O4  NDG F   2                 C1  BMA F   3     1555   1555  1.39  
LINK         O3  BMA F   3                 C1  BMA F   4     1555   1555  1.40  
CISPEP   1 SER A   28    PRO A   29          0        -0.33                     
CISPEP   2 PHE A  127    PRO A  128          0        -0.65                     
CISPEP   3 TYR B  123    PRO B  124          0         0.35                     
CISPEP   4 SER C   28    PRO C   29          0        -0.15                     
CISPEP   5 PHE C  127    PRO C  128          0         0.45                     
CISPEP   6 TYR D  123    PRO D  124          0        -0.84                     
CRYST1   98.068  108.420  110.207  90.00  90.00  90.00 P 21 21 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      0.010197  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009223  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009074        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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