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Database: PDB
Entry: 5IOH
LinkDB: 5IOH
Original site: 5IOH 
HEADER    HYDROLASE/PROTEIN BINDING               08-MAR-16   5IOH              
TITLE     REPOMAN-PP1A (PROTEIN PHOSPHATASE 1, ALPHA ISOFORM) HOLOENZYME COMPLEX
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, C;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 7-300;                                        
COMPND   6 SYNONYM: PP-1A;                                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CELL DIVISION CYCLE-ASSOCIATED PROTEIN 2;                  
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 383-441;                                      
COMPND  13 SYNONYM: RECRUITS PP1 ONTO MITOTIC CHROMATIN AT ANAPHASE PROTEIN,    
COMPND  14 REPO-MAN;                                                            
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: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: RP1B;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: CDCA2;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PP1 ALPHA; REPOMAN, KI-67; PHOSPHATASE, HYDROLASE-PROTEIN BINDING     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.KUMAR,W.PETI,R.PAGE                                               
REVDAT   3   27-SEP-17 5IOH    1       REMARK                                   
REVDAT   2   12-OCT-16 5IOH    1       JRNL                                     
REVDAT   1   05-OCT-16 5IOH    0                                                
JRNL        AUTH   G.S.KUMAR,E.GOKHAN,S.DE MUNTER,M.BOLLEN,P.VAGNARELLI,W.PETI, 
JRNL        AUTH 2 R.PAGE                                                       
JRNL        TITL   THE KI-67 AND REPOMAN MITOTIC PHOSPHATASES ASSEMBLE VIA AN   
JRNL        TITL 2 IDENTICAL, YET NOVEL MECHANISM.                              
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27572260                                                     
JRNL        DOI    10.7554/ELIFE.16539                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22041                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1118                            
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 46.5527 -  5.1303    1.00     2823   147  0.1718 0.1993        
REMARK   3     2  5.1303 -  4.0729    1.00     2689   140  0.1377 0.1537        
REMARK   3     3  4.0729 -  3.5582    1.00     2667   139  0.1643 0.1941        
REMARK   3     4  3.5582 -  3.2330    1.00     2626   152  0.1814 0.2703        
REMARK   3     5  3.2330 -  3.0013    1.00     2604   142  0.1976 0.2138        
REMARK   3     6  3.0013 -  2.8244    1.00     2619   142  0.2024 0.2712        
REMARK   3     7  2.8244 -  2.6829    1.00     2622   151  0.2142 0.2755        
REMARK   3     8  2.6829 -  2.5662    0.87     2273   105  0.2291 0.2797        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.002           5186                                  
REMARK   3   ANGLE     :  0.610           7036                                  
REMARK   3   CHIRALITY :  0.024            772                                  
REMARK   3   PLANARITY :  0.002            924                                  
REMARK   3   DIHEDRAL  : 10.516           1881                                  
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 5IOH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219119.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22441                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.566                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 11.50                              
REMARK 200  R MERGE                    (I) : 0.01700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4MOV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM MALONATE, 12% PEG 3350,    
REMARK 280  PH 4.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       80.38450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.54450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       80.38450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       28.54450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     GLY B   378                                                      
REMARK 465     ALA B   379                                                      
REMARK 465     MET B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     TYR B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     PHE B   384                                                      
REMARK 465     LEU B   385                                                      
REMARK 465     ASN B   386                                                      
REMARK 465     MET B   387                                                      
REMARK 465     ARG B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     ARG B   390                                                      
REMARK 465     LYS B   424                                                      
REMARK 465     ASP B   425                                                      
REMARK 465     PHE B   426                                                      
REMARK 465     SER B   427                                                      
REMARK 465     GLY B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     SER B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     LEU B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     GLN B   436                                                      
REMARK 465     SER B   437                                                      
REMARK 465     PRO B   438                                                      
REMARK 465     VAL B   439                                                      
REMARK 465     PRO B   440                                                      
REMARK 465     GLU B   441                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLY D   378                                                      
REMARK 465     ALA D   379                                                      
REMARK 465     MET D   380                                                      
REMARK 465     GLY D   381                                                      
REMARK 465     TYR D   382                                                      
REMARK 465     ALA D   383                                                      
REMARK 465     PHE D   384                                                      
REMARK 465     LEU D   385                                                      
REMARK 465     ASN D   386                                                      
REMARK 465     MET D   387                                                      
REMARK 465     ARG D   388                                                      
REMARK 465     LYS D   389                                                      
REMARK 465     ARG D   390                                                      
REMARK 465     LYS D   391                                                      
REMARK 465     CYS D   422                                                      
REMARK 465     LYS D   423                                                      
REMARK 465     LYS D   424                                                      
REMARK 465     ASP D   425                                                      
REMARK 465     PHE D   426                                                      
REMARK 465     SER D   427                                                      
REMARK 465     GLY D   428                                                      
REMARK 465     LEU D   429                                                      
REMARK 465     SER D   430                                                      
REMARK 465     SER D   431                                                      
REMARK 465     LEU D   432                                                      
REMARK 465     LEU D   433                                                      
REMARK 465     LEU D   434                                                      
REMARK 465     GLU D   435                                                      
REMARK 465     GLN D   436                                                      
REMARK 465     SER D   437                                                      
REMARK 465     PRO D   438                                                      
REMARK 465     VAL D   439                                                      
REMARK 465     PRO D   440                                                      
REMARK 465     GLU D   441                                                      
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     GLU A  18    CD   OE1  OE2                                       
REMARK 470     SER A  22    OG                                                  
REMARK 470     ARG A  23    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  26    CD   CE   NZ                                        
REMARK 470     LEU A  40    CD1  CD2                                            
REMARK 470     LYS A  41    CD   CE   NZ                                        
REMARK 470     GLU A  56    CD   OE1  OE2                                       
REMARK 470     LYS A  98    CD   CE                                             
REMARK 470     LYS A 141    CD   CE   NZ                                        
REMARK 470     ILE A 146    CD1                                                 
REMARK 470     LYS A 147    CD   CE   NZ                                        
REMARK 470     LYS A 150    CD   CE   NZ                                        
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 220    CG   OD1  OD2                                       
REMARK 470     GLU A 230    CD   OE1  OE2                                       
REMARK 470     LYS A 234    CD   CE   NZ                                        
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 297    NZ                                                  
REMARK 470     ARG B 392    CZ   NH1  NH2                                       
REMARK 470     GLU B 397    CD   OE1  OE2                                       
REMARK 470     GLU B 406    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 416    CD   CE   NZ                                        
REMARK 470     CYS B 422    SG                                                  
REMARK 470     LYS B 423    CD   CE   NZ                                        
REMARK 470     LEU C   7    CG   CD1  CD2                                       
REMARK 470     LYS C  26    CD   CE   NZ                                        
REMARK 470     LYS C  41    CD   CE   NZ                                        
REMARK 470     GLU C  56    CD   OE1  OE2                                       
REMARK 470     LYS C  98    CD   CE                                             
REMARK 470     LYS C 141    NZ                                                  
REMARK 470     ILE C 146    CD1                                                 
REMARK 470     LYS C 150    CD   CE   NZ                                        
REMARK 470     MET C 190    CE                                                  
REMARK 470     LYS C 211    CD   CE                                             
REMARK 470     GLN C 214    CD   OE1  NE2                                       
REMARK 470     ASP C 220    CG   OD1  OD2                                       
REMARK 470     PHE C 225    O                                                   
REMARK 470     GLU C 230    CD   OE1  OE2                                       
REMARK 470     LYS C 234    CD   CE   NZ                                        
REMARK 470     LYS C 260    NZ                                                  
REMARK 470     GLU C 275    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 416    CE   NZ                                             
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    ASP A  92       70.85     56.28                                   
REMARK 500    ASP A  95      157.89     68.62                                   
REMARK 500    ARG A  96      -44.53     67.67                                   
REMARK 500    GLU A 126       47.06    -86.16                                   
REMARK 500    TYR A 144     -111.11   -143.31                                   
REMARK 500    LYS A 168      -32.95   -134.21                                   
REMARK 500    SER A 224     -151.51     61.78                                   
REMARK 500    ALA A 247     -118.25   -135.73                                   
REMARK 500    HIS A 248      -13.28     66.51                                   
REMARK 500    CYS A 273       42.93     37.03                                   
REMARK 500    ASP C  92       70.36     56.20                                   
REMARK 500    ASP C  95      158.06     68.55                                   
REMARK 500    ARG C  96      -44.82     67.73                                   
REMARK 500    GLU C 126       47.30    -86.37                                   
REMARK 500    TYR C 144     -111.24   -143.38                                   
REMARK 500    LYS C 168      -32.55   -134.73                                   
REMARK 500    SER C 224     -150.80     61.19                                   
REMARK 500    ALA C 247     -118.35   -136.05                                   
REMARK 500    HIS C 248      -13.45     66.42                                   
REMARK 500    CYS C 273       43.11     36.81                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 25981   RELATED DB: BMRB                                 
REMARK 900 25981 CONTAINS NMR CHEMICAL SHIFT ASSIGNMENTS OF REPOMAN PP1         
REMARK 900 BINDING DOMAIN                                                       
REMARK 900 RELATED ID: 5INB   RELATED DB: PDB                                   
REMARK 900 5INB CONTAINS PP1 GAMMA-REPOMAN COMPLEX STRUCTURE                    
REMARK 900 RELATED ID: 5J28   RELATED DB: PDB                                   
DBREF  5IOH A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  5IOH B  383   441  UNP    Q69YH5   CDCA2_HUMAN    383    441             
DBREF  5IOH C    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  5IOH D  383   441  UNP    Q69YH5   CDCA2_HUMAN    383    441             
SEQADV 5IOH GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH GLY B  378  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH ALA B  379  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH MET B  380  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH GLY B  381  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH TYR B  382  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH GLY C    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH HIS C    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH MET C    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH GLY C    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH SER C    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 5IOH GLY D  378  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH ALA D  379  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH MET D  380  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH GLY D  381  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5IOH TYR D  382  UNP  Q69YH5              EXPRESSION TAG                 
SEQRES   1 A  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 A  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 A  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 A  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 A  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 A  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 A  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 A  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 A  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 A  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 A  299  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 A  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 A  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 A  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 A  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 A  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 A  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 A  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 A  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 A  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 A  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 A  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 A  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 B   64  GLY ALA MET GLY TYR ALA PHE LEU ASN MET ARG LYS ARG          
SEQRES   2 B   64  LYS ARG VAL THR PHE GLY GLU ASP LEU SER PRO GLU VAL          
SEQRES   3 B   64  PHE ASP GLU SER LEU PRO ALA ASN THR PRO LEU ARG LYS          
SEQRES   4 B   64  GLY GLY THR PRO VAL CYS LYS LYS ASP PHE SER GLY LEU          
SEQRES   5 B   64  SER SER LEU LEU LEU GLU GLN SER PRO VAL PRO GLU              
SEQRES   1 C  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 C  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 C  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 C  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 C  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 C  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 C  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 C  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 C  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 C  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 C  299  ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 C  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 C  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 C  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 C  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 C  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 C  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 C  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 C  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 C  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 C  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 C  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 C  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 D   64  GLY ALA MET GLY TYR ALA PHE LEU ASN MET ARG LYS ARG          
SEQRES   2 D   64  LYS ARG VAL THR PHE GLY GLU ASP LEU SER PRO GLU VAL          
SEQRES   3 D   64  PHE ASP GLU SER LEU PRO ALA ASN THR PRO LEU ARG LYS          
SEQRES   4 D   64  GLY GLY THR PRO VAL CYS LYS LYS ASP PHE SER GLY LEU          
SEQRES   5 D   64  SER SER LEU LEU LEU GLU GLN SER PRO VAL PRO GLU              
FORMUL   5  HOH   *152(H2 O)                                                    
HELIX    1 AA1 ASN A    8  GLU A   18  1                                  11    
HELIX    2 AA2 VAL A   19  GLY A   21  5                                   3    
HELIX    3 AA3 THR A   31  GLN A   49  1                                  19    
HELIX    4 AA4 GLN A   68  GLY A   80  1                                  13    
HELIX    5 AA5 GLN A   99  TYR A  114  1                                  16    
HELIX    6 AA6 CYS A  127  ARG A  132  1                                   6    
HELIX    7 AA7 GLY A  135  TYR A  144  1                                  10    
HELIX    8 AA8 ASN A  145  ASN A  157  1                                  13    
HELIX    9 AA9 MET A  183  ARG A  188  1                                   6    
HELIX   10 AB1 GLY A  199  SER A  207  1                                   9    
HELIX   11 AB2 GLY A  228  HIS A  239  1                                  12    
HELIX   12 AB3 ASN A  271  GLU A  275  5                                   5    
HELIX   13 AB4 ASN C    8  GLU C   18  1                                  11    
HELIX   14 AB5 VAL C   19  GLY C   21  5                                   3    
HELIX   15 AB6 THR C   31  GLN C   49  1                                  19    
HELIX   16 AB7 GLN C   68  GLY C   80  1                                  13    
HELIX   17 AB8 GLN C   99  TYR C  114  1                                  16    
HELIX   18 AB9 CYS C  127  ARG C  132  1                                   6    
HELIX   19 AC1 GLY C  135  TYR C  144  1                                  10    
HELIX   20 AC2 ASN C  145  ASN C  157  1                                  13    
HELIX   21 AC3 MET C  183  ARG C  188  1                                   6    
HELIX   22 AC4 GLY C  199  SER C  207  1                                   9    
HELIX   23 AC5 GLY C  228  HIS C  239  1                                  12    
HELIX   24 AC6 ASN C  271  GLU C  275  5                                   5    
SHEET    1 AA1 6 LEU A  52  LEU A  55  0                                        
SHEET    2 AA1 6 ALA A 162  VAL A 165  1  O  ILE A 164   N  LEU A  53           
SHEET    3 AA1 6 ILE A 169  CYS A 171 -1  O  CYS A 171   N  ALA A 163           
SHEET    4 AA1 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5 AA1 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6 AA1 6 TYR A 255  PHE A 258 -1  N  PHE A 258   O  LEU A 263           
SHEET    1 AA2 6 PHE A 118  LEU A 120  0                                        
SHEET    2 AA2 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA2 6 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4 AA2 6 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5 AA2 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6 AA2 6 THR B 394  PHE B 395  1  O  THR B 394   N  CYS A 291           
SHEET    1 AA3 6 PHE A 118  LEU A 120  0                                        
SHEET    2 AA3 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA3 6 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4 AA3 6 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5 AA3 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6 AA3 6 GLU B 402  PHE B 404  1  O  GLU B 402   N  ILE A 295           
SHEET    1 AA4 3 ASP A 208  PRO A 209  0                                        
SHEET    2 AA4 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3 AA4 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1 AA5 6 LEU C  52  LEU C  55  0                                        
SHEET    2 AA5 6 ALA C 162  VAL C 165  1  O  ILE C 164   N  LEU C  53           
SHEET    3 AA5 6 ILE C 169  CYS C 171 -1  O  CYS C 171   N  ALA C 163           
SHEET    4 AA5 6 LEU C 243  ARG C 246  1  O  CYS C 245   N  PHE C 170           
SHEET    5 AA5 6 LEU C 263  LEU C 266  1  O  LEU C 266   N  ARG C 246           
SHEET    6 AA5 6 TYR C 255  PHE C 258 -1  N  GLU C 256   O  THR C 265           
SHEET    1 AA6 6 PHE C 118  LEU C 120  0                                        
SHEET    2 AA6 6 TYR C  87  PHE C  89  1  N  PHE C  89   O  PHE C 119           
SHEET    3 AA6 6 LEU C  59  CYS C  62  1  N  LYS C  60   O  LEU C  88           
SHEET    4 AA6 6 GLY C 280  VAL C 285 -1  O  MET C 283   N  ILE C  61           
SHEET    5 AA6 6 MET C 290  PRO C 298 -1  O  LEU C 296   N  GLY C 280           
SHEET    6 AA6 6 THR D 394  PHE D 395  1  O  THR D 394   N  CYS C 291           
SHEET    1 AA7 6 PHE C 118  LEU C 120  0                                        
SHEET    2 AA7 6 TYR C  87  PHE C  89  1  N  PHE C  89   O  PHE C 119           
SHEET    3 AA7 6 LEU C  59  CYS C  62  1  N  LYS C  60   O  LEU C  88           
SHEET    4 AA7 6 GLY C 280  VAL C 285 -1  O  MET C 283   N  ILE C  61           
SHEET    5 AA7 6 MET C 290  PRO C 298 -1  O  LEU C 296   N  GLY C 280           
SHEET    6 AA7 6 GLU D 402  PHE D 404  1  O  GLU D 402   N  ILE C 295           
CISPEP   1 ALA A   57    PRO A   58          0         3.40                     
CISPEP   2 PRO A   82    PRO A   83          0         1.61                     
CISPEP   3 ARG A  191    PRO A  192          0        -0.33                     
CISPEP   4 ALA C   57    PRO C   58          0         2.12                     
CISPEP   5 PRO C   82    PRO C   83          0         1.50                     
CISPEP   6 ARG C  191    PRO C  192          0         0.11                     
CRYST1  160.769   57.089   73.635  90.00  90.00  90.00 P 21 21 2     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      0.006220  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.017517  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013580        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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