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Database: PDB
Entry: 5INB
LinkDB: 5INB
Original site: 5INB 
HEADER    HYDROLASE/PROTEIN BINDING               07-MAR-16   5INB              
TITLE     REPOMAN-PP1G (PROTEIN PHOSPHATASE 1, GAMMA ISOFORM) HOLOENZYME COMPLEX
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 FRAGMENT: UNP RESIDUES 7-308;                                        
COMPND   6 SYNONYM: PP-1G,PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT;             
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;                                                            
COMPND  12 FRAGMENT: PP1 BINDING DOMAIN (UNP RESIDUES 383-423);                 
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: PPP1CC;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: RP1B;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CDCA2;                                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PETM30-MBP                                
KEYWDS    PP1 GAMMA; 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 5INB    1       REMARK                                   
REVDAT   2   12-OCT-16 5INB    1       JRNL                                     
REVDAT   1   05-OCT-16 5INB    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.    1.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.40                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.890                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 221393                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.133                           
REMARK   3   R VALUE            (WORKING SET) : 0.132                           
REMARK   3   FREE R VALUE                     : 0.153                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10829                           
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 37.4152 -  4.0388    1.00     7007   368  0.1511 0.1603        
REMARK   3     2  4.0388 -  3.2062    1.00     7074   325  0.1384 0.1520        
REMARK   3     3  3.2062 -  2.8011    1.00     7040   335  0.1419 0.1554        
REMARK   3     4  2.8011 -  2.5451    1.00     7068   293  0.1324 0.1439        
REMARK   3     5  2.5451 -  2.3627    1.00     7094   317  0.1308 0.1450        
REMARK   3     6  2.3627 -  2.2234    1.00     6996   374  0.1229 0.1570        
REMARK   3     7  2.2234 -  2.1120    1.00     7006   355  0.1133 0.1439        
REMARK   3     8  2.1120 -  2.0201    1.00     6979   394  0.1123 0.1338        
REMARK   3     9  2.0201 -  1.9424    1.00     7075   348  0.1102 0.1301        
REMARK   3    10  1.9424 -  1.8753    1.00     6934   381  0.1068 0.1234        
REMARK   3    11  1.8753 -  1.8167    1.00     7024   407  0.1009 0.1453        
REMARK   3    12  1.8167 -  1.7648    1.00     6987   381  0.1045 0.1222        
REMARK   3    13  1.7648 -  1.7183    1.00     7003   387  0.1034 0.1298        
REMARK   3    14  1.7183 -  1.6764    1.00     7008   390  0.1034 0.1339        
REMARK   3    15  1.6764 -  1.6383    1.00     7036   352  0.1034 0.1335        
REMARK   3    16  1.6383 -  1.6034    1.00     7035   337  0.1093 0.1536        
REMARK   3    17  1.6034 -  1.5713    1.00     6984   336  0.1081 0.1359        
REMARK   3    18  1.5713 -  1.5417    1.00     7060   342  0.1174 0.1559        
REMARK   3    19  1.5417 -  1.5141    1.00     7022   396  0.1246 0.1461        
REMARK   3    20  1.5141 -  1.4885    1.00     6999   365  0.1298 0.1706        
REMARK   3    21  1.4885 -  1.4645    1.00     7003   370  0.1404 0.1868        
REMARK   3    22  1.4645 -  1.4419    1.00     7012   357  0.1497 0.1823        
REMARK   3    23  1.4419 -  1.4207    1.00     7019   407  0.1598 0.1932        
REMARK   3    24  1.4207 -  1.4007    1.00     7046   369  0.1642 0.1843        
REMARK   3    25  1.4007 -  1.3818    1.00     6985   374  0.1719 0.1809        
REMARK   3    26  1.3818 -  1.3638    1.00     7024   388  0.1878 0.2263        
REMARK   3    27  1.3638 -  1.3468    1.00     6967   354  0.1976 0.2179        
REMARK   3    28  1.3468 -  1.3306    1.00     7036   325  0.2096 0.2294        
REMARK   3    29  1.3306 -  1.3151    1.00     7071   355  0.2166 0.2344        
REMARK   3    30  1.3151 -  1.3003    0.99     6970   347  0.2406 0.2641        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.110            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.010           
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      :  0.008           2905                                  
REMARK   3   ANGLE     :  1.243           3962                                  
REMARK   3   CHIRALITY :  0.089            425                                  
REMARK   3   PLANARITY :  0.005            526                                  
REMARK   3   DIHEDRAL  : 12.824           1134                                  
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 5INB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219110.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL, NON FIXED EXIT SLIT       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOV 3, 2014                    
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS NOV 3, 2014                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 234338                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.400                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.900                              
REMARK 200  R MERGE                    (I) : 0.04900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.09270                            
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 2.5.6                                          
REMARK 200 STARTING MODEL: 1JK7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M SODIUM MALONATE, PH 4.3, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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       71.96467            
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      143.92933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      107.94700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      179.91167            
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       35.98233            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.96467            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      143.92933            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      179.91167            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      107.94700            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       35.98233            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ASN A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     ARG A   308                                                      
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     LYS B   423                                                      
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  56    CD   OE1  OE2                                       
REMARK 470     LYS A  98    CD   CE   NZ                                        
REMARK 470     LYS A 147    CD   CE   NZ                                        
REMARK 470     LYS A 211    CD   CE   NZ                                        
REMARK 470     LYS A 260    CE   NZ                                             
REMARK 470     ARG B 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 415    NE   CZ   NH1  NH2                                  
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    HOH A   709     O    HOH A   739              2.02            
REMARK 500   OE2  GLU A    84     O    HOH A   501              2.03            
REMARK 500   O    HOH A   534     O    HOH A   725              2.06            
REMARK 500   O    HOH A   519     O    HOH A   702              2.06            
REMARK 500   O    HOH B   503     O    HOH B   544              2.12            
REMARK 500   O    HOH A   515     O    HOH A   630              2.18            
REMARK 500   O    HOH A   703     O    HOH A   709              2.19            
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    ASP A  92       64.67     63.32                                   
REMARK 500    ASP A  95      151.87     77.33                                   
REMARK 500    ARG A  96      -50.46     78.46                                   
REMARK 500    TYR A 144     -112.38   -133.84                                   
REMARK 500    GLU A 167       19.07     59.43                                   
REMARK 500    SER A 224     -151.11     63.93                                   
REMARK 500    ALA A 247     -132.71   -132.52                                   
REMARK 500    HIS A 248      -13.05     81.85                                   
REMARK 500    ASP A 277       52.29    -94.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 408  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  54   OE1                                                    
REMARK 620 2 GLU A  54   OE2  43.1                                              
REMARK 620 3 GLU A 167   OE2  64.0 106.2                                        
REMARK 620 4 HOH A 721   O   149.1 106.3 146.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 408                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IOH   RELATED DB: PDB                                   
REMARK 900 5IOH CONTAINS PP1 ALPHA ISOFORM:REPOMAN COMPLEX                      
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: 5J28   RELATED DB: PDB                                   
DBREF  5INB A    7   308  UNP    P36873   PP1G_HUMAN       7    308             
DBREF  5INB B  383   423  UNP    Q69YH5   CDCA2_HUMAN    383    423             
SEQADV 5INB GLY A    4  UNP  P36873              EXPRESSION TAG                 
SEQADV 5INB HIS A    5  UNP  P36873              EXPRESSION TAG                 
SEQADV 5INB MET A    6  UNP  P36873              EXPRESSION TAG                 
SEQADV 5INB GLY B  378  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5INB ALA B  379  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5INB MET B  380  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5INB GLY B  381  UNP  Q69YH5              EXPRESSION TAG                 
SEQADV 5INB TYR B  382  UNP  Q69YH5              EXPRESSION TAG                 
SEQRES   1 A  305  GLY HIS MET LEU ASN ILE ASP SER ILE ILE GLN ARG LEU          
SEQRES   2 A  305  LEU GLU VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN          
SEQRES   3 A  305  LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER          
SEQRES   4 A  305  ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU          
SEQRES   5 A  305  GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN          
SEQRES   6 A  305  TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE          
SEQRES   7 A  305  PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL          
SEQRES   8 A  305  ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU          
SEQRES   9 A  305  LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU          
SEQRES  10 A  305  LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE          
SEQRES  11 A  305  TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE          
SEQRES  12 A  305  LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU          
SEQRES  13 A  305  PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS          
SEQRES  14 A  305  HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN          
SEQRES  15 A  305  ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN          
SEQRES  16 A  305  GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS          
SEQRES  17 A  305  ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER          
SEQRES  18 A  305  PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS          
SEQRES  19 A  305  LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL          
SEQRES  20 A  305  VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU          
SEQRES  21 A  305  VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY GLU PHE          
SEQRES  22 A  305  ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU THR LEU          
SEQRES  23 A  305  MET CYS SER PHE GLN ILE LEU LYS PRO ALA GLU LYS LYS          
SEQRES  24 A  305  LYS PRO ASN ALA THR ARG                                      
SEQRES   1 B   46  GLY ALA MET GLY TYR ALA PHE LEU ASN MET ARG LYS ARG          
SEQRES   2 B   46  LYS ARG VAL THR PHE GLY GLU ASP LEU SER PRO GLU VAL          
SEQRES   3 B   46  PHE ASP GLU SER LEU PRO ALA ASN THR PRO LEU ARG LYS          
SEQRES   4 B   46  GLY GLY THR PRO VAL CYS LYS                                  
HET    MLI  A 401       7                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HET     NA  A 408       1                                                       
HETNAM     MLI MALONATE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  MLI    C3 H2 O4 2-                                                  
FORMUL   4  GOL    6(C3 H8 O3)                                                  
FORMUL  10   NA    NA 1+                                                        
FORMUL  11  HOH   *304(H2 O)                                                    
HELIX    1 AA1 ASN A    8  GLU A   18  1                                  11    
HELIX    2 AA2 VAL A   19  SER A   22  5                                   4    
HELIX    3 AA3 GLN 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 SER A  182  ARG A  188  1                                   7    
HELIX   10 AB1 GLY A  199  SER A  207  1                                   9    
HELIX   11 AB2 GLY A  228  ASP A  240  1                                  13    
HELIX   12 AB3 ASN A  271  GLU A  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  ALA A 162   N  LEU A  53           
SHEET    3 AA1 6 ILE A 169  CYS A 172 -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  GLU A 256   O  THR A 265           
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  CYS A  62   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  CYS A  62   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           
LINK         OE1 GLU A  54                NA    NA A 408     1555   1555  3.17  
LINK         OE2 GLU A  54                NA    NA A 408     1555   1555  2.57  
LINK         OE2 GLU A 167                NA    NA A 408     1555   1555  2.58  
LINK        NA    NA A 408                 O   HOH A 721     1555   1555  2.09  
CISPEP   1 ALA A   57    PRO A   58          0         6.75                     
CISPEP   2 PRO A   82    PRO A   83          0         6.46                     
CISPEP   3 ARG A  191    PRO A  192          0        -0.69                     
SITE     1 AC1 12 ASP A  64  HIS A  66  ASP A  92  GLU A 218                    
SITE     2 AC1 12 ASP A 220  ARG A 221  HIS A 248  TYR A 272                    
SITE     3 AC1 12 GOL A 402  HOH A 538  HOH A 542  HOH A 614                    
SITE     1 AC2  9 GLU A 218  ASN A 219  ASP A 220  GLN A 249                    
SITE     2 AC2  9 VAL A 250  MLI A 401  HOH A 513  HOH A 598                    
SITE     3 AC2  9 HOH A 630                                                     
SITE     1 AC3  7 GLN A 185  ARG A 188  SER A 224  PHE A 225                    
SITE     2 AC3  7 HOH A 505  HOH A 516  HOH A 520                               
SITE     1 AC4  8 CYS A 127  SER A 129  VAL A 195  PRO A 196                    
SITE     2 AC4  8 ASP A 197  CYS A 202  TRP A 206  HOH A 649                    
SITE     1 AC5  9 PRO A  50  LEU A  53  GLU A  54  GLU A 116                    
SITE     2 AC5  9 PHE A 119  LYS A 141  HOH A 621  HOH A 653                    
SITE     3 AC5  9 HOH A 674                                                     
SITE     1 AC6  8 PRO A  58  LEU A  59  LYS A  60  SER A  85                    
SITE     2 AC6  8 ASN A  86  SER A 284  VAL A 285  HOH A 528                    
SITE     1 AC7  8 PRO A 209  GLN A 249  VAL A 251  GLU A 256                    
SITE     2 AC7  8 HOH A 515  HOH A 552  HOH A 577  HOH A 592                    
SITE     1 AC8  4 GLU A  54  ILE A 164  GLU A 167  HOH A 721                    
CRYST1   86.371   86.371  215.894  90.00  90.00 120.00 P 61 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011578  0.006685  0.000000        0.00000                         
SCALE2      0.000000  0.013369  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004632        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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