GenomeNet

Database: PDB
Entry: 4QIA
LinkDB: 4QIA
Original site: 4QIA 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-MAY-14   4QIA              
TITLE     CRYSTAL STRUCTURE OF HUMAN INSULIN DEGRADING ENZYME (IDE) IN COMPLEX  
TITLE    2 WITH INHIBITOR N-BENZYL-N-(CARBOXYMETHYL)GLYCYL-L-HISTIDINE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN-DEGRADING ENZYME;                                  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ABETA-DEGRADING PROTEASE, INSULIN PROTEASE, INSULINASE,     
COMPND   5 INSULYSIN;                                                           
COMPND   6 EC: 3.4.24.56;                                                       
COMPND   7 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: IDE;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX, INHIBITOR:41371                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.GUO,R.DEPREZ-POULAIN,B.DEPREZ,W.J.TANG                              
REVDAT   3   28-FEB-24 4QIA    1       REMARK SEQADV LINK                       
REVDAT   2   17-JUN-15 4QIA    1       JRNL                                     
REVDAT   1   13-MAY-15 4QIA    0                                                
JRNL        AUTH   J.CHARTON,M.GAURIOT,J.TOTOBENAZARA,N.HENNUYER,J.DUMONT,      
JRNL        AUTH 2 D.BOSC,X.MARECHAL,J.ELBAKALI,A.HERLEDAN,X.WEN,C.RONCO,       
JRNL        AUTH 3 H.GRAS-MASSE,A.HENINOT,V.POTTIEZ,V.LANDRY,B.STAELS,          
JRNL        AUTH 4 W.G.LIANG,F.LEROUX,W.J.TANG,B.DEPREZ,R.DEPREZ-POULAIN        
JRNL        TITL   STRUCTURE-ACTIVITY RELATIONSHIPS OF IMIDAZOLE-DERIVED        
JRNL        TITL 2 2-[N-CARBAMOYLMETHYL-ALKYLAMINO]ACETIC ACIDS, DUAL BINDERS   
JRNL        TITL 3 OF HUMAN INSULIN-DEGRADING ENZYME.                           
JRNL        REF    EUR.J.MED.CHEM.               V.  90   547 2015              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   25489670                                                     
JRNL        DOI    10.1016/J.EJMECH.2014.12.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.45                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 56451                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.540                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1999                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 45.4555 -  7.7047    0.91     3891   147  0.1441 0.1444        
REMARK   3     2  7.7047 -  6.1202    0.94     3905   143  0.1771 0.2024        
REMARK   3     3  6.1202 -  5.3480    0.94     3897   139  0.1839 0.2204        
REMARK   3     4  5.3480 -  4.8596    0.94     3884   143  0.1556 0.1999        
REMARK   3     5  4.8596 -  4.5116    0.94     3851   143  0.1450 0.1751        
REMARK   3     6  4.5116 -  4.2458    0.94     3917   137  0.1604 0.2050        
REMARK   3     7  4.2458 -  4.0333    0.95     3901   139  0.1738 0.2304        
REMARK   3     8  4.0333 -  3.8579    0.95     3923   141  0.1886 0.2639        
REMARK   3     9  3.8579 -  3.7094    0.96     3942   146  0.1905 0.2656        
REMARK   3    10  3.7094 -  3.5815    0.96     3897   148  0.1955 0.2276        
REMARK   3    11  3.5815 -  3.4695    0.96     3915   149  0.2087 0.2925        
REMARK   3    12  3.4695 -  3.3704    0.96     3930   140  0.2246 0.2794        
REMARK   3    13  3.3704 -  3.2817    0.96     3944   148  0.2404 0.2932        
REMARK   3    14  3.2817 -  3.2016    0.89     3655   136  0.2727 0.3761        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          16017                                  
REMARK   3   ANGLE     :  0.819          21663                                  
REMARK   3   CHIRALITY :  0.032           2324                                  
REMARK   3   PLANARITY :  0.004           2809                                  
REMARK   3   DIHEDRAL  : 14.892           6064                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  72.8403 -78.6871  35.3371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4227 T22:   0.4513                                     
REMARK   3      T33:   0.3497 T12:  -0.0308                                     
REMARK   3      T13:  -0.0396 T23:  -0.0635                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4162 L22:   0.1988                                     
REMARK   3      L33:   0.1827 L12:   0.1961                                     
REMARK   3      L13:  -0.2885 L23:  -0.2181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0133 S12:   0.0141 S13:   0.0279                       
REMARK   3      S21:   0.0296 S22:  -0.0002 S23:   0.0116                       
REMARK   3      S31:  -0.0103 S32:  -0.0717 S33:  -0.0102                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4QIA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086089.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56516                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.600                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-13% PEG MME 5000, 100 MM HEPES PH     
REMARK 280  7.0, 4-14% TACSIMATE, 10% DIOXANE, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 287K                                                    
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       60.36200            
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       30.18100            
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       45.27150            
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       15.09050            
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       75.45250            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     THR A   797                                                      
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     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     THR B   797                                                      
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     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 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     HIS A1011    O                                                   
REMARK 470     LYS B 542    CG   CD   CE   NZ                                   
REMARK 470     GLU B 543    CG   CD   OE1  OE2                                  
REMARK 470     HIS B1011    O                                                   
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    GLU A 784       -6.22     86.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     33K B 1101                                                       
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 A1102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 108   NE2                                                    
REMARK 620 2 HIS A 112   NE2  84.1                                              
REMARK 620 3 GLU A 189   OE1  93.9  83.7                                        
REMARK 620 4 GLU A 189   OE2  92.1 137.4  54.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 108   NE2                                                    
REMARK 620 2 HIS B 112   NE2  87.7                                              
REMARK 620 3 GLU B 189   OE1  92.0  93.0                                        
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 33K A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 33K B 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1102                 
DBREF  4QIA A   42  1019  UNP    P14735   IDE_HUMAN       42   1019             
DBREF  4QIA B   42  1019  UNP    P14735   IDE_HUMAN       42   1019             
SEQADV 4QIA MET A   30  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   31  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   32  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   33  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   34  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   35  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS A   36  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ALA A   37  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ALA A   38  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA GLY A   39  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ILE A   40  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA PRO A   41  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA LEU A  110  UNP  P14735    CYS   110 ENGINEERED MUTATION            
SEQADV 4QIA GLN A  111  UNP  P14735    GLU   111 ENGINEERED MUTATION            
SEQADV 4QIA SER A  171  UNP  P14735    CYS   171 ENGINEERED MUTATION            
SEQADV 4QIA ALA A  178  UNP  P14735    CYS   178 ENGINEERED MUTATION            
SEQADV 4QIA VAL A  257  UNP  P14735    CYS   257 ENGINEERED MUTATION            
SEQADV 4QIA LEU A  414  UNP  P14735    CYS   414 ENGINEERED MUTATION            
SEQADV 4QIA ASN A  573  UNP  P14735    CYS   573 ENGINEERED MUTATION            
SEQADV 4QIA SER A  590  UNP  P14735    CYS   590 ENGINEERED MUTATION            
SEQADV 4QIA SER A  789  UNP  P14735    CYS   789 ENGINEERED MUTATION            
SEQADV 4QIA ALA A  812  UNP  P14735    CYS   812 ENGINEERED MUTATION            
SEQADV 4QIA ALA A  819  UNP  P14735    CYS   819 ENGINEERED MUTATION            
SEQADV 4QIA SER A  904  UNP  P14735    CYS   904 ENGINEERED MUTATION            
SEQADV 4QIA ASN A  966  UNP  P14735    CYS   966 ENGINEERED MUTATION            
SEQADV 4QIA ALA A  974  UNP  P14735    CYS   974 ENGINEERED MUTATION            
SEQADV 4QIA MET B   30  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   31  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   32  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   33  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   34  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   35  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA HIS B   36  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ALA B   37  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ALA B   38  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA GLY B   39  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA ILE B   40  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA PRO B   41  UNP  P14735              EXPRESSION TAG                 
SEQADV 4QIA LEU B  110  UNP  P14735    CYS   110 ENGINEERED MUTATION            
SEQADV 4QIA GLN B  111  UNP  P14735    GLU   111 ENGINEERED MUTATION            
SEQADV 4QIA SER B  171  UNP  P14735    CYS   171 ENGINEERED MUTATION            
SEQADV 4QIA ALA B  178  UNP  P14735    CYS   178 ENGINEERED MUTATION            
SEQADV 4QIA VAL B  257  UNP  P14735    CYS   257 ENGINEERED MUTATION            
SEQADV 4QIA LEU B  414  UNP  P14735    CYS   414 ENGINEERED MUTATION            
SEQADV 4QIA ASN B  573  UNP  P14735    CYS   573 ENGINEERED MUTATION            
SEQADV 4QIA SER B  590  UNP  P14735    CYS   590 ENGINEERED MUTATION            
SEQADV 4QIA SER B  789  UNP  P14735    CYS   789 ENGINEERED MUTATION            
SEQADV 4QIA ALA B  812  UNP  P14735    CYS   812 ENGINEERED MUTATION            
SEQADV 4QIA ALA B  819  UNP  P14735    CYS   819 ENGINEERED MUTATION            
SEQADV 4QIA SER B  904  UNP  P14735    CYS   904 ENGINEERED MUTATION            
SEQADV 4QIA ASN B  966  UNP  P14735    CYS   966 ENGINEERED MUTATION            
SEQADV 4QIA 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                                                      
HET    33K  A1101      26                                                       
HET     ZN  A1102       1                                                       
HET    33K  B1101      20                                                       
HET     ZN  B1102       1                                                       
HETNAM     33K N-BENZYL-N-(CARBOXYMETHYL)GLYCYL-L-HISTIDINE                     
HETNAM      ZN ZINC ION                                                         
FORMUL   3  33K    2(C17 H20 N4 O5)                                             
FORMUL   4   ZN    2(ZN 2+)                                                     
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  GLU A  233  1                                   7    
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 LEU A  322  TYR A  326  5                                   5    
HELIX   17  17 ASN A  329  HIS A  340  1                                  12    
HELIX   18  18 SER A  345  LYS A  353  1                                   9    
HELIX   19  19 GLU A  382  LEU A  385  5                                   4    
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  ILE A  440  1                                  12    
HELIX   23  23 PRO A  445  VAL A  449  5                                   5    
HELIX   24  24 ARG A  460  LEU A  471  1                                  12    
HELIX   25  25 ARG A  472  ASN A  475  5                                   4    
HELIX   26  26 LYS A  483  GLU A  486  5                                   4    
HELIX   27  27 PRO A  506  ASN A  515  1                                  10    
HELIX   28  28 SER A  580  TYR A  584  5                                   5    
HELIX   29  29 ASP A  586  ALA A  614  1                                  29    
HELIX   30  30 LYS A  637  THR A  651  1                                  15    
HELIX   31  31 ASP A  655  PHE A  673  1                                  19    
HELIX   32  32 ARG A  674  GLU A  676  5                                   3    
HELIX   33  33 GLN A  677  THR A  691  1                                  15    
HELIX   34  34 THR A  696  ASP A  705  1                                  10    
HELIX   35  35 THR A  708  LEU A  720  1                                  13    
HELIX   36  36 THR A  734  HIS A  754  1                                  21    
HELIX   37  37 SER A  801  ARG A  824  1                                  24    
HELIX   38  38 PRO A  855  MET A  877  1                                  23    
HELIX   39  39 THR A  878  ASP A  895  1                                  18    
HELIX   40  40 LYS A  899  SER A  913  1                                  15    
HELIX   41  41 ASP A  919  LYS A  929  1                                  11    
HELIX   42  42 THR A  932  LEU A  944  1                                  13    
HELIX   43  43 ASN A  994  GLY A 1001  1                                   8    
HELIX   44  44 GLY B   95  ASP B   99  5                                   5    
HELIX   45  45 GLY B  105  PHE B  115  1                                  11    
HELIX   46  46 ASN B  125  HIS B  134  1                                  10    
HELIX   47  47 HIS B  157  GLN B  167  1                                  11    
HELIX   48  48 PHE B  168  LEU B  170  5                                   3    
HELIX   49  49 ASP B  175  MET B  195  1                                  21    
HELIX   50  50 ASN B  196  ALA B  207  1                                  12    
HELIX   51  51 HIS B  213  LYS B  217  5                                   5    
HELIX   52  52 ASN B  222  GLU B  227  1                                   6    
HELIX   53  53 GLU B  227  GLU B  233  1                                   7    
HELIX   54  54 ASP B  236  TYR B  249  1                                  14    
HELIX   55  55 SER B  250  ASN B  252  5                                   3    
HELIX   56  56 SER B  263  SER B  276  1                                  14    
HELIX   57  57 GLN B  294  LEU B  298  5                                   5    
HELIX   58  58 LEU B  322  TYR B  326  5                                   5    
HELIX   59  59 ASN B  329  GLY B  339  1                                  11    
HELIX   60  60 SER B  345  LYS B  353  1                                   9    
HELIX   61  61 GLU B  382  LEU B  385  5                                   4    
HELIX   62  62 HIS B  386  GLY B  405  1                                  20    
HELIX   63  63 GLN B  407  PHE B  424  1                                  18    
HELIX   64  64 ARG B  429  LEU B  441  1                                  13    
HELIX   65  65 GLU B  448  GLU B  453  1                                   6    
HELIX   66  66 ARG B  460  ASP B  469  1                                  10    
HELIX   67  67 LYS B  470  LEU B  471  5                                   2    
HELIX   68  68 ARG B  472  ASN B  475  5                                   4    
HELIX   69  69 LYS B  483  GLU B  486  5                                   4    
HELIX   70  70 PRO B  506  ASN B  515  1                                  10    
HELIX   71  71 SER B  580  TYR B  584  5                                   5    
HELIX   72  72 ASP B  586  ALA B  614  1                                  29    
HELIX   73  73 LYS B  637  THR B  651  1                                  15    
HELIX   74  74 ASP B  655  ASN B  672  1                                  18    
HELIX   75  75 PHE B  673  GLU B  676  5                                   4    
HELIX   76  76 GLN B  677  THR B  691  1                                  15    
HELIX   77  77 THR B  696  ASP B  705  1                                  10    
HELIX   78  78 THR B  708  SER B  721  1                                  14    
HELIX   79  79 THR B  734  HIS B  754  1                                  21    
HELIX   80  80 SER B  801  ARG B  824  1                                  24    
HELIX   81  81 HIS B  857  MET B  877  1                                  21    
HELIX   82  82 THR B  878  LEU B  894  1                                  17    
HELIX   83  83 LYS B  899  SER B  913  1                                  15    
HELIX   84  84 ASP B  919  LEU B  931  1                                  13    
HELIX   85  85 THR B  932  LEU B  944  1                                  13    
HELIX   86  86 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  ARG A  49           
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 258   N  ILE A  78           
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  TYR A 149   N  LEU A  90           
SHEET    7   A 7 SER A 137  THR A 142 -1  N  ASN A 139   O  TYR A 150           
SHEET    1   B 7 VAL A 356  ALA A 367  0                                        
SHEET    2   B 7 PHE A 370  LEU A 379 -1  O  PHE A 372   N  LYS A 364           
SHEET    3   B 7 ASN A 312  ILE A 319 -1  N  ILE A 319   O  MET A 371           
SHEET    4   B 7 ARG A 477  VAL A 481 -1  O  VAL A 481   N  ASN A 312           
SHEET    5   B 7 GLN A 300  VAL A 305  1  N  TYR A 302   O  ILE A 480           
SHEET    6   B 7 GLN A 499  ALA A 504 -1  O  GLN A 499   N  VAL A 305           
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 575   O  LEU A 728           
SHEET    5   C 6 GLY A 626  TYR A 634 -1  O  LEU A 629   N  PHE A 576           
SHEET    6   C 6 LEU A 616  THR A 623 -1  N  ASP A 619   O  SER A 630           
SHEET    1   D 6 GLY A 830  ALA A 840  0                                        
SHEET    2   D 6 ILE A 843  SER A 852 -1  O  ARG A 847   N  GLY A 836           
SHEET    3   D 6 SER A 789  TYR A 795 -1  N  TYR A 795   O  LEU A 846           
SHEET    4   D 6 HIS A 952  LEU A 959 -1  O  VAL A 956   N  GLU A 792           
SHEET    5   D 6 GLY A 775  ARG A 782  1  N  GLN A 781   O  LEU A 959           
SHEET    6   D 6 GLU A 990  ILE A 992  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  ARG B  49           
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 256   N  LYS B  74           
SHEET    5   E 7 LYS B  85  VAL B  92 -1  N  SER B  87   O  LEU B 259           
SHEET    6   E 7 HIS B 146  SER B 154 -1  O  TYR B 149   N  LEU B  90           
SHEET    7   E 7 SER B 137  SER B 143 -1  N  PHE B 141   O  ASN B 148           
SHEET    1   F 7 VAL B 356  ALA B 367  0                                        
SHEET    2   F 7 PHE B 370  LEU B 379 -1  O  ILE B 374   N  GLY B 362           
SHEET    3   F 7 ASN B 312  PRO B 320 -1  N  ILE B 319   O  MET B 371           
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  ILE B 304  1  N  ILE B 304   O  ILE B 480           
SHEET    6   F 7 GLN B 499  ALA B 504 -1  O  GLU B 503   N  LEU B 301           
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 ARG B 722  GLY B 731  1  O  ALA B 727   N  LYS B 558           
SHEET    4   G 6 LYS B 571  PHE B 579 -1  N  ASN B 575   O  LEU B 728           
SHEET    5   G 6 GLY B 626  TYR B 634 -1  O  VAL B 631   N  LEU B 574           
SHEET    6   G 6 LEU B 616  THR B 623 -1  N  ASP B 619   O  SER B 630           
SHEET    1   H 4 ALA B 549  ASP B 553  0                                        
SHEET    2   H 4 SER B 557  GLN B 563 -1  O  PHE B 561   N  ALA B 549           
SHEET    3   H 4 ARG B 722  GLY B 731  1  O  ALA B 727   N  LYS B 558           
SHEET    4   H 4 LYS B 756  PRO B 757  1  O  LYS B 756   N  LEU B 723           
SHEET    1   I 6 ILE B 832  ALA B 840  0                                        
SHEET    2   I 6 ILE B 843  SER B 852 -1  O  ILE B 843   N  ALA B 840           
SHEET    3   I 6 SER B 789  TYR B 795 -1  N  SER B 789   O  SER B 852           
SHEET    4   I 6 HIS B 952  LEU B 959 -1  O  VAL B 956   N  GLU B 792           
SHEET    5   I 6 GLY B 775  ARG B 782  1  N  GLN B 781   O  LEU B 959           
SHEET    6   I 6 GLU B 990  VAL B 991  1  O  GLU B 990   N  VAL B 778           
LINK         NE2 HIS A 108                ZN    ZN A1102     1555   1555  2.09  
LINK         NE2 HIS A 112                ZN    ZN A1102     1555   1555  2.21  
LINK         OE1 GLU A 189                ZN    ZN A1102     1555   1555  2.24  
LINK         OE2 GLU A 189                ZN    ZN A1102     1555   1555  2.55  
LINK         NE2 HIS B 108                ZN    ZN B1102     1555   1555  2.14  
LINK         NE2 HIS B 112                ZN    ZN B1102     1555   1555  2.13  
LINK         OE1 GLU B 189                ZN    ZN B1102     1555   1555  2.32  
CISPEP   1 PRO B  856    HIS B  857          0        13.20                     
SITE     1 AC1  6 GLY A 335  GLY A 339  GLU A 341  LEU A 359                    
SITE     2 AC1  6 GLY A 361  LYS A 364                                          
SITE     1 AC2  3 HIS A 108  HIS A 112  GLU A 189                               
SITE     1 AC3  6 GLY B 339  GLU B 341  LEU B 359  VAL B 360                    
SITE     2 AC3  6 GLY B 361  GLY B 362                                          
SITE     1 AC4  3 HIS B 108  HIS B 112  GLU B 189                               
CRYST1  264.505  264.505   90.543  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      0.003781  0.002183  0.000000        0.00000                         
SCALE2      0.000000  0.004366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011044        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system