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Database: PDB
Entry: 6G0I
LinkDB: 6G0I
Original site: 6G0I 
HEADER    HYDROLASE                               18-MAR-18   6G0I              
TITLE     ACTIVE FE-PP1                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PP-1A;                                                      
COMPND   6 EC: 3.1.3.16;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: TWO CYSTEINE RESIDUES ARE MODELED AS CSO              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHATASE, IRON, OXIDATIVE STRESS, CELL CYCLE, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.SALVI,O.BARABAS,M.KOEHN                                             
REVDAT   3   09-JAN-19 6G0I    1       JRNL                                     
REVDAT   2   02-JAN-19 6G0I    1       JRNL                                     
REVDAT   1   21-NOV-18 6G0I    0                                                
JRNL        AUTH   F.SALVI,M.TREBACZ,T.KOKOT,B.HOERMANN,P.RIOS,O.BARABAS,       
JRNL        AUTH 2 M.KOEHN                                                      
JRNL        TITL   EFFECTS OF STABLY INCORPORATED IRON ON PROTEIN PHOSPHATASE-1 
JRNL        TITL 2 STRUCTURE AND ACTIVITY.                                      
JRNL        REF    FEBS LETT.                    V. 592  4028 2018              
JRNL        REFN                   ISSN 1873-3468                               
JRNL        PMID   30403291                                                     
JRNL        DOI    10.1002/1873-3468.13284                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0218                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 21795                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1097                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1576                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2253                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 116                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.57                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.56000                                             
REMARK   3    B22 (A**2) : -1.16000                                             
REMARK   3    B33 (A**2) : 2.72000                                              
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.169         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.144         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.678         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2309 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2089 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3126 ; 1.510 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4824 ; 0.858 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   284 ; 6.370 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   110 ;35.361 ;23.727       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   372 ;12.088 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;15.094 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   342 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2575 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   500 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1142 ; 2.498 ; 3.721       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1141 ; 2.498 ; 3.719       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1424 ; 3.484 ; 5.570       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1425 ; 3.485 ; 5.572       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1167 ; 2.998 ; 3.949       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1164 ; 3.001 ; 3.952       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  1697 ; 4.398 ; 5.837       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  2543 ; 5.455 ;43.535       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  2528 ; 5.410 ;43.418       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6G0I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009230.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-NOV-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96770                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22907                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99500                            
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: 4MOV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% W/V PEG 3350, 0.1 M TRIS-CL, PH      
REMARK 280  8.0 RT, 1 M LITHIUM CHLORIDE SOAKED IN 18 MM ASCORBATE., VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 291K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,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        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.34300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.49750            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.34300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.49750            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 800 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     0                                                      
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     LEU A     7                                                      
REMARK 465     GLN A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ALA A   299                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     ASN A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     TYR A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     SER A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     LEU A   312                                                      
REMARK 465     ASN A   313                                                      
REMARK 465     PRO A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     ILE A   319                                                      
REMARK 465     THR A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     ARG A   323                                                      
REMARK 465     ASN A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ALA A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     LYS A   329                                                      
REMARK 465     LYS A   330                                                      
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     ASN A   8    CG   OD1  ND2                                       
REMARK 470     GLU A  18    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  26    CG   CD   CE   NZ                                   
REMARK 470     ASN A  33    CG   OD1  ND2                                       
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     LYS A 141    CG   CD   CE   NZ                                   
REMARK 470     LYS A 147    CG   CD   CE   NZ                                   
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 277    CG   OD1  OD2                                       
REMARK 470     MET A 290    CG   SD   CE                                        
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  95      155.03     78.59                                   
REMARK 500    ARG A  96      -51.65     67.33                                   
REMARK 500    GLU A 126       59.82    -90.51                                   
REMARK 500    TYR A 144     -117.09   -147.89                                   
REMARK 500    GLU A 167       14.62     55.26                                   
REMARK 500    SER A 224     -147.54     56.55                                   
REMARK 500    ALA A 247     -130.06   -132.26                                   
REMARK 500    HIS A 248      -16.96     82.58                                   
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                              FE A 403  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 HIS A  66   NE2  95.2                                              
REMARK 620 3 ASP A  92   OD2  92.9  96.8                                        
REMARK 620 4 PO4 A 401   O1  166.7  91.7  97.6                                  
REMARK 620 5 HOH A 554   O    85.1  86.8 176.1  83.9                            
REMARK 620 6 HOH A 536   O    87.1 177.7  82.8  86.1  93.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 404  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 HIS A  66   NE2  95.1                                              
REMARK 620 3 ASP A  92   OD2  92.8  96.7                                        
REMARK 620 4 PO4 A 401   O1  166.9  91.7  97.6                                  
REMARK 620 5 HOH A 554   O    85.2  86.7 176.2  84.0                            
REMARK 620 6 HOH A 536   O    87.1 177.8  82.8  86.2  93.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1  95.2                                              
REMARK 620 3 HIS A 173   NE2  80.0  86.1                                        
REMARK 620 4 HIS A 248   ND1 164.7  91.4  86.7                                  
REMARK 620 5 PO4 A 401   O2   96.2  81.6 166.8  98.4                            
REMARK 620 6 HOH A 536   O    82.4 165.5 107.4  94.6  84.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 405  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1  95.2                                              
REMARK 620 3 HIS A 173   NE2  80.1  86.2                                        
REMARK 620 4 HIS A 248   ND1 164.7  91.4  86.7                                  
REMARK 620 5 PO4 A 401   O2   96.2  81.7 166.9  98.4                            
REMARK 620 6 HOH A 536   O    82.4 165.5 107.4  94.5  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 405                  
DBREF  6G0I A    1   330  UNP    P62136   PP1A_HUMAN       1    330             
SEQADV 6G0I GLY A    0  UNP  P62136              EXPRESSION TAG                 
SEQRES   1 A  331  GLY MET SER ASP SER GLU LYS LEU ASN LEU ASP SER ILE          
SEQRES   2 A  331  ILE GLY ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY          
SEQRES   3 A  331  LYS ASN VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU          
SEQRES   4 A  331  CYS LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE          
SEQRES   5 A  331  LEU LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP          
SEQRES   6 A  331  ILE HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU          
SEQRES   7 A  331  TYR GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU          
SEQRES   8 A  331  GLY ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR          
SEQRES   9 A  331  ILE CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU          
SEQRES  10 A  331  ASN PHE PHE LEU LEU ARG GLY ASN HIS GLU CSO ALA SER          
SEQRES  11 A  331  ILE ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG          
SEQRES  12 A  331  ARG TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS          
SEQRES  13 A  331  PHE ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS          
SEQRES  14 A  331  ILE PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN          
SEQRES  15 A  331  SER MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP          
SEQRES  16 A  331  VAL PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER          
SEQRES  17 A  331  ASP PRO ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP          
SEQRES  18 A  331  ARG GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA          
SEQRES  19 A  331  LYS PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG          
SEQRES  20 A  331  ALA HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA          
SEQRES  21 A  331  LYS ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR          
SEQRES  22 A  331  CSO GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL          
SEQRES  23 A  331  ASP GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO          
SEQRES  24 A  331  ALA ASP LYS ASN LYS GLY LYS TYR GLY GLN PHE SER GLY          
SEQRES  25 A  331  LEU ASN PRO GLY GLY ARG PRO ILE THR PRO PRO ARG ASN          
SEQRES  26 A  331  SER ALA LYS ALA LYS LYS                                      
MODRES 6G0I CSO A  127  CYS  MODIFIED RESIDUE                                   
MODRES 6G0I CSO A  273  CYS  MODIFIED RESIDUE                                   
HET    CSO  A 127       7                                                       
HET    CSO  A 273       7                                                       
HET    PO4  A 401       5                                                       
HET     FE  A 402       1                                                       
HET     FE  A 403       1                                                       
HET     MN  A 404       1                                                       
HET     MN  A 405       1                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      FE FE (III) ION                                                     
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   2  PO4    O4 P 3-                                                      
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5   MN    2(MN 2+)                                                     
FORMUL   7  HOH   *116(H2 O)                                                    
HELIX    1 AA1 ASN A    8  VAL A   19  1                                  12    
HELIX    2 AA2 THR A   31  GLN A   49  1                                  19    
HELIX    3 AA3 GLN A   68  GLY A   80  1                                  13    
HELIX    4 AA4 GLN A   99  TYR A  114  1                                  16    
HELIX    5 AA5 CSO A  127  GLY A  135  1                                   9    
HELIX    6 AA6 GLY A  135  TYR A  144  1                                  10    
HELIX    7 AA7 ASN A  145  ASN A  157  1                                  13    
HELIX    8 AA8 SER A  182  ARG A  188  1                                   7    
HELIX    9 AA9 GLY A  199  SER A  207  1                                   9    
HELIX   10 AB1 GLY A  228  ASP A  240  1                                  13    
HELIX   11 AB2 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  ILE A 164   N  LEU A  53           
SHEET    3 AA1 6 ILE A 169  CYS A 171 -1  O  CYS A 171   N  ALA A 163           
SHEET    4 AA1 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5 AA1 6 LEU A 263  LEU A 266  1  O  VAL A 264   N  ILE A 244           
SHEET    6 AA1 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1 AA2 5 PHE A 118  LEU A 120  0                                        
SHEET    2 AA2 5 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA2 5 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4 AA2 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5 AA2 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1 AA3 3 ASP A 208  PRO A 209  0                                        
SHEET    2 AA3 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3 AA3 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
LINK         OD2 ASP A  64                FE    FE A 403     1555   1555  2.17  
LINK         OD2 ASP A  64                MN    MN A 404     1555   1555  2.17  
LINK         NE2 HIS A  66                FE    FE A 403     1555   1555  2.13  
LINK         NE2 HIS A  66                MN    MN A 404     1555   1555  2.13  
LINK         OD2 ASP A  92                FE    FE A 402     1555   1555  2.34  
LINK         OD2 ASP A  92                FE    FE A 403     1555   1555  2.28  
LINK         OD2 ASP A  92                MN    MN A 404     1555   1555  2.28  
LINK         OD2 ASP A  92                MN    MN A 405     1555   1555  2.34  
LINK         OD1 ASN A 124                FE    FE A 402     1555   1555  2.18  
LINK         OD1 ASN A 124                MN    MN A 405     1555   1555  2.18  
LINK         C   GLU A 126                 N   CSO A 127     1555   1555  1.32  
LINK         C   CSO A 127                 N   ALA A 128     1555   1555  1.33  
LINK         NE2 HIS A 173                FE    FE A 402     1555   1555  2.20  
LINK         NE2 HIS A 173                MN    MN A 405     1555   1555  2.20  
LINK         ND1 HIS A 248                FE    FE A 402     1555   1555  2.22  
LINK         ND1 HIS A 248                MN    MN A 405     1555   1555  2.23  
LINK         C   TYR A 272                 N   CSO A 273     1555   1555  1.34  
LINK         C   CSO A 273                 N   GLY A 274     1555   1555  1.34  
LINK         O1  PO4 A 401                FE    FE A 403     1555   1555  2.22  
LINK         O1  PO4 A 401                MN    MN A 404     1555   1555  2.22  
LINK         O2  PO4 A 401                FE    FE A 402     1555   1555  2.14  
LINK         O2  PO4 A 401                MN    MN A 405     1555   1555  2.14  
LINK        FE    FE A 402                 O   HOH A 536     1555   1555  2.01  
LINK        FE    FE A 403                 O   HOH A 554     1555   1555  2.27  
LINK        FE    FE A 403                 O   HOH A 536     1555   1555  2.07  
LINK        MN    MN A 404                 O   HOH A 554     1555   1555  2.27  
LINK        MN    MN A 404                 O   HOH A 536     1555   1555  2.07  
LINK        MN    MN A 405                 O   HOH A 536     1555   1555  2.01  
CISPEP   1 ALA A   57    PRO A   58          0         7.89                     
CISPEP   2 PRO A   82    PRO A   83          0         2.35                     
CISPEP   3 ARG A  191    PRO A  192          0        -2.70                     
SITE     1 AC1 16 HIS A  66  ASP A  92  ARG A  96  ASN A 124                    
SITE     2 AC1 16 HIS A 125  ARG A 221  HIS A 248   FE A 402                    
SITE     3 AC1 16  FE A 403   MN A 404   MN A 405  HOH A 502                    
SITE     4 AC1 16 HOH A 506  HOH A 536  HOH A 550  HOH A 554                    
SITE     1 AC2  8 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC2  8 PO4 A 401   FE A 403   MN A 404  HOH A 536                    
SITE     1 AC3  8 ASP A  64  HIS A  66  ASP A  92  PO4 A 401                    
SITE     2 AC3  8  FE A 402   MN A 405  HOH A 536  HOH A 554                    
SITE     1 AC4  8 ASP A  64  HIS A  66  ASP A  92  PO4 A 401                    
SITE     2 AC4  8  FE A 402   MN A 405  HOH A 536  HOH A 554                    
SITE     1 AC5  8 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC5  8 PO4 A 401   FE A 403   MN A 404  HOH A 536                    
CRYST1   38.365   68.686  126.995  90.00  90.00  90.00 P 2 21 21     4          
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      0.026065  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014559  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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