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Database: PDB
Entry: 2XAA
LinkDB: 2XAA
Original site: 2XAA 
HEADER    OXIDOREDUCTASE                          30-MAR-10   2XAA              
TITLE     ALCOHOL DEHYDROGENASE ADH-'A' FROM RHODOCOCCUS RUBER DSM 44541 AT PH  
TITLE    2 8.5 IN COMPLEX WITH NAD AND BUTANE-1,4-DIOL                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SECONDARY ALCOHOL DEHYDROGENASE;                           
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RESIDUES 1-345;                                            
COMPND   5 SYNONYM: ADH-'A';                                                    
COMPND   6 EC: 1.1.1.1;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RUBER;                              
SOURCE   3 ORGANISM_TAXID: 1830;                                                
SOURCE   4 STRAIN: DSM 44541;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: TUNER (DE3);                               
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B;                                   
SOURCE  10 OTHER_DETAILS: DSM                                                   
KEYWDS    CARBONYL REDUCTASE, KETOREDUCTASE, OXIDOREDUCTASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.KROUTIL,K.GRUBER,G.GROGAN                                           
REVDAT   3   20-DEC-23 2XAA    1       REMARK LINK                              
REVDAT   2   01-SEP-10 2XAA    1       JRNL   REMARK                            
REVDAT   1   11-AUG-10 2XAA    0                                                
JRNL        AUTH   M.KARABEC,A.LYSKOWSKI,K.C.TAUBER,G.STEINKELLNER,W.KROUTIL,   
JRNL        AUTH 2 G.GROGAN,K.GRUBER                                            
JRNL        TITL   STRUCTURAL INSIGHTS INTO SUBSTRATE SPECIFICITY AND SOLVENT   
JRNL        TITL 2 TOLERANCE IN ALCOHOL DEHYDROGENASE ADH-'A' FROM RHODOCOCCUS  
JRNL        TITL 3 RUBER DSM 44541.                                             
JRNL        REF    CHEM.COMMUN.(CAMB.)           V.  46  6314 2010              
JRNL        REFN                   ISSN 1359-7345                               
JRNL        PMID   20676439                                                     
JRNL        DOI    10.1039/C0CC00929F                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 109.15                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 34356                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1807                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2238                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 101                          
REMARK   3   BIN FREE R VALUE                    : 0.3390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9731                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 202                                     
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.43                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.79000                                             
REMARK   3    B22 (A**2) : 3.02000                                              
REMARK   3    B33 (A**2) : -0.19000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.94000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.399         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.299         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.282        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.893                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10136 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13859 ; 1.635 ; 1.990       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1354 ; 6.403 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   351 ;33.413 ;22.650       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1379 ;17.195 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    71 ;17.264 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1621 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7683 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6708 ; 0.503 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10665 ; 0.947 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3428 ; 1.420 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3193 ; 2.422 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     345      4                      
REMARK   3           1     B      1       B     345      4                      
REMARK   3           1     C      1       C     345      4                      
REMARK   3           1     D      1       D     345      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2341 ;  0.38 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2341 ;  0.33 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2341 ;  0.32 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2341 ;  0.31 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2341 ;  1.01 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2341 ;  0.81 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2341 ;  0.95 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2341 ;  0.86 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY                            
REMARK   4                                                                      
REMARK   4 2XAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290043471.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9789                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34356                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 109.500                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 9.0                                
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3JV7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BISTRIS PROPANE BUFFER PH 8.5,    
REMARK 280  20% (W/V) PEG MW 4000, 5 MM CDCL2, 6% V/V 2-PROPANOL, 5% (V/V) 1,   
REMARK 280  4-BUTANEDIOL. PROTEIN AT 10 MG/ML                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.55000            
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, 3                                                 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16010 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 44340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -256.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -116.2 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.9 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     VAL A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLY A    26                                                      
REMARK 465     ALA A    53                                                      
REMARK 465     GLU A    70                                                      
REMARK 465     LEU A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     GLU A    73                                                      
REMARK 465     GLY A    74                                                      
REMARK 465     VAL A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ALA B    69                                                      
REMARK 465     GLU B    73                                                      
REMARK 465     GLN C   238                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   2    CG   CD   CE   NZ                                   
REMARK 470     VAL A   4    CG1  CG2                                            
REMARK 470     ILE A   9    CG1  CG2  CD1                                       
REMARK 470     ILE A  18    CG1  CG2  CD1                                       
REMARK 470     ILE A  42    CG1  CG2  CD1                                       
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 315    CD1                                                 
REMARK 470     ARG A 330    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 332    CG   CD1  CD2                                       
REMARK 470     VAL B   4    CG1  CG2                                            
REMARK 470     VAL B  14    CG1  CG2                                            
REMARK 470     THR B  22    OG1  CG2                                            
REMARK 470     LYS B  31    CG   CD   CE   NZ                                   
REMARK 470     ILE B  42    CG1  CG2  CD1                                       
REMARK 470     GLU B  70    CG   CD   OE1  OE2                                  
REMARK 470     VAL B  80    CG1  CG2                                            
REMARK 470     GLU C  73    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  73    CG   CD   OE1  OE2                                  
REMARK 470     ILE D 271    CD1                                                 
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   3      102.88   -162.26                                   
REMARK 500    VAL A   4      106.37    -56.55                                   
REMARK 500    SER A  11     -134.86   -111.85                                   
REMARK 500    PRO A  13     -169.23    -76.23                                   
REMARK 500    PRO A  23     -134.82    -74.13                                   
REMARK 500    ALA A  50      -81.84    -54.45                                   
REMARK 500    ARG A 102       49.87    -89.89                                   
REMARK 500    ASP A 142       30.27    -83.96                                   
REMARK 500    THR A 152       -9.36    -58.55                                   
REMARK 500    ASP A 153      -50.91   -155.09                                   
REMARK 500    LEU A 169       49.88   -106.20                                   
REMARK 500    PHE A 282      -16.71     79.29                                   
REMARK 500    TRP A 295     -131.30     40.55                                   
REMARK 500    GLU A 324        8.18    -68.67                                   
REMARK 500    GLU B  12      150.47    -47.96                                   
REMARK 500    ALA B  34      140.96   -170.23                                   
REMARK 500    ILE B  42       13.04    -65.11                                   
REMARK 500    LEU B 112        7.66    -68.10                                   
REMARK 500    ASP B 153      -61.73   -142.59                                   
REMARK 500    LEU B 169       47.17    -85.82                                   
REMARK 500    ALA B 273       90.60     10.65                                   
REMARK 500    PHE B 282       -7.20     78.86                                   
REMARK 500    PHE B 286      133.42    -33.90                                   
REMARK 500    TRP B 295     -132.80     50.65                                   
REMARK 500    LEU C  60      173.14    -59.42                                   
REMARK 500    ALA C 273      109.45    -50.13                                   
REMARK 500    TRP C 295     -127.15     43.21                                   
REMARK 500    ARG D 102       49.51    -82.17                                   
REMARK 500    LEU D 119       48.18   -141.54                                   
REMARK 500    ASP D 142       20.39    -79.07                                   
REMARK 500    ASP D 153      -66.42   -144.83                                   
REMARK 500    LEU D 169       48.62    -87.45                                   
REMARK 500    VAL D 180       64.38   -103.48                                   
REMARK 500    PHE D 282      -15.09     82.42                                   
REMARK 500    TRP D 295     -116.55     47.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS B  272     ALA B  273                  148.40                    
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 B2005        DISTANCE =  6.26 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1346  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  38   SG                                                     
REMARK 620 2 ASP A 153   OD2 106.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  92   SG                                                     
REMARK 620 2 CYS A  95   SG  111.1                                              
REMARK 620 3 CYS A  98   SG  113.0 106.8                                        
REMARK 620 4 CYS A 106   SG  112.0 111.8 101.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1346  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  38   SG                                                     
REMARK 620 2 HIS B  62   NE2  95.8                                              
REMARK 620 3 ASP B 153   OD2 101.0  79.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B  92   SG                                                     
REMARK 620 2 CYS B  95   SG  109.7                                              
REMARK 620 3 CYS B  98   SG  116.5 103.5                                        
REMARK 620 4 CYS B 106   SG  113.1 108.9 104.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1346  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  38   SG                                                     
REMARK 620 2 HIS C  62   NE2 103.9                                              
REMARK 620 3 ASP C 153   OD2  99.2  86.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1347  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  92   SG                                                     
REMARK 620 2 CYS C  95   SG  112.5                                              
REMARK 620 3 CYS C  98   SG  116.6 103.6                                        
REMARK 620 4 CYS C 106   SG  106.9 112.9 104.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1346  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  38   SG                                                     
REMARK 620 2 HIS D  62   NE2 107.0                                              
REMARK 620 3 ASP D 153   OD2 118.1  84.0                                        
REMARK 620 4 BU1 D1347   O6  126.3 102.2 108.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1348  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  92   SG                                                     
REMARK 620 2 CYS D  95   SG  113.0                                              
REMARK 620 3 CYS D  98   SG  111.3  96.7                                        
REMARK 620 4 CYS D 106   SG  114.8 118.5  99.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 B 1347                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 D 1347                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BU1 C 1348                
DBREF  2XAA A    1   345  UNP    Q8KLT9   Q8KLT9_9NOCA     1    345             
DBREF  2XAA B    1   345  UNP    Q8KLT9   Q8KLT9_9NOCA     1    345             
DBREF  2XAA C    1   345  UNP    Q8KLT9   Q8KLT9_9NOCA     1    345             
DBREF  2XAA D    1   345  UNP    Q8KLT9   Q8KLT9_9NOCA     1    345             
SEQADV 2XAA VAL A    4  UNP  Q8KLT9    LEU     4 CONFLICT                       
SEQADV 2XAA ILE A   18  UNP  Q8KLT9    VAL    18 CONFLICT                       
SEQADV 2XAA THR A   22  UNP  Q8KLT9    ALA    22 CONFLICT                       
SEQADV 2XAA GLU A   73  UNP  Q8KLT9    ALA    73 CONFLICT                       
SEQADV 2XAA VAL A   80  UNP  Q8KLT9    THR    80 CONFLICT                       
SEQADV 2XAA ASP A  111  UNP  Q8KLT9    GLU   111 CONFLICT                       
SEQADV 2XAA GLN A  238  UNP  Q8KLT9    GLU   238 CONFLICT                       
SEQADV 2XAA VAL A  262  UNP  Q8KLT9    ILE   262 CONFLICT                       
SEQADV 2XAA GLU A  303  UNP  Q8KLT9    ASP   303 CONFLICT                       
SEQADV 2XAA VAL B    4  UNP  Q8KLT9    LEU     4 CONFLICT                       
SEQADV 2XAA ILE B   18  UNP  Q8KLT9    VAL    18 CONFLICT                       
SEQADV 2XAA THR B   22  UNP  Q8KLT9    ALA    22 CONFLICT                       
SEQADV 2XAA GLU B   73  UNP  Q8KLT9    ALA    73 CONFLICT                       
SEQADV 2XAA VAL B   80  UNP  Q8KLT9    THR    80 CONFLICT                       
SEQADV 2XAA ASP B  111  UNP  Q8KLT9    GLU   111 CONFLICT                       
SEQADV 2XAA GLN B  238  UNP  Q8KLT9    GLU   238 CONFLICT                       
SEQADV 2XAA VAL B  262  UNP  Q8KLT9    ILE   262 CONFLICT                       
SEQADV 2XAA GLU B  303  UNP  Q8KLT9    ASP   303 CONFLICT                       
SEQADV 2XAA VAL C    4  UNP  Q8KLT9    LEU     4 CONFLICT                       
SEQADV 2XAA ILE C   18  UNP  Q8KLT9    VAL    18 CONFLICT                       
SEQADV 2XAA THR C   22  UNP  Q8KLT9    ALA    22 CONFLICT                       
SEQADV 2XAA GLU C   73  UNP  Q8KLT9    ALA    73 CONFLICT                       
SEQADV 2XAA VAL C   80  UNP  Q8KLT9    THR    80 CONFLICT                       
SEQADV 2XAA ASP C  111  UNP  Q8KLT9    GLU   111 CONFLICT                       
SEQADV 2XAA GLN C  238  UNP  Q8KLT9    GLU   238 CONFLICT                       
SEQADV 2XAA VAL C  262  UNP  Q8KLT9    ILE   262 CONFLICT                       
SEQADV 2XAA GLU C  303  UNP  Q8KLT9    ASP   303 CONFLICT                       
SEQADV 2XAA VAL D    4  UNP  Q8KLT9    LEU     4 CONFLICT                       
SEQADV 2XAA ILE D   18  UNP  Q8KLT9    VAL    18 CONFLICT                       
SEQADV 2XAA THR D   22  UNP  Q8KLT9    ALA    22 CONFLICT                       
SEQADV 2XAA GLU D   73  UNP  Q8KLT9    ALA    73 CONFLICT                       
SEQADV 2XAA VAL D   80  UNP  Q8KLT9    THR    80 CONFLICT                       
SEQADV 2XAA ASP D  111  UNP  Q8KLT9    GLU   111 CONFLICT                       
SEQADV 2XAA GLN D  238  UNP  Q8KLT9    GLU   238 CONFLICT                       
SEQADV 2XAA VAL D  262  UNP  Q8KLT9    ILE   262 CONFLICT                       
SEQADV 2XAA GLU D  303  UNP  Q8KLT9    ASP   303 CONFLICT                       
SEQRES   1 A  345  MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO          
SEQRES   2 A  345  VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY          
SEQRES   3 A  345  GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS          
SEQRES   4 A  345  SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR          
SEQRES   5 A  345  ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL          
SEQRES   6 A  345  GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE          
SEQRES   7 A  345  GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY          
SEQRES   8 A  345  CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN          
SEQRES   9 A  345  TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO          
SEQRES  10 A  345  GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE          
SEQRES  11 A  345  VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU          
SEQRES  12 A  345  ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU          
SEQRES  13 A  345  THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU          
SEQRES  14 A  345  GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY          
SEQRES  15 A  345  LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER          
SEQRES  16 A  345  ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG          
SEQRES  17 A  345  LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL          
SEQRES  18 A  345  LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU          
SEQRES  19 A  345  THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL          
SEQRES  20 A  345  GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL          
SEQRES  21 A  345  ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA          
SEQRES  22 A  345  GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE          
SEQRES  23 A  345  GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER          
SEQRES  24 A  345  GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG          
SEQRES  25 A  345  LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY          
SEQRES  26 A  345  PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG          
SEQRES  27 A  345  GLY ARG GLY VAL VAL VAL PRO                                  
SEQRES   1 B  345  MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO          
SEQRES   2 B  345  VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY          
SEQRES   3 B  345  GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS          
SEQRES   4 B  345  SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR          
SEQRES   5 B  345  ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL          
SEQRES   6 B  345  GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE          
SEQRES   7 B  345  GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY          
SEQRES   8 B  345  CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN          
SEQRES   9 B  345  TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO          
SEQRES  10 B  345  GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE          
SEQRES  11 B  345  VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU          
SEQRES  12 B  345  ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU          
SEQRES  13 B  345  THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU          
SEQRES  14 B  345  GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY          
SEQRES  15 B  345  LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER          
SEQRES  16 B  345  ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG          
SEQRES  17 B  345  LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL          
SEQRES  18 B  345  LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU          
SEQRES  19 B  345  THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL          
SEQRES  20 B  345  GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL          
SEQRES  21 B  345  ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA          
SEQRES  22 B  345  GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE          
SEQRES  23 B  345  GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER          
SEQRES  24 B  345  GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG          
SEQRES  25 B  345  LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY          
SEQRES  26 B  345  PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG          
SEQRES  27 B  345  GLY ARG GLY VAL VAL VAL PRO                                  
SEQRES   1 C  345  MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO          
SEQRES   2 C  345  VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY          
SEQRES   3 C  345  GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS          
SEQRES   4 C  345  SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR          
SEQRES   5 C  345  ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL          
SEQRES   6 C  345  GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE          
SEQRES   7 C  345  GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY          
SEQRES   8 C  345  CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN          
SEQRES   9 C  345  TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO          
SEQRES  10 C  345  GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE          
SEQRES  11 C  345  VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU          
SEQRES  12 C  345  ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU          
SEQRES  13 C  345  THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU          
SEQRES  14 C  345  GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY          
SEQRES  15 C  345  LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER          
SEQRES  16 C  345  ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG          
SEQRES  17 C  345  LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL          
SEQRES  18 C  345  LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU          
SEQRES  19 C  345  THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL          
SEQRES  20 C  345  GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL          
SEQRES  21 C  345  ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA          
SEQRES  22 C  345  GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE          
SEQRES  23 C  345  GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER          
SEQRES  24 C  345  GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG          
SEQRES  25 C  345  LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY          
SEQRES  26 C  345  PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG          
SEQRES  27 C  345  GLY ARG GLY VAL VAL VAL PRO                                  
SEQRES   1 D  345  MET LYS ALA VAL GLN TYR THR GLU ILE GLY SER GLU PRO          
SEQRES   2 D  345  VAL VAL VAL ASP ILE PRO THR PRO THR PRO GLY PRO GLY          
SEQRES   3 D  345  GLU ILE LEU LEU LYS VAL THR ALA ALA GLY LEU CYS HIS          
SEQRES   4 D  345  SER ASP ILE PHE VAL MET ASP MET PRO ALA ALA GLN TYR          
SEQRES   5 D  345  ALA TYR GLY LEU PRO LEU THR LEU GLY HIS GLU GLY VAL          
SEQRES   6 D  345  GLY THR VAL ALA GLU LEU GLY GLU GLY VAL THR GLY PHE          
SEQRES   7 D  345  GLY VAL GLY ASP ALA VAL ALA VAL TYR GLY PRO TRP GLY          
SEQRES   8 D  345  CYS GLY ALA CYS HIS ALA CYS ALA ARG GLY ARG GLU ASN          
SEQRES   9 D  345  TYR CYS THR ARG ALA ALA ASP LEU GLY ILE THR PRO PRO          
SEQRES  10 D  345  GLY LEU GLY SER PRO GLY SER MET ALA GLU TYR MET ILE          
SEQRES  11 D  345  VAL ASP SER ALA ARG HIS LEU VAL PRO ILE GLY ASP LEU          
SEQRES  12 D  345  ASP PRO VAL ALA ALA ALA PRO LEU THR ASP ALA GLY LEU          
SEQRES  13 D  345  THR PRO TYR HIS ALA ILE SER ARG VAL LEU PRO LEU LEU          
SEQRES  14 D  345  GLY PRO GLY SER THR ALA VAL VAL ILE GLY VAL GLY GLY          
SEQRES  15 D  345  LEU GLY HIS VAL GLY ILE GLN ILE LEU ARG ALA VAL SER          
SEQRES  16 D  345  ALA ALA ARG VAL ILE ALA VAL ASP LEU ASP ASP ASP ARG          
SEQRES  17 D  345  LEU ALA LEU ALA ARG GLU VAL GLY ALA ASP ALA ALA VAL          
SEQRES  18 D  345  LYS SER GLY ALA GLY ALA ALA ASP ALA ILE ARG GLU LEU          
SEQRES  19 D  345  THR GLY GLY GLN GLY ALA THR ALA VAL PHE ASP PHE VAL          
SEQRES  20 D  345  GLY ALA GLN SER THR ILE ASP THR ALA GLN GLN VAL VAL          
SEQRES  21 D  345  ALA VAL ASP GLY HIS ILE SER VAL VAL GLY ILE HIS ALA          
SEQRES  22 D  345  GLY ALA HIS ALA LYS VAL GLY PHE PHE MET ILE PRO PHE          
SEQRES  23 D  345  GLY ALA SER VAL VAL THR PRO TYR TRP GLY THR ARG SER          
SEQRES  24 D  345  GLU LEU MET GLU VAL VAL ALA LEU ALA ARG ALA GLY ARG          
SEQRES  25 D  345  LEU ASP ILE HIS THR GLU THR PHE THR LEU ASP GLU GLY          
SEQRES  26 D  345  PRO ALA ALA TYR ARG ARG LEU ARG GLU GLY SER ILE ARG          
SEQRES  27 D  345  GLY ARG GLY VAL VAL VAL PRO                                  
HET    NAD  A 503      44                                                       
HET     ZN  A1346       1                                                       
HET     ZN  A1347       1                                                       
HET    NAD  B 503      44                                                       
HET     ZN  B1346       1                                                       
HET    BU1  B1347       6                                                       
HET     ZN  B1348       1                                                       
HET    NAD  C 503      44                                                       
HET     ZN  C1346       1                                                       
HET     ZN  C1347       1                                                       
HET    BU1  C1348       6                                                       
HET    NAD  D 503      44                                                       
HET     ZN  D1346       1                                                       
HET    BU1  D1347       6                                                       
HET     ZN  D1348       1                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM      ZN ZINC ION                                                         
HETNAM     BU1 1,4-BUTANEDIOL                                                   
FORMUL   5  NAD    4(C21 H27 N7 O14 P2)                                         
FORMUL   6   ZN    8(ZN 2+)                                                     
FORMUL  10  BU1    3(C4 H10 O2)                                                 
FORMUL  20  HOH   *142(H2 O)                                                    
HELIX    1   1 CYS A   38  MET A   45  1                                   8    
HELIX    2   2 CYS A   95  ARG A  100  1                                   6    
HELIX    3   3 ARG A  102  CYS A  106  5                                   5    
HELIX    4   4 ARG A  108  GLY A  113  1                                   6    
HELIX    5   5 SER A  133  ARG A  135  5                                   3    
HELIX    6   6 ASP A  144  GLY A  155  1                                  12    
HELIX    7   7 GLY A  155  ARG A  164  1                                  10    
HELIX    8   8 VAL A  165  LEU A  169  5                                   5    
HELIX    9   9 GLY A  181  SER A  195  1                                  15    
HELIX   10  10 ASP A  205  VAL A  215  1                                  11    
HELIX   11  11 GLY A  226  GLY A  236  1                                  11    
HELIX   12  12 ALA A  249  VAL A  259  1                                  11    
HELIX   13  13 THR A  297  ALA A  310  1                                  14    
HELIX   14  14 GLU A  324  GLY A  335  1                                  12    
HELIX   15  15 SER B   40  MET B   45  1                                   6    
HELIX   16  16 CYS B   95  ARG B  100  1                                   6    
HELIX   17  17 ARG B  102  CYS B  106  5                                   5    
HELIX   18  18 SER B  133  ARG B  135  5                                   3    
HELIX   19  19 ASP B  144  ALA B  149  1                                   6    
HELIX   20  20 PRO B  150  ASP B  153  5                                   4    
HELIX   21  21 GLY B  155  ARG B  164  1                                  10    
HELIX   22  22 VAL B  165  LEU B  169  5                                   5    
HELIX   23  23 LEU B  183  SER B  195  1                                  13    
HELIX   24  24 ASP B  205  VAL B  215  1                                  11    
HELIX   25  25 GLY B  226  GLY B  236  1                                  11    
HELIX   26  26 ALA B  249  VAL B  259  1                                  11    
HELIX   27  27 THR B  297  ALA B  310  1                                  14    
HELIX   28  28 GLU B  324  GLY B  335  1                                  12    
HELIX   29  29 CYS C   38  MET C   47  1                                  10    
HELIX   30  30 ALA C   97  GLY C  101  5                                   5    
HELIX   31  31 ARG C  102  CYS C  106  5                                   5    
HELIX   32  32 ARG C  108  GLY C  113  1                                   6    
HELIX   33  33 SER C  133  ARG C  135  5                                   3    
HELIX   34  34 ASP C  144  ALA C  148  5                                   5    
HELIX   35  35 ALA C  148  THR C  152  5                                   5    
HELIX   36  36 GLY C  155  ARG C  164  1                                  10    
HELIX   37  37 VAL C  165  LEU C  169  5                                   5    
HELIX   38  38 GLY C  181  SER C  195  1                                  15    
HELIX   39  39 ASP C  205  VAL C  215  1                                  11    
HELIX   40  40 GLY C  226  GLY C  236  1                                  11    
HELIX   41  41 ALA C  249  VAL C  259  1                                  11    
HELIX   42  42 THR C  297  ALA C  310  1                                  14    
HELIX   43  43 GLU C  324  GLY C  335  1                                  12    
HELIX   44  44 CYS D   38  ASP D   46  1                                   9    
HELIX   45  45 ALA D   97  GLY D  101  5                                   5    
HELIX   46  46 ARG D  102  CYS D  106  5                                   5    
HELIX   47  47 SER D  133  ARG D  135  5                                   3    
HELIX   48  48 ASP D  144  ALA D  149  1                                   6    
HELIX   49  49 PRO D  150  ASP D  153  5                                   4    
HELIX   50  50 GLY D  155  ARG D  164  1                                  10    
HELIX   51  51 VAL D  165  LEU D  169  5                                   5    
HELIX   52  52 GLY D  181  SER D  195  1                                  15    
HELIX   53  53 ASP D  205  VAL D  215  1                                  11    
HELIX   54  54 GLY D  226  GLY D  236  1                                  11    
HELIX   55  55 ALA D  249  VAL D  259  1                                  11    
HELIX   56  56 THR D  297  ALA D  310  1                                  14    
HELIX   57  57 THR D  321  ASP D  323  5                                   3    
HELIX   58  58 GLU D  324  GLY D  335  1                                  12    
SHEET    1  AA 2 TYR A 128  VAL A 131  0                                        
SHEET    2  AA 2 ILE A  28  GLY A  36 -1  O  ILE A  28   N  VAL A 131           
SHEET    1  AB 6 LEU A 137  PRO A 139  0                                        
SHEET    2  AB 6 ALA A  83  VAL A  86 -1  O  ALA A  85   N  VAL A 138           
SHEET    3  AB 6 GLU A  63  VAL A  68 -1  O  GLY A  64   N  VAL A  86           
SHEET    4  AB 6 ILE A  28  GLY A  36 -1  O  LYS A  31   N  THR A  67           
SHEET    5  AB 6 VAL A 342  VAL A 343 -1  O  VAL A 343   N  ALA A  35           
SHEET    6  AB 6 THR A 319  PHE A 320 -1  N  PHE A 320   O  VAL A 342           
SHEET    1  AC 5 LEU A 137  PRO A 139  0                                        
SHEET    2  AC 5 ALA A  83  VAL A  86 -1  O  ALA A  85   N  VAL A 138           
SHEET    3  AC 5 GLU A  63  VAL A  68 -1  O  GLY A  64   N  VAL A  86           
SHEET    4  AC 5 ILE A  28  GLY A  36 -1  O  LYS A  31   N  THR A  67           
SHEET    5  AC 5 TYR A 128  VAL A 131 -1  O  MET A 129   N  LEU A  30           
SHEET    1  AD 6 ALA A 219  LYS A 222  0                                        
SHEET    2  AD 6 ARG A 198  ASP A 203  1  O  ALA A 201   N  VAL A 221           
SHEET    3  AD 6 THR A 174  ILE A 178  1  O  ALA A 175   N  ILE A 200           
SHEET    4  AD 6 ALA A 240  ASP A 245  1  O  ALA A 242   N  VAL A 176           
SHEET    5  AD 6 VAL A 260  VAL A 268  1  N  ALA A 261   O  ALA A 240           
SHEET    6  AD 6 SER A 289  VAL A 291  1  O  SER A 289   N  ILE A 266           
SHEET    1  AE 2 ALA A 277  VAL A 279  0                                        
SHEET    2  AE 2 ALA D 277  VAL D 279 -1  O  ALA D 277   N  VAL A 279           
SHEET    1  BA 3 VAL B  14  ASP B  17  0                                        
SHEET    2  BA 3 LYS B   2  TYR B   6 -1  O  ALA B   3   N  VAL B  16           
SHEET    3  BA 3 LEU B  58  THR B  59 -1  O  LEU B  58   N  TYR B   6           
SHEET    1  BB 2 TYR B 128  VAL B 131  0                                        
SHEET    2  BB 2 ILE B  28  GLY B  36 -1  O  ILE B  28   N  VAL B 131           
SHEET    1  BC 6 LEU B 137  PRO B 139  0                                        
SHEET    2  BC 6 ALA B  83  VAL B  86 -1  O  ALA B  85   N  VAL B 138           
SHEET    3  BC 6 GLU B  63  THR B  67 -1  O  GLY B  64   N  VAL B  86           
SHEET    4  BC 6 ILE B  28  GLY B  36 -1  O  LYS B  31   N  THR B  67           
SHEET    5  BC 6 ARG B 340  VAL B 343 -1  O  VAL B 343   N  ALA B  35           
SHEET    6  BC 6 THR B 317  PHE B 320 -1  O  GLU B 318   N  VAL B 342           
SHEET    1  BD 5 LEU B 137  PRO B 139  0                                        
SHEET    2  BD 5 ALA B  83  VAL B  86 -1  O  ALA B  85   N  VAL B 138           
SHEET    3  BD 5 GLU B  63  THR B  67 -1  O  GLY B  64   N  VAL B  86           
SHEET    4  BD 5 ILE B  28  GLY B  36 -1  O  LYS B  31   N  THR B  67           
SHEET    5  BD 5 TYR B 128  VAL B 131 -1  O  MET B 129   N  LEU B  30           
SHEET    1  BE 6 ALA B 219  LYS B 222  0                                        
SHEET    2  BE 6 ARG B 198  ASP B 203  1  O  VAL B 199   N  ALA B 219           
SHEET    3  BE 6 THR B 174  ILE B 178  1  O  ALA B 175   N  ILE B 200           
SHEET    4  BE 6 ALA B 240  ASP B 245  1  N  THR B 241   O  THR B 174           
SHEET    5  BE 6 VAL B 260  VAL B 268  1  N  ALA B 261   O  ALA B 240           
SHEET    6  BE 6 SER B 289  VAL B 291  1  O  SER B 289   N  ILE B 266           
SHEET    1  BF 2 ALA B 277  VAL B 279  0                                        
SHEET    2  BF 2 ALA C 277  VAL C 279 -1  O  ALA C 277   N  VAL B 279           
SHEET    1  CA 3 VAL C  14  ASP C  17  0                                        
SHEET    2  CA 3 LYS C   2  TYR C   6 -1  O  ALA C   3   N  VAL C  16           
SHEET    3  CA 3 LEU C  58  THR C  59 -1  O  LEU C  58   N  TYR C   6           
SHEET    1  CB 2 TYR C 128  VAL C 131  0                                        
SHEET    2  CB 2 ILE C  28  GLY C  36 -1  O  ILE C  28   N  VAL C 131           
SHEET    1  CC 6 LEU C 137  PRO C 139  0                                        
SHEET    2  CC 6 ALA C  83  VAL C  86 -1  O  ALA C  85   N  VAL C 138           
SHEET    3  CC 6 GLU C  63  LEU C  71 -1  O  GLY C  64   N  VAL C  86           
SHEET    4  CC 6 ILE C  28  GLY C  36 -1  O  LEU C  29   N  ALA C  69           
SHEET    5  CC 6 ARG C 340  VAL C 343 -1  O  VAL C 343   N  ALA C  35           
SHEET    6  CC 6 THR C 317  PHE C 320 -1  O  GLU C 318   N  VAL C 342           
SHEET    1  CD 5 LEU C 137  PRO C 139  0                                        
SHEET    2  CD 5 ALA C  83  VAL C  86 -1  O  ALA C  85   N  VAL C 138           
SHEET    3  CD 5 GLU C  63  LEU C  71 -1  O  GLY C  64   N  VAL C  86           
SHEET    4  CD 5 ILE C  28  GLY C  36 -1  O  LEU C  29   N  ALA C  69           
SHEET    5  CD 5 TYR C 128  VAL C 131 -1  O  MET C 129   N  LEU C  30           
SHEET    1  CE 6 ALA C 219  LYS C 222  0                                        
SHEET    2  CE 6 ARG C 198  ASP C 203  1  O  ALA C 201   N  VAL C 221           
SHEET    3  CE 6 THR C 174  ILE C 178  1  O  ALA C 175   N  ILE C 200           
SHEET    4  CE 6 ALA C 240  ASP C 245  1  O  ALA C 242   N  VAL C 176           
SHEET    5  CE 6 VAL C 260  VAL C 268  1  N  ALA C 261   O  ALA C 240           
SHEET    6  CE 6 SER C 289  VAL C 291  1  O  SER C 289   N  ILE C 266           
SHEET    1  DA 3 VAL D  14  ASP D  17  0                                        
SHEET    2  DA 3 LYS D   2  TYR D   6 -1  O  ALA D   3   N  VAL D  16           
SHEET    3  DA 3 LEU D  58  THR D  59 -1  O  LEU D  58   N  TYR D   6           
SHEET    1  DB 2 TYR D 128  VAL D 131  0                                        
SHEET    2  DB 2 ILE D  28  LEU D  37 -1  O  ILE D  28   N  VAL D 131           
SHEET    1  DC 6 LEU D 137  PRO D 139  0                                        
SHEET    2  DC 6 ALA D  83  VAL D  86 -1  O  ALA D  85   N  VAL D 138           
SHEET    3  DC 6 GLU D  63  LEU D  71 -1  O  GLY D  64   N  VAL D  86           
SHEET    4  DC 6 ILE D  28  LEU D  37 -1  O  LEU D  29   N  ALA D  69           
SHEET    5  DC 6 ARG D 340  VAL D 343 -1  O  GLY D 341   N  LEU D  37           
SHEET    6  DC 6 THR D 317  PHE D 320 -1  O  GLU D 318   N  VAL D 342           
SHEET    1  DD 5 LEU D 137  PRO D 139  0                                        
SHEET    2  DD 5 ALA D  83  VAL D  86 -1  O  ALA D  85   N  VAL D 138           
SHEET    3  DD 5 GLU D  63  LEU D  71 -1  O  GLY D  64   N  VAL D  86           
SHEET    4  DD 5 ILE D  28  LEU D  37 -1  O  LEU D  29   N  ALA D  69           
SHEET    5  DD 5 TYR D 128  VAL D 131 -1  O  MET D 129   N  LEU D  30           
SHEET    1  DE 6 ALA D 219  LYS D 222  0                                        
SHEET    2  DE 6 ARG D 198  ASP D 203  1  O  VAL D 199   N  ALA D 219           
SHEET    3  DE 6 THR D 174  ILE D 178  1  O  ALA D 175   N  ILE D 200           
SHEET    4  DE 6 ALA D 240  ASP D 245  1  O  ALA D 242   N  VAL D 176           
SHEET    5  DE 6 VAL D 260  VAL D 268  1  N  ALA D 261   O  ALA D 240           
SHEET    6  DE 6 SER D 289  VAL D 291  1  O  SER D 289   N  ILE D 266           
LINK         SG BCYS A  38                ZN    ZN A1346     1555   1555  2.52  
LINK         SG  CYS A  92                ZN    ZN A1347     1555   1555  2.26  
LINK         SG  CYS A  95                ZN    ZN A1347     1555   1555  2.24  
LINK         SG  CYS A  98                ZN    ZN A1347     1555   1555  2.16  
LINK         SG  CYS A 106                ZN    ZN A1347     1555   1555  2.33  
LINK         OD2 ASP A 153                ZN    ZN A1346     1555   1555  2.17  
LINK         SG  CYS B  38                ZN    ZN B1346     1555   1555  2.28  
LINK         NE2 HIS B  62                ZN    ZN B1346     1555   1555  2.17  
LINK         SG  CYS B  92                ZN    ZN B1348     1555   1555  2.23  
LINK         SG  CYS B  95                ZN    ZN B1348     1555   1555  2.19  
LINK         SG  CYS B  98                ZN    ZN B1348     1555   1555  2.43  
LINK         SG  CYS B 106                ZN    ZN B1348     1555   1555  2.18  
LINK         OD2 ASP B 153                ZN    ZN B1346     1555   1555  2.00  
LINK         SG  CYS C  38                ZN    ZN C1346     1555   1555  2.31  
LINK         NE2 HIS C  62                ZN    ZN C1346     1555   1555  2.12  
LINK         SG  CYS C  92                ZN    ZN C1347     1555   1555  2.27  
LINK         SG  CYS C  95                ZN    ZN C1347     1555   1555  2.23  
LINK         SG  CYS C  98                ZN    ZN C1347     1555   1555  2.22  
LINK         SG  CYS C 106                ZN    ZN C1347     1555   1555  2.37  
LINK         OD2 ASP C 153                ZN    ZN C1346     1555   1555  1.71  
LINK         SG  CYS D  38                ZN    ZN D1346     1555   1555  2.23  
LINK         NE2 HIS D  62                ZN    ZN D1346     1555   1555  2.07  
LINK         SG  CYS D  92                ZN    ZN D1348     1555   1555  2.41  
LINK         SG  CYS D  95                ZN    ZN D1348     1555   1555  2.43  
LINK         SG  CYS D  98                ZN    ZN D1348     1555   1555  2.24  
LINK         SG  CYS D 106                ZN    ZN D1348     1555   1555  2.36  
LINK         OD2 ASP D 153                ZN    ZN D1346     1555   1555  1.95  
LINK        ZN    ZN D1346                 O6  BU1 D1347     1555   1555  2.32  
CISPEP   1 LEU A   56    PRO A   57          0        10.21                     
CISPEP   2 LEU B   56    PRO B   57          0        -3.26                     
CISPEP   3 LEU C   56    PRO C   57          0        -3.23                     
CISPEP   4 LEU D   56    PRO D   57          0         1.13                     
SITE     1 AC1  5 CYS A  38  SER A  40  HIS A  62  ASP A 153                    
SITE     2 AC1  5 NAD A 503                                                     
SITE     1 AC2  4 CYS A  92  CYS A  95  CYS A  98  CYS A 106                    
SITE     1 AC3 23 CYS A  38  HIS A  39  SER A  40  ASP A 153                    
SITE     2 AC3 23 THR A 157  GLY A 181  GLY A 182  LEU A 183                    
SITE     3 AC3 23 ASP A 203  LEU A 204  ARG A 208  SER A 223                    
SITE     4 AC3 23 PHE A 246  VAL A 247  VAL A 269  ILE A 271                    
SITE     5 AC3 23 PRO A 293  TYR A 294  TRP A 295  ARG A 340                    
SITE     6 AC3 23  ZN A1346  HOH A2010  PHE D 281                               
SITE     1 AC4  6 CYS B  38  SER B  40  HIS B  62  ASP B 153                    
SITE     2 AC4  6 NAD B 503  BU1 B1347                                          
SITE     1 AC5  4 SER B  40  ILE B 271  NAD B 503   ZN B1346                    
SITE     1 AC6  4 CYS B  92  CYS B  95  CYS B  98  CYS B 106                    
SITE     1 AC7 28 HIS B  39  SER B  40  ASP B 153  THR B 157                    
SITE     2 AC7 28 GLY B 179  VAL B 180  GLY B 181  GLY B 182                    
SITE     3 AC7 28 LEU B 183  ASP B 203  LEU B 204  ARG B 208                    
SITE     4 AC7 28 SER B 223  PHE B 246  VAL B 247  THR B 252                    
SITE     5 AC7 28 VAL B 269  GLY B 270  ILE B 271  PRO B 293                    
SITE     6 AC7 28 TYR B 294  TRP B 295  LEU B 332  ARG B 340                    
SITE     7 AC7 28  ZN B1346  BU1 B1347  HOH B2039  PHE C 281                    
SITE     1 AC8  6 CYS C  38  SER C  40  HIS C  62  ASP C 153                    
SITE     2 AC8  6 NAD C 503  BU1 C1348                                          
SITE     1 AC9  4 CYS C  92  CYS C  95  CYS C  98  CYS C 106                    
SITE     1 BC1 29 PHE B 281  HIS C  39  SER C  40  ASP C 153                    
SITE     2 BC1 29 THR C 157  ILE C 178  GLY C 179  VAL C 180                    
SITE     3 BC1 29 GLY C 181  GLY C 182  LEU C 183  VAL C 202                    
SITE     4 BC1 29 ASP C 203  LEU C 204  ARG C 208  SER C 223                    
SITE     5 BC1 29 PHE C 246  VAL C 247  VAL C 269  GLY C 270                    
SITE     6 BC1 29 ILE C 271  PRO C 293  TYR C 294  TRP C 295                    
SITE     7 BC1 29 LEU C 332  ARG C 340   ZN C1346  BU1 C1348                    
SITE     8 BC1 29 HOH C2038                                                     
SITE     1 BC2  6 CYS D  38  SER D  40  HIS D  62  ASP D 153                    
SITE     2 BC2  6 NAD D 503  BU1 D1347                                          
SITE     1 BC3  5 SER D  40  HIS D  62  ASP D 153  NAD D 503                    
SITE     2 BC3  5  ZN D1346                                                     
SITE     1 BC4  4 CYS D  92  CYS D  95  CYS D  98  CYS D 106                    
SITE     1 BC5 27 HIS D  39  SER D  40  ASP D 153  GLY D 179                    
SITE     2 BC5 27 VAL D 180  GLY D 181  GLY D 182  LEU D 183                    
SITE     3 BC5 27 ASP D 203  LEU D 204  ARG D 208  SER D 223                    
SITE     4 BC5 27 PHE D 246  VAL D 247  VAL D 269  GLY D 270                    
SITE     5 BC5 27 ILE D 271  PRO D 293  TYR D 294  TRP D 295                    
SITE     6 BC5 27 ARG D 340   ZN D1346  BU1 D1347  HOH D2015                    
SITE     7 BC5 27 HOH D2020  HOH D2036  HOH D2037                               
SITE     1 BC6  4 SER C  40  ILE C 271  NAD C 503   ZN C1346                    
CRYST1   65.674  105.100  109.176  90.00  91.27  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015227  0.000000  0.000338        0.00000                         
SCALE2      0.000000  0.009515  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009162        0.00000                         
MTRIX1   1  0.982000 -0.158500  0.103100       -2.51800    1                    
MTRIX2   1 -0.157000 -0.987300 -0.023000        1.59200    1                    
MTRIX3   1  0.105400  0.006406 -0.994400       51.24000    1                    
MTRIX1   2 -0.982200  0.153100 -0.108500       31.02000    1                    
MTRIX2   2  0.155700  0.342000 -0.926700       21.83000    1                    
MTRIX3   2 -0.104800 -0.927100 -0.359800       36.94000    1                    
MTRIX1   3 -1.000000 -0.002726  0.004900       28.23000    1                    
MTRIX2   3  0.005550 -0.356100  0.934400      -25.58000    1                    
MTRIX3   3  0.000802  0.934400  0.356100       17.63000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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