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Database: PDB
Entry: 1PZ1
LinkDB: 1PZ1
Original site: 1PZ1 
HEADER    OXIDOREDUCTASE                          09-JUL-03   1PZ1              
TITLE     STRUCTURE OF NADPH-DEPENDENT FAMILY 11 ALDO-KETO REDUCTASE            
TITLE    2 AKR11B(HOLO)                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GENERAL STRESS PROTEIN 69;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GSP69;                                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: YHDN;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21*;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PTYB2                                     
KEYWDS    BETA-ALPHA BARREL, ALDO-KETO REDUCTASE, TIM BARREL,                   
KEYWDS   2 OXIDOREDUCTASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.H.EHRENSBERGER,D.K.WILSON                                           
REVDAT   2   24-FEB-09 1PZ1    1       VERSN                                    
REVDAT   1   30-MAR-04 1PZ1    0                                                
JRNL        AUTH   A.H.EHRENSBERGER,D.K.WILSON                                  
JRNL        TITL   STRUCTURAL AND CATALYTIC DIVERSITY IN THE TWO                
JRNL        TITL 2 FAMILY 11 ALDO-KETO REDUCTASES                               
JRNL        REF    J.MOL.BIOL.                   V. 337   661 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15019785                                                     
JRNL        DOI    10.1016/J.JMB.2004.01.059                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 36232                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1799                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5290                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 96                                      
REMARK   3   SOLVENT ATOMS            : 413                                     
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.012                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.47                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PZ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019712.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.74                               
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) : 0.97903, 0.88557, 0.97922          
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : DOUBLE MIRROR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36239                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.4900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.020                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM ACETATE,                
REMARK 280  IMIDAZOLE, PH 7.74, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       58.68300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL UNIT CONSISTS OF A MONOMER. EACH              
REMARK 300 ASYMMETRIC UNITS CONSISTS OF TWO BIOLOGICAL UNITS.                   
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 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 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 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    ALA A   7     -121.86     49.64                                   
REMARK 500    ALA A  86       11.60     90.49                                   
REMARK 500    HIS A  97       87.31   -163.90                                   
REMARK 500    ASN A  99      157.38    -48.27                                   
REMARK 500    TYR A 178      123.08   -170.55                                   
REMARK 500    SER A 188      -23.79   -148.19                                   
REMARK 500    ALA A 289       57.57    -91.95                                   
REMARK 500    ILE A 331      -52.57   -158.22                                   
REMARK 500    PRO A 332     -145.50    -88.80                                   
REMARK 500    ALA B   7     -134.85     46.97                                   
REMARK 500    ALA B  86       22.10     90.63                                   
REMARK 500    HIS B  97       87.46   -159.50                                   
REMARK 500    TYR B 178      127.69   -176.50                                   
REMARK 500    SER B 188      -35.37   -138.46                                   
REMARK 500    ILE B 331      -32.90   -155.10                                   
REMARK 500    PRO B 332     -145.17    -61.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B  73         0.06    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 610        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B 640        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH B 666        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B 678        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH B 679        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH B 687        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH B 710        DISTANCE =  8.26 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 500                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 501                 
DBREF  1PZ1 A    1   331  UNP    P80874   GS69_BACSU       1    331             
DBREF  1PZ1 B    1   331  UNP    P80874   GS69_BACSU       1    331             
SEQADV 1PZ1 MSE A    1  UNP  P80874    MET     1 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A   27  UNP  P80874    MET    27 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A   74  UNP  P80874    GLY    74 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A  140  UNP  P80874    MET   140 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A  162  UNP  P80874    MET   162 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A  185  UNP  P80874    MET   185 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A  215  UNP  P80874    MET   215 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE A  323  UNP  P80874    MET   323 MODIFIED RESIDUE               
SEQADV 1PZ1 PRO A  332  UNP  P80874              CLONING ARTIFACT               
SEQADV 1PZ1 GLY A  333  UNP  P80874              CLONING ARTIFACT               
SEQADV 1PZ1 MSE B    1  UNP  P80874    MET     1 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B   27  UNP  P80874    MET    27 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B   74  UNP  P80874    GLY    74 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B  140  UNP  P80874    MET   140 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B  162  UNP  P80874    MET   162 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B  185  UNP  P80874    MET   185 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B  215  UNP  P80874    MET   215 MODIFIED RESIDUE               
SEQADV 1PZ1 MSE B  323  UNP  P80874    MET   323 MODIFIED RESIDUE               
SEQADV 1PZ1 PRO B  332  UNP  P80874              CLONING ARTIFACT               
SEQADV 1PZ1 GLY B  333  UNP  P80874              CLONING ARTIFACT               
SEQRES   1 A  333  MSE GLU TYR THR SER ILE ALA ASP THR GLY ILE GLU ALA          
SEQRES   2 A  333  SER ARG ILE GLY LEU GLY THR TRP ALA ILE GLY GLY THR          
SEQRES   3 A  333  MSE TRP GLY GLY THR ASP GLU LYS THR SER ILE GLU THR          
SEQRES   4 A  333  ILE ARG ALA ALA LEU ASP GLN GLY ILE THR LEU ILE ASP          
SEQRES   5 A  333  THR ALA PRO ALA TYR GLY PHE GLY GLN SER GLU GLU ILE          
SEQRES   6 A  333  VAL GLY LYS ALA ILE LYS GLU TYR MSE LYS ARG ASP GLN          
SEQRES   7 A  333  VAL ILE LEU ALA THR LYS THR ALA LEU ASP TRP LYS ASN          
SEQRES   8 A  333  ASN GLN LEU PHE ARG HIS ALA ASN ARG ALA ARG ILE VAL          
SEQRES   9 A  333  GLU GLU VAL GLU ASN SER LEU LYS ARG LEU GLN THR ASP          
SEQRES  10 A  333  TYR ILE ASP LEU TYR GLN VAL HIS TRP PRO ASP PRO LEU          
SEQRES  11 A  333  VAL PRO ILE GLU GLU THR ALA GLU VAL MSE LYS GLU LEU          
SEQRES  12 A  333  TYR ASP ALA GLY LYS ILE ARG ALA ILE GLY VAL SER ASN          
SEQRES  13 A  333  PHE SER ILE GLU GLN MSE ASP THR PHE ARG ALA VAL ALA          
SEQRES  14 A  333  PRO LEU HIS THR ILE GLN PRO PRO TYR ASN LEU PHE GLU          
SEQRES  15 A  333  ARG GLU MSE GLU GLU SER VAL LEU PRO TYR ALA LYS ASP          
SEQRES  16 A  333  ASN LYS ILE THR THR LEU LEU TYR GLY SER LEU CYS ARG          
SEQRES  17 A  333  GLY LEU LEU THR GLY LYS MSE THR GLU GLU TYR THR PHE          
SEQRES  18 A  333  GLU GLY ASP ASP LEU ARG ASN HIS ASP PRO LYS PHE GLN          
SEQRES  19 A  333  LYS PRO ARG PHE LYS GLU TYR LEU SER ALA VAL ASN GLN          
SEQRES  20 A  333  LEU ASP LYS LEU ALA LYS THR ARG TYR GLY LYS SER VAL          
SEQRES  21 A  333  ILE HIS LEU ALA VAL ARG TRP ILE LEU ASP GLN PRO GLY          
SEQRES  22 A  333  ALA ASP ILE ALA LEU TRP GLY ALA ARG LYS PRO GLY GLN          
SEQRES  23 A  333  LEU GLU ALA LEU SER GLU ILE THR GLY TRP THR LEU ASN          
SEQRES  24 A  333  SER GLU ASP GLN LYS ASP ILE ASN THR ILE LEU GLU ASN          
SEQRES  25 A  333  THR ILE SER ASP PRO VAL GLY PRO GLU PHE MSE ALA PRO          
SEQRES  26 A  333  PRO THR ARG GLU GLU ILE PRO GLY                              
SEQRES   1 B  333  MSE GLU TYR THR SER ILE ALA ASP THR GLY ILE GLU ALA          
SEQRES   2 B  333  SER ARG ILE GLY LEU GLY THR TRP ALA ILE GLY GLY THR          
SEQRES   3 B  333  MSE TRP GLY GLY THR ASP GLU LYS THR SER ILE GLU THR          
SEQRES   4 B  333  ILE ARG ALA ALA LEU ASP GLN GLY ILE THR LEU ILE ASP          
SEQRES   5 B  333  THR ALA PRO ALA TYR GLY PHE GLY GLN SER GLU GLU ILE          
SEQRES   6 B  333  VAL GLY LYS ALA ILE LYS GLU TYR MSE LYS ARG ASP GLN          
SEQRES   7 B  333  VAL ILE LEU ALA THR LYS THR ALA LEU ASP TRP LYS ASN          
SEQRES   8 B  333  ASN GLN LEU PHE ARG HIS ALA ASN ARG ALA ARG ILE VAL          
SEQRES   9 B  333  GLU GLU VAL GLU ASN SER LEU LYS ARG LEU GLN THR ASP          
SEQRES  10 B  333  TYR ILE ASP LEU TYR GLN VAL HIS TRP PRO ASP PRO LEU          
SEQRES  11 B  333  VAL PRO ILE GLU GLU THR ALA GLU VAL MSE LYS GLU LEU          
SEQRES  12 B  333  TYR ASP ALA GLY LYS ILE ARG ALA ILE GLY VAL SER ASN          
SEQRES  13 B  333  PHE SER ILE GLU GLN MSE ASP THR PHE ARG ALA VAL ALA          
SEQRES  14 B  333  PRO LEU HIS THR ILE GLN PRO PRO TYR ASN LEU PHE GLU          
SEQRES  15 B  333  ARG GLU MSE GLU GLU SER VAL LEU PRO TYR ALA LYS ASP          
SEQRES  16 B  333  ASN LYS ILE THR THR LEU LEU TYR GLY SER LEU CYS ARG          
SEQRES  17 B  333  GLY LEU LEU THR GLY LYS MSE THR GLU GLU TYR THR PHE          
SEQRES  18 B  333  GLU GLY ASP ASP LEU ARG ASN HIS ASP PRO LYS PHE GLN          
SEQRES  19 B  333  LYS PRO ARG PHE LYS GLU TYR LEU SER ALA VAL ASN GLN          
SEQRES  20 B  333  LEU ASP LYS LEU ALA LYS THR ARG TYR GLY LYS SER VAL          
SEQRES  21 B  333  ILE HIS LEU ALA VAL ARG TRP ILE LEU ASP GLN PRO GLY          
SEQRES  22 B  333  ALA ASP ILE ALA LEU TRP GLY ALA ARG LYS PRO GLY GLN          
SEQRES  23 B  333  LEU GLU ALA LEU SER GLU ILE THR GLY TRP THR LEU ASN          
SEQRES  24 B  333  SER GLU ASP GLN LYS ASP ILE ASN THR ILE LEU GLU ASN          
SEQRES  25 B  333  THR ILE SER ASP PRO VAL GLY PRO GLU PHE MSE ALA PRO          
SEQRES  26 B  333  PRO THR ARG GLU GLU ILE PRO GLY                              
MODRES 1PZ1 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A   27  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A   74  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A  162  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A  185  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A  215  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE A  323  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B   27  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B   74  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B  140  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B  162  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B  185  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B  215  MET  SELENOMETHIONINE                                   
MODRES 1PZ1 MSE B  323  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  27       8                                                       
HET    MSE  A  74       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 162       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 215       8                                                       
HET    MSE  A 323       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  27       8                                                       
HET    MSE  B  74       8                                                       
HET    MSE  B 140       8                                                       
HET    MSE  B 162       8                                                       
HET    MSE  B 185       8                                                       
HET    MSE  B 215       8                                                       
HET    MSE  B 323       8                                                       
HET    NAP  A 500      48                                                       
HET    NAP  B 501      48                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE                 
HETSYN     NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE                       
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  NAP    2(C21 H28 N7 O17 P3)                                         
FORMUL   5  HOH   *413(H2 O)                                                    
HELIX    1   1 TRP A   21  GLY A   25  5                                   5    
HELIX    2   2 ASP A   32  GLN A   46  1                                  15    
HELIX    3   3 ALA A   56  PHE A   59  5                                   4    
HELIX    4   4 GLY A   60  MSE A   74  1                                  15    
HELIX    5   5 LYS A   75  VAL A   79  5                                   5    
HELIX    6   6 ASN A   99  LEU A  114  1                                  16    
HELIX    7   7 PRO A  132  ALA A  146  1                                  15    
HELIX    8   8 SER A  158  ALA A  167  1                                  10    
HELIX    9   9 ARG A  183  GLU A  187  5                                   5    
HELIX   10  10 SER A  188  ASN A  196  1                                   9    
HELIX   11  11 LEU A  206  LEU A  210  5                                   5    
HELIX   12  12 ASP A  225  HIS A  229  5                                   5    
HELIX   13  13 ASP A  230  GLN A  234  5                                   5    
HELIX   14  14 ARG A  237  GLY A  257  1                                  21    
HELIX   15  15 SER A  259  ASP A  270  1                                  12    
HELIX   16  16 LYS A  283  GLU A  288  5                                   6    
HELIX   17  17 ASN A  299  ILE A  314  1                                  16    
HELIX   18  18 PRO A  320  ALA A  324  5                                   5    
HELIX   19  19 TRP B   21  GLY B   25  5                                   5    
HELIX   20  20 ASP B   32  ASP B   45  1                                  14    
HELIX   21  21 ALA B   56  PHE B   59  5                                   4    
HELIX   22  22 GLY B   60  MSE B   74  1                                  15    
HELIX   23  23 LYS B   75  VAL B   79  5                                   5    
HELIX   24  24 ASN B   99  GLN B  115  1                                  17    
HELIX   25  25 PRO B  132  ALA B  146  1                                  15    
HELIX   26  26 SER B  158  ALA B  167  1                                  10    
HELIX   27  27 ARG B  183  GLU B  187  5                                   5    
HELIX   28  28 SER B  188  LYS B  197  1                                  10    
HELIX   29  29 LEU B  206  LEU B  210  5                                   5    
HELIX   30  30 ASP B  225  HIS B  229  5                                   5    
HELIX   31  31 ASP B  230  GLN B  234  5                                   5    
HELIX   32  32 PRO B  236  GLY B  257  1                                  22    
HELIX   33  33 SER B  259  ASP B  270  1                                  12    
HELIX   34  34 LYS B  283  ILE B  293  5                                  11    
HELIX   35  35 ASN B  299  ILE B  314  1                                  16    
HELIX   36  36 PRO B  320  ALA B  324  5                                   5    
HELIX   37  37 THR B  327  ILE B  331  5                                   5    
SHEET    1   A 2 TYR A   3  SER A   5  0                                        
SHEET    2   A 2 GLU A  12  SER A  14 -1  O  ALA A  13   N  THR A   4           
SHEET    1   B 9 ILE A  16  GLY A  19  0                                        
SHEET    2   B 9 LEU A  50  ASP A  52  1  O  LEU A  50   N  LEU A  18           
SHEET    3   B 9 ILE A  80  THR A  85  1  O  ALA A  82   N  ILE A  51           
SHEET    4   B 9 LEU A 121  VAL A 124  1  O  GLN A 123   N  THR A  85           
SHEET    5   B 9 ILE A 152  VAL A 154  1  O  GLY A 153   N  VAL A 124           
SHEET    6   B 9 THR A 173  ILE A 174  1  O  THR A 173   N  VAL A 154           
SHEET    7   B 9 THR A 199  LEU A 202  1  O  LEU A 201   N  ILE A 174           
SHEET    8   B 9 ILE A 276  GLY A 280  1  O  ILE A 276   N  LEU A 202           
SHEET    9   B 9 ILE A  16  GLY A  19  1  N  GLY A  17   O  TRP A 279           
SHEET    1   C 2 LEU A  87  TRP A  89  0                                        
SHEET    2   C 2 LEU A  94  ARG A  96 -1  O  PHE A  95   N  ASP A  88           
SHEET    1   D 2 TYR B   3  SER B   5  0                                        
SHEET    2   D 2 GLU B  12  SER B  14 -1  O  ALA B  13   N  THR B   4           
SHEET    1   E 9 ILE B  16  GLY B  19  0                                        
SHEET    2   E 9 LEU B  50  ASP B  52  1  O  ASP B  52   N  LEU B  18           
SHEET    3   E 9 ILE B  80  THR B  85  1  O  ALA B  82   N  ILE B  51           
SHEET    4   E 9 LEU B 121  VAL B 124  1  O  GLN B 123   N  THR B  85           
SHEET    5   E 9 ILE B 152  VAL B 154  1  O  GLY B 153   N  TYR B 122           
SHEET    6   E 9 THR B 173  ILE B 174  1  O  THR B 173   N  VAL B 154           
SHEET    7   E 9 THR B 199  LEU B 202  1  O  LEU B 201   N  ILE B 174           
SHEET    8   E 9 ILE B 276  GLY B 280  1  O  ILE B 276   N  LEU B 202           
SHEET    9   E 9 ILE B  16  GLY B  19  1  N  GLY B  17   O  TRP B 279           
SHEET    1   F 2 LEU B  87  LYS B  90  0                                        
SHEET    2   F 2 GLN B  93  ARG B  96 -1  O  PHE B  95   N  ASP B  88           
LINK         C   MSE A   1                 N   GLU A   2     1555   1555  1.33  
LINK         C   THR A  26                 N   MSE A  27     1555   1555  1.34  
LINK         C   MSE A  27                 N   TRP A  28     1555   1555  1.34  
LINK         C   TYR A  73                 N   MSE A  74     1555   1555  1.34  
LINK         C   MSE A  74                 N   LYS A  75     1555   1555  1.33  
LINK         C   VAL A 139                 N   MSE A 140     1555   1555  1.33  
LINK         C   MSE A 140                 N   LYS A 141     1555   1555  1.33  
LINK         C   GLN A 161                 N   MSE A 162     1555   1555  1.33  
LINK         C   MSE A 162                 N   ASP A 163     1555   1555  1.34  
LINK         C   GLU A 184                 N   MSE A 185     1555   1555  1.33  
LINK         C   MSE A 185                 N   GLU A 186     1555   1555  1.33  
LINK         C   LYS A 214                 N   MSE A 215     1555   1555  1.33  
LINK         C   MSE A 215                 N   THR A 216     1555   1555  1.34  
LINK         C   PHE A 322                 N   MSE A 323     1555   1555  1.33  
LINK         C   MSE A 323                 N   ALA A 324     1555   1555  1.33  
LINK         C   MSE B   1                 N   GLU B   2     1555   1555  1.33  
LINK         C   THR B  26                 N   MSE B  27     1555   1555  1.34  
LINK         C   MSE B  27                 N   TRP B  28     1555   1555  1.33  
LINK         C   TYR B  73                 N   MSE B  74     1555   1555  1.33  
LINK         C   MSE B  74                 N   LYS B  75     1555   1555  1.34  
LINK         C   VAL B 139                 N   MSE B 140     1555   1555  1.33  
LINK         C   MSE B 140                 N   LYS B 141     1555   1555  1.34  
LINK         C   GLN B 161                 N   MSE B 162     1555   1555  1.33  
LINK         C   MSE B 162                 N   ASP B 163     1555   1555  1.34  
LINK         C   GLU B 184                 N   MSE B 185     1555   1555  1.33  
LINK         C   MSE B 185                 N   GLU B 186     1555   1555  1.33  
LINK         C   LYS B 214                 N   MSE B 215     1555   1555  1.33  
LINK         C   MSE B 215                 N   THR B 216     1555   1555  1.33  
LINK         C   PHE B 322                 N   MSE B 323     1555   1555  1.34  
LINK         C   MSE B 323                 N   ALA B 324     1555   1555  1.33  
CISPEP   1 LYS A  235    PRO A  236          0         0.10                     
CISPEP   2 LYS B  235    PRO B  236          0        -1.46                     
SITE     1 AC1 25 GLY A  19  THR A  20  TRP A  21  TRP A  28                    
SITE     2 AC1 25 ASP A  52  TYR A  57  LYS A  84  SER A 155                    
SITE     3 AC1 25 GLN A 175  TYR A 203  GLY A 204  LEU A 206                    
SITE     4 AC1 25 CYS A 207  ARG A 208  GLY A 209  LYS A 214                    
SITE     5 AC1 25 ARG A 227  LEU A 278  TRP A 279  GLY A 280                    
SITE     6 AC1 25 ARG A 282  GLN A 286  HOH A 510  HOH A 679                    
SITE     7 AC1 25 HOH A 682                                                     
SITE     1 AC2 27 GLY B  19  THR B  20  TRP B  21  TRP B  28                    
SITE     2 AC2 27 ASP B  52  TYR B  57  LYS B  84  SER B 155                    
SITE     3 AC2 27 ASN B 156  GLN B 175  TYR B 203  GLY B 204                    
SITE     4 AC2 27 LEU B 206  CYS B 207  ARG B 208  GLY B 209                    
SITE     5 AC2 27 THR B 212  LYS B 214  ARG B 227  ILE B 261                    
SITE     6 AC2 27 GLY B 280  ARG B 282  GLN B 286  HOH B 504                    
SITE     7 AC2 27 HOH B 574  HOH B 576  HOH B 701                               
CRYST1   58.255  117.366   59.787  90.00  91.88  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017166  0.000000  0.000563        0.00000                         
SCALE2      0.000000  0.008520  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016735        0.00000                         
HETATM    1  N   MSE A   1     -16.167  32.357  -6.074  1.00 21.00           N  
HETATM    2  CA  MSE A   1     -14.956  31.645  -6.587  1.00 19.98           C  
HETATM    3  C   MSE A   1     -14.555  32.204  -7.952  1.00 19.52           C  
HETATM    4  O   MSE A   1     -15.411  32.606  -8.736  1.00 19.88           O  
HETATM    5  CB  MSE A   1     -15.238  30.141  -6.703  1.00 19.43           C  
HETATM    6  CG  MSE A   1     -14.044  29.297  -7.152  1.00 17.80           C  
HETATM    7 SE   MSE A   1     -12.512  29.420  -5.961  1.00 21.15          SE  
HETATM    8  CE  MSE A   1     -13.368  28.763  -4.345  1.00 18.63           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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