GenomeNet

Database: PDB
Entry: 3N5U
LinkDB: 3N5U
Original site: 3N5U 
HEADER    HYDROLASE, TRANSCRIPTION REGULATION     25-MAY-10   3N5U              
TITLE     CRYSTAL STRUCTURE OF AN RB C-TERMINAL PEPTIDE BOUND TO THE CATALYTIC  
TITLE    2 SUBUNIT OF PP1                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 1-300;                                        
COMPND   6 SYNONYM: PP-1A;                                                      
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: RETINOBLASTOMA-ASSOCIATED PROTEIN;                         
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 870-882;                                      
COMPND  13 SYNONYM: PRB, RB, PP110, P105-RB;                                    
COMPND  14 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: PPP1A, PPP1CA;                                                 
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: PFLAG-CTS;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 OTHER_DETAILS: SYNTHETIC 13-MER PEPTIDE                              
KEYWDS    RETINOBLASTOMA, PRB, RB, PROTEIN PHOSPHATASE-1, PP1, PHOSPHATASE,     
KEYWDS   2 HYDROLASE, TRANSCRIPTION REGULATION                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.HIRSCHI,M.CECCHINI,R.C.STEINHARDT,F.A.DICK,S.M.RUBIN              
REVDAT   3   27-OCT-10 3N5U    1       MTRIX1                                   
REVDAT   2   15-SEP-10 3N5U    1       JRNL                                     
REVDAT   1   11-AUG-10 3N5U    0                                                
JRNL        AUTH   A.HIRSCHI,M.CECCHINI,R.C.STEINHARDT,M.R.SCHAMBER,F.A.DICK,   
JRNL        AUTH 2 S.M.RUBIN                                                    
JRNL        TITL   AN OVERLAPPING KINASE AND PHOSPHATASE DOCKING SITE REGULATES 
JRNL        TITL 2 ACTIVITY OF THE RETINOBLASTOMA PROTEIN.                      
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17  1051 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20694007                                                     
JRNL        DOI    10.1038/NSMB.1868                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 83.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 13588                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1358                            
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 83.7190 -  6.8930    0.97     1413   140  0.1940 0.2040        
REMARK   3     2  6.8930 -  5.4720    0.96     1288   145  0.2220 0.2830        
REMARK   3     3  5.4720 -  4.7800    0.95     1286   126  0.2130 0.2490        
REMARK   3     4  4.7800 -  4.3430    0.96     1251   136  0.1950 0.2450        
REMARK   3     5  4.3430 -  4.0320    0.95     1207   157  0.1990 0.2370        
REMARK   3     6  4.0320 -  3.7940    0.93     1218   134  0.2230 0.2830        
REMARK   3     7  3.7940 -  3.6040    0.93     1210   128  0.2460 0.2820        
REMARK   3     8  3.6040 -  3.4470    0.91     1131   137  0.2440 0.2740        
REMARK   3     9  3.4470 -  3.3140    0.90     1153   132  0.2580 0.2970        
REMARK   3    10  3.3140 -  3.2000    0.85     1073   123  0.2750 0.3120        
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              : 0.34                                          
REMARK   3   B_SOL              : 20.56                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.450            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 16.06200                                             
REMARK   3    B22 (A**2) : 16.06200                                             
REMARK   3    B33 (A**2) : -32.12300                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           4900                                  
REMARK   3   ANGLE     :  0.789           6616                                  
REMARK   3   CHIRALITY :  0.058            709                                  
REMARK   3   PLANARITY :  0.003            863                                  
REMARK   3   DIHEDRAL  : 14.918           1809                                  
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 : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: chain A and (resseq 7:300 )                 
REMARK   3     SELECTION          : chain B and (resseq 7:300 )                 
REMARK   3     ATOM PAIRS NUMBER  : 2364                                        
REMARK   3     RMSD               : 0.015                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3N5U COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059417.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : ASSYMETRIC CURVED CRYSTAL          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD AREA DETECTOR                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13588                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 200MM MGCL2, 18% PEG        
REMARK 280  4000, PH 7.5, HANGING DROP, TEMPERATURE 298K                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       96.19050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.47300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.47300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       48.09525            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.47300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.47300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      144.28575            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.47300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.47300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       48.09525            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.47300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.47300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      144.28575            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.19050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLU B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     LYS C   870                                                      
REMARK 465     PRO C   871                                                      
REMARK 465     LEU C   872                                                      
REMARK 465     GLU C   880                                                      
REMARK 465     GLY C   881                                                      
REMARK 465     SER C   882                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PHE C 877   CB  -  CA  -  C   ANGL. DEV. = -18.1 DEGREES          
REMARK 500    ASP C 878   N   -  CA  -  CB  ANGL. DEV. = -12.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  20      104.87    -53.76                                   
REMARK 500    SER A  22       56.51   -148.64                                   
REMARK 500    ARG A  23      146.70     75.31                                   
REMARK 500    HIS A  66       59.80     38.46                                   
REMARK 500    ASP A  95      144.83     83.45                                   
REMARK 500    ARG A  96      -52.35     69.62                                   
REMARK 500    GLU A 126       59.76    -93.24                                   
REMARK 500    TYR A 144     -107.03   -131.66                                   
REMARK 500    ASN A 157       -6.14    -58.71                                   
REMARK 500    SER A 224     -162.33     59.98                                   
REMARK 500    ALA A 247     -117.98   -122.24                                   
REMARK 500    HIS A 248      -26.83     74.89                                   
REMARK 500    TYR A 272      -34.56    -32.44                                   
REMARK 500    CYS A 273       19.86   -149.67                                   
REMARK 500    PHE A 276      -34.54   -141.82                                   
REMARK 500    ASP A 277       17.87     59.18                                   
REMARK 500    LEU A 289       36.20     71.34                                   
REMARK 500    PRO A 298     -104.42    -76.10                                   
REMARK 500    ALA A 299      123.65   -174.72                                   
REMARK 500    GLN B  20      104.84    -54.24                                   
REMARK 500    SER B  22       56.75   -148.97                                   
REMARK 500    ARG B  23      146.81     75.77                                   
REMARK 500    LEU B  59      147.97   -170.15                                   
REMARK 500    HIS B  66       59.72     38.98                                   
REMARK 500    ASP B  95      144.66     83.04                                   
REMARK 500    ARG B  96      -51.95     68.83                                   
REMARK 500    GLU B 126       59.43    -93.56                                   
REMARK 500    TYR B 144     -107.56   -131.42                                   
REMARK 500    ASN B 157       -6.84    -58.54                                   
REMARK 500    SER B 224     -162.64     60.07                                   
REMARK 500    ALA B 247     -117.92   -121.11                                   
REMARK 500    HIS B 248      -27.26     75.29                                   
REMARK 500    TYR B 272      -33.93    -33.09                                   
REMARK 500    CYS B 273       20.42   -149.71                                   
REMARK 500    PHE B 276      -34.18   -141.94                                   
REMARK 500    ASP B 277       17.77     58.93                                   
REMARK 500    LEU B 289       36.28     71.02                                   
REMARK 500    PRO B 298     -104.34    -75.81                                   
REMARK 500    ALA B 299      122.92   -175.67                                   
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                              MN B   4  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  92   OD2                                                    
REMARK 620 2 HIS B 248   ND1 152.1                                              
REMARK 620 3 ASN B 124   OD1 101.2  77.2                                        
REMARK 620 4 HIS B 173   NE2  81.0  73.2  64.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B   3  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  64   OD2                                                    
REMARK 620 2 ASP B  92   OD2  72.0                                              
REMARK 620 3 HIS B  66   NE2  89.7  73.4                                        
REMARK 620 4  MN B   4  MN    90.1  48.3 118.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A   2  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 HIS A 248   ND1 153.8                                              
REMARK 620 3 ASN A 124   OD1 100.5  76.6                                        
REMARK 620 4 HIS A 173   NE2  81.8  73.5  64.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A   1  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  66   NE2                                                    
REMARK 620 2 ASP A  64   OD2  89.3                                              
REMARK 620 3 ASP A  92   OD2  74.5  70.8                                        
REMARK 620 4  MN A   2  MN   119.8  87.3  47.9                                  
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 MN A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 2                    
DBREF  3N5U A    1   300  UNP    P62136   PP1A_HUMAN       1    300             
DBREF  3N5U B    1   300  UNP    P62136   PP1A_HUMAN       1    300             
DBREF  3N5U C  870   882  UNP    P06400   RB_HUMAN       870    882             
SEQRES   1 A  300  MET SER ASP SER GLU LYS LEU ASN LEU ASP SER ILE ILE          
SEQRES   2 A  300  GLY ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS          
SEQRES   3 A  300  ASN VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS          
SEQRES   4 A  300  LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU          
SEQRES   5 A  300  LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE          
SEQRES   6 A  300  HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR          
SEQRES   7 A  300  GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY          
SEQRES   8 A  300  ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE          
SEQRES   9 A  300  CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN          
SEQRES  10 A  300  PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE          
SEQRES  11 A  300  ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG          
SEQRES  12 A  300  TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE          
SEQRES  13 A  300  ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE          
SEQRES  14 A  300  PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER          
SEQRES  15 A  300  MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL          
SEQRES  16 A  300  PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP          
SEQRES  17 A  300  PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG          
SEQRES  18 A  300  GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS          
SEQRES  19 A  300  PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA          
SEQRES  20 A  300  HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS          
SEQRES  21 A  300  ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS          
SEQRES  22 A  300  GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP          
SEQRES  23 A  300  GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA          
SEQRES  24 A  300  ASP                                                          
SEQRES   1 B  300  MET SER ASP SER GLU LYS LEU ASN LEU ASP SER ILE ILE          
SEQRES   2 B  300  GLY ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS          
SEQRES   3 B  300  ASN VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS          
SEQRES   4 B  300  LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU          
SEQRES   5 B  300  LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE          
SEQRES   6 B  300  HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR          
SEQRES   7 B  300  GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY          
SEQRES   8 B  300  ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE          
SEQRES   9 B  300  CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN          
SEQRES  10 B  300  PHE PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE          
SEQRES  11 B  300  ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG          
SEQRES  12 B  300  TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE          
SEQRES  13 B  300  ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE          
SEQRES  14 B  300  PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER          
SEQRES  15 B  300  MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL          
SEQRES  16 B  300  PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP          
SEQRES  17 B  300  PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG          
SEQRES  18 B  300  GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS          
SEQRES  19 B  300  PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA          
SEQRES  20 B  300  HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS          
SEQRES  21 B  300  ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS          
SEQRES  22 B  300  GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP          
SEQRES  23 B  300  GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA          
SEQRES  24 B  300  ASP                                                          
SEQRES   1 C   13  LYS PRO LEU LYS LYS LEU ARG PHE ASP ILE GLU GLY SER          
HET     MN  A   1       1                                                       
HET     MN  A   2       1                                                       
HET     MN  B   3       1                                                       
HET     MN  B   4       1                                                       
HET     CL  A 301       1                                                       
HET     CL  B   2       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM      CL CHLORIDE ION                                                     
FORMUL   4   MN    4(MN 2+)                                                     
FORMUL   8   CL    2(CL 1-)                                                     
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 THR A   31  GLN A   49  1                                  19    
HELIX    3   3 GLN A   68  GLY A   80  1                                  13    
HELIX    4   4 GLN A   99  TYR A  114  1                                  16    
HELIX    5   5 CYS A  127  ARG A  132  1                                   6    
HELIX    6   6 GLY A  135  TYR A  144  1                                  10    
HELIX    7   7 ASN A  145  ASN A  157  1                                  13    
HELIX    8   8 SER A  182  ARG A  188  1                                   7    
HELIX    9   9 GLN A  198  SER A  207  1                                  10    
HELIX   10  10 GLY A  228  HIS A  239  1                                  12    
HELIX   11  11 ASN B    8  GLU B   18  1                                  11    
HELIX   12  12 THR B   31  GLN B   49  1                                  19    
HELIX   13  13 GLN B   68  GLY B   80  1                                  13    
HELIX   14  14 GLN B   99  TYR B  114  1                                  16    
HELIX   15  15 CYS B  127  ARG B  132  1                                   6    
HELIX   16  16 GLY B  135  TYR B  144  1                                  10    
HELIX   17  17 ASN B  145  ASN B  157  1                                  13    
HELIX   18  18 SER B  182  ARG B  188  1                                   7    
HELIX   19  19 GLN B  198  SER B  207  1                                  10    
HELIX   20  20 GLY B  228  HIS B  239  1                                  12    
SHEET    1   A 6 LEU A  52  LEU A  53  0                                        
SHEET    2   A 6 ALA A 162  VAL A 165  1  O  ALA A 162   N  LEU A  53           
SHEET    3   A 6 ILE A 169  CYS A 171 -1  O  CYS A 171   N  ALA A 163           
SHEET    4   A 6 LEU A 243  ARG A 246  1  O  LEU A 243   N  PHE A 170           
SHEET    5   A 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6   A 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1   B 6 PHE A 118  LEU A 120  0                                        
SHEET    2   B 6 TYR A  87  PHE A  89  1  N  TYR A  87   O  PHE A 119           
SHEET    3   B 6 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4   B 6 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5   B 6 MET A 290  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    6   B 6 ARG C 876  PHE C 877  1  O  ARG C 876   N  CYS A 291           
SHEET    1   C 3 ASP A 208  PRO A 209  0                                        
SHEET    2   C 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3   C 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1   D 6 LEU B  52  LEU B  53  0                                        
SHEET    2   D 6 ALA B 162  VAL B 165  1  O  ALA B 162   N  LEU B  53           
SHEET    3   D 6 ILE B 169  CYS B 171 -1  O  CYS B 171   N  ALA B 163           
SHEET    4   D 6 LEU B 243  ARG B 246  1  O  LEU B 243   N  PHE B 170           
SHEET    5   D 6 LEU B 263  LEU B 266  1  O  LEU B 266   N  ARG B 246           
SHEET    6   D 6 TYR B 255  PHE B 258 -1  N  GLU B 256   O  THR B 265           
SHEET    1   E 5 PHE B 118  LEU B 120  0                                        
SHEET    2   E 5 TYR B  87  PHE B  89  1  N  TYR B  87   O  PHE B 119           
SHEET    3   E 5 LEU B  59  CYS B  62  1  N  CYS B  62   O  LEU B  88           
SHEET    4   E 5 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5   E 5 CYS B 291  LEU B 296 -1  O  LEU B 296   N  GLY B 280           
SHEET    1   F 3 ASP B 208  PRO B 209  0                                        
SHEET    2   F 3 PHE B 225  PHE B 227  1  O  PHE B 227   N  ASP B 208           
SHEET    3   F 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         OD2 ASP B  92                MN    MN B   4     1555   1555  2.22  
LINK         OD2 ASP B  64                MN    MN B   3     1555   1555  2.22  
LINK         OD2 ASP A  92                MN    MN A   2     1555   1555  2.22  
LINK         NE2 HIS A  66                MN    MN A   1     1555   1555  2.27  
LINK         OD2 ASP A  64                MN    MN A   1     1555   1555  2.29  
LINK         ND1 HIS A 248                MN    MN A   2     1555   1555  2.30  
LINK         ND1 HIS B 248                MN    MN B   4     1555   1555  2.32  
LINK         OD1 ASN B 124                MN    MN B   4     1555   1555  2.34  
LINK         OD2 ASP B  92                MN    MN B   3     1555   1555  2.34  
LINK         OD2 ASP A  92                MN    MN A   1     1555   1555  2.34  
LINK         NE2 HIS B  66                MN    MN B   3     1555   1555  2.36  
LINK         OD1 ASN A 124                MN    MN A   2     1555   1555  2.37  
LINK         NE2 HIS A 173                MN    MN A   2     1555   1555  2.42  
LINK         NE2 HIS B 173                MN    MN B   4     1555   1555  2.44  
LINK        MN    MN B   3                MN    MN B   4     1555   1555  2.92  
LINK        MN    MN A   1                MN    MN A   2     1555   1555  2.96  
CISPEP   1 ALA A   57    PRO A   58          0         0.64                     
CISPEP   2 PRO A   82    PRO A   83          0        -0.15                     
CISPEP   3 ARG A  191    PRO A  192          0         2.06                     
CISPEP   4 ALA B   57    PRO B   58          0         0.04                     
CISPEP   5 PRO B   82    PRO B   83          0        -0.49                     
CISPEP   6 ARG B  191    PRO B  192          0         1.64                     
SITE     1 AC1  6  MN A   2  ASP A  64  HIS A  66  ASP A  92                    
SITE     2 AC1  6 TYR A 272   CL A 301                                          
SITE     1 AC2  7  MN A   1  ASP A  64  ASP A  92  ASN A 124                    
SITE     2 AC2  7 HIS A 173  HIS A 248   CL A 301                               
SITE     1 AC3  6  CL B   2   MN B   4  ASP B  64  HIS B  66                    
SITE     2 AC3  6 ASP B  92  TYR B 272                                          
SITE     1 AC4  7  CL B   2   MN B   3  ASP B  64  ASP B  92                    
SITE     2 AC4  7 ASN B 124  HIS B 173  HIS B 248                               
SITE     1 AC5  5  MN A   1   MN A   2  ARG A  96  HIS A 125                    
SITE     2 AC5  5 ARG A 221                                                     
SITE     1 AC6  6  MN B   3   MN B   4  ARG B  96  ASN B 124                    
SITE     2 AC6  6 HIS B 125  ARG B 221                                          
CRYST1   92.946   92.946  192.381  90.00  90.00  90.00 P 41 21 2    16          
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      0.010759  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010759  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005198        0.00000                         
MTRIX1   1 -0.386983  0.921948 -0.016028       65.74210    1                    
MTRIX2   1  0.921479  0.386038 -0.043035      -42.63000    1                    
MTRIX3   1 -0.033489 -0.031423 -0.998945       43.08720    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system