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Database: PDB
Entry: 2QYF
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Original site: 2QYF 
HEADER    CELL CYCLE                              14-AUG-07   2QYF              
TITLE     CRYSTAL STRUCTURE OF THE MAD2/P31(COMET)/MAD2-BINDING PEPTIDE TERNARY 
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A;         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: MAD2-LIKE 1, HSMAD2;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: MAD2L1-BINDING PROTEIN;                                    
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 36-274;                                       
COMPND  11 SYNONYM: CAUGHT BY MAD2 PROTEIN;                                     
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PEPTIDE;                                                   
COMPND  15 CHAIN: E, F;                                                         
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAD2L1, MAD2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: MAD2L1BP, CMT2, KIAA0110;                                      
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PETDUET-1;                                
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 SYNTHETIC: YES;                                                      
SOURCE  23 OTHER_DETAILS: SYNTHETIC 12-MER                                      
KEYWDS    PROTEIN-PEPTIDE COMPLEX, MAD2 FAMILY, SPINDLE ASSEMBLY CHECKPOINT,    
KEYWDS   2 CELL CYCLE, CELL DIVISION, MITOSIS, NUCLEUS, PHOSPHORYLATION         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.R.TOMCHICK,X.LUO                                                    
REVDAT   3   18-SEP-13 2QYF    1       REMARK VERSN                             
REVDAT   2   24-FEB-09 2QYF    1       VERSN                                    
REVDAT   1   29-JAN-08 2QYF    0                                                
JRNL        AUTH   M.YANG,B.LI,D.R.TOMCHICK,M.MACHIUS,J.RIZO,H.YU,X.LUO         
JRNL        TITL   P31COMET BLOCKS MAD2 ACTIVATION THROUGH STRUCTURAL MIMICRY.  
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 131   744 2007              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   18022368                                                     
JRNL        DOI    10.1016/J.CELL.2007.08.048                                   
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   X.LUO,Z.TANG,G.XIA,K.WASSMANN,T.MATSUMOTO,J.RIZO,H.YU        
REMARK   1  TITL   THE MAD2 SPINDLE CHECKPOINT PROTEIN HAS TWO DISTINCT         
REMARK   1  TITL 2 NATIVELY FOLDED STATES.                                      
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  11   338 2004              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1  PMID   15024386                                                     
REMARK   1  DOI    10.1038/NSMB748                                              
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   X.LUO,Z.TANG,J.RIZO,H.YU                                     
REMARK   1  TITL   THE MAD2 SPINDLE CHECKPOINT PROTEIN UNDERGOES SIMILAR MAJOR  
REMARK   1  TITL 2 CONFORMATIONAL CHANGES UPON BINDING TO EITHER MAD1 OR CDC20  
REMARK   1  REF    MOL.CELL                      V.   9    59 2002              
REMARK   1  REFN                   ISSN 1097-2765                               
REMARK   1  PMID   11804586                                                     
REMARK   1  DOI    10.1016/S1097-2765(01)00435-X                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   X.LUO,G.FANG,M.COLDIRON,Y.LIN,H.YU,M.W.KIRSCHNER,G.WAGNER    
REMARK   1  TITL   STRUCTURE OF THE MAD2 SPINDLE ASSEMBLY CHECKPOINT PROTEIN    
REMARK   1  TITL 2 AND ITS INTERACTION WITH CDC20.                              
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.   7   224 2000              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1  PMID   10700282                                                     
REMARK   1  DOI    10.1038/73338                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 42193                          
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 + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1771                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3156                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1990                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6286                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 658                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.16000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 0.79000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.306         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.160         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.432         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6433 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8728 ; 1.552 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   768 ; 6.782 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   291 ;36.993 ;23.608       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1116 ;15.310 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;20.179 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   988 ; 0.103 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4823 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3100 ; 0.213 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4422 ; 0.308 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   559 ; 0.185 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.193 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.232 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4037 ; 2.098 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6357 ; 3.106 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2765 ; 2.136 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2371 ; 3.020 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2QYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044201.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97912                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44434                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% (W/V) PEG 3350, 16% (V/V)            
REMARK 280  GLYCEROL, 125 MM SODIUM PHOSPHATE (PH 5.0), 100 MM NACL, 25 MM      
REMARK 280  DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K                
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       34.33350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.41250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.25950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.41250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.33350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.25950            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     MSE B    35                                                      
REMARK 465     THR B    36                                                      
REMARK 465     SER B    37                                                      
REMARK 465     SER B    38                                                      
REMARK 465     THR B    39                                                      
REMARK 465     GLN B    40                                                      
REMARK 465     GLU B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     LEU B    43                                                      
REMARK 465     ASN B    44                                                      
REMARK 465     ALA B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     GLU B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     PHE B    49                                                      
REMARK 465     CYS B    50                                                      
REMARK 465     PRO B    51                                                      
REMARK 465     ARG B    52                                                      
REMARK 465     ASP B    53                                                      
REMARK 465     SER B    65                                                      
REMARK 465     PHE B    97                                                      
REMARK 465     TYR B    98                                                      
REMARK 465     ARG B    99                                                      
REMARK 465     LYS B   100                                                      
REMARK 465     PRO B   101                                                      
REMARK 465     SER B   102                                                      
REMARK 465     PRO B   103                                                      
REMARK 465     GLN B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     GLU B   106                                                      
REMARK 465     GLU B   107                                                      
REMARK 465     MSE B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     LYS B   110                                                      
REMARK 465     LYS B   111                                                      
REMARK 465     LYS B   112                                                      
REMARK 465     PRO B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     ALA B   115                                                      
REMARK 465     THR B   116                                                      
REMARK 465     THR B   117                                                      
REMARK 465     GLU B   118                                                      
REMARK 465     VAL B   119                                                      
REMARK 465     SER B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     ARG B   122                                                      
REMARK 465     LYS B   123                                                      
REMARK 465     TYR B   175                                                      
REMARK 465     SER B   176                                                      
REMARK 465     VAL B   177                                                      
REMARK 465     ARG B   273                                                      
REMARK 465     GLU B   274                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     LEU C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     ARG C     7                                                      
REMARK 465     GLU C     8                                                      
REMARK 465     GLN C     9                                                      
REMARK 465     GLY C    10                                                      
REMARK 465     ILE C    11                                                      
REMARK 465     LYS C   108                                                      
REMARK 465     THR C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     LYS C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     ALA C   115                                                      
REMARK 465     PRO C   116                                                      
REMARK 465     ARG C   117                                                      
REMARK 465     GLU C   118                                                      
REMARK 465     MSE D    35                                                      
REMARK 465     THR D    36                                                      
REMARK 465     SER D    37                                                      
REMARK 465     SER D    38                                                      
REMARK 465     THR D    39                                                      
REMARK 465     GLN D    40                                                      
REMARK 465     GLU D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     LEU D    43                                                      
REMARK 465     ASN D    44                                                      
REMARK 465     ALA D    45                                                      
REMARK 465     SER D    46                                                      
REMARK 465     GLU D    47                                                      
REMARK 465     ALA D    48                                                      
REMARK 465     PHE D    49                                                      
REMARK 465     CYS D    50                                                      
REMARK 465     PRO D    51                                                      
REMARK 465     ARG D    52                                                      
REMARK 465     ASP D    53                                                      
REMARK 465     PHE D    97                                                      
REMARK 465     TYR D    98                                                      
REMARK 465     ARG D    99                                                      
REMARK 465     LYS D   100                                                      
REMARK 465     PRO D   101                                                      
REMARK 465     SER D   102                                                      
REMARK 465     PRO D   103                                                      
REMARK 465     GLN D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     GLU D   106                                                      
REMARK 465     GLU D   107                                                      
REMARK 465     MSE D   108                                                      
REMARK 465     LEU D   109                                                      
REMARK 465     LYS D   110                                                      
REMARK 465     LYS D   111                                                      
REMARK 465     LYS D   112                                                      
REMARK 465     PRO D   113                                                      
REMARK 465     ARG D   114                                                      
REMARK 465     ALA D   115                                                      
REMARK 465     THR D   116                                                      
REMARK 465     THR D   117                                                      
REMARK 465     GLU D   118                                                      
REMARK 465     PRO D   174                                                      
REMARK 465     TYR D   175                                                      
REMARK 465     SER D   176                                                      
REMARK 465     VAL D   177                                                      
REMARK 465     ASP D   178                                                      
REMARK 465     GLN D   179                                                      
REMARK 465     SER D   180                                                      
REMARK 465     GLU D   274                                                      
REMARK 465     VAL E    12                                                      
REMARK 465     ALA F    11                                                      
REMARK 465     VAL F    12                                                      
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    THR A 189      -18.39     90.96                                   
REMARK 500    PRO B  61        3.77    -69.92                                   
REMARK 500    CYS B 247       45.79   -148.85                                   
REMARK 500    PRO B 250      -65.03    -90.89                                   
REMARK 500    LEU C 161      171.89    -41.55                                   
REMARK 500    THR C 189      -19.80     84.68                                   
REMARK 500    PRO D  61       27.33    -77.24                                   
REMARK 500    LEU D 171        0.64    -63.33                                   
REMARK 500    SER D 251      -35.84   -138.23                                   
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 LEU D  181     SER D  182                  143.77                    
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    VAL B  64        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 319        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 348        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH B 422        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH C 322        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH D 364        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH D 387        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D 397        DISTANCE =  5.71 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1S2H   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE CLOSED CONFORMATION OF THE             
REMARK 900 MAD2 PROTEIN.                                                        
REMARK 900 RELATED ID: 1KLQ   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE MAD2 PROTEIN COMPLEXED TO A            
REMARK 900 MAD2-BINDING PEPTIDE.                                                
REMARK 900 RELATED ID: 1DUJ   RELATED DB: PDB                                   
REMARK 900 SOLUTION NMR STRUCTURE OF THE OPEN CONFORMATION OF THE MAD2          
REMARK 900 PROTEIN.                                                             
DBREF  2QYF A    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2QYF B   36   274  UNP    Q15013   MD2BP_HUMAN     36    274             
DBREF  2QYF C    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  2QYF D   36   274  UNP    Q15013   MD2BP_HUMAN     36    274             
DBREF  2QYF E    1    12  PDB    2QYF     2QYF             1     12             
DBREF  2QYF F    1    12  PDB    2QYF     2QYF             1     12             
SEQADV 2QYF GLY A    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 2QYF ALA A   13  UNP  Q13257    LEU    13 ENGINEERED                     
SEQADV 2QYF MSE B   35  UNP  Q15013              EXPRESSION TAG                 
SEQADV 2QYF GLY C    0  UNP  Q13257              EXPRESSION TAG                 
SEQADV 2QYF ALA C   13  UNP  Q13257    LEU    13 ENGINEERED                     
SEQADV 2QYF MSE D   35  UNP  Q15013              EXPRESSION TAG                 
SEQRES   1 A  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 A  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 A  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 A  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 A  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 A  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 A  206  LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 A  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 A  206  ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 A  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 A  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 A  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 A  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 A  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 A  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 A  206  SER MSE VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 B  240  MSE THR SER SER THR GLN GLU PRO LEU ASN ALA SER GLU          
SEQRES   2 B  240  ALA PHE CYS PRO ARG ASP CYS MSE VAL PRO VAL VAL PHE          
SEQRES   3 B  240  PRO GLY PRO VAL SER GLN GLU GLY CYS CYS GLN PHE THR          
SEQRES   4 B  240  CYS GLU LEU LEU LYS HIS ILE MSE TYR GLN ARG GLN GLN          
SEQRES   5 B  240  LEU PRO LEU PRO TYR GLU GLN LEU LYS HIS PHE TYR ARG          
SEQRES   6 B  240  LYS PRO SER PRO GLN ALA GLU GLU MSE LEU LYS LYS LYS          
SEQRES   7 B  240  PRO ARG ALA THR THR GLU VAL SER SER ARG LYS CYS GLN          
SEQRES   8 B  240  GLN ALA LEU ALA GLU LEU GLU SER VAL LEU SER HIS LEU          
SEQRES   9 B  240  GLU ASP PHE PHE ALA ARG THR LEU VAL PRO ARG VAL LEU          
SEQRES  10 B  240  ILE LEU LEU GLY GLY ASN ALA LEU SER PRO LYS GLU PHE          
SEQRES  11 B  240  TYR GLU LEU ASP LEU SER LEU LEU ALA PRO TYR SER VAL          
SEQRES  12 B  240  ASP GLN SER LEU SER THR ALA ALA CYS LEU ARG ARG LEU          
SEQRES  13 B  240  PHE ARG ALA ILE PHE MSE ALA ASP ALA PHE SER GLU LEU          
SEQRES  14 B  240  GLN ALA PRO PRO LEU MSE GLY THR VAL VAL MSE ALA GLN          
SEQRES  15 B  240  GLY HIS ARG ASN CYS GLY GLU ASP TRP PHE ARG PRO LYS          
SEQRES  16 B  240  LEU ASN TYR ARG VAL PRO SER ARG GLY HIS LYS LEU THR          
SEQRES  17 B  240  VAL THR LEU SER CYS GLY ARG PRO SER ILE ARG THR THR          
SEQRES  18 B  240  ALA TRP GLU ASP TYR ILE TRP PHE GLN ALA PRO VAL THR          
SEQRES  19 B  240  PHE LYS GLY PHE ARG GLU                                      
SEQRES   1 C  206  GLY MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR          
SEQRES   2 C  206  ALA ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER          
SEQRES   3 C  206  PHE GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR          
SEQRES   4 C  206  PRO SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU          
SEQRES   5 C  206  THR LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR          
SEQRES   6 C  206  LEU ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR          
SEQRES   7 C  206  LYS CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN          
SEQRES   8 C  206  ILE GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP          
SEQRES   9 C  206  ILE GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO          
SEQRES  10 C  206  ARG GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG          
SEQRES  11 C  206  SER VAL ILE ARG GLN ILE THR ALA THR VAL THR PHE LEU          
SEQRES  12 C  206  PRO LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE          
SEQRES  13 C  206  TYR THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU          
SEQRES  14 C  206  GLU SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL          
SEQRES  15 C  206  ARG LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN          
SEQRES  16 C  206  SER MSE VAL ALA TYR LYS ILE PRO VAL ASN ASP                  
SEQRES   1 D  240  MSE THR SER SER THR GLN GLU PRO LEU ASN ALA SER GLU          
SEQRES   2 D  240  ALA PHE CYS PRO ARG ASP CYS MSE VAL PRO VAL VAL PHE          
SEQRES   3 D  240  PRO GLY PRO VAL SER GLN GLU GLY CYS CYS GLN PHE THR          
SEQRES   4 D  240  CYS GLU LEU LEU LYS HIS ILE MSE TYR GLN ARG GLN GLN          
SEQRES   5 D  240  LEU PRO LEU PRO TYR GLU GLN LEU LYS HIS PHE TYR ARG          
SEQRES   6 D  240  LYS PRO SER PRO GLN ALA GLU GLU MSE LEU LYS LYS LYS          
SEQRES   7 D  240  PRO ARG ALA THR THR GLU VAL SER SER ARG LYS CYS GLN          
SEQRES   8 D  240  GLN ALA LEU ALA GLU LEU GLU SER VAL LEU SER HIS LEU          
SEQRES   9 D  240  GLU ASP PHE PHE ALA ARG THR LEU VAL PRO ARG VAL LEU          
SEQRES  10 D  240  ILE LEU LEU GLY GLY ASN ALA LEU SER PRO LYS GLU PHE          
SEQRES  11 D  240  TYR GLU LEU ASP LEU SER LEU LEU ALA PRO TYR SER VAL          
SEQRES  12 D  240  ASP GLN SER LEU SER THR ALA ALA CYS LEU ARG ARG LEU          
SEQRES  13 D  240  PHE ARG ALA ILE PHE MSE ALA ASP ALA PHE SER GLU LEU          
SEQRES  14 D  240  GLN ALA PRO PRO LEU MSE GLY THR VAL VAL MSE ALA GLN          
SEQRES  15 D  240  GLY HIS ARG ASN CYS GLY GLU ASP TRP PHE ARG PRO LYS          
SEQRES  16 D  240  LEU ASN TYR ARG VAL PRO SER ARG GLY HIS LYS LEU THR          
SEQRES  17 D  240  VAL THR LEU SER CYS GLY ARG PRO SER ILE ARG THR THR          
SEQRES  18 D  240  ALA TRP GLU ASP TYR ILE TRP PHE GLN ALA PRO VAL THR          
SEQRES  19 D  240  PHE LYS GLY PHE ARG GLU                                      
SEQRES   1 E   12  SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL              
SEQRES   1 F   12  SER TRP TYR SER TYR PRO PRO PRO GLN ARG ALA VAL              
MODRES 2QYF MSE A  196  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE B   55  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE B   81  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE B  196  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE B  209  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE B  214  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE C  196  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE D   55  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE D   81  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE D  196  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE D  209  MET  SELENOMETHIONINE                                   
MODRES 2QYF MSE D  214  MET  SELENOMETHIONINE                                   
HET    MSE  A 196       8                                                       
HET    MSE  B  55       8                                                       
HET    MSE  B  81       8                                                       
HET    MSE  B 196       8                                                       
HET    MSE  B 209       8                                                       
HET    MSE  B 214       8                                                       
HET    MSE  C 196       8                                                       
HET    MSE  D  55       8                                                       
HET    MSE  D  81       8                                                       
HET    MSE  D 196       8                                                       
HET    MSE  D 209       8                                                       
HET    MSE  D 214       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   7  HOH   *658(H2 O)                                                    
HELIX    1   1 THR A   12  ARG A   35  1                                  24    
HELIX    2   2 PRO A   39  GLU A   41  5                                   3    
HELIX    3   3 ASP A   58  LYS A   78  1                                  21    
HELIX    4   4 LYS A  108  ASP A  112  5                                   5    
HELIX    5   5 SER A  120  THR A  138  1                                  19    
HELIX    6   6 VAL A  139  PHE A  141  5                                   3    
HELIX    7   7 LYS A  159  VAL A  163  5                                   5    
HELIX    8   8 GLN B   66  ARG B   84  1                                  19    
HELIX    9   9 PRO B   90  LYS B   95  1                                   6    
HELIX   10  10 GLN B  125  THR B  145  1                                  21    
HELIX   11  11 SER B  182  ALA B  197  1                                  16    
HELIX   12  12 THR C   12  ARG C   35  1                                  24    
HELIX   13  13 PRO C   39  GLU C   41  5                                   3    
HELIX   14  14 ASP C   58  LYS C   78  1                                  21    
HELIX   15  15 SER C  120  THR C  138  1                                  19    
HELIX   16  16 VAL C  139  PHE C  141  5                                   3    
HELIX   17  17 SER D   65  ARG D   84  1                                  20    
HELIX   18  18 PRO D   90  LYS D   95  1                                   6    
HELIX   19  19 VAL D  119  THR D  145  1                                  27    
HELIX   20  20 LEU D  181  ALA D  197  1                                  17    
HELIX   21  21 ASN D  220  GLY D  222  5                                   3    
SHEET    1   A 2 PHE A  43  LYS A  48  0                                        
SHEET    2   A 2 LEU A  51  THR A  56 -1  O  VAL A  55   N  THR A  44           
SHEET    1   B14 GLU A 168  SER A 170  0                                        
SHEET    2   B14 TRP E   2  TYR E   5 -1  O  SER E   4   N  GLU A 168           
SHEET    3   B14 CYS A 149  TYR A 156 -1  N  ILE A 155   O  TYR E   3           
SHEET    4   B14 LYS A  83  ASN A  90 -1  N  VAL A  85   O  LEU A 154           
SHEET    5   B14 VAL A  96  CYS A 106 -1  O  LEU A  97   N  ILE A  88           
SHEET    6   B14 HIS A 191  LYS A 200 -1  O  LYS A 192   N  GLU A 105           
SHEET    7   B14 ASN A 177  ARG A 182 -1  N  GLU A 179   O  TYR A 199           
SHEET    8   B14 SER C 178  ARG C 182 -1  O  GLU C 180   N  SER A 178           
SHEET    9   B14 HIS C 191  LYS C 200 -1  O  VAL C 197   N  VAL C 181           
SHEET   10   B14 VAL C  96  CYS C 106 -1  N  GLU C 105   O  LYS C 192           
SHEET   11   B14 LYS C  83  ASN C  90 -1  N  ILE C  88   O  LEU C  97           
SHEET   12   B14 CYS C 149  TYR C 156 -1  O  LEU C 154   N  VAL C  85           
SHEET   13   B14 TRP F   2  TYR F   5 -1  O  TYR F   3   N  ILE C 155           
SHEET   14   B14 GLU C 168  SER C 170 -1  N  GLU C 168   O  SER F   4           
SHEET    1   C 6 PHE A 186  THR A 187  0                                        
SHEET    2   C 6 HIS A 191  LYS A 200 -1  O  VAL A 193   N  PHE A 186           
SHEET    3   C 6 ASN A 177  ARG A 182 -1  N  GLU A 179   O  TYR A 199           
SHEET    4   C 6 SER C 178  ARG C 182 -1  O  GLU C 180   N  SER A 178           
SHEET    5   C 6 HIS C 191  LYS C 200 -1  O  VAL C 197   N  VAL C 181           
SHEET    6   C 6 PHE C 186  THR C 187 -1  N  PHE C 186   O  VAL C 193           
SHEET    1   D 7 MSE B  55  VAL B  59  0                                        
SHEET    2   D 7 HIS B 239  SER B 246  1  O  THR B 242   N  VAL B  56           
SHEET    3   D 7 GLU B 163  ASP B 168  1  N  ASP B 168   O  VAL B 243           
SHEET    4   D 7 ARG B 149  LEU B 154 -1  N  LEU B 154   O  GLU B 163           
SHEET    5   D 7 GLY B 210  HIS B 218 -1  O  VAL B 212   N  LEU B 153           
SHEET    6   D 7 TYR B 260  GLN B 264 -1  O  ILE B 261   N  GLY B 217           
SHEET    7   D 7 ARG B 227  LYS B 229 -1  N  LYS B 229   O  TRP B 262           
SHEET    1   E 6 MSE B  55  VAL B  59  0                                        
SHEET    2   E 6 HIS B 239  SER B 246  1  O  THR B 242   N  VAL B  56           
SHEET    3   E 6 GLU B 163  ASP B 168  1  N  ASP B 168   O  VAL B 243           
SHEET    4   E 6 ARG B 149  LEU B 154 -1  N  LEU B 154   O  GLU B 163           
SHEET    5   E 6 GLY B 210  HIS B 218 -1  O  VAL B 212   N  LEU B 153           
SHEET    6   E 6 PHE B 269  LYS B 270 -1  O  PHE B 269   N  THR B 211           
SHEET    1   F 2 PHE C  43  LYS C  48  0                                        
SHEET    2   F 2 LEU C  51  THR C  56 -1  O  LEU C  53   N  VAL C  46           
SHEET    1   G 7 MSE D  55  VAL D  59  0                                        
SHEET    2   G 7 HIS D 239  SER D 246  1  O  THR D 244   N  VAL D  58           
SHEET    3   G 7 GLU D 163  ASP D 168  1  N  ASP D 168   O  VAL D 243           
SHEET    4   G 7 ARG D 149  LEU D 154 -1  N  LEU D 154   O  GLU D 163           
SHEET    5   G 7 GLY D 210  HIS D 218 -1  O  MSE D 214   N  LEU D 151           
SHEET    6   G 7 TYR D 260  GLN D 264 -1  O  ILE D 261   N  GLY D 217           
SHEET    7   G 7 ARG D 227  LYS D 229 -1  N  ARG D 227   O  GLN D 264           
SHEET    1   H 6 MSE D  55  VAL D  59  0                                        
SHEET    2   H 6 HIS D 239  SER D 246  1  O  THR D 244   N  VAL D  58           
SHEET    3   H 6 GLU D 163  ASP D 168  1  N  ASP D 168   O  VAL D 243           
SHEET    4   H 6 ARG D 149  LEU D 154 -1  N  LEU D 154   O  GLU D 163           
SHEET    5   H 6 GLY D 210  HIS D 218 -1  O  MSE D 214   N  LEU D 151           
SHEET    6   H 6 PHE D 269  LYS D 270 -1  O  PHE D 269   N  THR D 211           
SSBOND   1 CYS A   79    CYS A  106                          1555   1555  2.09  
LINK         C   SER A 195                 N   MSE A 196     1555   1555  1.32  
LINK         C   MSE A 196                 N   VAL A 197     1555   1555  1.31  
LINK         C   CYS B  54                 N   MSE B  55     1555   1555  1.33  
LINK         C   MSE B  55                 N   VAL B  56     1555   1555  1.34  
LINK         C   ILE B  80                 N   MSE B  81     1555   1555  1.33  
LINK         C   MSE B  81                 N   TYR B  82     1555   1555  1.34  
LINK         C   PHE B 195                 N   MSE B 196     1555   1555  1.34  
LINK         C   MSE B 196                 N   ALA B 197     1555   1555  1.34  
LINK         C   LEU B 208                 N   MSE B 209     1555   1555  1.34  
LINK         C   MSE B 209                 N   GLY B 210     1555   1555  1.33  
LINK         C   VAL B 213                 N   MSE B 214     1555   1555  1.33  
LINK         C   MSE B 214                 N   ALA B 215     1555   1555  1.32  
LINK         C   SER C 195                 N   MSE C 196     1555   1555  1.32  
LINK         C   MSE C 196                 N   VAL C 197     1555   1555  1.32  
LINK         C   CYS D  54                 N   MSE D  55     1555   1555  1.33  
LINK         C   MSE D  55                 N   VAL D  56     1555   1555  1.33  
LINK         C   ILE D  80                 N   MSE D  81     1555   1555  1.33  
LINK         C   MSE D  81                 N   TYR D  82     1555   1555  1.33  
LINK         C   PHE D 195                 N   MSE D 196     1555   1555  1.32  
LINK         C   MSE D 196                 N   ALA D 197     1555   1555  1.34  
LINK         C   LEU D 208                 N   MSE D 209     1555   1555  1.34  
LINK         C   MSE D 209                 N   GLY D 210     1555   1555  1.33  
LINK         C   VAL D 213                 N   MSE D 214     1555   1555  1.32  
LINK         C   MSE D 214                 N   ALA D 215     1555   1555  1.32  
CRYST1   68.667  104.519  138.825  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014563  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009568  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007203        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system