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Database: PDB
Entry: 5J28
LinkDB: 5J28
Original site: 5J28 
HEADER    HYDROLASE/PROTEIN BINDING               29-MAR-16   5J28              
TITLE     KI67-PP1G (PROTEIN PHOSPHATASE 1, GAMMA ISOFORM) HOLOENZYME COMPLEX   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-GAMMA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 7-308;                                        
COMPND   6 SYNONYM: PP-1G,PROTEIN PHOSPHATASE 1C CATALYTIC SUBUNIT;             
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ANTIGEN KI-67;                                             
COMPND  11 CHAIN: C, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 496-536;                                      
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CC;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: RP1B;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: MKI67;                                                         
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET-M30 MBP                               
KEYWDS    PP1 GAMMA; REPOMAN, KI-67; PHOSPHATASE, HYDROLASE-PROTEIN BINDING     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.S.KUMAR,W.PETI,R.PAGE                                               
REVDAT   3   27-SEP-17 5J28    1       REMARK                                   
REVDAT   2   12-OCT-16 5J28    1       JRNL                                     
REVDAT   1   05-OCT-16 5J28    0                                                
JRNL        AUTH   G.S.KUMAR,E.GOKHAN,S.DE MUNTER,M.BOLLEN,P.VAGNARELLI,W.PETI, 
JRNL        AUTH 2 R.PAGE                                                       
JRNL        TITL   THE KI-67 AND REPOMAN MITOTIC PHOSPHATASES ASSEMBLE VIA AN   
JRNL        TITL 2 IDENTICAL, YET NOVEL MECHANISM.                              
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27572260                                                     
JRNL        DOI    10.7554/ELIFE.16539                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 64920                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.159                           
REMARK   3   R VALUE            (WORKING SET) : 0.154                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 38.6454 -  4.8179    0.97     4534   145  0.1386 0.2018        
REMARK   3     2  4.8179 -  3.8252    0.97     4504   143  0.1209 0.1199        
REMARK   3     3  3.8252 -  3.3420    0.97     4505   138  0.1449 0.1839        
REMARK   3     4  3.3420 -  3.0366    0.97     4490   142  0.1631 0.2185        
REMARK   3     5  3.0366 -  2.8190    0.97     4490   142  0.1568 0.1957        
REMARK   3     6  2.8190 -  2.6528    0.97     4495   145  0.1706 0.2157        
REMARK   3     7  2.6528 -  2.5200    0.97     4481   146  0.1733 0.2256        
REMARK   3     8  2.5200 -  2.4103    0.97     4510   144  0.1725 0.1832        
REMARK   3     9  2.4103 -  2.3175    0.97     4464   143  0.1819 0.2461        
REMARK   3    10  2.3175 -  2.2376    0.97     4479   141  0.1990 0.2412        
REMARK   3    11  2.2376 -  2.1676    0.97     4465   144  0.1987 0.2332        
REMARK   3    12  2.1676 -  2.1057    0.97     4501   142  0.2013 0.2312        
REMARK   3    13  2.1057 -  2.0502    0.97     4500   141  0.2077 0.2533        
REMARK   3    14  2.0502 -  2.0002    0.97     4470   142  0.2159 0.2797        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           5283                                  
REMARK   3   ANGLE     :  0.861           7156                                  
REMARK   3   CHIRALITY :  0.047            770                                  
REMARK   3   PLANARITY :  0.005            946                                  
REMARK   3   DIHEDRAL  : 11.732           3160                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5J28 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219710.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950                            
REMARK 200  MONOCHROMATOR                  : LIQUID NITROGEN-COOLED DOUBLE      
REMARK 200                                   CRYSTAL, NON FIXED EXIT SLIT       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOV 3, 2014                    
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS NOV 3, 2014                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64993                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.331                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 10.40                              
REMARK 200  R MERGE                    (I) : 0.09200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.5000                            
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     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.08610                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: 5INB                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9 M SODIUM MALONATE PH 4.0, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.90567            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      137.81133            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      103.35850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      172.26417            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       34.45283            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     MET A     6                                                      
REMARK 465     GLU A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ASN A   305                                                      
REMARK 465     ALA A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     ARG A   308                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     MET B     6                                                      
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     GLY C   491                                                      
REMARK 465     ALA C   492                                                      
REMARK 465     MET C   493                                                      
REMARK 465     GLY C   494                                                      
REMARK 465     TYR C   495                                                      
REMARK 465     SER C   496                                                      
REMARK 465     GLU C   497                                                      
REMARK 465     GLY C   498                                                      
REMARK 465     ILE C   499                                                      
REMARK 465     PRO C   500                                                      
REMARK 465     LEU C   501                                                      
REMARK 465     LYS C   502                                                      
REMARK 465     ARG C   536                                                      
REMARK 465     GLY D   491                                                      
REMARK 465     ALA D   492                                                      
REMARK 465     MET D   493                                                      
REMARK 465     GLY D   494                                                      
REMARK 465     TYR D   495                                                      
REMARK 465     SER D   496                                                      
REMARK 465     GLU D   497                                                      
REMARK 465     GLY D   498                                                      
REMARK 465     ILE D   499                                                      
REMARK 465     PRO D   500                                                      
REMARK 465     LEU D   501                                                      
REMARK 465     LYS D   502                                                      
REMARK 465     ARG D   536                                                      
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     GLN A  31    CD   OE1  NE2                                       
REMARK 470     LEU A  40    CD1  CD2                                            
REMARK 470     GLU A  56    CD   OE1  OE2                                       
REMARK 470     LYS A  98    CD   CE   NZ                                        
REMARK 470     LYS A 147    CD   CE   NZ                                        
REMARK 470     LYS A 211    CD   CE   NZ                                        
REMARK 470     LYS A 260    CE   NZ                                             
REMARK 470     LYS B  23    CD   CE   NZ                                        
REMARK 470     GLN B  29    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  31    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  41    CD   CE   NZ                                        
REMARK 470     GLU B  56    CD   OE1  OE2                                       
REMARK 470     LYS B  98    CD   CE   NZ                                        
REMARK 470     ILE B 133    CD1                                                 
REMARK 470     LYS B 147    CD   CE   NZ                                        
REMARK 470     GLU B 184    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 211    CD   CE   NZ                                        
REMARK 470     LYS B 260    CE   NZ                                             
REMARK 470     ARG C 503    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 504    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET C 525    CG   SD   CE                                        
REMARK 470     LYS C 528    CG   CD   CE   NZ                                   
REMARK 470     THR C 534    OG1  CG2                                            
REMARK 470     LYS C 535    CG   CD   CE   NZ                                   
REMARK 470     ARG D 503    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 504    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 505    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS D 511    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU D 516    CG   CD1  CD2                                       
REMARK 470     ASP D 518    CG   OD1  OD2                                       
REMARK 470     ASN D 520    CG   OD1  ND2                                       
REMARK 470     LEU D 521    CG   CD1  CD2                                       
REMARK 470     LYS D 528    CG   CD   CE   NZ                                   
REMARK 470     ARG D 529    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 535    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   506     O    HOH A   510              1.99            
REMARK 500   O    HOH A   556     O    HOH A   590              2.01            
REMARK 500   O    HOH A   508     O    HOH C   612              2.11            
REMARK 500   O    HOH A   581     O    HOH A   584              2.14            
REMARK 500   O    HOH A   532     O    HOH A   595              2.15            
REMARK 500   O    HOH B   585     O    HOH B   591              2.18            
REMARK 500   O    HOH A   536     O    HOH A   578              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   576     O    HOH B   579     5554     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 273   CB    CYS A 273   SG     -0.107                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  92       70.09     60.65                                   
REMARK 500    ASP A  95      147.91     78.56                                   
REMARK 500    ARG A  96      -48.17     82.36                                   
REMARK 500    TYR A 144     -104.87   -134.22                                   
REMARK 500    SER A 224     -149.95     68.62                                   
REMARK 500    ALA A 247     -124.65   -128.33                                   
REMARK 500    HIS A 248      -12.19     78.39                                   
REMARK 500    CYS A 273       16.06     56.22                                   
REMARK 500    ASP A 277       70.00   -111.50                                   
REMARK 500    ASP B  95      150.23     71.84                                   
REMARK 500    ARG B  96      -47.59     76.52                                   
REMARK 500    TYR B 144     -104.45   -132.19                                   
REMARK 500    ARG B 221       -9.99    -59.42                                   
REMARK 500    SER B 224     -146.98     62.18                                   
REMARK 500    ALA B 247     -125.72   -126.24                                   
REMARK 500    HIS B 248      -14.16     80.02                                   
REMARK 500    ASN B 271       59.53     39.82                                   
REMARK 500    ASP B 277       52.30    -99.97                                   
REMARK 500    ARG C 504       80.40     50.88                                   
REMARK 500    MET C 525       78.14   -118.09                                   
REMARK 500    ASN D 524       32.59    -83.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  54   OE2                                                    
REMARK 620 2 GLU A 167   OE1  94.7                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI B 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5INB   RELATED DB: PDB                                   
REMARK 900 PP1 GAMMA IN COMPLEX WITH REPOMAN                                    
REMARK 900 RELATED ID: 5IOH   RELATED DB: PDB                                   
REMARK 900 PP1 ALPHA IN COMPLEX WITH REPOMAN                                    
REMARK 900 RELATED ID: 25981   RELATED DB: BMRB                                 
REMARK 900 ASSIGNMENTS OF REPOMAN PP1 BINDING DOMAIN                            
DBREF  5J28 A    7   308  UNP    P36873   PP1G_HUMAN       7    308             
DBREF  5J28 B    7   308  UNP    P36873   PP1G_HUMAN       7    308             
DBREF  5J28 C  496   536  UNP    P46013   KI67_HUMAN     496    536             
DBREF  5J28 D  496   536  UNP    P46013   KI67_HUMAN     496    536             
SEQADV 5J28 GLY A    4  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 HIS A    5  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 MET A    6  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 GLY B    4  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 HIS B    5  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 MET B    6  UNP  P36873              EXPRESSION TAG                 
SEQADV 5J28 GLY C  491  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 ALA C  492  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 MET C  493  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 GLY C  494  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 TYR C  495  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 MET C  525  UNP  P46013    THR   525 ENGINEERED MUTATION            
SEQADV 5J28 GLY D  491  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 ALA D  492  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 MET D  493  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 GLY D  494  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 TYR D  495  UNP  P46013              EXPRESSION TAG                 
SEQADV 5J28 MET D  525  UNP  P46013    THR   525 ENGINEERED MUTATION            
SEQRES   1 A  305  GLY HIS MET LEU ASN ILE ASP SER ILE ILE GLN ARG LEU          
SEQRES   2 A  305  LEU GLU VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN          
SEQRES   3 A  305  LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER          
SEQRES   4 A  305  ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU          
SEQRES   5 A  305  GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN          
SEQRES   6 A  305  TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE          
SEQRES   7 A  305  PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL          
SEQRES   8 A  305  ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU          
SEQRES   9 A  305  LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU          
SEQRES  10 A  305  LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE          
SEQRES  11 A  305  TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE          
SEQRES  12 A  305  LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU          
SEQRES  13 A  305  PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS          
SEQRES  14 A  305  HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN          
SEQRES  15 A  305  ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN          
SEQRES  16 A  305  GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS          
SEQRES  17 A  305  ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER          
SEQRES  18 A  305  PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS          
SEQRES  19 A  305  LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL          
SEQRES  20 A  305  VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU          
SEQRES  21 A  305  VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY GLU PHE          
SEQRES  22 A  305  ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU THR LEU          
SEQRES  23 A  305  MET CYS SER PHE GLN ILE LEU LYS PRO ALA GLU LYS LYS          
SEQRES  24 A  305  LYS PRO ASN ALA THR ARG                                      
SEQRES   1 B  305  GLY HIS MET LEU ASN ILE ASP SER ILE ILE GLN ARG LEU          
SEQRES   2 B  305  LEU GLU VAL ARG GLY SER LYS PRO GLY LYS ASN VAL GLN          
SEQRES   3 B  305  LEU GLN GLU ASN GLU ILE ARG GLY LEU CYS LEU LYS SER          
SEQRES   4 B  305  ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU GLU LEU          
SEQRES   5 B  305  GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS GLY GLN          
SEQRES   6 B  305  TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY GLY PHE          
SEQRES   7 B  305  PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP TYR VAL          
SEQRES   8 B  305  ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS LEU LEU          
SEQRES   9 B  305  LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE PHE LEU          
SEQRES  10 B  305  LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN ARG ILE          
SEQRES  11 B  305  TYR GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR ASN ILE          
SEQRES  12 B  305  LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN CYS LEU          
SEQRES  13 B  305  PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE CYS CYS          
SEQRES  14 B  305  HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET GLU GLN          
SEQRES  15 B  305  ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO ASP GLN          
SEQRES  16 B  305  GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO ASP LYS          
SEQRES  17 B  305  ASP VAL LEU GLY TRP GLY GLU ASN ASP ARG GLY VAL SER          
SEQRES  18 B  305  PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE LEU HIS          
SEQRES  19 B  305  LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS GLN VAL          
SEQRES  20 B  305  VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG GLN LEU          
SEQRES  21 B  305  VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY GLU PHE          
SEQRES  22 B  305  ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU THR LEU          
SEQRES  23 B  305  MET CYS SER PHE GLN ILE LEU LYS PRO ALA GLU LYS LYS          
SEQRES  24 B  305  LYS PRO ASN ALA THR ARG                                      
SEQRES   1 C   46  GLY ALA MET GLY TYR SER GLU GLY ILE PRO LEU LYS ARG          
SEQRES   2 C   46  ARG ARG VAL SER PHE GLY GLY HIS LEU ARG PRO GLU LEU          
SEQRES   3 C   46  PHE ASP GLU ASN LEU PRO PRO ASN MET PRO LEU LYS ARG          
SEQRES   4 C   46  GLY GLU ALA PRO THR LYS ARG                                  
SEQRES   1 D   46  GLY ALA MET GLY TYR SER GLU GLY ILE PRO LEU LYS ARG          
SEQRES   2 D   46  ARG ARG VAL SER PHE GLY GLY HIS LEU ARG PRO GLU LEU          
SEQRES   3 D   46  PHE ASP GLU ASN LEU PRO PRO ASN MET PRO LEU LYS ARG          
SEQRES   4 D   46  GLY GLU ALA PRO THR LYS ARG                                  
HET    MLI  A 401       7                                                       
HET     NA  A 402       1                                                       
HET    MLI  B 401       7                                                       
HETNAM     MLI MALONATE ION                                                     
HETNAM      NA SODIUM ION                                                       
FORMUL   5  MLI    2(C3 H2 O4 2-)                                               
FORMUL   6   NA    NA 1+                                                        
FORMUL   8  HOH   *232(H2 O)                                                    
HELIX    1 AA1 ASN A    8  LEU A   17  1                                  10    
HELIX    2 AA2 GLU A   18  SER A   22  5                                   5    
HELIX    3 AA3 GLN A   31  GLN A   49  1                                  19    
HELIX    4 AA4 GLN A   68  GLY A   80  1                                  13    
HELIX    5 AA5 GLN A   99  TYR A  114  1                                  16    
HELIX    6 AA6 CYS A  127  ARG A  132  1                                   6    
HELIX    7 AA7 GLY A  135  TYR A  144  1                                  10    
HELIX    8 AA8 ASN A  145  ASN A  157  1                                  13    
HELIX    9 AA9 MET A  183  ARG A  188  1                                   6    
HELIX   10 AB1 GLY A  199  SER A  207  1                                   9    
HELIX   11 AB2 GLY A  228  ASP A  240  1                                  13    
HELIX   12 AB3 ASN A  271  GLU A  275  5                                   5    
HELIX   13 AB4 ASN B    8  LEU B   17  1                                  10    
HELIX   14 AB5 GLU B   18  SER B   22  5                                   5    
HELIX   15 AB6 GLN B   31  GLN B   49  1                                  19    
HELIX   16 AB7 GLN B   68  GLY B   80  1                                  13    
HELIX   17 AB8 GLN B   99  TYR B  114  1                                  16    
HELIX   18 AB9 CYS B  127  ARG B  132  1                                   6    
HELIX   19 AC1 GLY B  135  TYR B  144  1                                  10    
HELIX   20 AC2 ASN B  145  ASN B  157  1                                  13    
HELIX   21 AC3 MET B  183  ARG B  188  1                                   6    
HELIX   22 AC4 GLY B  199  SER B  207  1                                   9    
HELIX   23 AC5 GLY B  228  ASP B  240  1                                  13    
HELIX   24 AC6 ASN B  271  GLU B  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 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4 AA1 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5 AA1 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6 AA1 6 TYR A 255  PHE A 258 -1  N  GLU A 256   O  THR A 265           
SHEET    1 AA2 6 PHE A 118  LEU A 120  0                                        
SHEET    2 AA2 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA2 6 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4 AA2 6 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5 AA2 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6 AA2 6 SER C 507  PHE C 508  1  O  SER C 507   N  CYS A 291           
SHEET    1 AA3 6 PHE A 118  LEU A 120  0                                        
SHEET    2 AA3 6 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA3 6 LEU A  59  CYS A  62  1  N  CYS A  62   O  LEU A  88           
SHEET    4 AA3 6 GLY A 280  VAL A 285 -1  O  VAL A 285   N  LEU A  59           
SHEET    5 AA3 6 MET A 290  PRO A 298 -1  O  LEU A 296   N  GLY A 280           
SHEET    6 AA3 6 GLU C 515  PHE C 517  1  O  GLU C 515   N  ILE A 295           
SHEET    1 AA4 3 ASP A 208  PRO A 209  0                                        
SHEET    2 AA4 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3 AA4 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1 AA5 6 LEU B  52  LEU B  55  0                                        
SHEET    2 AA5 6 ALA B 162  VAL B 165  1  O  ILE B 164   N  LEU B  55           
SHEET    3 AA5 6 ILE B 169  CYS B 172 -1  O  CYS B 171   N  ALA B 163           
SHEET    4 AA5 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5 AA5 6 LEU B 263  LEU B 266  1  O  LEU B 266   N  ARG B 246           
SHEET    6 AA5 6 TYR B 255  PHE B 258 -1  N  PHE B 258   O  LEU B 263           
SHEET    1 AA6 6 PHE B 118  LEU B 120  0                                        
SHEET    2 AA6 6 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3 AA6 6 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4 AA6 6 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5 AA6 6 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6 AA6 6 SER D 507  PHE D 508  1  O  SER D 507   N  CYS B 291           
SHEET    1 AA7 6 PHE B 118  LEU B 120  0                                        
SHEET    2 AA7 6 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3 AA7 6 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4 AA7 6 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5 AA7 6 MET B 290  PRO B 298 -1  O  LEU B 296   N  GLY B 280           
SHEET    6 AA7 6 GLU D 515  PHE D 517  1  O  GLU D 515   N  ILE B 295           
SHEET    1 AA8 3 ASP B 208  PRO B 209  0                                        
SHEET    2 AA8 3 PHE B 225  PHE B 227  1  O  PHE B 225   N  ASP B 208           
SHEET    3 AA8 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         OE2 GLU A  54                NA    NA A 402     1555   1555  2.98  
LINK         OE1 GLU A 167                NA    NA A 402     1555   1555  2.74  
CISPEP   1 ALA A   57    PRO A   58          0         1.58                     
CISPEP   2 PRO A   82    PRO A   83          0        -1.06                     
CISPEP   3 ARG A  191    PRO A  192          0        -2.04                     
CISPEP   4 ALA B   57    PRO B   58          0         0.84                     
CISPEP   5 PRO B   82    PRO B   83          0         5.51                     
CISPEP   6 ARG B  191    PRO B  192          0        -1.03                     
SITE     1 AC1 11 ASP A  64  HIS A  66  ASP A  92  ARG A 221                    
SITE     2 AC1 11 HIS A 248  TYR A 272  HOH A 514  HOH A 526                    
SITE     3 AC1 11 HOH A 528  GLU B 218  ASP B 220                               
SITE     1 AC2  3 GLU A  54  ILE A 164  GLU A 167                               
SITE     1 AC3 10 GLU A 218  ASP A 220  ASP B  64  HIS B  66                    
SITE     2 AC3 10 ASP B  92  ARG B 221  HIS B 248  TYR B 272                    
SITE     3 AC3 10 HOH B 527  HOH B 528                                          
CRYST1   90.832   90.832  206.717  90.00  90.00 120.00 P 61         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011009  0.006356  0.000000        0.00000                         
SCALE2      0.000000  0.012712  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004838        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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