GenomeNet

Database: PDB
Entry: 6OBU
LinkDB: 6OBU
Original site: 6OBU 
HEADER    HYDROLASE/TOXIN                         21-MAR-19   6OBU              
TITLE     PP1 Y134K IN COMPLEX WITH MICROCYSTIN LR                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN PHOSPHATASE PP1-ALPHA CATALYTIC   
COMPND   3 SUBUNIT;                                                             
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: UNP RESIDUES 7-300;                                        
COMPND   6 SYNONYM: PP-1A, PROTEIN PHOSPHATASE 1;                               
COMPND   7 EC: 3.1.3.16;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: MICROCYSTIN LR;                                            
COMPND  12 CHAIN: C, D                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPP1CA, PPP1A;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: MICROCYSTIS AERUGINOSA;                         
SOURCE  10 ORGANISM_TAXID: 1126                                                 
KEYWDS    PHOSPHATASE, HYDROLASE-TOXIN COMPLEX                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.CHOY,T.M.MOON,J.A.BRAY,T.L.ARCHULETA,W.SHI,W.PETI,R.PAGE          
REVDAT   4   23-OCT-19 6OBU    1       JRNL                                     
REVDAT   3   02-OCT-19 6OBU    1       JRNL                                     
REVDAT   2   25-SEP-19 6OBU    1       JRNL                                     
REVDAT   1   18-SEP-19 6OBU    0                                                
JRNL        AUTH   M.S.CHOY,T.M.MOON,R.RAVINDRAN,J.A.BRAY,L.C.ROBINSON,         
JRNL        AUTH 2 T.L.ARCHULETA,W.SHI,W.PETI,K.TATCHELL,R.PAGE                 
JRNL        TITL   SDS22 SELECTIVELY RECOGNIZES AND TRAPS METAL-DEFICIENT       
JRNL        TITL 2 INACTIVE PP1.                                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 116 20472 2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   31548429                                                     
JRNL        DOI    10.1073/PNAS.1908718116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 49556                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.230                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2589                            
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 40.1804 -  6.0504    1.00     3054   160  0.1708 0.1912        
REMARK   3     2  6.0504 -  4.8049    1.00     3071   168  0.1676 0.2150        
REMARK   3     3  4.8049 -  4.1983    1.00     3081   180  0.1326 0.1625        
REMARK   3     4  4.1983 -  3.8147    1.00     3026   174  0.1379 0.1605        
REMARK   3     5  3.8147 -  3.5415    1.00     3028   184  0.1400 0.1649        
REMARK   3     6  3.5415 -  3.3328    1.00     3103   158  0.1398 0.1893        
REMARK   3     7  3.3328 -  3.1660    1.00     3104   116  0.1446 0.1793        
REMARK   3     8  3.1660 -  3.0282    1.00     3077   168  0.1538 0.1930        
REMARK   3     9  3.0282 -  2.9117    1.00     3049   159  0.1483 0.2007        
REMARK   3    10  2.9117 -  2.8112    1.00     3023   191  0.1605 0.2028        
REMARK   3    11  2.8112 -  2.7233    1.00     3106   172  0.1509 0.2118        
REMARK   3    12  2.7233 -  2.6455    1.00     3046   184  0.1634 0.2187        
REMARK   3    13  2.6455 -  2.5759    1.00     3036   164  0.1646 0.1863        
REMARK   3    14  2.5759 -  2.5130    1.00     3052   169  0.1655 0.2238        
REMARK   3    15  2.5130 -  2.4559    1.00     3097   159  0.1723 0.2139        
REMARK   3    16  2.4559 -  2.4037    0.99     3036   178  0.1800 0.2296        
REMARK   3    17  2.4037 -  2.3556    1.00     3039   180  0.1645 0.1944        
REMARK   3    18  2.3556 -  2.3111    1.00     3060   148  0.1749 0.2409        
REMARK   3    19  2.3111 -  2.2699    1.00     3060   184  0.1858 0.2220        
REMARK   3    20  2.2699 -  2.2314    1.00     3062   179  0.1833 0.2074        
REMARK   3    21  2.2314 -  2.1954    1.00     3087   154  0.1836 0.2189        
REMARK   3    22  2.1954 -  2.1616    1.00     3011   177  0.1900 0.2341        
REMARK   3    23  2.1616 -  2.1298    1.00     3078   160  0.1947 0.2517        
REMARK   3    24  2.1298 -  2.0998    0.98     3026   157  0.2154 0.2602        
REMARK   3    25  2.0998 -  2.0715    0.95     2927   192  0.2323 0.2718        
REMARK   3    26  2.0715 -  2.0446    0.92     2790   148  0.2435 0.2341        
REMARK   3    27  2.0446 -  2.0190    0.88     2731   142  0.2455 0.3157        
REMARK   3    28  2.0190 -  1.9947    0.85     2606   127  0.2545 0.3002        
REMARK   3    29  1.9947 -  1.9715    0.81     2487   146  0.2672 0.2817        
REMARK   3    30  1.9715 -  1.9493    0.75     2281   143  0.2901 0.3157        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.730           
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      :  0.009           5062                                  
REMARK   3   ANGLE     :  0.900           6842                                  
REMARK   3   CHIRALITY :  0.050            742                                  
REMARK   3   PLANARITY :  0.007            891                                  
REMARK   3   DIHEDRAL  : 18.085           2979                                  
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 6OBU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240409.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49637                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.11700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4MOV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG6000, 1 M LITHIUM CHLORIDE, 0.1   
REMARK 280  M MES, PH 6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       32.67400            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.01900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.18100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.01900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.67400            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.18100            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 2050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE MICROCYSTIN LR IS OLIGOPEPTIDE, A MEMBER OF TOXIN CLASS.         
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MICROCYSTIN LR                                               
REMARK 400   CHAIN: C, D                                                        
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
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     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASP A   300                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ASP B   300                                                      
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     ARG A  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  44    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  98    CD   CE   NZ                                        
REMARK 470     LYS A 211    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 218    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     LYS A 260    CD   CE   NZ                                        
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  98    CD   CE   NZ                                        
REMARK 470     LYS B 211    CG   CD   CE   NZ                                   
REMARK 470     GLU B 218    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 220    CG   OD1  OD2                                       
REMARK 470     GLU B 230    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 260    CD   CE   NZ                                        
REMARK 470     ASN B 271    CG   OD1  ND2                                       
REMARK 470     GLU B 275    CG   CD   OE1  OE2                                  
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   OXT  FGA C     6     O    HOH C   401              2.01            
REMARK 500   O    LEU A     7     O    HOH A   501              2.04            
REMARK 500   O    HOH B   505     O    HOH B   521              2.07            
REMARK 500   O    HOH B   599     O    HOH B   654              2.11            
REMARK 500   OE2  GLU B    32     O    HOH B   501              2.12            
REMARK 500   O    HOH B   511     O    HOH B   598              2.16            
REMARK 500   NH2  ARG B   261     O    HOH B   502              2.17            
REMARK 500   O    HOH A   566     O    HOH A   604              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 B   607     O    HOH B   649     3445     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      154.99     80.65                                   
REMARK 500    ARG A  96      -57.20     71.90                                   
REMARK 500    TYR A 144     -112.83   -134.23                                   
REMARK 500    GLU A 167       17.09     57.93                                   
REMARK 500    SER A 224     -152.07     64.59                                   
REMARK 500    ALA A 247     -128.55   -132.94                                   
REMARK 500    HIS A 248      -29.55     80.31                                   
REMARK 500    ASP B  95      154.91     82.40                                   
REMARK 500    ARG B  96      -56.46     71.60                                   
REMARK 500    TYR B 144     -112.98   -132.97                                   
REMARK 500    GLU B 167       17.39     58.13                                   
REMARK 500    SER B 224     -152.41     63.30                                   
REMARK 500    ALA B 247     -128.62   -132.42                                   
REMARK 500    HIS B 248      -27.27     80.60                                   
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 401  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  64   OD2                                                    
REMARK 620 2 HIS A  66   NE2 105.7                                              
REMARK 620 3 ASP A  92   OD2  94.3  96.4                                        
REMARK 620 4 HOH C 403   O   100.7  85.6 163.8                                  
REMARK 620 5 HOH A 527   O    99.3 154.2  75.2  96.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  92   OD2                                                    
REMARK 620 2 ASN A 124   OD1  96.6                                              
REMARK 620 3 HIS A 173   NE2  89.1  91.5                                        
REMARK 620 4 HIS A 248   ND1 162.5 100.8  89.7                                  
REMARK 620 5 HOH A 527   O    76.3 136.2 130.8  91.4                            
REMARK 620 N                    1     2     3     4                             
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 ASP B  64   OD2                                                    
REMARK 620 2 HIS B  66   NE2 106.6                                              
REMARK 620 3 ASP B  92   OD2  95.0  96.4                                        
REMARK 620 4 HOH B 533   O    98.5 154.5  76.7                                  
REMARK 620 5 HOH D 101   O    96.8  85.0 167.1  96.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B 402  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  92   OD2                                                    
REMARK 620 2 ASN B 124   OD1  95.8                                              
REMARK 620 3 HIS B 173   NE2  89.8  90.8                                        
REMARK 620 4 HIS B 248   ND1 165.2  98.8  87.8                                  
REMARK 620 5 HOH B 533   O    79.0 136.4 132.0  91.9                            
REMARK 620 N                    1     2     3     4                             
DBREF  6OBU A    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  6OBU B    7   300  UNP    P62136   PP1A_HUMAN       7    300             
DBREF  6OBU C    1     7  NOR    6OBU     6OBU             1      7             
DBREF  6OBU D    1     7  NOR    6OBU     6OBU             1      7             
SEQADV 6OBU GLY A    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU HIS A    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU MET A    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU GLY A    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU SER A    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU LYS A  134  UNP  P62136    TYR   134 ENGINEERED MUTATION            
SEQADV 6OBU GLY B    2  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU HIS B    3  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU MET B    4  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU GLY B    5  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU SER B    6  UNP  P62136              EXPRESSION TAG                 
SEQADV 6OBU LYS B  134  UNP  P62136    TYR   134 ENGINEERED MUTATION            
SEQRES   1 A  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 A  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 A  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 A  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 A  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 A  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 A  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 A  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 A  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 A  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 A  299  ARG ILE LYS GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 A  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 A  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 A  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 A  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 A  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 A  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 A  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 A  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 A  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 A  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 A  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 A  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 B  299  GLY HIS MET GLY SER LEU ASN LEU ASP SER ILE ILE GLY          
SEQRES   2 B  299  ARG LEU LEU GLU VAL GLN GLY SER ARG PRO GLY LYS ASN          
SEQRES   3 B  299  VAL GLN LEU THR GLU ASN GLU ILE ARG GLY LEU CYS LEU          
SEQRES   4 B  299  LYS SER ARG GLU ILE PHE LEU SER GLN PRO ILE LEU LEU          
SEQRES   5 B  299  GLU LEU GLU ALA PRO LEU LYS ILE CYS GLY ASP ILE HIS          
SEQRES   6 B  299  GLY GLN TYR TYR ASP LEU LEU ARG LEU PHE GLU TYR GLY          
SEQRES   7 B  299  GLY PHE PRO PRO GLU SER ASN TYR LEU PHE LEU GLY ASP          
SEQRES   8 B  299  TYR VAL ASP ARG GLY LYS GLN SER LEU GLU THR ILE CYS          
SEQRES   9 B  299  LEU LEU LEU ALA TYR LYS ILE LYS TYR PRO GLU ASN PHE          
SEQRES  10 B  299  PHE LEU LEU ARG GLY ASN HIS GLU CYS ALA SER ILE ASN          
SEQRES  11 B  299  ARG ILE LYS GLY PHE TYR ASP GLU CYS LYS ARG ARG TYR          
SEQRES  12 B  299  ASN ILE LYS LEU TRP LYS THR PHE THR ASP CYS PHE ASN          
SEQRES  13 B  299  CYS LEU PRO ILE ALA ALA ILE VAL ASP GLU LYS ILE PHE          
SEQRES  14 B  299  CYS CYS HIS GLY GLY LEU SER PRO ASP LEU GLN SER MET          
SEQRES  15 B  299  GLU GLN ILE ARG ARG ILE MET ARG PRO THR ASP VAL PRO          
SEQRES  16 B  299  ASP GLN GLY LEU LEU CYS ASP LEU LEU TRP SER ASP PRO          
SEQRES  17 B  299  ASP LYS ASP VAL GLN GLY TRP GLY GLU ASN ASP ARG GLY          
SEQRES  18 B  299  VAL SER PHE THR PHE GLY ALA GLU VAL VAL ALA LYS PHE          
SEQRES  19 B  299  LEU HIS LYS HIS ASP LEU ASP LEU ILE CYS ARG ALA HIS          
SEQRES  20 B  299  GLN VAL VAL GLU ASP GLY TYR GLU PHE PHE ALA LYS ARG          
SEQRES  21 B  299  GLN LEU VAL THR LEU PHE SER ALA PRO ASN TYR CYS GLY          
SEQRES  22 B  299  GLU PHE ASP ASN ALA GLY ALA MET MET SER VAL ASP GLU          
SEQRES  23 B  299  THR LEU MET CYS SER PHE GLN ILE LEU LYS PRO ALA ASP          
SEQRES   1 C    7  DAL LEU ACB ARG 1ZN FGA DAM                                  
SEQRES   1 D    7  DAL LEU ACB ARG 1ZN FGA DAM                                  
HET    DAL  C   1       5                                                       
HET    ACB  C   3       9                                                       
HET    1ZN  C   5      23                                                       
HET    FGA  C   6       9                                                       
HET    DAM  C   7       6                                                       
HET    DAL  D   1       5                                                       
HET    ACB  D   3       9                                                       
HET    1ZN  D   5      23                                                       
HET    FGA  D   6       9                                                       
HET    DAM  D   7       6                                                       
HET     MN  A 401       1                                                       
HET     MN  A 402       1                                                       
HET    GOL  A 403       6                                                       
HET    GOL  A 404       6                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    GOL  A 407       6                                                       
HET    DMS  A 408       4                                                       
HET     MN  B 401       1                                                       
HET     MN  B 402       1                                                       
HET    GOL  B 403       6                                                       
HET    GOL  B 404       6                                                       
HET     CL  B 405       1                                                       
HETNAM     DAL D-ALANINE                                                        
HETNAM     ACB 3-METHYL-BETA-D-ASPARTIC ACID                                    
HETNAM     1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-           
HETNAM   2 1ZN  10-PHENYLDECA-4,6-DIENOIC ACID                                  
HETNAM     FGA GAMMA-D-GLUTAMIC ACID                                            
HETNAM     DAM N-METHYL-ALPHA-BETA-DEHYDROALANINE                               
HETNAM      MN MANGANESE (II) ION                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM      CL CHLORIDE ION                                                     
HETSYN     ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID            
HETSYN     FGA D-GLUTAMIC ACID                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  DAL    2(C3 H7 N O2)                                                
FORMUL   3  ACB    2(C5 H9 N O4)                                                
FORMUL   3  1ZN    2(C20 H29 N O3)                                              
FORMUL   3  FGA    2(C5 H9 N O4)                                                
FORMUL   3  DAM    2(C4 H7 N O2)                                                
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   7  GOL    7(C3 H8 O3)                                                  
FORMUL  12  DMS    C2 H6 O S                                                    
FORMUL  17   CL    CL 1-                                                        
FORMUL  18  HOH   *342(H2 O)                                                    
HELIX    1 AA1 ASN A    8  GLU A   18  1                                  11    
HELIX    2 AA2 THR A   31  GLN A   49  1                                  19    
HELIX    3 AA3 GLN A   68  GLY A   80  1                                  13    
HELIX    4 AA4 GLN A   99  TYR A  114  1                                  16    
HELIX    5 AA5 CYS A  127  ARG A  132  1                                   6    
HELIX    6 AA6 GLY A  135  TYR A  144  1                                  10    
HELIX    7 AA7 ASN A  145  ASN A  157  1                                  13    
HELIX    8 AA8 SER A  182  ARG A  188  1                                   7    
HELIX    9 AA9 GLY A  199  SER A  207  1                                   9    
HELIX   10 AB1 GLY A  228  ASP A  240  1                                  13    
HELIX   11 AB2 ASN B    8  GLU B   18  1                                  11    
HELIX   12 AB3 THR B   31  GLN B   49  1                                  19    
HELIX   13 AB4 GLN B   68  GLY B   80  1                                  13    
HELIX   14 AB5 GLN B   99  TYR B  114  1                                  16    
HELIX   15 AB6 CYS B  127  ARG B  132  1                                   6    
HELIX   16 AB7 GLY B  135  TYR B  144  1                                  10    
HELIX   17 AB8 ASN B  145  ASN B  157  1                                  13    
HELIX   18 AB9 SER B  182  ARG B  188  1                                   7    
HELIX   19 AC1 GLY B  199  SER B  207  1                                   9    
HELIX   20 AC2 GLY B  228  ASP B  240  1                                  13    
SHEET    1 AA1 6 LEU A  52  LEU A  55  0                                        
SHEET    2 AA1 6 ALA A 162  VAL A 165  1  O  ALA A 162   N  LEU A  53           
SHEET    3 AA1 6 ILE A 169  CYS A 172 -1  O  CYS A 171   N  ALA A 163           
SHEET    4 AA1 6 LEU A 243  ARG A 246  1  O  CYS A 245   N  PHE A 170           
SHEET    5 AA1 6 LEU A 263  LEU A 266  1  O  LEU A 266   N  ARG A 246           
SHEET    6 AA1 6 TYR A 255  PHE A 258 -1  N  PHE A 258   O  LEU A 263           
SHEET    1 AA2 5 PHE A 118  LEU A 120  0                                        
SHEET    2 AA2 5 TYR A  87  PHE A  89  1  N  PHE A  89   O  PHE A 119           
SHEET    3 AA2 5 LEU A  59  CYS A  62  1  N  LYS A  60   O  LEU A  88           
SHEET    4 AA2 5 GLY A 280  VAL A 285 -1  O  MET A 283   N  ILE A  61           
SHEET    5 AA2 5 CYS A 291  LEU A 296 -1  O  LEU A 296   N  GLY A 280           
SHEET    1 AA3 3 ASP A 208  PRO A 209  0                                        
SHEET    2 AA3 3 PHE A 225  PHE A 227  1  O  PHE A 227   N  ASP A 208           
SHEET    3 AA3 3 TRP A 216  GLU A 218 -1  N  GLY A 217   O  THR A 226           
SHEET    1 AA4 6 LEU B  52  LEU B  55  0                                        
SHEET    2 AA4 6 ALA B 162  VAL B 165  1  O  ALA B 162   N  LEU B  53           
SHEET    3 AA4 6 ILE B 169  CYS B 172 -1  O  CYS B 171   N  ALA B 163           
SHEET    4 AA4 6 LEU B 243  ARG B 246  1  O  CYS B 245   N  PHE B 170           
SHEET    5 AA4 6 LEU B 263  LEU B 266  1  O  VAL B 264   N  ARG B 246           
SHEET    6 AA4 6 TYR B 255  PHE B 258 -1  N  GLU B 256   O  THR B 265           
SHEET    1 AA5 5 PHE B 118  LEU B 120  0                                        
SHEET    2 AA5 5 TYR B  87  PHE B  89  1  N  PHE B  89   O  PHE B 119           
SHEET    3 AA5 5 LEU B  59  CYS B  62  1  N  LYS B  60   O  LEU B  88           
SHEET    4 AA5 5 GLY B 280  VAL B 285 -1  O  VAL B 285   N  LEU B  59           
SHEET    5 AA5 5 CYS B 291  LEU B 296 -1  O  LEU B 296   N  GLY B 280           
SHEET    1 AA6 3 ASP B 208  PRO B 209  0                                        
SHEET    2 AA6 3 PHE B 225  PHE B 227  1  O  PHE B 225   N  ASP B 208           
SHEET    3 AA6 3 TRP B 216  GLU B 218 -1  N  GLY B 217   O  THR B 226           
LINK         OD2 ASP A  64                MN    MN A 401     1555   1555  2.08  
LINK         NE2 HIS A  66                MN    MN A 401     1555   1555  2.21  
LINK         OD2 ASP A  92                MN    MN A 401     1555   1555  2.19  
LINK         OD2 ASP A  92                MN    MN A 402     1555   1555  2.23  
LINK         OD1 ASN A 124                MN    MN A 402     1555   1555  2.11  
LINK         NE2 HIS A 173                MN    MN A 402     1555   1555  2.14  
LINK         ND1 HIS A 248                MN    MN A 402     1555   1555  2.31  
LINK         SG  CYS A 273                 CB  DAM C   7     1555   1555  1.77  
LINK         OD2 ASP B  64                MN    MN B 401     1555   1555  2.13  
LINK         NE2 HIS B  66                MN    MN B 401     1555   1555  2.24  
LINK         OD2 ASP B  92                MN    MN B 401     1555   1555  2.18  
LINK         OD2 ASP B  92                MN    MN B 402     1555   1555  2.24  
LINK         OD1 ASN B 124                MN    MN B 402     1555   1555  2.14  
LINK         NE2 HIS B 173                MN    MN B 402     1555   1555  2.13  
LINK         ND1 HIS B 248                MN    MN B 402     1555   1555  2.26  
LINK         SG  CYS B 273                 CB  DAM D   7     1555   1555  1.75  
LINK         N   DAL C   1                 C   DAM C   7     1555   1555  1.40  
LINK         C   DAL C   1                 N   LEU C   2     1555   1555  1.37  
LINK         C   LEU C   2                 N   ACB C   3     1555   1555  1.36  
LINK         CG  ACB C   3                 N   ARG C   4     1555   1555  1.41  
LINK         C   ARG C   4                 N1  1ZN C   5     1555   1555  1.41  
LINK         C20 1ZN C   5                 N   FGA C   6     1555   1555  1.37  
LINK         CD  FGA C   6                 N   DAM C   7     1555   1555  1.43  
LINK         N   DAL D   1                 C   DAM D   7     1555   1555  1.41  
LINK         C   DAL D   1                 N   LEU D   2     1555   1555  1.37  
LINK         C   LEU D   2                 N   ACB D   3     1555   1555  1.36  
LINK         CG  ACB D   3                 N   ARG D   4     1555   1555  1.41  
LINK         C   ARG D   4                 N1  1ZN D   5     1555   1555  1.40  
LINK         C20 1ZN D   5                 N   FGA D   6     1555   1555  1.37  
LINK         CD  FGA D   6                 N   DAM D   7     1555   1555  1.46  
LINK        MN    MN A 401                 O   HOH C 403     1555   1555  2.20  
LINK        MN    MN A 401                 O   HOH A 527     1555   1555  2.06  
LINK        MN    MN A 402                 O   HOH A 527     1555   1555  1.94  
LINK        MN    MN B 401                 O   HOH B 533     1555   1555  2.08  
LINK        MN    MN B 401                 O   HOH D 101     1555   1555  2.23  
LINK        MN    MN B 402                 O   HOH B 533     1555   1555  1.91  
CISPEP   1 ALA A   57    PRO A   58          0         3.11                     
CISPEP   2 PRO A   82    PRO A   83          0         5.48                     
CISPEP   3 ARG A  191    PRO A  192          0        -0.96                     
CISPEP   4 ALA B   57    PRO B   58          0         2.80                     
CISPEP   5 PRO B   82    PRO B   83          0         6.14                     
CISPEP   6 ARG B  191    PRO B  192          0         2.10                     
CRYST1   65.348   78.362  134.038  90.00  90.00  90.00 P 21 21 21    8          
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      0.015303  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012761  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007461        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system