GenomeNet

Database: PDB
Entry: 3N7N
LinkDB: 3N7N
Original site: 3N7N 
HEADER    REPLICATION                             27-MAY-10   3N7N              
TITLE     STRUCTURE OF CSM1/LRS4 COMPLEX                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MONOPOLIN COMPLEX SUBUNIT CSM1;                            
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: CHROMOSOME SEGREGATION IN MEIOSIS PROTEIN 1;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MONOPOLIN COMPLEX SUBUNIT LRS4;                            
COMPND   8 CHAIN: E, F;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 1-102, DELTA 38-44;                           
COMPND  10 SYNONYM: LOSS OF RDNA SILENCING PROTEIN 4;                           
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: CSM1, SPO86, YCR086W, YCR86W;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PST39;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  13 ORGANISM_COMMON: BREWER'S YEAST,LAGER BEER YEAST,YEAST;              
SOURCE  14 ORGANISM_TAXID: 4932;                                                
SOURCE  15 GENE: D9461.25, LRS4, YDR439W;                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2 PLYSS;                           
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PST39                                     
KEYWDS    MEIOSIS, RDNA, REPLICATION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.D.CORBETT,S.C.HARRISON                                              
REVDAT   2   17-JUL-19 3N7N    1       REMARK                                   
REVDAT   1   01-SEP-10 3N7N    0                                                
JRNL        AUTH   K.D.CORBETT,C.K.YIP,L.S.EE,T.WALZ,A.AMON,S.C.HARRISON        
JRNL        TITL   THE MONOPOLIN COMPLEX CROSSLINKS KINETOCHORE COMPONENTS TO   
JRNL        TITL 2 REGULATE CHROMOSOME-MICROTUBULE ATTACHMENTS.                 
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 142   556 2010              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   20723757                                                     
JRNL        DOI    10.1016/J.CELL.2010.07.017                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 44.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 6642                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.333                           
REMARK   3   FREE R VALUE                     : 0.355                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 321                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 50.0000 -  8.3900    0.95     1436    65  0.2978 0.2953        
REMARK   3     2  8.3900 -  6.6600    0.97     1388    73  0.3800 0.4305        
REMARK   3     3  6.6600 -  5.8200    0.92     1312    73  0.4227 0.4941        
REMARK   3     4  5.8200 -  5.2900    0.51      723    38  0.4221 0.4715        
REMARK   3     5  5.2900 -  4.9100    0.34      474    24  0.3767 0.3605        
REMARK   3     6  4.9100 -  4.6200    0.24      336    18  0.3458 0.3998        
REMARK   3     7  4.6200 -  4.3900    0.17      243    14  0.4165 0.4562        
REMARK   3     8  4.3900 -  4.2000    0.13      183     5  0.3631 0.3903        
REMARK   3     9  4.2000 -  4.0400    0.10      135     6  0.2919 0.4866        
REMARK   3    10  4.0400 -  3.9000    0.07       91     5  0.3493 0.2647        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : 318.5                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 358.0                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 103.66200                                            
REMARK   3    B22 (A**2) : 103.66200                                            
REMARK   3    B33 (A**2) : -207.32500                                           
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059482.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97918                            
REMARK 200  MONOCHROMATOR                  : SIDE-BOUNCE CRYOGENICALLY COOLED   
REMARK 200                                   220 SILICON MONOCHROMATOR          
REMARK 200  OPTICS                         : MIRRORS                            
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   : 6644                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 43.4                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 5.8                                
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.46400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.5, 120 MM MGCL2,     
REMARK 280  16% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        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: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     ASP A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     TYR A   113                                                      
REMARK 465     SER A   114                                                      
REMARK 465     LYS A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     GLN A   126                                                      
REMARK 465     ALA A   127                                                      
REMARK 465     GLN A   128                                                      
REMARK 465     ASN A   180                                                      
REMARK 465     LYS A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     ARG A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     LYS A   185                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     GLU A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     GLU A   190                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     THR B   104                                                      
REMARK 465     HIS B   105                                                      
REMARK 465     SER B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     GLY B   108                                                      
REMARK 465     SER B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     ASP B   112                                                      
REMARK 465     TYR B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     ASN B   180                                                      
REMARK 465     LYS B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     ARG B   183                                                      
REMARK 465     GLU B   184                                                      
REMARK 465     LYS B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     ASP B   187                                                      
REMARK 465     GLU B   188                                                      
REMARK 465     THR B   189                                                      
REMARK 465     GLU B   190                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ASP C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     TYR C     7                                                      
REMARK 465     SER C   106                                                      
REMARK 465     GLY C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     SER C   109                                                      
REMARK 465     SER C   110                                                      
REMARK 465     ASP C   111                                                      
REMARK 465     ASP C   112                                                      
REMARK 465     TYR C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     LYS C   124                                                      
REMARK 465     GLY C   125                                                      
REMARK 465     GLN C   126                                                      
REMARK 465     ALA C   127                                                      
REMARK 465     GLN C   128                                                      
REMARK 465     ASN C   180                                                      
REMARK 465     LYS C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     ARG C   183                                                      
REMARK 465     GLU C   184                                                      
REMARK 465     LYS C   185                                                      
REMARK 465     LYS C   186                                                      
REMARK 465     ASP C   187                                                      
REMARK 465     GLU C   188                                                      
REMARK 465     THR C   189                                                      
REMARK 465     GLU C   190                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ASP D     2                                                      
REMARK 465     GLN D   102                                                      
REMARK 465     GLY D   103                                                      
REMARK 465     THR D   104                                                      
REMARK 465     HIS D   105                                                      
REMARK 465     SER D   106                                                      
REMARK 465     GLY D   107                                                      
REMARK 465     GLY D   108                                                      
REMARK 465     SER D   109                                                      
REMARK 465     SER D   110                                                      
REMARK 465     ASP D   111                                                      
REMARK 465     ASP D   112                                                      
REMARK 465     TYR D   113                                                      
REMARK 465     SER D   114                                                      
REMARK 465     LYS D   124                                                      
REMARK 465     GLY D   125                                                      
REMARK 465     GLN D   126                                                      
REMARK 465     ALA D   127                                                      
REMARK 465     GLN D   128                                                      
REMARK 465     VAL D   129                                                      
REMARK 465     ASN D   180                                                      
REMARK 465     LYS D   181                                                      
REMARK 465     LYS D   182                                                      
REMARK 465     ARG D   183                                                      
REMARK 465     GLU D   184                                                      
REMARK 465     LYS D   185                                                      
REMARK 465     LYS D   186                                                      
REMARK 465     ASP D   187                                                      
REMARK 465     GLU D   188                                                      
REMARK 465     THR D   189                                                      
REMARK 465     GLU D   190                                                      
REMARK 465     MET E     1                                                      
REMARK 465     THR E     2                                                      
REMARK 465     SER E    34                                                      
REMARK 465     LEU E    35                                                      
REMARK 465     ASP E    36                                                      
REMARK 465     LYS E    37                                                      
REMARK 465     PRO E    38                                                      
REMARK 465     LYS E    39                                                      
REMARK 465     LYS E    40                                                      
REMARK 465     VAL E    41                                                      
REMARK 465     VAL E    42                                                      
REMARK 465     ASP E    43                                                      
REMARK 465     GLU E    44                                                      
REMARK 465     THR E    45                                                      
REMARK 465     LEU E    46                                                      
REMARK 465     PHE E    47                                                      
REMARK 465     LEU E    48                                                      
REMARK 465     GLN E    49                                                      
REMARK 465     ARG E    50                                                      
REMARK 465     GLN E    51                                                      
REMARK 465     ILE E    52                                                      
REMARK 465     ALA E    53                                                      
REMARK 465     GLN E    54                                                      
REMARK 465     LEU E    55                                                      
REMARK 465     ASN E    56                                                      
REMARK 465     LYS E    57                                                      
REMARK 465     GLN E    58                                                      
REMARK 465     LEU E    59                                                      
REMARK 465     GLN E    60                                                      
REMARK 465     LEU E    61                                                      
REMARK 465     SER E    62                                                      
REMARK 465     PHE E    63                                                      
REMARK 465     GLN E    64                                                      
REMARK 465     GLU E    65                                                      
REMARK 465     ASN E    66                                                      
REMARK 465     GLU E    67                                                      
REMARK 465     LYS E    68                                                      
REMARK 465     LEU E    69                                                      
REMARK 465     LEU E    70                                                      
REMARK 465     SER E    71                                                      
REMARK 465     VAL E    72                                                      
REMARK 465     GLN E    73                                                      
REMARK 465     LYS E    74                                                      
REMARK 465     ASN E    75                                                      
REMARK 465     GLN E    76                                                      
REMARK 465     LYS E    77                                                      
REMARK 465     ALA E    78                                                      
REMARK 465     LEU E    79                                                      
REMARK 465     TYR E    80                                                      
REMARK 465     GLN E    81                                                      
REMARK 465     SER E    82                                                      
REMARK 465     LYS E    83                                                      
REMARK 465     LEU E    84                                                      
REMARK 465     SER E    85                                                      
REMARK 465     SER E    86                                                      
REMARK 465     LYS E    87                                                      
REMARK 465     ASP E    88                                                      
REMARK 465     ALA E    89                                                      
REMARK 465     PHE E    90                                                      
REMARK 465     ILE E    91                                                      
REMARK 465     ASP E    92                                                      
REMARK 465     ASP E    93                                                      
REMARK 465     LEU E    94                                                      
REMARK 465     LYS E    95                                                      
REMARK 465     MET F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     ALA F    33                                                      
REMARK 465     SER F    34                                                      
REMARK 465     LEU F    35                                                      
REMARK 465     ASP F    36                                                      
REMARK 465     LYS F    37                                                      
REMARK 465     PRO F    38                                                      
REMARK 465     LYS F    39                                                      
REMARK 465     LYS F    40                                                      
REMARK 465     VAL F    41                                                      
REMARK 465     VAL F    42                                                      
REMARK 465     ASP F    43                                                      
REMARK 465     GLU F    44                                                      
REMARK 465     THR F    45                                                      
REMARK 465     LEU F    46                                                      
REMARK 465     PHE F    47                                                      
REMARK 465     LEU F    48                                                      
REMARK 465     GLN F    49                                                      
REMARK 465     ARG F    50                                                      
REMARK 465     GLN F    51                                                      
REMARK 465     ILE F    52                                                      
REMARK 465     ALA F    53                                                      
REMARK 465     GLN F    54                                                      
REMARK 465     LEU F    55                                                      
REMARK 465     ASN F    56                                                      
REMARK 465     LYS F    57                                                      
REMARK 465     GLN F    58                                                      
REMARK 465     LEU F    59                                                      
REMARK 465     GLN F    60                                                      
REMARK 465     LEU F    61                                                      
REMARK 465     SER F    62                                                      
REMARK 465     PHE F    63                                                      
REMARK 465     GLN F    64                                                      
REMARK 465     GLU F    65                                                      
REMARK 465     ASN F    66                                                      
REMARK 465     GLU F    67                                                      
REMARK 465     LYS F    68                                                      
REMARK 465     LEU F    69                                                      
REMARK 465     LEU F    70                                                      
REMARK 465     SER F    71                                                      
REMARK 465     VAL F    72                                                      
REMARK 465     GLN F    73                                                      
REMARK 465     LYS F    74                                                      
REMARK 465     ASN F    75                                                      
REMARK 465     GLN F    76                                                      
REMARK 465     LYS F    77                                                      
REMARK 465     ALA F    78                                                      
REMARK 465     LEU F    79                                                      
REMARK 465     TYR F    80                                                      
REMARK 465     GLN F    81                                                      
REMARK 465     SER F    82                                                      
REMARK 465     LYS F    83                                                      
REMARK 465     LEU F    84                                                      
REMARK 465     SER F    85                                                      
REMARK 465     SER F    86                                                      
REMARK 465     LYS F    87                                                      
REMARK 465     ASP F    88                                                      
REMARK 465     ALA F    89                                                      
REMARK 465     PHE F    90                                                      
REMARK 465     ILE F    91                                                      
REMARK 465     ASP F    92                                                      
REMARK 465     ASP F    93                                                      
REMARK 465     LEU F    94                                                      
REMARK 465     LYS F    95                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     HIS A 105    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     LYS C   8    CG   CD   CE   NZ                                   
REMARK 470     HIS C 105    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     LYS D   8    CG   CD   CE   NZ                                   
REMARK 470     THR E   3    OG1  CG2                                            
REMARK 470     LEU E   4    CG   CD1  CD2                                       
REMARK 470     LEU E   5    CG   CD1  CD2                                       
REMARK 470     GLN E   6    CG   CD   OE1  NE2                                  
REMARK 470     LEU E   7    CG   CD1  CD2                                       
REMARK 470     LEU E   8    CG   CD1  CD2                                       
REMARK 470     SER E   9    OG                                                  
REMARK 470     ASN E  10    CG   OD1  ND2                                       
REMARK 470     TYR E  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR E  12    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS E  13    CG   CD   CE   NZ                                   
REMARK 470     LYS E  15    CG   CD   CE   NZ                                   
REMARK 470     LEU E  16    CG   CD1  CD2                                       
REMARK 470     ASP E  17    CG   OD1  OD2                                       
REMARK 470     SER E  18    OG                                                  
REMARK 470     GLU E  19    CG   CD   OE1  OE2                                  
REMARK 470     ARG E  20    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE E  21    CG1  CG2  CD1                                       
REMARK 470     TYR E  22    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN E  23    CG   OD1  ND2                                       
REMARK 470     GLU E  24    CG   CD   OE1  OE2                                  
REMARK 470     TYR E  25    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL E  26    CG1  CG2                                            
REMARK 470     GLN E  27    CG   CD   OE1  NE2                                  
REMARK 470     SER E  28    OG                                                  
REMARK 470     GLN E  29    CG   CD   OE1  NE2                                  
REMARK 470     TYR E  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU E  31    CG   CD   OE1  OE2                                  
REMARK 470     PHE E  32    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR F   3    OG1  CG2                                            
REMARK 470     LEU F   4    CG   CD1  CD2                                       
REMARK 470     LEU F   5    CG   CD1  CD2                                       
REMARK 470     GLN F   6    CG   CD   OE1  NE2                                  
REMARK 470     LEU F   7    CG   CD1  CD2                                       
REMARK 470     LEU F   8    CG   CD1  CD2                                       
REMARK 470     SER F   9    OG                                                  
REMARK 470     ASN F  10    CG   OD1  ND2                                       
REMARK 470     TYR F  11    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR F  12    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS F  13    CG   CD   CE   NZ                                   
REMARK 470     LYS F  15    CG   CD   CE   NZ                                   
REMARK 470     LEU F  16    CG   CD1  CD2                                       
REMARK 470     ASP F  17    CG   OD1  OD2                                       
REMARK 470     SER F  18    OG                                                  
REMARK 470     GLU F  19    CG   CD   OE1  OE2                                  
REMARK 470     ARG F  20    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE F  21    CG1  CG2  CD1                                       
REMARK 470     TYR F  22    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN F  23    CG   OD1  ND2                                       
REMARK 470     GLU F  24    CG   CD   OE1  OE2                                  
REMARK 470     TYR F  25    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL F  26    CG1  CG2                                            
REMARK 470     GLN F  27    CG   CD   OE1  NE2                                  
REMARK 470     SER F  28    OG                                                  
REMARK 470     GLN F  29    CG   CD   OE1  NE2                                  
REMARK 470     TYR F  30    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU F  31    CG   CD   OE1  OE2                                  
REMARK 470     PHE F  32    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN C    66     OD1  ASN C    70              1.98            
REMARK 500   CD1  TYR A     7     CE1  TYR B     7              2.02            
REMARK 500   O    GLN C    66     N    ASN C    70              2.06            
REMARK 500   CD1  LEU C    36     CD1  LEU D    36              2.07            
REMARK 500   CG2  THR C    62     NE2  GLN C    66              2.14            
REMARK 500   CE2  TYR C   134     O    LEU C   157              2.16            
REMARK 500   CG   PRO C   136     O    PHE C   158              2.16            
REMARK 500   O    VAL C    26     CD2  PHE C    30              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CE   LYS C    39     CD2  PHE D    30     2545     1.98            
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    PRO B 136   C   -  N   -  CD  ANGL. DEV. = -18.1 DEGREES          
REMARK 500    PRO C 136   C   -  N   -  CD  ANGL. DEV. = -18.1 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    VAL A  22      -34.66    -39.05                                   
REMARK 500    ASP A  93     -116.42     58.23                                   
REMARK 500    ASP B  93     -118.63     56.12                                   
REMARK 500    GLN B 126     -129.70     62.49                                   
REMARK 500    LEU B 138       67.90   -110.51                                   
REMARK 500    ALA C  40       -9.22    -58.43                                   
REMARK 500    ASP C  93     -116.42     58.46                                   
REMARK 500    SER D  33      -29.97    -35.03                                   
REMARK 500    ALA D  40       -9.23    -58.25                                   
REMARK 500    TYR D  80      -76.82    -49.92                                   
REMARK 500    LEU D  81       48.77    -74.44                                   
REMARK 500    CYS D  82      -11.65   -158.71                                   
REMARK 500    ASN D  83       24.14     45.61                                   
REMARK 500    ASP D  93     -118.67     55.98                                   
REMARK 500    PHE D 158       11.94    -64.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3N4R   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CSM1 C-TERMINAL DOMAIN, R3 FORM                         
REMARK 900 RELATED ID: 3N4S   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CSM1 C-TERMINAL DOMAIN, P21212 FORM                     
REMARK 900 RELATED ID: 3N4X   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CSM1 FULL-LENGTH                                        
DBREF  3N7N A    1   190  UNP    P25651   CSM1_YEAST       1    190             
DBREF  3N7N B    1   190  UNP    P25651   CSM1_YEAST       1    190             
DBREF  3N7N C    1   190  UNP    P25651   CSM1_YEAST       1    190             
DBREF  3N7N D    1   190  UNP    P25651   CSM1_YEAST       1    190             
DBREF  3N7N E    1    95  UNP    Q04087   LRS4_YEAST       1    102             
DBREF  3N7N F    1    95  UNP    Q04087   LRS4_YEAST       1    102             
SEQADV 3N7N     E       UNP  Q04087    LEU    38 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    ASN    39 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    ASN    40 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    ASN    41 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    LYS    42 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    GLY    43 DELETION                       
SEQADV 3N7N     E       UNP  Q04087    ASP    44 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    LEU    38 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    ASN    39 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    ASN    40 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    ASN    41 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    LYS    42 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    GLY    43 DELETION                       
SEQADV 3N7N     F       UNP  Q04087    ASP    44 DELETION                       
SEQRES   1 A  190  MET ASP PRO LEU THR VAL TYR LYS ASN SER VAL LYS GLN          
SEQRES   2 A  190  GLN ILE ASP SER ALA ASP LEU LEU VAL ALA ASN LEU VAL          
SEQRES   3 A  190  ASN GLU ASN PHE VAL LEU SER GLU LYS LEU ASP THR LYS          
SEQRES   4 A  190  ALA THR GLU ILE LYS GLN LEU GLN LYS GLN ILE ASP SER          
SEQRES   5 A  190  LEU ASN ALA GLN VAL LYS GLU LEU LYS THR GLN THR SER          
SEQRES   6 A  190  GLN GLN ALA GLU ASN SER GLU VAL ILE LYS ASP LEU TYR          
SEQRES   7 A  190  GLU TYR LEU CYS ASN VAL ARG VAL HIS LYS SER TYR GLU          
SEQRES   8 A  190  ASP ASP SER GLY LEU TRP PHE ASP ILE SER GLN GLY THR          
SEQRES   9 A  190  HIS SER GLY GLY SER SER ASP ASP TYR SER ILE MET ASP          
SEQRES  10 A  190  TYR LYS LEU GLY PHE VAL LYS GLY GLN ALA GLN VAL THR          
SEQRES  11 A  190  GLU VAL ILE TYR ALA PRO VAL LEU LYS GLN ARG SER THR          
SEQRES  12 A  190  GLU GLU LEU TYR SER LEU GLN SER LYS LEU PRO GLU TYR          
SEQRES  13 A  190  LEU PHE GLU THR LEU SER PHE PRO LEU SER SER LEU ASN          
SEQRES  14 A  190  GLN PHE TYR ASN LYS ILE ALA LYS SER LEU ASN LYS LYS          
SEQRES  15 A  190  ARG GLU LYS LYS ASP GLU THR GLU                              
SEQRES   1 B  190  MET ASP PRO LEU THR VAL TYR LYS ASN SER VAL LYS GLN          
SEQRES   2 B  190  GLN ILE ASP SER ALA ASP LEU LEU VAL ALA ASN LEU VAL          
SEQRES   3 B  190  ASN GLU ASN PHE VAL LEU SER GLU LYS LEU ASP THR LYS          
SEQRES   4 B  190  ALA THR GLU ILE LYS GLN LEU GLN LYS GLN ILE ASP SER          
SEQRES   5 B  190  LEU ASN ALA GLN VAL LYS GLU LEU LYS THR GLN THR SER          
SEQRES   6 B  190  GLN GLN ALA GLU ASN SER GLU VAL ILE LYS ASP LEU TYR          
SEQRES   7 B  190  GLU TYR LEU CYS ASN VAL ARG VAL HIS LYS SER TYR GLU          
SEQRES   8 B  190  ASP ASP SER GLY LEU TRP PHE ASP ILE SER GLN GLY THR          
SEQRES   9 B  190  HIS SER GLY GLY SER SER ASP ASP TYR SER ILE MET ASP          
SEQRES  10 B  190  TYR LYS LEU GLY PHE VAL LYS GLY GLN ALA GLN VAL THR          
SEQRES  11 B  190  GLU VAL ILE TYR ALA PRO VAL LEU LYS GLN ARG SER THR          
SEQRES  12 B  190  GLU GLU LEU TYR SER LEU GLN SER LYS LEU PRO GLU TYR          
SEQRES  13 B  190  LEU PHE GLU THR LEU SER PHE PRO LEU SER SER LEU ASN          
SEQRES  14 B  190  GLN PHE TYR ASN LYS ILE ALA LYS SER LEU ASN LYS LYS          
SEQRES  15 B  190  ARG GLU LYS LYS ASP GLU THR GLU                              
SEQRES   1 C  190  MET ASP PRO LEU THR VAL TYR LYS ASN SER VAL LYS GLN          
SEQRES   2 C  190  GLN ILE ASP SER ALA ASP LEU LEU VAL ALA ASN LEU VAL          
SEQRES   3 C  190  ASN GLU ASN PHE VAL LEU SER GLU LYS LEU ASP THR LYS          
SEQRES   4 C  190  ALA THR GLU ILE LYS GLN LEU GLN LYS GLN ILE ASP SER          
SEQRES   5 C  190  LEU ASN ALA GLN VAL LYS GLU LEU LYS THR GLN THR SER          
SEQRES   6 C  190  GLN GLN ALA GLU ASN SER GLU VAL ILE LYS ASP LEU TYR          
SEQRES   7 C  190  GLU TYR LEU CYS ASN VAL ARG VAL HIS LYS SER TYR GLU          
SEQRES   8 C  190  ASP ASP SER GLY LEU TRP PHE ASP ILE SER GLN GLY THR          
SEQRES   9 C  190  HIS SER GLY GLY SER SER ASP ASP TYR SER ILE MET ASP          
SEQRES  10 C  190  TYR LYS LEU GLY PHE VAL LYS GLY GLN ALA GLN VAL THR          
SEQRES  11 C  190  GLU VAL ILE TYR ALA PRO VAL LEU LYS GLN ARG SER THR          
SEQRES  12 C  190  GLU GLU LEU TYR SER LEU GLN SER LYS LEU PRO GLU TYR          
SEQRES  13 C  190  LEU PHE GLU THR LEU SER PHE PRO LEU SER SER LEU ASN          
SEQRES  14 C  190  GLN PHE TYR ASN LYS ILE ALA LYS SER LEU ASN LYS LYS          
SEQRES  15 C  190  ARG GLU LYS LYS ASP GLU THR GLU                              
SEQRES   1 D  190  MET ASP PRO LEU THR VAL TYR LYS ASN SER VAL LYS GLN          
SEQRES   2 D  190  GLN ILE ASP SER ALA ASP LEU LEU VAL ALA ASN LEU VAL          
SEQRES   3 D  190  ASN GLU ASN PHE VAL LEU SER GLU LYS LEU ASP THR LYS          
SEQRES   4 D  190  ALA THR GLU ILE LYS GLN LEU GLN LYS GLN ILE ASP SER          
SEQRES   5 D  190  LEU ASN ALA GLN VAL LYS GLU LEU LYS THR GLN THR SER          
SEQRES   6 D  190  GLN GLN ALA GLU ASN SER GLU VAL ILE LYS ASP LEU TYR          
SEQRES   7 D  190  GLU TYR LEU CYS ASN VAL ARG VAL HIS LYS SER TYR GLU          
SEQRES   8 D  190  ASP ASP SER GLY LEU TRP PHE ASP ILE SER GLN GLY THR          
SEQRES   9 D  190  HIS SER GLY GLY SER SER ASP ASP TYR SER ILE MET ASP          
SEQRES  10 D  190  TYR LYS LEU GLY PHE VAL LYS GLY GLN ALA GLN VAL THR          
SEQRES  11 D  190  GLU VAL ILE TYR ALA PRO VAL LEU LYS GLN ARG SER THR          
SEQRES  12 D  190  GLU GLU LEU TYR SER LEU GLN SER LYS LEU PRO GLU TYR          
SEQRES  13 D  190  LEU PHE GLU THR LEU SER PHE PRO LEU SER SER LEU ASN          
SEQRES  14 D  190  GLN PHE TYR ASN LYS ILE ALA LYS SER LEU ASN LYS LYS          
SEQRES  15 D  190  ARG GLU LYS LYS ASP GLU THR GLU                              
SEQRES   1 E   95  MET THR THR LEU LEU GLN LEU LEU SER ASN TYR TYR LYS          
SEQRES   2 E   95  ALA LYS LEU ASP SER GLU ARG ILE TYR ASN GLU TYR VAL          
SEQRES   3 E   95  GLN SER GLN TYR GLU PHE ALA SER LEU ASP LYS PRO LYS          
SEQRES   4 E   95  LYS VAL VAL ASP GLU THR LEU PHE LEU GLN ARG GLN ILE          
SEQRES   5 E   95  ALA GLN LEU ASN LYS GLN LEU GLN LEU SER PHE GLN GLU          
SEQRES   6 E   95  ASN GLU LYS LEU LEU SER VAL GLN LYS ASN GLN LYS ALA          
SEQRES   7 E   95  LEU TYR GLN SER LYS LEU SER SER LYS ASP ALA PHE ILE          
SEQRES   8 E   95  ASP ASP LEU LYS                                              
SEQRES   1 F   95  MET THR THR LEU LEU GLN LEU LEU SER ASN TYR TYR LYS          
SEQRES   2 F   95  ALA LYS LEU ASP SER GLU ARG ILE TYR ASN GLU TYR VAL          
SEQRES   3 F   95  GLN SER GLN TYR GLU PHE ALA SER LEU ASP LYS PRO LYS          
SEQRES   4 F   95  LYS VAL VAL ASP GLU THR LEU PHE LEU GLN ARG GLN ILE          
SEQRES   5 F   95  ALA GLN LEU ASN LYS GLN LEU GLN LEU SER PHE GLN GLU          
SEQRES   6 F   95  ASN GLU LYS LEU LEU SER VAL GLN LYS ASN GLN LYS ALA          
SEQRES   7 F   95  LEU TYR GLN SER LYS LEU SER SER LYS ASP ALA PHE ILE          
SEQRES   8 F   95  ASP ASP LEU LYS                                              
HELIX    1   1 PRO A    3  ASN A   83  1                                  81    
HELIX    2   2 SER A  142  LEU A  153  1                                  12    
HELIX    3   3 PRO A  154  GLU A  159  5                                   6    
HELIX    4   4 PRO A  164  SER A  166  5                                   3    
HELIX    5   5 SER A  167  LEU A  179  1                                  13    
HELIX    6   6 LEU B    4  ASN B   83  1                                  80    
HELIX    7   7 SER B  142  LEU B  153  1                                  12    
HELIX    8   8 PRO B  154  PHE B  158  5                                   5    
HELIX    9   9 SER B  167  LEU B  179  1                                  13    
HELIX   10  10 LYS C    8  THR C   38  1                                  31    
HELIX   11  11 THR C   38  CYS C   82  1                                  45    
HELIX   12  12 SER C  142  LEU C  153  1                                  12    
HELIX   13  13 PRO C  154  GLU C  159  5                                   6    
HELIX   14  14 PRO C  164  SER C  166  5                                   3    
HELIX   15  15 SER C  167  LEU C  179  1                                  13    
HELIX   16  16 PRO D    3  THR D   38  1                                  36    
HELIX   17  17 THR D   38  LEU D   81  1                                  44    
HELIX   18  18 SER D  142  LEU D  153  1                                  12    
HELIX   19  19 PRO D  164  SER D  166  5                                   3    
HELIX   20  20 SER D  167  LEU D  179  1                                  13    
HELIX   21  21 THR E    3  ALA E   33  1                                  31    
HELIX   22  22 THR F    3  PHE F   32  1                                  30    
SHEET    1   A 3 VAL A  84  ARG A  85  0                                        
SHEET    2   A 3 LEU A  96  GLN A 102 -1  O  SER A 101   N  ARG A  85           
SHEET    3   A 3 TYR A  90  GLU A  91 -1  N  TYR A  90   O  TRP A  97           
SHEET    1   B 5 VAL A  84  ARG A  85  0                                        
SHEET    2   B 5 LEU A  96  GLN A 102 -1  O  SER A 101   N  ARG A  85           
SHEET    3   B 5 MET A 116  VAL A 123 -1  O  MET A 116   N  GLN A 102           
SHEET    4   B 5 GLU A 131  PRO A 136 -1  O  ALA A 135   N  LYS A 119           
SHEET    5   B 5 LEU A 161  PHE A 163 -1  O  PHE A 163   N  VAL A 132           
SHEET    1   C 3 ARG B  85  VAL B  86  0                                        
SHEET    2   C 3 LEU B  96  SER B 101 -1  O  SER B 101   N  ARG B  85           
SHEET    3   C 3 TYR B  90  GLU B  91 -1  N  TYR B  90   O  TRP B  97           
SHEET    1   D 5 ARG B  85  VAL B  86  0                                        
SHEET    2   D 5 LEU B  96  SER B 101 -1  O  SER B 101   N  ARG B  85           
SHEET    3   D 5 ASP B 117  VAL B 123 -1  O  TYR B 118   N  ILE B 100           
SHEET    4   D 5 GLU B 131  PRO B 136 -1  O  ALA B 135   N  LYS B 119           
SHEET    5   D 5 LEU B 161  PRO B 164 -1  O  PHE B 163   N  VAL B 132           
SHEET    1   E 3 VAL C  84  ARG C  85  0                                        
SHEET    2   E 3 LEU C  96  GLN C 102 -1  O  SER C 101   N  ARG C  85           
SHEET    3   E 3 TYR C  90  GLU C  91 -1  N  TYR C  90   O  TRP C  97           
SHEET    1   F 5 VAL C  84  ARG C  85  0                                        
SHEET    2   F 5 LEU C  96  GLN C 102 -1  O  SER C 101   N  ARG C  85           
SHEET    3   F 5 MET C 116  VAL C 123 -1  O  MET C 116   N  GLN C 102           
SHEET    4   F 5 GLU C 131  PRO C 136 -1  O  ALA C 135   N  LYS C 119           
SHEET    5   F 5 LEU C 161  PHE C 163 -1  O  PHE C 163   N  VAL C 132           
SHEET    1   G 3 ARG D  85  VAL D  86  0                                        
SHEET    2   G 3 LEU D  96  SER D 101 -1  O  SER D 101   N  ARG D  85           
SHEET    3   G 3 TYR D  90  GLU D  91 -1  N  TYR D  90   O  TRP D  97           
SHEET    1   H 4 ARG D  85  VAL D  86  0                                        
SHEET    2   H 4 LEU D  96  SER D 101 -1  O  SER D 101   N  ARG D  85           
SHEET    3   H 4 TYR D 118  PHE D 122 -1  O  TYR D 118   N  ILE D 100           
SHEET    4   H 4 VAL D 132  PRO D 136 -1  O  ALA D 135   N  LYS D 119           
CRYST1  152.624  152.624  118.794  90.00  90.00 120.00 P 3 2 1      24          
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      0.006552  0.003783  0.000000        0.00000                         
SCALE2      0.000000  0.007566  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008418        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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