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Database: PDB
Entry: 3PZV
LinkDB: 3PZV
Original site: 3PZV 
HEADER    HYDROLASE                               14-DEC-10   3PZV              
TITLE     C2 CRYSTAL FORM OF THE ENDO-1,4-BETA-GLUCANASE FROM BACILLUS SUBTILIS 
TITLE    2 168                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOGLUCANASE;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 27-332;                     
COMPND   5 SYNONYM: CARBOXYMETHYL-CELLULASE, CMCASE, CELLULASE, ENDO-1,4-BETA-  
COMPND   6 GLUCANASE;                                                           
COMPND   7 EC: 3.2.1.4;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: EGLS, BGLC, GLD, BSU18130;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA BARREL, GLYCOSYL HYDROLASE, CELLULOSE BINDING, HYDROLASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.R.SANTOS,J.H.PAIVA,P.K.AKAO,A.N.MEZA,J.C.SILVA,F.M.SQUINA,R.J.WARD, 
AUTHOR   2 R.RULLER,M.T.MURAKAMI                                                
REVDAT   3   21-FEB-24 3PZV    1       SEQADV                                   
REVDAT   2   28-DEC-11 3PZV    1       JRNL                                     
REVDAT   1   14-SEP-11 3PZV    0                                                
JRNL        AUTH   C.R.SANTOS,J.H.PAIVA,M.L.SFORCA,J.L.NEVES,R.Z.NAVARRO,       
JRNL        AUTH 2 J.COTA,P.K.AKAO,Z.B.HOFFMAM,A.N.MEZA,J.H.SMETANA,            
JRNL        AUTH 3 M.L.NOGUEIRA,I.POLIKARPOV,J.XAVIER-NETO,F.M.SQUINA,R.J.WARD, 
JRNL        AUTH 4 R.RULLER,A.C.ZERI,M.T.MURAKAMI                               
JRNL        TITL   DISSECTING STRUCTURE-FUNCTION-STABILITY RELATIONSHIPS OF A   
JRNL        TITL 2 THERMOSTABLE GH5-CBM3 CELLULASE FROM BACILLUS SUBTILIS 168.  
JRNL        REF    BIOCHEM.J.                    V. 441    95 2012              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   21880019                                                     
JRNL        DOI    10.1042/BJ20110869                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.87 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28575                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1456                            
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 41.4684 -  6.1704    0.97     2994   178  0.2027 0.2738        
REMARK   3     2  6.1704 -  4.9001    0.97     2966   149  0.2347 0.2851        
REMARK   3     3  4.9001 -  4.2814    0.97     2937   164  0.2001 0.2764        
REMARK   3     4  4.2814 -  3.8903    0.96     2917   136  0.2077 0.2556        
REMARK   3     5  3.8903 -  3.6116    0.96     2905   165  0.2370 0.3232        
REMARK   3     6  3.6116 -  3.3988    0.94     2833   149  0.2647 0.2887        
REMARK   3     7  3.3988 -  3.2286    0.93     2776   165  0.2716 0.3544        
REMARK   3     8  3.2286 -  3.0881    0.89     2679   138  0.2858 0.3606        
REMARK   3     9  3.0881 -  2.9693    0.80     2383   137  0.3200 0.3779        
REMARK   3    10  2.9693 -  2.8670    0.57     1729    75  0.3203 0.4494        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.29                                          
REMARK   3   B_SOL              : 38.06                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 18.14860                                             
REMARK   3    B22 (A**2) : -6.20130                                             
REMARK   3    B33 (A**2) : -11.94730                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 10.05620                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           9584                                  
REMARK   3   ANGLE     :  1.261          12996                                  
REMARK   3   CHIRALITY :  0.088           1376                                  
REMARK   3   PLANARITY :  0.006           1684                                  
REMARK   3   DIHEDRAL  : 16.235           3452                                  
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 3PZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000063017.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LNLS                               
REMARK 200  BEAMLINE                       : W01B-MX2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.4586                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.867                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350 200 MM SODIUM NITRATE, PH    
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       77.67950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.54000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       77.67950            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       40.54000            
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     MET A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     ARG A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     SER A    24                                                      
REMARK 465     HIS A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     LYS A    33                                                      
REMARK 465     THR A   332                                                      
REMARK 465     MET B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     HIS B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     ARG B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     HIS B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ALA B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     THR B    32                                                      
REMARK 465     LYS B    33                                                      
REMARK 465     THR B   332                                                      
REMARK 465     MET C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     HIS C    13                                                      
REMARK 465     HIS C    14                                                      
REMARK 465     HIS C    15                                                      
REMARK 465     SER C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     LEU C    19                                                      
REMARK 465     VAL C    20                                                      
REMARK 465     PRO C    21                                                      
REMARK 465     ARG C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     SER C    24                                                      
REMARK 465     HIS C    25                                                      
REMARK 465     MET C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     ALA C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     THR C    32                                                      
REMARK 465     LYS C    33                                                      
REMARK 465     THR C   332                                                      
REMARK 465     MET D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     HIS D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     HIS D    13                                                      
REMARK 465     HIS D    14                                                      
REMARK 465     HIS D    15                                                      
REMARK 465     SER D    16                                                      
REMARK 465     SER D    17                                                      
REMARK 465     GLY D    18                                                      
REMARK 465     LEU D    19                                                      
REMARK 465     VAL D    20                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     ARG D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     SER D    24                                                      
REMARK 465     HIS D    25                                                      
REMARK 465     MET D    26                                                      
REMARK 465     ALA D    27                                                      
REMARK 465     SER D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     ALA D    30                                                      
REMARK 465     GLY D    31                                                      
REMARK 465     THR D    32                                                      
REMARK 465     LYS D    33                                                      
REMARK 465     THR D   332                                                      
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    PRO A  35     -171.40    -68.39                                   
REMARK 500    VAL A  36      -48.57     52.06                                   
REMARK 500    LEU A 133      -77.07   -157.21                                   
REMARK 500    ALA A 167       89.89   -169.08                                   
REMARK 500    ASP A 217       62.99   -105.20                                   
REMARK 500    ASN A 266     -159.74   -142.04                                   
REMARK 500    GLN A 297       30.26    -66.71                                   
REMARK 500    ASP A 317      -16.70    -48.35                                   
REMARK 500    LEU A 330       23.10    -57.34                                   
REMARK 500    ASN B  51     -168.54   -110.33                                   
REMARK 500    ASN B 105       80.54   -161.78                                   
REMARK 500    LEU B 133      -76.29   -161.19                                   
REMARK 500    ALA B 167       88.20   -163.76                                   
REMARK 500    ASN B 168      -74.08    -36.03                                   
REMARK 500    SER B 208       46.95     75.64                                   
REMARK 500    ASP B 217       57.02   -154.74                                   
REMARK 500    SER B 248        7.97    -59.45                                   
REMARK 500    SER B 261     -166.45   -103.94                                   
REMARK 500    ASN B 266     -149.22   -132.01                                   
REMARK 500    PHE B 270       78.89   -119.49                                   
REMARK 500    PRO C  35      -85.80    -96.59                                   
REMARK 500    VAL C  36       10.34    -63.96                                   
REMARK 500    ASN C  39       53.88   -109.84                                   
REMARK 500    ASN C  51     -132.42    -75.19                                   
REMARK 500    ILE C  88      143.15    -38.39                                   
REMARK 500    PRO C 106       45.57    -77.00                                   
REMARK 500    TRP C 130       84.15    -62.59                                   
REMARK 500    LEU C 133      -77.89   -143.08                                   
REMARK 500    ASP C 135       63.86    -64.02                                   
REMARK 500    PRO C 138       -5.22    -59.73                                   
REMARK 500    PHE C 148      -70.69    -77.09                                   
REMARK 500    PHE C 149      -15.16    -41.19                                   
REMARK 500    ASN C 194      -24.60   -160.66                                   
REMARK 500    SER C 208       68.97     38.67                                   
REMARK 500    ASP C 216      -18.13   -141.36                                   
REMARK 500    GLN C 218     -161.78    -75.06                                   
REMARK 500    VAL C 255       90.97    -59.43                                   
REMARK 500    ASP C 262     -157.85    -73.91                                   
REMARK 500    ASN C 266     -127.36   -140.45                                   
REMARK 500    GLN C 297       72.83    -60.58                                   
REMARK 500    LEU C 330      -74.72    -70.96                                   
REMARK 500    ASN D  51     -152.12    -96.63                                   
REMARK 500    HIS D  65     -157.15    -87.45                                   
REMARK 500    ASN D  75      167.02    162.76                                   
REMARK 500    ASP D  85      -73.72    -94.21                                   
REMARK 500    VAL D  90      155.72    175.48                                   
REMARK 500    THR D  97      -82.50    -70.76                                   
REMARK 500    ALA D  98     -171.91    -68.06                                   
REMARK 500    ASP D  99       61.21     62.05                                   
REMARK 500    LEU D 133      -75.20   -172.27                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      68 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3PZT   RELATED DB: PDB                                   
REMARK 900 WITH MANGANESE(II) ION                                               
REMARK 900 RELATED ID: 3PZU   RELATED DB: PDB                                   
REMARK 900 P212121 CRYSTAL FORM                                                 
DBREF  3PZV A   27   332  UNP    P10475   GUN2_BACSU      27    332             
DBREF  3PZV B   27   332  UNP    P10475   GUN2_BACSU      27    332             
DBREF  3PZV C   27   332  UNP    P10475   GUN2_BACSU      27    332             
DBREF  3PZV D   27   332  UNP    P10475   GUN2_BACSU      27    332             
SEQADV 3PZV MET A    6  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY A    7  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER A    8  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER A    9  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   10  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   11  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   12  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   13  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   14  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   15  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER A   16  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER A   17  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY A   18  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV LEU A   19  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV VAL A   20  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV PRO A   21  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV ARG A   22  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY A   23  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER A   24  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS A   25  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET A   26  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET B    6  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY B    7  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER B    8  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER B    9  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   10  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   11  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   12  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   13  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   14  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   15  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER B   16  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER B   17  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY B   18  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV LEU B   19  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV VAL B   20  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV PRO B   21  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV ARG B   22  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY B   23  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER B   24  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS B   25  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET B   26  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET C    6  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY C    7  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER C    8  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER C    9  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   10  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   11  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   12  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   13  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   14  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   15  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER C   16  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER C   17  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY C   18  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV LEU C   19  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV VAL C   20  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV PRO C   21  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV ARG C   22  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY C   23  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER C   24  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS C   25  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET C   26  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET D    6  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY D    7  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER D    8  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER D    9  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   10  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   11  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   12  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   13  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   14  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   15  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER D   16  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER D   17  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY D   18  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV LEU D   19  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV VAL D   20  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV PRO D   21  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV ARG D   22  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV GLY D   23  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV SER D   24  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV HIS D   25  UNP  P10475              EXPRESSION TAG                 
SEQADV 3PZV MET D   26  UNP  P10475              EXPRESSION TAG                 
SEQRES   1 A  327  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  327  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY          
SEQRES   3 A  327  THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE          
SEQRES   4 A  327  LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL          
SEQRES   5 A  327  GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR          
SEQRES   6 A  327  GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG          
SEQRES   7 A  327  ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR          
SEQRES   8 A  327  THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS          
SEQRES   9 A  327  ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU          
SEQRES  10 A  327  GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP          
SEQRES  11 A  327  GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE          
SEQRES  12 A  327  PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN          
SEQRES  13 A  327  VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL          
SEQRES  14 A  327  ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL          
SEQRES  15 A  327  ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE          
SEQRES  16 A  327  ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP          
SEQRES  17 A  327  ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR          
SEQRES  18 A  327  ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU          
SEQRES  19 A  327  ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO          
SEQRES  20 A  327  ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY          
SEQRES  21 A  327  ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU          
SEQRES  22 A  327  LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP          
SEQRES  23 A  327  ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS          
SEQRES  24 A  327  PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP          
SEQRES  25 A  327  LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU          
SEQRES  26 A  327  GLY THR                                                      
SEQRES   1 B  327  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  327  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY          
SEQRES   3 B  327  THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE          
SEQRES   4 B  327  LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL          
SEQRES   5 B  327  GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR          
SEQRES   6 B  327  GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG          
SEQRES   7 B  327  ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR          
SEQRES   8 B  327  THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS          
SEQRES   9 B  327  ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU          
SEQRES  10 B  327  GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP          
SEQRES  11 B  327  GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE          
SEQRES  12 B  327  PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN          
SEQRES  13 B  327  VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL          
SEQRES  14 B  327  ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL          
SEQRES  15 B  327  ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE          
SEQRES  16 B  327  ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP          
SEQRES  17 B  327  ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR          
SEQRES  18 B  327  ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU          
SEQRES  19 B  327  ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO          
SEQRES  20 B  327  ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY          
SEQRES  21 B  327  ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU          
SEQRES  22 B  327  LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP          
SEQRES  23 B  327  ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS          
SEQRES  24 B  327  PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP          
SEQRES  25 B  327  LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU          
SEQRES  26 B  327  GLY THR                                                      
SEQRES   1 C  327  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  327  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY          
SEQRES   3 C  327  THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE          
SEQRES   4 C  327  LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL          
SEQRES   5 C  327  GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR          
SEQRES   6 C  327  GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG          
SEQRES   7 C  327  ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR          
SEQRES   8 C  327  THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS          
SEQRES   9 C  327  ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU          
SEQRES  10 C  327  GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP          
SEQRES  11 C  327  GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE          
SEQRES  12 C  327  PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN          
SEQRES  13 C  327  VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL          
SEQRES  14 C  327  ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL          
SEQRES  15 C  327  ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE          
SEQRES  16 C  327  ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP          
SEQRES  17 C  327  ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR          
SEQRES  18 C  327  ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU          
SEQRES  19 C  327  ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO          
SEQRES  20 C  327  ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY          
SEQRES  21 C  327  ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU          
SEQRES  22 C  327  LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP          
SEQRES  23 C  327  ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS          
SEQRES  24 C  327  PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP          
SEQRES  25 C  327  LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU          
SEQRES  26 C  327  GLY THR                                                      
SEQRES   1 D  327  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  327  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY          
SEQRES   3 D  327  THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE          
SEQRES   4 D  327  LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL          
SEQRES   5 D  327  GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR          
SEQRES   6 D  327  GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG          
SEQRES   7 D  327  ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR          
SEQRES   8 D  327  THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS          
SEQRES   9 D  327  ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU          
SEQRES  10 D  327  GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP          
SEQRES  11 D  327  GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE          
SEQRES  12 D  327  PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN          
SEQRES  13 D  327  VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL          
SEQRES  14 D  327  ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL          
SEQRES  15 D  327  ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE          
SEQRES  16 D  327  ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP          
SEQRES  17 D  327  ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR          
SEQRES  18 D  327  ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU          
SEQRES  19 D  327  ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO          
SEQRES  20 D  327  ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY          
SEQRES  21 D  327  ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU          
SEQRES  22 D  327  LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP          
SEQRES  23 D  327  ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS          
SEQRES  24 D  327  PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP          
SEQRES  25 D  327  LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU          
SEQRES  26 D  327  GLY THR                                                      
FORMUL   5  HOH   *30(H2 O)                                                     
HELIX    1   1 GLY A   66  GLY A   71  1                                   6    
HELIX    2   2 GLU A   72  VAL A   74  5                                   3    
HELIX    3   3 ASN A   75  GLY A   87  1                                  13    
HELIX    4   4 ASN A  105  SER A  107  5                                   3    
HELIX    5   5 VAL A  108  GLY A  123  1                                  16    
HELIX    6   6 ASN A  137  GLN A  140  5                                   4    
HELIX    7   7 ASN A  141  GLY A  157  1                                  17    
HELIX    8   8 ASP A  179  LYS A  193  1                                  15    
HELIX    9   9 THR A  204  GLN A  209  1                                   6    
HELIX   10  10 ASP A  210  ASP A  217  1                                   8    
HELIX   11  11 GLY A  236  LYS A  249  1                                  14    
HELIX   12  12 PHE A  270  LYS A  284  1                                  15    
HELIX   13  13 SER A  319  ASN A  328  1                                  10    
HELIX   14  14 THR B   34  GLY B   40  1                                   7    
HELIX   15  15 GLY B   66  GLY B   71  1                                   6    
HELIX   16  16 GLU B   72  VAL B   74  5                                   3    
HELIX   17  17 ASN B   75  ASP B   85  1                                  11    
HELIX   18  18 ASN B  105  SER B  107  5                                   3    
HELIX   19  19 VAL B  108  GLY B  123  1                                  16    
HELIX   20  20 ASN B  141  GLY B  157  1                                  17    
HELIX   21  21 ASP B  179  ASP B  195  1                                  17    
HELIX   22  22 THR B  204  GLN B  209  1                                   6    
HELIX   23  23 ASP B  210  ASP B  216  1                                   7    
HELIX   24  24 GLY B  236  SER B  248  1                                  13    
HELIX   25  25 PHE B  270  LYS B  284  1                                  15    
HELIX   26  26 ARG B  314  LEU B  318  5                                   5    
HELIX   27  27 SER B  319  GLY B  331  1                                  13    
HELIX   28  28 TYR C   70  VAL C   74  5                                   5    
HELIX   29  29 ASN C   75  TRP C   86  1                                  12    
HELIX   30  30 VAL C  108  GLY C  123  1                                  16    
HELIX   31  31 ASN C  141  GLY C  157  1                                  17    
HELIX   32  32 ASP C  179  LYS C  193  1                                  15    
HELIX   33  33 THR C  204  GLN C  209  1                                   6    
HELIX   34  34 ASP C  210  ALA C  215  1                                   6    
HELIX   35  35 GLY C  236  LYS C  249  1                                  14    
HELIX   36  36 PHE C  270  LYS C  284  1                                  15    
HELIX   37  37 ARG C  314  LEU C  318  5                                   5    
HELIX   38  38 SER C  319  GLY C  331  1                                  13    
HELIX   39  39 PRO D   35  GLY D   40  1                                   6    
HELIX   40  40 GLY D   66  GLY D   71  1                                   6    
HELIX   41  41 GLU D   72  VAL D   74  5                                   3    
HELIX   42  42 ASN D   75  ASP D   85  1                                  11    
HELIX   43  43 ASN D  105  SER D  107  5                                   3    
HELIX   44  44 VAL D  108  GLU D  121  1                                  14    
HELIX   45  45 ASN D  137  GLN D  140  5                                   4    
HELIX   46  46 ASN D  141  TYR D  156  1                                  16    
HELIX   47  47 ASP D  179  LYS D  193  1                                  15    
HELIX   48  48 THR D  204  GLN D  209  1                                   6    
HELIX   49  49 VAL D  211  ASP D  216  1                                   6    
HELIX   50  50 GLY D  236  SER D  248  1                                  13    
HELIX   51  51 PHE D  270  LYS D  284  1                                  15    
HELIX   52  52 SER D  319  LEU D  330  1                                  12    
SHEET    1   A 2 SER A  43  LYS A  45  0                                        
SHEET    2   A 2 GLN A  48  VAL A  50 -1  O  VAL A  50   N  SER A  43           
SHEET    1   B 9 LYS A  60  SER A  64  0                                        
SHEET    2   B 9 VAL A  90  TYR A  96  1  O  ARG A  92   N  SER A  64           
SHEET    3   B 9 TYR A 125  HIS A 131  1  O  ILE A 127   N  ALA A  93           
SHEET    4   B 9 VAL A 162  GLU A 165  1  O  GLU A 165   N  TRP A 130           
SHEET    5   B 9 ILE A 200  VAL A 202  1  O  ILE A 201   N  TYR A 164           
SHEET    6   B 9 VAL A 224  TYR A 231  1  O  MET A 225   N  VAL A 202           
SHEET    7   B 9 ILE A 253  GLY A 259  1  O  PHE A 254   N  TYR A 226           
SHEET    8   B 9 TRP A 288  LEU A 293  1  O  TRP A 291   N  TRP A 258           
SHEET    9   B 9 LYS A  60  SER A  64  1  N  SER A  63   O  LEU A 293           
SHEET    1   C 2 SER B  43  LYS B  45  0                                        
SHEET    2   C 2 GLN B  48  VAL B  50 -1  O  VAL B  50   N  SER B  43           
SHEET    1   D 9 LYS B  60  SER B  64  0                                        
SHEET    2   D 9 VAL B  90  TYR B  96  1  O  ARG B  92   N  SER B  64           
SHEET    3   D 9 TYR B 125  HIS B 131  1  O  ILE B 127   N  ALA B  93           
SHEET    4   D 9 VAL B 162  GLU B 165  1  O  ILE B 163   N  ILE B 128           
SHEET    5   D 9 ILE B 200  VAL B 202  1  O  ILE B 201   N  TYR B 164           
SHEET    6   D 9 VAL B 224  TYR B 231  1  O  MET B 225   N  VAL B 202           
SHEET    7   D 9 ILE B 253  GLY B 259  1  O  PHE B 254   N  TYR B 226           
SHEET    8   D 9 TRP B 288  LEU B 293  1  O  TRP B 291   N  TRP B 258           
SHEET    9   D 9 LYS B  60  SER B  64  1  N  SER B  63   O  ASN B 290           
SHEET    1   E 2 SER C  43  LYS C  45  0                                        
SHEET    2   E 2 GLN C  48  VAL C  50 -1  O  VAL C  50   N  SER C  43           
SHEET    1   F 8 ILE C 200  ILE C 201  0                                        
SHEET    2   F 8 VAL C 162  GLU C 165  1  N  TYR C 164   O  ILE C 201           
SHEET    3   F 8 TYR C 125  HIS C 131  1  N  ILE C 128   O  ILE C 163           
SHEET    4   F 8 VAL C  90  TYR C  96  1  N  PHE C  91   O  TYR C 125           
SHEET    5   F 8 LYS C  60  SER C  64  1  N  ILE C  62   O  ARG C  92           
SHEET    6   F 8 TRP C 288  LEU C 293  1  O  LEU C 293   N  SER C  63           
SHEET    7   F 8 ILE C 253  GLY C 259  1  N  VAL C 255   O  VAL C 289           
SHEET    8   F 8 TYR C 226  ALA C 227  1  N  TYR C 226   O  PHE C 254           
SHEET    1   G 8 ILE C 200  ILE C 201  0                                        
SHEET    2   G 8 VAL C 162  GLU C 165  1  N  TYR C 164   O  ILE C 201           
SHEET    3   G 8 TYR C 125  HIS C 131  1  N  ILE C 128   O  ILE C 163           
SHEET    4   G 8 VAL C  90  TYR C  96  1  N  PHE C  91   O  TYR C 125           
SHEET    5   G 8 LYS C  60  SER C  64  1  N  ILE C  62   O  ARG C  92           
SHEET    6   G 8 TRP C 288  LEU C 293  1  O  LEU C 293   N  SER C  63           
SHEET    7   G 8 ILE C 253  GLY C 259  1  N  VAL C 255   O  VAL C 289           
SHEET    8   G 8 PHE C 230  TYR C 231  1  N  PHE C 230   O  GLY C 259           
SHEET    1   H 2 SER D  43  LYS D  45  0                                        
SHEET    2   H 2 GLN D  48  VAL D  50 -1  O  VAL D  50   N  SER D  43           
SHEET    1   I 9 LYS D  60  SER D  63  0                                        
SHEET    2   I 9 PHE D  91  TYR D  96  1  O  ARG D  92   N  ILE D  62           
SHEET    3   I 9 VAL D 126  HIS D 131  1  O  ILE D 127   N  ALA D  93           
SHEET    4   I 9 VAL D 162  GLU D 165  1  O  GLU D 165   N  ILE D 128           
SHEET    5   I 9 ILE D 199  VAL D 202  1  O  ILE D 201   N  TYR D 164           
SHEET    6   I 9 VAL D 224  TYR D 231  1  O  MET D 225   N  ILE D 200           
SHEET    7   I 9 ILE D 253  GLY D 259  1  O  PHE D 254   N  LEU D 228           
SHEET    8   I 9 TRP D 288  ASN D 290  1  O  VAL D 289   N  VAL D 255           
SHEET    9   I 9 LYS D  60  SER D  63  1  N  GLY D  61   O  ASN D 290           
CISPEP   1 TRP A  291    ASN A  292          0         7.62                     
CISPEP   2 TRP B  291    ASN B  292          0         3.06                     
CISPEP   3 TRP C  291    ASN C  292          0        -1.11                     
CISPEP   4 TRP D  291    ASN D  292          0         0.91                     
CRYST1  155.359   81.080  114.270  90.00 104.29  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006437  0.000000  0.001639        0.00000                         
SCALE2      0.000000  0.012333  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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