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Database: PDB
Entry: 1QFW
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HEADER    IMMUNE SYSTEM                           15-APR-99   1QFW              
TITLE     TERNARY COMPLEX OF HUMAN CHORIONIC GONADOTROPIN WITH FV ANTI ALPHA    
TITLE    2 SUBUNIT AND FV ANTI BETA SUBUNIT                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GONADOTROPIN ALPHA SUBUNIT;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HCG;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: GONADOTROPHIN BETA SUBUNIT;                                
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: HCG;                                                        
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: ANTIBODY (ANTI ALPHA SUBUNIT) (LIGHT CHAIN);               
COMPND  11 CHAIN: L;                                                            
COMPND  12 FRAGMENT: FV;                                                        
COMPND  13 SYNONYM: FV;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: ANTIBODY (ANTI ALPHA SUBUNIT) (HEAVY CHAIN);               
COMPND  17 CHAIN: H;                                                            
COMPND  18 FRAGMENT: FV;                                                        
COMPND  19 SYNONYM: FV;                                                         
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: ANTIBODY (ANTI BETA SUBUNIT) (LIGHT CHAIN);                
COMPND  23 CHAIN: M;                                                            
COMPND  24 FRAGMENT: FV;                                                        
COMPND  25 SYNONYM: FV;                                                         
COMPND  26 ENGINEERED: YES;                                                     
COMPND  27 MOL_ID: 6;                                                           
COMPND  28 MOLECULE: ANTIBODY (ANTI BETA SUBUNIT) (HEAVY CHAIN);                
COMPND  29 CHAIN: I;                                                            
COMPND  30 FRAGMENT: FV;                                                        
COMPND  31 SYNONYM: FV;                                                         
COMPND  32 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 SECRETION: HUMAN PREGNANCY URINE;                                    
SOURCE   6 OTHER_DETAILS: SUGAR RESIDUES LINKED TO ASN52 AND ASN78;             
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 SECRETION: HUMAN PREGNANCY URINE;                                    
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  14 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  15 ORGANISM_TAXID: 10090;                                               
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  18 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  19 ORGANISM_TAXID: 10090;                                               
SOURCE  20 MOL_ID: 5;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  22 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  23 ORGANISM_TAXID: 10090;                                               
SOURCE  24 MOL_ID: 6;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  26 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  27 ORGANISM_TAXID: 10090                                                
KEYWDS    GLYCOPROTEIN HORMONE, STIMULATION OF PRODUCTION OF PROGESTERONE, FVS  
KEYWDS   2 SPECIFICALLY DIRECTED AGAINST ALPHA AND BETA SUBUNIT, IMMUNE SYSTEM  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.TEGONI,S.SPINELLI,C.CAMBILLAU                                       
REVDAT   5   27-NOV-19 1QFW    1       JRNL   REMARK SEQADV LINK                
REVDAT   4   13-JUL-11 1QFW    1       VERSN                                    
REVDAT   3   24-FEB-09 1QFW    1       VERSN                                    
REVDAT   2   01-APR-03 1QFW    1       JRNL                                     
REVDAT   1   26-APR-00 1QFW    0                                                
JRNL        AUTH   M.TEGONI,S.SPINELLI,M.VERHOEYEN,P.DAVIS,C.CAMBILLAU          
JRNL        TITL   CRYSTAL STRUCTURE OF A TERNARY COMPLEX BETWEEN HUMAN         
JRNL        TITL 2 CHORIONIC GONADOTROPIN (HCG) AND TWO FV FRAGMENTS SPECIFIC   
JRNL        TITL 3 FOR THE ALPHA AND BETA-SUBUNITS.                             
JRNL        REF    J.MOL.BIOL.                   V. 289  1375 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10373373                                                     
JRNL        DOI    10.1006/JMBI.1999.2845                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.C.HEIKOOP,P.VAN DEN BOOGAART,R.DE LEEUW,U.M.ROSE,          
REMARK   1  AUTH 2 J.W.MULDERS,P.D.GROOTENHUIS                                  
REMARK   1  TITL   PARTIALLY DEGLYCOSYLATED HUMAN CHORIOGONADOTROPIN,           
REMARK   1  TITL 2 STABILIZED BY INTERSUBUNIT DISULFIDE BONDS, SHOWS FULL       
REMARK   1  TITL 3 BIOACTIVITY.                                                 
REMARK   1  REF    EUR.J.BIOCHEM.                V. 253   354 1998              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   9578495                                                      
REMARK   1  DOI    10.1046/J.1432-1327.1998.2530354.X                           
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.J.LAPTHORN,D.C.HARRIS,A.LITTLEJOHN,J.W.LUSTBADER,          
REMARK   1  AUTH 2 R.E.CANFIELD,K.J.MACHIN,F.J.MORGAN,N.W.ISAACS                
REMARK   1  TITL   CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN.           
REMARK   1  REF    NATURE                        V. 369   455 1994              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   1  PMID   8202136                                                      
REMARK   1  DOI    10.1038/369455A0                                             
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   H.WU,J.W.LUSTBADER,Y.LIU,R.E.CANFIELD,W.A.HENDRICKSON        
REMARK   1  TITL   STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN AT 2.6 A           
REMARK   1  TITL 2 RESOLUTION FROM MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN. 
REMARK   1  REF    STRUCTURE                     V.   2   545 1994              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   7922031                                                      
REMARK   1  DOI    10.1016/S0969-2126(00)00054-X                                
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   J.W.LUSTBADER,S.BIRKEN,N.F.PILEGGI,M.A.KOLKS,S.POLLAK,       
REMARK   1  AUTH 2 M.E.CUFF,W.YANG,W.A.HENDRICKSON,R.E.CANFIELD                 
REMARK   1  TITL   CRYSTALLIZATION AND CHARACTERIZATION OF HUMAN CHORIONIC      
REMARK   1  TITL 2 GONADOTROPIN IN CHEMICALLY DEGLYCOSYLATED AND ENZYMATICALLY  
REMARK   1  TITL 3 DESIALYLATED STATES.                                         
REMARK   1  REF    BIOCHEMISTRY                  V.  28  9239 1989              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   2611225                                                      
REMARK   1  DOI    10.1021/BI00450A001                                          
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   M.M.MATZUK,J.L.KEENE,I.BOIME                                 
REMARK   1  TITL   SITE SPECIFICITY OF THE CHORIONIC GONADOTROPIN N-LINKED      
REMARK   1  TITL 2 OLIGOSACCHARIDES IN SIGNAL TRANSDUCTION.                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 264  2409 1989              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   2536708                                                      
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   W.R.MOYLE,O.P.BAHL,L.MARZ                                    
REMARK   1  TITL   ROLE OF CARBOHYDRATE OF HUMAN CHORIONIC GONADOTROPIN IN THE  
REMARK   1  TITL 2 MECHANISM OF HORMONE ACTION.                                 
REMARK   1  REF    J.BIOL.CHEM.                  V. 250  9163 1975              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   172504                                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.843                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 9.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 250.000                        
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9772                           
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) : 0.260                           
REMARK   3   FREE R VALUE                     : 0.310                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 890                             
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.65                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1261                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3600                       
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 116                          
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            : 4910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 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) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.620                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 29.14                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.290                           
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  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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QFW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000000856.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 297.0                              
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12096                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.16600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1HRP, 1IGC, 2IMN                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 100 MM           
REMARK 280  TRIS/HCL PH 8.0, PROTEIN CONCENTRATION 3 MG/ML                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       50.03333            
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      100.06667            
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        0.00000            
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      100.06667            
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       50.03333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, L, H, M, I                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     SER B     1                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     PHE B   115                                                      
REMARK 465     GLN B   116                                                      
REMARK 465     ASP B   117                                                      
REMARK 465     SER B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     SER B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     LYS B   122                                                      
REMARK 465     ALA B   123                                                      
REMARK 465     PRO B   124                                                      
REMARK 465     PRO B   125                                                      
REMARK 465     PRO B   126                                                      
REMARK 465     SER B   127                                                      
REMARK 465     LEU B   128                                                      
REMARK 465     PRO B   129                                                      
REMARK 465     SER B   130                                                      
REMARK 465     PRO B   131                                                      
REMARK 465     SER B   132                                                      
REMARK 465     ARG B   133                                                      
REMARK 465     LEU B   134                                                      
REMARK 465     PRO B   135                                                      
REMARK 465     GLY B   136                                                      
REMARK 465     PRO B   137                                                      
REMARK 465     SER B   138                                                      
REMARK 465     ASP B   139                                                      
REMARK 465     THR B   140                                                      
REMARK 465     PRO B   141                                                      
REMARK 465     ILE B   142                                                      
REMARK 465     LEU B   143                                                      
REMARK 465     PRO B   144                                                      
REMARK 465     GLN B   145                                                      
REMARK 465     SER L    28                                                      
REMARK 465     VAL L    29                                                      
REMARK 465     GLN H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PHE H    64                                                      
REMARK 465     LYS H    65                                                      
REMARK 465     SER H    66                                                      
REMARK 465     SER I   322                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  45    CG   CD   CE   NZ                                   
REMARK 470     LYS B   2    CG   CD   CE   NZ                                   
REMARK 470     ARG B   6    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  89    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 112    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP L   1    CG   OD1  OD2                                       
REMARK 470     ARG L  24    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L  27    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLU L  27    OE2                                                 
REMARK 470     ASP L  30    CG   OD1  OD2                                       
REMARK 470     LYS L  43    CG   CD   CE   NZ                                   
REMARK 470     ARG L  65    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H   3    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  13    CG   CD   CE   NZ                                   
REMARK 470     LYS H  19    CG   CD   CE   NZ                                   
REMARK 470     LYS H  23    CG   CD   CE   NZ                                   
REMARK 470     GLN H  43    CG   CD   OE1  NE2                                  
REMARK 470     LYS H  63    CA   C    O    CB   CG   CD   CE                    
REMARK 470     LYS H  63    NZ                                                  
REMARK 470     LYS H  67    CG   CD   CE   NZ                                   
REMARK 470     GLN H 109    CG   CD   OE1  NE2                                  
REMARK 470     SER H 117    OG                                                  
REMARK 470     ARG M 308    CA   C    O    CB   CG   CD   NE                    
REMARK 470     ARG M 308    CZ   NH1  NH2                                       
REMARK 470     SER I 321    CA   C    O    CB   OG                              
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     THR I   256                                                      
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     MET A   29   CE                                                  
REMARK 480     ARG A   42   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN A   50   CG   CD   OE1  NE2                                  
REMARK 480     LYS A   51   CE   NZ                                             
REMARK 480     ARG A   67   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG B   60   CD                                                  
REMARK 480     ARG B   74   CG                                                  
REMARK 480     ARG B   95   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     GLU M  241   CG   CD   OE1  OE2                                  
REMARK 480     LYS M  245   CE   NZ                                             
REMARK 480     ASP M  260   CG   OD1  OD2                                       
REMARK 480     ASP M  270   CB   CG   OD1  OD2                                  
REMARK 480     ASN M  293   CB   CG   OD1  ND2                                  
REMARK 480     LYS M  303   CE   NZ                                             
REMARK 480     GLN I  201   CG   CD                                             
REMARK 480     GLN I  205   CG   CD   OE1  NE2                                  
REMARK 480     GLU I  242   CG   CD   OE1  OE2                                  
REMARK 480     LYS I  265   CG   CD   CE                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER L    26     N    GLU L    27              0.95            
REMARK 500   O    LEU B     5     N    ARG B     6              1.21            
REMARK 500   O    ASP M   230     N    SER M   231              1.60            
REMARK 500   OD1  ASN H    52     OG1  THR H    53              2.01            
REMARK 500   O    GLY B    47     N    LEU B    49              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR A    46     O    THR A    46     6765     1.97            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    GLU A   9   CG    GLU A   9   CD      0.099                       
REMARK 500    SER A  92   C     SER A  92   O      -0.185                       
REMARK 500    GLU B   3   CA    GLU B   3   CB      0.132                       
REMARK 500    GLU B   3   CB    GLU B   3   CG      0.123                       
REMARK 500    GLU B   3   CG    GLU B   3   CD      0.093                       
REMARK 500    GLU B   3   CA    GLU B   3   C       0.193                       
REMARK 500    GLU B   3   C     GLU B   3   O      -0.158                       
REMARK 500    PRO B   4   N     PRO B   4   CA      0.244                       
REMARK 500    PRO B   4   CD    PRO B   4   N      -0.182                       
REMARK 500    PRO B   4   CA    PRO B   4   C       0.145                       
REMARK 500    PRO B   4   C     LEU B   5   N      -0.299                       
REMARK 500    LEU B   5   C     ARG B   6   N      -0.240                       
REMARK 500    SER L  26   C     SER L  26   O      -0.207                       
REMARK 500    ASP H  26   C     TYR H  27   N      -0.169                       
REMARK 500    TYR H 100   C     GLY H 101   N      -0.165                       
REMARK 500    ASP M 230   C     SER M 231   N      -0.374                       
REMARK 500    THR I 252   C     THR I 252   O      -0.316                       
REMARK 500    GLY I 255   CA    GLY I 255   C      -0.238                       
REMARK 500    ARG I 298   C     GLN I 299   N       0.156                       
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    CYS A   7   CA  -  CB  -  SG  ANGL. DEV. =   7.9 DEGREES          
REMARK 500    PRO A   8   C   -  N   -  CA  ANGL. DEV. =  13.7 DEGREES          
REMARK 500    LYS A  91   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    SER A  92   CA  -  C   -  O   ANGL. DEV. =  13.6 DEGREES          
REMARK 500    GLU B   3   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    GLU B   3   N   -  CA  -  C   ANGL. DEV. = -17.2 DEGREES          
REMARK 500    GLU B   3   O   -  C   -  N   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    PRO B   4   C   -  N   -  CA  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    PRO B   4   C   -  N   -  CD  ANGL. DEV. = -16.5 DEGREES          
REMARK 500    PRO B   4   N   -  CA  -  C   ANGL. DEV. =  29.4 DEGREES          
REMARK 500    PRO B   4   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    LEU B   5   CA  -  C   -  N   ANGL. DEV. =  30.0 DEGREES          
REMARK 500    LEU B   5   O   -  C   -  N   ANGL. DEV. = -59.2 DEGREES          
REMARK 500    ARG B   8   CA  -  C   -  N   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ARG B   8   O   -  C   -  N   ANGL. DEV. =  10.9 DEGREES          
REMARK 500    CYS B   9   CB  -  CA  -  C   ANGL. DEV. =  14.6 DEGREES          
REMARK 500    CYS B   9   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    CYS B   9   CA  -  C   -  N   ANGL. DEV. = -19.1 DEGREES          
REMARK 500    CYS B   9   O   -  C   -  N   ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG B  10   C   -  N   -  CA  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B  10   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLN B  46   C   -  N   -  CA  ANGL. DEV. = -15.7 DEGREES          
REMARK 500    LEU B  49   CA  -  CB  -  CG  ANGL. DEV. =  22.0 DEGREES          
REMARK 500    LYS B 104   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU B 108   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    CYS B 110   CA  -  CB  -  SG  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    SER L  26   CA  -  C   -  O   ANGL. DEV. =  13.6 DEGREES          
REMARK 500    SER L  26   O   -  C   -  N   ANGL. DEV. = -77.7 DEGREES          
REMARK 500    ARG L  54   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ALA L  55   O   -  C   -  N   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ARG L  72   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    GLY H   8   N   -  CA  -  C   ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ALA H  16   N   -  CA  -  C   ANGL. DEV. =  19.8 DEGREES          
REMARK 500    ASP H  26   CB  -  CA  -  C   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    ASP H  26   N   -  CA  -  CB  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ASP H  26   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP H  26   O   -  C   -  N   ANGL. DEV. = -10.4 DEGREES          
REMARK 500    TYR H  27   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    THR H  28   CB  -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    THR H  28   N   -  CA  -  CB  ANGL. DEV. = -25.2 DEGREES          
REMARK 500    SER H  91   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    TYR H 100   O   -  C   -  N   ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ASN H 102   CA  -  CB  -  CG  ANGL. DEV. =  23.7 DEGREES          
REMARK 500    ASP M 230   CA  -  C   -  N   ANGL. DEV. =  32.5 DEGREES          
REMARK 500    ASP M 230   O   -  C   -  N   ANGL. DEV. = -31.3 DEGREES          
REMARK 500    SER M 231   C   -  N   -  CA  ANGL. DEV. =  44.9 DEGREES          
REMARK 500    GLY I 255   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    GLY I 255   CA  -  C   -  O   ANGL. DEV. =  14.3 DEGREES          
REMARK 500    THR I 256   C   -  N   -  CA  ANGL. DEV. = -16.3 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    PRO A   8      137.60    -38.33                                   
REMARK 500    CYS A  10       94.71    -69.29                                   
REMARK 500    PRO A  21      127.92    -39.70                                   
REMARK 500    GLN A  50       93.42    -50.35                                   
REMARK 500    LYS A  51     -151.64    -72.36                                   
REMARK 500    ASN A  52      -10.15   -157.60                                   
REMARK 500    MET A  71      -44.21    -27.56                                   
REMARK 500    GLU B   3     -152.38   -131.78                                   
REMARK 500    PRO B   4     -128.27    -53.67                                   
REMARK 500    ALA B  14      149.34   -174.52                                   
REMARK 500    GLU B  21       93.25    -69.73                                   
REMARK 500    ILE B  27     -168.90   -113.45                                   
REMARK 500    LEU B  49      144.47    162.49                                   
REMARK 500    ARG B  60      -61.68   -132.44                                   
REMARK 500    CYS B  72      151.50    -47.21                                   
REMARK 500    VAL B  79      102.81    -40.49                                   
REMARK 500    PRO B 103       97.21    -57.19                                   
REMARK 500    ASP B 105      -78.65    -23.27                                   
REMARK 500    LEU B 108       86.18    -63.16                                   
REMARK 500    SER L  10       79.71   -157.24                                   
REMARK 500    SER L  26       87.26    -62.79                                   
REMARK 500    TYR L  32      116.15   -170.12                                   
REMARK 500    ARG L  54     -142.96     55.03                                   
REMARK 500    PRO L  63      177.12    -52.51                                   
REMARK 500    ARG L  65      -80.78    -47.75                                   
REMARK 500    PHE L  66      118.57    -35.87                                   
REMARK 500    SER L  71      -47.82   -140.37                                   
REMARK 500    ARG L  72      -78.44   -107.69                                   
REMARK 500    ASP L  86       38.59    -81.83                                   
REMARK 500    GLU L  97      -95.17    -86.35                                   
REMARK 500    LYS L 109      125.88    -39.36                                   
REMARK 500    LEU H   4       82.23   -162.75                                   
REMARK 500    VAL H  12      135.75   -175.71                                   
REMARK 500    LYS H  13      173.01    -51.81                                   
REMARK 500    PRO H  14       68.62    -68.74                                   
REMARK 500    ALA H  16      -49.38     -7.32                                   
REMARK 500    TYR H  27      173.35    154.09                                   
REMARK 500    THR H  28       98.38    -12.66                                   
REMARK 500    THR H  30       26.19    -77.58                                   
REMARK 500    TRP H  33     -161.91    -59.13                                   
REMARK 500    MET H  34      127.53   -175.89                                   
REMARK 500    PRO H  52A       1.31    -61.41                                   
REMARK 500    THR H  53      -63.65    -95.50                                   
REMARK 500    TYR H  60     -154.45    -90.92                                   
REMARK 500    ALA H  68       38.95   -146.97                                   
REMARK 500    THR H  69      105.30    -46.43                                   
REMARK 500    ALA H  80       88.07   -153.65                                   
REMARK 500    THR H  87     -160.80   -107.71                                   
REMARK 500    ASP H  90     -153.33    -97.05                                   
REMARK 500    ALA H  92     -151.06   -120.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP H   26     TYR H   27                  144.12                    
REMARK 500 ASP M  230     SER M  231                   52.92                    
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    ARG L  72         0.30    SIDE CHAIN                              
REMARK 500    TYR L  98         0.08    SIDE CHAIN                              
REMARK 500    TYR H 106         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LEU B   5         61.47                                           
REMARK 500    PRO B   7        -10.98                                           
REMARK 500    GLY B  47        -12.05                                           
REMARK 500    SER L  26        -40.13                                           
REMARK 500    LEU H  11         17.39                                           
REMARK 500    VAL M 229         12.95                                           
REMARK 500    ASP M 230         10.51                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 93                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 94                  
DBREF  1QFW A    1    92  UNP    P01215   GLHA_HUMAN      25    116             
DBREF  1QFW B    1   145  UNP    P01233   CGHB_HUMAN       1    145             
DBREF  1QFW L    1   114  PDB    1QFW     1QFW             1    114             
DBREF  1QFW H    1   117  PDB    1QFW     1QFW             1    117             
DBREF  1QFW M  201   308  PDB    1QFW     1QFW           201    308             
DBREF  1QFW I  201   322  PDB    1QFW     1QFW           201    322             
SEQADV 1QFW THR A    4  UNP  P01215    VAL    28 CONFLICT                       
SEQRES   1 A   92  ALA PRO ASP THR GLN ASP CYS PRO GLU CYS THR LEU GLN          
SEQRES   2 A   92  GLU ASN PRO PHE PHE SER GLN PRO GLY ALA PRO ILE LEU          
SEQRES   3 A   92  GLN CYS MET GLY CYS CYS PHE SER ARG ALA TYR PRO THR          
SEQRES   4 A   92  PRO LEU ARG SER LYS LYS THR MET LEU VAL GLN LYS ASN          
SEQRES   5 A   92  VAL THR SER GLU SER THR CYS CYS VAL ALA LYS SER TYR          
SEQRES   6 A   92  ASN ARG VAL THR VAL MET GLY GLY PHE LYS VAL GLU ASN          
SEQRES   7 A   92  HIS THR ALA CYS HIS CYS SER THR CYS TYR TYR HIS LYS          
SEQRES   8 A   92  SER                                                          
SEQRES   1 B  145  SER LYS GLU PRO LEU ARG PRO ARG CYS ARG PRO ILE ASN          
SEQRES   2 B  145  ALA THR LEU ALA VAL GLU LYS GLU GLY CYS PRO VAL CYS          
SEQRES   3 B  145  ILE THR VAL ASN THR THR ILE CYS ALA GLY TYR CYS PRO          
SEQRES   4 B  145  THR MET THR ARG VAL LEU GLN GLY VAL LEU PRO ALA LEU          
SEQRES   5 B  145  PRO GLN VAL VAL CYS ASN TYR ARG ASP VAL ARG PHE GLU          
SEQRES   6 B  145  SER ILE ARG LEU PRO GLY CYS PRO ARG GLY VAL ASN PRO          
SEQRES   7 B  145  VAL VAL SER TYR ALA VAL ALA LEU SER CYS GLN CYS ALA          
SEQRES   8 B  145  LEU CYS ARG ARG SER THR THR ASP CYS GLY GLY PRO LYS          
SEQRES   9 B  145  ASP HIS PRO LEU THR CYS ASP ASP PRO ARG PHE GLN ASP          
SEQRES  10 B  145  SER SER SER SER LYS ALA PRO PRO PRO SER LEU PRO SER          
SEQRES  11 B  145  PRO SER ARG LEU PRO GLY PRO SER ASP THR PRO ILE LEU          
SEQRES  12 B  145  PRO GLN                                                      
SEQRES   1 L  114  ASP ILE GLU LEU THR GLN SER PRO ASP SER LEU ALA VAL          
SEQRES   2 L  114  SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER          
SEQRES   3 L  114  GLU SER VAL ASP SER TYR GLY ASN SER PHE MET GLN TRP          
SEQRES   4 L  114  TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE          
SEQRES   5 L  114  TYR ARG ALA SER ASN LEU GLU SER GLY ILE PRO ALA ARG          
SEQRES   6 L  114  PHE SER GLY THR GLY SER ARG THR ASP PHE THR LEU THR          
SEQRES   7 L  114  ILE ASN PRO VAL GLU ALA ASP ASP VAL ALA THR TYR TYR          
SEQRES   8 L  114  CYS GLN GLN SER ASP GLU TYR PRO TYR MET TYR THR PHE          
SEQRES   9 L  114  GLY GLY GLY THR LYS LEU GLU ILE LYS ARG                      
SEQRES   1 H  117  GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  117  PRO GLY ALA SER VAL LYS LEU SER CYS LYS ALA SER ASP          
SEQRES   3 H  117  TYR THR PHE THR SER TYR TRP MET HIS TRP VAL LYS GLN          
SEQRES   4 H  117  ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY GLU ILE ASN          
SEQRES   5 H  117  PRO THR ASN GLY ARG THR TYR TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  117  SER LYS ALA THR LEU THR VAL ALA ALA SER ALA SER THR          
SEQRES   7 H  117  ALA ALA MET GLN ALA SER SER LEU THR SER GLU ASP SER          
SEQRES   8 H  117  ALA VAL TYR TYR CYS ALA ARG ARG TYR GLY ASN SER PHE          
SEQRES   9 H  117  ASP TYR TRP GLY GLN GLY THR THR VAL THR VAL SER SER          
SEQRES   1 M  108  ASP ILE GLU LEU THR GLN SER PRO LYS SER MET SER MET          
SEQRES   2 M  108  SER VAL GLY GLU ARG VAL THR LEU SER CYS LYS ALA SER          
SEQRES   3 M  108  GLU THR VAL ASP SER PHE VAL SER TRP TYR GLN GLN LYS          
SEQRES   4 M  108  PRO GLU GLN SER PRO LYS LEU LEU ILE PHE GLY ALA SER          
SEQRES   5 M  108  ASN ARG PHE SER GLY VAL PRO ASP ARG PHE THR GLY SER          
SEQRES   6 M  108  GLY SER ALA THR ASP PHE THR LEU THR ILE SER SER VAL          
SEQRES   7 M  108  GLN ALA GLU ASP PHE ALA ASP TYR HIS CYS GLY GLN THR          
SEQRES   8 M  108  TYR ASN HIS PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 M  108  GLU ILE LYS ARG                                              
SEQRES   1 I  122  GLN VAL GLN LEU GLN GLU SER GLY GLY HIS LEU VAL LYS          
SEQRES   2 I  122  PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 I  122  PHE ALA PHE SER SER PHE ASP MET SER TRP ILE ARG GLN          
SEQRES   4 I  122  THR PRO GLU LYS ARG LEU GLU TRP VAL ALA SER ILE THR          
SEQRES   5 I  122  ASN VAL GLY THR TYR THR TYR TYR PRO GLY SER VAL LYS          
SEQRES   6 I  122  GLY ARG PHE SER ILE SER ARG ASP ASN ALA ARG ASN THR          
SEQRES   7 I  122  LEU ASN LEU GLN MET SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 I  122  ALA LEU TYR PHE CYS ALA ARG GLN GLY THR ALA ALA GLN          
SEQRES   9 I  122  PRO TYR TRP TYR PHE ASP VAL TRP GLY ALA GLY THR THR          
SEQRES  10 I  122  VAL THR VAL SER SER                                          
MODRES 1QFW ASN A   52  ASN  GLYCOSYLATION SITE                                 
MODRES 1QFW ASN A   78  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A  93      14                                                       
HET    NAG  A  94      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   7  NAG    2(C8 H15 N O6)                                               
HELIX    1   1 PRO A   40  LYS A   45  1                                   6    
HELIX    2   2 THR H   28  TYR H   32  5                                   5    
HELIX    3   3 ALA I  228  PHE I  232  5                                   5    
HELIX    4   4 ARG I  287  THR I  291  5                                   5    
SHEET    1   A 4 LYS A  75  THR A  86  0                                        
SHEET    2   A 4 VAL A  53  THR A  69 -1  N  CYS A  59   O  SER A  85           
SHEET    3   A 4 LEU A  26  PRO A  38 -1  O  PHE A  33   N  THR A  58           
SHEET    4   A 4 THR A  11  GLU A  14 -1  O  THR A  11   N  MET A  29           
SHEET    1   B 5 LYS A  75  THR A  86  0                                        
SHEET    2   B 5 VAL A  53  THR A  69 -1  N  CYS A  59   O  SER A  85           
SHEET    3   B 5 LEU A  26  PRO A  38 -1  O  PHE A  33   N  THR A  58           
SHEET    4   B 5 ILE B  27  MET B  41 -1  O  CYS B  34   N  ALA A  36           
SHEET    5   B 5 ARG B  10  VAL B  18 -1  N  ARG B  10   O  ALA B  35           
SHEET    1   C 2 LYS A  91  SER A  92  0                                        
SHEET    2   C 2 CYS B  93  ARG B  94  1  O  CYS B  93   N  SER A  92           
SHEET    1   D 2 VAL B  56  ARG B  68  0                                        
SHEET    2   D 2 VAL B  79  ALA B  91 -1  N  VAL B  80   O  ILE B  67           
SHEET    1   E 4 THR L   5  GLN L   6  0                                        
SHEET    2   E 4 CYS L  23  ARG L  24 -1  N  ARG L  24   O  THR L   5           
SHEET    3   E 4 ASP L  74  THR L  78 -1  N  PHE L  75   O  CYS L  23           
SHEET    4   E 4 SER L  67  THR L  69 -1  O  SER L  67   N  THR L  78           
SHEET    1   F 2 SER L  10  SER L  14  0                                        
SHEET    2   F 2 LYS L 109  LYS L 113  1  O  LYS L 109   N  LEU L  11           
SHEET    1   G 4 LEU L  50  ILE L  52  0                                        
SHEET    2   G 4 SER L  35  GLN L  42 -1  O  TRP L  39   N  LEU L  51           
SHEET    3   G 4 THR L  89  ASP L  96 -1  O  THR L  89   N  GLN L  42           
SHEET    4   G 4 TYR L 102  PHE L 104 -1  O  THR L 103   N  GLN L  94           
SHEET    1   H 4 LEU H   4  SER H   7  0                                        
SHEET    2   H 4 SER H  21  ALA H  24 -1  O  SER H  21   N  SER H   7           
SHEET    3   H 4 THR H  78  ALA H  79 -1  O  ALA H  79   N  CYS H  22           
SHEET    4   H 4 VAL H  72  ALA H  73 -1  N  ALA H  73   O  THR H  78           
SHEET    1   I 2 SER H  17  VAL H  18  0                                        
SHEET    2   I 2 ALA H  83  SER H  84 -1  O  ALA H  83   N  VAL H  18           
SHEET    1   J 4 THR H  57  TYR H  59  0                                        
SHEET    2   J 4 LEU H  45  ILE H  51 -1  N  GLU H  50   O  TYR H  59           
SHEET    3   J 4 HIS H  35  GLN H  39 -1  O  TRP H  36   N  ILE H  48           
SHEET    4   J 4 VAL H  93  ALA H  97 -1  O  VAL H  93   N  GLN H  39           
SHEET    1   K 4 LEU M 204  SER M 207  0                                        
SHEET    2   K 4 VAL M 219  ALA M 225 -1  N  SER M 222   O  SER M 207           
SHEET    3   K 4 ASP M 270  ILE M 275 -1  N  PHE M 271   O  CYS M 223           
SHEET    4   K 4 PHE M 262  THR M 263 -1  N  THR M 263   O  THR M 274           
SHEET    1   L 4 LYS M 245  ILE M 248  0                                        
SHEET    2   L 4 VAL M 233  GLN M 238 -1  O  TRP M 235   N  LEU M 247           
SHEET    3   L 4 ASP M 285  GLN M 290 -1  N  ASP M 285   O  GLN M 238           
SHEET    4   L 4 THR M 297  PHE M 298 -1  O  THR M 297   N  GLN M 290           
SHEET    1   M 5 LYS M 245  ILE M 248  0                                        
SHEET    2   M 5 VAL M 233  GLN M 238 -1  O  TRP M 235   N  LEU M 247           
SHEET    3   M 5 ASP M 285  GLN M 290 -1  N  ASP M 285   O  GLN M 238           
SHEET    4   M 5 THR M 302  GLU M 305 -1  O  THR M 302   N  TYR M 286           
SHEET    5   M 5 MET M 211  SER M 212  1  O  MET M 211   N  GLU M 305           
SHEET    1   N 4 LEU I 204  SER I 207  0                                        
SHEET    2   N 4 LEU I 218  ALA I 224 -1  N  SER I 221   O  SER I 207           
SHEET    3   N 4 THR I 278  MET I 283 -1  O  LEU I 279   N  CYS I 222           
SHEET    4   N 4 PHE I 268  ILE I 270 -1  O  SER I 269   N  GLN I 282           
SHEET    1   O 4 LEU I 245  TRP I 247  0                                        
SHEET    2   O 4 MET I 234  GLN I 239 -1  N  ARG I 238   O  GLU I 246           
SHEET    3   O 4 ALA I 292  ARG I 298 -1  N  LEU I 293   O  GLN I 239           
SHEET    4   O 4 THR I 317  VAL I 318 -1  N  VAL I 318   O  ALA I 292           
SHEET    1   P 2 SER I 250  ILE I 251  0                                        
SHEET    2   P 2 THR I 258  TYR I 259 -1  N  TYR I 259   O  SER I 250           
SSBOND   1 CYS A    7    CYS A   31                          1555   1555  2.02  
SSBOND   2 CYS A   10    CYS A   60                          1555   1555  2.03  
SSBOND   3 CYS A   28    CYS A   82                          1555   1555  2.04  
SSBOND   4 CYS A   32    CYS A   84                          1555   1555  2.01  
SSBOND   5 CYS A   59    CYS A   87                          1555   1555  2.01  
SSBOND   6 CYS B    9    CYS B   57                          1555   1555  2.08  
SSBOND   7 CYS B   23    CYS B   72                          1555   1555  2.02  
SSBOND   8 CYS B   26    CYS B  110                          1555   1555  2.03  
SSBOND   9 CYS B   34    CYS B   88                          1555   1555  2.02  
SSBOND  10 CYS B   38    CYS B   90                          1555   1555  2.01  
SSBOND  11 CYS B   93    CYS B  100                          1555   1555  2.02  
SSBOND  12 CYS L   23    CYS L   92                          1555   1555  2.17  
SSBOND  13 CYS H   22    CYS H   96                          1555   1555  2.03  
SSBOND  14 CYS M  223    CYS M  288                          1555   1555  2.01  
SSBOND  15 CYS I  222    CYS I  296                          1555   1555  2.03  
LINK         ND2 ASN A  52                 C1  NAG A  93     1555   1555  1.42  
LINK         ND2 ASN A  78                 C1  NAG A  94     1555   1555  1.42  
CISPEP   1 SER M  207    PRO M  208          0         0.09                     
CISPEP   2 HIS M  294    PRO M  295          0        -0.53                     
SITE     1 AC1  6 ASN A  52  VAL A  53  VAL B  62  PHE B  64                    
SITE     2 AC1  6 ALA B  83  SER M 226                                          
SITE     1 AC2  7 ALA A  23  PRO A  24  ILE A  25  LEU A  26                    
SITE     2 AC2  7 VAL A  68  ASN A  78  GLN I 201                               
CRYST1  104.900  104.900  150.100  90.00  90.00 120.00 P 31 2 1      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      0.009533  0.005504  0.000000        0.00000                         
SCALE2      0.000000  0.011008  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006662        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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