GenomeNet

Database: PDB
Entry: 4UT3
LinkDB: 4UT3
Original site: 4UT3 
HEADER    HYDROLASE                               17-JUL-14   4UT3              
TITLE     X-RAY STRUCTURE OF THE HUMAN PP1 GAMMA CATALYTIC SUBUNIT              
TITLE    2 TREATED WITH HYDROGEN PEROXIDE                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC   
COMPND   3  SUBUNIT;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PP-1G, PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT, PROTEIN    
COMPND   6  PHOSPHATASE 1 GAMMA ISOFORM;                                        
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC   
COMPND  11  SUBUNIT;                                                            
COMPND  12 CHAIN: B;                                                            
COMPND  13 SYNONYM: PP-1G, PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT, PROTEIN    
COMPND  14  PHOSPHATASE 1 GAMMA ISOFORM;                                        
COMPND  15 EC: 3.1.3.16;                                                        
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];                      
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 668369;                                     
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI DH5[ALPHA];                      
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 668369                                      
KEYWDS    METAL CENTER, METALLOPROTEIN, ENZYME ACTIVATION, PHOSPHOPROTEIN       
KEYWDS   2 PHOSPHATASES, PROTEIN PHOSPHATASE 1, HYDROLASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZEH SILVA,J.KOPEC,D.FOTINOU,R.A.STEINER                             
REVDAT   2   25-JAN-17 4UT3    1       AUTHOR JRNL                              
REVDAT   1   22-JUL-15 4UT3    0                                                
JRNL        AUTH   C.X.SANTOS,A.D.HAFSTAD,M.BERETTA,M.ZHANG,C.MOLENAAR,J.KOPEC, 
JRNL        AUTH 2 D.FOTINOU,T.V.MURRAY,A.M.COBB,D.MARTIN,M.ZEH SILVA,          
JRNL        AUTH 3 N.ANILKUMAR,K.SCHRODER,C.M.SHANAHAN,A.C.BREWER,R.P.BRANDES,  
JRNL        AUTH 4 E.BLANC,M.PARSONS,V.BELOUSOV,R.CAMMACK,R.C.HIDER,            
JRNL        AUTH 5 R.A.STEINER,A.M.SHAH                                         
JRNL        TITL   TARGETED REDOX INHIBITION OF PROTEIN PHOSPHATASE 1 BY NOX4   
JRNL        TITL 2 REGULATES EIF2ALPHA-MEDIATED STRESS SIGNALING.               
JRNL        REF    EMBO J.                       V.  35   319 2016              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   26742780                                                     
JRNL        DOI    10.15252/EMBJ.201592394                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.69                          
REMARK   3   NUMBER OF REFLECTIONS             : 33509                          
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) : 0.17518                         
REMARK   3   R VALUE            (WORKING SET) : 0.17336                         
REMARK   3   FREE R VALUE                     : 0.21146                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1742                            
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) : 2.189                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.246                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1959                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.315                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 114                          
REMARK   3   BIN FREE R VALUE                    : 0.339                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4740                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 160                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.211                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -32.79                                               
REMARK   3    B22 (A**2) : 46.00                                                
REMARK   3    B33 (A**2) : -13.21                                               
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -4.58                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.050         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.039         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.460         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4879 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4640 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6583 ; 1.267 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10690 ; 0.810 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   590 ; 5.955 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   242 ;36.751 ;23.967       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   863 ;13.870 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;16.118 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   704 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5480 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1154 ; 0.003 ; 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):  2354 ; 2.918 ; 4.391       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2353 ; 2.917 ; 4.390       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2940 ; 4.351 ; 6.580       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2525 ; 3.882 ; 4.901       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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          
REMARK   3   RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY                    
REMARK   4                                                                      
REMARK   4 4UT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-61269.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97620                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL (PILATUS 6M)                 
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35328                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.20                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.40                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.3                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.62                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.10                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2O8A                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7-12% PEG3350, 0.1 M BICINE, PH          
REMARK 280  9.0 SOAKING IN RESERVOIR ENRICHED WITH 50MM H2O2 FOR 10             
REMARK 280  MINS CRYOPROTECTION IN RESEVOIR ENRICHED WITH 25% MPD               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.61000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ASN A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     ARG A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     VAL A   310                                                      
REMARK 465     THR A   311                                                      
REMARK 465     PRO A   312                                                      
REMARK 465     PRO A   313                                                      
REMARK 465     ARG A   314                                                      
REMARK 465     GLY A   315                                                      
REMARK 465     MET A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     LYS A   319                                                      
REMARK 465     GLN A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     GLU B   300                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     LYS B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     PRO B   304                                                      
REMARK 465     ASN B   305                                                      
REMARK 465     ALA B   306                                                      
REMARK 465     THR B   307                                                      
REMARK 465     ARG B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     VAL B   310                                                      
REMARK 465     THR B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     PRO B   313                                                      
REMARK 465     ARG B   314                                                      
REMARK 465     GLY B   315                                                      
REMARK 465     MET B   316                                                      
REMARK 465     ILE B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     LYS B   319                                                      
REMARK 465     GLN B   320                                                      
REMARK 465     ALA B   321                                                      
REMARK 465     LYS B   322                                                      
REMARK 465     LYS B   323                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   PO4 A   501     O    HOH A  2021              2.19            
REMARK 500   O1   PO4 B   501     O    HOH B  2017              2.13            
REMARK 500   O    HOH A  2028     O    HOH A  2063              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  95      152.74     83.06                                   
REMARK 500    ARG A  96      -49.60     70.08                                   
REMARK 500    TYR A 144     -109.91   -135.24                                   
REMARK 500    SER A 224     -154.44     61.22                                   
REMARK 500    ALA A 247     -130.85   -126.87                                   
REMARK 500    HIS A 248      -22.68     85.14                                   
REMARK 500    CYS A 273       -1.09     72.05                                   
REMARK 500    ASP B  95      151.77     83.27                                   
REMARK 500    ARG B  96      -49.94     71.45                                   
REMARK 500    TYR B 144     -109.88   -134.55                                   
REMARK 500    SER B 224     -153.49     60.70                                   
REMARK 500    ALA B 247     -130.62   -126.35                                   
REMARK 500    HIS B 248      -23.37     85.67                                   
REMARK 500    CSO B 273       -0.79     72.07                                   
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 A 400  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 HOH A2021   O    69.7                                              
REMARK 620 3 PO4 A 501   O3   91.7  74.2                                        
REMARK 620 4 ASP A  64   OD2  96.2  93.6 162.2                                  
REMARK 620 5 HIS A  66   NE2  97.5 161.8  93.9 100.9                            
REMARK 620 6 HOH A2022   O   175.5 106.0  88.1  82.8  87.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 400  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  64   OD2                                                    
REMARK 620 2 HIS B  66   NE2  98.3                                              
REMARK 620 3 HOH B2018   O    89.3  96.6                                        
REMARK 620 4 ASP B  92   OD2  96.0  98.0 163.6                                  
REMARK 620 5 PO4 B 501   O3  164.5  91.7  77.7  94.3                            
REMARK 620 6 HOH B2017   O    90.9 166.1  93.9  70.6  81.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 248   ND1                                                    
REMARK 620 2 PO4 A 501   O4   88.3                                              
REMARK 620 3 ASP A  92   OD2 155.7  94.7                                        
REMARK 620 4 ASN A 124   OD1 100.2  87.8 104.0                                  
REMARK 620 5 HIS A 173   NE2  88.8 175.1  89.6  88.7                            
REMARK 620 6 HOH A2021   O    84.5  66.5  74.7 153.8 117.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 173   NE2                                                    
REMARK 620 2 ASP B  92   OD2  91.9                                              
REMARK 620 3 ASN B 124   OD1  90.1 102.6                                        
REMARK 620 4 HIS B 248   ND1  91.9 156.2 101.0                                  
REMARK 620 5 PO4 B 501   O1  176.9  91.2  89.0  85.4                            
REMARK 620 6 HOH B2017   O   117.1  74.0 152.5  83.3  64.1                      
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  MN A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UT2   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF THE HUMAN PP1 GAMMA CATALYTIC                    
REMARK 900  SUBUNIT TREATED WITH ASCORBATE                                      
DBREF  4UT3 A    1   323  UNP    P36873   PP1G_HUMAN       1    323             
DBREF  4UT3 B    1   323  UNP    P36873   PP1G_HUMAN       1    323             
SEQRES   1 A  323  MET ALA ASP LEU ASP LYS LEU ASN ILE ASP SER ILE ILE          
SEQRES   2 A  323  GLN ARG LEU LEU GLU VAL ARG GLY SER LYS PRO GLY LYS          
SEQRES   3 A  323  ASN VAL GLN LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS          
SEQRES   4 A  323  LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU          
SEQRES   5 A  323  LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE          
SEQRES   6 A  323  HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR          
SEQRES   7 A  323  GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY          
SEQRES   8 A  323  ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE          
SEQRES   9 A  323  CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN          
SEQRES  10 A  323  PHE PHE LEU LEU ARG GLY ASN HIS GLU CSO ALA SER ILE          
SEQRES  11 A  323  ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG          
SEQRES  12 A  323  TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE          
SEQRES  13 A  323  ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE          
SEQRES  14 A  323  PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER          
SEQRES  15 A  323  MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL          
SEQRES  16 A  323  PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP          
SEQRES  17 A  323  PRO ASP LYS ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG          
SEQRES  18 A  323  GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS          
SEQRES  19 A  323  PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA          
SEQRES  20 A  323  HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS          
SEQRES  21 A  323  ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS          
SEQRES  22 A  323  GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP          
SEQRES  23 A  323  GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA          
SEQRES  24 A  323  GLU LYS LYS LYS PRO ASN ALA THR ARG PRO VAL THR PRO          
SEQRES  25 A  323  PRO ARG GLY MET ILE THR LYS GLN ALA LYS LYS                  
SEQRES   1 B  323  MET ALA ASP LEU ASP LYS LEU ASN ILE ASP SER ILE ILE          
SEQRES   2 B  323  GLN ARG LEU LEU GLU VAL ARG GLY SER LYS PRO GLY LYS          
SEQRES   3 B  323  ASN VAL GLN LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS          
SEQRES   4 B  323  LEU LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU          
SEQRES   5 B  323  LEU GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE          
SEQRES   6 B  323  HIS GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR          
SEQRES   7 B  323  GLY GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY          
SEQRES   8 B  323  ASP TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE          
SEQRES   9 B  323  CYS LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN          
SEQRES  10 B  323  PHE PHE LEU LEU ARG GLY ASN HIS GLU CSO ALA SER ILE          
SEQRES  11 B  323  ASN ARG ILE TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG          
SEQRES  12 B  323  TYR ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE          
SEQRES  13 B  323  ASN CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE          
SEQRES  14 B  323  PHE CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER          
SEQRES  15 B  323  MET GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL          
SEQRES  16 B  323  PRO ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP          
SEQRES  17 B  323  PRO ASP LYS ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG          
SEQRES  18 B  323  GLY VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS          
SEQRES  19 B  323  PHE LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA          
SEQRES  20 B  323  HIS GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS          
SEQRES  21 B  323  ARG GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CSO          
SEQRES  22 B  323  GLY GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP          
SEQRES  23 B  323  GLU THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA          
SEQRES  24 B  323  GLU LYS LYS LYS PRO ASN ALA THR ARG PRO VAL THR PRO          
SEQRES  25 B  323  PRO ARG GLY MET ILE THR LYS GLN ALA LYS LYS                  
MODRES 4UT3 CSO A  127  CYS  S-HYDROXYCYSTEINE                                  
MODRES 4UT3 CSO B  127  CYS  S-HYDROXYCYSTEINE                                  
MODRES 4UT3 CSO B  273  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  A 127       7                                                       
HET     MN  A 400       1                                                       
HET     MN  A 401       1                                                       
HET    PO4  A 501       5                                                       
HET    CSO  B 127       7                                                       
HET    CSO  B 273       7                                                       
HET     MN  B 400       1                                                       
HET     MN  B 401       1                                                       
HET    PO4  B 501       5                                                       
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     CSO S-HYDROXYCYSTEINE                                                
FORMUL   2   MN    4(MN 2+)                                                     
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   4  CSO    3(C3 H7 N O3 S)                                              
FORMUL   5  HOH   *160(H2 O)                                                    
HELIX    1   1 ASN A    8  GLU A   18  1                                  11    
HELIX    2   2 GLN 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 CSO 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 GLY A  199  SER A  207  1                                   9    
HELIX   10  10 GLY A  228  ASP A  240  1                                  13    
HELIX   11  11 ASN A  271  GLU A  275  5                                   5    
HELIX   12  12 ASN B    8  GLU B   18  1                                  11    
HELIX   13  13 GLN B   31  GLN B   49  1                                  19    
HELIX   14  14 GLN B   68  GLY B   80  1                                  13    
HELIX   15  15 GLN B   99  TYR B  114  1                                  16    
HELIX   16  16 CSO B  127  ARG B  132  1                                   6    
HELIX   17  17 GLY B  135  TYR B  144  1                                  10    
HELIX   18  18 ASN B  145  ASN B  157  1                                  13    
HELIX   19  19 SER B  182  ARG B  188  1                                   7    
HELIX   20  20 GLY B  199  SER B  207  1                                   9    
HELIX   21  21 GLY B  228  ASP B  240  1                                  13    
HELIX   22  22 ASN B  271  GLU B  275  5                                   5    
SHEET    1  AA 6 LEU A  52  LEU A  55  0                                        
SHEET    2  AA 6 ALA A 162  VAL A 165  1  O  ALA A 162   N  LEU A  53           
SHEET    3  AA 6 ILE A 169  CYS A 172 -1  O  ILE A 169   N  VAL A 165           
SHEET    4  AA 6 LEU A 243  ARG A 246  1  O  LEU A 243   N  PHE A 170           
SHEET    5  AA 6 LEU A 263  LEU A 266  1  O  VAL A 264   N  ARG A 246           
SHEET    6  AA 6 TYR A 255  PHE A 258 -1  O  GLU A 256   N  THR A 265           
SHEET    1  AB 5 PHE A 118  LEU A 120  0                                        
SHEET    2  AB 5 TYR A  87  PHE A  89  1  O  TYR A  87   N  PHE A 119           
SHEET    3  AB 5 LEU A  59  CYS A  62  1  O  LYS A  60   N  LEU A  88           
SHEET    4  AB 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5  AB 5 CYS A 291  LEU A 296 -1  O  SER A 292   N  SER A 284           
SHEET    1  AC 3 ASP A 208  PRO A 209  0                                        
SHEET    2  AC 3 PHE A 225  PHE A 227  1  O  PHE A 225   N  ASP A 208           
SHEET    3  AC 3 TRP A 216  GLU A 218 -1  O  GLY A 217   N  THR A 226           
SHEET    1  BA 6 LEU B  52  LEU B  55  0                                        
SHEET    2  BA 6 ALA B 162  VAL B 165  1  O  ALA B 162   N  LEU B  53           
SHEET    3  BA 6 ILE B 169  CYS B 172 -1  O  ILE B 169   N  VAL B 165           
SHEET    4  BA 6 LEU B 243  ARG B 246  1  O  LEU B 243   N  PHE B 170           
SHEET    5  BA 6 LEU B 263  LEU B 266  1  O  VAL B 264   N  ARG B 246           
SHEET    6  BA 6 TYR B 255  PHE B 258 -1  O  GLU B 256   N  THR B 265           
SHEET    1  BB 5 PHE B 118  LEU B 120  0                                        
SHEET    2  BB 5 TYR B  87  PHE B  89  1  O  TYR B  87   N  PHE B 119           
SHEET    3  BB 5 LEU B  59  CYS B  62  1  O  LYS B  60   N  LEU B  88           
SHEET    4  BB 5 GLY B 280  VAL B 285 -1  O  MET B 283   N  ILE B  61           
SHEET    5  BB 5 CYS B 291  LEU B 296 -1  O  SER B 292   N  SER B 284           
SHEET    1  BC 3 ASP B 208  PRO B 209  0                                        
SHEET    2  BC 3 PHE B 225  PHE B 227  1  O  PHE B 225   N  ASP B 208           
SHEET    3  BC 3 TRP B 216  GLU B 218 -1  O  GLY B 217   N  THR B 226           
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        MN    MN A 400                 O3  PO4 A 501     1555   1555  1.99  
LINK        MN    MN A 400                 OD2 ASP A  64     1555   1555  1.96  
LINK        MN    MN A 400                 NE2 HIS A  66     1555   1555  2.22  
LINK        MN    MN A 400                 O   HOH A2022     1555   1555  1.96  
LINK        MN    MN A 400                 O   HOH A2021     1555   1555  2.23  
LINK        MN    MN A 400                 OD2 ASP A  92     1555   1555  2.06  
LINK        MN    MN A 401                 ND1 HIS A 248     1555   1555  2.32  
LINK        MN    MN A 401                 O4  PO4 A 501     1555   1555  2.17  
LINK        MN    MN A 401                 OD2 ASP A  92     1555   1555  2.22  
LINK        MN    MN A 401                 OD1 ASN A 124     1555   1555  1.89  
LINK        MN    MN A 401                 NE2 HIS A 173     1555   1555  2.24  
LINK        MN    MN A 401                 O   HOH A2021     1555   1555  1.79  
LINK         C   GLU B 126                 N   CSO B 127     1555   1555  1.32  
LINK         C   CSO B 127                 N   ALA B 128     1555   1555  1.33  
LINK         C   TYR B 272                 N   CSO B 273     1555   1555  1.34  
LINK         C   CSO B 273                 N   GLY B 274     1555   1555  1.33  
LINK        MN    MN B 400                 O   HOH B2017     1555   1555  2.20  
LINK        MN    MN B 400                 O3  PO4 B 501     1555   1555  2.25  
LINK        MN    MN B 400                 OD2 ASP B  92     1555   1555  2.04  
LINK        MN    MN B 400                 O   HOH B2018     1555   1555  2.11  
LINK        MN    MN B 400                 NE2 HIS B  66     1555   1555  2.25  
LINK        MN    MN B 400                 OD2 ASP B  64     1555   1555  1.99  
LINK        MN    MN B 401                 O   HOH B2017     1555   1555  1.81  
LINK        MN    MN B 401                 O1  PO4 B 501     1555   1555  2.17  
LINK        MN    MN B 401                 ND1 HIS B 248     1555   1555  2.32  
LINK        MN    MN B 401                 OD1 ASN B 124     1555   1555  1.94  
LINK        MN    MN B 401                 OD2 ASP B  92     1555   1555  2.22  
LINK        MN    MN B 401                 NE2 HIS B 173     1555   1555  2.15  
CISPEP   1 ALA A   57    PRO A   58          0         0.21                     
CISPEP   2 PRO A   82    PRO A   83          0         9.40                     
CISPEP   3 ARG A  191    PRO A  192          0        -5.42                     
CISPEP   4 ALA B   57    PRO B   58          0         4.41                     
CISPEP   5 PRO B   82    PRO B   83          0         6.12                     
CISPEP   6 ARG B  191    PRO B  192          0        -8.19                     
SITE     1 AC1  7 ASP A  64  HIS A  66  ASP A  92   MN A 401                    
SITE     2 AC1  7 PO4 A 501  HOH A2021  HOH A2022                               
SITE     1 AC2  7 ASP A  92  ASN A 124  HIS A 173  HIS A 248                    
SITE     2 AC2  7  MN A 400  PO4 A 501  HOH A2021                               
SITE     1 AC3 14 HIS A  66  ASP A  92  ARG A  96  ASN A 124                    
SITE     2 AC3 14 HIS A 125  ARG A 221  HIS A 248   MN A 400                    
SITE     3 AC3 14  MN A 401  HOH A2021  HOH A2022  HOH A2034                    
SITE     4 AC3 14 HOH A2035  HOH A2074                                          
SITE     1 AC4  7 ASP B  64  HIS B  66  ASP B  92   MN B 401                    
SITE     2 AC4  7 PO4 B 501  HOH B2017  HOH B2018                               
SITE     1 AC5  7 ASP B  92  ASN B 124  HIS B 173  HIS B 248                    
SITE     2 AC5  7  MN B 400  PO4 B 501  HOH B2017                               
SITE     1 AC6 13 HIS B  66  ASP B  92  ARG B  96  ASN B 124                    
SITE     2 AC6 13 HIS B 125  ARG B 221  HIS B 248   MN B 400                    
SITE     3 AC6 13  MN B 401  HOH B2017  HOH B2018  HOH B2030                    
SITE     4 AC6 13 HOH B2064                                                     
CRYST1   38.450  105.220   89.820  90.00  90.34  90.00 P 1 21 1      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      0.026008  0.000000  0.000154        0.00000                         
SCALE2      0.000000  0.009504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011134        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system