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Database: PDB
Entry: 3N56
LinkDB: 3N56
Original site: 3N56 
HEADER    HYDROLASE/HORMONE                       24-MAY-10   3N56              
TITLE     CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME (IDE) IN COMPLEX  
TITLE    2 WITH HUMAN B-TYPE NATRIURETIC PEPTIDE (BNP)                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN-DEGRADING ENZYME;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 42-1019;                                      
COMPND   5 SYNONYM: INSULIN PROTEASE, INSULINASE, INSULYSIN, ABETA-DEGRADING    
COMPND   6 PROTEASE;                                                            
COMPND   7 EC: 3.4.24.56;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: NATRIURETIC PEPTIDES B;                                    
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 103-134;                                      
COMPND  14 SYNONYM: GAMMA-BRAIN NATRIURETIC PEPTIDE;                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HCG_1810909, IDE, RP11-366I13.1-001;                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX-H6;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: NPPB                                                           
KEYWDS    INSULYSIN, INSULINASE, A-BETA DEGRADING ENZYME, CRYPTIDASE,           
KEYWDS   2 HYDROLASE, HORMONE, DISEASE MUTATION, DIABETES MELLITUS, INSULIN,    
KEYWDS   3 CARDIAC, SECRETED, PROTEASE, DISULFIDE BOND, METALLOPROTEASE, HUMAN  
KEYWDS   4 INSULIN-DEGRADNG ENZYME, METAL-BINDING, NATRIURETIC PEPTIDE,         
KEYWDS   5 NATRIURETIC FACTOR, CARDIOVASCULAR REGULATION, HYDROLASE-HORMONE     
KEYWDS   6 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.FUNKE,Q.GUO,W.-J.TANG                                               
REVDAT   2   08-NOV-17 3N56    1       REMARK                                   
REVDAT   1   17-NOV-10 3N56    0                                                
JRNL        AUTH   L.A.RALAT,T.FUNKE,M.REN,Q.GUO,D.M.DICKEY,L.R.POTTER,         
JRNL        AUTH 2 W.-J.TANG                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME (IDE) IN 
JRNL        TITL 2 COMPLEX WITH HUMAN B-TYPE NATRIURETIC PEPTIDE (BNP)          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 62152                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1206                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4642                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.64                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 76                           
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 15572                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.26000                                              
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.88000                                             
REMARK   3    B12 (A**2) : 0.63000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
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): 0.385         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.291         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.517        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15996 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 21641 ; 1.166 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1904 ; 5.375 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   793 ;35.363 ;24.477       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2859 ;18.821 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    82 ;18.483 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2325 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12194 ; 0.005 ; 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):  9552 ; 0.381 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15464 ; 0.728 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  6444 ; 0.725 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6175 ; 1.356 ; 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 : NULL                              
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 3N56 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : SI(111) AND SI(220)-SAGITALLY      
REMARK 200                                   FOCUSED DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62152                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.102                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : 0.20299                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3CWW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEGMME-5000, 10% TACSIMATE, 10%      
REMARK 280  DIOXANE, 100 MM NA-HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.43000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       30.21500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.32250            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       15.10750            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       75.53750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    30                                                      
REMARK 465     HIS A    31                                                      
REMARK 465     HIS A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     HIS A    35                                                      
REMARK 465     HIS A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     MET A    42                                                      
REMARK 465     ASN A    43                                                      
REMARK 465     ASP A   964                                                      
REMARK 465     SER A   965                                                      
REMARK 465     ASN A   966                                                      
REMARK 465     PRO A   967                                                      
REMARK 465     VAL A   968                                                      
REMARK 465     VAL A   969                                                      
REMARK 465     GLY A   970                                                      
REMARK 465     GLU A   971                                                      
REMARK 465     PHE A   972                                                      
REMARK 465     PRO A   973                                                      
REMARK 465     ALA A   974                                                      
REMARK 465     GLN A   975                                                      
REMARK 465     ASN A   976                                                      
REMARK 465     ASP A   977                                                      
REMARK 465     ILE A   978                                                      
REMARK 465     ASN A   979                                                      
REMARK 465     LEU A   980                                                      
REMARK 465     ILE A  1012                                                      
REMARK 465     ASN A  1013                                                      
REMARK 465     PHE A  1014                                                      
REMARK 465     MET A  1015                                                      
REMARK 465     ALA A  1016                                                      
REMARK 465     ALA A  1017                                                      
REMARK 465     LYS A  1018                                                      
REMARK 465     LEU A  1019                                                      
REMARK 465     MET B    30                                                      
REMARK 465     HIS B    31                                                      
REMARK 465     HIS B    32                                                      
REMARK 465     HIS B    33                                                      
REMARK 465     HIS B    34                                                      
REMARK 465     HIS B    35                                                      
REMARK 465     HIS B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     ILE B    40                                                      
REMARK 465     PRO B    41                                                      
REMARK 465     MET B    42                                                      
REMARK 465     ASN B    43                                                      
REMARK 465     ASN B    44                                                      
REMARK 465     ASP B   964                                                      
REMARK 465     SER B   965                                                      
REMARK 465     ASN B   966                                                      
REMARK 465     PRO B   967                                                      
REMARK 465     VAL B   968                                                      
REMARK 465     VAL B   969                                                      
REMARK 465     GLY B   970                                                      
REMARK 465     GLU B   971                                                      
REMARK 465     PHE B   972                                                      
REMARK 465     PRO B   973                                                      
REMARK 465     ALA B   974                                                      
REMARK 465     GLN B   975                                                      
REMARK 465     ASN B   976                                                      
REMARK 465     ASP B   977                                                      
REMARK 465     ILE B   978                                                      
REMARK 465     ASN B   979                                                      
REMARK 465     ILE B  1012                                                      
REMARK 465     ASN B  1013                                                      
REMARK 465     PHE B  1014                                                      
REMARK 465     MET B  1015                                                      
REMARK 465     ALA B  1016                                                      
REMARK 465     ALA B  1017                                                      
REMARK 465     LYS B  1018                                                      
REMARK 465     LEU B  1019                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     VAL C     5                                                      
REMARK 465     GLN C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     CYS C    10                                                      
REMARK 465     PHE C    11                                                      
REMARK 465     GLY C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     LYS C    14                                                      
REMARK 465     MET C    15                                                      
REMARK 465     ASP C    16                                                      
REMARK 465     ARG C    17                                                      
REMARK 465     ILE C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     SER C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     CYS C    26                                                      
REMARK 465     LYS C    27                                                      
REMARK 465     VAL C    28                                                      
REMARK 465     LEU C    29                                                      
REMARK 465     ARG C    30                                                      
REMARK 465     ARG C    31                                                      
REMARK 465     HIS C    32                                                      
REMARK 465     LYS D     3                                                      
REMARK 465     MET D     4                                                      
REMARK 465     VAL D     5                                                      
REMARK 465     GLN D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     SER D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     CYS D    10                                                      
REMARK 465     PHE D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     LYS D    14                                                      
REMARK 465     MET D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     ARG D    17                                                      
REMARK 465     ILE D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     SER D    21                                                      
REMARK 465     SER D    22                                                      
REMARK 465     GLY D    23                                                      
REMARK 465     LEU D    24                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     CYS D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     VAL D    28                                                      
REMARK 465     LEU D    29                                                      
REMARK 465     ARG D    30                                                      
REMARK 465     ARG D    31                                                      
REMARK 465     HIS D    32                                                      
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 542    CG   CD   CE   NZ                                   
REMARK 470     GLU A 543    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 872    CG   CD   CE   NZ                                   
REMARK 470     LYS B 542    CG   CD   CE   NZ                                   
REMARK 470     GLU B 543    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP B   517     O    HOH B  1023              1.79            
REMARK 500   CB   ASP B   517     O    HOH B  1035              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  52     -156.13    -72.19                                   
REMARK 500    HIS A  93       49.23    -79.06                                   
REMARK 500    LEU A 116       33.32    -94.04                                   
REMARK 500    SER A 143     -164.74   -116.40                                   
REMARK 500    HIS A 157       31.35    -99.33                                   
REMARK 500    SER A 171       87.13   -160.94                                   
REMARK 500    GLU A 227      -55.24   -134.36                                   
REMARK 500    ARG A 368      108.94    -56.18                                   
REMARK 500    GLU A 453       32.86    -84.55                                   
REMARK 500    TYR A 454      -49.40   -139.27                                   
REMARK 500    GLU A 457      -68.99   -130.11                                   
REMARK 500    GLU A 543       43.10    -97.04                                   
REMARK 500    TYR A 584       21.96   -140.20                                   
REMARK 500    ILE A 624        0.59    -69.94                                   
REMARK 500    THR A 797      -84.06    -98.96                                   
REMARK 500    PRO A1006     -178.85    -64.50                                   
REMARK 500    ARG B  49      154.30    179.77                                   
REMARK 500    HIS B  53      122.71    -27.91                                   
REMARK 500    GLU B 156       40.60   -109.83                                   
REMARK 500    SER B 171       72.06   -155.73                                   
REMARK 500    PHE B 174       60.74     34.36                                   
REMARK 500    GLU B 227      -65.78   -141.76                                   
REMARK 500    ASN B 329       65.10     66.85                                   
REMARK 500    ARG B 368      103.41    -50.05                                   
REMARK 500    SER B 484        6.64    -69.24                                   
REMARK 500    ALA B 516      102.42    -57.32                                   
REMARK 500    LYS B 566      -54.32   -132.79                                   
REMARK 500    THR B 651       32.49   -141.48                                   
REMARK 500    ASN B 787       53.46    -92.78                                   
REMARK 500    THR B 797      -83.55   -115.70                                   
REMARK 500    MET B 799      150.05    -43.87                                   
REMARK 500    SER B 801      130.88   -175.72                                   
REMARK 500    ARG B 824      -74.21   -106.05                                   
REMARK 500    ASN B 917       67.06   -105.49                                   
REMARK 500    PRO B1006     -177.18    -67.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A2001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE1                                                    
REMARK 620 2 HIS A 112   NE2 108.4                                              
REMARK 620 3 HIS A 108   NE2 107.4 100.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B2002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 189   OE1                                                    
REMARK 620 2 HIS B 112   NE2 101.0                                              
REMARK 620 3 HIS B 108   NE2 106.5  92.2                                        
REMARK 620 N                    1     2                                         
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 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2002                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2G47   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME IN COMPLEX WITH  
REMARK 900 AMYLOID-BETA (1-40)                                                  
REMARK 900 RELATED ID: 2WBY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN INSULIN-DEGRADING ENZYME IN COMPLEX WITH  
REMARK 900 INSULIN                                                              
REMARK 900 RELATED ID: 3CWW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF IDE-BRADYKININ COMPLEX                          
REMARK 900 RELATED ID: 3H44   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF INSULIN DEGRADING ENZYME IN COMPLEX WITH        
REMARK 900 MACROPHAGE INFLAMMATORY PROTEIN 1 ALPHA                              
REMARK 900 RELATED ID: 3E4Z   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN INSULIN DEGRADING ENZYME IN COMPLEX WITH  
REMARK 900 INSULIN-LIKE GROWTH FACTOR II                                        
REMARK 900 RELATED ID: 1YK1   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF NATRIURETIC PEPTIDE RECEPTOR-C COMPLEXED WITH BRAIN     
REMARK 900 NATRIURETIC PEPTIDE                                                  
REMARK 900 RELATED ID: 3N57   RELATED DB: PDB                                   
DBREF  3N56 A   42  1019  UNP    P14735   IDE_HUMAN       42   1019             
DBREF  3N56 B   42  1019  UNP    P14735   IDE_HUMAN       42   1019             
DBREF  3N56 C    1    32  UNP    P16860   ANFB_HUMAN     103    134             
DBREF  3N56 D    1    32  UNP    P16860   ANFB_HUMAN     103    134             
SEQADV 3N56 MET A   30  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   31  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   32  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   33  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   34  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   35  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS A   36  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ALA A   37  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ALA A   38  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 GLY A   39  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ILE A   40  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 PRO A   41  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 LEU A  110  UNP  P14735    CYS   110 ENGINEERED MUTATION            
SEQADV 3N56 GLN A  111  UNP  P14735    GLU   111 ENGINEERED MUTATION            
SEQADV 3N56 SER A  171  UNP  P14735    CYS   171 ENGINEERED MUTATION            
SEQADV 3N56 ALA A  178  UNP  P14735    CYS   178 ENGINEERED MUTATION            
SEQADV 3N56 VAL A  257  UNP  P14735    CYS   257 ENGINEERED MUTATION            
SEQADV 3N56 LEU A  414  UNP  P14735    CYS   414 ENGINEERED MUTATION            
SEQADV 3N56 ASN A  573  UNP  P14735    CYS   573 ENGINEERED MUTATION            
SEQADV 3N56 SER A  590  UNP  P14735    CYS   590 ENGINEERED MUTATION            
SEQADV 3N56 SER A  789  UNP  P14735    CYS   789 ENGINEERED MUTATION            
SEQADV 3N56 ALA A  812  UNP  P14735    CYS   812 ENGINEERED MUTATION            
SEQADV 3N56 ALA A  819  UNP  P14735    CYS   819 ENGINEERED MUTATION            
SEQADV 3N56 SER A  904  UNP  P14735    CYS   904 ENGINEERED MUTATION            
SEQADV 3N56 ASN A  966  UNP  P14735    CYS   966 ENGINEERED MUTATION            
SEQADV 3N56 ALA A  974  UNP  P14735    CYS   974 ENGINEERED MUTATION            
SEQADV 3N56 MET B   30  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   31  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   32  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   33  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   34  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   35  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 HIS B   36  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ALA B   37  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ALA B   38  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 GLY B   39  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 ILE B   40  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 PRO B   41  UNP  P14735              EXPRESSION TAG                 
SEQADV 3N56 LEU B  110  UNP  P14735    CYS   110 ENGINEERED MUTATION            
SEQADV 3N56 GLN B  111  UNP  P14735    GLU   111 ENGINEERED MUTATION            
SEQADV 3N56 SER B  171  UNP  P14735    CYS   171 ENGINEERED MUTATION            
SEQADV 3N56 ALA B  178  UNP  P14735    CYS   178 ENGINEERED MUTATION            
SEQADV 3N56 VAL B  257  UNP  P14735    CYS   257 ENGINEERED MUTATION            
SEQADV 3N56 LEU B  414  UNP  P14735    CYS   414 ENGINEERED MUTATION            
SEQADV 3N56 ASN B  573  UNP  P14735    CYS   573 ENGINEERED MUTATION            
SEQADV 3N56 SER B  590  UNP  P14735    CYS   590 ENGINEERED MUTATION            
SEQADV 3N56 SER B  789  UNP  P14735    CYS   789 ENGINEERED MUTATION            
SEQADV 3N56 ALA B  812  UNP  P14735    CYS   812 ENGINEERED MUTATION            
SEQADV 3N56 ALA B  819  UNP  P14735    CYS   819 ENGINEERED MUTATION            
SEQADV 3N56 SER B  904  UNP  P14735    CYS   904 ENGINEERED MUTATION            
SEQADV 3N56 ASN B  966  UNP  P14735    CYS   966 ENGINEERED MUTATION            
SEQADV 3N56 ALA B  974  UNP  P14735    CYS   974 ENGINEERED MUTATION            
SEQRES   1 A  990  MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET          
SEQRES   2 A  990  ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR          
SEQRES   3 A  990  LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU          
SEQRES   4 A  990  LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO          
SEQRES   5 A  990  THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE          
SEQRES   6 A  990  GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER          
SEQRES   7 A  990  HIS PHE LEU GLN HIS MET LEU PHE LEU GLY THR LYS LYS          
SEQRES   8 A  990  TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU          
SEQRES   9 A  990  HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS          
SEQRES  10 A  990  THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU          
SEQRES  11 A  990  GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU SER PRO          
SEQRES  12 A  990  LEU PHE ASP GLU SER ALA LYS ASP ARG GLU VAL ASN ALA          
SEQRES  13 A  990  VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA          
SEQRES  14 A  990  TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO          
SEQRES  15 A  990  LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR          
SEQRES  16 A  990  THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL          
SEQRES  17 A  990  ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER          
SEQRES  18 A  990  SER ASN LEU MET ALA VAL VAL VAL LEU GLY ARG GLU SER          
SEQRES  19 A  990  LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER          
SEQRES  20 A  990  GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO          
SEQRES  21 A  990  GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR          
SEQRES  22 A  990  LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL          
SEQRES  23 A  990  THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER          
SEQRES  24 A  990  ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU          
SEQRES  25 A  990  GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY          
SEQRES  26 A  990  TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA          
SEQRES  27 A  990  ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR          
SEQRES  28 A  990  GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS          
SEQRES  29 A  990  MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO          
SEQRES  30 A  990  GLN GLU TRP VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA          
SEQRES  31 A  990  VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY          
SEQRES  32 A  990  TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO          
SEQRES  33 A  990  LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU          
SEQRES  34 A  990  PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU          
SEQRES  35 A  990  ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER          
SEQRES  36 A  990  PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY          
SEQRES  37 A  990  THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE          
SEQRES  38 A  990  LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS          
SEQRES  39 A  990  LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU          
SEQRES  40 A  990  ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA          
SEQRES  41 A  990  LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS          
SEQRES  42 A  990  GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN          
SEQRES  43 A  990  PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU          
SEQRES  44 A  990  HIS SER ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS          
SEQRES  45 A  990  ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA          
SEQRES  46 A  990  GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET          
SEQRES  47 A  990  TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE          
SEQRES  48 A  990  LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU          
SEQRES  49 A  990  ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR          
SEQRES  50 A  990  MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS          
SEQRES  51 A  990  GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU          
SEQRES  52 A  990  VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP          
SEQRES  53 A  990  ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN          
SEQRES  54 A  990  LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY          
SEQRES  55 A  990  ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET          
SEQRES  56 A  990  VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO          
SEQRES  57 A  990  LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN          
SEQRES  58 A  990  LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN          
SEQRES  59 A  990  GLU VAL HIS ASN ASN SER GLY ILE GLU ILE TYR TYR GLN          
SEQRES  60 A  990  THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU          
SEQRES  61 A  990  LEU PHE ALA GLN ILE ILE SER GLU PRO ALA PHE ASN THR          
SEQRES  62 A  990  LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER          
SEQRES  63 A  990  GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE          
SEQRES  64 A  990  ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER          
SEQRES  65 A  990  ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE          
SEQRES  66 A  990  GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN          
SEQRES  67 A  990  ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU          
SEQRES  68 A  990  SER ALA GLU SER ALA LYS TYR TRP GLY GLU ILE ILE SER          
SEQRES  69 A  990  GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA          
SEQRES  70 A  990  TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE          
SEQRES  71 A  990  TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS          
SEQRES  72 A  990  LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER          
SEQRES  73 A  990  ASN PRO VAL VAL GLY GLU PHE PRO ALA GLN ASN ASP ILE          
SEQRES  74 A  990  ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL          
SEQRES  75 A  990  ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU          
SEQRES  76 A  990  PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA          
SEQRES  77 A  990  LYS LEU                                                      
SEQRES   1 B  990  MET HIS HIS HIS HIS HIS HIS ALA ALA GLY ILE PRO MET          
SEQRES   2 B  990  ASN ASN PRO ALA ILE LYS ARG ILE GLY ASN HIS ILE THR          
SEQRES   3 B  990  LYS SER PRO GLU ASP LYS ARG GLU TYR ARG GLY LEU GLU          
SEQRES   4 B  990  LEU ALA ASN GLY ILE LYS VAL LEU LEU ILE SER ASP PRO          
SEQRES   5 B  990  THR THR ASP LYS SER SER ALA ALA LEU ASP VAL HIS ILE          
SEQRES   6 B  990  GLY SER LEU SER ASP PRO PRO ASN ILE ALA GLY LEU SER          
SEQRES   7 B  990  HIS PHE LEU GLN HIS MET LEU PHE LEU GLY THR LYS LYS          
SEQRES   8 B  990  TYR PRO LYS GLU ASN GLU TYR SER GLN PHE LEU SER GLU          
SEQRES   9 B  990  HIS ALA GLY SER SER ASN ALA PHE THR SER GLY GLU HIS          
SEQRES  10 B  990  THR ASN TYR TYR PHE ASP VAL SER HIS GLU HIS LEU GLU          
SEQRES  11 B  990  GLY ALA LEU ASP ARG PHE ALA GLN PHE PHE LEU SER PRO          
SEQRES  12 B  990  LEU PHE ASP GLU SER ALA LYS ASP ARG GLU VAL ASN ALA          
SEQRES  13 B  990  VAL ASP SER GLU HIS GLU LYS ASN VAL MET ASN ASP ALA          
SEQRES  14 B  990  TRP ARG LEU PHE GLN LEU GLU LYS ALA THR GLY ASN PRO          
SEQRES  15 B  990  LYS HIS PRO PHE SER LYS PHE GLY THR GLY ASN LYS TYR          
SEQRES  16 B  990  THR LEU GLU THR ARG PRO ASN GLN GLU GLY ILE ASP VAL          
SEQRES  17 B  990  ARG GLN GLU LEU LEU LYS PHE HIS SER ALA TYR TYR SER          
SEQRES  18 B  990  SER ASN LEU MET ALA VAL VAL VAL LEU GLY ARG GLU SER          
SEQRES  19 B  990  LEU ASP ASP LEU THR ASN LEU VAL VAL LYS LEU PHE SER          
SEQRES  20 B  990  GLU VAL GLU ASN LYS ASN VAL PRO LEU PRO GLU PHE PRO          
SEQRES  21 B  990  GLU HIS PRO PHE GLN GLU GLU HIS LEU LYS GLN LEU TYR          
SEQRES  22 B  990  LYS ILE VAL PRO ILE LYS ASP ILE ARG ASN LEU TYR VAL          
SEQRES  23 B  990  THR PHE PRO ILE PRO ASP LEU GLN LYS TYR TYR LYS SER          
SEQRES  24 B  990  ASN PRO GLY HIS TYR LEU GLY HIS LEU ILE GLY HIS GLU          
SEQRES  25 B  990  GLY PRO GLY SER LEU LEU SER GLU LEU LYS SER LYS GLY          
SEQRES  26 B  990  TRP VAL ASN THR LEU VAL GLY GLY GLN LYS GLU GLY ALA          
SEQRES  27 B  990  ARG GLY PHE MET PHE PHE ILE ILE ASN VAL ASP LEU THR          
SEQRES  28 B  990  GLU GLU GLY LEU LEU HIS VAL GLU ASP ILE ILE LEU HIS          
SEQRES  29 B  990  MET PHE GLN TYR ILE GLN LYS LEU ARG ALA GLU GLY PRO          
SEQRES  30 B  990  GLN GLU TRP VAL PHE GLN GLU LEU LYS ASP LEU ASN ALA          
SEQRES  31 B  990  VAL ALA PHE ARG PHE LYS ASP LYS GLU ARG PRO ARG GLY          
SEQRES  32 B  990  TYR THR SER LYS ILE ALA GLY ILE LEU HIS TYR TYR PRO          
SEQRES  33 B  990  LEU GLU GLU VAL LEU THR ALA GLU TYR LEU LEU GLU GLU          
SEQRES  34 B  990  PHE ARG PRO ASP LEU ILE GLU MET VAL LEU ASP LYS LEU          
SEQRES  35 B  990  ARG PRO GLU ASN VAL ARG VAL ALA ILE VAL SER LYS SER          
SEQRES  36 B  990  PHE GLU GLY LYS THR ASP ARG THR GLU GLU TRP TYR GLY          
SEQRES  37 B  990  THR GLN TYR LYS GLN GLU ALA ILE PRO ASP GLU VAL ILE          
SEQRES  38 B  990  LYS LYS TRP GLN ASN ALA ASP LEU ASN GLY LYS PHE LYS          
SEQRES  39 B  990  LEU PRO THR LYS ASN GLU PHE ILE PRO THR ASN PHE GLU          
SEQRES  40 B  990  ILE LEU PRO LEU GLU LYS GLU ALA THR PRO TYR PRO ALA          
SEQRES  41 B  990  LEU ILE LYS ASP THR ALA MET SER LYS LEU TRP PHE LYS          
SEQRES  42 B  990  GLN ASP ASP LYS PHE PHE LEU PRO LYS ALA ASN LEU ASN          
SEQRES  43 B  990  PHE GLU PHE PHE SER PRO PHE ALA TYR VAL ASP PRO LEU          
SEQRES  44 B  990  HIS SER ASN MET ALA TYR LEU TYR LEU GLU LEU LEU LYS          
SEQRES  45 B  990  ASP SER LEU ASN GLU TYR ALA TYR ALA ALA GLU LEU ALA          
SEQRES  46 B  990  GLY LEU SER TYR ASP LEU GLN ASN THR ILE TYR GLY MET          
SEQRES  47 B  990  TYR LEU SER VAL LYS GLY TYR ASN ASP LYS GLN PRO ILE          
SEQRES  48 B  990  LEU LEU LYS LYS ILE ILE GLU LYS MET ALA THR PHE GLU          
SEQRES  49 B  990  ILE ASP GLU LYS ARG PHE GLU ILE ILE LYS GLU ALA TYR          
SEQRES  50 B  990  MET ARG SER LEU ASN ASN PHE ARG ALA GLU GLN PRO HIS          
SEQRES  51 B  990  GLN HIS ALA MET TYR TYR LEU ARG LEU LEU MET THR GLU          
SEQRES  52 B  990  VAL ALA TRP THR LYS ASP GLU LEU LYS GLU ALA LEU ASP          
SEQRES  53 B  990  ASP VAL THR LEU PRO ARG LEU LYS ALA PHE ILE PRO GLN          
SEQRES  54 B  990  LEU LEU SER ARG LEU HIS ILE GLU ALA LEU LEU HIS GLY          
SEQRES  55 B  990  ASN ILE THR LYS GLN ALA ALA LEU GLY ILE MET GLN MET          
SEQRES  56 B  990  VAL GLU ASP THR LEU ILE GLU HIS ALA HIS THR LYS PRO          
SEQRES  57 B  990  LEU LEU PRO SER GLN LEU VAL ARG TYR ARG GLU VAL GLN          
SEQRES  58 B  990  LEU PRO ASP ARG GLY TRP PHE VAL TYR GLN GLN ARG ASN          
SEQRES  59 B  990  GLU VAL HIS ASN ASN SER GLY ILE GLU ILE TYR TYR GLN          
SEQRES  60 B  990  THR ASP MET GLN SER THR SER GLU ASN MET PHE LEU GLU          
SEQRES  61 B  990  LEU PHE ALA GLN ILE ILE SER GLU PRO ALA PHE ASN THR          
SEQRES  62 B  990  LEU ARG THR LYS GLU GLN LEU GLY TYR ILE VAL PHE SER          
SEQRES  63 B  990  GLY PRO ARG ARG ALA ASN GLY ILE GLN GLY LEU ARG PHE          
SEQRES  64 B  990  ILE ILE GLN SER GLU LYS PRO PRO HIS TYR LEU GLU SER          
SEQRES  65 B  990  ARG VAL GLU ALA PHE LEU ILE THR MET GLU LYS SER ILE          
SEQRES  66 B  990  GLU ASP MET THR GLU GLU ALA PHE GLN LYS HIS ILE GLN          
SEQRES  67 B  990  ALA LEU ALA ILE ARG ARG LEU ASP LYS PRO LYS LYS LEU          
SEQRES  68 B  990  SER ALA GLU SER ALA LYS TYR TRP GLY GLU ILE ILE SER          
SEQRES  69 B  990  GLN GLN TYR ASN PHE ASP ARG ASP ASN THR GLU VAL ALA          
SEQRES  70 B  990  TYR LEU LYS THR LEU THR LYS GLU ASP ILE ILE LYS PHE          
SEQRES  71 B  990  TYR LYS GLU MET LEU ALA VAL ASP ALA PRO ARG ARG HIS          
SEQRES  72 B  990  LYS VAL SER VAL HIS VAL LEU ALA ARG GLU MET ASP SER          
SEQRES  73 B  990  ASN PRO VAL VAL GLY GLU PHE PRO ALA GLN ASN ASP ILE          
SEQRES  74 B  990  ASN LEU SER GLN ALA PRO ALA LEU PRO GLN PRO GLU VAL          
SEQRES  75 B  990  ILE GLN ASN MET THR GLU PHE LYS ARG GLY LEU PRO LEU          
SEQRES  76 B  990  PHE PRO LEU VAL LYS PRO HIS ILE ASN PHE MET ALA ALA          
SEQRES  77 B  990  LYS LEU                                                      
SEQRES   1 C   32  SER PRO LYS MET VAL GLN GLY SER GLY CYS PHE GLY ARG          
SEQRES   2 C   32  LYS MET ASP ARG ILE SER SER SER SER GLY LEU GLY CYS          
SEQRES   3 C   32  LYS VAL LEU ARG ARG HIS                                      
SEQRES   1 D   32  SER PRO LYS MET VAL GLN GLY SER GLY CYS PHE GLY ARG          
SEQRES   2 D   32  LYS MET ASP ARG ILE SER SER SER SER GLY LEU GLY CYS          
SEQRES   3 D   32  LYS VAL LEU ARG ARG HIS                                      
HET     ZN  A2001       1                                                       
HET    DIO  A4001       6                                                       
HET    DIO  B4006       6                                                       
HET     ZN  B2002       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   6  DIO    2(C4 H8 O2)                                                  
FORMUL   9  HOH   *54(H2 O)                                                     
HELIX    1   1 GLY A   95  ASP A   99  5                                   5    
HELIX    2   2 GLY A  105  LEU A  114  1                                  10    
HELIX    3   3 PHE A  115  GLY A  117  5                                   3    
HELIX    4   4 ASN A  125  HIS A  134  1                                  10    
HELIX    5   5 HIS A  157  GLN A  167  1                                  11    
HELIX    6   6 PHE A  168  LEU A  170  5                                   3    
HELIX    7   7 ASP A  175  MET A  195  1                                  21    
HELIX    8   8 ASN A  196  THR A  208  1                                  13    
HELIX    9   9 HIS A  213  LYS A  217  5                                   5    
HELIX   10  10 ASN A  222  GLU A  227  1                                   6    
HELIX   11  11 GLU A  227  GLY A  234  1                                   8    
HELIX   12  12 ASP A  236  TYR A  249  1                                  14    
HELIX   13  13 SER A  250  ASN A  252  5                                   3    
HELIX   14  14 SER A  263  SER A  276  1                                  14    
HELIX   15  15 GLN A  294  LEU A  298  5                                   5    
HELIX   16  16 ASP A  321  TYR A  326  5                                   6    
HELIX   17  17 ASN A  329  GLY A  339  1                                  11    
HELIX   18  18 SER A  345  LYS A  353  1                                   9    
HELIX   19  19 THR A  380  HIS A  386  1                                   7    
HELIX   20  20 HIS A  386  GLY A  405  1                                  20    
HELIX   21  21 GLN A  407  PHE A  424  1                                  18    
HELIX   22  22 ARG A  429  LEU A  441  1                                  13    
HELIX   23  23 PRO A  445  GLU A  447  5                                   3    
HELIX   24  24 GLU A  448  GLU A  453  1                                   6    
HELIX   25  25 ARG A  460  ASP A  469  1                                  10    
HELIX   26  26 LYS A  470  LEU A  471  5                                   2    
HELIX   27  27 ARG A  472  ASN A  475  5                                   4    
HELIX   28  28 LYS A  483  GLU A  486  5                                   4    
HELIX   29  29 PRO A  506  ASN A  515  1                                  10    
HELIX   30  30 PRO A  581  TYR A  584  5                                   4    
HELIX   31  31 ASP A  586  ALA A  614  1                                  29    
HELIX   32  32 LYS A  637  THR A  651  1                                  15    
HELIX   33  33 ASP A  655  ASN A  672  1                                  18    
HELIX   34  34 PHE A  673  GLU A  676  5                                   4    
HELIX   35  35 GLN A  677  THR A  691  1                                  15    
HELIX   36  36 THR A  696  LEU A  704  1                                   9    
HELIX   37  37 ASP A  705  VAL A  707  5                                   3    
HELIX   38  38 THR A  708  SER A  721  1                                  14    
HELIX   39  39 THR A  734  HIS A  754  1                                  21    
HELIX   40  40 LEU A  759  LEU A  763  5                                   5    
HELIX   41  41 SER A  801  ARG A  824  1                                  24    
HELIX   42  42 PRO A  855  ASP A  876  1                                  22    
HELIX   43  43 THR A  878  LEU A  894  1                                  17    
HELIX   44  44 LYS A  899  SER A  913  1                                  15    
HELIX   45  45 ASP A  919  LEU A  931  1                                  13    
HELIX   46  46 THR A  932  LEU A  944  1                                  13    
HELIX   47  47 ASN A  994  GLY A 1001  1                                   8    
HELIX   48  48 GLY B   95  ASP B   99  5                                   5    
HELIX   49  49 GLY B  105  LEU B  114  1                                  10    
HELIX   50  50 PHE B  115  GLY B  117  5                                   3    
HELIX   51  51 ASN B  125  GLU B  133  1                                   9    
HELIX   52  52 HIS B  157  GLN B  167  1                                  11    
HELIX   53  53 PHE B  168  LEU B  170  5                                   3    
HELIX   54  54 ASP B  175  MET B  195  1                                  21    
HELIX   55  55 ASN B  196  THR B  208  1                                  13    
HELIX   56  56 HIS B  213  LYS B  217  5                                   5    
HELIX   57  57 ASN B  222  GLU B  227  1                                   6    
HELIX   58  58 GLU B  227  GLU B  233  1                                   7    
HELIX   59  59 ASP B  236  TYR B  249  1                                  14    
HELIX   60  60 SER B  250  ASN B  252  5                                   3    
HELIX   61  61 SER B  263  SER B  276  1                                  14    
HELIX   62  62 GLN B  294  LEU B  298  5                                   5    
HELIX   63  63 LEU B  322  TYR B  326  5                                   5    
HELIX   64  64 ASN B  329  GLY B  339  1                                  11    
HELIX   65  65 SER B  345  LYS B  353  1                                   9    
HELIX   66  66 THR B  380  LEU B  385  1                                   6    
HELIX   67  67 HIS B  386  GLY B  405  1                                  20    
HELIX   68  68 GLN B  407  PHE B  424  1                                  18    
HELIX   69  69 ARG B  429  LEU B  441  1                                  13    
HELIX   70  70 PRO B  445  VAL B  449  5                                   5    
HELIX   71  71 ARG B  460  ASP B  469  1                                  10    
HELIX   72  72 LYS B  470  LEU B  471  5                                   2    
HELIX   73  73 ARG B  472  ASN B  475  5                                   4    
HELIX   74  74 LYS B  483  GLU B  486  5                                   4    
HELIX   75  75 PRO B  506  ASN B  515  1                                  10    
HELIX   76  76 PRO B  581  TYR B  584  5                                   4    
HELIX   77  77 ASP B  586  ALA B  614  1                                  29    
HELIX   78  78 LYS B  637  THR B  651  1                                  15    
HELIX   79  79 ASP B  655  ASN B  672  1                                  18    
HELIX   80  80 PHE B  673  GLU B  676  5                                   4    
HELIX   81  81 GLN B  677  THR B  691  1                                  15    
HELIX   82  82 THR B  696  ASP B  705  1                                  10    
HELIX   83  83 THR B  708  SER B  721  1                                  14    
HELIX   84  84 THR B  734  HIS B  754  1                                  21    
HELIX   85  85 LEU B  759  LEU B  763  5                                   5    
HELIX   86  86 SER B  801  ILE B  815  1                                  15    
HELIX   87  87 ILE B  815  ARG B  824  1                                  10    
HELIX   88  88 PRO B  855  ASP B  876  1                                  22    
HELIX   89  89 THR B  878  ASP B  895  1                                  18    
HELIX   90  90 LYS B  899  SER B  913  1                                  15    
HELIX   91  91 ASP B  919  LYS B  929  1                                  11    
HELIX   92  92 THR B  932  LEU B  944  1                                  13    
HELIX   93  93 ASN B  994  GLY B 1001  1                                   8    
SHEET    1   A 7 ILE A  47  ILE A  50  0                                        
SHEET    2   A 7 GLU A  63  LEU A  69 -1  O  GLU A  68   N  LYS A  48           
SHEET    3   A 7 LYS A  74  SER A  79 -1  O  SER A  79   N  GLU A  63           
SHEET    4   A 7 MET A 254  GLY A 260  1  O  VAL A 256   N  LYS A  74           
SHEET    5   A 7 LYS A  85  VAL A  92 -1  N  SER A  87   O  LEU A 259           
SHEET    6   A 7 THR A 147  SER A 154 -1  O  THR A 147   N  VAL A  92           
SHEET    7   A 7 SER A 137  THR A 142 -1  N  ASN A 139   O  TYR A 150           
SHEET    1   B 7 LEU A 359  ALA A 367  0                                        
SHEET    2   B 7 PHE A 370  ASP A 378 -1  O  ASN A 376   N  VAL A 360           
SHEET    3   B 7 ASN A 312  ILE A 319 -1  N  LEU A 313   O  VAL A 377           
SHEET    4   B 7 ARG A 477  VAL A 481 -1  O  ALA A 479   N  TYR A 314           
SHEET    5   B 7 GLN A 300  ILE A 304  1  N  TYR A 302   O  ILE A 480           
SHEET    6   B 7 GLN A 499  ALA A 504 -1  O  GLU A 503   N  LEU A 301           
SHEET    7   B 7 ARG A 491  THR A 492 -1  N  ARG A 491   O  TYR A 500           
SHEET    1   C 6 ALA A 549  ASP A 553  0                                        
SHEET    2   C 6 SER A 557  GLN A 563 -1  O  PHE A 561   N  ALA A 549           
SHEET    3   C 6 HIS A 724  GLY A 731  1  O  ALA A 727   N  TRP A 560           
SHEET    4   C 6 LYS A 571  PHE A 579 -1  N  ASN A 573   O  HIS A 730           
SHEET    5   C 6 GLY A 626  TYR A 634 -1  O  MET A 627   N  PHE A 578           
SHEET    6   C 6 LEU A 616  THR A 623 -1  N  SER A 617   O  LYS A 632           
SHEET    1   D 6 VAL A 833  ALA A 840  0                                        
SHEET    2   D 6 ILE A 843  SER A 852 -1  O  ILE A 849   N  PHE A 834           
SHEET    3   D 6 SER A 789  MET A 799 -1  N  SER A 789   O  SER A 852           
SHEET    4   D 6 LYS A 953  LEU A 959 -1  O  VAL A 958   N  GLY A 790           
SHEET    5   D 6 TRP A 776  ARG A 782  1  N  PHE A 777   O  SER A 955           
SHEET    6   D 6 GLU A 990  VAL A 991  1  O  GLU A 990   N  TRP A 776           
SHEET    1   E 7 ILE B  47  ILE B  50  0                                        
SHEET    2   E 7 GLU B  63  LEU B  69 -1  O  GLU B  68   N  LYS B  48           
SHEET    3   E 7 LYS B  74  SER B  79 -1  O  SER B  79   N  GLU B  63           
SHEET    4   E 7 MET B 254  GLY B 260  1  O  VAL B 258   N  ILE B  78           
SHEET    5   E 7 LYS B  85  VAL B  92 -1  N  SER B  87   O  LEU B 259           
SHEET    6   E 7 THR B 147  SER B 154 -1  O  VAL B 153   N  SER B  86           
SHEET    7   E 7 SER B 137  THR B 142 -1  N  ASN B 139   O  TYR B 150           
SHEET    1   F 7 LEU B 359  ALA B 367  0                                        
SHEET    2   F 7 PHE B 370  ASP B 378 -1  O  ILE B 374   N  GLY B 362           
SHEET    3   F 7 ASN B 312  PRO B 320 -1  N  LEU B 313   O  VAL B 377           
SHEET    4   F 7 ARG B 477  VAL B 481 -1  O  VAL B 481   N  ASN B 312           
SHEET    5   F 7 GLN B 300  VAL B 305  1  N  TYR B 302   O  ILE B 480           
SHEET    6   F 7 GLN B 499  ALA B 504 -1  O  GLN B 499   N  VAL B 305           
SHEET    7   F 7 ARG B 491  THR B 492 -1  N  ARG B 491   O  TYR B 500           
SHEET    1   G 6 ALA B 549  ASP B 553  0                                        
SHEET    2   G 6 SER B 557  GLN B 563 -1  O  PHE B 561   N  ALA B 549           
SHEET    3   G 6 HIS B 724  GLY B 731  1  O  ALA B 727   N  TRP B 560           
SHEET    4   G 6 LYS B 571  PHE B 579 -1  N  GLU B 577   O  GLU B 726           
SHEET    5   G 6 GLY B 626  TYR B 634 -1  O  MET B 627   N  PHE B 578           
SHEET    6   G 6 LEU B 616  THR B 623 -1  N  THR B 623   O  GLY B 626           
SHEET    1   H 6 VAL B 833  ALA B 840  0                                        
SHEET    2   H 6 ILE B 843  SER B 852 -1  O  ILE B 849   N  PHE B 834           
SHEET    3   H 6 SER B 789  GLN B 796 -1  N  TYR B 795   O  LEU B 846           
SHEET    4   H 6 HIS B 952  LEU B 959 -1  O  VAL B 954   N  TYR B 794           
SHEET    5   H 6 TRP B 776  ARG B 782  1  N  TYR B 779   O  HIS B 957           
SHEET    6   H 6 GLU B 990  ILE B 992  1  O  GLU B 990   N  TRP B 776           
LINK         OE1 GLU A 189                ZN    ZN A2001     1555   1555  1.86  
LINK         NE2 HIS A 112                ZN    ZN A2001     1555   1555  1.96  
LINK         OE1 GLU B 189                ZN    ZN B2002     1555   1555  2.04  
LINK         NE2 HIS B 112                ZN    ZN B2002     1555   1555  2.04  
LINK         NE2 HIS B 108                ZN    ZN B2002     1555   1555  2.05  
LINK         NE2 HIS A 108                ZN    ZN A2001     1555   1555  2.13  
SITE     1 AC1  3 HIS A 108  HIS A 112  GLU A 189                               
SITE     1 AC2  2 GLU A 205  ARG A 477                                          
SITE     1 AC3  3 GLU B 205  ARG B 477  ALA B 479                               
SITE     1 AC4  3 HIS B 108  HIS B 112  GLU B 189                               
CRYST1  264.036  264.036   90.645  90.00  90.00 120.00 P 65         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.003787  0.002187  0.000000        0.00000                         
SCALE2      0.000000  0.004373  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011032        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system