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Database: PDB
Entry: 1GO4
LinkDB: 1GO4
Original site: 1GO4 
HEADER    CELL CYCLE                              17-OCT-01   1GO4              
TITLE     CRYSTAL STRUCTURE OF MAD1-MAD2 REVEALS A CONSERVED MAD2 BINDING MOTIF 
TITLE    2 IN MAD1 AND CDC20.                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A;         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HSMAD2,MITOTIC ARREST DEFICIENT 2-LIKE PROTEIN 1,MAD2-LIKE  
COMPND   5 PROTEIN 1;                                                           
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD1;          
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: RESIDUES 485-584;                                          
COMPND  12 SYNONYM: MITOTIC ARREST DEFICIENT 1-LIKE PROTEIN 1,MAD1-LIKE PROTEIN 
COMPND  13 1,MITOTIC CHECKPOINT MAD1 PROTEIN HOMOLOG,HMAD1,TAX-BINDING PROTEIN  
COMPND  14 181;                                                                 
COMPND  15 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;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: XL1BLUE;                                   
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PQE30;                                    
SOURCE  10 OTHER_DETAILS: DICISTRONIC VECTOR;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: MAD1L1, MAD1, TXBP181;                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: XL1BLUE;                                   
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PQE30;                                    
SOURCE  20 OTHER_DETAILS: DICISTRONIC VECTOR                                    
KEYWDS    MITOTIC SPINDLE CHECKPOINT, CELL CYCLE, MITOSIS, NUCLEAR PRO          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.SIRONI,M.MAPELLI,K.T.JEANG,A.MUSACCHIO                              
REVDAT   6   16-OCT-19 1GO4    1       REMARK                                   
REVDAT   5   08-MAY-19 1GO4    1       REMARK                                   
REVDAT   4   20-JUN-18 1GO4    1       COMPND SOURCE JRNL   DBREF               
REVDAT   3   05-JUL-17 1GO4    1       REMARK                                   
REVDAT   2   24-FEB-09 1GO4    1       VERSN                                    
REVDAT   1   16-MAY-02 1GO4    0                                                
JRNL        AUTH   L.SIRONI,M.MAPELLI,S.KNAPP,A.DE ANTONI,K.T.JEANG,A.MUSACCHIO 
JRNL        TITL   CRYSTAL STRUCTURE OF THE TETRAMERIC MAD1-MAD2 CORE COMPLEX:  
JRNL        TITL 2 IMPLICATIONS OF A 'SAFETY BELT' BINDING MECHANISM FOR THE    
JRNL        TITL 3 SPINDLE CHECKPOINT.                                          
JRNL        REF    EMBO J.                       V.  21  2496 2002              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   12006501                                                     
JRNL        DOI    10.1093/EMBOJ/21.10.2496                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2022904.010                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 112652                         
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) : 0.240                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5665                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.18                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17599                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2780                       
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 946                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9300                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 628                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.63000                                              
REMARK   3    B22 (A**2) : -0.43000                                             
REMARK   3    B33 (A**2) : -2.20000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.20000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.900                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.760                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.670 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.290 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.770 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.820 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 53.04                                                
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   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-OCT-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290008702.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 287.0                              
REMARK 200  PH                             : 5.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113010                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.03800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.960                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SNB                                                   
REMARK 200 STARTING MODEL: 1DUJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN CONCENTRATION 7.5 MG/ML          
REMARK 280  HANGING DROP METHOD, WELL=100 MM AMMONIUM SULPHATE, 100 MM          
REMARK 280  AMMONIUM CITRATE PH 5.2, 10 MM DTT, PH 5.20, VAPOR DIFFUSION,       
REMARK 280  HANGING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.51150            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHAIN A, B, C, D ENGINEERED MUTATION ARG133ALA                       
REMARK 400  REQUIRED FOR THE EXECUTION OF THE MITOTIC CHECKPOINT                
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     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     ASN A   204                                                      
REMARK 465     ASP A   205                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     GLU B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     ASP B   205                                                      
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     ASP C   205                                                      
REMARK 465     MET 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     GLU D     8                                                      
REMARK 465     GLN D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     ASN D   204                                                      
REMARK 465     ASP D   205                                                      
REMARK 465     SER E   485                                                      
REMARK 465     SER E   486                                                      
REMARK 465     ALA E   487                                                      
REMARK 465     GLU E   488                                                      
REMARK 465     GLN E   489                                                      
REMARK 465     SER E   490                                                      
REMARK 465     PHE E   491                                                      
REMARK 465     LEU E   492                                                      
REMARK 465     ARG E   580                                                      
REMARK 465     GLY E   581                                                      
REMARK 465     GLY E   582                                                      
REMARK 465     THR E   583                                                      
REMARK 465     VAL E   584                                                      
REMARK 465     SER F   485                                                      
REMARK 465     SER F   486                                                      
REMARK 465     ALA F   487                                                      
REMARK 465     GLU F   488                                                      
REMARK 465     GLN F   489                                                      
REMARK 465     SER F   490                                                      
REMARK 465     PHE F   491                                                      
REMARK 465     LEU F   492                                                      
REMARK 465     ARG F   580                                                      
REMARK 465     GLY F   581                                                      
REMARK 465     GLY F   582                                                      
REMARK 465     THR F   583                                                      
REMARK 465     VAL F   584                                                      
REMARK 465     SER H   485                                                      
REMARK 465     SER H   486                                                      
REMARK 465     ARG H   580                                                      
REMARK 465     GLY H   581                                                      
REMARK 465     GLY H   582                                                      
REMARK 465     THR H   583                                                      
REMARK 465     VAL H   584                                                      
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   CE2  TYR D    64     O    HOH D  2012              1.52            
REMARK 500   CD1  LEU D   142     O    HOH D  2018              1.52            
REMARK 500   OD2  ASP D   152     O    HOH D  2030              1.57            
REMARK 500   CB   ILE D    62     O    HOH D  2011              1.63            
REMARK 500   N    MET E   578     N    GLU E   579              1.63            
REMARK 500   OG1  THR B    56     O    HOH B  2031              1.69            
REMARK 500   O    LYS A   166     O    HOH A  2075              1.70            
REMARK 500   O    ASP D    58     O    HOH D  2011              1.71            
REMARK 500   CG2  ILE D    62     O    HOH D  2011              1.75            
REMARK 500   N    SER G   546     O    HOH A  2075              1.76            
REMARK 500   O    ASN D   194     O    HOH D  2043              1.76            
REMARK 500   N    ILE C    37     O    HOH C  2035              1.79            
REMARK 500   CZ   ARG E   529     O    HOH E  2018              1.81            
REMARK 500   N    LYS C   166     O    HOH C  2169              1.85            
REMARK 500   NE   ARG E   529     O    HOH E  2018              1.85            
REMARK 500   O    MET G   578     OXT  VAL G   584              1.87            
REMARK 500   NH2  ARG E   529     O    HOH E  2018              1.93            
REMARK 500   OD2  ASP B   160     O    HOH B  2083              1.97            
REMARK 500   O    HOH E  2037     O    HOH E  2047              1.98            
REMARK 500   OE1  GLU D   180     O    HOH D  2037              1.99            
REMARK 500   C    GLY C    36     O    HOH C  2035              2.06            
REMARK 500   O    HOH D  2030     O    HOH H  2022              2.06            
REMARK 500   O    ASP G   536     O    HOH G  2014              2.07            
REMARK 500   O    HOH C  2080     O    HOH C  2157              2.09            
REMARK 500   N    ARG G   539     O    HOH G  2014              2.11            
REMARK 500   NH2  ARG D    35     O    PRO D   143              2.12            
REMARK 500   OE1  GLU C   180     O    HOH C  2197              2.12            
REMARK 500   O    HOH C  2193     O    HOH C  2195              2.12            
REMARK 500   O    HOH C  2190     O    HOH C  2192              2.13            
REMARK 500   O    HOH A  2078     O    HOH A  2086              2.15            
REMARK 500   O    HOH A  2023     O    HOH A  2024              2.16            
REMARK 500   O    HOH E  2037     O    HOH E  2042              2.17            
REMARK 500   O    HOH E  2005     O    HOH E  2031              2.18            
REMARK 500   N    MET H   545     O    HOH H  2022              2.18            
REMARK 500   NE   ARG C   182     O    HOH C  2197              2.18            
REMARK 500   OE1  GLU H   523     O    HOH H  2010              2.18            
REMARK 500   N    THR G   540     O    HOH G  2014              2.19            
REMARK 500   OH   TYR D    64     O    HOH D  2030              2.19            
REMARK 500   OG1  THR D   138     O    HOH D  2029              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A   8   CG    GLU A   8   CD     -0.132                       
REMARK 500    GLN A   9   CG    GLN A   9   CD     -0.147                       
REMARK 500    GLY A  10   N     GLY A  10   CA      0.328                       
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    GLY A  10   C   -  N   -  CA  ANGL. DEV. = -27.8 DEGREES          
REMARK 500    GLY A  10   N   -  CA  -  C   ANGL. DEV. =  23.7 DEGREES          
REMARK 500    CYS B 106   CA  -  CB  -  SG  ANGL. DEV. =   7.0 DEGREES          
REMARK 500    VAL C 203   CA  -  C   -  O   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    VAL C 203   CA  -  C   -  N   ANGL. DEV. = -33.8 DEGREES          
REMARK 500    VAL C 203   O   -  C   -  N   ANGL. DEV. =  17.8 DEGREES          
REMARK 500    ASN C 204   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    LEU D  51   N   -  CA  -  C   ANGL. DEV. = -19.7 DEGREES          
REMARK 500    THR D  52   N   -  CA  -  CB  ANGL. DEV. = -17.8 DEGREES          
REMARK 500    LEU D  59   N   -  CA  -  CB  ANGL. DEV. = -25.6 DEGREES          
REMARK 500    ASN D 194   CB  -  CA  -  C   ANGL. DEV. = -19.4 DEGREES          
REMARK 500    SER D 195   N   -  CA  -  CB  ANGL. DEV. = -43.3 DEGREES          
REMARK 500    SER D 195   N   -  CA  -  C   ANGL. DEV. =  22.0 DEGREES          
REMARK 500    PHE E 493   CB  -  CA  -  C   ANGL. DEV. =  12.8 DEGREES          
REMARK 500    PHE E 493   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    PHE E 493   CB  -  CG  -  CD1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    MET E 578   N   -  CA  -  C   ANGL. DEV. = -17.5 DEGREES          
REMARK 500    MET E 578   CA  -  C   -  N   ANGL. DEV. = -23.9 DEGREES          
REMARK 500    MET E 578   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    THR G 583   N   -  CA  -  C   ANGL. DEV. = -22.7 DEGREES          
REMARK 500    VAL G 584   N   -  CA  -  C   ANGL. DEV. = -26.4 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    GLN A   9       71.35   -156.85                                   
REMARK 500    LYS A 108       -8.00    -57.64                                   
REMARK 500    ALA A 110       -4.72    -59.62                                   
REMARK 500    PRO A 116      158.71    -46.95                                   
REMARK 500    PHE A 141      -20.55   -141.09                                   
REMARK 500    LYS A 166       -9.06     77.13                                   
REMARK 500    ALA B 115      145.08    169.15                                   
REMARK 500    LEU B 183     -147.40   -107.83                                   
REMARK 500    THR B 189       -7.36     80.28                                   
REMARK 500    THR C 189       -8.54     86.43                                   
REMARK 500    PRO C 202      155.74    -44.63                                   
REMARK 500    GLU D  41       29.51    -68.52                                   
REMARK 500    THR D  42       13.02   -142.81                                   
REMARK 500    THR D  44       95.25   -162.26                                   
REMARK 500    TYR D  49     -153.25     52.14                                   
REMARK 500    SER D 114      -15.57   -163.72                                   
REMARK 500    THR D 138       66.09   -108.01                                   
REMARK 500    THR D 140       53.26   -109.18                                   
REMARK 500    PHE D 141      -53.04   -153.68                                   
REMARK 500    PRO D 143      163.56    -46.20                                   
REMARK 500    GLU D 146       33.75    -80.24                                   
REMARK 500    SER D 150     -169.97   -128.81                                   
REMARK 500    LYS D 166       -5.21     80.40                                   
REMARK 500    LEU D 183      -75.14   -110.72                                   
REMARK 500    ARG D 184     -159.11   -158.75                                   
REMARK 500    SER D 185     -173.81   -171.94                                   
REMARK 500    THR D 188      -81.73   -109.71                                   
REMARK 500    THR D 189      -32.47   -158.61                                   
REMARK 500    ALA E 577       56.30    -91.67                                   
REMARK 500    MET E 578      -10.19   -150.03                                   
REMARK 500    SER H 490        5.65    -60.53                                   
REMARK 500    PHE H 491       76.79   -102.71                                   
REMARK 500    PHE H 493       57.78   -103.15                                   
REMARK 500    LEU H 557      -55.21   -145.44                                   
REMARK 500    MET H 578       89.73    -67.54                                   
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 B2037        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH C2019        DISTANCE =  6.87 ANGSTROMS                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DUJ   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF THE SPINDLE ASSEMBLY CHECKPOINTPROTEIN HUMAN   
REMARK 900 MAD2                                                                 
DBREF  1GO4 A    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  1GO4 B    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  1GO4 C    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  1GO4 D    1   205  UNP    Q13257   MD2L1_HUMAN      1    205             
DBREF  1GO4 E  485   584  UNP    Q9Y6D9   MD1L1_HUMAN    393    492             
DBREF  1GO4 F  485   584  UNP    Q9Y6D9   MD1L1_HUMAN    393    492             
DBREF  1GO4 G  485   584  UNP    Q9Y6D9   MD1L1_HUMAN    393    492             
DBREF  1GO4 H  485   584  UNP    Q9Y6D9   MD1L1_HUMAN    393    492             
SEQADV 1GO4 ALA A  133  UNP  Q13257    ARG   133 ENGINEERED MUTATION            
SEQADV 1GO4 ALA B  133  UNP  Q13257    ARG   133 ENGINEERED MUTATION            
SEQADV 1GO4 ALA C  133  UNP  Q13257    ARG   133 ENGINEERED MUTATION            
SEQADV 1GO4 ALA D  133  UNP  Q13257    ARG   133 ENGINEERED MUTATION            
SEQRES   1 A  205  MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR LEU          
SEQRES   2 A  205  ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER PHE          
SEQRES   3 A  205  GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR PRO          
SEQRES   4 A  205  SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU THR          
SEQRES   5 A  205  LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR LEU          
SEQRES   6 A  205  ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR LYS          
SEQRES   7 A  205  CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN ILE          
SEQRES   8 A  205  GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP ILE          
SEQRES   9 A  205  GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO ARG          
SEQRES  10 A  205  GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG SER          
SEQRES  11 A  205  VAL ILE ALA GLN ILE THR ALA THR VAL THR PHE LEU PRO          
SEQRES  12 A  205  LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE TYR          
SEQRES  13 A  205  THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU GLU          
SEQRES  14 A  205  SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL ARG          
SEQRES  15 A  205  LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN SER          
SEQRES  16 A  205  MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                      
SEQRES   1 B  205  MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR LEU          
SEQRES   2 B  205  ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER PHE          
SEQRES   3 B  205  GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR PRO          
SEQRES   4 B  205  SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU THR          
SEQRES   5 B  205  LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR LEU          
SEQRES   6 B  205  ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR LYS          
SEQRES   7 B  205  CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN ILE          
SEQRES   8 B  205  GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP ILE          
SEQRES   9 B  205  GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO ARG          
SEQRES  10 B  205  GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG SER          
SEQRES  11 B  205  VAL ILE ALA GLN ILE THR ALA THR VAL THR PHE LEU PRO          
SEQRES  12 B  205  LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE TYR          
SEQRES  13 B  205  THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU GLU          
SEQRES  14 B  205  SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL ARG          
SEQRES  15 B  205  LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN SER          
SEQRES  16 B  205  MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                      
SEQRES   1 C  205  MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR LEU          
SEQRES   2 C  205  ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER PHE          
SEQRES   3 C  205  GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR PRO          
SEQRES   4 C  205  SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU THR          
SEQRES   5 C  205  LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR LEU          
SEQRES   6 C  205  ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR LYS          
SEQRES   7 C  205  CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN ILE          
SEQRES   8 C  205  GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP ILE          
SEQRES   9 C  205  GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO ARG          
SEQRES  10 C  205  GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG SER          
SEQRES  11 C  205  VAL ILE ALA GLN ILE THR ALA THR VAL THR PHE LEU PRO          
SEQRES  12 C  205  LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE TYR          
SEQRES  13 C  205  THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU GLU          
SEQRES  14 C  205  SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL ARG          
SEQRES  15 C  205  LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN SER          
SEQRES  16 C  205  MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                      
SEQRES   1 D  205  MET ALA LEU GLN LEU SER ARG GLU GLN GLY ILE THR LEU          
SEQRES   2 D  205  ARG GLY SER ALA GLU ILE VAL ALA GLU PHE PHE SER PHE          
SEQRES   3 D  205  GLY ILE ASN SER ILE LEU TYR GLN ARG GLY ILE TYR PRO          
SEQRES   4 D  205  SER GLU THR PHE THR ARG VAL GLN LYS TYR GLY LEU THR          
SEQRES   5 D  205  LEU LEU VAL THR THR ASP LEU GLU LEU ILE LYS TYR LEU          
SEQRES   6 D  205  ASN ASN VAL VAL GLU GLN LEU LYS ASP TRP LEU TYR LYS          
SEQRES   7 D  205  CYS SER VAL GLN LYS LEU VAL VAL VAL ILE SER ASN ILE          
SEQRES   8 D  205  GLU SER GLY GLU VAL LEU GLU ARG TRP GLN PHE ASP ILE          
SEQRES   9 D  205  GLU CYS ASP LYS THR ALA LYS ASP ASP SER ALA PRO ARG          
SEQRES  10 D  205  GLU LYS SER GLN LYS ALA ILE GLN ASP GLU ILE ARG SER          
SEQRES  11 D  205  VAL ILE ALA GLN ILE THR ALA THR VAL THR PHE LEU PRO          
SEQRES  12 D  205  LEU LEU GLU VAL SER CYS SER PHE ASP LEU LEU ILE TYR          
SEQRES  13 D  205  THR ASP LYS ASP LEU VAL VAL PRO GLU LYS TRP GLU GLU          
SEQRES  14 D  205  SER GLY PRO GLN PHE ILE THR ASN SER GLU GLU VAL ARG          
SEQRES  15 D  205  LEU ARG SER PHE THR THR THR ILE HIS LYS VAL ASN SER          
SEQRES  16 D  205  MET VAL ALA TYR LYS ILE PRO VAL ASN ASP                      
SEQRES   1 E  100  SER SER ALA GLU GLN SER PHE LEU PHE SER ARG GLU GLU          
SEQRES   2 E  100  ALA ASP THR LEU ARG LEU LYS VAL GLU GLU LEU GLU GLY          
SEQRES   3 E  100  GLU ARG SER ARG LEU GLU GLU GLU LYS ARG MET LEU GLU          
SEQRES   4 E  100  ALA GLN LEU GLU ARG ARG ALA LEU GLN GLY ASP TYR ASP          
SEQRES   5 E  100  GLN SER ARG THR LYS VAL LEU HIS MET SER LEU ASN PRO          
SEQRES   6 E  100  THR SER VAL ALA ARG GLN ARG LEU ARG GLU ASP HIS SER          
SEQRES   7 E  100  GLN LEU GLN ALA GLU CYS GLU ARG LEU ARG GLY LEU LEU          
SEQRES   8 E  100  ARG ALA MET GLU ARG GLY GLY THR VAL                          
SEQRES   1 F  100  SER SER ALA GLU GLN SER PHE LEU PHE SER ARG GLU GLU          
SEQRES   2 F  100  ALA ASP THR LEU ARG LEU LYS VAL GLU GLU LEU GLU GLY          
SEQRES   3 F  100  GLU ARG SER ARG LEU GLU GLU GLU LYS ARG MET LEU GLU          
SEQRES   4 F  100  ALA GLN LEU GLU ARG ARG ALA LEU GLN GLY ASP TYR ASP          
SEQRES   5 F  100  GLN SER ARG THR LYS VAL LEU HIS MET SER LEU ASN PRO          
SEQRES   6 F  100  THR SER VAL ALA ARG GLN ARG LEU ARG GLU ASP HIS SER          
SEQRES   7 F  100  GLN LEU GLN ALA GLU CYS GLU ARG LEU ARG GLY LEU LEU          
SEQRES   8 F  100  ARG ALA MET GLU ARG GLY GLY THR VAL                          
SEQRES   1 G  100  SER SER ALA GLU GLN SER PHE LEU PHE SER ARG GLU GLU          
SEQRES   2 G  100  ALA ASP THR LEU ARG LEU LYS VAL GLU GLU LEU GLU GLY          
SEQRES   3 G  100  GLU ARG SER ARG LEU GLU GLU GLU LYS ARG MET LEU GLU          
SEQRES   4 G  100  ALA GLN LEU GLU ARG ARG ALA LEU GLN GLY ASP TYR ASP          
SEQRES   5 G  100  GLN SER ARG THR LYS VAL LEU HIS MET SER LEU ASN PRO          
SEQRES   6 G  100  THR SER VAL ALA ARG GLN ARG LEU ARG GLU ASP HIS SER          
SEQRES   7 G  100  GLN LEU GLN ALA GLU CYS GLU ARG LEU ARG GLY LEU LEU          
SEQRES   8 G  100  ARG ALA MET GLU ARG GLY GLY THR VAL                          
SEQRES   1 H  100  SER SER ALA GLU GLN SER PHE LEU PHE SER ARG GLU GLU          
SEQRES   2 H  100  ALA ASP THR LEU ARG LEU LYS VAL GLU GLU LEU GLU GLY          
SEQRES   3 H  100  GLU ARG SER ARG LEU GLU GLU GLU LYS ARG MET LEU GLU          
SEQRES   4 H  100  ALA GLN LEU GLU ARG ARG ALA LEU GLN GLY ASP TYR ASP          
SEQRES   5 H  100  GLN SER ARG THR LYS VAL LEU HIS MET SER LEU ASN PRO          
SEQRES   6 H  100  THR SER VAL ALA ARG GLN ARG LEU ARG GLU ASP HIS SER          
SEQRES   7 H  100  GLN LEU GLN ALA GLU CYS GLU ARG LEU ARG GLY LEU LEU          
SEQRES   8 H  100  ARG ALA MET GLU ARG GLY GLY THR VAL                          
FORMUL   9  HOH   *628(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 THR B   12  ARG B   35  1                                  24    
HELIX    8   8 PRO B   39  GLU B   41  5                                   3    
HELIX    9   9 ASP B   58  CYS B   79  1                                  22    
HELIX   10  10 LYS B  108  ASP B  113  5                                   6    
HELIX   11  11 SER B  120  THR B  140  1                                  21    
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 LYS C  108  ASP C  113  5                                   6    
HELIX   16  16 SER C  120  THR C  138  1                                  19    
HELIX   17  17 VAL C  139  PHE C  141  5                                   3    
HELIX   18  18 THR D   12  ARG D   35  1                                  24    
HELIX   19  19 PRO D   39  GLU D   41  5                                   3    
HELIX   20  20 GLU D   60  LYS D   78  1                                  19    
HELIX   21  21 LYS D  108  ASP D  113  5                                   6    
HELIX   22  22 SER D  120  THR D  138  1                                  19    
HELIX   23  23 PHE E  493  ARG E  529  1                                  37    
HELIX   24  24 ASN E  548  ARG E  576  1                                  29    
HELIX   25  25 ALA F  498  GLY F  533  1                                  36    
HELIX   26  26 ASN F  548  MET F  578  1                                  31    
HELIX   27  27 SER G  486  ARG G  528  1                                  43    
HELIX   28  28 ASN G  548  GLU G  579  1                                  32    
HELIX   29  29 PHE H  493  LEU H  531  1                                  39    
HELIX   30  30 ASN H  548  MET H  578  1                                  31    
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 TRP A 167  GLU A 169  0                                        
SHEET    2  AB 7 THR G 540  MET G 545 -1  O  HIS G 544   N  GLU A 168           
SHEET    3  AB 7 CYS A 149  ASP A 158 -1  O  ILE A 155   N  LEU G 543           
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  TYR A 199 -1  O  LYS A 192   N  GLU A 105           
SHEET    7  AB 7 GLU A 179  ARG A 182 -1  O  GLU A 179   N  TYR A 199           
SHEET    1  AC 7 TRP A 167  GLU A 169  0                                        
SHEET    2  AC 7 THR G 540  MET G 545 -1  O  HIS G 544   N  GLU A 168           
SHEET    3  AC 7 CYS A 149  ASP A 158 -1  O  ILE A 155   N  LEU G 543           
SHEET    4  AC 7 VAL A  81  ASN A  90 -1  N  GLN A  82   O  TYR A 156           
SHEET    5  AC 7 VAL A  96  CYS A 106 -1  N  LEU A  97   O  ILE A  88           
SHEET    6  AC 7 HIS A 191  TYR A 199 -1  O  LYS A 192   N  GLU A 105           
SHEET    7  AC 7 PHE A 186  THR A 187 -1  O  PHE A 186   N  VAL A 193           
SHEET    1  BA 2 PHE B  43  LYS B  48  0                                        
SHEET    2  BA 2 LEU B  51  THR B  56 -1  O  LEU B  51   N  LYS B  48           
SHEET    1  BB 7 TRP B 167  GLU B 169  0                                        
SHEET    2  BB 7 THR F 540  MET F 545 -1  O  HIS F 544   N  GLU B 168           
SHEET    3  BB 7 CYS B 149  ASP B 158 -1  O  ILE B 155   N  LEU F 543           
SHEET    4  BB 7 VAL B  81  ASN B  90 -1  N  GLN B  82   O  TYR B 156           
SHEET    5  BB 7 VAL B  96  CYS B 106 -1  N  LEU B  97   O  ILE B  88           
SHEET    6  BB 7 HIS B 191  LYS B 200 -1  O  LYS B 192   N  GLU B 105           
SHEET    7  BB 7 SER B 178  THR B 187 -1  O  GLU B 179   N  TYR B 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 TRP C 167  GLU C 169  0                                        
SHEET    2  CB 7 THR E 540  MET E 545 -1  O  HIS E 544   N  GLU C 168           
SHEET    3  CB 7 CYS C 149  ASP C 158 -1  O  ILE C 155   N  LEU E 543           
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  ARG C 182 -1  O  GLU C 179   N  TYR C 199           
SHEET    1  CC 7 TRP C 167  GLU C 169  0                                        
SHEET    2  CC 7 THR E 540  MET E 545 -1  O  HIS E 544   N  GLU C 168           
SHEET    3  CC 7 CYS C 149  ASP C 158 -1  O  ILE C 155   N  LEU E 543           
SHEET    4  CC 7 VAL C  81  ASN C  90 -1  N  GLN C  82   O  TYR C 156           
SHEET    5  CC 7 VAL C  96  CYS C 106 -1  N  LEU C  97   O  ILE C  88           
SHEET    6  CC 7 HIS C 191  LYS C 200 -1  O  LYS C 192   N  GLU C 105           
SHEET    7  CC 7 PHE C 186  THR C 187 -1  O  PHE C 186   N  VAL C 193           
SHEET    1  DA 2 PHE D  43  LYS D  48  0                                        
SHEET    2  DA 2 LEU D  51  THR D  56 -1  O  LEU D  51   N  LYS D  48           
SHEET    1  DB 7 TRP D 167  GLU D 169  0                                        
SHEET    2  DB 7 THR H 540  MET H 545 -1  O  HIS H 544   N  GLU D 168           
SHEET    3  DB 7 CYS D 149  ASP D 158 -1  O  ILE D 155   N  LEU H 543           
SHEET    4  DB 7 VAL D  81  ASN D  90 -1  N  GLN D  82   O  TYR D 156           
SHEET    5  DB 7 VAL D  96  CYS D 106 -1  N  LEU D  97   O  ILE D  88           
SHEET    6  DB 7 HIS D 191  LYS D 200 -1  O  LYS D 192   N  GLU D 105           
SHEET    7  DB 7 SER D 178  THR D 187 -1  O  GLU D 179   N  TYR D 199           
CRYST1  111.037   63.023  139.511  90.00 111.65  90.00 P 1 21 1      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      0.009006  0.000000  0.003575        0.00000                         
SCALE2      0.000000  0.015867  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system