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Database: PDB
Entry: 2V64
LinkDB: 2V64
Original site: 2V64 
HEADER    CELL CYCLE                              13-JUL-07   2V64              
TITLE     CRYSTALLOGRAPHIC STRUCTURE OF THE CONFORMATIONAL DIMER OF             
TITLE    2 THE SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2.                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN                
COMPND   3  MAD2A;                                                              
COMPND   4 CHAIN: A, F, C;                                                      
COMPND   5 FRAGMENT: RESIDUES 2-205;                                            
COMPND   6 SYNONYM: MAD2-LIKE 1, HSMAD2, MAD2;                                  
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MBP1;                                                      
COMPND  10 CHAIN: B, G, I;                                                      
COMPND  11 OTHER_DETAILS: SEQUENCE SWYSYPPPQRAV;                                
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN                
COMPND  14  MAD2A;                                                              
COMPND  15 CHAIN: E, H, D;                                                      
COMPND  16 FRAGMENT: RESIDUES 2-108,118-205;                                    
COMPND  17 SYNONYM: MAD2-LIKE 1, HSMAD2, MAD2;                                  
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630;                                               
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    SPINDLE ASSEMBLY CHECKPOINT, MAD2, NUCLEUS, MITOSIS,                  
KEYWDS   2 APOPTOSIS, CELL CYCLE, CELL DIVISION, PHOSPHORYLATION,               
KEYWDS   3 CONFORMATIONAL DIMER                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MAPELLI,L.MASSIMILIANO,S.SANTAGUIDA,A.MUSACCHIO                     
REVDAT   4   21-DEC-16 2V64    1       SOURCE REMARK VERSN  FORMUL              
REVDAT   3   09-JUN-09 2V64    1       REMARK                                   
REVDAT   2   24-FEB-09 2V64    1       VERSN                                    
REVDAT   1   27-NOV-07 2V64    0                                                
JRNL        AUTH   M.MAPELLI,L.MASSIMILIANO,S.SANTAGUIDA,A.MUSACCHIO            
JRNL        TITL   THE MAD2 CONFORMATIONAL DIMER: STRUCTURE AND                 
JRNL        TITL 2 IMPLICATIONS FOR THE SPINDLE ASSEMBLY CHECKPOINT             
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 131   730 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   18022367                                                     
JRNL        DOI    10.1016/J.CELL.2007.08.049                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : MAXIMUM LIKELIHOOD                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2539666.54                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 35593                          
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) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1766                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.6                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5527                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.308                        
REMARK   3   BIN FREE R VALUE                    : 0.359                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.2                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 303                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 6                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.0                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.1                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.19                                                
REMARK   3    B22 (A**2) : 0.21                                                 
REMARK   3    B33 (A**2) : 3.98                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.43                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.50                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.7                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.4                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.04                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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 : FLAT MODEL                                           
REMARK   3   KSOL        : 0.385076                                             
REMARK   3   BSOL        : 33.5759                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2V64 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JUL-07.                  
REMARK 100 THE PDBE ID CODE IS EBI-33131.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9333                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL2000                            
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37591                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.90                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.01                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1GO4                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAACETATE PH 4.6, 3.5M              
REMARK 280  NAFORMATE                                                           
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       56.29000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.88000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.94000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.88000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       56.29000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.94000            
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.81 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I, D                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.15 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H                               
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     MET A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     VAL B    12                                                      
REMARK 465     MET C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     MET D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     HIS D    -3                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     HIS D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     LEU D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     VAL D   162                                                      
REMARK 465     VAL D   163                                                      
REMARK 465     PRO D   164                                                      
REMARK 465     GLU D   165                                                      
REMARK 465     LYS D   166                                                      
REMARK 465     TRP D   167                                                      
REMARK 465     GLU D   168                                                      
REMARK 465     GLU D   169                                                      
REMARK 465     SER D   170                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     MET D   196                                                      
REMARK 465     VAL D   197                                                      
REMARK 465     ALA D   198                                                      
REMARK 465     TYR D   199                                                      
REMARK 465     LYS D   200                                                      
REMARK 465     ILE D   201                                                      
REMARK 465     PRO D   202                                                      
REMARK 465     VAL D   203                                                      
REMARK 465     ASN D   204                                                      
REMARK 465     ASP D   205                                                      
REMARK 465     MET E    -7                                                      
REMARK 465     HIS E    -6                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     HIS E    -3                                                      
REMARK 465     HIS E    -2                                                      
REMARK 465     HIS E    -1                                                      
REMARK 465     GLY E     0                                                      
REMARK 465     SER E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     LEU E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     LEU E     5                                                      
REMARK 465     SER E     6                                                      
REMARK 465     ARG E     7                                                      
REMARK 465     GLU E     8                                                      
REMARK 465     GLY E   115                                                      
REMARK 465     SER E   116                                                      
REMARK 465     GLY E   117                                                      
REMARK 465     GLU E   118                                                      
REMARK 465     LYS E   119                                                      
REMARK 465     MET E   196                                                      
REMARK 465     VAL E   197                                                      
REMARK 465     ALA E   198                                                      
REMARK 465     TYR E   199                                                      
REMARK 465     LYS E   200                                                      
REMARK 465     ILE E   201                                                      
REMARK 465     PRO E   202                                                      
REMARK 465     VAL E   203                                                      
REMARK 465     ASN E   204                                                      
REMARK 465     ASP E   205                                                      
REMARK 465     MET F    -7                                                      
REMARK 465     HIS F    -6                                                      
REMARK 465     VAL G    12                                                      
REMARK 465     MET H    -7                                                      
REMARK 465     HIS H    -6                                                      
REMARK 465     HIS H    -5                                                      
REMARK 465     HIS H    -4                                                      
REMARK 465     HIS H    -3                                                      
REMARK 465     HIS H    -2                                                      
REMARK 465     HIS H    -1                                                      
REMARK 465     GLY H     0                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ALA H     2                                                      
REMARK 465     LEU H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     LEU H     5                                                      
REMARK 465     SER H     6                                                      
REMARK 465     ARG H     7                                                      
REMARK 465     GLU H     8                                                      
REMARK 465     MET H   196                                                      
REMARK 465     VAL H   197                                                      
REMARK 465     ALA H   198                                                      
REMARK 465     TYR H   199                                                      
REMARK 465     LYS H   200                                                      
REMARK 465     ILE H   201                                                      
REMARK 465     PRO H   202                                                      
REMARK 465     VAL H   203                                                      
REMARK 465     ASN H   204                                                      
REMARK 465     ASP H   205                                                      
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     ASP A 205    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ALA B  11    CA   C    O    CB                                   
REMARK 470     ASP C 205    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     SER D 195    CA   C    O    CB   OG                              
REMARK 470     SER E 195    CA   C    O    CB   OG                              
REMARK 470     ASP F 205    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ALA G  11    CA   C    O    CB                                   
REMARK 470     SER H 195    CA   C    O    CB   OG                              
REMARK 470     VAL I  12    CA   C    O    CB   CG1  CG2                        
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   NE2  HIS A    -3     CE1  HIS F    -3              2.16            
REMARK 500   NH1  ARG E    14     OE1  GLU E   127              2.18            
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   OD1  ASP C    74     NZ   LYS E    63     2455     2.16            
REMARK 500   N    ASN C   204     NZ   LYS E    78     4545     2.13            
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    HIS A  -4   CB    HIS A  -4   CG      0.126                       
REMARK 500    HIS C  -4   CB    HIS C  -4   CG      0.115                       
REMARK 500    HIS C  -3   C     HIS C  -3   O      -0.148                       
REMARK 500    GLU D  18   CB    GLU D  18   CG     -0.114                       
REMARK 500    LEU D  54   CG    LEU D  54   CD1    -0.260                       
REMARK 500    LEU D  54   CG    LEU D  54   CD2    -0.226                       
REMARK 500    TYR D  77   CD1   TYR D  77   CE1    -0.127                       
REMARK 500    TYR D  77   CD2   TYR D  77   CE2    -0.096                       
REMARK 500    LYS D  78   CD    LYS D  78   CE     -0.160                       
REMARK 500    ASP D 160   CB    ASP D 160   CG     -0.132                       
REMARK 500    GLU E  18   CB    GLU E  18   CG     -0.133                       
REMARK 500    GLU E  70   CG    GLU E  70   CD     -0.131                       
REMARK 500    TYR E  77   CD1   TYR E  77   CE1    -0.159                       
REMARK 500    TYR E  77   CE2   TYR E  77   CZ     -0.086                       
REMARK 500    LYS E 122   CB    LYS E 122   CG     -0.207                       
REMARK 500    LYS E 122   CD    LYS E 122   CE     -0.153                       
REMARK 500    ASP E 158   CB    ASP E 158   CG     -0.153                       
REMARK 500    LYS E 159   CB    LYS E 159   CG     -0.180                       
REMARK 500    ASP E 160   CB    ASP E 160   CG     -0.142                       
REMARK 500    HIS F  -4   CB    HIS F  -4   CG      0.115                       
REMARK 500    HIS F  -3   C     HIS F  -3   O      -0.160                       
REMARK 500    GLU H  18   CB    GLU H  18   CG     -0.205                       
REMARK 500    GLU H  18   CD    GLU H  18   OE2    -0.090                       
REMARK 500    LYS H 122   CB    LYS H 122   CG     -0.165                       
REMARK 500    ASP H 158   CB    ASP H 158   CG     -0.161                       
REMARK 500    LYS H 159   CB    LYS H 159   CG     -0.168                       
REMARK 500    LYS H 159   CD    LYS H 159   CE     -0.181                       
REMARK 500    ASP H 160   CB    ASP H 160   CG     -0.147                       
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    HIS A  -3   N   -  CA  -  C   ANGL. DEV. =  31.4 DEGREES          
REMARK 500    HIS A  -2   N   -  CA  -  CB  ANGL. DEV. = -11.1 DEGREES          
REMARK 500    HIS C  -3   N   -  CA  -  C   ANGL. DEV. =  39.3 DEGREES          
REMARK 500    HIS C  -3   C   -  N   -  CA  ANGL. DEV. = -16.1 DEGREES          
REMARK 500    HIS C  -2   N   -  CA  -  CB  ANGL. DEV. = -16.6 DEGREES          
REMARK 500    CYS C 106   CA  -  CB  -  SG  ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ARG D  14   CD  -  NE  -  CZ  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG D  14   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    LEU D  54   CD1 -  CG  -  CD2 ANGL. DEV. = -25.3 DEGREES          
REMARK 500    LYS D  78   CB  -  CG  -  CD  ANGL. DEV. = -16.0 DEGREES          
REMARK 500    CYS D 106   CA  -  CB  -  SG  ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP D 158   CB  -  CG  -  OD1 ANGL. DEV. = -13.0 DEGREES          
REMARK 500    ASP D 158   CB  -  CG  -  OD2 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP D 160   CB  -  CG  -  OD1 ANGL. DEV. =  -8.1 DEGREES          
REMARK 500    ASP D 160   CB  -  CG  -  OD2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    GLU E  70   CA  -  CB  -  CG  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    TYR E  77   CB  -  CG  -  CD1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TYR E  77   CB  -  CG  -  CD2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    LYS E 122   CG  -  CD  -  CE  ANGL. DEV. = -19.1 DEGREES          
REMARK 500    ASP E 158   CB  -  CG  -  OD1 ANGL. DEV. = -11.9 DEGREES          
REMARK 500    LYS E 159   CB  -  CG  -  CD  ANGL. DEV. = -22.0 DEGREES          
REMARK 500    ASP E 160   CB  -  CG  -  OD1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP E 160   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    HIS F  -3   N   -  CA  -  C   ANGL. DEV. =  42.0 DEGREES          
REMARK 500    HIS F  -2   N   -  CA  -  CB  ANGL. DEV. = -17.6 DEGREES          
REMARK 500    HIS F  -3   O   -  C   -  N   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    CYS F 106   CA  -  CB  -  SG  ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    GLU H  18   CG  -  CD  -  OE1 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLU H  18   OE1 -  CD  -  OE2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ASP H 158   CB  -  CG  -  OD1 ANGL. DEV. = -17.6 DEGREES          
REMARK 500    ASP H 158   CB  -  CG  -  OD2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    LYS H 159   CB  -  CG  -  CD  ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ASP H 160   CB  -  CG  -  OD1 ANGL. DEV. =  -9.9 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    HIS A  -4      162.72    173.74                                   
REMARK 500    HIS A  -2       74.57   -156.34                                   
REMARK 500    GLN A   9      -48.34     78.87                                   
REMARK 500    TYR A  49       19.21     58.89                                   
REMARK 500    GLU A  92      -64.85    -94.56                                   
REMARK 500    THR A 157     -158.48   -130.51                                   
REMARK 500    LYS A 159       16.66    -44.31                                   
REMARK 500    THR A 189       -7.71     75.18                                   
REMARK 500    HIS C  -4      156.94    179.31                                   
REMARK 500    HIS C  -2       78.98   -153.07                                   
REMARK 500    GLN C   9      -47.77     70.41                                   
REMARK 500    GLU C  92      -67.99    -98.70                                   
REMARK 500    LYS C 159       16.08    -46.44                                   
REMARK 500    THR C 189       -3.73     77.97                                   
REMARK 500    LYS D  48      136.70   -171.55                                   
REMARK 500    LYS D 108      -43.50   -143.75                                   
REMARK 500    SER D 116       41.58    -82.51                                   
REMARK 500    GLU D 146       37.74   -140.64                                   
REMARK 500    ASP D 158     -166.61    -69.79                                   
REMARK 500    ASN D 177      -25.83    133.67                                   
REMARK 500    GLU D 179     -159.35    105.65                                   
REMARK 500    GLU D 180       47.06    -99.99                                   
REMARK 500    ARG D 182      -44.85     98.18                                   
REMARK 500    GLU E  41        6.18    -63.77                                   
REMARK 500    LYS E  78       37.67   -145.54                                   
REMARK 500    CYS E  79       45.32     36.82                                   
REMARK 500    GLU E 105       71.38   -116.94                                   
REMARK 500    CYS E 106       74.37    -64.45                                   
REMARK 500    ASP E 160      128.04   -179.92                                   
REMARK 500    LYS E 166      -29.09    101.26                                   
REMARK 500    TRP E 167     -128.65    140.51                                   
REMARK 500    GLU E 168       60.41   -100.93                                   
REMARK 500    GLU E 169       18.81    125.01                                   
REMARK 500    PRO E 172      125.87    -37.05                                   
REMARK 500    THR E 176      126.38   -176.13                                   
REMARK 500    SER E 178       32.14    -55.00                                   
REMARK 500    GLU E 179     -131.12    114.98                                   
REMARK 500    HIS F  -4      156.47    179.97                                   
REMARK 500    GLN F   9      -48.99     79.49                                   
REMARK 500    GLU F  92      -65.25    -95.23                                   
REMARK 500    LYS F 159       11.33    -45.53                                   
REMARK 500    THR F 189       -4.88     73.79                                   
REMARK 500    TYR H  49       29.77     45.92                                   
REMARK 500    LEU H 161      156.43    173.24                                   
REMARK 500    PRO H 164       95.08    -65.69                                   
REMARK 500    GLU H 165       52.51     84.72                                   
REMARK 500    TRP H 167      176.35    118.42                                   
REMARK 500    GLU H 168      100.09    -49.77                                   
REMARK 500    SER H 170      175.00     61.72                                   
REMARK 500    THR H 176      -97.21   -102.16                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      53 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 VAL H  162     VAL H  163                  127.67                    
REMARK 500 VAL H  163     PRO H  164                  132.05                    
REMARK 500 PRO H  164     GLU H  165                  145.07                    
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    HIS A  -3         0.10    SIDE CHAIN                              
REMARK 500    TRP E 167         0.06    SIDE CHAIN                              
REMARK 500    ARG E 184         0.14    SIDE CHAIN                              
REMARK 500    HIS F  -5         0.16    SIDE CHAIN                              
REMARK 500    HIS F  -2         0.09    SIDE CHAIN                              
REMARK 500    ARG H 184         0.12    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    HIS A  -3        -11.85                                           
REMARK 500    HIS C  -3        -13.97                                           
REMARK 500    HIS F  -3        -14.99                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A  -3        11.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS A  -2        47.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS C  -3        10.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS C  -2        48.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS C 159        24.6      L          L   OUTSIDE RANGE           
REMARK 500    HIS F  -3         7.5      L          L   EXPECTING SP3           
REMARK 500    HIS F  -2        48.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DUJ   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY                          
REMARK 900  CHECKPOINTPROTEIN HUMAN MAD2                                        
REMARK 900 RELATED ID: 1GO4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MAD1-MAD2 REVEALS A                            
REMARK 900  CONSERVED MAD2 BINDING MOTIF IN MAD1 AND                            
REMARK 900  CDC20.                                                              
REMARK 900 RELATED ID: 1KLQ   RELATED DB: PDB                                   
REMARK 900  THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES                       
REMARK 900   SIMILAR MAJORCONFORMATIONAL CHANGES UPON                           
REMARK 900  BINDING TO EITHER MAD1 OR CDC20                                     
REMARK 900 RELATED ID: 1S2H   RELATED DB: PDB                                   
REMARK 900  THE MAD2 SPINDLE CHECKPOINT PROTEIN POSSESSES                       
REMARK 900   TWO DISTINCTNATIVELY FOLDED STATES                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 N-TERMINAL HISTIDINE TAG IN CHAINS A, C, F.                          
REMARK 999 N-TERMINAL HISTIDINE TAG AND SUBSTITUTION OF RESIDUES 109-           
REMARK 999 117 WITH GSG IN CHAINS D, E, H.                                      
DBREF  2V64 A   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 A    2   205  UNP    Q13257   MD2L1_HUMAN      2    205             
DBREF  2V64 B    1    12  PDB    2V64     2V64             1     12             
DBREF  2V64 C   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 C    2   205  UNP    Q13257   MD2L1_HUMAN      2    205             
DBREF  2V64 D   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 D    2   108  UNP    Q13257   MD2L1_HUMAN      2    108             
DBREF  2V64 D  115   117  PDB    2V64     2V64           115    117             
DBREF  2V64 D  118   205  UNP    Q13257   MD2L1_HUMAN    118    205             
DBREF  2V64 E   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 E    2   108  UNP    Q13257   MD2L1_HUMAN      2    108             
DBREF  2V64 E  115   117  PDB    2V64     2V64           115    117             
DBREF  2V64 E  118   205  UNP    Q13257   MD2L1_HUMAN    118    205             
DBREF  2V64 F   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 F    2   205  UNP    Q13257   MD2L1_HUMAN      2    205             
DBREF  2V64 G    1    12  PDB    2V64     2V64             1     12             
DBREF  2V64 H   -7     1  PDB    2V64     2V64            -7      1             
DBREF  2V64 H    2   108  UNP    Q13257   MD2L1_HUMAN      2    108             
DBREF  2V64 H  115   117  PDB    2V64     2V64           115    117             
DBREF  2V64 H  118   205  UNP    Q13257   MD2L1_HUMAN    118    205             
DBREF  2V64 I    1    12  PDB    2V64     2V64             1     12             
SEQRES   1 A  213  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 A  213  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 A  213  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 A  213  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 A  213  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 A  213  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 A  213  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 A  213  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 A  213  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS THR          
SEQRES  10 A  213  ALA LYS ASP ASP SER ALA PRO ARG GLU LYS SER GLN LYS          
SEQRES  11 A  213  ALA ILE GLN ASP GLU ILE ARG SER VAL ILE ARG GLN ILE          
SEQRES  12 A  213  THR ALA THR VAL THR PHE LEU PRO LEU LEU GLU VAL SER          
SEQRES  13 A  213  CYS SER PHE ASP LEU LEU ILE TYR THR ASP LYS ASP LEU          
SEQRES  14 A  213  VAL VAL PRO GLU LYS TRP GLU GLU SER GLY PRO GLN PHE          
SEQRES  15 A  213  ILE THR ASN SER GLU GLU VAL ARG LEU ARG SER PHE THR          
SEQRES  16 A  213  THR THR ILE HIS LYS VAL ASN SER MET VAL ALA TYR LYS          
SEQRES  17 A  213  ILE PRO VAL ASN ASP                                          
SEQRES   1 B   12  SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL              
SEQRES   1 C  213  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 C  213  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 C  213  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 C  213  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 C  213  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 C  213  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 C  213  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 C  213  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 C  213  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS THR          
SEQRES  10 C  213  ALA LYS ASP ASP SER ALA PRO ARG GLU LYS SER GLN LYS          
SEQRES  11 C  213  ALA ILE GLN ASP GLU ILE ARG SER VAL ILE ARG GLN ILE          
SEQRES  12 C  213  THR ALA THR VAL THR PHE LEU PRO LEU LEU GLU VAL SER          
SEQRES  13 C  213  CYS SER PHE ASP LEU LEU ILE TYR THR ASP LYS ASP LEU          
SEQRES  14 C  213  VAL VAL PRO GLU LYS TRP GLU GLU SER GLY PRO GLN PHE          
SEQRES  15 C  213  ILE THR ASN SER GLU GLU VAL ARG LEU ARG SER PHE THR          
SEQRES  16 C  213  THR THR ILE HIS LYS VAL ASN SER MET VAL ALA TYR LYS          
SEQRES  17 C  213  ILE PRO VAL ASN ASP                                          
SEQRES   1 D  207  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 D  207  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 D  207  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 D  207  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 D  207  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 D  207  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 D  207  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 D  207  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 D  207  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS GLY          
SEQRES  10 D  207  SER GLY GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 D  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 D  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 D  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 D  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 D  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 D  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 E  207  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 E  207  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 E  207  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 E  207  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 E  207  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 E  207  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 E  207  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 E  207  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 E  207  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS GLY          
SEQRES  10 E  207  SER GLY GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 E  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 E  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 E  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 E  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 E  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 E  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 F  213  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 F  213  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 F  213  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 F  213  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 F  213  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 F  213  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 F  213  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 F  213  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 F  213  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS THR          
SEQRES  10 F  213  ALA LYS ASP ASP SER ALA PRO ARG GLU LYS SER GLN LYS          
SEQRES  11 F  213  ALA ILE GLN ASP GLU ILE ARG SER VAL ILE ARG GLN ILE          
SEQRES  12 F  213  THR ALA THR VAL THR PHE LEU PRO LEU LEU GLU VAL SER          
SEQRES  13 F  213  CYS SER PHE ASP LEU LEU ILE TYR THR ASP LYS ASP LEU          
SEQRES  14 F  213  VAL VAL PRO GLU LYS TRP GLU GLU SER GLY PRO GLN PHE          
SEQRES  15 F  213  ILE THR ASN SER GLU GLU VAL ARG LEU ARG SER PHE THR          
SEQRES  16 F  213  THR THR ILE HIS LYS VAL ASN SER MET VAL ALA TYR LYS          
SEQRES  17 F  213  ILE PRO VAL ASN ASP                                          
SEQRES   1 G   12  SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL              
SEQRES   1 H  207  MET HIS HIS HIS HIS HIS HIS GLY SER ALA LEU GLN LEU          
SEQRES   2 H  207  SER ARG GLU GLN GLY ILE THR LEU ARG GLY SER ALA GLU          
SEQRES   3 H  207  ILE VAL ALA GLU PHE PHE SER PHE GLY ILE ASN SER ILE          
SEQRES   4 H  207  LEU TYR GLN ARG GLY ILE TYR PRO SER GLU THR PHE THR          
SEQRES   5 H  207  ARG VAL GLN LYS TYR GLY LEU THR LEU LEU VAL THR THR          
SEQRES   6 H  207  ASP LEU GLU LEU ILE LYS TYR LEU ASN ASN VAL VAL GLU          
SEQRES   7 H  207  GLN LEU LYS ASP TRP LEU TYR LYS CYS SER VAL GLN LYS          
SEQRES   8 H  207  LEU VAL VAL VAL ILE SER ASN ILE GLU SER GLY GLU VAL          
SEQRES   9 H  207  LEU GLU ARG TRP GLN PHE ASP ILE GLU CYS ASP LYS GLY          
SEQRES  10 H  207  SER GLY GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE          
SEQRES  11 H  207  ARG SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE          
SEQRES  12 H  207  LEU PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU          
SEQRES  13 H  207  ILE TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP          
SEQRES  14 H  207  GLU GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU          
SEQRES  15 H  207  VAL ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL          
SEQRES  16 H  207  ASN SER MET VAL ALA TYR LYS ILE PRO VAL ASN ASP              
SEQRES   1 I   12  SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL              
FORMUL  10  HOH   *6(H2 O)                                                      
HELIX    1   1 SER A    1  GLN A    9  1                                   9    
HELIX    2   2 THR A   12  ARG A   35  1                                  24    
HELIX    3   3 PRO A   39  GLU A   41  5                                   3    
HELIX    4   4 ASP A   58  LYS A   78  1                                  21    
HELIX    5   5 LYS A  108  ASP A  113  5                                   6    
HELIX    6   6 SER A  120  THR A  138  1                                  19    
HELIX    7   7 VAL A  139  PHE A  141  5                                   3    
HELIX    8   8 SER C    1  GLN C    9  1                                   9    
HELIX    9   9 THR C   12  ARG C   35  1                                  24    
HELIX   10  10 PRO C   39  GLU C   41  5                                   3    
HELIX   11  11 ASP C   58  LYS C   78  1                                  21    
HELIX   12  12 THR C  109  ASP C  113  5                                   5    
HELIX   13  13 SER C  120  THR C  138  1                                  19    
HELIX   14  14 SER D   16  ARG D   35  1                                  20    
HELIX   15  15 PRO D   39  GLU D   41  5                                   3    
HELIX   16  16 ASP D   58  TYR D   77  1                                  20    
HELIX   17  17 SER D  120  THR D  140  1                                  21    
HELIX   18  18 SER E   16  ARG E   35  1                                  20    
HELIX   19  19 PRO E   39  GLU E   41  5                                   3    
HELIX   20  20 ASP E   58  TYR E   77  1                                  20    
HELIX   21  21 SER E  120  THR E  140  1                                  21    
HELIX   22  22 SER F    1  GLN F    9  1                                   9    
HELIX   23  23 THR F   12  ARG F   35  1                                  24    
HELIX   24  24 PRO F   39  GLU F   41  5                                   3    
HELIX   25  25 ASP F   58  LYS F   78  1                                  21    
HELIX   26  26 LYS F  108  ASP F  113  5                                   6    
HELIX   27  27 SER F  120  THR F  138  1                                  19    
HELIX   28  28 VAL F  139  PHE F  141  5                                   3    
HELIX   29  29 SER H   16  ARG H   35  1                                  20    
HELIX   30  30 PRO H   39  GLU H   41  5                                   3    
HELIX   31  31 ASP H   58  TYR H   77  1                                  20    
HELIX   32  32 SER H  120  THR H  140  1                                  21    
SHEET    1  AA 2 PHE A  43  LYS A  48  0                                        
SHEET    2  AA 2 LEU A  51  THR A  56 -1  O  LEU A  51   N  LYS A  48           
SHEET    1  AB 7 GLU A 168  SER A 170  0                                        
SHEET    2  AB 7 TRP B   2  SER B   4 -1  O  TRP B   2   N  SER A 170           
SHEET    3  AB 7 CYS A 149  THR A 157 -1  O  ILE A 155   N  TYR B   3           
SHEET    4  AB 7 VAL A  81  ASN A  90 -1  N  GLN A  82   O  TYR A 156           
SHEET    5  AB 7 VAL A  96  CYS A 106 -1  N  LEU A  97   O  ILE A  88           
SHEET    6  AB 7 HIS A 191  LYS A 200 -1  O  LYS A 192   N  GLU A 105           
SHEET    7  AB 7 SER A 178  THR A 187 -1  O  GLU A 179   N  TYR A 199           
SHEET    1  CA 2 PHE C  43  LYS C  48  0                                        
SHEET    2  CA 2 LEU C  51  THR C  56 -1  O  LEU C  51   N  LYS C  48           
SHEET    1  CB 7 GLU C 168  SER C 170  0                                        
SHEET    2  CB 7 TRP I   2  TYR I   5 -1  O  TRP I   2   N  SER C 170           
SHEET    3  CB 7 CYS C 149  THR C 157 -1  O  LEU C 153   N  TYR I   5           
SHEET    4  CB 7 VAL C  81  ASN C  90 -1  N  GLN C  82   O  TYR C 156           
SHEET    5  CB 7 VAL C  96  CYS C 106 -1  N  LEU C  97   O  ILE C  88           
SHEET    6  CB 7 HIS C 191  LYS C 200 -1  O  LYS C 192   N  GLU C 105           
SHEET    7  CB 7 SER C 178  THR C 187 -1  O  GLU C 179   N  TYR C 199           
SHEET    1  DA 6 ILE D  11  GLY D  15  0                                        
SHEET    2  DA 6 VAL D  96  CYS D 106  1  O  GLN D 101   N  ILE D  11           
SHEET    3  DA 6 VAL D  81  ASN D  90 -1  O  GLN D  82   N  ILE D 104           
SHEET    4  DA 6 CYS D 149  THR D 157 -1  O  SER D 150   N  SER D  89           
SHEET    5  DA 6 LEU D 183  LYS D 192  1  N  ARG D 184   O  CYS D 149           
SHEET    6  DA 6 GLN D 173  ILE D 175 -1  O  PHE D 174   N  PHE D 186           
SHEET    1  DB 2 PHE D  43  LYS D  48  0                                        
SHEET    2  DB 2 LEU D  51  THR D  56 -1  O  LEU D  51   N  LYS D  48           
SHEET    1  EA 6 ILE E  11  ARG E  14  0                                        
SHEET    2  EA 6 VAL E  96  GLU E 105  1  O  GLN E 101   N  ILE E  11           
SHEET    3  EA 6 VAL E  81  ASN E  90 -1  O  GLN E  82   N  ILE E 104           
SHEET    4  EA 6 CYS E 149  THR E 157 -1  O  SER E 150   N  SER E  89           
SHEET    5  EA 6 LEU E 183  LYS E 192  1  N  ARG E 184   O  CYS E 149           
SHEET    6  EA 6 GLN E 173  ILE E 175 -1  O  PHE E 174   N  PHE E 186           
SHEET    1  EB 2 PHE E  43  LYS E  48  0                                        
SHEET    2  EB 2 LEU E  51  THR E  56 -1  O  LEU E  51   N  LYS E  48           
SHEET    1  FA 2 PHE F  43  LYS F  48  0                                        
SHEET    2  FA 2 LEU F  51  THR F  56 -1  O  LEU F  51   N  LYS F  48           
SHEET    1  FB 7 GLU F 168  SER F 170  0                                        
SHEET    2  FB 7 TRP G   2  SER G   4 -1  O  TRP G   2   N  SER F 170           
SHEET    3  FB 7 CYS F 149  THR F 157 -1  O  ILE F 155   N  TYR G   3           
SHEET    4  FB 7 VAL F  81  ASN F  90 -1  N  GLN F  82   O  TYR F 156           
SHEET    5  FB 7 VAL F  96  CYS F 106 -1  N  LEU F  97   O  ILE F  88           
SHEET    6  FB 7 HIS F 191  LYS F 200 -1  O  LYS F 192   N  GLU F 105           
SHEET    7  FB 7 SER F 178  THR F 187 -1  O  GLU F 179   N  TYR F 199           
SHEET    1  HA 6 ILE H  11  GLY H  15  0                                        
SHEET    2  HA 6 VAL H  96  CYS H 106  1  O  GLN H 101   N  ILE H  11           
SHEET    3  HA 6 VAL H  81  ASN H  90 -1  O  GLN H  82   N  ILE H 104           
SHEET    4  HA 6 CYS H 149  THR H 157 -1  O  SER H 150   N  SER H  89           
SHEET    5  HA 6 LEU H 183  LYS H 192  1  N  ARG H 184   O  CYS H 149           
SHEET    6  HA 6 GLN H 173  ILE H 175 -1  O  PHE H 174   N  PHE H 186           
SHEET    1  HB 2 PHE H  43  LYS H  48  0                                        
SHEET    2  HB 2 LEU H  51  THR H  56 -1  O  LEU H  51   N  LYS H  48           
SSBOND   1 CYS A   79    CYS A  106                          1555   1555  2.03  
SSBOND   2 CYS C   79    CYS C  106                          1555   1555  2.03  
SSBOND   3 CYS D   79    CYS D  106                          1555   1555  2.03  
SSBOND   4 CYS F   79    CYS F  106                          1555   1555  2.03  
CRYST1  112.580  111.880  131.760  90.00  90.00  90.00 P 21 21 21   12          
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      0.008883  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008938  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007590        0.00000                         
MTRIX1   1 -0.339060 -0.240220  0.909580       -7.24540    1                    
MTRIX2   1  0.906720  0.174310  0.384030        2.38500    1                    
MTRIX3   1 -0.250800  0.954940  0.158710        0.48970    1                    
MTRIX1   2 -0.342870  0.906200 -0.247490       -2.92110    1                    
MTRIX2   2 -0.259190  0.161980  0.952150        5.39610    1                    
MTRIX3   2  0.902920  0.390610  0.179340       -4.08500    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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